NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|281359561|ref|NP_001162825|]
View 

bent, isoform F [Drosophila melanogaster]

Protein Classification

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

Name Accession Description Interval E-value
STKc_Twitchin_like cd14114
The catalytic domain of the Giant Serine/Threonine Kinases, Twitchin and Projectin; STKs ...
7986-8244 7.64e-177

The catalytic domain of the Giant Serine/Threonine Kinases, Twitchin and Projectin; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily is composed of Caenorhabditis elegans and Aplysia californica Twitchin, Drosophila melanogaster Projectin, and similar proteins. These are very large muscle proteins containing multiple immunoglobulin (Ig)-like and fibronectin type III (FN3) domains and a single kinase domain near the C-terminus. Twitchin and Projectin are both associated with thick filaments. Twitchin is localized in the outer parts of A-bands and is involved in regulating muscle contraction. It interacts with the myofibrillar proteins myosin and actin in a phosphorylation-dependent manner, and may be involved in regulating the myosin cross-bridge cycle. The kinase activity of Twitchen is activated by Ca2+ and the Ca2+ binding protein S100A1. Projectin is associated with the end of thick filaments and is a component of flight muscle connecting filaments. The kinase domain of Projectin may play roles in autophosphorylation and transphosphorylation, which impact the formation of myosin filaments. The Twitchin-like subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


:

Pssm-ID: 271016 [Multi-domain]  Cd Length: 259  Bit Score: 544.49  E-value: 7.64e-177
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 7986 YDRYDILEEIGTGAFGVVHRCRERSTGNIFAAKFIPVSHSVEKDLIRREIDIMNQLHHQKLINLHDAFEDDDEMILILEF 8065
Cdd:cd14114     1 YDHYDILEELGTGAFGVVHRCTERATGNNFAAKFIMTPHESDKETVRKEIQIMNQLHHPKLINLHDAFEDDNEMVLILEF 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 8066 LSGGELFERITAEGYVMTEAEVINYMRQICEGIRHMHEQNIIHLDIKPENIMCQTRSSTNVKLIDFGLATRLDPNEVVKI 8145
Cdd:cd14114    81 LSGGELFERIAAEHYKMSEAEVINYMRQVCEGLCHMHENNIVHLDIKPENIMCTTKRSNEVKLIDFGLATHLDPKESVKV 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 8146 TTGTAEFAAPEIVNREPVGFYTDMWATGVLSYVLLSGLSPFAGDNDVQTLKNVKACDWDFDVESFKYISEEAKDFIRKLL 8225
Cdd:cd14114   161 TTGTAEFAAPEIVEREPVGFYTDMWAVGVLSYVLLSGLSPFAGENDDETLRNVKSCDWNFDDSAFSGISEEAKDFIRKLL 240
                         250
                  ....*....|....*....
gi 281359561 8226 VRNKEKRMTAHECLLHPWL 8244
Cdd:cd14114   241 LADPNKRMTIHQALEHPWL 259
I-set pfam07679
Immunoglobulin I-set domain;
8632-8721 2.67e-31

Immunoglobulin I-set domain;


:

Pssm-ID: 400151 [Multi-domain]  Cd Length: 90  Bit Score: 120.44  E-value: 2.67e-31
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561  8632 PEFTKPLHDLTIHDGEQLILTCYVKGDPEPQISWSKNGKSLSSSDILDLRYKNGIATLTINEVFPEDEGVITCTATNSVG 8711
Cdd:pfam07679    1 PKFTQKPKDVEVQEGESARFTCTVTGTPDPEVSWFKDGQPLRSSDRFKVTYEGGTYTLTISNVQPDDSGKYTCVATNSAG 80
                           90
                   ....*....|
gi 281359561  8712 AVETKCKLTI 8721
Cdd:pfam07679   81 EAEASAELTV 90
Ig_Titin_like cd05748
Immunoglobulin (Ig)-like domain of titin and similar proteins; The members here are composed ...
6174-6255 1.01e-30

Immunoglobulin (Ig)-like domain of titin and similar proteins; The members here are composed of the immunoglobulin (Ig)-like domain found in titin-like proteins and similar proteins. Titin (also called connectin) is a fibrous sarcomeric protein specifically found in vertebrate striated muscle. Titin is a giant protein; depending on isoform composition, it ranges from 2970 to 3700 kDa, and is of a length that spans half a sarcomere. Titin largely consists of multiple repeats of Ig-like and fibronectin type 3 (FN-III)-like domains. Titin connects the ends of myosin thick filaments to Z disks and extends along the thick filament to the H zone. It appears to function similarly to an elastic band, keeping the myosin filaments centered in the sarcomere during muscle contraction or stretching. Within the sarcomere, titin is also attached to or is associated with myosin binding protein C (MyBP-C). MyBP-C appears to contribute to the generation of passive tension by titin and like titin has repeated Ig-like and FN-III domains. Also included in this group are worm twitchin and insect projectin, thick filament proteins of invertebrate muscle which also have repeated Ig-like and FN-III domains.


:

Pssm-ID: 409406 [Multi-domain]  Cd Length: 82  Bit Score: 118.46  E-value: 1.01e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 6174 RIKVRAGEPVNLNIPISGAPTPTIEWKRGDLKLEEGKRISYETNSERTLFRIDDSNRRDSGKYTVTAANEFGKDTADIEV 6253
Cdd:cd05748     1 TIVVRAGESLRLDIPIKGRPTPTVTWSKDGQPLKETGRVQIETTASSTSLVIKNAKRSDSGKYTLTLKNSAGEKSATINV 80

                  ..
gi 281359561 6254 IV 6255
Cdd:cd05748    81 KV 82
FN3 COG3401
Fibronectin type 3 domain [General function prediction only];
6236-6552 1.54e-28

Fibronectin type 3 domain [General function prediction only];


:

Pssm-ID: 442628 [Multi-domain]  Cd Length: 603  Bit Score: 125.89  E-value: 1.54e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 6236 YTVTAANEFGKDTADIEVIVVDKPSPPEGP--LSYTETAPDHISLHWYSPKDdggSDITGYIIEFTEFGVDDWKPVpGTC 6313
Cdd:COG3401   207 YRVAATDTGGESAPSNEVSVTTPTTPPSAPtgLTATADTPGSVTLSWDPVTE---SDATGYRVYRSNSGDGPFTKV-ATV 282
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 6314 PNTNFTVKNLVEGKKYVFRIRAENIYG----ASEALEGKPVLAkspfdPPGAPSQPTISAYTPNSANLEWHPPDDcggKP 6389
Cdd:COG3401   283 TTTSYTDTGLTNGTTYYYRVTAVDAAGnesaPSNVVSVTTDLT-----PPAAPSGLTATAVGSSSITLSWTASSD---AD 354
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 6390 ITGYIVERRER-GGEWIKCNNYPTpNTSYTVSNLRDGARYEFRVLAVNEAGPGhpSKPSDPMTAEHQRYRPDPPEPPKPD 6468
Cdd:COG3401   355 VTGYNVYRSTSgGGTYTKIAETVT-TTSYTDTGLTPGTTYYYKVTAVDAAGNE--SAPSEEVSATTASAASGESLTASVD 431
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 6469 RITRNGV------TLSWRPPRTDGKSRIKGYYVEMRPKNGKDWKTVNDiPINSTVYTVPSLKEGEEYSFRVVAENEVGRS 6542
Cdd:COG3401   432 AVPLTDVagataaASAASNPGVSAAVLADGGDTGNAVPFTTTSSTVTA-TTTDTTTANLSVTTGSLVGGSGASSVTNSVS 510
                         330
                  ....*....|
gi 281359561 6543 DPSKPSQPIT 6552
Cdd:COG3401   511 VIGASAAAAV 520
FN3 COG3401
Fibronectin type 3 domain [General function prediction only];
3866-4181 1.85e-26

Fibronectin type 3 domain [General function prediction only];


:

Pssm-ID: 442628 [Multi-domain]  Cd Length: 603  Bit Score: 119.34  E-value: 1.85e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 3866 YIVTAKNDSG----SDTVEVeLEVLCKPSKPKGpLAVSNVTAETLHLKWEKPEDDGgdpIEQYLVERMDTETGRWVPVLT 3941
Cdd:COG3401   207 YRVAATDTGGesapSNEVSV-TTPTTPPSAPTG-LTATADTPGSVTLSWDPVTESD---ATGYRVYRSNSGDGPFTKVAT 281
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 3942 TKTPEADVTGLTEGKEYLFRVKAVNSEG-ESEPLVTDIPTKAKNPfdaadtPGKPQIVD---WSGNHCDLKWRAPEDDGg 4017
Cdd:COG3401   282 VTTTSYTDTGLTNGTTYYYRVTAVDAAGnESAPSNVVSVTTDLTP------PAAPSGLTataVGSSSITLSWTASSDAD- 354
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 4018 asITGYIVERKDPNTGKWQKALETSTpDCKARVNDLIAGNKYQFRIMAVNKAG-KSKPSEPSDQMTAKDRFAPPKIDRTN 4096
Cdd:COG3401   355 --VTGYNVYRSTSGGGTYTKIAETVT-TTSYTDTGLTPGTTYYYKVTAVDAAGnESAPSEEVSATTASAASGESLTASVD 431
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 4097 IKDITIKAGQHIRfdIKVSGEPPATKVWLHNKARLENDDSNYNIDMESYRTKLTVPIS-KRFHSGKYTLKAENESGRDEA 4175
Cdd:COG3401   432 AVPLTDVAGATAA--ASAASNPGVSAAVLADGGDTGNAVPFTTTSSTVTATTTDTTTAnLSVTTGSLVGGSGASSVTNSV 509

                  ....*.
gi 281359561 4176 SFEVIV 4181
Cdd:COG3401   510 SVIGAS 515
Ig_Titin_like cd05748
Immunoglobulin (Ig)-like domain of titin and similar proteins; The members here are composed ...
6570-6650 2.18e-24

Immunoglobulin (Ig)-like domain of titin and similar proteins; The members here are composed of the immunoglobulin (Ig)-like domain found in titin-like proteins and similar proteins. Titin (also called connectin) is a fibrous sarcomeric protein specifically found in vertebrate striated muscle. Titin is a giant protein; depending on isoform composition, it ranges from 2970 to 3700 kDa, and is of a length that spans half a sarcomere. Titin largely consists of multiple repeats of Ig-like and fibronectin type 3 (FN-III)-like domains. Titin connects the ends of myosin thick filaments to Z disks and extends along the thick filament to the H zone. It appears to function similarly to an elastic band, keeping the myosin filaments centered in the sarcomere during muscle contraction or stretching. Within the sarcomere, titin is also attached to or is associated with myosin binding protein C (MyBP-C). MyBP-C appears to contribute to the generation of passive tension by titin and like titin has repeated Ig-like and FN-III domains. Also included in this group are worm twitchin and insect projectin, thick filament proteins of invertebrate muscle which also have repeated Ig-like and FN-III domains.


:

Pssm-ID: 409406 [Multi-domain]  Cd Length: 82  Bit Score: 100.36  E-value: 2.18e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 6570 IVCRAGDDFSIHVPYLAFPKPNAFWYSNDNMLDDNNRVHKHLTDDAASVVVKNSKRADSGQYRLQLKNTSGFDTATINVR 6649
Cdd:cd05748     2 IVVRAGESLRLDIPIKGRPTPTVTWSKDGQPLKETGRVQIETTASSTSLVIKNAKRSDSGKYTLTLKNSAGEKSATINVK 81

                  .
gi 281359561 6650 V 6650
Cdd:cd05748    82 V 82
FN3 COG3401
Fibronectin type 3 domain [General function prediction only];
6905-7189 1.11e-23

Fibronectin type 3 domain [General function prediction only];


:

Pssm-ID: 442628 [Multi-domain]  Cd Length: 603  Bit Score: 110.48  E-value: 1.11e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 6905 FDSNDYASMYYNKSAKRDETGSYTITLTNNKGSDTASCHVTVVDRPLPPQGP--LNAYDITPDTCTLAWKTPLDDGgspI 6982
Cdd:COG3401   185 LTVTSTTLVDGGGDIEPGTTYYYRVAATDTGGESAPSNEVSVTTPTTPPSAPtgLTATADTPGSVTLSWDPVTESD---A 261
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 6983 TNYVVE-KLDNSGSWVKISSfVRNTHYDVMGLEPHYKYNFRVRAENQYGL-SDPLDIIEPIVAKhqfTVPDEPGQPKVID 7060
Cdd:COG3401   262 TGYRVYrSNSGDGPFTKVAT-VTTTSYTDTGLTNGTTYYYRVTAVDAAGNeSAPSNVVSVTTDL---TPPAAPSGLTATA 337
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 7061 WDSGNVTLIWTRPLSDGgsrIQGYQIeYRDILNDSSWNAYDYIIKDTKYQLYNLINGSEYEFRIKAKNAAGLSKPSSPSL 7140
Cdd:COG3401   338 VGSSSITLSWTASSDAD---VTGYNV-YRSTSGGGTYTKIAETVTTTSYTDTGLTPGTTYYYKVTAVDAAGNESAPSEEV 413
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*....
gi 281359561 7141 RFKlkgKFTVPSPPGAPQVTRVGKNYVDLKWEKPLRDGGSRITGYIIER 7189
Cdd:COG3401   414 SAT---TASAASGESLTASVDAVPLTDVAGATAAASAASNPGVSAAVLA 459
I-set pfam07679
Immunoglobulin I-set domain;
3494-3590 1.25e-22

Immunoglobulin I-set domain;


:

Pssm-ID: 400151 [Multi-domain]  Cd Length: 90  Bit Score: 95.79  E-value: 1.25e-22
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561  3494 PRFLKPhidrvnLKPVIVKTGLSISLDINIRGEPAPKVEWFFNNSSVTSDEHsVKIDNVDYNTKFFVMRAQRSQSGKYII 3573
Cdd:pfam07679    1 PKFTQK------PKDVEVQEGESARFTCTVTGTPDPEVSWFKDGQPLRSSDR-FKVTYEGGTYTLTISNVQPDDSGKYTC 73
                           90
                   ....*....|....*..
gi 281359561  3574 KATNEVGEDEAELEVTV 3590
Cdd:pfam07679   74 VATNSAGEAEASAELTV 90
FN3 cd00063
Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein ...
2203-2292 2.49e-22

Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein fibronectin. Its tenth fibronectin type III repeat contains an RGD cell recognition sequence in a flexible loop between 2 strands. Approximately 2% of all animal proteins contain the FN3 repeat; including extracellular and intracellular proteins, membrane spanning cytokine receptors, growth hormone receptors, tyrosine phosphatase receptors, and adhesion molecules. FN3-like domains are also found in bacterial glycosyl hydrolases.


:

Pssm-ID: 238020 [Multi-domain]  Cd Length: 93  Bit Score: 94.87  E-value: 2.49e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 2203 PGKPKAVDLTDWDKDHADLKWEAPETDGGdPITAYIVEYKEKFSNDWVSGKEVDGDARTATVDGLKEGQQYEFRVRAVNR 2282
Cdd:cd00063     1 PSPPTNLRVTDVTSTSVTLSWTPPEDDGG-PITGYVVEYREKGSGDWKEVEVTPGSETSYTLTGLKPGTEYEFRVRAVNG 79
                          90
                  ....*....|
gi 281359561 2283 AGPGEPSDKT 2292
Cdd:cd00063    80 GGESPPSESV 89
FN3 cd00063
Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein ...
5764-5853 6.16e-22

Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein fibronectin. Its tenth fibronectin type III repeat contains an RGD cell recognition sequence in a flexible loop between 2 strands. Approximately 2% of all animal proteins contain the FN3 repeat; including extracellular and intracellular proteins, membrane spanning cytokine receptors, growth hormone receptors, tyrosine phosphatase receptors, and adhesion molecules. FN3-like domains are also found in bacterial glycosyl hydrolases.


:

Pssm-ID: 238020 [Multi-domain]  Cd Length: 93  Bit Score: 93.72  E-value: 6.16e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 5764 PDAPGKPIITDWDRDHIDLQWAVPKSDGGaPISEYIIQKKEKGSPYWTNVRHVPSNKNTTTIPELTEGQEYEFRVIAVNQ 5843
Cdd:cd00063     1 PSPPTNLRVTDVTSTSVTLSWTPPEDDGG-PITGYVVEYREKGSGDWKEVEVTPGSETSYTLTGLKPGTEYEFRVRAVNG 79
                          90
                  ....*....|
gi 281359561 5844 AGQSEPSEPS 5853
Cdd:cd00063    80 GGESPPSESV 89
Ig super family cl11960
Immunoglobulin domain; The members here are composed of the immunoglobulin (Ig) domain found ...
8313-8401 7.94e-22

Immunoglobulin domain; The members here are composed of the immunoglobulin (Ig) domain found in the Ig superfamily. The Ig superfamily is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. Members of this group are components of immunoglobulin, neuroglia, cell surface glycoproteins, including T-cell receptors, CD2, CD4, CD8, and membrane glycoproteins, including butyrophilin and chondroitin sulfate proteoglycan core protein. A predominant feature of most Ig domains is a disulfide bridge connecting the two beta-sheets with a tryptophan residue packed against the disulfide bond. Ig superfamily (IgSF) domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. Typically, the V-set domains have A, B, E, and D strands in one sheet and A', G, F, C, C' and C" in the other. The structures in C1-set are smaller than those in the V-set; they have one beta sheet that is formed by strands A, B, E, and D and the other by strands G, F, C, and C'. Moreover, a C1-set Ig domain contains a short C' strand (three residues) and lacks A' and C" strand. Unlike other Ig domain sets, C2-set structures do not have a D strand. Like the V-set Ig domains, members of the I-set have a discontinuous A strand, but lack a C" strand.


The actual alignment was detected with superfamily member cd20949:

Pssm-ID: 472250 [Multi-domain]  Cd Length: 89  Bit Score: 93.55  E-value: 7.94e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 8313 RFVIRPSSQFCYEGQSVKFYCRCIAIATPTLTWSHNNIELRQSVKFMKRYVGDDYYFIINRVKLDDRGEYIIRAENHYGS 8392
Cdd:cd20949     1 TFTENAYVTTVKEGQSATILCEVKGEPQPNVTWHFNGQPISASVADMSKYRILADGLLINKVTQDDTGEYTCRAYQVNSI 80

                  ....*....
gi 281359561 8393 REEVVFLNV 8401
Cdd:cd20949    81 ASDMQERTV 89
FN3 cd00063
Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein ...
5073-5166 1.28e-21

Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein fibronectin. Its tenth fibronectin type III repeat contains an RGD cell recognition sequence in a flexible loop between 2 strands. Approximately 2% of all animal proteins contain the FN3 repeat; including extracellular and intracellular proteins, membrane spanning cytokine receptors, growth hormone receptors, tyrosine phosphatase receptors, and adhesion molecules. FN3-like domains are also found in bacterial glycosyl hydrolases.


:

Pssm-ID: 238020 [Multi-domain]  Cd Length: 93  Bit Score: 92.94  E-value: 1.28e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 5073 PAPPNGpLKVDEINSESCTLHWNPPDDDGGqPIDNYVVEKLDETTGRWIPAGETDGPVTALKVGGLTPGHKYKFRVRAKN 5152
Cdd:cd00063     1 PSPPTN-LRVTDVTSTSVTLSWTPPEDDGG-PITGYVVEYREKGSGDWKEVEVTPGSETSYTLTGLKPGTEYEFRVRAVN 78
                          90
                  ....*....|....
gi 281359561 5153 RQGTSEPLTTAQAI 5166
Cdd:cd00063    79 GGGESPPSESVTVT 92
FN3 COG3401
Fibronectin type 3 domain [General function prediction only];
6630-7006 2.27e-21

Fibronectin type 3 domain [General function prediction only];


:

Pssm-ID: 442628 [Multi-domain]  Cd Length: 603  Bit Score: 103.16  E-value: 2.27e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 6630 QYRLQLKNTSGFDTATINVRVLDR---PSPPTRLRADEFSGDSLTLYWNPPNDDGgsaIQNYIIEKKEARSSTWSKVSSF 6706
Cdd:COG3401   206 YYRVAATDTGGESAPSNEVSVTTPttpPSAPTGLTATADTPGSVTLSWDPVTESD---ATGYRVYRSNSGDGPFTKVATV 282
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 6707 CTVPFVrIRNLVLNKEYDFRVIAENKYG-QSDPANTSEPILARHPfdiPNTPGIPHGIDSTEDSITIAWTKPKhdgGSPI 6785
Cdd:COG3401   283 TTTSYT-DTGLTNGTTYYYRVTAVDAAGnESAPSNVVSVTTDLTP---PAAPSGLTATAVGSSSITLSWTASS---DADV 355
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 6786 TGYIIEKRLLSDDKWTKaVHALCPDLSCKIPNLIENAEYEFRVAAVNAAGqsAYSGSSDLIFCRRPPHAPKITSDLSIRD 6865
Cdd:COG3401   356 TGYNVYRSTSGGGTYTK-IAETVTTTSYTDTGLTPGTTYYYKVTAVDAAG--NESAPSEEVSATTASAASGESLTASVDA 432
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 6866 MTVIAGDefRITVPYHASPRPTASWSLNGLEVIPGERIKFDSNDYASMYYNKSAKRDETGSYTITLTNNKGSDTASCHVT 6945
Cdd:COG3401   433 VPLTDVA--GATAAASAASNPGVSAAVLADGGDTGNAVPFTTTSSTVTATTTDTTTANLSVTTGSLVGGSGASSVTNSVS 510
                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 281359561 6946 VVDRPLPPQGPLNAYDITPDTC--TLAWKTPLDDGGSPITNYVVEKLDNSGSWVKISSFVRNT 7006
Cdd:COG3401   511 VIGASAAAAVGGAPDGTPNVTGasPVTVGASTGDVLITDLVSLTTSASSSVSGAGLGSGNLYL 573
FN3 cd00063
Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein ...
2999-3088 2.31e-21

Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein fibronectin. Its tenth fibronectin type III repeat contains an RGD cell recognition sequence in a flexible loop between 2 strands. Approximately 2% of all animal proteins contain the FN3 repeat; including extracellular and intracellular proteins, membrane spanning cytokine receptors, growth hormone receptors, tyrosine phosphatase receptors, and adhesion molecules. FN3-like domains are also found in bacterial glycosyl hydrolases.


:

Pssm-ID: 238020 [Multi-domain]  Cd Length: 93  Bit Score: 92.17  E-value: 2.31e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 2999 PSKPRGpLDVKDVTKDSCKLKWKKPEDDGGkPISAYQVEKFDKKQGRWVPLGRTSANDTEFDVKGLQEGHEYQFRVKAIN 3078
Cdd:cd00063     1 PSPPTN-LRVTDVTSTSVTLSWTPPEDDGG-PITGYVVEYREKGSGDWKEVEVTPGSETSYTLTGLKPGTEYEFRVRAVN 78
                          90
                  ....*....|
gi 281359561 3079 EEGESDPLDS 3088
Cdd:cd00063    79 GGGESPPSES 88
FN3 cd00063
Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein ...
2501-2590 2.43e-21

Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein fibronectin. Its tenth fibronectin type III repeat contains an RGD cell recognition sequence in a flexible loop between 2 strands. Approximately 2% of all animal proteins contain the FN3 repeat; including extracellular and intracellular proteins, membrane spanning cytokine receptors, growth hormone receptors, tyrosine phosphatase receptors, and adhesion molecules. FN3-like domains are also found in bacterial glycosyl hydrolases.


:

Pssm-ID: 238020 [Multi-domain]  Cd Length: 93  Bit Score: 92.17  E-value: 2.43e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 2501 PSPPSQPVIDDYDNKSVLLKWKRPPSDGGrPITHYIVEIKDKFAPSWSEVAKTDDPNPECNVEGLKEKMVYQFRVRAVNK 2580
Cdd:cd00063     1 PSPPTNLRVTDVTSTSVTLSWTPPEDDGG-PITGYVVEYREKGSGDWKEVEVTPGSETSYTLTGLKPGTEYEFRVRAVNG 79
                          90
                  ....*....|
gi 281359561 2581 AGPSEPSQPT 2590
Cdd:cd00063    80 GGESPPSESV 89
FN3 COG3401
Fibronectin type 3 domain [General function prediction only];
5972-6384 3.24e-21

Fibronectin type 3 domain [General function prediction only];


:

Pssm-ID: 442628 [Multi-domain]  Cd Length: 603  Bit Score: 102.77  E-value: 3.24e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 5972 ANSVTISWKPPKDNGGSEISSYVIEKRDLTHGGGWVPAVNYVSAKYNHAVVPRLLEGTMYELRVMAENLQGRSDPltsDQ 6051
Cdd:COG3401   146 GLYGVDGANASGTTASSVAGAGVVVSPDTSATAAVATTSLTVTSTTLVDGGGDIEPGTTYYYRVAATDTGGESAP---SN 222
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 6052 PVVAKSQYTVPGAPGKPELTDSDKNHITIKWKqpiSNGGSPIIGYDIERRDVNTGRWIKINGqpVPTAEYQDDRVTSNHQ 6131
Cdd:COG3401   223 EVSVTTPTTPPSAPTGLTATADTPGSVTLSWD---PVTESDATGYRVYRSNSGDGPFTKVAT--VTTTSYTDTGLTNGTT 297
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 6132 YQYRISAVNAAGNgkTSEPSAifnarplrekprfyfdgligkrikvragepvnlnipisgaptptiewkrgdlkleegkr 6211
Cdd:COG3401   298 YYYRVTAVDAAGN--ESAPSN----------------------------------------------------------- 316
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 6212 isyetnsertlfriddsnrrdsgkyTVTAanefgkdTADIEvivvdKPSPPEGpLSYTETAPDHISLHWYSPKDdggSDI 6291
Cdd:COG3401   317 -------------------------VVSV-------TTDLT-----PPAAPSG-LTATAVGSSSITLSWTASSD---ADV 355
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 6292 TGYIIEFTEFGVDDWKPVPGTCPNTNFTVKNLVEGKKYVFRIRAENIYG----ASEALEGKPVLAKSPFDPPGAPSQPTI 6367
Cdd:COG3401   356 TGYNVYRSTSGGGTYTKIAETVTTTSYTDTGLTPGTTYYYKVTAVDAAGnesaPSEEVSATTASAASGESLTASVDAVPL 435
                         410
                  ....*....|....*..
gi 281359561 6368 SAYTPNSANLEWHPPDD 6384
Cdd:COG3401   436 TDVAGATAAASAASNPG 452
FN3 COG3401
Fibronectin type 3 domain [General function prediction only];
4356-4776 6.18e-21

Fibronectin type 3 domain [General function prediction only];


:

Pssm-ID: 442628 [Multi-domain]  Cd Length: 603  Bit Score: 102.00  E-value: 6.18e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 4356 NCEYEFRVKAINAAGPGEPSDASKPIITKPRKLAPKIDRKNIRTYNFKSGEPIFLDINISGEPAPDVTWNQNNKSVQTTS 4435
Cdd:COG3401   108 NTGLTSSDEVPSPAVGTATTATAVAGGAATAGTYALGAGLYGVDGANASGTTASSVAGAGVVVSPDTSATAAVATTSLTV 187
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 4436 fshienLPYNTKYINNNPERKDTGLYKISAHNFYGQ----DQVEFqINIITKPGKPEGpLEVSEVHKDGCKLKWKKPKDD 4511
Cdd:COG3401   188 ------TSTTLVDGGGDIEPGTTYYYRVAATDTGGEsapsNEVSV-TTPTTPPSAPTG-LTATADTPGSVTLSWDPVTES 259
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 4512 GgepVESYLVEKFDPDTGIWLPVGRSDGPEYNVDGLVPGHDYKFRVKAVNKEG-ESEPLETLgsiiakdpfSVPTKPGVP 4590
Cdd:COG3401   260 D---ATGYRVYRSNSGDGPFTKVATVTTTSYTDTGLTNGTTYYYRVTAVDAAGnESAPSNVV---------SVTTDLTPP 327
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 4591 EP------TDWTANKVELAWpEPASDGGspIQGYIVEVKDKYSPLWEKALETNSpTPTATVQGLIEGNEYQFRVVALNKG 4664
Cdd:COG3401   328 AApsgltaTAVGSSSITLSW-TASSDAD--VTGYNVYRSTSGGGTYTKIAETVT-TTSYTDTGLTPGTTYYYKVTAVDAA 403
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 4665 GL-SEPSDPSKIFTAKPRYLAPKIDRRNLRNITLSSG-TALKLDANITGEPAPKVEWKLSNYHLQSGKNVTIETPDYYTk 4742
Cdd:COG3401   404 GNeSAPSEEVSATTASAASGESLTASVDAVPLTDVAGaTAAASAASNPGVSAAVLADGGDTGNAVPFTTTSSTVTATTT- 482
                         410       420       430
                  ....*....|....*....|....*....|....
gi 281359561 4743 LVIRPTQRSDSGEYLVTATNTSGKDSVLVNVVIT 4776
Cdd:COG3401   483 DTTTANLSVTTGSLVGGSGASSVTNSVSVIGASA 516
I-set pfam07679
Immunoglobulin I-set domain;
8740-8831 6.23e-21

Immunoglobulin I-set domain;


:

Pssm-ID: 400151 [Multi-domain]  Cd Length: 90  Bit Score: 90.78  E-value: 6.23e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561  8740 PKIVSHLESRFVRDGDAVNLACRIIGAQHFDVVWLHNNKEIKPSKDFQYTNEANIYRLQIAEIFPEDGGTYTCEAFNDIG 8819
Cdd:pfam07679    1 PKFTQKPKDVEVQEGESARFTCTVTGTPDPEVSWFKDGQPLRSSDRFKVTYEGGTYTLTISNVQPDDSGKYTCVATNSAG 80
                           90
                   ....*....|..
gi 281359561  8820 EsfSTCTINVTV 8831
Cdd:pfam07679   81 E--AEASAELTV 90
FN3 cd00063
Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein ...
4879-4970 9.76e-21

Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein fibronectin. Its tenth fibronectin type III repeat contains an RGD cell recognition sequence in a flexible loop between 2 strands. Approximately 2% of all animal proteins contain the FN3 repeat; including extracellular and intracellular proteins, membrane spanning cytokine receptors, growth hormone receptors, tyrosine phosphatase receptors, and adhesion molecules. FN3-like domains are also found in bacterial glycosyl hydrolases.


:

Pssm-ID: 238020 [Multi-domain]  Cd Length: 93  Bit Score: 90.25  E-value: 9.76e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 4879 PGKPENLKATDWDKDHVDLAWTPPLiDGGSPISCYIIEKQDKY-GKWERALDVPADQCKATIPDLVEGQTYKFRVSAVNA 4957
Cdd:cd00063     1 PSPPTNLRVTDVTSTSVTLSWTPPE-DDGGPITGYVVEYREKGsGDWKEVEVTPGSETSYTLTGLKPGTEYEFRVRAVNG 79
                          90
                  ....*....|...
gi 281359561 4958 AGTGEPSDSTPPI 4970
Cdd:cd00063    80 GGESPPSESVTVT 92
FN3 cd00063
Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein ...
7151-7237 1.31e-20

Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein fibronectin. Its tenth fibronectin type III repeat contains an RGD cell recognition sequence in a flexible loop between 2 strands. Approximately 2% of all animal proteins contain the FN3 repeat; including extracellular and intracellular proteins, membrane spanning cytokine receptors, growth hormone receptors, tyrosine phosphatase receptors, and adhesion molecules. FN3-like domains are also found in bacterial glycosyl hydrolases.


:

Pssm-ID: 238020 [Multi-domain]  Cd Length: 93  Bit Score: 90.25  E-value: 1.31e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 7151 PSPPGAPQVTRVGKNYVDLKWEKPlRDGGSRITGYIIERRDIGGAVWVKCNDYNVLDTEYTVMNLIEMGDYEFRVFAVNS 7230
Cdd:cd00063     1 PSPPTNLRVTDVTSTSVTLSWTPP-EDDGGPITGYVVEYREKGSGDWKEVEVTPGSETSYTLTGLKPGTEYEFRVRAVNG 79

                  ....*..
gi 281359561 7231 AGRSEPS 7237
Cdd:cd00063    80 GGESPPS 86
FN3 COG3401
Fibronectin type 3 domain [General function prediction only];
2673-2891 1.71e-20

Fibronectin type 3 domain [General function prediction only];


:

Pssm-ID: 442628 [Multi-domain]  Cd Length: 603  Bit Score: 100.46  E-value: 1.71e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 2673 FYTLKAEN--RNGIDRETVELVVLGKPSSPKGPLAVSDVTASGCKLQWKKPEDDGgvpIKEYVVEKMDTATGKWVRVGRS 2750
Cdd:COG3401   206 YYRVAATDtgGESAPSNEVSVTTPTTPPSAPTGLTATADTPGSVTLSWDPVTESD---ATGYRVYRSNSGDGPFTKVATV 282
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 2751 PGekepPSFDVTGLSLGSEYMFRVSAVNEEG-ESEPLTTLVGVVAKDPfdePNKPGTPEVTDYDNQSISLKWAAPnndGG 2829
Cdd:COG3401   283 TT----TSYTDTGLTNGTTYYYRVTAVDAAGnESAPSNVVSVTTDLTP---PAAPSGLTATAVGSSSITLSWTAS---SD 352
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 281359561 2830 APIQKYIIEKKNKNKTEWEKaLEIPGDQLEATVAGLQEYGEYQFRVIAVNKAGLSPPSDASV 2891
Cdd:COG3401   353 ADVTGYNVYRSTSGGGTYTK-IAETVTTTSYTDTGLTPGTTYYYKVTAVDAAGNESAPSEEV 413
FN3 COG3401
Fibronectin type 3 domain [General function prediction only];
2957-3191 1.93e-20

Fibronectin type 3 domain [General function prediction only];


:

Pssm-ID: 442628 [Multi-domain]  Cd Length: 603  Bit Score: 100.46  E-value: 1.93e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 2957 IPYNTKISIIETVRKHTGIYKIIAVNEHGQDEATVEVNILA---PPSKPRGpLDVKDVTKDSCKLKWKKPEDDGgkpISA 3033
Cdd:COG3401   188 TSTTLVDGGGDIEPGTTYYYRVAATDTGGESAPSNEVSVTTpttPPSAPTG-LTATADTPGSVTLSWDPVTESD---ATG 263
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 3034 YQVEKFDKKQGRWVPLGRTsaNDTEFDVKGLQEGHEYQFRVKAINEEG-ESDPLDSDDSIIAKNPydaaskPGTPNIVDY 3112
Cdd:COG3401   264 YRVYRSNSGDGPFTKVATV--TTTSYTDTGLTNGTTYYYRVTAVDAAGnESAPSNVVSVTTDLTP------PAAPSGLTA 335
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 3113 NEHM---VKLKWEAPrSDGGApiSGYIIEKKDKFSPIWDEILSTNTSvPEATVEGLVEGNIYQFRVRAVNKAG-FSDPSD 3188
Cdd:COG3401   336 TAVGsssITLSWTAS-SDADV--TGYNVYRSTSGGGTYTKIAETVTT-TSYTDTGLTPGTTYYYKVTAVDAAGnESAPSE 411

                  ...
gi 281359561 3189 ATE 3191
Cdd:COG3401   412 EVS 414
I-set pfam07679
Immunoglobulin I-set domain;
7648-7737 2.95e-20

Immunoglobulin I-set domain;


:

Pssm-ID: 400151 [Multi-domain]  Cd Length: 90  Bit Score: 88.85  E-value: 2.95e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561  7648 PLIVKPLRDANCIQNHNAQFTCTINGVPKPTISWYKGAREISNGARYHMYSEGDNHFLNINDVFGEDADEYVCRAVNKAG 7727
Cdd:pfam07679    1 PKFTQKPKDVEVQEGESARFTCTVTGTPDPEVSWFKDGQPLRSSDRFKVTYEGGTYTLTISNVQPDDSGKYTCVATNSAG 80
                           90
                   ....*....|
gi 281359561  7728 AKSTRATLAI 7737
Cdd:pfam07679   81 EAEASAELTV 90
FN3 cd00063
Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein ...
3296-3390 5.46e-20

Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein fibronectin. Its tenth fibronectin type III repeat contains an RGD cell recognition sequence in a flexible loop between 2 strands. Approximately 2% of all animal proteins contain the FN3 repeat; including extracellular and intracellular proteins, membrane spanning cytokine receptors, growth hormone receptors, tyrosine phosphatase receptors, and adhesion molecules. FN3-like domains are also found in bacterial glycosyl hydrolases.


:

Pssm-ID: 238020 [Multi-domain]  Cd Length: 93  Bit Score: 88.32  E-value: 5.46e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 3296 PSKPEGpIEVSDIHKEGCKLKWRKPKDDGGiPITGYVIEKMDTATGKWVPAGSVDPEKYDIEIKGLDPNHRYQFRVKAVN 3375
Cdd:cd00063     1 PSPPTN-LRVTDVTSTSVTLSWTPPEDDGG-PITGYVVEYREKGSGDWKEVEVTPGSETSYTLTGLKPGTEYEFRVRAVN 78
                          90
                  ....*....|....*
gi 281359561 3376 EEGESEPLETESAIT 3390
Cdd:cd00063    79 GGGESPPSESVTVTT 93
FN3 COG3401
Fibronectin type 3 domain [General function prediction only];
5021-5264 7.24e-20

Fibronectin type 3 domain [General function prediction only];


:

Pssm-ID: 442628 [Multi-domain]  Cd Length: 603  Bit Score: 98.54  E-value: 7.24e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 5021 YSKDNVKVTNVDYNTKLKVNSATRSDSGI---YTVFAENANGEDSADVKVTVIDKPAPPNGP--LKVDEINSESCTLHWN 5095
Cdd:COG3401   175 SATAAVATTSLTVTSTTLVDGGGDIEPGTtyyYRVAATDTGGESAPSNEVSVTTPTTPPSAPtgLTATADTPGSVTLSWD 254
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 5096 PPDDDGgqpIDNYVVEKLDETTGRWIPAGETDGpvTALKVGGLTPGHKYKFRVRAKNRQGT-SEPLTTAQAIIAKNPfdv 5174
Cdd:COG3401   255 PVTESD---ATGYRVYRSNSGDGPFTKVATVTT--TSYTDTGLTNGTTYYYRVTAVDAAGNeSAPSNVVSVTTDLTP--- 326
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 5175 PTKPGTPTIKDFDKEFVDLEWTrpeADGGSPITGYVVEKRDKFSPDWEKCAEISDDiTNAHVPDLIEGLKYEFRVRAVNK 5254
Cdd:COG3401   327 PAAPSGLTATAVGSSSITLSWT---ASSDADVTGYNVYRSTSGGGTYTKIAETVTT-TSYTDTGLTPGTTYYYKVTAVDA 402
                         250
                  ....*....|
gi 281359561 5255 AGPGSPSDAT 5264
Cdd:COG3401   403 AGNESAPSEE 412
FN3 COG3401
Fibronectin type 3 domain [General function prediction only];
7421-7762 1.31e-19

Fibronectin type 3 domain [General function prediction only];


:

Pssm-ID: 442628 [Multi-domain]  Cd Length: 603  Bit Score: 97.77  E-value: 1.31e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 7421 YQIEFTNESGSATGEFYVHITGMPSAPTGPMGISYINK--NSCMLNWRPPSYDGglkVSHYVIERKDVSSPHWITVSSTc 7498
Cdd:COG3401   207 YRVAATDTGGESAPSNEVSVTTPTTPPSAPTGLTATADtpGSVTLSWDPVTESD---ATGYRVYRSNSGDGPFTKVATV- 282
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 7499 KDTAFNVQGLIENQEYIFRVMAVNENG-MGPPlegLNPIRAKDPIDPPSPPGSPQITEIGGDFVHLEWEKPESdggAHIQ 7577
Cdd:COG3401   283 TTTSYTDTGLTNGTTYYYRVTAVDAAGnESAP---SNVVSVTTDLTPPAAPSGLTATAVGSSSITLSWTASSD---ADVT 356
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 7578 GYWIDKREVGSNTWQRVNATICAANQINcINLIEGRQYEFRIFAQNVAGLstESSASQAVKIIDPQAASPPLIVKPLRDA 7657
Cdd:COG3401   357 GYNVYRSTSGGGTYTKIAETVTTTSYTD-TGLTPGTTYYYKVTAVDAAGN--ESAPSEEVSATTASAASGESLTASVDAV 433
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 7658 NCIQNHNAQFTCTINGVPKPTISWYKGAREISNGARYHMYSEGDNHFLNINDVFGEDADEYVcrAVNKAGAKSTRATLAI 7737
Cdd:COG3401   434 PLTDVAGATAAASAASNPGVSAAVLADGGDTGNAVPFTTTSSTVTATTTDTTTANLSVTTGS--LVGGSGASSVTNSVSV 511
                         330       340
                  ....*....|....*....|....*
gi 281359561 7738 MTAPKLNVPPRFRDTAYFDKGENVV 7762
Cdd:COG3401   512 IGASAAAAVGGAPDGTPNVTGASPV 536
FN3 cd00063
Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein ...
3400-3489 4.38e-19

Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein fibronectin. Its tenth fibronectin type III repeat contains an RGD cell recognition sequence in a flexible loop between 2 strands. Approximately 2% of all animal proteins contain the FN3 repeat; including extracellular and intracellular proteins, membrane spanning cytokine receptors, growth hormone receptors, tyrosine phosphatase receptors, and adhesion molecules. FN3-like domains are also found in bacterial glycosyl hydrolases.


:

Pssm-ID: 238020 [Multi-domain]  Cd Length: 93  Bit Score: 85.63  E-value: 4.38e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 3400 PPGLPELEDWDEHHVKLKWEPPiRDGGSPITNYIIEVMDKDSGEFVKAVETDSPVCKGVVKKLEEGQQYKFRVRAVNKAG 3479
Cdd:cd00063     3 PPTNLRVTDVTSTSVTLSWTPP-EDDGGPITGYVVEYREKGSGDWKEVEVTPGSETSYTLTGLKPGTEYEFRVRAVNGGG 81
                          90
                  ....*....|
gi 281359561 3480 PSDPSEQTNW 3489
Cdd:cd00063    82 ESPPSESVTV 91
FN3 COG3401
Fibronectin type 3 domain [General function prediction only];
2376-2753 6.78e-19

Fibronectin type 3 domain [General function prediction only];


:

Pssm-ID: 442628 [Multi-domain]  Cd Length: 603  Bit Score: 95.45  E-value: 6.78e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 2376 YKLVLSNSSGTIESEAQVVVLDRPLPPGgpfEPEEIRAS-----HIKMKWKRPDDDGgceISGYALERMDEETGRWIPAG 2450
Cdd:COG3401   207 YRVAATDTGGESAPSNEVSVTTPTTPPS---APTGLTATadtpgSVTLSWDPVTESD---ATGYRVYRSNSGDGPFTKVA 280
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 2451 EVgpNETSFDFKGLTPNKKYKFRVKAINKEG-ESEPLETFDAIVARNpydPPSPPSQPVIDDYDNKSVLLKWKrPPSDGG 2529
Cdd:COG3401   281 TV--TTTSYTDTGLTNGTTYYYRVTAVDAAGnESAPSNVVSVTTDLT---PPAAPSGLTATAVGSSSITLSWT-ASSDAD 354
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 2530 rpITHYIVEIKDKFAPSWSEVAKTDDpNPECNVEGLKEKMVYQFRVRAVNKAG----PSEPSQPTDNHLCKHKNLKPQID 2605
Cdd:COG3401   355 --VTGYNVYRSTSGGGTYTKIAETVT-TTSYTDTGLTPGTTYYYKVTAVDAAGnesaPSEEVSATTASAASGESLTASVD 431
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 2606 RSTFKRVTIKSGRTHKWSVDVLGEPI----PELHWSWRDDIPLTNGDRIKIENVDYHTDFSITNvlrKDSGFYTLKAENR 2681
Cdd:COG3401   432 AVPLTDVAGATAAASAASNPGVSAAVladgGDTGNAVPFTTTSSTVTATTTDTTTANLSVTTGS---LVGGSGASSVTNS 508
                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 281359561 2682 NGIDRETVELVVLGKPSSPKGPLAVSDVTASGCKLQWKKPEDDGGVPIKEYVVEkmDTATGKWVRVGRSPGE 2753
Cdd:COG3401   509 VSVIGASAAAAVGGAPDGTPNVTGASPVTVGASTGDVLITDLVSLTTSASSSVS--GAGLGSGNLYLITTLG 578
FN3 cd00063
Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein ...
3694-3781 9.35e-19

Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein fibronectin. Its tenth fibronectin type III repeat contains an RGD cell recognition sequence in a flexible loop between 2 strands. Approximately 2% of all animal proteins contain the FN3 repeat; including extracellular and intracellular proteins, membrane spanning cytokine receptors, growth hormone receptors, tyrosine phosphatase receptors, and adhesion molecules. FN3-like domains are also found in bacterial glycosyl hydrolases.


:

Pssm-ID: 238020 [Multi-domain]  Cd Length: 93  Bit Score: 84.86  E-value: 9.35e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 3694 PDRPGKPEPTNWDKDFVDLAWDPPKNDGGaPIQKYVIQMRDKSGRAWVDSATVPGDKCNGTVTGVEEGHEYEFRIVAVNK 3773
Cdd:cd00063     1 PSPPTNLRVTDVTSTSVTLSWTPPEDDGG-PITGYVVEYREKGSGDWKEVEVTPGSETSYTLTGLKPGTEYEFRVRAVNG 79

                  ....*...
gi 281359561 3774 AGPSDPSD 3781
Cdd:cd00063    80 GGESPPSE 87
FN3 cd00063
Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein ...
5470-5561 1.81e-18

Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein fibronectin. Its tenth fibronectin type III repeat contains an RGD cell recognition sequence in a flexible loop between 2 strands. Approximately 2% of all animal proteins contain the FN3 repeat; including extracellular and intracellular proteins, membrane spanning cytokine receptors, growth hormone receptors, tyrosine phosphatase receptors, and adhesion molecules. FN3-like domains are also found in bacterial glycosyl hydrolases.


:

Pssm-ID: 238020 [Multi-domain]  Cd Length: 93  Bit Score: 84.09  E-value: 1.81e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 5470 PDKPGQPQATDWGKHFVDLEWSTPKRDGGaPISSYIIEKRPKF-GQWERAAVVLGDNCKAHVPELTNGGEYEFRVIAVNR 5548
Cdd:cd00063     1 PSPPTNLRVTDVTSTSVTLSWTPPEDDGG-PITGYVVEYREKGsGDWKEVEVTPGSETSYTLTGLKPGTEYEFRVRAVNG 79
                          90
                  ....*....|...
gi 281359561 5549 GGPSDPSDPSSTI 5561
Cdd:cd00063    80 GGESPPSESVTVT 92
FN3 cd00063
Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein ...
5370-5462 4.35e-18

Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein fibronectin. Its tenth fibronectin type III repeat contains an RGD cell recognition sequence in a flexible loop between 2 strands. Approximately 2% of all animal proteins contain the FN3 repeat; including extracellular and intracellular proteins, membrane spanning cytokine receptors, growth hormone receptors, tyrosine phosphatase receptors, and adhesion molecules. FN3-like domains are also found in bacterial glycosyl hydrolases.


:

Pssm-ID: 238020 [Multi-domain]  Cd Length: 93  Bit Score: 82.93  E-value: 4.35e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 5370 PSVPEGpLRNGDVSKNSIVLRWRPPKDDGGsEITHYVVEKMDNEAMRW--VPVGDCTDTEIRADNLIENHDYSFRVRAVN 5447
Cdd:cd00063     1 PSPPTN-LRVTDVTSTSVTLSWTPPEDDGG-PITGYVVEYREKGSGDWkeVEVTPGSETSYTLTGLKPGTEYEFRVRAVN 78
                          90
                  ....*....|....*
gi 281359561 5448 KQGQSQPLTTSQPIT 5462
Cdd:cd00063    79 GGGESPPSESVTVTT 93
Ig super family cl11960
Immunoglobulin domain; The members here are composed of the immunoglobulin (Ig) domain found ...
5286-5366 5.47e-18

Immunoglobulin domain; The members here are composed of the immunoglobulin (Ig) domain found in the Ig superfamily. The Ig superfamily is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. Members of this group are components of immunoglobulin, neuroglia, cell surface glycoproteins, including T-cell receptors, CD2, CD4, CD8, and membrane glycoproteins, including butyrophilin and chondroitin sulfate proteoglycan core protein. A predominant feature of most Ig domains is a disulfide bridge connecting the two beta-sheets with a tryptophan residue packed against the disulfide bond. Ig superfamily (IgSF) domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. Typically, the V-set domains have A, B, E, and D strands in one sheet and A', G, F, C, C' and C" in the other. The structures in C1-set are smaller than those in the V-set; they have one beta sheet that is formed by strands A, B, E, and D and the other by strands G, F, C, and C'. Moreover, a C1-set Ig domain contains a short C' strand (three residues) and lacks A' and C" strand. Unlike other Ig domain sets, C2-set structures do not have a D strand. Like the V-set Ig domains, members of the I-set have a discontinuous A strand, but lack a C" strand.


The actual alignment was detected with superfamily member cd05748:

Pssm-ID: 472250 [Multi-domain]  Cd Length: 82  Bit Score: 82.25  E-value: 5.47e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 5286 IKIKAGNVFEFDVPVTGEPLPSKDWTHEGNMIINTDRVKISNFDDRTKIRILDAKRSDTGVYTLTARNINGTDRHNVKVT 5365
Cdd:cd05748     2 IVVRAGESLRLDIPIKGRPTPTVTWSKDGQPLKETGRVQIETTASSTSLVIKNAKRSDSGKYTLTLKNSAGEKSATINVK 81

                  .
gi 281359561 5366 I 5366
Cdd:cd05748    82 V 82
I-set pfam07679
Immunoglobulin I-set domain;
8437-8525 9.29e-18

Immunoglobulin I-set domain;


:

Pssm-ID: 400151 [Multi-domain]  Cd Length: 90  Bit Score: 81.92  E-value: 9.29e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561  8437 PSFTFLLRPRVMQARDTCKLLCCLSGKPVPNVRWYKDGREL-SKYEYAMTHSDGVVTMEIIDCKPSDSGKYSCKATNCHG 8515
Cdd:pfam07679    1 PKFTQKPKDVEVQEGESARFTCTVTGTPDPEVSWFKDGQPLrSSDRFKVTYEGGTYTLTISNVQPDDSGKYTCVATNSAG 80
                           90
                   ....*....|
gi 281359561  8516 TDETDCVVIV 8525
Cdd:pfam07679   81 EAEASAELTV 90
FN3 cd00063
Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein ...
4285-4383 1.13e-17

Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein fibronectin. Its tenth fibronectin type III repeat contains an RGD cell recognition sequence in a flexible loop between 2 strands. Approximately 2% of all animal proteins contain the FN3 repeat; including extracellular and intracellular proteins, membrane spanning cytokine receptors, growth hormone receptors, tyrosine phosphatase receptors, and adhesion molecules. FN3-like domains are also found in bacterial glycosyl hydrolases.


:

Pssm-ID: 238020 [Multi-domain]  Cd Length: 93  Bit Score: 81.77  E-value: 1.13e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 4285 PGKPGTPEAVDWDKDHVDLVWRPPiNDGGSPITGYVVEKREKGTDKWikgTEITIPClGEECKATVPTLNENCEYEFRVK 4364
Cdd:cd00063     1 PSPPTNLRVTDVTSTSVTLSWTPP-EDDGGPITGYVVEYREKGSGDW---KEVEVTP-GSETSYTLTGLKPGTEYEFRVR 75
                          90
                  ....*....|....*....
gi 281359561 4365 AINAAGPGEPSDaSKPIIT 4383
Cdd:cd00063    76 AVNGGGESPPSE-SVTVTT 93
Ig super family cl11960
Immunoglobulin domain; The members here are composed of the immunoglobulin (Ig) domain found ...
7758-7833 1.24e-17

Immunoglobulin domain; The members here are composed of the immunoglobulin (Ig) domain found in the Ig superfamily. The Ig superfamily is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. Members of this group are components of immunoglobulin, neuroglia, cell surface glycoproteins, including T-cell receptors, CD2, CD4, CD8, and membrane glycoproteins, including butyrophilin and chondroitin sulfate proteoglycan core protein. A predominant feature of most Ig domains is a disulfide bridge connecting the two beta-sheets with a tryptophan residue packed against the disulfide bond. Ig superfamily (IgSF) domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. Typically, the V-set domains have A, B, E, and D strands in one sheet and A', G, F, C, C' and C" in the other. The structures in C1-set are smaller than those in the V-set; they have one beta sheet that is formed by strands A, B, E, and D and the other by strands G, F, C, and C'. Moreover, a C1-set Ig domain contains a short C' strand (three residues) and lacks A' and C" strand. Unlike other Ig domain sets, C2-set structures do not have a D strand. Like the V-set Ig domains, members of the I-set have a discontinuous A strand, but lack a C" strand.


The actual alignment was detected with superfamily member cd05748:

Pssm-ID: 472250 [Multi-domain]  Cd Length: 82  Bit Score: 81.10  E-value: 1.24e-17
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 281359561 7758 GENVVIKIPFTGFPKPRIHWVRDGENIESGGHYTVEVKERHAVLIIRDGSHLDSGPYRITAENELGSDTAIIQVQI 7833
Cdd:cd05748     7 GESLRLDIPIKGRPTPTVTWSKDGQPLKETGRVQIETTASSTSLVIKNAKRSDSGKYTLTLKNSAGEKSATINVKV 82
Ig super family cl11960
Immunoglobulin domain; The members here are composed of the immunoglobulin (Ig) domain found ...
7254-7344 2.34e-17

Immunoglobulin domain; The members here are composed of the immunoglobulin (Ig) domain found in the Ig superfamily. The Ig superfamily is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. Members of this group are components of immunoglobulin, neuroglia, cell surface glycoproteins, including T-cell receptors, CD2, CD4, CD8, and membrane glycoproteins, including butyrophilin and chondroitin sulfate proteoglycan core protein. A predominant feature of most Ig domains is a disulfide bridge connecting the two beta-sheets with a tryptophan residue packed against the disulfide bond. Ig superfamily (IgSF) domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. Typically, the V-set domains have A, B, E, and D strands in one sheet and A', G, F, C, C' and C" in the other. The structures in C1-set are smaller than those in the V-set; they have one beta sheet that is formed by strands A, B, E, and D and the other by strands G, F, C, and C'. Moreover, a C1-set Ig domain contains a short C' strand (three residues) and lacks A' and C" strand. Unlike other Ig domain sets, C2-set structures do not have a D strand. Like the V-set Ig domains, members of the I-set have a discontinuous A strand, but lack a C" strand.


The actual alignment was detected with superfamily member cd20976:

Pssm-ID: 472250 [Multi-domain]  Cd Length: 90  Bit Score: 80.76  E-value: 2.34e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 7254 PDWITRLQDKVAPFGKDYTLQCAASGKPSPTARWLRNGKEIQMNGGRMTCDSkdGVFRLHISNVQTGDDGDYTCEAMNSL 7333
Cdd:cd20976     2 PSFSSVPKDLEAVEGQDFVAQCSARGKPVPRITWIRNAQPLQYAADRSTCEA--GVGELHIQDVLPEDHGTYTCLAKNAA 79
                          90
                  ....*....|.
gi 281359561 7334 GFVNTSGYLKI 7344
Cdd:cd20976    80 GQVSCSAWVTV 90
FN3 cd00063
Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein ...
4185-4271 5.79e-17

Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein fibronectin. Its tenth fibronectin type III repeat contains an RGD cell recognition sequence in a flexible loop between 2 strands. Approximately 2% of all animal proteins contain the FN3 repeat; including extracellular and intracellular proteins, membrane spanning cytokine receptors, growth hormone receptors, tyrosine phosphatase receptors, and adhesion molecules. FN3-like domains are also found in bacterial glycosyl hydrolases.


:

Pssm-ID: 238020 [Multi-domain]  Cd Length: 93  Bit Score: 79.85  E-value: 5.79e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 4185 PGPPEGpLRVTDVHKEGCKLKWNAPLDDGGlPIDHYIIEKMDVESGRW--LPSGRFKESFAELNNLEPSHEYKFRVLAVN 4262
Cdd:cd00063     1 PSPPTN-LRVTDVTSTSVTLSWTPPEDDGG-PITGYVVEYREKGSGDWkeVEVTPGSETSYTLTGLKPGTEYEFRVRAVN 78

                  ....*....
gi 281359561 4263 TEGESEPLT 4271
Cdd:cd00063    79 GGGESPPSE 87
I-set pfam07679
Immunoglobulin I-set domain;
119-210 6.70e-17

Immunoglobulin I-set domain;


:

Pssm-ID: 400151 [Multi-domain]  Cd Length: 90  Bit Score: 79.22  E-value: 6.70e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561   119 PTFAKKP--AIRQEedGKRLLFECRVNADPIPAIIWFHNGAAVKESERHKITVDKDVHsyfaTLEILNVTVEDAGKYKVN 196
Cdd:pfam07679    1 PKFTQKPkdVEVQE--GESARFTCTVTGTPDPEVSWFKDGQPLRSSDRFKVTYEGGTY----TLTISNVQPDDSGKYTCV 74
                           90
                   ....*....|....
gi 281359561   197 AKNELGESNATISL 210
Cdd:pfam07679   75 ATNSAGEAEASAEL 88
FN3 cd00063
Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein ...
3594-3682 8.89e-17

Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein fibronectin. Its tenth fibronectin type III repeat contains an RGD cell recognition sequence in a flexible loop between 2 strands. Approximately 2% of all animal proteins contain the FN3 repeat; including extracellular and intracellular proteins, membrane spanning cytokine receptors, growth hormone receptors, tyrosine phosphatase receptors, and adhesion molecules. FN3-like domains are also found in bacterial glycosyl hydrolases.


:

Pssm-ID: 238020 [Multi-domain]  Cd Length: 93  Bit Score: 79.08  E-value: 8.89e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 3594 PGKPKGpLQVNDITKHSCKLKWEKPDDDGGsPIDYYEIEKLDPHTGQWLPCGK--STEPEAKVIGLHEGKAYKFRVRAVN 3671
Cdd:cd00063     1 PSPPTN-LRVTDVTSTSVTLSWTPPEDDGG-PITGYVVEYREKGSGDWKEVEVtpGSETSYTLTGLKPGTEYEFRVRAVN 78
                          90
                  ....*....|.
gi 281359561 3672 KEGESEDLETE 3682
Cdd:cd00063    79 GGGESPPSESV 89
Ig super family cl11960
Immunoglobulin domain; The members here are composed of the immunoglobulin (Ig) domain found ...
3212-3292 1.35e-16

Immunoglobulin domain; The members here are composed of the immunoglobulin (Ig) domain found in the Ig superfamily. The Ig superfamily is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. Members of this group are components of immunoglobulin, neuroglia, cell surface glycoproteins, including T-cell receptors, CD2, CD4, CD8, and membrane glycoproteins, including butyrophilin and chondroitin sulfate proteoglycan core protein. A predominant feature of most Ig domains is a disulfide bridge connecting the two beta-sheets with a tryptophan residue packed against the disulfide bond. Ig superfamily (IgSF) domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. Typically, the V-set domains have A, B, E, and D strands in one sheet and A', G, F, C, C' and C" in the other. The structures in C1-set are smaller than those in the V-set; they have one beta sheet that is formed by strands A, B, E, and D and the other by strands G, F, C, and C'. Moreover, a C1-set Ig domain contains a short C' strand (three residues) and lacks A' and C" strand. Unlike other Ig domain sets, C2-set structures do not have a D strand. Like the V-set Ig domains, members of the I-set have a discontinuous A strand, but lack a C" strand.


The actual alignment was detected with superfamily member cd05748:

Pssm-ID: 472250 [Multi-domain]  Cd Length: 82  Bit Score: 78.02  E-value: 1.35e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 3212 IKVRAGQPVKFDVDVKGEPAPSLTWFLKETELTSTGQVRLENIDYNTKLTLLDTDRKQSGQYKLRAENINGVDEAVVEVI 3291
Cdd:cd05748     2 IVVRAGESLRLDIPIKGRPTPTVTWSKDGQPLKETGRVQIETTASSTSLVIKNAKRSDSGKYTLTLKNSAGEKSATINVK 81

                  .
gi 281359561 3292 I 3292
Cdd:cd05748    82 V 82
FN3 cd00063
Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein ...
2100-2194 2.28e-16

Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein fibronectin. Its tenth fibronectin type III repeat contains an RGD cell recognition sequence in a flexible loop between 2 strands. Approximately 2% of all animal proteins contain the FN3 repeat; including extracellular and intracellular proteins, membrane spanning cytokine receptors, growth hormone receptors, tyrosine phosphatase receptors, and adhesion molecules. FN3-like domains are also found in bacterial glycosyl hydrolases.


:

Pssm-ID: 238020 [Multi-domain]  Cd Length: 93  Bit Score: 77.92  E-value: 2.28e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 2100 PQPPQDVDITDVYQTSCVVSFNPPSDDGGtPITKYVIERQDLSKKhGWESVAEVLPSEPCLKkIDDLIPKKQYRFRIRAV 2179
Cdd:cd00063     1 PSPPTNLRVTDVTSTSVTLSWTPPEDDGG-PITGYVVEYREKGSG-DWKEVEVTPGSETSYT-LTGLKPGTEYEFRVRAV 77
                          90
                  ....*....|....*
gi 281359561 2180 NAIGQSDPATFKNTI 2194
Cdd:cd00063    78 NGGGESPPSESVTVT 92
FN3 cd00063
Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein ...
7837-7927 5.43e-16

Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein fibronectin. Its tenth fibronectin type III repeat contains an RGD cell recognition sequence in a flexible loop between 2 strands. Approximately 2% of all animal proteins contain the FN3 repeat; including extracellular and intracellular proteins, membrane spanning cytokine receptors, growth hormone receptors, tyrosine phosphatase receptors, and adhesion molecules. FN3-like domains are also found in bacterial glycosyl hydrolases.


:

Pssm-ID: 238020 [Multi-domain]  Cd Length: 93  Bit Score: 76.77  E-value: 5.43e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 7837 PDPPRFPLIESIGTESLSLSWKAPVWDGcSDITNYYVERREHPLSSWIRVGNTRF--TSMAVSGLTPGKEYDFRIFADNV 7914
Cdd:cd00063     1 PSPPTNLRVTDVTSTSVTLSWTPPEDDG-GPITGYVVEYREKGSGDWKEVEVTPGseTSYTLTGLKPGTEYEFRVRAVNG 79
                          90
                  ....*....|...
gi 281359561 7915 YGRSDASDTSTLI 7927
Cdd:cd00063    80 GGESPPSESVTVT 92
I-set pfam07679
Immunoglobulin I-set domain;
3795-3885 1.17e-15

Immunoglobulin I-set domain;


:

Pssm-ID: 400151 [Multi-domain]  Cd Length: 90  Bit Score: 75.76  E-value: 1.17e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561  3795 PHIDRKnLQKKIMRSGQMLHIDALIKAEPPAKVTWTYNKTEIKTSDHIKIENEDYKTTFIMPKVKRADRGIYIVTAKNDS 3874
Cdd:pfam07679    1 PKFTQK-PKDVEVQEGESARFTCTVTGTPDPEVSWFKDGQPLRSSDRFKVTYEGGTYTLTISNVQPDDSGKYTCVATNSA 79
                           90
                   ....*....|.
gi 281359561  3875 GSDTVEVELEV 3885
Cdd:pfam07679   80 GEAEASAELTV 90
Ig super family cl11960
Immunoglobulin domain; The members here are composed of the immunoglobulin (Ig) domain found ...
2314-2395 1.53e-14

Immunoglobulin domain; The members here are composed of the immunoglobulin (Ig) domain found in the Ig superfamily. The Ig superfamily is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. Members of this group are components of immunoglobulin, neuroglia, cell surface glycoproteins, including T-cell receptors, CD2, CD4, CD8, and membrane glycoproteins, including butyrophilin and chondroitin sulfate proteoglycan core protein. A predominant feature of most Ig domains is a disulfide bridge connecting the two beta-sheets with a tryptophan residue packed against the disulfide bond. Ig superfamily (IgSF) domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. Typically, the V-set domains have A, B, E, and D strands in one sheet and A', G, F, C, C' and C" in the other. The structures in C1-set are smaller than those in the V-set; they have one beta sheet that is formed by strands A, B, E, and D and the other by strands G, F, C, and C'. Moreover, a C1-set Ig domain contains a short C' strand (three residues) and lacks A' and C" strand. Unlike other Ig domain sets, C2-set structures do not have a D strand. Like the V-set Ig domains, members of the I-set have a discontinuous A strand, but lack a C" strand.


The actual alignment was detected with superfamily member cd05748:

Pssm-ID: 472250 [Multi-domain]  Cd Length: 82  Bit Score: 72.24  E-value: 1.53e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 2314 VTVKKGQTIRFDIKYDGEPEPAATWVKGTDNLKfDNQRICLDQLERNSSITIKKSVRKDTGKYKLVLSNSSGTIESEAQV 2393
Cdd:cd05748     2 IVVRAGESLRLDIPIKGRPTPTVTWSKDGQPLK-ETGRVQIETTASSTSLVIKNAKRSDSGKYTLTLKNSAGEKSATINV 80

                  ..
gi 281359561 2394 VV 2395
Cdd:cd05748    81 KV 82
Ig super family cl11960
Immunoglobulin domain; The members here are composed of the immunoglobulin (Ig) domain found ...
228-320 6.42e-14

Immunoglobulin domain; The members here are composed of the immunoglobulin (Ig) domain found in the Ig superfamily. The Ig superfamily is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. Members of this group are components of immunoglobulin, neuroglia, cell surface glycoproteins, including T-cell receptors, CD2, CD4, CD8, and membrane glycoproteins, including butyrophilin and chondroitin sulfate proteoglycan core protein. A predominant feature of most Ig domains is a disulfide bridge connecting the two beta-sheets with a tryptophan residue packed against the disulfide bond. Ig superfamily (IgSF) domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. Typically, the V-set domains have A, B, E, and D strands in one sheet and A', G, F, C, C' and C" in the other. The structures in C1-set are smaller than those in the V-set; they have one beta sheet that is formed by strands A, B, E, and D and the other by strands G, F, C, and C'. Moreover, a C1-set Ig domain contains a short C' strand (three residues) and lacks A' and C" strand. Unlike other Ig domain sets, C2-set structures do not have a D strand. Like the V-set Ig domains, members of the I-set have a discontinuous A strand, but lack a C" strand.


The actual alignment was detected with superfamily member pfam07679:

Pssm-ID: 472250 [Multi-domain]  Cd Length: 90  Bit Score: 70.75  E-value: 6.42e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561   228 PTFTERPVIRQSEDGGNVTFECRCVGDPTPTVTWSHGETELNESNRYKMslTMDQKLYHiacLEISSVVSSDQGEYRAQA 307
Cdd:pfam07679    1 PKFTQKPKDVEVQEGESARFTCTVTGTPDPEVSWFKDGQPLRSSDRFKV--TYEGGTYT---LTISNVQPDDSGKYTCVA 75
                           90
                   ....*....|...
gi 281359561   308 KNKHGSGVATINL 320
Cdd:pfam07679   76 TNSAGEAEASAEL 88
FN3 cd00063
Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein ...
4779-4863 6.74e-14

Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein fibronectin. Its tenth fibronectin type III repeat contains an RGD cell recognition sequence in a flexible loop between 2 strands. Approximately 2% of all animal proteins contain the FN3 repeat; including extracellular and intracellular proteins, membrane spanning cytokine receptors, growth hormone receptors, tyrosine phosphatase receptors, and adhesion molecules. FN3-like domains are also found in bacterial glycosyl hydrolases.


:

Pssm-ID: 238020 [Multi-domain]  Cd Length: 93  Bit Score: 70.99  E-value: 6.74e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 4779 PSPPNGpLQISDVHKEGCHLKWKRPSDDGGTPIEYF-QIDKLEPETGCWIPSCRSTEPQVDVTGLSPGNEYKFRVSAVNA 4857
Cdd:cd00063     1 PSPPTN-LRVTDVTSTSVTLSWTPPEDDGGPITGYVvEYREKGSGDWKEVEVTPGSETSYTLTGLKPGTEYEFRVRAVNG 79

                  ....*.
gi 281359561 4858 EGESQP 4863
Cdd:cd00063    80 GGESPP 85
FN3 cd00063
Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein ...
5664-5755 9.11e-14

Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein fibronectin. Its tenth fibronectin type III repeat contains an RGD cell recognition sequence in a flexible loop between 2 strands. Approximately 2% of all animal proteins contain the FN3 repeat; including extracellular and intracellular proteins, membrane spanning cytokine receptors, growth hormone receptors, tyrosine phosphatase receptors, and adhesion molecules. FN3-like domains are also found in bacterial glycosyl hydrolases.


:

Pssm-ID: 238020 [Multi-domain]  Cd Length: 93  Bit Score: 70.60  E-value: 9.11e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 5664 PSPPKGpLDITKITRDGCHLTWNVPDDDGGsPILHYIIEKMDLSRSTWS--DAGMSTHIVHDVTRLVHRKEYLFRVKAVN 5741
Cdd:cd00063     1 PSPPTN-LRVTDVTSTSVTLSWTPPEDDGG-PITGYVVEYREKGSGDWKevEVTPGSETSYTLTGLKPGTEYEFRVRAVN 78
                          90
                  ....*....|....
gi 281359561 5742 AIGESDPLEAVNTI 5755
Cdd:cd00063    79 GGGESPPSESVTVT 92
Ig super family cl11960
Immunoglobulin domain; The members here are composed of the immunoglobulin (Ig) domain found ...
545-636 1.31e-13

Immunoglobulin domain; The members here are composed of the immunoglobulin (Ig) domain found in the Ig superfamily. The Ig superfamily is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. Members of this group are components of immunoglobulin, neuroglia, cell surface glycoproteins, including T-cell receptors, CD2, CD4, CD8, and membrane glycoproteins, including butyrophilin and chondroitin sulfate proteoglycan core protein. A predominant feature of most Ig domains is a disulfide bridge connecting the two beta-sheets with a tryptophan residue packed against the disulfide bond. Ig superfamily (IgSF) domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. Typically, the V-set domains have A, B, E, and D strands in one sheet and A', G, F, C, C' and C" in the other. The structures in C1-set are smaller than those in the V-set; they have one beta sheet that is formed by strands A, B, E, and D and the other by strands G, F, C, and C'. Moreover, a C1-set Ig domain contains a short C' strand (three residues) and lacks A' and C" strand. Unlike other Ig domain sets, C2-set structures do not have a D strand. Like the V-set Ig domains, members of the I-set have a discontinuous A strand, but lack a C" strand.


The actual alignment was detected with superfamily member pfam07679:

Pssm-ID: 472250 [Multi-domain]  Cd Length: 90  Bit Score: 69.98  E-value: 1.31e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561   545 FIEKPRIVSENNGKLVIMECKVKADPKPDVIWFRNGEVIKESNKIKtfIEQRGDQYyiKLELLDPQLEDSGLYKCNIKNT 624
Cdd:pfam07679    3 FTQKPKDVEVQEGESARFTCTVTGTPDPEVSWFKDGQPLRSSDRFK--VTYEGGTY--TLTISNVQPDDSGKYTCVATNS 78
                           90
                   ....*....|..
gi 281359561   625 LGELNANLTLNI 636
Cdd:pfam07679   79 AGEAEASAELTV 90
Ig super family cl11960
Immunoglobulin domain; The members here are composed of the immunoglobulin (Ig) domain found ...
5874-5954 6.36e-13

Immunoglobulin domain; The members here are composed of the immunoglobulin (Ig) domain found in the Ig superfamily. The Ig superfamily is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. Members of this group are components of immunoglobulin, neuroglia, cell surface glycoproteins, including T-cell receptors, CD2, CD4, CD8, and membrane glycoproteins, including butyrophilin and chondroitin sulfate proteoglycan core protein. A predominant feature of most Ig domains is a disulfide bridge connecting the two beta-sheets with a tryptophan residue packed against the disulfide bond. Ig superfamily (IgSF) domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. Typically, the V-set domains have A, B, E, and D strands in one sheet and A', G, F, C, C' and C" in the other. The structures in C1-set are smaller than those in the V-set; they have one beta sheet that is formed by strands A, B, E, and D and the other by strands G, F, C, and C'. Moreover, a C1-set Ig domain contains a short C' strand (three residues) and lacks A' and C" strand. Unlike other Ig domain sets, C2-set structures do not have a D strand. Like the V-set Ig domains, members of the I-set have a discontinuous A strand, but lack a C" strand.


The actual alignment was detected with superfamily member cd05748:

Pssm-ID: 472250 [Multi-domain]  Cd Length: 82  Bit Score: 67.61  E-value: 6.36e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 5874 VRIKCGLIFHTDIHFIGEPAPEATWTLNSNPLLSNDRSTITSIGHHSVVHTVNCQRSDSGIYHLLLRNSSGIDEGSFELV 5953
Cdd:cd05748     2 IVVRAGESLRLDIPIKGRPTPTVTWSKDGQPLKETGRVQIETTASSTSLVIKNAKRSDSGKYTLTLKNSAGEKSATINVK 81

                  .
gi 281359561 5954 V 5954
Cdd:cd05748    82 V 82
Ig super family cl11960
Immunoglobulin domain; The members here are composed of the immunoglobulin (Ig) domain found ...
2902-2995 2.79e-12

Immunoglobulin domain; The members here are composed of the immunoglobulin (Ig) domain found in the Ig superfamily. The Ig superfamily is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. Members of this group are components of immunoglobulin, neuroglia, cell surface glycoproteins, including T-cell receptors, CD2, CD4, CD8, and membrane glycoproteins, including butyrophilin and chondroitin sulfate proteoglycan core protein. A predominant feature of most Ig domains is a disulfide bridge connecting the two beta-sheets with a tryptophan residue packed against the disulfide bond. Ig superfamily (IgSF) domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. Typically, the V-set domains have A, B, E, and D strands in one sheet and A', G, F, C, C' and C" in the other. The structures in C1-set are smaller than those in the V-set; they have one beta sheet that is formed by strands A, B, E, and D and the other by strands G, F, C, and C'. Moreover, a C1-set Ig domain contains a short C' strand (three residues) and lacks A' and C" strand. Unlike other Ig domain sets, C2-set structures do not have a D strand. Like the V-set Ig domains, members of the I-set have a discontinuous A strand, but lack a C" strand.


The actual alignment was detected with superfamily member pfam07679:

Pssm-ID: 472250 [Multi-domain]  Cd Length: 90  Bit Score: 66.13  E-value: 2.79e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561  2902 PRIDRSnLKPLLIRAGKPIRYDVNVRGEPAPVITWYQNDKELKPEelpSSSEIKNIPYNTKISIIETVRKHTGIYKIIAV 2981
Cdd:pfam07679    1 PKFTQK-PKDVEVQEGESARFTCTVTGTPDPEVSWFKDGQPLRSS---DRFKVTYEGGTYTLTISNVQPDDSGKYTCVAT 76
                           90
                   ....*....|....
gi 281359561  2982 NEHGQDEATVEVNI 2995
Cdd:pfam07679   77 NSAGEAEASAELTV 90
Ig super family cl11960
Immunoglobulin domain; The members here are composed of the immunoglobulin (Ig) domain found ...
8839-8922 1.07e-11

Immunoglobulin domain; The members here are composed of the immunoglobulin (Ig) domain found in the Ig superfamily. The Ig superfamily is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. Members of this group are components of immunoglobulin, neuroglia, cell surface glycoproteins, including T-cell receptors, CD2, CD4, CD8, and membrane glycoproteins, including butyrophilin and chondroitin sulfate proteoglycan core protein. A predominant feature of most Ig domains is a disulfide bridge connecting the two beta-sheets with a tryptophan residue packed against the disulfide bond. Ig superfamily (IgSF) domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. Typically, the V-set domains have A, B, E, and D strands in one sheet and A', G, F, C, C' and C" in the other. The structures in C1-set are smaller than those in the V-set; they have one beta sheet that is formed by strands A, B, E, and D and the other by strands G, F, C, and C'. Moreover, a C1-set Ig domain contains a short C' strand (three residues) and lacks A' and C" strand. Unlike other Ig domain sets, C2-set structures do not have a D strand. Like the V-set Ig domains, members of the I-set have a discontinuous A strand, but lack a C" strand.


The actual alignment was detected with superfamily member pfam07679:

Pssm-ID: 472250 [Multi-domain]  Cd Length: 90  Bit Score: 64.59  E-value: 1.07e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561  8839 PSFVKFPTSVSVLEGEGTTFECEID-SELLNLVWLKDGKPIDETlPRYSFTKDGHRYSFAVAKCNMDDVGQYQAKAV--S 8915
Cdd:pfam07679    1 PKFTQKPKDVEVQEGESARFTCTVTgTPDPEVSWFKDGQPLRSS-DRFKVTYEGGTYTLTISNVQPDDSGKYTCVATnsA 79

                   ....*..
gi 281359561  8916 GKAESIC 8922
Cdd:pfam07679   80 GEAEASA 86
Ig super family cl11960
Immunoglobulin domain; The members here are composed of the immunoglobulin (Ig) domain found ...
9-101 2.06e-11

Immunoglobulin domain; The members here are composed of the immunoglobulin (Ig) domain found in the Ig superfamily. The Ig superfamily is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. Members of this group are components of immunoglobulin, neuroglia, cell surface glycoproteins, including T-cell receptors, CD2, CD4, CD8, and membrane glycoproteins, including butyrophilin and chondroitin sulfate proteoglycan core protein. A predominant feature of most Ig domains is a disulfide bridge connecting the two beta-sheets with a tryptophan residue packed against the disulfide bond. Ig superfamily (IgSF) domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. Typically, the V-set domains have A, B, E, and D strands in one sheet and A', G, F, C, C' and C" in the other. The structures in C1-set are smaller than those in the V-set; they have one beta sheet that is formed by strands A, B, E, and D and the other by strands G, F, C, and C'. Moreover, a C1-set Ig domain contains a short C' strand (three residues) and lacks A' and C" strand. Unlike other Ig domain sets, C2-set structures do not have a D strand. Like the V-set Ig domains, members of the I-set have a discontinuous A strand, but lack a C" strand.


The actual alignment was detected with superfamily member pfam07679:

Pssm-ID: 472250 [Multi-domain]  Cd Length: 90  Bit Score: 63.82  E-value: 2.06e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561     9 PSFVKKPQLHQEDDGNRLIFECQLLSSPKPDIEWFRSDNKVVEDVRtkFKIQPVGeNKYTvvLELDDVVETDAGLYKVKA 88
Cdd:pfam07679    1 PKFTQKPKDVEVQEGESARFTCTVTGTPDPEVSWFKDGQPLRSSDR--FKVTYEG-GTYT--LTISNVQPDDSGKYTCVA 75
                           90
                   ....*....|...
gi 281359561    89 KNKSGEVSASINL 101
Cdd:pfam07679   76 TNSAGEAEASAEL 88
Ig super family cl11960
Immunoglobulin domain; The members here are composed of the immunoglobulin (Ig) domain found ...
438-532 4.11e-11

Immunoglobulin domain; The members here are composed of the immunoglobulin (Ig) domain found in the Ig superfamily. The Ig superfamily is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. Members of this group are components of immunoglobulin, neuroglia, cell surface glycoproteins, including T-cell receptors, CD2, CD4, CD8, and membrane glycoproteins, including butyrophilin and chondroitin sulfate proteoglycan core protein. A predominant feature of most Ig domains is a disulfide bridge connecting the two beta-sheets with a tryptophan residue packed against the disulfide bond. Ig superfamily (IgSF) domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. Typically, the V-set domains have A, B, E, and D strands in one sheet and A', G, F, C, C' and C" in the other. The structures in C1-set are smaller than those in the V-set; they have one beta sheet that is formed by strands A, B, E, and D and the other by strands G, F, C, and C'. Moreover, a C1-set Ig domain contains a short C' strand (three residues) and lacks A' and C" strand. Unlike other Ig domain sets, C2-set structures do not have a D strand. Like the V-set Ig domains, members of the I-set have a discontinuous A strand, but lack a C" strand.


The actual alignment was detected with superfamily member pfam07679:

Pssm-ID: 472250 [Multi-domain]  Cd Length: 90  Bit Score: 63.05  E-value: 4.11e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561   438 PSFIEKPRIIPNESGTLITMKCKCKAKPEPTVTWYRGQDLVEKSKKIKInttviAEDTYELTLEIKDPGATDGGTYRCNV 517
Cdd:pfam07679    1 PKFTQKPKDVEVQEGESARFTCTVTGTPDPEVSWFKDGQPLRSSDRFKV-----TYEGGTYTLTISNVQPDDSGKYTCVA 75
                           90
                   ....*....|....*
gi 281359561   518 KNEYGESNANLNLNI 532
Cdd:pfam07679   76 TNSAGEAEASAELTV 90
Ig_3 pfam13927
Immunoglobulin domain; This family contains immunoglobulin-like domains.
4978-5056 6.99e-11

Immunoglobulin domain; This family contains immunoglobulin-like domains.


:

Pssm-ID: 464046 [Multi-domain]  Cd Length: 78  Bit Score: 61.81  E-value: 6.99e-11
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 281359561  4978 PPIIdRSSLVEVRIKAGQSFTFDCKVSGEPAPQTKWLLKKKEVYSKDNVKVTNVDYNTKLKVNSATRSDSGIYTVFAEN 5056
Cdd:pfam13927    1 KPVI-TVSPSSVTVREGETVTLTCEATGSPPPTITWYKNGEPISSGSTRSRSLSGSNSTLTISNVTRSDAGTYTCVASN 78
Ig super family cl11960
Immunoglobulin domain; The members here are composed of the immunoglobulin (Ig) domain found ...
1826-1909 8.13e-11

Immunoglobulin domain; The members here are composed of the immunoglobulin (Ig) domain found in the Ig superfamily. The Ig superfamily is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. Members of this group are components of immunoglobulin, neuroglia, cell surface glycoproteins, including T-cell receptors, CD2, CD4, CD8, and membrane glycoproteins, including butyrophilin and chondroitin sulfate proteoglycan core protein. A predominant feature of most Ig domains is a disulfide bridge connecting the two beta-sheets with a tryptophan residue packed against the disulfide bond. Ig superfamily (IgSF) domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. Typically, the V-set domains have A, B, E, and D strands in one sheet and A', G, F, C, C' and C" in the other. The structures in C1-set are smaller than those in the V-set; they have one beta sheet that is formed by strands A, B, E, and D and the other by strands G, F, C, and C'. Moreover, a C1-set Ig domain contains a short C' strand (three residues) and lacks A' and C" strand. Unlike other Ig domain sets, C2-set structures do not have a D strand. Like the V-set Ig domains, members of the I-set have a discontinuous A strand, but lack a C" strand.


The actual alignment was detected with superfamily member pfam07679:

Pssm-ID: 472250 [Multi-domain]  Cd Length: 90  Bit Score: 61.89  E-value: 8.13e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561  1826 KFVKVLKSQQCIEKDTVTLACEIddaMG----EVQWLRNGEEIKPDKRIQIVKDGRKRKLVIKDCKVTDAGQFKCT-TNA 1900
Cdd:pfam07679    2 KFTQKPKDVEVQEGESARFTCTV---TGtpdpEVSWFKDGQPLRSSDRFKVTYEGGTYTLTISNVQPDDSGKYTCVaTNS 78
                           90
                   ....*....|..
gi 281359561  1901 ---DTTESEIII 1909
Cdd:pfam07679   79 ageAEASAELTV 90
Ig super family cl11960
Immunoglobulin domain; The members here are composed of the immunoglobulin (Ig) domain found ...
1508-1588 9.98e-11

Immunoglobulin domain; The members here are composed of the immunoglobulin (Ig) domain found in the Ig superfamily. The Ig superfamily is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. Members of this group are components of immunoglobulin, neuroglia, cell surface glycoproteins, including T-cell receptors, CD2, CD4, CD8, and membrane glycoproteins, including butyrophilin and chondroitin sulfate proteoglycan core protein. A predominant feature of most Ig domains is a disulfide bridge connecting the two beta-sheets with a tryptophan residue packed against the disulfide bond. Ig superfamily (IgSF) domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. Typically, the V-set domains have A, B, E, and D strands in one sheet and A', G, F, C, C' and C" in the other. The structures in C1-set are smaller than those in the V-set; they have one beta sheet that is formed by strands A, B, E, and D and the other by strands G, F, C, and C'. Moreover, a C1-set Ig domain contains a short C' strand (three residues) and lacks A' and C" strand. Unlike other Ig domain sets, C2-set structures do not have a D strand. Like the V-set Ig domains, members of the I-set have a discontinuous A strand, but lack a C" strand.


The actual alignment was detected with superfamily member pfam07679:

Pssm-ID: 472250 [Multi-domain]  Cd Length: 90  Bit Score: 61.89  E-value: 9.98e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561  1508 VVEDSTAYLTVGVEGSPAPTFKFYKGVSEILEGGRFKFLTDGQTNTITlcMRKCKPNDESKYKIVVSNIHGEDSAEMQLY 1587
Cdd:pfam07679   12 VQEGESARFTCTVTGTPDPEVSWFKDGQPLRSSDRFKVTYEGGTYTLT--ISNVQPDDSGKYTCVATNSAGEAEASAELT 89

                   .
gi 281359561  1588 V 1588
Cdd:pfam07679   90 V 90
Ig super family cl11960
Immunoglobulin domain; The members here are composed of the immunoglobulin (Ig) domain found ...
335-425 7.81e-10

Immunoglobulin domain; The members here are composed of the immunoglobulin (Ig) domain found in the Ig superfamily. The Ig superfamily is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. Members of this group are components of immunoglobulin, neuroglia, cell surface glycoproteins, including T-cell receptors, CD2, CD4, CD8, and membrane glycoproteins, including butyrophilin and chondroitin sulfate proteoglycan core protein. A predominant feature of most Ig domains is a disulfide bridge connecting the two beta-sheets with a tryptophan residue packed against the disulfide bond. Ig superfamily (IgSF) domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. Typically, the V-set domains have A, B, E, and D strands in one sheet and A', G, F, C, C' and C" in the other. The structures in C1-set are smaller than those in the V-set; they have one beta sheet that is formed by strands A, B, E, and D and the other by strands G, F, C, and C'. Moreover, a C1-set Ig domain contains a short C' strand (three residues) and lacks A' and C" strand. Unlike other Ig domain sets, C2-set structures do not have a D strand. Like the V-set Ig domains, members of the I-set have a discontinuous A strand, but lack a C" strand.


The actual alignment was detected with superfamily member pfam07679:

Pssm-ID: 472250 [Multi-domain]  Cd Length: 90  Bit Score: 59.19  E-value: 7.81e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561   335 PRFPKKP--TIRQEEDLLIMECVLEAHPVPDIVWYCSEKEICNNQRTKMTrkaitKDSYILTLEIQNPTKEDGGNYRCNA 412
Cdd:pfam07679    1 PKFTQKPkdVEVQEGESARFTCTVTGTPDPEVSWFKDGQPLRSSDRFKVT-----YEGGTYTLTISNVQPDDSGKYTCVA 75
                           90
                   ....*....|...
gi 281359561   413 INMYGESNANIAL 425
Cdd:pfam07679   76 TNSAGEAEASAEL 88
Ig super family cl11960
Immunoglobulin domain; The members here are composed of the immunoglobulin (Ig) domain found ...
5559-5654 3.69e-09

Immunoglobulin domain; The members here are composed of the immunoglobulin (Ig) domain found in the Ig superfamily. The Ig superfamily is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. Members of this group are components of immunoglobulin, neuroglia, cell surface glycoproteins, including T-cell receptors, CD2, CD4, CD8, and membrane glycoproteins, including butyrophilin and chondroitin sulfate proteoglycan core protein. A predominant feature of most Ig domains is a disulfide bridge connecting the two beta-sheets with a tryptophan residue packed against the disulfide bond. Ig superfamily (IgSF) domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. Typically, the V-set domains have A, B, E, and D strands in one sheet and A', G, F, C, C' and C" in the other. The structures in C1-set are smaller than those in the V-set; they have one beta sheet that is formed by strands A, B, E, and D and the other by strands G, F, C, and C'. Moreover, a C1-set Ig domain contains a short C' strand (three residues) and lacks A' and C" strand. Unlike other Ig domain sets, C2-set structures do not have a D strand. Like the V-set Ig domains, members of the I-set have a discontinuous A strand, but lack a C" strand.


The actual alignment was detected with superfamily member cd05747:

Pssm-ID: 472250 [Multi-domain]  Cd Length: 92  Bit Score: 57.37  E-value: 3.69e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 5559 STIICKPRflapffdksllnDITVHAGKRLGWTLPIEASPRPLITWLYNGKEIGSNSRGESGLFQNELTFEIVSSLRSDE 5638
Cdd:cd05747     4 ATILTKPR------------SLTVSEGESARFSCDVDGEPAPTVTWMREGQIIVSSQRHQITSTEYKSTFEISKVQMSDE 71
                          90
                  ....*....|....*.
gi 281359561 5639 GRYTLILKNEHGSFDA 5654
Cdd:cd05747    72 GNYTVVVENSEGKQEA 87
Ig super family cl11960
Immunoglobulin domain; The members here are composed of the immunoglobulin (Ig) domain found ...
746-835 1.10e-08

Immunoglobulin domain; The members here are composed of the immunoglobulin (Ig) domain found in the Ig superfamily. The Ig superfamily is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. Members of this group are components of immunoglobulin, neuroglia, cell surface glycoproteins, including T-cell receptors, CD2, CD4, CD8, and membrane glycoproteins, including butyrophilin and chondroitin sulfate proteoglycan core protein. A predominant feature of most Ig domains is a disulfide bridge connecting the two beta-sheets with a tryptophan residue packed against the disulfide bond. Ig superfamily (IgSF) domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. Typically, the V-set domains have A, B, E, and D strands in one sheet and A', G, F, C, C' and C" in the other. The structures in C1-set are smaller than those in the V-set; they have one beta sheet that is formed by strands A, B, E, and D and the other by strands G, F, C, and C'. Moreover, a C1-set Ig domain contains a short C' strand (three residues) and lacks A' and C" strand. Unlike other Ig domain sets, C2-set structures do not have a D strand. Like the V-set Ig domains, members of the I-set have a discontinuous A strand, but lack a C" strand.


The actual alignment was detected with superfamily member pfam07679:

Pssm-ID: 472250 [Multi-domain]  Cd Length: 90  Bit Score: 56.11  E-value: 1.10e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561   746 PEISRKLADQKVAESKTFELlvslsqtdrKCK--------VEWYKGSTVIRETKDITTTFDGTTARLTFSSARTEHTSNY 817
Cdd:pfam07679    1 PKFTQKPKDVEVQEGESARF---------TCTvtgtpdpeVSWFKDGQPLRSSDRFKVTYEGGTYTLTISNVQPDDSGKY 71
                           90
                   ....*....|....*...
gi 281359561   818 KVIVTNEVGKDESSCKIT 835
Cdd:pfam07679   72 TCVATNSAGEAEASAELT 89
IG_like smart00410
Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.
1750-1821 4.54e-08

Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.


:

Pssm-ID: 214653 [Multi-domain]  Cd Length: 85  Bit Score: 54.05  E-value: 4.54e-08
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 281359561   1750 TLECSVSSS-MANVHWFKNNTKLESDDPRYLISKDiNGNLKLIIKDSVLDDAGLYRCQLDKQPDKTECNLKVT 1821
Cdd:smart00410   13 TLSCEASGSpPPEVTWYKQGGKLLAESGRFSVSRS-GSTSTLTISNVTPEDSGTYTCAATNSSGSASSGTTLT 84
Ig super family cl11960
Immunoglobulin domain; The members here are composed of the immunoglobulin (Ig) domain found ...
656-726 1.01e-07

Immunoglobulin domain; The members here are composed of the immunoglobulin (Ig) domain found in the Ig superfamily. The Ig superfamily is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. Members of this group are components of immunoglobulin, neuroglia, cell surface glycoproteins, including T-cell receptors, CD2, CD4, CD8, and membrane glycoproteins, including butyrophilin and chondroitin sulfate proteoglycan core protein. A predominant feature of most Ig domains is a disulfide bridge connecting the two beta-sheets with a tryptophan residue packed against the disulfide bond. Ig superfamily (IgSF) domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. Typically, the V-set domains have A, B, E, and D strands in one sheet and A', G, F, C, C' and C" in the other. The structures in C1-set are smaller than those in the V-set; they have one beta sheet that is formed by strands A, B, E, and D and the other by strands G, F, C, and C'. Moreover, a C1-set Ig domain contains a short C' strand (three residues) and lacks A' and C" strand. Unlike other Ig domain sets, C2-set structures do not have a D strand. Like the V-set Ig domains, members of the I-set have a discontinuous A strand, but lack a C" strand.


The actual alignment was detected with superfamily member pfam07679:

Pssm-ID: 472250 [Multi-domain]  Cd Length: 90  Bit Score: 53.42  E-value: 1.01e-07
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 281359561   656 TVVIECTVASKFEPKCTWYKETSTVKESKRHVYQVEqtkegEFAVKLEINDVEESDKGAYKLVASNEKGEA 726
Cdd:pfam07679   17 SARFTCTVTGTPDPEVSWFKDGQPLRSSDRFKVTYE-----GGTYTLTISNVQPDDSGKYTCVATNSAGEA 82
Ig super family cl11960
Immunoglobulin domain; The members here are composed of the immunoglobulin (Ig) domain found ...
1639-1724 2.18e-06

Immunoglobulin domain; The members here are composed of the immunoglobulin (Ig) domain found in the Ig superfamily. The Ig superfamily is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. Members of this group are components of immunoglobulin, neuroglia, cell surface glycoproteins, including T-cell receptors, CD2, CD4, CD8, and membrane glycoproteins, including butyrophilin and chondroitin sulfate proteoglycan core protein. A predominant feature of most Ig domains is a disulfide bridge connecting the two beta-sheets with a tryptophan residue packed against the disulfide bond. Ig superfamily (IgSF) domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. Typically, the V-set domains have A, B, E, and D strands in one sheet and A', G, F, C, C' and C" in the other. The structures in C1-set are smaller than those in the V-set; they have one beta sheet that is formed by strands A, B, E, and D and the other by strands G, F, C, and C'. Moreover, a C1-set Ig domain contains a short C' strand (three residues) and lacks A' and C" strand. Unlike other Ig domain sets, C2-set structures do not have a D strand. Like the V-set Ig domains, members of the I-set have a discontinuous A strand, but lack a C" strand.


The actual alignment was detected with superfamily member pfam07679:

Pssm-ID: 472250 [Multi-domain]  Cd Length: 90  Bit Score: 49.56  E-value: 2.18e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561  1639 SFLSPLIDQFAKEGKDkkVVFEARFS-KPNCKPKWLFRKDEVFTGSKFKFKQENDTYQLIITTPKVEDTGKYTI----EI 1713
Cdd:pfam07679    2 KFTQKPKDVEVQEGES--ARFTCTVTgTPDPEVSWFKDGQPLRSSDRFKVTYEGGTYTLTISNVQPDDSGKYTCvatnSA 79
                           90
                   ....*....|.
gi 281359561  1714 GGVSSTAFLNV 1724
Cdd:pfam07679   80 GEAEASAELTV 90
Ig super family cl11960
Immunoglobulin domain; The members here are composed of the immunoglobulin (Ig) domain found ...
2020-2095 1.34e-05

Immunoglobulin domain; The members here are composed of the immunoglobulin (Ig) domain found in the Ig superfamily. The Ig superfamily is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. Members of this group are components of immunoglobulin, neuroglia, cell surface glycoproteins, including T-cell receptors, CD2, CD4, CD8, and membrane glycoproteins, including butyrophilin and chondroitin sulfate proteoglycan core protein. A predominant feature of most Ig domains is a disulfide bridge connecting the two beta-sheets with a tryptophan residue packed against the disulfide bond. Ig superfamily (IgSF) domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. Typically, the V-set domains have A, B, E, and D strands in one sheet and A', G, F, C, C' and C" in the other. The structures in C1-set are smaller than those in the V-set; they have one beta sheet that is formed by strands A, B, E, and D and the other by strands G, F, C, and C'. Moreover, a C1-set Ig domain contains a short C' strand (three residues) and lacks A' and C" strand. Unlike other Ig domain sets, C2-set structures do not have a D strand. Like the V-set Ig domains, members of the I-set have a discontinuous A strand, but lack a C" strand.


The actual alignment was detected with superfamily member cd05748:

Pssm-ID: 472250 [Multi-domain]  Cd Length: 82  Bit Score: 46.81  E-value: 1.34e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 281359561 2020 PVLLEVPFKvsGtKQTPvEAKLFKDGKPLPVKD-VEVAVTDDKVTFKIKKPSRDLSGPYQIKISNGQGEDTKDVQII 2095
Cdd:cd05748     9 SLRLDIPIK--G-RPTP-TVTWSKDGQPLKETGrVQIETTASSTSLVIKNAKRSDSGKYTLTLKNSAGEKSATINVK 81
Ig super family cl11960
Immunoglobulin domain; The members here are composed of the immunoglobulin (Ig) domain found ...
1914-1998 3.73e-05

Immunoglobulin domain; The members here are composed of the immunoglobulin (Ig) domain found in the Ig superfamily. The Ig superfamily is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. Members of this group are components of immunoglobulin, neuroglia, cell surface glycoproteins, including T-cell receptors, CD2, CD4, CD8, and membrane glycoproteins, including butyrophilin and chondroitin sulfate proteoglycan core protein. A predominant feature of most Ig domains is a disulfide bridge connecting the two beta-sheets with a tryptophan residue packed against the disulfide bond. Ig superfamily (IgSF) domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. Typically, the V-set domains have A, B, E, and D strands in one sheet and A', G, F, C, C' and C" in the other. The structures in C1-set are smaller than those in the V-set; they have one beta sheet that is formed by strands A, B, E, and D and the other by strands G, F, C, and C'. Moreover, a C1-set Ig domain contains a short C' strand (three residues) and lacks A' and C" strand. Unlike other Ig domain sets, C2-set structures do not have a D strand. Like the V-set Ig domains, members of the I-set have a discontinuous A strand, but lack a C" strand.


The actual alignment was detected with superfamily member pfam07679:

Pssm-ID: 472250 [Multi-domain]  Cd Length: 90  Bit Score: 46.10  E-value: 3.73e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561  1914 RFNKKLKDTEAVEREKLILDIELQDQTAP-CDWKFNGEPIVPSESIEIKNMGGgKHQLIFSSLDMSNEGEITC----ESG 1988
Cdd:pfam07679    2 KFTQKPKDVEVQEGESARFTCTVTGTPDPeVSWFKDGQPLRSSDRFKVTYEGG-TYTLTISNVQPDDSGKYTCvatnSAG 80
                           90
                   ....*....|
gi 281359561  1989 QLSSKCKLSI 1998
Cdd:pfam07679   81 EAEASAELTV 90
Ig super family cl11960
Immunoglobulin domain; The members here are composed of the immunoglobulin (Ig) domain found ...
7361-7438 9.04e-05

Immunoglobulin domain; The members here are composed of the immunoglobulin (Ig) domain found in the Ig superfamily. The Ig superfamily is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. Members of this group are components of immunoglobulin, neuroglia, cell surface glycoproteins, including T-cell receptors, CD2, CD4, CD8, and membrane glycoproteins, including butyrophilin and chondroitin sulfate proteoglycan core protein. A predominant feature of most Ig domains is a disulfide bridge connecting the two beta-sheets with a tryptophan residue packed against the disulfide bond. Ig superfamily (IgSF) domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. Typically, the V-set domains have A, B, E, and D strands in one sheet and A', G, F, C, C' and C" in the other. The structures in C1-set are smaller than those in the V-set; they have one beta sheet that is formed by strands A, B, E, and D and the other by strands G, F, C, and C'. Moreover, a C1-set Ig domain contains a short C' strand (three residues) and lacks A' and C" strand. Unlike other Ig domain sets, C2-set structures do not have a D strand. Like the V-set Ig domains, members of the I-set have a discontinuous A strand, but lack a C" strand.


The actual alignment was detected with superfamily member cd05748:

Pssm-ID: 472250 [Multi-domain]  Cd Length: 82  Bit Score: 44.50  E-value: 9.04e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 281359561 7361 EGDNSKIKIFYSGDQPLTVILKKNNEVIcdsNDDTHVKVNIFDDYVAIYIRNIVKSDGGPYQIEFTNESGSATGEFYV 7438
Cdd:cd05748     6 AGESLRLDIPIKGRPTPTVTWSKDGQPL---KETGRVQIETTASSTSLVIKNAKRSDSGKYTLTLKNSAGEKSATINV 80
 
Name Accession Description Interval E-value
STKc_Twitchin_like cd14114
The catalytic domain of the Giant Serine/Threonine Kinases, Twitchin and Projectin; STKs ...
7986-8244 7.64e-177

The catalytic domain of the Giant Serine/Threonine Kinases, Twitchin and Projectin; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily is composed of Caenorhabditis elegans and Aplysia californica Twitchin, Drosophila melanogaster Projectin, and similar proteins. These are very large muscle proteins containing multiple immunoglobulin (Ig)-like and fibronectin type III (FN3) domains and a single kinase domain near the C-terminus. Twitchin and Projectin are both associated with thick filaments. Twitchin is localized in the outer parts of A-bands and is involved in regulating muscle contraction. It interacts with the myofibrillar proteins myosin and actin in a phosphorylation-dependent manner, and may be involved in regulating the myosin cross-bridge cycle. The kinase activity of Twitchen is activated by Ca2+ and the Ca2+ binding protein S100A1. Projectin is associated with the end of thick filaments and is a component of flight muscle connecting filaments. The kinase domain of Projectin may play roles in autophosphorylation and transphosphorylation, which impact the formation of myosin filaments. The Twitchin-like subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271016 [Multi-domain]  Cd Length: 259  Bit Score: 544.49  E-value: 7.64e-177
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 7986 YDRYDILEEIGTGAFGVVHRCRERSTGNIFAAKFIPVSHSVEKDLIRREIDIMNQLHHQKLINLHDAFEDDDEMILILEF 8065
Cdd:cd14114     1 YDHYDILEELGTGAFGVVHRCTERATGNNFAAKFIMTPHESDKETVRKEIQIMNQLHHPKLINLHDAFEDDNEMVLILEF 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 8066 LSGGELFERITAEGYVMTEAEVINYMRQICEGIRHMHEQNIIHLDIKPENIMCQTRSSTNVKLIDFGLATRLDPNEVVKI 8145
Cdd:cd14114    81 LSGGELFERIAAEHYKMSEAEVINYMRQVCEGLCHMHENNIVHLDIKPENIMCTTKRSNEVKLIDFGLATHLDPKESVKV 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 8146 TTGTAEFAAPEIVNREPVGFYTDMWATGVLSYVLLSGLSPFAGDNDVQTLKNVKACDWDFDVESFKYISEEAKDFIRKLL 8225
Cdd:cd14114   161 TTGTAEFAAPEIVEREPVGFYTDMWAVGVLSYVLLSGLSPFAGENDDETLRNVKSCDWNFDDSAFSGISEEAKDFIRKLL 240
                         250
                  ....*....|....*....
gi 281359561 8226 VRNKEKRMTAHECLLHPWL 8244
Cdd:cd14114   241 LADPNKRMTIHQALEHPWL 259
S_TKc smart00220
Serine/Threonine protein kinases, catalytic domain; Phosphotransferases. Serine or ...
7989-8244 1.26e-95

Serine/Threonine protein kinases, catalytic domain; Phosphotransferases. Serine or threonine-specific kinase subfamily.


Pssm-ID: 214567 [Multi-domain]  Cd Length: 254  Bit Score: 311.39  E-value: 1.26e-95
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561   7989 YDILEEIGTGAFGVVHRCRERSTGNIFAAKFIPVSHSVEK-DLIRREIDIMNQLHHQKLINLHDAFEDDDEMILILEFLS 8067
Cdd:smart00220    1 YEILEKLGEGSFGKVYLARDKKTGKLVAIKVIKKKKIKKDrERILREIKILKKLKHPNIVRLYDVFEDEDKLYLVMEYCE 80
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561   8068 GGELFERITAEGYvMTEAEVINYMRQICEGIRHMHEQNIIHLDIKPENIMCQtrSSTNVKLIDFGLATRLDPNEVVKITT 8147
Cdd:smart00220   81 GGDLFDLLKKRGR-LSEDEARFYLRQILSALEYLHSKGIVHRDLKPENILLD--EDGHVKLADFGLARQLDPGEKLTTFV 157
                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561   8148 GTAEFAAPEIVNREPVGFYTDMWATGVLSYVLLSGLSPFAGDNDVQTL-KNVKACDWDFDvESFKYISEEAKDFIRKLLV 8226
Cdd:smart00220  158 GTPEYMAPEVLLGKGYGKAVDIWSLGVILYELLTGKPPFPGDDQLLELfKKIGKPKPPFP-PPEWDISPEAKDLIRKLLV 236
                           250
                    ....*....|....*...
gi 281359561   8227 RNKEKRMTAHECLLHPWL 8244
Cdd:smart00220  237 KDPEKRLTAEEALQHPFF 254
Pkinase pfam00069
Protein kinase domain;
7989-8244 6.14e-61

Protein kinase domain;


Pssm-ID: 459660 [Multi-domain]  Cd Length: 217  Bit Score: 210.18  E-value: 6.14e-61
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561  7989 YDILEEIGTGAFGVVHRCRERSTGNIFAAKFIPVSH--SVEKDLIRREIDIMNQLHHQKLINLHDAFEDDDEMILILEFL 8066
Cdd:pfam00069    1 YEVLRKLGSGSFGTVYKAKHRDTGKIVAIKKIKKEKikKKKDKNILREIKILKKLNHPNIVRLYDAFEDKDNLYLVLEYV 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561  8067 SGGELFERITAEGYvMTEAEVINYMRQICEgirhmheqniihldikpenimcqtrsstnvklidfGLATRLDPNEVVkit 8146
Cdd:pfam00069   81 EGGSLFDLLSEKGA-FSEREAKFIMKQILE-----------------------------------GLESGSSLTTFV--- 121
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561  8147 tGTAEFAAPEIVNREPVGFYTDMWATGVLSYVLLSGLSPFAGDNDVQTLKNVKACDWDFDVEsFKYISEEAKDFIRKLLV 8226
Cdd:pfam00069  122 -GTPWYMAPEVLGGNPYGPKVDVWSLGCILYELLTGKPPFPGINGNEIYELIIDQPYAFPEL-PSNLSEEAKDLLKKLLK 199
                          250
                   ....*....|....*...
gi 281359561  8227 RNKEKRMTAHECLLHPWL 8244
Cdd:pfam00069  200 KDPSKRLTATQALQHPWF 217
SPS1 COG0515
Serine/threonine protein kinase [Signal transduction mechanisms];
7987-8232 7.81e-56

Serine/threonine protein kinase [Signal transduction mechanisms];


Pssm-ID: 440281 [Multi-domain]  Cd Length: 482  Bit Score: 205.25  E-value: 7.81e-56
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 7987 DRYDILEEIGTGAFGVVHRCRERSTGNIFAAKFIPVSHSVEKDLI---RREIDIMNQLHHQKLINLHDAFEDDDEMILIL 8063
Cdd:COG0515     7 GRYRILRLLGRGGMGVVYLARDLRLGRPVALKVLRPELAADPEARerfRREARALARLNHPNIVRVYDVGEEDGRPYLVM 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 8064 EFLSGGELFERITAEGyVMTEAEVINYMRQICEGIRHMHEQNIIHLDIKPENIMCqtRSSTNVKLIDFGLATRLDPNEVV 8143
Cdd:COG0515    87 EYVEGESLADLLRRRG-PLPPAEALRILAQLAEALAAAHAAGIVHRDIKPANILL--TPDGRVKLIDFGIARALGGATLT 163
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 8144 KITT--GTAEFAAPEIVNREPVGFYTDMWATGVLSYVLLSGLSPFAGDNDVQTLKNVKACDWDFDVESFKYISEEAKDFI 8221
Cdd:COG0515   164 QTGTvvGTPGYMAPEQARGEPVDPRSDVYSLGVTLYELLTGRPPFDGDSPAELLRAHLREPPPPPSELRPDLPPALDAIV 243
                         250
                  ....*....|.
gi 281359561 8222 RKLLVRNKEKR 8232
Cdd:COG0515   244 LRALAKDPEER 254
pk1 PHA03390
serine/threonine-protein kinase 1; Provisional
7998-8244 1.21e-32

serine/threonine-protein kinase 1; Provisional


Pssm-ID: 223069 [Multi-domain]  Cd Length: 267  Bit Score: 130.75  E-value: 1.21e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 7998 GAFGVVHRCRERSTGNIFAAKFIPVSHSvekdlirREIDIM-NQL--HHQKLINLHDAFEDDDEMILILEFLSGGELFER 8074
Cdd:PHA03390   27 GKFGKVSVLKHKPTQKLFVQKIIKAKNF-------NAIEPMvHQLmkDNPNFIKLYYSVTTLKGHVLIMDYIKDGDLFDL 99
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 8075 ITAEGYVmTEAEVINYMRQICEGIRHMHEQNIIHLDIKPENIMCqTRSSTNVKLIDFGLATRLDpneVVKITTGTAEFAA 8154
Cdd:PHA03390  100 LKKEGKL-SEAEVKKIIRQLVEALNDLHKHNIIHNDIKLENVLY-DRAKDRIYLCDYGLCKIIG---TPSCYDGTLDYFS 174
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 8155 PEIVNREPVGFYTDMWATGVLSYVLLSGLSPFAGDND----VQTLKNVKAcdwdFDVESFKYISEEAKDFIRKLLVRNKE 8230
Cdd:PHA03390  175 PEKIKGHNYDVSFDWWAVGVLTYELLTGKHPFKEDEDeeldLESLLKRQQ----KKLPFIKNVSKNANDFVQSMLKYNIN 250
                         250
                  ....*....|....*
gi 281359561 8231 KRMTAHECLL-HPWL 8244
Cdd:PHA03390  251 YRLTNYNEIIkHPFL 265
I-set pfam07679
Immunoglobulin I-set domain;
8632-8721 2.67e-31

Immunoglobulin I-set domain;


Pssm-ID: 400151 [Multi-domain]  Cd Length: 90  Bit Score: 120.44  E-value: 2.67e-31
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561  8632 PEFTKPLHDLTIHDGEQLILTCYVKGDPEPQISWSKNGKSLSSSDILDLRYKNGIATLTINEVFPEDEGVITCTATNSVG 8711
Cdd:pfam07679    1 PKFTQKPKDVEVQEGESARFTCTVTGTPDPEVSWFKDGQPLRSSDRFKVTYEGGTYTLTISNVQPDDSGKYTCVATNSAG 80
                           90
                   ....*....|
gi 281359561  8712 AVETKCKLTI 8721
Cdd:pfam07679   81 EAEASAELTV 90
Ig_Titin_like cd05748
Immunoglobulin (Ig)-like domain of titin and similar proteins; The members here are composed ...
6174-6255 1.01e-30

Immunoglobulin (Ig)-like domain of titin and similar proteins; The members here are composed of the immunoglobulin (Ig)-like domain found in titin-like proteins and similar proteins. Titin (also called connectin) is a fibrous sarcomeric protein specifically found in vertebrate striated muscle. Titin is a giant protein; depending on isoform composition, it ranges from 2970 to 3700 kDa, and is of a length that spans half a sarcomere. Titin largely consists of multiple repeats of Ig-like and fibronectin type 3 (FN-III)-like domains. Titin connects the ends of myosin thick filaments to Z disks and extends along the thick filament to the H zone. It appears to function similarly to an elastic band, keeping the myosin filaments centered in the sarcomere during muscle contraction or stretching. Within the sarcomere, titin is also attached to or is associated with myosin binding protein C (MyBP-C). MyBP-C appears to contribute to the generation of passive tension by titin and like titin has repeated Ig-like and FN-III domains. Also included in this group are worm twitchin and insect projectin, thick filament proteins of invertebrate muscle which also have repeated Ig-like and FN-III domains.


Pssm-ID: 409406 [Multi-domain]  Cd Length: 82  Bit Score: 118.46  E-value: 1.01e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 6174 RIKVRAGEPVNLNIPISGAPTPTIEWKRGDLKLEEGKRISYETNSERTLFRIDDSNRRDSGKYTVTAANEFGKDTADIEV 6253
Cdd:cd05748     1 TIVVRAGESLRLDIPIKGRPTPTVTWSKDGQPLKETGRVQIETTASSTSLVIKNAKRSDSGKYTLTLKNSAGEKSATINV 80

                  ..
gi 281359561 6254 IV 6255
Cdd:cd05748    81 KV 82
FN3 COG3401
Fibronectin type 3 domain [General function prediction only];
6236-6552 1.54e-28

Fibronectin type 3 domain [General function prediction only];


Pssm-ID: 442628 [Multi-domain]  Cd Length: 603  Bit Score: 125.89  E-value: 1.54e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 6236 YTVTAANEFGKDTADIEVIVVDKPSPPEGP--LSYTETAPDHISLHWYSPKDdggSDITGYIIEFTEFGVDDWKPVpGTC 6313
Cdd:COG3401   207 YRVAATDTGGESAPSNEVSVTTPTTPPSAPtgLTATADTPGSVTLSWDPVTE---SDATGYRVYRSNSGDGPFTKV-ATV 282
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 6314 PNTNFTVKNLVEGKKYVFRIRAENIYG----ASEALEGKPVLAkspfdPPGAPSQPTISAYTPNSANLEWHPPDDcggKP 6389
Cdd:COG3401   283 TTTSYTDTGLTNGTTYYYRVTAVDAAGnesaPSNVVSVTTDLT-----PPAAPSGLTATAVGSSSITLSWTASSD---AD 354
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 6390 ITGYIVERRER-GGEWIKCNNYPTpNTSYTVSNLRDGARYEFRVLAVNEAGPGhpSKPSDPMTAEHQRYRPDPPEPPKPD 6468
Cdd:COG3401   355 VTGYNVYRSTSgGGTYTKIAETVT-TTSYTDTGLTPGTTYYYKVTAVDAAGNE--SAPSEEVSATTASAASGESLTASVD 431
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 6469 RITRNGV------TLSWRPPRTDGKSRIKGYYVEMRPKNGKDWKTVNDiPINSTVYTVPSLKEGEEYSFRVVAENEVGRS 6542
Cdd:COG3401   432 AVPLTDVagataaASAASNPGVSAAVLADGGDTGNAVPFTTTSSTVTA-TTTDTTTANLSVTTGSLVGGSGASSVTNSVS 510
                         330
                  ....*....|
gi 281359561 6543 DPSKPSQPIT 6552
Cdd:COG3401   511 VIGASAAAAV 520
FN3 COG3401
Fibronectin type 3 domain [General function prediction only];
3866-4181 1.85e-26

Fibronectin type 3 domain [General function prediction only];


Pssm-ID: 442628 [Multi-domain]  Cd Length: 603  Bit Score: 119.34  E-value: 1.85e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 3866 YIVTAKNDSG----SDTVEVeLEVLCKPSKPKGpLAVSNVTAETLHLKWEKPEDDGgdpIEQYLVERMDTETGRWVPVLT 3941
Cdd:COG3401   207 YRVAATDTGGesapSNEVSV-TTPTTPPSAPTG-LTATADTPGSVTLSWDPVTESD---ATGYRVYRSNSGDGPFTKVAT 281
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 3942 TKTPEADVTGLTEGKEYLFRVKAVNSEG-ESEPLVTDIPTKAKNPfdaadtPGKPQIVD---WSGNHCDLKWRAPEDDGg 4017
Cdd:COG3401   282 VTTTSYTDTGLTNGTTYYYRVTAVDAAGnESAPSNVVSVTTDLTP------PAAPSGLTataVGSSSITLSWTASSDAD- 354
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 4018 asITGYIVERKDPNTGKWQKALETSTpDCKARVNDLIAGNKYQFRIMAVNKAG-KSKPSEPSDQMTAKDRFAPPKIDRTN 4096
Cdd:COG3401   355 --VTGYNVYRSTSGGGTYTKIAETVT-TTSYTDTGLTPGTTYYYKVTAVDAAGnESAPSEEVSATTASAASGESLTASVD 431
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 4097 IKDITIKAGQHIRfdIKVSGEPPATKVWLHNKARLENDDSNYNIDMESYRTKLTVPIS-KRFHSGKYTLKAENESGRDEA 4175
Cdd:COG3401   432 AVPLTDVAGATAA--ASAASNPGVSAAVLADGGDTGNAVPFTTTSSTVTATTTDTTTAnLSVTTGSLVGGSGASSVTNSV 509

                  ....*.
gi 281359561 4176 SFEVIV 4181
Cdd:COG3401   510 SVIGAS 515
Ig_Titin_like cd05748
Immunoglobulin (Ig)-like domain of titin and similar proteins; The members here are composed ...
6570-6650 2.18e-24

Immunoglobulin (Ig)-like domain of titin and similar proteins; The members here are composed of the immunoglobulin (Ig)-like domain found in titin-like proteins and similar proteins. Titin (also called connectin) is a fibrous sarcomeric protein specifically found in vertebrate striated muscle. Titin is a giant protein; depending on isoform composition, it ranges from 2970 to 3700 kDa, and is of a length that spans half a sarcomere. Titin largely consists of multiple repeats of Ig-like and fibronectin type 3 (FN-III)-like domains. Titin connects the ends of myosin thick filaments to Z disks and extends along the thick filament to the H zone. It appears to function similarly to an elastic band, keeping the myosin filaments centered in the sarcomere during muscle contraction or stretching. Within the sarcomere, titin is also attached to or is associated with myosin binding protein C (MyBP-C). MyBP-C appears to contribute to the generation of passive tension by titin and like titin has repeated Ig-like and FN-III domains. Also included in this group are worm twitchin and insect projectin, thick filament proteins of invertebrate muscle which also have repeated Ig-like and FN-III domains.


Pssm-ID: 409406 [Multi-domain]  Cd Length: 82  Bit Score: 100.36  E-value: 2.18e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 6570 IVCRAGDDFSIHVPYLAFPKPNAFWYSNDNMLDDNNRVHKHLTDDAASVVVKNSKRADSGQYRLQLKNTSGFDTATINVR 6649
Cdd:cd05748     2 IVVRAGESLRLDIPIKGRPTPTVTWSKDGQPLKETGRVQIETTASSTSLVIKNAKRSDSGKYTLTLKNSAGEKSATINVK 81

                  .
gi 281359561 6650 V 6650
Cdd:cd05748    82 V 82
FN3 COG3401
Fibronectin type 3 domain [General function prediction only];
6905-7189 1.11e-23

Fibronectin type 3 domain [General function prediction only];


Pssm-ID: 442628 [Multi-domain]  Cd Length: 603  Bit Score: 110.48  E-value: 1.11e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 6905 FDSNDYASMYYNKSAKRDETGSYTITLTNNKGSDTASCHVTVVDRPLPPQGP--LNAYDITPDTCTLAWKTPLDDGgspI 6982
Cdd:COG3401   185 LTVTSTTLVDGGGDIEPGTTYYYRVAATDTGGESAPSNEVSVTTPTTPPSAPtgLTATADTPGSVTLSWDPVTESD---A 261
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 6983 TNYVVE-KLDNSGSWVKISSfVRNTHYDVMGLEPHYKYNFRVRAENQYGL-SDPLDIIEPIVAKhqfTVPDEPGQPKVID 7060
Cdd:COG3401   262 TGYRVYrSNSGDGPFTKVAT-VTTTSYTDTGLTNGTTYYYRVTAVDAAGNeSAPSNVVSVTTDL---TPPAAPSGLTATA 337
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 7061 WDSGNVTLIWTRPLSDGgsrIQGYQIeYRDILNDSSWNAYDYIIKDTKYQLYNLINGSEYEFRIKAKNAAGLSKPSSPSL 7140
Cdd:COG3401   338 VGSSSITLSWTASSDAD---VTGYNV-YRSTSGGGTYTKIAETVTTTSYTDTGLTPGTTYYYKVTAVDAAGNESAPSEEV 413
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*....
gi 281359561 7141 RFKlkgKFTVPSPPGAPQVTRVGKNYVDLKWEKPLRDGGSRITGYIIER 7189
Cdd:COG3401   414 SAT---TASAASGESLTASVDAVPLTDVAGATAAASAASNPGVSAAVLA 459
FN3 cd00063
Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein ...
6359-6451 6.78e-23

Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein fibronectin. Its tenth fibronectin type III repeat contains an RGD cell recognition sequence in a flexible loop between 2 strands. Approximately 2% of all animal proteins contain the FN3 repeat; including extracellular and intracellular proteins, membrane spanning cytokine receptors, growth hormone receptors, tyrosine phosphatase receptors, and adhesion molecules. FN3-like domains are also found in bacterial glycosyl hydrolases.


Pssm-ID: 238020 [Multi-domain]  Cd Length: 93  Bit Score: 96.41  E-value: 6.78e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 6359 PGAPSQPTISAYTPNSANLEWHPPDDCGGkPITGYIVERRERG-GEWIKCNNYPTPNTSYTVSNLRDGARYEFRVLAVNE 6437
Cdd:cd00063     1 PSPPTNLRVTDVTSTSVTLSWTPPEDDGG-PITGYVVEYREKGsGDWKEVEVTPGSETSYTLTGLKPGTEYEFRVRAVNG 79
                          90
                  ....*....|....
gi 281359561 6438 AGPGHPSKPSDPMT 6451
Cdd:cd00063    80 GGESPPSESVTVTT 93
I-set pfam07679
Immunoglobulin I-set domain;
3494-3590 1.25e-22

Immunoglobulin I-set domain;


Pssm-ID: 400151 [Multi-domain]  Cd Length: 90  Bit Score: 95.79  E-value: 1.25e-22
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561  3494 PRFLKPhidrvnLKPVIVKTGLSISLDINIRGEPAPKVEWFFNNSSVTSDEHsVKIDNVDYNTKFFVMRAQRSQSGKYII 3573
Cdd:pfam07679    1 PKFTQK------PKDVEVQEGESARFTCTVTGTPDPEVSWFKDGQPLRSSDR-FKVTYEGGTYTLTISNVQPDDSGKYTC 73
                           90
                   ....*....|....*..
gi 281359561  3574 KATNEVGEDEAELEVTV 3590
Cdd:pfam07679   74 VATNSAGEAEASAELTV 90
FN3 cd00063
Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein ...
2203-2292 2.49e-22

Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein fibronectin. Its tenth fibronectin type III repeat contains an RGD cell recognition sequence in a flexible loop between 2 strands. Approximately 2% of all animal proteins contain the FN3 repeat; including extracellular and intracellular proteins, membrane spanning cytokine receptors, growth hormone receptors, tyrosine phosphatase receptors, and adhesion molecules. FN3-like domains are also found in bacterial glycosyl hydrolases.


Pssm-ID: 238020 [Multi-domain]  Cd Length: 93  Bit Score: 94.87  E-value: 2.49e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 2203 PGKPKAVDLTDWDKDHADLKWEAPETDGGdPITAYIVEYKEKFSNDWVSGKEVDGDARTATVDGLKEGQQYEFRVRAVNR 2282
Cdd:cd00063     1 PSPPTNLRVTDVTSTSVTLSWTPPEDDGG-PITGYVVEYREKGSGDWKEVEVTPGSETSYTLTGLKPGTEYEFRVRAVNG 79
                          90
                  ....*....|
gi 281359561 2283 AGPGEPSDKT 2292
Cdd:cd00063    80 GGESPPSESV 89
I-set pfam07679
Immunoglobulin I-set domain;
6173-6255 4.42e-22

Immunoglobulin I-set domain;


Pssm-ID: 400151 [Multi-domain]  Cd Length: 90  Bit Score: 94.25  E-value: 4.42e-22
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561  6173 KRIKVRAGEPVNLNIPISGAPTPTIEWKRGDLKLEEGKRISYETNSERTLFRIDDSNRRDSGKYTVTAANEFGKDTADIE 6252
Cdd:pfam07679    8 KDVEVQEGESARFTCTVTGTPDPEVSWFKDGQPLRSSDRFKVTYEGGTYTLTISNVQPDDSGKYTCVATNSAGEAEASAE 87

                   ...
gi 281359561  6253 VIV 6255
Cdd:pfam07679   88 LTV 90
FN3 cd00063
Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein ...
5764-5853 6.16e-22

Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein fibronectin. Its tenth fibronectin type III repeat contains an RGD cell recognition sequence in a flexible loop between 2 strands. Approximately 2% of all animal proteins contain the FN3 repeat; including extracellular and intracellular proteins, membrane spanning cytokine receptors, growth hormone receptors, tyrosine phosphatase receptors, and adhesion molecules. FN3-like domains are also found in bacterial glycosyl hydrolases.


Pssm-ID: 238020 [Multi-domain]  Cd Length: 93  Bit Score: 93.72  E-value: 6.16e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 5764 PDAPGKPIITDWDRDHIDLQWAVPKSDGGaPISEYIIQKKEKGSPYWTNVRHVPSNKNTTTIPELTEGQEYEFRVIAVNQ 5843
Cdd:cd00063     1 PSPPTNLRVTDVTSTSVTLSWTPPEDDGG-PITGYVVEYREKGSGDWKEVEVTPGSETSYTLTGLKPGTEYEFRVRAVNG 79
                          90
                  ....*....|
gi 281359561 5844 AGQSEPSEPS 5853
Cdd:cd00063    80 GGESPPSESV 89
IgI_Twitchin_like cd20949
C-terminal immunoglobulin-like domain of the myosin-associated giant protein kinase Twitchin, ...
8313-8401 7.94e-22

C-terminal immunoglobulin-like domain of the myosin-associated giant protein kinase Twitchin, and similar domains; member of the I-set IgSF domains; The members here are composed of the C-terminal immunoglobulin-like domain of the myosin-associated giant protein kinase Twitchin and similar proteins, including Caenorhabditis elegans and Aplysia californica Twitchin, Drosophila melanogaster Projectin, and similar proteins. These are very large muscle proteins containing multiple immunoglobulin (Ig)-like and fibronectin type III (FN3) domains and a single kinase domain near the C-terminus. In humans these proteins are called Titin. The Ig superfamily (IgSF) is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. The Ig-like domain of the Twitchin is a member of the I-set IgSF domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand but lack a C" strand. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors, the hemolymph protein hemolin, the muscle proteins (titin, telokin, and twitchin), the neuronal adhesion molecule axonin-1, and the signaling molecule semaphorin 4D.


Pssm-ID: 409541 [Multi-domain]  Cd Length: 89  Bit Score: 93.55  E-value: 7.94e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 8313 RFVIRPSSQFCYEGQSVKFYCRCIAIATPTLTWSHNNIELRQSVKFMKRYVGDDYYFIINRVKLDDRGEYIIRAENHYGS 8392
Cdd:cd20949     1 TFTENAYVTTVKEGQSATILCEVKGEPQPNVTWHFNGQPISASVADMSKYRILADGLLINKVTQDDTGEYTCRAYQVNSI 80

                  ....*....
gi 281359561 8393 REEVVFLNV 8401
Cdd:cd20949    81 ASDMQERTV 89
FN3 cd00063
Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein ...
5073-5166 1.28e-21

Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein fibronectin. Its tenth fibronectin type III repeat contains an RGD cell recognition sequence in a flexible loop between 2 strands. Approximately 2% of all animal proteins contain the FN3 repeat; including extracellular and intracellular proteins, membrane spanning cytokine receptors, growth hormone receptors, tyrosine phosphatase receptors, and adhesion molecules. FN3-like domains are also found in bacterial glycosyl hydrolases.


Pssm-ID: 238020 [Multi-domain]  Cd Length: 93  Bit Score: 92.94  E-value: 1.28e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 5073 PAPPNGpLKVDEINSESCTLHWNPPDDDGGqPIDNYVVEKLDETTGRWIPAGETDGPVTALKVGGLTPGHKYKFRVRAKN 5152
Cdd:cd00063     1 PSPPTN-LRVTDVTSTSVTLSWTPPEDDGG-PITGYVVEYREKGSGDWKEVEVTPGSETSYTLTGLKPGTEYEFRVRAVN 78
                          90
                  ....*....|....
gi 281359561 5153 RQGTSEPLTTAQAI 5166
Cdd:cd00063    79 GGGESPPSESVTVT 92
FN3 COG3401
Fibronectin type 3 domain [General function prediction only];
6630-7006 2.27e-21

Fibronectin type 3 domain [General function prediction only];


Pssm-ID: 442628 [Multi-domain]  Cd Length: 603  Bit Score: 103.16  E-value: 2.27e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 6630 QYRLQLKNTSGFDTATINVRVLDR---PSPPTRLRADEFSGDSLTLYWNPPNDDGgsaIQNYIIEKKEARSSTWSKVSSF 6706
Cdd:COG3401   206 YYRVAATDTGGESAPSNEVSVTTPttpPSAPTGLTATADTPGSVTLSWDPVTESD---ATGYRVYRSNSGDGPFTKVATV 282
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 6707 CTVPFVrIRNLVLNKEYDFRVIAENKYG-QSDPANTSEPILARHPfdiPNTPGIPHGIDSTEDSITIAWTKPKhdgGSPI 6785
Cdd:COG3401   283 TTTSYT-DTGLTNGTTYYYRVTAVDAAGnESAPSNVVSVTTDLTP---PAAPSGLTATAVGSSSITLSWTASS---DADV 355
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 6786 TGYIIEKRLLSDDKWTKaVHALCPDLSCKIPNLIENAEYEFRVAAVNAAGqsAYSGSSDLIFCRRPPHAPKITSDLSIRD 6865
Cdd:COG3401   356 TGYNVYRSTSGGGTYTK-IAETVTTTSYTDTGLTPGTTYYYKVTAVDAAG--NESAPSEEVSATTASAASGESLTASVDA 432
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 6866 MTVIAGDefRITVPYHASPRPTASWSLNGLEVIPGERIKFDSNDYASMYYNKSAKRDETGSYTITLTNNKGSDTASCHVT 6945
Cdd:COG3401   433 VPLTDVA--GATAAASAASNPGVSAAVLADGGDTGNAVPFTTTSSTVTATTTDTTTANLSVTTGSLVGGSGASSVTNSVS 510
                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 281359561 6946 VVDRPLPPQGPLNAYDITPDTC--TLAWKTPLDDGGSPITNYVVEKLDNSGSWVKISSFVRNT 7006
Cdd:COG3401   511 VIGASAAAAVGGAPDGTPNVTGasPVTVGASTGDVLITDLVSLTTSASSSVSGAGLGSGNLYL 573
FN3 cd00063
Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein ...
2999-3088 2.31e-21

Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein fibronectin. Its tenth fibronectin type III repeat contains an RGD cell recognition sequence in a flexible loop between 2 strands. Approximately 2% of all animal proteins contain the FN3 repeat; including extracellular and intracellular proteins, membrane spanning cytokine receptors, growth hormone receptors, tyrosine phosphatase receptors, and adhesion molecules. FN3-like domains are also found in bacterial glycosyl hydrolases.


Pssm-ID: 238020 [Multi-domain]  Cd Length: 93  Bit Score: 92.17  E-value: 2.31e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 2999 PSKPRGpLDVKDVTKDSCKLKWKKPEDDGGkPISAYQVEKFDKKQGRWVPLGRTSANDTEFDVKGLQEGHEYQFRVKAIN 3078
Cdd:cd00063     1 PSPPTN-LRVTDVTSTSVTLSWTPPEDDGG-PITGYVVEYREKGSGDWKEVEVTPGSETSYTLTGLKPGTEYEFRVRAVN 78
                          90
                  ....*....|
gi 281359561 3079 EEGESDPLDS 3088
Cdd:cd00063    79 GGGESPPSES 88
FN3 cd00063
Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein ...
2501-2590 2.43e-21

Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein fibronectin. Its tenth fibronectin type III repeat contains an RGD cell recognition sequence in a flexible loop between 2 strands. Approximately 2% of all animal proteins contain the FN3 repeat; including extracellular and intracellular proteins, membrane spanning cytokine receptors, growth hormone receptors, tyrosine phosphatase receptors, and adhesion molecules. FN3-like domains are also found in bacterial glycosyl hydrolases.


Pssm-ID: 238020 [Multi-domain]  Cd Length: 93  Bit Score: 92.17  E-value: 2.43e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 2501 PSPPSQPVIDDYDNKSVLLKWKRPPSDGGrPITHYIVEIKDKFAPSWSEVAKTDDPNPECNVEGLKEKMVYQFRVRAVNK 2580
Cdd:cd00063     1 PSPPTNLRVTDVTSTSVTLSWTPPEDDGG-PITGYVVEYREKGSGDWKEVEVTPGSETSYTLTGLKPGTEYEFRVRAVNG 79
                          90
                  ....*....|
gi 281359561 2581 AGPSEPSQPT 2590
Cdd:cd00063    80 GGESPPSESV 89
FN3 COG3401
Fibronectin type 3 domain [General function prediction only];
5972-6384 3.24e-21

Fibronectin type 3 domain [General function prediction only];


Pssm-ID: 442628 [Multi-domain]  Cd Length: 603  Bit Score: 102.77  E-value: 3.24e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 5972 ANSVTISWKPPKDNGGSEISSYVIEKRDLTHGGGWVPAVNYVSAKYNHAVVPRLLEGTMYELRVMAENLQGRSDPltsDQ 6051
Cdd:COG3401   146 GLYGVDGANASGTTASSVAGAGVVVSPDTSATAAVATTSLTVTSTTLVDGGGDIEPGTTYYYRVAATDTGGESAP---SN 222
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 6052 PVVAKSQYTVPGAPGKPELTDSDKNHITIKWKqpiSNGGSPIIGYDIERRDVNTGRWIKINGqpVPTAEYQDDRVTSNHQ 6131
Cdd:COG3401   223 EVSVTTPTTPPSAPTGLTATADTPGSVTLSWD---PVTESDATGYRVYRSNSGDGPFTKVAT--VTTTSYTDTGLTNGTT 297
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 6132 YQYRISAVNAAGNgkTSEPSAifnarplrekprfyfdgligkrikvragepvnlnipisgaptptiewkrgdlkleegkr 6211
Cdd:COG3401   298 YYYRVTAVDAAGN--ESAPSN----------------------------------------------------------- 316
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 6212 isyetnsertlfriddsnrrdsgkyTVTAanefgkdTADIEvivvdKPSPPEGpLSYTETAPDHISLHWYSPKDdggSDI 6291
Cdd:COG3401   317 -------------------------VVSV-------TTDLT-----PPAAPSG-LTATAVGSSSITLSWTASSD---ADV 355
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 6292 TGYIIEFTEFGVDDWKPVPGTCPNTNFTVKNLVEGKKYVFRIRAENIYG----ASEALEGKPVLAKSPFDPPGAPSQPTI 6367
Cdd:COG3401   356 TGYNVYRSTSGGGTYTKIAETVTTTSYTDTGLTPGTTYYYKVTAVDAAGnesaPSEEVSATTASAASGESLTASVDAVPL 435
                         410
                  ....*....|....*..
gi 281359561 6368 SAYTPNSANLEWHPPDD 6384
Cdd:COG3401   436 TDVAGATAAASAASNPG 452
FN3 COG3401
Fibronectin type 3 domain [General function prediction only];
4356-4776 6.18e-21

Fibronectin type 3 domain [General function prediction only];


Pssm-ID: 442628 [Multi-domain]  Cd Length: 603  Bit Score: 102.00  E-value: 6.18e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 4356 NCEYEFRVKAINAAGPGEPSDASKPIITKPRKLAPKIDRKNIRTYNFKSGEPIFLDINISGEPAPDVTWNQNNKSVQTTS 4435
Cdd:COG3401   108 NTGLTSSDEVPSPAVGTATTATAVAGGAATAGTYALGAGLYGVDGANASGTTASSVAGAGVVVSPDTSATAAVATTSLTV 187
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 4436 fshienLPYNTKYINNNPERKDTGLYKISAHNFYGQ----DQVEFqINIITKPGKPEGpLEVSEVHKDGCKLKWKKPKDD 4511
Cdd:COG3401   188 ------TSTTLVDGGGDIEPGTTYYYRVAATDTGGEsapsNEVSV-TTPTTPPSAPTG-LTATADTPGSVTLSWDPVTES 259
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 4512 GgepVESYLVEKFDPDTGIWLPVGRSDGPEYNVDGLVPGHDYKFRVKAVNKEG-ESEPLETLgsiiakdpfSVPTKPGVP 4590
Cdd:COG3401   260 D---ATGYRVYRSNSGDGPFTKVATVTTTSYTDTGLTNGTTYYYRVTAVDAAGnESAPSNVV---------SVTTDLTPP 327
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 4591 EP------TDWTANKVELAWpEPASDGGspIQGYIVEVKDKYSPLWEKALETNSpTPTATVQGLIEGNEYQFRVVALNKG 4664
Cdd:COG3401   328 AApsgltaTAVGSSSITLSW-TASSDAD--VTGYNVYRSTSGGGTYTKIAETVT-TTSYTDTGLTPGTTYYYKVTAVDAA 403
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 4665 GL-SEPSDPSKIFTAKPRYLAPKIDRRNLRNITLSSG-TALKLDANITGEPAPKVEWKLSNYHLQSGKNVTIETPDYYTk 4742
Cdd:COG3401   404 GNeSAPSEEVSATTASAASGESLTASVDAVPLTDVAGaTAAASAASNPGVSAAVLADGGDTGNAVPFTTTSSTVTATTT- 482
                         410       420       430
                  ....*....|....*....|....*....|....
gi 281359561 4743 LVIRPTQRSDSGEYLVTATNTSGKDSVLVNVVIT 4776
Cdd:COG3401   483 DTTTANLSVTTGSLVGGSGASSVTNSVSVIGASA 516
I-set pfam07679
Immunoglobulin I-set domain;
8740-8831 6.23e-21

Immunoglobulin I-set domain;


Pssm-ID: 400151 [Multi-domain]  Cd Length: 90  Bit Score: 90.78  E-value: 6.23e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561  8740 PKIVSHLESRFVRDGDAVNLACRIIGAQHFDVVWLHNNKEIKPSKDFQYTNEANIYRLQIAEIFPEDGGTYTCEAFNDIG 8819
Cdd:pfam07679    1 PKFTQKPKDVEVQEGESARFTCTVTGTPDPEVSWFKDGQPLRSSDRFKVTYEGGTYTLTISNVQPDDSGKYTCVATNSAG 80
                           90
                   ....*....|..
gi 281359561  8820 EsfSTCTINVTV 8831
Cdd:pfam07679   81 E--AEASAELTV 90
FN3 cd00063
Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein ...
4879-4970 9.76e-21

Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein fibronectin. Its tenth fibronectin type III repeat contains an RGD cell recognition sequence in a flexible loop between 2 strands. Approximately 2% of all animal proteins contain the FN3 repeat; including extracellular and intracellular proteins, membrane spanning cytokine receptors, growth hormone receptors, tyrosine phosphatase receptors, and adhesion molecules. FN3-like domains are also found in bacterial glycosyl hydrolases.


Pssm-ID: 238020 [Multi-domain]  Cd Length: 93  Bit Score: 90.25  E-value: 9.76e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 4879 PGKPENLKATDWDKDHVDLAWTPPLiDGGSPISCYIIEKQDKY-GKWERALDVPADQCKATIPDLVEGQTYKFRVSAVNA 4957
Cdd:cd00063     1 PSPPTNLRVTDVTSTSVTLSWTPPE-DDGGPITGYVVEYREKGsGDWKEVEVTPGSETSYTLTGLKPGTEYEFRVRAVNG 79
                          90
                  ....*....|...
gi 281359561 4958 AGTGEPSDSTPPI 4970
Cdd:cd00063    80 GGESPPSESVTVT 92
FN3 cd00063
Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein ...
4584-4677 1.09e-20

Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein fibronectin. Its tenth fibronectin type III repeat contains an RGD cell recognition sequence in a flexible loop between 2 strands. Approximately 2% of all animal proteins contain the FN3 repeat; including extracellular and intracellular proteins, membrane spanning cytokine receptors, growth hormone receptors, tyrosine phosphatase receptors, and adhesion molecules. FN3-like domains are also found in bacterial glycosyl hydrolases.


Pssm-ID: 238020 [Multi-domain]  Cd Length: 93  Bit Score: 90.25  E-value: 1.09e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 4584 PTKPGVPEPTDWTANKVELAWpEPASDGGSPIQGYIVEVKDKYSPLWEKALETNSPTPTATVQGLIEGNEYQFRVVALNK 4663
Cdd:cd00063     1 PSPPTNLRVTDVTSTSVTLSW-TPPEDDGGPITGYVVEYREKGSGDWKEVEVTPGSETSYTLTGLKPGTEYEFRVRAVNG 79
                          90
                  ....*....|....
gi 281359561 4664 GGLSEPSDPSKIFT 4677
Cdd:cd00063    80 GGESPPSESVTVTT 93
FN3 cd00063
Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein ...
7151-7237 1.31e-20

Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein fibronectin. Its tenth fibronectin type III repeat contains an RGD cell recognition sequence in a flexible loop between 2 strands. Approximately 2% of all animal proteins contain the FN3 repeat; including extracellular and intracellular proteins, membrane spanning cytokine receptors, growth hormone receptors, tyrosine phosphatase receptors, and adhesion molecules. FN3-like domains are also found in bacterial glycosyl hydrolases.


Pssm-ID: 238020 [Multi-domain]  Cd Length: 93  Bit Score: 90.25  E-value: 1.31e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 7151 PSPPGAPQVTRVGKNYVDLKWEKPlRDGGSRITGYIIERRDIGGAVWVKCNDYNVLDTEYTVMNLIEMGDYEFRVFAVNS 7230
Cdd:cd00063     1 PSPPTNLRVTDVTSTSVTLSWTPP-EDDGGPITGYVVEYREKGSGDWKEVEVTPGSETSYTLTGLKPGTEYEFRVRAVNG 79

                  ....*..
gi 281359561 7231 AGRSEPS 7237
Cdd:cd00063    80 GGESPPS 86
FN3 COG3401
Fibronectin type 3 domain [General function prediction only];
2673-2891 1.71e-20

Fibronectin type 3 domain [General function prediction only];


Pssm-ID: 442628 [Multi-domain]  Cd Length: 603  Bit Score: 100.46  E-value: 1.71e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 2673 FYTLKAEN--RNGIDRETVELVVLGKPSSPKGPLAVSDVTASGCKLQWKKPEDDGgvpIKEYVVEKMDTATGKWVRVGRS 2750
Cdd:COG3401   206 YYRVAATDtgGESAPSNEVSVTTPTTPPSAPTGLTATADTPGSVTLSWDPVTESD---ATGYRVYRSNSGDGPFTKVATV 282
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 2751 PGekepPSFDVTGLSLGSEYMFRVSAVNEEG-ESEPLTTLVGVVAKDPfdePNKPGTPEVTDYDNQSISLKWAAPnndGG 2829
Cdd:COG3401   283 TT----TSYTDTGLTNGTTYYYRVTAVDAAGnESAPSNVVSVTTDLTP---PAAPSGLTATAVGSSSITLSWTAS---SD 352
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 281359561 2830 APIQKYIIEKKNKNKTEWEKaLEIPGDQLEATVAGLQEYGEYQFRVIAVNKAGLSPPSDASV 2891
Cdd:COG3401   353 ADVTGYNVYRSTSGGGTYTK-IAETVTTTSYTDTGLTPGTTYYYKVTAVDAAGNESAPSEEV 413
FN3 COG3401
Fibronectin type 3 domain [General function prediction only];
2957-3191 1.93e-20

Fibronectin type 3 domain [General function prediction only];


Pssm-ID: 442628 [Multi-domain]  Cd Length: 603  Bit Score: 100.46  E-value: 1.93e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 2957 IPYNTKISIIETVRKHTGIYKIIAVNEHGQDEATVEVNILA---PPSKPRGpLDVKDVTKDSCKLKWKKPEDDGgkpISA 3033
Cdd:COG3401   188 TSTTLVDGGGDIEPGTTYYYRVAATDTGGESAPSNEVSVTTpttPPSAPTG-LTATADTPGSVTLSWDPVTESD---ATG 263
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 3034 YQVEKFDKKQGRWVPLGRTsaNDTEFDVKGLQEGHEYQFRVKAINEEG-ESDPLDSDDSIIAKNPydaaskPGTPNIVDY 3112
Cdd:COG3401   264 YRVYRSNSGDGPFTKVATV--TTTSYTDTGLTNGTTYYYRVTAVDAAGnESAPSNVVSVTTDLTP------PAAPSGLTA 335
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 3113 NEHM---VKLKWEAPrSDGGApiSGYIIEKKDKFSPIWDEILSTNTSvPEATVEGLVEGNIYQFRVRAVNKAG-FSDPSD 3188
Cdd:COG3401   336 TAVGsssITLSWTAS-SDADV--TGYNVYRSTSGGGTYTKIAETVTT-TSYTDTGLTPGTTYYYKVTAVDAAGnESAPSE 411

                  ...
gi 281359561 3189 ATE 3191
Cdd:COG3401   412 EVS 414
I-set pfam07679
Immunoglobulin I-set domain;
8312-8401 2.68e-20

Immunoglobulin I-set domain;


Pssm-ID: 400151 [Multi-domain]  Cd Length: 90  Bit Score: 88.85  E-value: 2.68e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561  8312 PRFVIRPSSQFCYEGQSVKFYCRCIAIATPTLTWSHNNIELRQSVKFMKRYVGDDYYFIINRVKLDDRGEYIIRAENHYG 8391
Cdd:pfam07679    1 PKFTQKPKDVEVQEGESARFTCTVTGTPDPEVSWFKDGQPLRSSDRFKVTYEGGTYTLTISNVQPDDSGKYTCVATNSAG 80
                           90
                   ....*....|
gi 281359561  8392 SREEVVFLNV 8401
Cdd:pfam07679   81 EAEASAELTV 90
I-set pfam07679
Immunoglobulin I-set domain;
7648-7737 2.95e-20

Immunoglobulin I-set domain;


Pssm-ID: 400151 [Multi-domain]  Cd Length: 90  Bit Score: 88.85  E-value: 2.95e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561  7648 PLIVKPLRDANCIQNHNAQFTCTINGVPKPTISWYKGAREISNGARYHMYSEGDNHFLNINDVFGEDADEYVCRAVNKAG 7727
Cdd:pfam07679    1 PKFTQKPKDVEVQEGESARFTCTVTGTPDPEVSWFKDGQPLRSSDRFKVTYEGGTYTLTISNVQPDDSGKYTCVATNSAG 80
                           90
                   ....*....|
gi 281359561  7728 AKSTRATLAI 7737
Cdd:pfam07679   81 EAEASAELTV 90
FN3 cd00063
Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein ...
6754-6840 3.42e-20

Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein fibronectin. Its tenth fibronectin type III repeat contains an RGD cell recognition sequence in a flexible loop between 2 strands. Approximately 2% of all animal proteins contain the FN3 repeat; including extracellular and intracellular proteins, membrane spanning cytokine receptors, growth hormone receptors, tyrosine phosphatase receptors, and adhesion molecules. FN3-like domains are also found in bacterial glycosyl hydrolases.


Pssm-ID: 238020 [Multi-domain]  Cd Length: 93  Bit Score: 88.71  E-value: 3.42e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 6754 PNTPGIPHGIDSTEDSITIAWTKPKHDGGsPITGYIIEKRLLSDDKWTKAVHALCPDLSCKIPNLIENAEYEFRVAAVNA 6833
Cdd:cd00063     1 PSPPTNLRVTDVTSTSVTLSWTPPEDDGG-PITGYVVEYREKGSGDWKEVEVTPGSETSYTLTGLKPGTEYEFRVRAVNG 79

                  ....*..
gi 281359561 6834 AGQSAYS 6840
Cdd:cd00063    80 GGESPPS 86
FN3 cd00063
Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein ...
3296-3390 5.46e-20

Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein fibronectin. Its tenth fibronectin type III repeat contains an RGD cell recognition sequence in a flexible loop between 2 strands. Approximately 2% of all animal proteins contain the FN3 repeat; including extracellular and intracellular proteins, membrane spanning cytokine receptors, growth hormone receptors, tyrosine phosphatase receptors, and adhesion molecules. FN3-like domains are also found in bacterial glycosyl hydrolases.


Pssm-ID: 238020 [Multi-domain]  Cd Length: 93  Bit Score: 88.32  E-value: 5.46e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 3296 PSKPEGpIEVSDIHKEGCKLKWRKPKDDGGiPITGYVIEKMDTATGKWVPAGSVDPEKYDIEIKGLDPNHRYQFRVKAVN 3375
Cdd:cd00063     1 PSPPTN-LRVTDVTSTSVTLSWTPPEDDGG-PITGYVVEYREKGSGDWKEVEVTPGSETSYTLTGLKPGTEYEFRVRAVN 78
                          90
                  ....*....|....*
gi 281359561 3376 EEGESEPLETESAIT 3390
Cdd:cd00063    79 GGGESPPSESVTVTT 93
FN3 COG3401
Fibronectin type 3 domain [General function prediction only];
5021-5264 7.24e-20

Fibronectin type 3 domain [General function prediction only];


Pssm-ID: 442628 [Multi-domain]  Cd Length: 603  Bit Score: 98.54  E-value: 7.24e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 5021 YSKDNVKVTNVDYNTKLKVNSATRSDSGI---YTVFAENANGEDSADVKVTVIDKPAPPNGP--LKVDEINSESCTLHWN 5095
Cdd:COG3401   175 SATAAVATTSLTVTSTTLVDGGGDIEPGTtyyYRVAATDTGGESAPSNEVSVTTPTTPPSAPtgLTATADTPGSVTLSWD 254
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 5096 PPDDDGgqpIDNYVVEKLDETTGRWIPAGETDGpvTALKVGGLTPGHKYKFRVRAKNRQGT-SEPLTTAQAIIAKNPfdv 5174
Cdd:COG3401   255 PVTESD---ATGYRVYRSNSGDGPFTKVATVTT--TSYTDTGLTNGTTYYYRVTAVDAAGNeSAPSNVVSVTTDLTP--- 326
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 5175 PTKPGTPTIKDFDKEFVDLEWTrpeADGGSPITGYVVEKRDKFSPDWEKCAEISDDiTNAHVPDLIEGLKYEFRVRAVNK 5254
Cdd:COG3401   327 PAAPSGLTATAVGSSSITLSWT---ASSDADVTGYNVYRSTSGGGTYTKIAETVTT-TSYTDTGLTPGTTYYYKVTAVDA 402
                         250
                  ....*....|
gi 281359561 5255 AGPGSPSDAT 5264
Cdd:COG3401   403 AGNESAPSEE 412
FN3 cd00063
Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein ...
5175-5265 1.12e-19

Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein fibronectin. Its tenth fibronectin type III repeat contains an RGD cell recognition sequence in a flexible loop between 2 strands. Approximately 2% of all animal proteins contain the FN3 repeat; including extracellular and intracellular proteins, membrane spanning cytokine receptors, growth hormone receptors, tyrosine phosphatase receptors, and adhesion molecules. FN3-like domains are also found in bacterial glycosyl hydrolases.


Pssm-ID: 238020 [Multi-domain]  Cd Length: 93  Bit Score: 87.55  E-value: 1.12e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 5175 PTKPGTPTIKDFDKEFVDLEWTRPEADGGsPITGYVVEKRDKFSPDWEKCAEISDDITNAHVPDLIEGLKYEFRVRAVNK 5254
Cdd:cd00063     1 PSPPTNLRVTDVTSTSVTLSWTPPEDDGG-PITGYVVEYREKGSGDWKEVEVTPGSETSYTLTGLKPGTEYEFRVRAVNG 79
                          90
                  ....*....|.
gi 281359561 5255 AGPGSPSDATE 5265
Cdd:cd00063    80 GGESPPSESVT 90
FN3 COG3401
Fibronectin type 3 domain [General function prediction only];
7421-7762 1.31e-19

Fibronectin type 3 domain [General function prediction only];


Pssm-ID: 442628 [Multi-domain]  Cd Length: 603  Bit Score: 97.77  E-value: 1.31e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 7421 YQIEFTNESGSATGEFYVHITGMPSAPTGPMGISYINK--NSCMLNWRPPSYDGglkVSHYVIERKDVSSPHWITVSSTc 7498
Cdd:COG3401   207 YRVAATDTGGESAPSNEVSVTTPTTPPSAPTGLTATADtpGSVTLSWDPVTESD---ATGYRVYRSNSGDGPFTKVATV- 282
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 7499 KDTAFNVQGLIENQEYIFRVMAVNENG-MGPPlegLNPIRAKDPIDPPSPPGSPQITEIGGDFVHLEWEKPESdggAHIQ 7577
Cdd:COG3401   283 TTTSYTDTGLTNGTTYYYRVTAVDAAGnESAP---SNVVSVTTDLTPPAAPSGLTATAVGSSSITLSWTASSD---ADVT 356
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 7578 GYWIDKREVGSNTWQRVNATICAANQINcINLIEGRQYEFRIFAQNVAGLstESSASQAVKIIDPQAASPPLIVKPLRDA 7657
Cdd:COG3401   357 GYNVYRSTSGGGTYTKIAETVTTTSYTD-TGLTPGTTYYYKVTAVDAAGN--ESAPSEEVSATTASAASGESLTASVDAV 433
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 7658 NCIQNHNAQFTCTINGVPKPTISWYKGAREISNGARYHMYSEGDNHFLNINDVFGEDADEYVcrAVNKAGAKSTRATLAI 7737
Cdd:COG3401   434 PLTDVAGATAAASAASNPGVSAAVLADGGDTGNAVPFTTTSSTVTATTTDTTTANLSVTTGS--LVGGSGASSVTNSVSV 511
                         330       340
                  ....*....|....*....|....*
gi 281359561 7738 MTAPKLNVPPRFRDTAYFDKGENVV 7762
Cdd:COG3401   512 IGASAAAAVGGAPDGTPNVTGASPV 536
FN3 cd00063
Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein ...
2801-2893 2.03e-19

Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein fibronectin. Its tenth fibronectin type III repeat contains an RGD cell recognition sequence in a flexible loop between 2 strands. Approximately 2% of all animal proteins contain the FN3 repeat; including extracellular and intracellular proteins, membrane spanning cytokine receptors, growth hormone receptors, tyrosine phosphatase receptors, and adhesion molecules. FN3-like domains are also found in bacterial glycosyl hydrolases.


Pssm-ID: 238020 [Multi-domain]  Cd Length: 93  Bit Score: 86.78  E-value: 2.03e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 2801 PNKPGTPEVTDYDNQSISLKWAAPNNDGGaPIQKYIIEKKNKNKTEWEKALEIPGDQLEATVAGLQEYGEYQFRVIAVNK 2880
Cdd:cd00063     1 PSPPTNLRVTDVTSTSVTLSWTPPEDDGG-PITGYVVEYREKGSGDWKEVEVTPGSETSYTLTGLKPGTEYEFRVRAVNG 79
                          90
                  ....*....|...
gi 281359561 2881 AGLSPPSDASVPQ 2893
Cdd:cd00063    80 GGESPPSESVTVT 92
FN3 cd00063
Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein ...
3990-4082 2.72e-19

Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein fibronectin. Its tenth fibronectin type III repeat contains an RGD cell recognition sequence in a flexible loop between 2 strands. Approximately 2% of all animal proteins contain the FN3 repeat; including extracellular and intracellular proteins, membrane spanning cytokine receptors, growth hormone receptors, tyrosine phosphatase receptors, and adhesion molecules. FN3-like domains are also found in bacterial glycosyl hydrolases.


Pssm-ID: 238020 [Multi-domain]  Cd Length: 93  Bit Score: 86.40  E-value: 2.72e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 3990 DTPGKPQIVDWSGNHCDLKWRAPEDDGGAsITGYIVERKDPNTGKWQKALETSTPDCKARVNDLIAGNKYQFRIMAVNKA 4069
Cdd:cd00063     2 SPPTNLRVTDVTSTSVTLSWTPPEDDGGP-ITGYVVEYREKGSGDWKEVEVTPGSETSYTLTGLKPGTEYEFRVRAVNGG 80
                          90
                  ....*....|...
gi 281359561 4070 GKSKPSEPSDQMT 4082
Cdd:cd00063    81 GESPPSESVTVTT 93
FN3 smart00060
Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, ...
6359-6441 3.06e-19

Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, fibronectin. The tenth fibronectin type III repeat contains a RGD cell recognition sequence in a flexible loop between 2 strands. Type III modules are present in both extracellular and intracellular proteins.


Pssm-ID: 214495 [Multi-domain]  Cd Length: 83  Bit Score: 85.74  E-value: 3.06e-19
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561   6359 PGAPSQPTISAYTPNSANLEWHPP-DDCGGKPITGYIVERRERGGEWIKCNNyPTPNTSYTVSNLRDGARYEFRVLAVNE 6437
Cdd:smart00060    1 PSPPSNLRVTDVTSTSVTLSWEPPpDDGITGYIVGYRVEYREEGSEWKEVNV-TPSSTSYTLTGLKPGTEYEFRVRAVNG 79

                    ....
gi 281359561   6438 AGPG 6441
Cdd:smart00060   80 AGEG 83
PknB_PASTA_kin NF033483
Stk1 family PASTA domain-containing Ser/Thr kinase;
7987-8193 3.71e-19

Stk1 family PASTA domain-containing Ser/Thr kinase;


Pssm-ID: 468045 [Multi-domain]  Cd Length: 563  Bit Score: 96.02  E-value: 3.71e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 7987 DRYDILEEIGTGAFGVVHRCR----ER-----------STGNIFAAKFipvshsvekdliRREIDIMNQLHHQKLINLHD 8051
Cdd:NF033483    7 GRYEIGERIGRGGMAEVYLAKdtrlDRdvavkvlrpdlARDPEFVARF------------RREAQSAASLSHPNIVSVYD 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 8052 AFEDDDEMILILEFLSGGELFERITAEGyVMTEAEVINYMRQICEGIRHMHEQNIIHLDIKPENIMCqTRSStNVKLIDF 8131
Cdd:NF033483   75 VGEDGGIPYIVMEYVDGRTLKDYIREHG-PLSPEEAVEIMIQILSALEHAHRNGIVHRDIKPQNILI-TKDG-RVKVTDF 151
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 281359561 8132 GLATRLDpneVVKITT-----GTAEFAAPEIVNREPVGFYTDMWATGVLSYVLLSGLSPFAGDNDVQ 8193
Cdd:NF033483  152 GIARALS---STTMTQtnsvlGTVHYLSPEQARGGTVDARSDIYSLGIVLYEMLTGRPPFDGDSPVS 215
FN3 cd00063
Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein ...
3400-3489 4.38e-19

Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein fibronectin. Its tenth fibronectin type III repeat contains an RGD cell recognition sequence in a flexible loop between 2 strands. Approximately 2% of all animal proteins contain the FN3 repeat; including extracellular and intracellular proteins, membrane spanning cytokine receptors, growth hormone receptors, tyrosine phosphatase receptors, and adhesion molecules. FN3-like domains are also found in bacterial glycosyl hydrolases.


Pssm-ID: 238020 [Multi-domain]  Cd Length: 93  Bit Score: 85.63  E-value: 4.38e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 3400 PPGLPELEDWDEHHVKLKWEPPiRDGGSPITNYIIEVMDKDSGEFVKAVETDSPVCKGVVKKLEEGQQYKFRVRAVNKAG 3479
Cdd:cd00063     3 PPTNLRVTDVTSTSVTLSWTPP-EDDGGPITGYVVEYREKGSGDWKEVEVTPGSETSYTLTGLKPGTEYEFRVRAVNGGG 81
                          90
                  ....*....|
gi 281359561 3480 PSDPSEQTNW 3489
Cdd:cd00063    82 ESPPSESVTV 91
FN3 COG3401
Fibronectin type 3 domain [General function prediction only];
2376-2753 6.78e-19

Fibronectin type 3 domain [General function prediction only];


Pssm-ID: 442628 [Multi-domain]  Cd Length: 603  Bit Score: 95.45  E-value: 6.78e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 2376 YKLVLSNSSGTIESEAQVVVLDRPLPPGgpfEPEEIRAS-----HIKMKWKRPDDDGgceISGYALERMDEETGRWIPAG 2450
Cdd:COG3401   207 YRVAATDTGGESAPSNEVSVTTPTTPPS---APTGLTATadtpgSVTLSWDPVTESD---ATGYRVYRSNSGDGPFTKVA 280
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 2451 EVgpNETSFDFKGLTPNKKYKFRVKAINKEG-ESEPLETFDAIVARNpydPPSPPSQPVIDDYDNKSVLLKWKrPPSDGG 2529
Cdd:COG3401   281 TV--TTTSYTDTGLTNGTTYYYRVTAVDAAGnESAPSNVVSVTTDLT---PPAAPSGLTATAVGSSSITLSWT-ASSDAD 354
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 2530 rpITHYIVEIKDKFAPSWSEVAKTDDpNPECNVEGLKEKMVYQFRVRAVNKAG----PSEPSQPTDNHLCKHKNLKPQID 2605
Cdd:COG3401   355 --VTGYNVYRSTSGGGTYTKIAETVT-TTSYTDTGLTPGTTYYYKVTAVDAAGnesaPSEEVSATTASAASGESLTASVD 431
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 2606 RSTFKRVTIKSGRTHKWSVDVLGEPI----PELHWSWRDDIPLTNGDRIKIENVDYHTDFSITNvlrKDSGFYTLKAENR 2681
Cdd:COG3401   432 AVPLTDVAGATAAASAASNPGVSAAVladgGDTGNAVPFTTTSSTVTATTTDTTTANLSVTTGS---LVGGSGASSVTNS 508
                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 281359561 2682 NGIDRETVELVVLGKPSSPKGPLAVSDVTASGCKLQWKKPEDDGGVPIKEYVVEkmDTATGKWVRVGRSPGE 2753
Cdd:COG3401   509 VSVIGASAAAAVGGAPDGTPNVTGASPVTVGASTGDVLITDLVSLTTSASSSVS--GAGLGSGNLYLITTLG 578
FN3 cd00063
Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein ...
3694-3781 9.35e-19

Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein fibronectin. Its tenth fibronectin type III repeat contains an RGD cell recognition sequence in a flexible loop between 2 strands. Approximately 2% of all animal proteins contain the FN3 repeat; including extracellular and intracellular proteins, membrane spanning cytokine receptors, growth hormone receptors, tyrosine phosphatase receptors, and adhesion molecules. FN3-like domains are also found in bacterial glycosyl hydrolases.


Pssm-ID: 238020 [Multi-domain]  Cd Length: 93  Bit Score: 84.86  E-value: 9.35e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 3694 PDRPGKPEPTNWDKDFVDLAWDPPKNDGGaPIQKYVIQMRDKSGRAWVDSATVPGDKCNGTVTGVEEGHEYEFRIVAVNK 3773
Cdd:cd00063     1 PSPPTNLRVTDVTSTSVTLSWTPPEDDGG-PITGYVVEYREKGSGDWKEVEVTPGSETSYTLTGLKPGTEYEFRVRAVNG 79

                  ....*...
gi 281359561 3774 AGPSDPSD 3781
Cdd:cd00063    80 GGESPPSE 87
FN3 cd00063
Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein ...
3102-3191 9.91e-19

Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein fibronectin. Its tenth fibronectin type III repeat contains an RGD cell recognition sequence in a flexible loop between 2 strands. Approximately 2% of all animal proteins contain the FN3 repeat; including extracellular and intracellular proteins, membrane spanning cytokine receptors, growth hormone receptors, tyrosine phosphatase receptors, and adhesion molecules. FN3-like domains are also found in bacterial glycosyl hydrolases.


Pssm-ID: 238020 [Multi-domain]  Cd Length: 93  Bit Score: 84.86  E-value: 9.91e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 3102 SKPGTPNIVDYNEHMVKLKWEAPRSDGGaPISGYIIEKKDKFSPIWDEILSTNTSVPEATVEGLVEGNIYQFRVRAVNKA 3181
Cdd:cd00063     2 SPPTNLRVTDVTSTSVTLSWTPPEDDGG-PITGYVVEYREKGSGDWKEVEVTPGSETSYTLTGLKPGTEYEFRVRAVNGG 80
                          90
                  ....*....|
gi 281359561 3182 GFSDPSDATE 3191
Cdd:cd00063    81 GESPPSESVT 90
FN3 cd00063
Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein ...
5470-5561 1.81e-18

Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein fibronectin. Its tenth fibronectin type III repeat contains an RGD cell recognition sequence in a flexible loop between 2 strands. Approximately 2% of all animal proteins contain the FN3 repeat; including extracellular and intracellular proteins, membrane spanning cytokine receptors, growth hormone receptors, tyrosine phosphatase receptors, and adhesion molecules. FN3-like domains are also found in bacterial glycosyl hydrolases.


Pssm-ID: 238020 [Multi-domain]  Cd Length: 93  Bit Score: 84.09  E-value: 1.81e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 5470 PDKPGQPQATDWGKHFVDLEWSTPKRDGGaPISSYIIEKRPKF-GQWERAAVVLGDNCKAHVPELTNGGEYEFRVIAVNR 5548
Cdd:cd00063     1 PSPPTNLRVTDVTSTSVTLSWTPPEDDGG-PITGYVVEYREKGsGDWKEVEVTPGSETSYTLTGLKPGTEYEFRVRAVNG 79
                          90
                  ....*....|...
gi 281359561 5549 GGPSDPSDPSSTI 5561
Cdd:cd00063    80 GGESPPSESVTVT 92
Ig_Titin_like cd05748
Immunoglobulin (Ig)-like domain of titin and similar proteins; The members here are composed ...
3509-3590 2.06e-18

Immunoglobulin (Ig)-like domain of titin and similar proteins; The members here are composed of the immunoglobulin (Ig)-like domain found in titin-like proteins and similar proteins. Titin (also called connectin) is a fibrous sarcomeric protein specifically found in vertebrate striated muscle. Titin is a giant protein; depending on isoform composition, it ranges from 2970 to 3700 kDa, and is of a length that spans half a sarcomere. Titin largely consists of multiple repeats of Ig-like and fibronectin type 3 (FN-III)-like domains. Titin connects the ends of myosin thick filaments to Z disks and extends along the thick filament to the H zone. It appears to function similarly to an elastic band, keeping the myosin filaments centered in the sarcomere during muscle contraction or stretching. Within the sarcomere, titin is also attached to or is associated with myosin binding protein C (MyBP-C). MyBP-C appears to contribute to the generation of passive tension by titin and like titin has repeated Ig-like and FN-III domains. Also included in this group are worm twitchin and insect projectin, thick filament proteins of invertebrate muscle which also have repeated Ig-like and FN-III domains.


Pssm-ID: 409406 [Multi-domain]  Cd Length: 82  Bit Score: 83.41  E-value: 2.06e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 3509 VIVKTGLSISLDINIRGEPAPKVEWFFNNSSVTSDEHsVKIDNVDYNTKFFVMRAQRSQSGKYIIKATNEVGEDEAELEV 3588
Cdd:cd05748     2 IVVRAGESLRLDIPIKGRPTPTVTWSKDGQPLKETGR-VQIETTASSTSLVIKNAKRSDSGKYTLTLKNSAGEKSATINV 80

                  ..
gi 281359561 3589 TV 3590
Cdd:cd05748    81 KV 82
FN3 cd00063
Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein ...
5370-5462 4.35e-18

Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein fibronectin. Its tenth fibronectin type III repeat contains an RGD cell recognition sequence in a flexible loop between 2 strands. Approximately 2% of all animal proteins contain the FN3 repeat; including extracellular and intracellular proteins, membrane spanning cytokine receptors, growth hormone receptors, tyrosine phosphatase receptors, and adhesion molecules. FN3-like domains are also found in bacterial glycosyl hydrolases.


Pssm-ID: 238020 [Multi-domain]  Cd Length: 93  Bit Score: 82.93  E-value: 4.35e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 5370 PSVPEGpLRNGDVSKNSIVLRWRPPKDDGGsEITHYVVEKMDNEAMRW--VPVGDCTDTEIRADNLIENHDYSFRVRAVN 5447
Cdd:cd00063     1 PSPPTN-LRVTDVTSTSVTLSWTPPEDDGG-PITGYVVEYREKGSGDWkeVEVTPGSETSYTLTGLKPGTEYEFRVRAVN 78
                          90
                  ....*....|....*
gi 281359561 5448 KQGQSQPLTTSQPIT 5462
Cdd:cd00063    79 GGGESPPSESVTVTT 93
Ig_Titin_like cd05748
Immunoglobulin (Ig)-like domain of titin and similar proteins; The members here are composed ...
5286-5366 5.47e-18

Immunoglobulin (Ig)-like domain of titin and similar proteins; The members here are composed of the immunoglobulin (Ig)-like domain found in titin-like proteins and similar proteins. Titin (also called connectin) is a fibrous sarcomeric protein specifically found in vertebrate striated muscle. Titin is a giant protein; depending on isoform composition, it ranges from 2970 to 3700 kDa, and is of a length that spans half a sarcomere. Titin largely consists of multiple repeats of Ig-like and fibronectin type 3 (FN-III)-like domains. Titin connects the ends of myosin thick filaments to Z disks and extends along the thick filament to the H zone. It appears to function similarly to an elastic band, keeping the myosin filaments centered in the sarcomere during muscle contraction or stretching. Within the sarcomere, titin is also attached to or is associated with myosin binding protein C (MyBP-C). MyBP-C appears to contribute to the generation of passive tension by titin and like titin has repeated Ig-like and FN-III domains. Also included in this group are worm twitchin and insect projectin, thick filament proteins of invertebrate muscle which also have repeated Ig-like and FN-III domains.


Pssm-ID: 409406 [Multi-domain]  Cd Length: 82  Bit Score: 82.25  E-value: 5.47e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 5286 IKIKAGNVFEFDVPVTGEPLPSKDWTHEGNMIINTDRVKISNFDDRTKIRILDAKRSDTGVYTLTARNINGTDRHNVKVT 5365
Cdd:cd05748     2 IVVRAGESLRLDIPIKGRPTPTVTWSKDGQPLKETGRVQIETTASSTSLVIKNAKRSDSGKYTLTLKNSAGEKSATINVK 81

                  .
gi 281359561 5366 I 5366
Cdd:cd05748    82 V 82
I-set pfam07679
Immunoglobulin I-set domain;
8437-8525 9.29e-18

Immunoglobulin I-set domain;


Pssm-ID: 400151 [Multi-domain]  Cd Length: 90  Bit Score: 81.92  E-value: 9.29e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561  8437 PSFTFLLRPRVMQARDTCKLLCCLSGKPVPNVRWYKDGREL-SKYEYAMTHSDGVVTMEIIDCKPSDSGKYSCKATNCHG 8515
Cdd:pfam07679    1 PKFTQKPKDVEVQEGESARFTCTVTGTPDPEVSWFKDGQPLrSSDRFKVTYEGGTYTLTISNVQPDDSGKYTCVATNSAG 80
                           90
                   ....*....|
gi 281359561  8516 TDETDCVVIV 8525
Cdd:pfam07679   81 EAEASAELTV 90
FN3 cd00063
Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein ...
4285-4383 1.13e-17

Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein fibronectin. Its tenth fibronectin type III repeat contains an RGD cell recognition sequence in a flexible loop between 2 strands. Approximately 2% of all animal proteins contain the FN3 repeat; including extracellular and intracellular proteins, membrane spanning cytokine receptors, growth hormone receptors, tyrosine phosphatase receptors, and adhesion molecules. FN3-like domains are also found in bacterial glycosyl hydrolases.


Pssm-ID: 238020 [Multi-domain]  Cd Length: 93  Bit Score: 81.77  E-value: 1.13e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 4285 PGKPGTPEAVDWDKDHVDLVWRPPiNDGGSPITGYVVEKREKGTDKWikgTEITIPClGEECKATVPTLNENCEYEFRVK 4364
Cdd:cd00063     1 PSPPTNLRVTDVTSTSVTLSWTPP-EDDGGPITGYVVEYREKGSGDW---KEVEVTP-GSETSYTLTGLKPGTEYEFRVR 75
                          90
                  ....*....|....*....
gi 281359561 4365 AINAAGPGEPSDaSKPIIT 4383
Cdd:cd00063    76 AVNGGGESPPSE-SVTVTT 93
Ig_Titin_like cd05748
Immunoglobulin (Ig)-like domain of titin and similar proteins; The members here are composed ...
7758-7833 1.24e-17

Immunoglobulin (Ig)-like domain of titin and similar proteins; The members here are composed of the immunoglobulin (Ig)-like domain found in titin-like proteins and similar proteins. Titin (also called connectin) is a fibrous sarcomeric protein specifically found in vertebrate striated muscle. Titin is a giant protein; depending on isoform composition, it ranges from 2970 to 3700 kDa, and is of a length that spans half a sarcomere. Titin largely consists of multiple repeats of Ig-like and fibronectin type 3 (FN-III)-like domains. Titin connects the ends of myosin thick filaments to Z disks and extends along the thick filament to the H zone. It appears to function similarly to an elastic band, keeping the myosin filaments centered in the sarcomere during muscle contraction or stretching. Within the sarcomere, titin is also attached to or is associated with myosin binding protein C (MyBP-C). MyBP-C appears to contribute to the generation of passive tension by titin and like titin has repeated Ig-like and FN-III domains. Also included in this group are worm twitchin and insect projectin, thick filament proteins of invertebrate muscle which also have repeated Ig-like and FN-III domains.


Pssm-ID: 409406 [Multi-domain]  Cd Length: 82  Bit Score: 81.10  E-value: 1.24e-17
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 281359561 7758 GENVVIKIPFTGFPKPRIHWVRDGENIESGGHYTVEVKERHAVLIIRDGSHLDSGPYRITAENELGSDTAIIQVQI 7833
Cdd:cd05748     7 GESLRLDIPIKGRPTPTVTWSKDGQPLKETGRVQIETTASSTSLVIKNAKRSDSGKYTLTLKNSAGEKSATINVKV 82
FN3 cd00063
Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein ...
7444-7531 2.10e-17

Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein fibronectin. Its tenth fibronectin type III repeat contains an RGD cell recognition sequence in a flexible loop between 2 strands. Approximately 2% of all animal proteins contain the FN3 repeat; including extracellular and intracellular proteins, membrane spanning cytokine receptors, growth hormone receptors, tyrosine phosphatase receptors, and adhesion molecules. FN3-like domains are also found in bacterial glycosyl hydrolases.


Pssm-ID: 238020 [Multi-domain]  Cd Length: 93  Bit Score: 81.00  E-value: 2.10e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 7444 PSAPTGPMgISYINKNSCMLNWRPPSYDGGlKVSHYVIERKDVSSPHWITVSST-CKDTAFNVQGLIENQEYIFRVMAVN 7522
Cdd:cd00063     1 PSPPTNLR-VTDVTSTSVTLSWTPPEDDGG-PITGYVVEYREKGSGDWKEVEVTpGSETSYTLTGLKPGTEYEFRVRAVN 78

                  ....*....
gi 281359561 7523 ENGMGPPLE 7531
Cdd:cd00063    79 GGGESPPSE 87
IgI_4_MYLK-like cd20976
Fourth Ig-like domain from smooth muscle myosin light chain kinase and similar domains ; a ...
7254-7344 2.34e-17

Fourth Ig-like domain from smooth muscle myosin light chain kinase and similar domains ; a member of the I-set of IgSF domains; The members here are composed of the fourth immunoglobulin (Ig)-like domain from smooth muscle myosin light chain kinase (MYLK) and similar domains. The Ig superfamily (IgSF) is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. Unlike the V-set, one of the distinctive features of I-set domains is the lack of a C" strand. The structure of this group shows that the fourth Ig-like domain from myosin light chain kinase lacks this strand and thus belongs to the I-set of the IgSF. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors, the hemolymph protein hemolin, the muscle proteins titin, telokin, and twitchin, the neuronal adhesion molecule axonin-1, and the signaling molecule semaphorin 4D that is involved in axonal guidance, immune function and angiogenesis.


Pssm-ID: 409568 [Multi-domain]  Cd Length: 90  Bit Score: 80.76  E-value: 2.34e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 7254 PDWITRLQDKVAPFGKDYTLQCAASGKPSPTARWLRNGKEIQMNGGRMTCDSkdGVFRLHISNVQTGDDGDYTCEAMNSL 7333
Cdd:cd20976     2 PSFSSVPKDLEAVEGQDFVAQCSARGKPVPRITWIRNAQPLQYAADRSTCEA--GVGELHIQDVLPEDHGTYTCLAKNAA 79
                          90
                  ....*....|.
gi 281359561 7334 GFVNTSGYLKI 7344
Cdd:cd20976    80 GQVSCSAWVTV 90
fn3 pfam00041
Fibronectin type III domain;
6360-6444 2.43e-17

Fibronectin type III domain;


Pssm-ID: 394996 [Multi-domain]  Cd Length: 85  Bit Score: 80.54  E-value: 2.43e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561  6360 GAPSQPTISAYTPNSANLEWHPPDDCGGkPITGYIVERRERGGEWIKcNNYPTPNT--SYTVSNLRDGARYEFRVLAVNE 6437
Cdd:pfam00041    1 SAPSNLTVTDVTSTSLTVSWTPPPDGNG-PITGYEVEYRPKNSGEPW-NEITVPGTttSVTLTGLKPGTEYEVRVQAVNG 78

                   ....*..
gi 281359561  6438 AGPGHPS 6444
Cdd:pfam00041   79 GGEGPPS 85
FN3 cd00063
Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein ...
2399-2493 2.96e-17

Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein fibronectin. Its tenth fibronectin type III repeat contains an RGD cell recognition sequence in a flexible loop between 2 strands. Approximately 2% of all animal proteins contain the FN3 repeat; including extracellular and intracellular proteins, membrane spanning cytokine receptors, growth hormone receptors, tyrosine phosphatase receptors, and adhesion molecules. FN3-like domains are also found in bacterial glycosyl hydrolases.


Pssm-ID: 238020 [Multi-domain]  Cd Length: 93  Bit Score: 80.62  E-value: 2.96e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 2399 PLPPGGPfEPEEIRASHIKMKWKRPDDDGGcEISGYALERMDEETGRWIPAGEVGPNETSFDFKGLTPNKKYKFRVKAIN 2478
Cdd:cd00063     1 PSPPTNL-RVTDVTSTSVTLSWTPPEDDGG-PITGYVVEYREKGSGDWKEVEVTPGSETSYTLTGLKPGTEYEFRVRAVN 78
                          90
                  ....*....|....*
gi 281359561 2479 KEGESEPLETFDAIV 2493
Cdd:cd00063    79 GGGESPPSESVTVTT 93
FN3 cd00063
Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein ...
6950-7042 3.74e-17

Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein fibronectin. Its tenth fibronectin type III repeat contains an RGD cell recognition sequence in a flexible loop between 2 strands. Approximately 2% of all animal proteins contain the FN3 repeat; including extracellular and intracellular proteins, membrane spanning cytokine receptors, growth hormone receptors, tyrosine phosphatase receptors, and adhesion molecules. FN3-like domains are also found in bacterial glycosyl hydrolases.


Pssm-ID: 238020 [Multi-domain]  Cd Length: 93  Bit Score: 80.23  E-value: 3.74e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 6950 PLPPQGpLNAYDITPDTCTLAWKTPLDDGGsPITNYVVE-KLDNSGSWVKISS-FVRNTHYDVMGLEPHYKYNFRVRAEN 7027
Cdd:cd00063     1 PSPPTN-LRVTDVTSTSVTLSWTPPEDDGG-PITGYVVEyREKGSGDWKEVEVtPGSETSYTLTGLKPGTEYEFRVRAVN 78
                          90
                  ....*....|....*
gi 281359561 7028 QYGLSDPLDIIEPIV 7042
Cdd:cd00063    79 GGGESPPSESVTVTT 93
IgI_4_hemolin-like cd20978
Fourth immunoglobulin (Ig)-like domain of hemolin, and similar domains; a member of the I-set ...
8632-8721 4.21e-17

Fourth immunoglobulin (Ig)-like domain of hemolin, and similar domains; a member of the I-set of IgSF domains; The members here are composed of the fourth immunoglobulin (Ig)-like domain of hemolin and similar proteins. Hemolin, an insect immunoglobulin superfamily (IgSF) member containing four Ig-like domains, is a lipopolysaccharide-binding immune protein induced during bacterial infection. Hemolin shares significant sequence similarity with the first four Ig-like domains of the transmembrane cell adhesion molecules (CAMs) of the L1 family. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. The fourth Ig-like domain of hemolin is a member of the I-set Ig domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set domains, members of the I-set have a discontinuous A strand but lack a C" strand. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors, the muscle proteins titin, telokin, and twitchin, the neuronal adhesion molecule axonin-1, and the signaling molecule semaphorin 4D that is involved in axonal guidance, immune function and angiogenesis.


Pssm-ID: 409570 [Multi-domain]  Cd Length: 88  Bit Score: 79.74  E-value: 4.21e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 8632 PEFT-KPLHDLTIHDGEQLILTCYVKGDPEPQISWSKNGKSLSSSdilDLRYKNGIATLTINEVFPEDEGVITCTATNSV 8710
Cdd:cd20978     1 PKFIqKPEKNVVVKGGQDVTLPCQVTGVPQPKITWLHNGKPLQGP---MERATVEDGTLTIINVQPEDTGYYGCVATNEI 77
                          90
                  ....*....|.
gi 281359561 8711 GAVETKCKLTI 8721
Cdd:cd20978    78 GDIYTETLLHV 88
FN3 cd00063
Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein ...
4185-4271 5.79e-17

Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein fibronectin. Its tenth fibronectin type III repeat contains an RGD cell recognition sequence in a flexible loop between 2 strands. Approximately 2% of all animal proteins contain the FN3 repeat; including extracellular and intracellular proteins, membrane spanning cytokine receptors, growth hormone receptors, tyrosine phosphatase receptors, and adhesion molecules. FN3-like domains are also found in bacterial glycosyl hydrolases.


Pssm-ID: 238020 [Multi-domain]  Cd Length: 93  Bit Score: 79.85  E-value: 5.79e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 4185 PGPPEGpLRVTDVHKEGCKLKWNAPLDDGGlPIDHYIIEKMDVESGRW--LPSGRFKESFAELNNLEPSHEYKFRVLAVN 4262
Cdd:cd00063     1 PSPPTN-LRVTDVTSTSVTLSWTPPEDDGG-PITGYVVEYREKGSGDWkeVEVTPGSETSYTLTGLKPGTEYEFRVRAVN 78

                  ....*....
gi 281359561 4263 TEGESEPLT 4271
Cdd:cd00063    79 GGGESPPSE 87
I-set pfam07679
Immunoglobulin I-set domain;
4989-5069 6.38e-17

Immunoglobulin I-set domain;


Pssm-ID: 400151 [Multi-domain]  Cd Length: 90  Bit Score: 79.22  E-value: 6.38e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561  4989 VRIKAGQSFTFDCKVSGEPAPQTKWLLKKKEVYSKDNVKVTNVDYNTKLKVNSATRSDSGIYTVFAENANGEDSADVKVT 5068
Cdd:pfam07679   10 VEVQEGESARFTCTVTGTPDPEVSWFKDGQPLRSSDRFKVTYEGGTYTLTISNVQPDDSGKYTCVATNSAGEAEASAELT 89

                   .
gi 281359561  5069 V 5069
Cdd:pfam07679   90 V 90
I-set pfam07679
Immunoglobulin I-set domain;
119-210 6.70e-17

Immunoglobulin I-set domain;


Pssm-ID: 400151 [Multi-domain]  Cd Length: 90  Bit Score: 79.22  E-value: 6.70e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561   119 PTFAKKP--AIRQEedGKRLLFECRVNADPIPAIIWFHNGAAVKESERHKITVDKDVHsyfaTLEILNVTVEDAGKYKVN 196
Cdd:pfam07679    1 PKFTQKPkdVEVQE--GESARFTCTVTGTPDPEVSWFKDGQPLRSSDRFKVTYEGGTY----TLTISNVQPDDSGKYTCV 74
                           90
                   ....*....|....
gi 281359561   197 AKNELGESNATISL 210
Cdd:pfam07679   75 ATNSAGEAEASAEL 88
FN3 cd00063
Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein ...
6062-6153 7.39e-17

Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein fibronectin. Its tenth fibronectin type III repeat contains an RGD cell recognition sequence in a flexible loop between 2 strands. Approximately 2% of all animal proteins contain the FN3 repeat; including extracellular and intracellular proteins, membrane spanning cytokine receptors, growth hormone receptors, tyrosine phosphatase receptors, and adhesion molecules. FN3-like domains are also found in bacterial glycosyl hydrolases.


Pssm-ID: 238020 [Multi-domain]  Cd Length: 93  Bit Score: 79.46  E-value: 7.39e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 6062 PGAPGKPELTDSDKNHITIKWKQPiSNGGSPIIGYDIERRDVNTGRWIKINGQPVPTAEYQDDRVTSNHQYQYRISAVNA 6141
Cdd:cd00063     1 PSPPTNLRVTDVTSTSVTLSWTPP-EDDGGPITGYVVEYREKGSGDWKEVEVTPGSETSYTLTGLKPGTEYEFRVRAVNG 79
                          90
                  ....*....|..
gi 281359561 6142 AGNGKTSEPSAI 6153
Cdd:cd00063    80 GGESPPSESVTV 91
FN3 cd00063
Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein ...
3594-3682 8.89e-17

Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein fibronectin. Its tenth fibronectin type III repeat contains an RGD cell recognition sequence in a flexible loop between 2 strands. Approximately 2% of all animal proteins contain the FN3 repeat; including extracellular and intracellular proteins, membrane spanning cytokine receptors, growth hormone receptors, tyrosine phosphatase receptors, and adhesion molecules. FN3-like domains are also found in bacterial glycosyl hydrolases.


Pssm-ID: 238020 [Multi-domain]  Cd Length: 93  Bit Score: 79.08  E-value: 8.89e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 3594 PGKPKGpLQVNDITKHSCKLKWEKPDDDGGsPIDYYEIEKLDPHTGQWLPCGK--STEPEAKVIGLHEGKAYKFRVRAVN 3671
Cdd:cd00063     1 PSPPTN-LRVTDVTSTSVTLSWTPPEDDGG-PITGYVVEYREKGSGDWKEVEVtpGSETSYTLTGLKPGTEYEFRVRAVN 78
                          90
                  ....*....|.
gi 281359561 3672 KEGESEDLETE 3682
Cdd:cd00063    79 GGGESPPSESV 89
FN3 smart00060
Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, ...
6950-7032 9.20e-17

Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, fibronectin. The tenth fibronectin type III repeat contains a RGD cell recognition sequence in a flexible loop between 2 strands. Type III modules are present in both extracellular and intracellular proteins.


Pssm-ID: 214495 [Multi-domain]  Cd Length: 83  Bit Score: 78.81  E-value: 9.20e-17
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561   6950 PLPPQGpLNAYDITPDTCTLAWKTPLDDGG-SPITNYVVEKLDNSGSWVKISSFVRNTHYDVMGLEPHYKYNFRVRAENQ 7028
Cdd:smart00060    1 PSPPSN-LRVTDVTSTSVTLSWEPPPDDGItGYIVGYRVEYREEGSEWKEVNVTPSSTSYTLTGLKPGTEYEFRVRAVNG 79

                    ....
gi 281359561   7029 YGLS 7032
Cdd:smart00060   80 AGEG 83
FN3 smart00060
Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, ...
4879-4961 9.29e-17

Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, fibronectin. The tenth fibronectin type III repeat contains a RGD cell recognition sequence in a flexible loop between 2 strands. Type III modules are present in both extracellular and intracellular proteins.


Pssm-ID: 214495 [Multi-domain]  Cd Length: 83  Bit Score: 78.81  E-value: 9.29e-17
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561   4879 PGKPENLKATDWDKDHVDLAWTPPLIDGG-SPISCYIIEKQDKYGKWERaLDVPADQCKATIPDLVEGQTYKFRVSAVNA 4957
Cdd:smart00060    1 PSPPSNLRVTDVTSTSVTLSWEPPPDDGItGYIVGYRVEYREEGSEWKE-VNVTPSSTSYTLTGLKPGTEYEFRVRAVNG 79

                    ....
gi 281359561   4958 AGTG 4961
Cdd:smart00060   80 AGEG 83
Ig_Titin_like cd05748
Immunoglobulin (Ig)-like domain of titin and similar proteins; The members here are composed ...
3212-3292 1.35e-16

Immunoglobulin (Ig)-like domain of titin and similar proteins; The members here are composed of the immunoglobulin (Ig)-like domain found in titin-like proteins and similar proteins. Titin (also called connectin) is a fibrous sarcomeric protein specifically found in vertebrate striated muscle. Titin is a giant protein; depending on isoform composition, it ranges from 2970 to 3700 kDa, and is of a length that spans half a sarcomere. Titin largely consists of multiple repeats of Ig-like and fibronectin type 3 (FN-III)-like domains. Titin connects the ends of myosin thick filaments to Z disks and extends along the thick filament to the H zone. It appears to function similarly to an elastic band, keeping the myosin filaments centered in the sarcomere during muscle contraction or stretching. Within the sarcomere, titin is also attached to or is associated with myosin binding protein C (MyBP-C). MyBP-C appears to contribute to the generation of passive tension by titin and like titin has repeated Ig-like and FN-III domains. Also included in this group are worm twitchin and insect projectin, thick filament proteins of invertebrate muscle which also have repeated Ig-like and FN-III domains.


Pssm-ID: 409406 [Multi-domain]  Cd Length: 82  Bit Score: 78.02  E-value: 1.35e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 3212 IKVRAGQPVKFDVDVKGEPAPSLTWFLKETELTSTGQVRLENIDYNTKLTLLDTDRKQSGQYKLRAENINGVDEAVVEVI 3291
Cdd:cd05748     2 IVVRAGESLRLDIPIKGRPTPTVTWSKDGQPLKETGRVQIETTASSTSLVIKNAKRSDSGKYTLTLKNSAGEKSATINVK 81

                  .
gi 281359561 3292 I 3292
Cdd:cd05748    82 V 82
IgI_2_Titin_Z1z2-like cd20972
Second Ig-like domain of the giant muscle protein titin Z1z2 in the sarcomeric Z-disk, and ...
8739-8829 1.43e-16

Second Ig-like domain of the giant muscle protein titin Z1z2 in the sarcomeric Z-disk, and similar domains; a member of the I-set of IgSF domains; The members here are composed of the second immunoglobulin (Ig)-like domain of the giant muscle protein titin Z1z2 in the sarcomeric Z-disk and similar proteins. Titin is a key component in the assembly and functioning of vertebrate striated muscles. By providing connections at the level of individual microfilaments, it contributes to the fine balance of forces between the two halves of the sarcomere. The Ig superfamily (IgSF) is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. Unlike the V-set, one of the distinctive features of I-set domains is the lack of a C" strand. The structure of the titin Z1z2 lacks this strand and thus it belongs to the I-set of the IgSF. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors, the hemolymph protein hemolin, the muscle proteins titin, telokin, and twitchin, the neuronal adhesion molecule axonin-1, and the signaling molecule semaphorin 4D that is involved in axonal guidance, immune function and angiogenesis.


Pssm-ID: 409564 [Multi-domain]  Cd Length: 91  Bit Score: 78.39  E-value: 1.43e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 8739 APKIVSHLESRFVRDGDAVNLACRIIGAQHFDVVWLHNNKEIKPSKDFQYTNEANIYRLQIAEIFPEDGGTYTCEAFNDI 8818
Cdd:cd20972     1 PPQFIQKLRSQEVAEGSKVRLECRVTGNPTPVVRWFCEGKELQNSPDIQIHQEGDLHSLIIAEAFEEDTGRYSCLATNSV 80
                          90
                  ....*....|.
gi 281359561 8819 GESFSTCTINV 8829
Cdd:cd20972    81 GSDTTSAEIFV 91
FN3 cd00063
Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein ...
2100-2194 2.28e-16

Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein fibronectin. Its tenth fibronectin type III repeat contains an RGD cell recognition sequence in a flexible loop between 2 strands. Approximately 2% of all animal proteins contain the FN3 repeat; including extracellular and intracellular proteins, membrane spanning cytokine receptors, growth hormone receptors, tyrosine phosphatase receptors, and adhesion molecules. FN3-like domains are also found in bacterial glycosyl hydrolases.


Pssm-ID: 238020 [Multi-domain]  Cd Length: 93  Bit Score: 77.92  E-value: 2.28e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 2100 PQPPQDVDITDVYQTSCVVSFNPPSDDGGtPITKYVIERQDLSKKhGWESVAEVLPSEPCLKkIDDLIPKKQYRFRIRAV 2179
Cdd:cd00063     1 PSPPTNLRVTDVTSTSVTLSWTPPEDDGG-PITGYVVEYREKGSG-DWKEVEVTPGSETSYT-LTGLKPGTEYEFRVRAV 77
                          90
                  ....*....|....*
gi 281359561 2180 NAIGQSDPATFKNTI 2194
Cdd:cd00063    78 NGGGESPPSESVTVT 92
IG_like smart00410
Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.
8640-8721 3.99e-16

Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.


Pssm-ID: 214653 [Multi-domain]  Cd Length: 85  Bit Score: 77.16  E-value: 3.99e-16
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561   8640 DLTIHDGEQLILTCYVKGDPEPQISWSKNG-KSLSSSDILDLRYKNGIATLTINEVFPEDEGVITCTATNSVGAVETKCK 8718
Cdd:smart00410    3 SVTVKEGESVTLSCEASGSPPPEVTWYKQGgKLLAESGRFSVSRSGSTSTLTISNVTPEDSGTYTCAATNSSGSASSGTT 82

                    ...
gi 281359561   8719 LTI 8721
Cdd:smart00410   83 LTV 85
FN3 cd00063
Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein ...
7837-7927 5.43e-16

Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein fibronectin. Its tenth fibronectin type III repeat contains an RGD cell recognition sequence in a flexible loop between 2 strands. Approximately 2% of all animal proteins contain the FN3 repeat; including extracellular and intracellular proteins, membrane spanning cytokine receptors, growth hormone receptors, tyrosine phosphatase receptors, and adhesion molecules. FN3-like domains are also found in bacterial glycosyl hydrolases.


Pssm-ID: 238020 [Multi-domain]  Cd Length: 93  Bit Score: 76.77  E-value: 5.43e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 7837 PDPPRFPLIESIGTESLSLSWKAPVWDGcSDITNYYVERREHPLSSWIRVGNTRF--TSMAVSGLTPGKEYDFRIFADNV 7914
Cdd:cd00063     1 PSPPTNLRVTDVTSTSVTLSWTPPEDDG-GPITGYVVEYREKGSGDWKEVEVTPGseTSYTLTGLKPGTEYEFRVRAVNG 79
                          90
                  ....*....|...
gi 281359561 7915 YGRSDASDTSTLI 7927
Cdd:cd00063    80 GGESPPSESVTVT 92
fn3 pfam00041
Fibronectin type III domain;
2201-2289 1.01e-15

Fibronectin type III domain;


Pssm-ID: 394996 [Multi-domain]  Cd Length: 85  Bit Score: 75.91  E-value: 1.01e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561  2201 DEPGKPKAVDLTDwdkDHADLKWEAPEtDGGDPITAYIVEYKEKFSNDWVSGKEVDGDARTATVDGLKEGQQYEFRVRAV 2280
Cdd:pfam00041    1 SAPSNLTVTDVTS---TSLTVSWTPPP-DGNGPITGYEVEYRPKNSGEPWNEITVPGTTTSVTLTGLKPGTEYEVRVQAV 76

                   ....*....
gi 281359561  2281 NRAGPGEPS 2289
Cdd:pfam00041   77 NGGGEGPPS 85
I-set pfam07679
Immunoglobulin I-set domain;
3795-3885 1.17e-15

Immunoglobulin I-set domain;


Pssm-ID: 400151 [Multi-domain]  Cd Length: 90  Bit Score: 75.76  E-value: 1.17e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561  3795 PHIDRKnLQKKIMRSGQMLHIDALIKAEPPAKVTWTYNKTEIKTSDHIKIENEDYKTTFIMPKVKRADRGIYIVTAKNDS 3874
Cdd:pfam07679    1 PKFTQK-PKDVEVQEGESARFTCTVTGTPDPEVSWFKDGQPLRSSDRFKVTYEGGTYTLTISNVQPDDSGKYTCVATNSA 79
                           90
                   ....*....|.
gi 281359561  3875 GSDTVEVELEV 3885
Cdd:pfam07679   80 GEAEASAELTV 90
IgI_Myotilin_C_like cd05744
Immunoglobulin (Ig)-like domain of myotilin, palladin, and myopalladin; member of the I-set of ...
119-211 1.87e-15

Immunoglobulin (Ig)-like domain of myotilin, palladin, and myopalladin; member of the I-set of Ig superfamily (IgSF) domains; The members here are composed of the immunoglobulin (Ig)-like domain in myotilin, palladin, and myopalladin. Myotilin, palladin, and myopalladin function as scaffolds that regulate actin organization. Myotilin and myopalladin are most abundant in skeletal and cardiac muscle; palladin is ubiquitously expressed in the organs of developing vertebrates and plays a key role in cellular morphogenesis. The three family members each interact with specific molecular partners with all three binding to alpha-actinin; In addition, palladin also binds to vasodilator-stimulated phosphoprotein (VASP) and ezrin, myotilin binds to filamin and actin, and myopalladin also binds to nebulin and cardiac ankyrin repeat protein (CARP). This group belongs to the I-set of IgSF domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand, but lack a C" strand.


Pssm-ID: 409405 [Multi-domain]  Cd Length: 91  Bit Score: 75.22  E-value: 1.87e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561  119 PTFAKKPAIRQEEDGKRLLFECRVNADPIPAIIWFHNGAAVKESERHKITVDKD-VHSyfatLEILNVTVEDAGKYKVNA 197
Cdd:cd05744     1 PHFLQAPGDLEVQEGRLCRFDCKVSGLPTPDLFWQLNGKPVRPDSAHKMLVRENgRHS----LIIEPVTKRDAGIYTCIA 76
                          90
                  ....*....|....
gi 281359561  198 KNELGESNATISLN 211
Cdd:cd05744    77 RNRAGENSFNAELV 90
I-set pfam07679
Immunoglobulin I-set domain;
5276-5366 2.12e-15

Immunoglobulin I-set domain;


Pssm-ID: 400151 [Multi-domain]  Cd Length: 90  Bit Score: 74.99  E-value: 2.12e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561  5276 PKIDRnFMSDIKIKAGNVFEFDVPVTGEPLPSKDWTHEGNMIINTDRVKISNFDDRTKIRILDAKRSDTGVYTLTARNIN 5355
Cdd:pfam07679    1 PKFTQ-KPKDVEVQEGESARFTCTVTGTPDPEVSWFKDGQPLRSSDRFKVTYEGGTYTLTISNVQPDDSGKYTCVATNSA 79
                           90
                   ....*....|.
gi 281359561  5356 GTDRHNVKVTI 5366
Cdd:pfam07679   80 GEAEASAELTV 90
FN3 smart00060
Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, ...
6754-6837 2.55e-15

Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, fibronectin. The tenth fibronectin type III repeat contains a RGD cell recognition sequence in a flexible loop between 2 strands. Type III modules are present in both extracellular and intracellular proteins.


Pssm-ID: 214495 [Multi-domain]  Cd Length: 83  Bit Score: 74.57  E-value: 2.55e-15
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561   6754 PNTPGIPHGIDSTEDSITIAWTKPKHDGG-SPITGYIIEKRLlSDDKWTKaVHALCPDLSCKIPNLIENAEYEFRVAAVN 6832
Cdd:smart00060    1 PSPPSNLRVTDVTSTSVTLSWEPPPDDGItGYIVGYRVEYRE-EGSEWKE-VNVTPSSTSYTLTGLKPGTEYEFRVRAVN 78

                    ....*
gi 281359561   6833 AAGQS 6837
Cdd:smart00060   79 GAGEG 83
FN3 smart00060
Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, ...
5073-5157 2.60e-15

Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, fibronectin. The tenth fibronectin type III repeat contains a RGD cell recognition sequence in a flexible loop between 2 strands. Type III modules are present in both extracellular and intracellular proteins.


Pssm-ID: 214495 [Multi-domain]  Cd Length: 83  Bit Score: 74.57  E-value: 2.60e-15
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561   5073 PAPPnGPLKVDEINSESCTLHWNPPDDDGGQ-PIDNYVVEKlDETTGRWIPAgETDGPVTALKVGGLTPGHKYKFRVRAK 5151
Cdd:smart00060    1 PSPP-SNLRVTDVTSTSVTLSWEPPPDDGITgYIVGYRVEY-REEGSEWKEV-NVTPSSTSYTLTGLKPGTEYEFRVRAV 77

                    ....*.
gi 281359561   5152 NRQGTS 5157
Cdd:smart00060   78 NGAGEG 83
FN3 smart00060
Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, ...
2203-2286 2.98e-15

Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, fibronectin. The tenth fibronectin type III repeat contains a RGD cell recognition sequence in a flexible loop between 2 strands. Type III modules are present in both extracellular and intracellular proteins.


Pssm-ID: 214495 [Multi-domain]  Cd Length: 83  Bit Score: 74.57  E-value: 2.98e-15
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561   2203 PGKPKAVDLTDWDKDHADLKWEAPETDGGdpiTAYIVEYKEKFSNDWVSGKEV--DGDARTATVDGLKEGQQYEFRVRAV 2280
Cdd:smart00060    1 PSPPSNLRVTDVTSTSVTLSWEPPPDDGI---TGYIVGYRVEYREEGSEWKEVnvTPSSTSYTLTGLKPGTEYEFRVRAV 77

                    ....*.
gi 281359561   2281 NRAGPG 2286
Cdd:smart00060   78 NGAGEG 83
I-set pfam07679
Immunoglobulin I-set domain;
4685-4775 3.05e-15

Immunoglobulin I-set domain;


Pssm-ID: 400151 [Multi-domain]  Cd Length: 90  Bit Score: 74.60  E-value: 3.05e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561  4685 PKIDRRnLRNITLSSGTALKLDANITGEPAPKVEWKLSNYHLQSGKNVTIETPDYYTKLVIRPTQRSDSGEYLVTATNTS 4764
Cdd:pfam07679    1 PKFTQK-PKDVEVQEGESARFTCTVTGTPDPEVSWFKDGQPLRSSDRFKVTYEGGTYTLTISNVQPDDSGKYTCVATNSA 79
                           90
                   ....*....|.
gi 281359561  4765 GKDSVLVNVVI 4775
Cdd:pfam07679   80 GEAEASAELTV 90
fn3 pfam00041
Fibronectin type III domain;
5765-5850 3.29e-15

Fibronectin type III domain;


Pssm-ID: 394996 [Multi-domain]  Cd Length: 85  Bit Score: 74.37  E-value: 3.29e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561  5765 DAPGKPIITDWDRDHIDLQWAVPKsDGGAPISEYIIQKKEKGSPYWTNVRHVPSNKNTTTIPELTEGQEYEFRVIAVNQA 5844
Cdd:pfam00041    1 SAPSNLTVTDVTSTSLTVSWTPPP-DGNGPITGYEVEYRPKNSGEPWNEITVPGTTTSVTLTGLKPGTEYEVRVQAVNGG 79

                   ....*.
gi 281359561  5845 GQSEPS 5850
Cdd:pfam00041   80 GEGPPS 85
I-set pfam07679
Immunoglobulin I-set domain;
3208-3292 3.33e-15

Immunoglobulin I-set domain;


Pssm-ID: 400151 [Multi-domain]  Cd Length: 90  Bit Score: 74.60  E-value: 3.33e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561  3208 KMKPIKVRAGQPVKFDVDVKGEPAPSLTWFLKETELTSTGQVRLENIDYNTKLTLLDTDRKQSGQYKLRAENINGVDEAV 3287
Cdd:pfam07679    6 KPKDVEVQEGESARFTCTVTGTPDPEVSWFKDGQPLRSSDRFKVTYEGGTYTLTISNVQPDDSGKYTCVATNSAGEAEAS 85

                   ....*
gi 281359561  3288 VEVII 3292
Cdd:pfam07679   86 AELTV 90
FN3 smart00060
Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, ...
2501-2584 3.59e-15

Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, fibronectin. The tenth fibronectin type III repeat contains a RGD cell recognition sequence in a flexible loop between 2 strands. Type III modules are present in both extracellular and intracellular proteins.


Pssm-ID: 214495 [Multi-domain]  Cd Length: 83  Bit Score: 74.19  E-value: 3.59e-15
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561   2501 PSPPSQPVIDDYDNKSVLLKWKRPPSDGGR-PITHYIVEIKDKfAPSWSEVaKTDDPNPECNVEGLKEKMVYQFRVRAVN 2579
Cdd:smart00060    1 PSPPSNLRVTDVTSTSVTLSWEPPPDDGITgYIVGYRVEYREE-GSEWKEV-NVTPSSTSYTLTGLKPGTEYEFRVRAVN 78

                    ....*
gi 281359561   2580 KAGPS 2584
Cdd:smart00060   79 GAGEG 83
I-set pfam07679
Immunoglobulin I-set domain;
7254-7334 5.15e-15

Immunoglobulin I-set domain;


Pssm-ID: 400151 [Multi-domain]  Cd Length: 90  Bit Score: 73.83  E-value: 5.15e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561  7254 PDWITRLQDKVAPFGKDYTLQCAASGKPSPTARWLRNGKEIQmNGGRMTCDSKDGVFRLHISNVQTGDDGDYTCEAMNSL 7333
Cdd:pfam07679    1 PKFTQKPKDVEVQEGESARFTCTVTGTPDPEVSWFKDGQPLR-SSDRFKVTYEGGTYTLTISNVQPDDSGKYTCVATNSA 79

                   .
gi 281359561  7334 G 7334
Cdd:pfam07679   80 G 80
FN3 smart00060
Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, ...
2999-3083 5.89e-15

Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, fibronectin. The tenth fibronectin type III repeat contains a RGD cell recognition sequence in a flexible loop between 2 strands. Type III modules are present in both extracellular and intracellular proteins.


Pssm-ID: 214495 [Multi-domain]  Cd Length: 83  Bit Score: 73.80  E-value: 5.89e-15
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561   2999 PSKPRGpLDVKDVTKDSCKLKWKKPEDDGG-KPISAYQVEKfDKKQGRWVPLgRTSANDTEFDVKGLQEGHEYQFRVKAI 3077
Cdd:smart00060    1 PSPPSN-LRVTDVTSTSVTLSWEPPPDDGItGYIVGYRVEY-REEGSEWKEV-NVTPSSTSYTLTGLKPGTEYEFRVRAV 77

                    ....*.
gi 281359561   3078 NEEGES 3083
Cdd:smart00060   78 NGAGEG 83
IG_like smart00410
Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.
4989-5069 6.87e-15

Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.


Pssm-ID: 214653 [Multi-domain]  Cd Length: 85  Bit Score: 73.31  E-value: 6.87e-15
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561   4989 VRIKAGQSFTFDCKVSGEPAPQTKWLLKK-KEVYSKDNVKVTNVDYNTKLKVNSATRSDSGIYTVFAENANGEDSADVKV 5067
Cdd:smart00410    4 VTVKEGESVTLSCEASGSPPPEVTWYKQGgKLLAESGRFSVSRSGSTSTLTISNVTPEDSGTYTCAATNSSGSASSGTTL 83

                    ..
gi 281359561   5068 TV 5069
Cdd:smart00410   84 TV 85
FN3 smart00060
Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, ...
7151-7234 8.45e-15

Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, fibronectin. The tenth fibronectin type III repeat contains a RGD cell recognition sequence in a flexible loop between 2 strands. Type III modules are present in both extracellular and intracellular proteins.


Pssm-ID: 214495 [Multi-domain]  Cd Length: 83  Bit Score: 73.03  E-value: 8.45e-15
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561   7151 PSPPGAPQVTRVGKNYVDLKWEKPLRDGG-SRITGYIIERRDIGGAvWVKCNDyNVLDTEYTVMNLIEMGDYEFRVFAVN 7229
Cdd:smart00060    1 PSPPSNLRVTDVTSTSVTLSWEPPPDDGItGYIVGYRVEYREEGSE-WKEVNV-TPSSTSYTLTGLKPGTEYEFRVRAVN 78

                    ....*
gi 281359561   7230 SAGRS 7234
Cdd:smart00060   79 GAGEG 83
I-set pfam07679
Immunoglobulin I-set domain;
4090-4181 1.19e-14

Immunoglobulin I-set domain;


Pssm-ID: 400151 [Multi-domain]  Cd Length: 90  Bit Score: 73.06  E-value: 1.19e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561  4090 PKIDRTnIKDITIKAGQHIRFDIKVSGEPPATKVWLHNKARLENDDSnYNIDMESYRTKLTVPISKRFHSGKYTLKAENE 4169
Cdd:pfam07679    1 PKFTQK-PKDVEVQEGESARFTCTVTGTPDPEVSWFKDGQPLRSSDR-FKVTYEGGTYTLTISNVQPDDSGKYTCVATNS 78
                           90
                   ....*....|..
gi 281359561  4170 SGRDEASFEVIV 4181
Cdd:pfam07679   79 AGEAEASAELTV 90
fn3 pfam00041
Fibronectin type III domain;
2803-2887 1.49e-14

Fibronectin type III domain;


Pssm-ID: 394996 [Multi-domain]  Cd Length: 85  Bit Score: 72.45  E-value: 1.49e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561  2803 KPGTPEVTDYDNQSISLKWAAPNnDGGAPIQKYIIEKKNKNKTEWEKALEIPGDQLEATVAGLQEYGEYQFRVIAVNKAG 2882
Cdd:pfam00041    2 APSNLTVTDVTSTSLTVSWTPPP-DGNGPITGYEVEYRPKNSGEPWNEITVPGTTTSVTLTGLKPGTEYEVRVQAVNGGG 80

                   ....*
gi 281359561  2883 LSPPS 2887
Cdd:pfam00041   81 EGPPS 85
Ig_Titin_like cd05748
Immunoglobulin (Ig)-like domain of titin and similar proteins; The members here are composed ...
2314-2395 1.53e-14

Immunoglobulin (Ig)-like domain of titin and similar proteins; The members here are composed of the immunoglobulin (Ig)-like domain found in titin-like proteins and similar proteins. Titin (also called connectin) is a fibrous sarcomeric protein specifically found in vertebrate striated muscle. Titin is a giant protein; depending on isoform composition, it ranges from 2970 to 3700 kDa, and is of a length that spans half a sarcomere. Titin largely consists of multiple repeats of Ig-like and fibronectin type 3 (FN-III)-like domains. Titin connects the ends of myosin thick filaments to Z disks and extends along the thick filament to the H zone. It appears to function similarly to an elastic band, keeping the myosin filaments centered in the sarcomere during muscle contraction or stretching. Within the sarcomere, titin is also attached to or is associated with myosin binding protein C (MyBP-C). MyBP-C appears to contribute to the generation of passive tension by titin and like titin has repeated Ig-like and FN-III domains. Also included in this group are worm twitchin and insect projectin, thick filament proteins of invertebrate muscle which also have repeated Ig-like and FN-III domains.


Pssm-ID: 409406 [Multi-domain]  Cd Length: 82  Bit Score: 72.24  E-value: 1.53e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 2314 VTVKKGQTIRFDIKYDGEPEPAATWVKGTDNLKfDNQRICLDQLERNSSITIKKSVRKDTGKYKLVLSNSSGTIESEAQV 2393
Cdd:cd05748     2 IVVRAGESLRLDIPIKGRPTPTVTWSKDGQPLK-ETGRVQIETTASSTSLVIKNAKRSDSGKYTLTLKNSAGEKSATINV 80

                  ..
gi 281359561 2394 VV 2395
Cdd:cd05748    81 KV 82
IgI_titin_I1-like cd20951
Immunoglobulin domain I1 of the titin I-band and similar proteins; a member of the I-set of ...
7648-7735 1.70e-14

Immunoglobulin domain I1 of the titin I-band and similar proteins; a member of the I-set of IgSF domains; The members here are composed of the immunoglobulin domain I1 of the titin I-band and similar proteins. Titin is a key component in the assembly and functioning of vertebrate striated muscles. By providing connections at the level of individual microfilaments, it contributes to the fine balance of forces between the two halves of the sarcomere. The Ig superfamily (IgSF) is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. The two sheets are linked together by a conserved disulfide bond between B strand and F strand. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. The Ig I1 domain of the titin I-band is a member of the I-set Ig domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand but lack a C" strand. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors, the hemolymph protein hemolin, the muscle proteins titin, telokin, and twitchin, the neuronal adhesion molecule axonin-1, and the signaling molecule semaphorin 4D that is involved in axonal guidance, immune function and angiogenesis.


Pssm-ID: 409543 [Multi-domain]  Cd Length: 94  Bit Score: 72.84  E-value: 1.70e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 7648 PLIVKPLRDANCIQNHNAQFTCTINGVPKPTISWYKGAREI---SNGARYHMYSEGDNHFLNINDVFGEDADEYVCRAVN 7724
Cdd:cd20951     1 PEFIIRLQSHTVWEKSDAKLRVEVQGKPDPEVKWYKNGVPIdpsSIPGKYKIESEYGVHVLHIRRVTVEDSAVYSAVAKN 80
                          90
                  ....*....|.
gi 281359561 7725 KAGAKSTRATL 7735
Cdd:cd20951    81 IHGEASSSASV 91
FN3 smart00060
Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, ...
5764-5847 1.74e-14

Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, fibronectin. The tenth fibronectin type III repeat contains a RGD cell recognition sequence in a flexible loop between 2 strands. Type III modules are present in both extracellular and intracellular proteins.


Pssm-ID: 214495 [Multi-domain]  Cd Length: 83  Bit Score: 72.26  E-value: 1.74e-14
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561   5764 PDAPGKPIITDWDRDHIDLQWAVPKSDGG-APISEYIIQKKEKGSPyWTNVrHVPSNKNTTTIPELTEGQEYEFRVIAVN 5842
Cdd:smart00060    1 PSPPSNLRVTDVTSTSVTLSWEPPPDDGItGYIVGYRVEYREEGSE-WKEV-NVTPSSTSYTLTGLKPGTEYEFRVRAVN 78

                    ....*
gi 281359561   5843 QAGQS 5847
Cdd:smart00060   79 GAGEG 83
IG_like smart00410
Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.
7268-7344 2.17e-14

Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.


Pssm-ID: 214653 [Multi-domain]  Cd Length: 85  Bit Score: 72.15  E-value: 2.17e-14
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 281359561   7268 GKDYTLQCAASGKPSPTARWLRNGKEIQMNGGRMTCDSKDGVFRLHISNVQTGDDGDYTCEAMNSLGFVNTSGYLKI 7344
Cdd:smart00410    9 GESVTLSCEASGSPPPEVTWYKQGGKLLAESGRFSVSRSGSTSTLTISNVTPEDSGTYTCAATNSSGSASSGTTLTV 85
Ig_Titin_like cd05748
Immunoglobulin (Ig)-like domain of titin and similar proteins; The members here are composed ...
3806-3885 2.55e-14

Immunoglobulin (Ig)-like domain of titin and similar proteins; The members here are composed of the immunoglobulin (Ig)-like domain found in titin-like proteins and similar proteins. Titin (also called connectin) is a fibrous sarcomeric protein specifically found in vertebrate striated muscle. Titin is a giant protein; depending on isoform composition, it ranges from 2970 to 3700 kDa, and is of a length that spans half a sarcomere. Titin largely consists of multiple repeats of Ig-like and fibronectin type 3 (FN-III)-like domains. Titin connects the ends of myosin thick filaments to Z disks and extends along the thick filament to the H zone. It appears to function similarly to an elastic band, keeping the myosin filaments centered in the sarcomere during muscle contraction or stretching. Within the sarcomere, titin is also attached to or is associated with myosin binding protein C (MyBP-C). MyBP-C appears to contribute to the generation of passive tension by titin and like titin has repeated Ig-like and FN-III domains. Also included in this group are worm twitchin and insect projectin, thick filament proteins of invertebrate muscle which also have repeated Ig-like and FN-III domains.


Pssm-ID: 409406 [Multi-domain]  Cd Length: 82  Bit Score: 71.85  E-value: 2.55e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 3806 IMRSGQMLHIDALIKAEPPAKVTWTYNKTEIKTSDHIKIENEDYKTTFIMPKVKRADRGIYIVTAKNDSGSDTVEVELEV 3885
Cdd:cd05748     3 VVRAGESLRLDIPIKGRPTPTVTWSKDGQPLKETGRVQIETTASSTSLVIKNAKRSDSGKYTLTLKNSAGEKSATINVKV 82
FN3 smart00060
Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, ...
5370-5452 5.44e-14

Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, fibronectin. The tenth fibronectin type III repeat contains a RGD cell recognition sequence in a flexible loop between 2 strands. Type III modules are present in both extracellular and intracellular proteins.


Pssm-ID: 214495 [Multi-domain]  Cd Length: 83  Bit Score: 70.72  E-value: 5.44e-14
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561   5370 PSVPEGpLRNGDVSKNSIVLRWRPPKDDGG-SEITHYVVEKMDNEAmRWVPV-GDCTDTEIRADNLIENHDYSFRVRAVN 5447
Cdd:smart00060    1 PSPPSN-LRVTDVTSTSVTLSWEPPPDDGItGYIVGYRVEYREEGS-EWKEVnVTPSSTSYTLTGLKPGTEYEFRVRAVN 78

                    ....*
gi 281359561   5448 KQGQS 5452
Cdd:smart00060   79 GAGEG 83
FN3 smart00060
Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, ...
7444-7527 5.77e-14

Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, fibronectin. The tenth fibronectin type III repeat contains a RGD cell recognition sequence in a flexible loop between 2 strands. Type III modules are present in both extracellular and intracellular proteins.


Pssm-ID: 214495 [Multi-domain]  Cd Length: 83  Bit Score: 70.72  E-value: 5.77e-14
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561   7444 PSAPTGPMgISYINKNSCMLNWRPPSYDGGLK-VSHYVIERKDvSSPHWITVSSTCKDTAFNVQGLIENQEYIFRVMAVN 7522
Cdd:smart00060    1 PSPPSNLR-VTDVTSTSVTLSWEPPPDDGITGyIVGYRVEYRE-EGSEWKEVNVTPSSTSYTLTGLKPGTEYEFRVRAVN 78

                    ....*
gi 281359561   7523 ENGMG 7527
Cdd:smart00060   79 GAGEG 83
I-set pfam07679
Immunoglobulin I-set domain;
228-320 6.42e-14

Immunoglobulin I-set domain;


Pssm-ID: 400151 [Multi-domain]  Cd Length: 90  Bit Score: 70.75  E-value: 6.42e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561   228 PTFTERPVIRQSEDGGNVTFECRCVGDPTPTVTWSHGETELNESNRYKMslTMDQKLYHiacLEISSVVSSDQGEYRAQA 307
Cdd:pfam07679    1 PKFTQKPKDVEVQEGESARFTCTVTGTPDPEVSWFKDGQPLRSSDRFKV--TYEGGTYT---LTISNVQPDDSGKYTCVA 75
                           90
                   ....*....|...
gi 281359561   308 KNKHGSGVATINL 320
Cdd:pfam07679   76 TNSAGEAEASAEL 88
FN3 cd00063
Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein ...
4779-4863 6.74e-14

Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein fibronectin. Its tenth fibronectin type III repeat contains an RGD cell recognition sequence in a flexible loop between 2 strands. Approximately 2% of all animal proteins contain the FN3 repeat; including extracellular and intracellular proteins, membrane spanning cytokine receptors, growth hormone receptors, tyrosine phosphatase receptors, and adhesion molecules. FN3-like domains are also found in bacterial glycosyl hydrolases.


Pssm-ID: 238020 [Multi-domain]  Cd Length: 93  Bit Score: 70.99  E-value: 6.74e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 4779 PSPPNGpLQISDVHKEGCHLKWKRPSDDGGTPIEYF-QIDKLEPETGCWIPSCRSTEPQVDVTGLSPGNEYKFRVSAVNA 4857
Cdd:cd00063     1 PSPPTN-LRVTDVTSTSVTLSWTPPEDDGGPITGYVvEYREKGSGDWKEVEVTPGSETSYTLTGLKPGTEYEFRVRAVNG 79

                  ....*.
gi 281359561 4858 EGESQP 4863
Cdd:cd00063    80 GGESPP 85
FN3 cd00063
Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein ...
5664-5755 9.11e-14

Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein fibronectin. Its tenth fibronectin type III repeat contains an RGD cell recognition sequence in a flexible loop between 2 strands. Approximately 2% of all animal proteins contain the FN3 repeat; including extracellular and intracellular proteins, membrane spanning cytokine receptors, growth hormone receptors, tyrosine phosphatase receptors, and adhesion molecules. FN3-like domains are also found in bacterial glycosyl hydrolases.


Pssm-ID: 238020 [Multi-domain]  Cd Length: 93  Bit Score: 70.60  E-value: 9.11e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 5664 PSPPKGpLDITKITRDGCHLTWNVPDDDGGsPILHYIIEKMDLSRSTWS--DAGMSTHIVHDVTRLVHRKEYLFRVKAVN 5741
Cdd:cd00063     1 PSPPTN-LRVTDVTSTSVTLSWTPPEDDGG-PITGYVVEYREKGSGDWKevEVTPGSETSYTLTGLKPGTEYEFRVRAVN 78
                          90
                  ....*....|....
gi 281359561 5742 AIGESDPLEAVNTI 5755
Cdd:cd00063    79 GGGESPPSESVTVT 92
FN3 smart00060
Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, ...
3889-3971 9.66e-14

Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, fibronectin. The tenth fibronectin type III repeat contains a RGD cell recognition sequence in a flexible loop between 2 strands. Type III modules are present in both extracellular and intracellular proteins.


Pssm-ID: 214495 [Multi-domain]  Cd Length: 83  Bit Score: 70.34  E-value: 9.66e-14
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561   3889 PSKPKGpLAVSNVTAETLHLKWEKPEDDGGDPIEQYLVERMDTETGRWVPVLTT-KTPEADVTGLTEGKEYLFRVKAVNS 3967
Cdd:smart00060    1 PSPPSN-LRVTDVTSTSVTLSWEPPPDDGITGYIVGYRVEYREEGSEWKEVNVTpSSTSYTLTGLKPGTEYEFRVRAVNG 79

                    ....
gi 281359561   3968 EGES 3971
Cdd:smart00060   80 AGEG 83
IgI_titin_I1-like cd20951
Immunoglobulin domain I1 of the titin I-band and similar proteins; a member of the I-set of ...
8437-8526 1.27e-13

Immunoglobulin domain I1 of the titin I-band and similar proteins; a member of the I-set of IgSF domains; The members here are composed of the immunoglobulin domain I1 of the titin I-band and similar proteins. Titin is a key component in the assembly and functioning of vertebrate striated muscles. By providing connections at the level of individual microfilaments, it contributes to the fine balance of forces between the two halves of the sarcomere. The Ig superfamily (IgSF) is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. The two sheets are linked together by a conserved disulfide bond between B strand and F strand. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. The Ig I1 domain of the titin I-band is a member of the I-set Ig domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand but lack a C" strand. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors, the hemolymph protein hemolin, the muscle proteins titin, telokin, and twitchin, the neuronal adhesion molecule axonin-1, and the signaling molecule semaphorin 4D that is involved in axonal guidance, immune function and angiogenesis.


Pssm-ID: 409543 [Multi-domain]  Cd Length: 94  Bit Score: 70.14  E-value: 1.27e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 8437 PSFTFLLRPRVMQARDTCKLLCCLSGKPVPNVRWYKDGRELS------KYEYamtHS-DGVVTMEIIDCKPSDSGKYSCK 8509
Cdd:cd20951     1 PEFIIRLQSHTVWEKSDAKLRVEVQGKPDPEVKWYKNGVPIDpssipgKYKI---ESeYGVHVLHIRRVTVEDSAVYSAV 77
                          90
                  ....*....|....*..
gi 281359561 8510 ATNCHGTDETDCVVIVE 8526
Cdd:cd20951    78 AKNIHGEASSSASVVVE 94
I-set pfam07679
Immunoglobulin I-set domain;
545-636 1.31e-13

Immunoglobulin I-set domain;


Pssm-ID: 400151 [Multi-domain]  Cd Length: 90  Bit Score: 69.98  E-value: 1.31e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561   545 FIEKPRIVSENNGKLVIMECKVKADPKPDVIWFRNGEVIKESNKIKtfIEQRGDQYyiKLELLDPQLEDSGLYKCNIKNT 624
Cdd:pfam07679    3 FTQKPKDVEVQEGESARFTCTVTGTPDPEVSWFKDGQPLRSSDRFK--VTYEGGTY--TLTISNVQPDDSGKYTCVATNS 78
                           90
                   ....*....|..
gi 281359561   625 LGELNANLTLNI 636
Cdd:pfam07679   79 AGEAEASAELTV 90
fn3 pfam00041
Fibronectin type III domain;
5073-5159 1.67e-13

Fibronectin type III domain;


Pssm-ID: 394996 [Multi-domain]  Cd Length: 85  Bit Score: 69.37  E-value: 1.67e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561  5073 PAPPNgpLKVDEINSESCTLHWNPPDDDGGqPIDNYVVEKLDETTGRWIPAGETDGPVTALKVGGLTPGHKYKFRVRAKN 5152
Cdd:pfam00041    1 SAPSN--LTVTDVTSTSLTVSWTPPPDGNG-PITGYEVEYRPKNSGEPWNEITVPGTTTSVTLTGLKPGTEYEVRVQAVN 77

                   ....*..
gi 281359561  5153 RQGTSEP 5159
Cdd:pfam00041   78 GGGEGPP 84
FN3 smart00060
Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, ...
3400-3481 2.56e-13

Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, fibronectin. The tenth fibronectin type III repeat contains a RGD cell recognition sequence in a flexible loop between 2 strands. Type III modules are present in both extracellular and intracellular proteins.


Pssm-ID: 214495 [Multi-domain]  Cd Length: 83  Bit Score: 68.80  E-value: 2.56e-13
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561   3400 PPGLPELEDWDEHHVKLKWEPPIRDGG-SPITNYIIEvmDKDSGEFVKAVETDSPVCKGVVKKLEEGQQYKFRVRAVNKA 3478
Cdd:smart00060    3 PPSNLRVTDVTSTSVTLSWEPPPDDGItGYIVGYRVE--YREEGSEWKEVNVTPSSTSYTLTGLKPGTEYEFRVRAVNGA 80

                    ...
gi 281359561   3479 GPS 3481
Cdd:smart00060   81 GEG 83
fn3 pfam00041
Fibronectin type III domain;
6757-6840 2.56e-13

Fibronectin type III domain;


Pssm-ID: 394996 [Multi-domain]  Cd Length: 85  Bit Score: 68.98  E-value: 2.56e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561  6757 PGIPHGIDSTEDSITIAWTKPKhDGGSPITGYIIEKRLLSDDKWTKAVHALCPDLSCKIPNLIENAEYEFRVAAVNAAGQ 6836
Cdd:pfam00041    3 PSNLTVTDVTSTSLTVSWTPPP-DGNGPITGYEVEYRPKNSGEPWNEITVPGTTTSVTLTGLKPGTEYEVRVQAVNGGGE 81

                   ....
gi 281359561  6837 SAYS 6840
Cdd:pfam00041   82 GPPS 85
FN3 smart00060
Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, ...
3594-3676 2.66e-13

Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, fibronectin. The tenth fibronectin type III repeat contains a RGD cell recognition sequence in a flexible loop between 2 strands. Type III modules are present in both extracellular and intracellular proteins.


Pssm-ID: 214495 [Multi-domain]  Cd Length: 83  Bit Score: 68.80  E-value: 2.66e-13
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561   3594 PGKPKGpLQVNDITKHSCKLKWEKPDDDGG-SPIDYYEIEKLDPHTGQWLPCGKSTEPEAKVIGLHEGKAYKFRVRAVNK 3672
Cdd:smart00060    1 PSPPSN-LRVTDVTSTSVTLSWEPPPDDGItGYIVGYRVEYREEGSEWKEVNVTPSSTSYTLTGLKPGTEYEFRVRAVNG 79

                    ....
gi 281359561   3673 EGES 3676
Cdd:smart00060   80 AGEG 83
FN3 smart00060
Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, ...
2697-2783 4.05e-13

Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, fibronectin. The tenth fibronectin type III repeat contains a RGD cell recognition sequence in a flexible loop between 2 strands. Type III modules are present in both extracellular and intracellular proteins.


Pssm-ID: 214495 [Multi-domain]  Cd Length: 83  Bit Score: 68.41  E-value: 4.05e-13
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561   2697 PSSPKGpLAVSDVTASGCKLQWKKPEDDGGV-PIKEYVVEKMDTaTGKWVRVGRSPGEkepPSFDVTGLSLGSEYMFRVS 2775
Cdd:smart00060    1 PSPPSN-LRVTDVTSTSVTLSWEPPPDDGITgYIVGYRVEYREE-GSEWKEVNVTPSS---TSYTLTGLKPGTEYEFRVR 75

                    ....*...
gi 281359561   2776 AVNEEGES 2783
Cdd:smart00060   76 AVNGAGEG 83
Ig_Titin_like cd05748
Immunoglobulin (Ig)-like domain of titin and similar proteins; The members here are composed ...
5874-5954 6.36e-13

Immunoglobulin (Ig)-like domain of titin and similar proteins; The members here are composed of the immunoglobulin (Ig)-like domain found in titin-like proteins and similar proteins. Titin (also called connectin) is a fibrous sarcomeric protein specifically found in vertebrate striated muscle. Titin is a giant protein; depending on isoform composition, it ranges from 2970 to 3700 kDa, and is of a length that spans half a sarcomere. Titin largely consists of multiple repeats of Ig-like and fibronectin type 3 (FN-III)-like domains. Titin connects the ends of myosin thick filaments to Z disks and extends along the thick filament to the H zone. It appears to function similarly to an elastic band, keeping the myosin filaments centered in the sarcomere during muscle contraction or stretching. Within the sarcomere, titin is also attached to or is associated with myosin binding protein C (MyBP-C). MyBP-C appears to contribute to the generation of passive tension by titin and like titin has repeated Ig-like and FN-III domains. Also included in this group are worm twitchin and insect projectin, thick filament proteins of invertebrate muscle which also have repeated Ig-like and FN-III domains.


Pssm-ID: 409406 [Multi-domain]  Cd Length: 82  Bit Score: 67.61  E-value: 6.36e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 5874 VRIKCGLIFHTDIHFIGEPAPEATWTLNSNPLLSNDRSTITSIGHHSVVHTVNCQRSDSGIYHLLLRNSSGIDEGSFELV 5953
Cdd:cd05748     2 IVVRAGESLRLDIPIKGRPTPTVTWSKDGQPLKETGRVQIETTASSTSLVIKNAKRSDSGKYTLTLKNSAGEKSATINVK 81

                  .
gi 281359561 5954 V 5954
Cdd:cd05748    82 V 82
fn3 pfam00041
Fibronectin type III domain;
4880-4964 6.73e-13

Fibronectin type III domain;


Pssm-ID: 394996 [Multi-domain]  Cd Length: 85  Bit Score: 67.83  E-value: 6.73e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561  4880 GKPENLKATDWDKDHVDLAWTPPLiDGGSPISCYIIEKQDKY-GKWERALDVPADQCKATIPDLVEGQTYKFRVSAVNAA 4958
Cdd:pfam00041    1 SAPSNLTVTDVTSTSLTVSWTPPP-DGNGPITGYEVEYRPKNsGEPWNEITVPGTTTSVTLTGLKPGTEYEVRVQAVNGG 79

                   ....*.
gi 281359561  4959 GTGEPS 4964
Cdd:pfam00041   80 GEGPPS 85
FN3 smart00060
Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, ...
4779-4861 7.20e-13

Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, fibronectin. The tenth fibronectin type III repeat contains a RGD cell recognition sequence in a flexible loop between 2 strands. Type III modules are present in both extracellular and intracellular proteins.


Pssm-ID: 214495 [Multi-domain]  Cd Length: 83  Bit Score: 67.64  E-value: 7.20e-13
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561   4779 PSPPnGPLQISDVHKEGCHLKWKRPSDDGGT-PIEYFQIDKLEPETGCWIPSCRSTEPQVDVTGLSPGNEYKFRVSAVNA 4857
Cdd:smart00060    1 PSPP-SNLRVTDVTSTSVTLSWEPPPDDGITgYIVGYRVEYREEGSEWKEVNVTPSSTSYTLTGLKPGTEYEFRVRAVNG 79

                    ....
gi 281359561   4858 EGES 4861
Cdd:smart00060   80 AGEG 83
FN3 smart00060
Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, ...
5470-5552 7.20e-13

Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, fibronectin. The tenth fibronectin type III repeat contains a RGD cell recognition sequence in a flexible loop between 2 strands. Type III modules are present in both extracellular and intracellular proteins.


Pssm-ID: 214495 [Multi-domain]  Cd Length: 83  Bit Score: 67.64  E-value: 7.20e-13
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561   5470 PDKPGQPQATDWGKHFVDLEWSTPKRDGG-APISSYIIEKRPKFGQWERAAVVLGDNcKAHVPELTNGGEYEFRVIAVNR 5548
Cdd:smart00060    1 PSPPSNLRVTDVTSTSVTLSWEPPPDDGItGYIVGYRVEYREEGSEWKEVNVTPSST-SYTLTGLKPGTEYEFRVRAVNG 79

                    ....
gi 281359561   5549 GGPS 5552
Cdd:smart00060   80 AGEG 83
FN3 smart00060
Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, ...
2100-2185 7.86e-13

Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, fibronectin. The tenth fibronectin type III repeat contains a RGD cell recognition sequence in a flexible loop between 2 strands. Type III modules are present in both extracellular and intracellular proteins.


Pssm-ID: 214495 [Multi-domain]  Cd Length: 83  Bit Score: 67.64  E-value: 7.86e-13
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561   2100 PQPPQDVDITDVYQTSCVVSFNPPSDDGGT-PITKYVIERQDlsKKHGWESVAEVLPSEPClkKIDDLIPKKQYRFRIRA 2178
Cdd:smart00060    1 PSPPSNLRVTDVTSTSVTLSWEPPPDDGITgYIVGYRVEYRE--EGSEWKEVNVTPSSTSY--TLTGLKPGTEYEFRVRA 76

                    ....*..
gi 281359561   2179 VNAIGQS 2185
Cdd:smart00060   77 VNGAGEG 83
FN3 smart00060
Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, ...
4285-4372 1.00e-12

Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, fibronectin. The tenth fibronectin type III repeat contains a RGD cell recognition sequence in a flexible loop between 2 strands. Type III modules are present in both extracellular and intracellular proteins.


Pssm-ID: 214495 [Multi-domain]  Cd Length: 83  Bit Score: 67.25  E-value: 1.00e-12
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561   4285 PGKPGTPEAVDWDKDHVDLVWRPPINDGG-SPITGYVVEKREKGtdkwikGTEITIPCLGEECKATVPTLNENCEYEFRV 4363
Cdd:smart00060    1 PSPPSNLRVTDVTSTSVTLSWEPPPDDGItGYIVGYRVEYREEG------SEWKEVNVTPSSTSYTLTGLKPGTEYEFRV 74

                    ....*....
gi 281359561   4364 KAINAAGPG 4372
Cdd:smart00060   75 RAVNGAGEG 83
FN3 smart00060
Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, ...
5958-6044 1.10e-12

Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, fibronectin. The tenth fibronectin type III repeat contains a RGD cell recognition sequence in a flexible loop between 2 strands. Type III modules are present in both extracellular and intracellular proteins.


Pssm-ID: 214495 [Multi-domain]  Cd Length: 83  Bit Score: 67.25  E-value: 1.10e-12
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561   5958 PGPPEGPmEYEEITANSVTISWKPPK-DNGGSEISSYVIEKRDLthGGGWVPAVnyVSAKYNHAVVPRLLEGTMYELRVM 6036
Cdd:smart00060    1 PSPPSNL-RVTDVTSTSVTLSWEPPPdDGITGYIVGYRVEYREE--GSEWKEVN--VTPSSTSYTLTGLKPGTEYEFRVR 75

                    ....*...
gi 281359561   6037 AENLQGRS 6044
Cdd:smart00060   76 AVNGAGEG 83
I-set pfam07679
Immunoglobulin I-set domain;
7758-7833 1.12e-12

Immunoglobulin I-set domain;


Pssm-ID: 400151 [Multi-domain]  Cd Length: 90  Bit Score: 67.28  E-value: 1.12e-12
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 281359561  7758 GENVVIKIPFTGFPKPRIHWVRDGENIESGGHYTVEVKERHAVLIIRDGSHLDSGPYRITAENELGSDTAIIQVQI 7833
Cdd:pfam07679   15 GESARFTCTVTGTPDPEVSWFKDGQPLRSSDRFKVTYEGGTYTLTISNVQPDDSGKYTCVATNSAGEAEASAELTV 90
FN3 smart00060
Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, ...
4484-4566 1.15e-12

Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, fibronectin. The tenth fibronectin type III repeat contains a RGD cell recognition sequence in a flexible loop between 2 strands. Type III modules are present in both extracellular and intracellular proteins.


Pssm-ID: 214495 [Multi-domain]  Cd Length: 83  Bit Score: 67.25  E-value: 1.15e-12
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561   4484 PGKPEGpLEVSEVHKDGCKLKWKKPKDDGGEPVESYLVEKFDPDTGIWLPVGRSDG-PEYNVDGLVPGHDYKFRVKAVNK 4562
Cdd:smart00060    1 PSPPSN-LRVTDVTSTSVTLSWEPPPDDGITGYIVGYRVEYREEGSEWKEVNVTPSsTSYTLTGLKPGTEYEFRVRAVNG 79

                    ....
gi 281359561   4563 EGES 4566
Cdd:smart00060   80 AGEG 83
FN3 smart00060
Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, ...
3694-3777 1.45e-12

Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, fibronectin. The tenth fibronectin type III repeat contains a RGD cell recognition sequence in a flexible loop between 2 strands. Type III modules are present in both extracellular and intracellular proteins.


Pssm-ID: 214495 [Multi-domain]  Cd Length: 83  Bit Score: 66.87  E-value: 1.45e-12
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561   3694 PDRPGKPEPTNWDKDFVDLAWDPPKNDGG-APIQKYVIQMRDKSGRaWVdSATVPGDKCNGTVTGVEEGHEYEFRIVAVN 3772
Cdd:smart00060    1 PSPPSNLRVTDVTSTSVTLSWEPPPDDGItGYIVGYRVEYREEGSE-WK-EVNVTPSSTSYTLTGLKPGTEYEFRVRAVN 78

                    ....*
gi 281359561   3773 KAGPS 3777
Cdd:smart00060   79 GAGEG 83
FN3 smart00060
Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, ...
3296-3380 1.80e-12

Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, fibronectin. The tenth fibronectin type III repeat contains a RGD cell recognition sequence in a flexible loop between 2 strands. Type III modules are present in both extracellular and intracellular proteins.


Pssm-ID: 214495 [Multi-domain]  Cd Length: 83  Bit Score: 66.48  E-value: 1.80e-12
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561   3296 PSKPEGpIEVSDIHKEGCKLKWRKPKDDGGI-PITGYVIEKMDTaTGKWVPAgSVDPEKYDIEIKGLDPNHRYQFRVKAV 3374
Cdd:smart00060    1 PSPPSN-LRVTDVTSTSVTLSWEPPPDDGITgYIVGYRVEYREE-GSEWKEV-NVTPSSTSYTLTGLKPGTEYEFRVRAV 77

                    ....*.
gi 281359561   3375 NEEGES 3380
Cdd:smart00060   78 NGAGEG 83
IG_like smart00410
Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.
7664-7735 1.96e-12

Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.


Pssm-ID: 214653 [Multi-domain]  Cd Length: 85  Bit Score: 66.37  E-value: 1.96e-12
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 281359561   7664 NAQFTCTINGVPKPTISWYK-GAREISNGARYHMYSEGDNHFLNINDVFGEDADEYVCRAVNKAGAKSTRATL 7735
Cdd:smart00410   11 SVTLSCEASGSPPPEVTWYKqGGKLLAESGRFSVSRSGSTSTLTISNVTPEDSGTYTCAATNSSGSASSGTTL 83
I-set pfam07679
Immunoglobulin I-set domain;
2902-2995 2.79e-12

Immunoglobulin I-set domain;


Pssm-ID: 400151 [Multi-domain]  Cd Length: 90  Bit Score: 66.13  E-value: 2.79e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561  2902 PRIDRSnLKPLLIRAGKPIRYDVNVRGEPAPVITWYQNDKELKPEelpSSSEIKNIPYNTKISIIETVRKHTGIYKIIAV 2981
Cdd:pfam07679    1 PKFTQK-PKDVEVQEGESARFTCTVTGTPDPEVSWFKDGQPLRSS---DRFKVTYEGGTYTLTISNVQPDDSGKYTCVAT 76
                           90
                   ....*....|....
gi 281359561  2982 NEHGQDEATVEVNI 2995
Cdd:pfam07679   77 NSAGEAEASAELTV 90
IG_like smart00410
Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.
8751-8829 4.44e-12

Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.


Pssm-ID: 214653 [Multi-domain]  Cd Length: 85  Bit Score: 65.60  E-value: 4.44e-12
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561   8751 VRDGDAVNLACRIIGAQHFDVVWLHNN-KEIKPSKDFQYTNEANIYRLQIAEIFPEDGGTYTCEAFNDIGESFSTCTINV 8829
Cdd:smart00410    6 VKEGESVTLSCEASGSPPPEVTWYKQGgKLLAESGRFSVSRSGSTSTLTISNVTPEDSGTYTCAATNSSGSASSGTTLTV 85
FN3 smart00060
Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, ...
4185-4267 5.64e-12

Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, fibronectin. The tenth fibronectin type III repeat contains a RGD cell recognition sequence in a flexible loop between 2 strands. Type III modules are present in both extracellular and intracellular proteins.


Pssm-ID: 214495 [Multi-domain]  Cd Length: 83  Bit Score: 65.33  E-value: 5.64e-12
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561   4185 PGPPEGpLRVTDVHKEGCKLKWNAPLDDGGL-PIDHYIIEKMDVESGRWLPSGRFKESFAELNNLEPSHEYKFRVLAVNT 4263
Cdd:smart00060    1 PSPPSN-LRVTDVTSTSVTLSWEPPPDDGITgYIVGYRVEYREEGSEWKEVNVTPSSTSYTLTGLKPGTEYEFRVRAVNG 79

                    ....
gi 281359561   4264 EGES 4267
Cdd:smart00060   80 AGEG 83
I-set pfam07679
Immunoglobulin I-set domain;
2602-2693 7.54e-12

Immunoglobulin I-set domain;


Pssm-ID: 400151 [Multi-domain]  Cd Length: 90  Bit Score: 64.97  E-value: 7.54e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561  2602 PQIDRSTfKRVTIKSGRTHKWSVDVLGEPIPELHWSwRDDIPLTNGDRIKIENVDYHTDFSITNVLRKDSGFYTLKAENR 2681
Cdd:pfam07679    1 PKFTQKP-KDVEVQEGESARFTCTVTGTPDPEVSWF-KDGQPLRSSDRFKVTYEGGTYTLTISNVQPDDSGKYTCVATNS 78
                           90
                   ....*....|..
gi 281359561  2682 NGIDRETVELVV 2693
Cdd:pfam07679   79 AGEAEASAELTV 90
FN3 smart00060
Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, ...
7837-7918 7.86e-12

Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, fibronectin. The tenth fibronectin type III repeat contains a RGD cell recognition sequence in a flexible loop between 2 strands. Type III modules are present in both extracellular and intracellular proteins.


Pssm-ID: 214495 [Multi-domain]  Cd Length: 83  Bit Score: 64.56  E-value: 7.86e-12
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561   7837 PDPPRFPLIESIGTESLSLSWKAPVWDGC-SDITNYYVERREHPlSSWIRV-GNTRFTSMAVSGLTPGKEYDFRIFADNV 7914
Cdd:smart00060    1 PSPPSNLRVTDVTSTSVTLSWEPPPDDGItGYIVGYRVEYREEG-SEWKEVnVTPSSTSYTLTGLKPGTEYEFRVRAVNG 79

                    ....
gi 281359561   7915 YGRS 7918
Cdd:smart00060   80 AGEG 83
Ig_Titin_like cd05748
Immunoglobulin (Ig)-like domain of titin and similar proteins; The members here are composed ...
2914-2993 8.19e-12

Immunoglobulin (Ig)-like domain of titin and similar proteins; The members here are composed of the immunoglobulin (Ig)-like domain found in titin-like proteins and similar proteins. Titin (also called connectin) is a fibrous sarcomeric protein specifically found in vertebrate striated muscle. Titin is a giant protein; depending on isoform composition, it ranges from 2970 to 3700 kDa, and is of a length that spans half a sarcomere. Titin largely consists of multiple repeats of Ig-like and fibronectin type 3 (FN-III)-like domains. Titin connects the ends of myosin thick filaments to Z disks and extends along the thick filament to the H zone. It appears to function similarly to an elastic band, keeping the myosin filaments centered in the sarcomere during muscle contraction or stretching. Within the sarcomere, titin is also attached to or is associated with myosin binding protein C (MyBP-C). MyBP-C appears to contribute to the generation of passive tension by titin and like titin has repeated Ig-like and FN-III domains. Also included in this group are worm twitchin and insect projectin, thick filament proteins of invertebrate muscle which also have repeated Ig-like and FN-III domains.


Pssm-ID: 409406 [Multi-domain]  Cd Length: 82  Bit Score: 64.53  E-value: 8.19e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 2914 IRAGKPIRYDVNVRGEPAPVITWYQNDKELKPEELPSsseIKNIPYNTKISIIETVRKHTGIYKIIAVNEHGQDEATVEV 2993
Cdd:cd05748     4 VRAGESLRLDIPIKGRPTPTVTWSKDGQPLKETGRVQ---IETTASSTSLVIKNAKRSDSGKYTLTLKNSAGEKSATINV 80
FN3 smart00060
Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, ...
3102-3184 9.09e-12

Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, fibronectin. The tenth fibronectin type III repeat contains a RGD cell recognition sequence in a flexible loop between 2 strands. Type III modules are present in both extracellular and intracellular proteins.


Pssm-ID: 214495 [Multi-domain]  Cd Length: 83  Bit Score: 64.56  E-value: 9.09e-12
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561   3102 SKPGTPNIVDYNEHMVKLKWEAPRSDGG-APISGYIIEKKDKfSPIWDEIlSTNTSVPEATVEGLVEGNIYQFRVRAVNK 3180
Cdd:smart00060    2 SPPSNLRVTDVTSTSVTLSWEPPPDDGItGYIVGYRVEYREE-GSEWKEV-NVTPSSTSYTLTGLKPGTEYEFRVRAVNG 79

                    ....
gi 281359561   3181 AGFS 3184
Cdd:smart00060   80 AGEG 83
fn3 pfam00041
Fibronectin type III domain;
2502-2587 9.18e-12

Fibronectin type III domain;


Pssm-ID: 394996 [Multi-domain]  Cd Length: 85  Bit Score: 64.74  E-value: 9.18e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561  2502 SPPSQPVIDDYDNKSVLLKWKrPPSDGGRPITHYIVEIKDKFAPSWsEVAKTDDPNP-ECNVEGLKEKMVYQFRVRAVNK 2580
Cdd:pfam00041    1 SAPSNLTVTDVTSTSLTVSWT-PPPDGNGPITGYEVEYRPKNSGEP-WNEITVPGTTtSVTLTGLKPGTEYEVRVQAVNG 78

                   ....*..
gi 281359561  2581 AGPSEPS 2587
Cdd:pfam00041   79 GGEGPPS 85
fn3 pfam00041
Fibronectin type III domain;
7546-7631 9.93e-12

Fibronectin type III domain;


Pssm-ID: 394996 [Multi-domain]  Cd Length: 85  Bit Score: 64.36  E-value: 9.93e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561  7546 SPPGSPQITEIGGDFVHLEWEKPEsDGGAHIQGYWIDKREVGSNT-WQRVNATicaANQINCI--NLIEGRQYEFRIFAQ 7622
Cdd:pfam00041    1 SAPSNLTVTDVTSTSLTVSWTPPP-DGNGPITGYEVEYRPKNSGEpWNEITVP---GTTTSVTltGLKPGTEYEVRVQAV 76

                   ....*....
gi 281359561  7623 NVAGLSTES 7631
Cdd:pfam00041   77 NGGGEGPPS 85
I-set pfam07679
Immunoglobulin I-set domain;
8839-8922 1.07e-11

Immunoglobulin I-set domain;


Pssm-ID: 400151 [Multi-domain]  Cd Length: 90  Bit Score: 64.59  E-value: 1.07e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561  8839 PSFVKFPTSVSVLEGEGTTFECEID-SELLNLVWLKDGKPIDETlPRYSFTKDGHRYSFAVAKCNMDDVGQYQAKAV--S 8915
Cdd:pfam07679    1 PKFTQKPKDVEVQEGESARFTCTVTgTPDPEVSWFKDGQPLRSS-DRFKVTYEGGTYTLTISNVQPDDSGKYTCVATnsA 79

                   ....*..
gi 281359561  8916 GKAESIC 8922
Cdd:pfam07679   80 GEAEASA 86
fn3 pfam00041
Fibronectin type III domain;
7152-7237 1.41e-11

Fibronectin type III domain;


Pssm-ID: 394996 [Multi-domain]  Cd Length: 85  Bit Score: 63.97  E-value: 1.41e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561  7152 SPPGAPQVTRVGKNYVDLKWEKPlRDGGSRITGYIIERRDIG-GAVWVKCNDYNVLdTEYTVMNLIEMGDYEFRVFAVNS 7230
Cdd:pfam00041    1 SAPSNLTVTDVTSTSLTVSWTPP-PDGNGPITGYEVEYRPKNsGEPWNEITVPGTT-TSVTLTGLKPGTEYEVRVQAVNG 78

                   ....*..
gi 281359561  7231 AGRSEPS 7237
Cdd:pfam00041   79 GGEGPPS 85
FN3 smart00060
Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, ...
5664-5746 1.68e-11

Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, fibronectin. The tenth fibronectin type III repeat contains a RGD cell recognition sequence in a flexible loop between 2 strands. Type III modules are present in both extracellular and intracellular proteins.


Pssm-ID: 214495 [Multi-domain]  Cd Length: 83  Bit Score: 63.79  E-value: 1.68e-11
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561   5664 PSPPKGpLDITKITRDGCHLTWNVPDDDGG-SPILHYIIEKMDLSRSTWSDAGMSTHIVHDVTRLVHRKEYLFRVKAVNA 5742
Cdd:smart00060    1 PSPPSN-LRVTDVTSTSVTLSWEPPPDDGItGYIVGYRVEYREEGSEWKEVNVTPSSTSYTLTGLKPGTEYEFRVRAVNG 79

                    ....
gi 281359561   5743 IGES 5746
Cdd:smart00060   80 AGEG 83
I-set pfam07679
Immunoglobulin I-set domain;
9-101 2.06e-11

Immunoglobulin I-set domain;


Pssm-ID: 400151 [Multi-domain]  Cd Length: 90  Bit Score: 63.82  E-value: 2.06e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561     9 PSFVKKPQLHQEDDGNRLIFECQLLSSPKPDIEWFRSDNKVVEDVRtkFKIQPVGeNKYTvvLELDDVVETDAGLYKVKA 88
Cdd:pfam07679    1 PKFTQKPKDVEVQEGESARFTCTVTGTPDPEVSWFKDGQPLRSSDR--FKVTYEG-GTYT--LTISNVQPDDSGKYTCVA 75
                           90
                   ....*....|...
gi 281359561    89 KNKSGEVSASINL 101
Cdd:pfam07679   76 TNSAGEAEASAEL 88
IG_like smart00410
Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.
6177-6255 2.22e-11

Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.


Pssm-ID: 214653 [Multi-domain]  Cd Length: 85  Bit Score: 63.68  E-value: 2.22e-11
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561   6177 VRAGEPVNLNIPISGAPTPTIEWKRGDLK-LEEGKRISYETNSERTLFRIDDSNRRDSGKYTVTAANEFGKDTADIEVIV 6255
Cdd:smart00410    6 VKEGESVTLSCEASGSPPPEVTWYKQGGKlLAESGRFSVSRSGSTSTLTISNVTPEDSGTYTCAATNSSGSASSGTTLTV 85
I-set pfam07679
Immunoglobulin I-set domain;
2311-2395 2.22e-11

Immunoglobulin I-set domain;


Pssm-ID: 400151 [Multi-domain]  Cd Length: 90  Bit Score: 63.82  E-value: 2.22e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561  2311 LKNVTVKKGQTIRFDIKYDGEPEPAATWVKGTDNLKfDNQRICLDQLERNSSITIKKSVRKDTGKYKLVLSNSSGTIESE 2390
Cdd:pfam07679    7 PKDVEVQEGESARFTCTVTGTPDPEVSWFKDGQPLR-SSDRFKVTYEGGTYTLTISNVQPDDSGKYTCVATNSAGEAEAS 85

                   ....*
gi 281359561  2391 AQVVV 2395
Cdd:pfam07679   86 AELTV 90
IG_like smart00410
Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.
2610-2693 2.65e-11

Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.


Pssm-ID: 214653 [Multi-domain]  Cd Length: 85  Bit Score: 63.29  E-value: 2.65e-11
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561   2610 KRVTIKSGRTHKWSVDVLGEPIPELHWSWRDDIPLTNGDRIKIENVDYHTDFSITNVLRKDSGFYTLKAENRNGIDRETV 2689
Cdd:smart00410    2 PSVTVKEGESVTLSCEASGSPPPEVTWYKQGGKLLAESGRFSVSRSGSTSTLTISNVTPEDSGTYTCAATNSSGSASSGT 81

                    ....
gi 281359561   2690 ELVV 2693
Cdd:smart00410   82 TLTV 85
fn3 pfam00041
Fibronectin type III domain;
3400-3484 3.70e-11

Fibronectin type III domain;


Pssm-ID: 394996 [Multi-domain]  Cd Length: 85  Bit Score: 62.82  E-value: 3.70e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561  3400 PPGLPELEDWDEHHVKLKWEPPiRDGGSPITNYIIEVMDKDSGEFVKAVETDSPVCKGVVKKLEEGQQYKFRVRAVNKAG 3479
Cdd:pfam00041    2 APSNLTVTDVTSTSLTVSWTPP-PDGNGPITGYEVEYRPKNSGEPWNEITVPGTTTSVTLTGLKPGTEYEVRVQAVNGGG 80

                   ....*
gi 281359561  3480 PSDPS 3484
Cdd:pfam00041   81 EGPPS 85
I-set pfam07679
Immunoglobulin I-set domain;
438-532 4.11e-11

Immunoglobulin I-set domain;


Pssm-ID: 400151 [Multi-domain]  Cd Length: 90  Bit Score: 63.05  E-value: 4.11e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561   438 PSFIEKPRIIPNESGTLITMKCKCKAKPEPTVTWYRGQDLVEKSKKIKInttviAEDTYELTLEIKDPGATDGGTYRCNV 517
Cdd:pfam07679    1 PKFTQKPKDVEVQEGESARFTCTVTGTPDPEVSWFKDGQPLRSSDRFKV-----TYEGGTYTLTISNVQPDDSGKYTCVA 75
                           90
                   ....*....|....*
gi 281359561   518 KNEYGESNANLNLNI 532
Cdd:pfam07679   76 TNSAGEAEASAELTV 90
IG_like smart00410
Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.
242-320 4.90e-11

Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.


Pssm-ID: 214653 [Multi-domain]  Cd Length: 85  Bit Score: 62.52  E-value: 4.90e-11
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561    242 GGNVTFECRCVGDPTPTVTWSH-GETELNESNRYKMSltmdqKLYHIACLEISSVVSSDQGEYRAQAKNKHGSGVATINL 320
Cdd:smart00410    9 GESVTLSCEASGSPPPEVTWYKqGGKLLAESGRFSVS-----RSGSTSTLTISNVTPEDSGTYTCAATNSSGSASSGTTL 83
fn3 pfam00041
Fibronectin type III domain;
6952-7034 5.31e-11

Fibronectin type III domain;


Pssm-ID: 394996 [Multi-domain]  Cd Length: 85  Bit Score: 62.43  E-value: 5.31e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561  6952 PPQGpLNAYDITPDTCTLAWKTPlDDGGSPITNYVVEKLDNSGSWVKISSFVRNTH--YDVMGLEPHYKYNFRVRAENQY 7029
Cdd:pfam00041    2 APSN-LTVTDVTSTSLTVSWTPP-PDGNGPITGYEVEYRPKNSGEPWNEITVPGTTtsVTLTGLKPGTEYEVRVQAVNGG 79

                   ....*
gi 281359561  7030 GLSDP 7034
Cdd:pfam00041   80 GEGPP 84
Ig_3 pfam13927
Immunoglobulin domain; This family contains immunoglobulin-like domains.
4978-5056 6.99e-11

Immunoglobulin domain; This family contains immunoglobulin-like domains.


Pssm-ID: 464046 [Multi-domain]  Cd Length: 78  Bit Score: 61.81  E-value: 6.99e-11
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 281359561  4978 PPIIdRSSLVEVRIKAGQSFTFDCKVSGEPAPQTKWLLKKKEVYSKDNVKVTNVDYNTKLKVNSATRSDSGIYTVFAEN 5056
Cdd:pfam13927    1 KPVI-TVSPSSVTVREGETVTLTCEATGSPPPTITWYKNGEPISSGSTRSRSLSGSNSTLTISNVTRSDAGTYTCVASN 78
I-set pfam07679
Immunoglobulin I-set domain;
1826-1909 8.13e-11

Immunoglobulin I-set domain;


Pssm-ID: 400151 [Multi-domain]  Cd Length: 90  Bit Score: 61.89  E-value: 8.13e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561  1826 KFVKVLKSQQCIEKDTVTLACEIddaMG----EVQWLRNGEEIKPDKRIQIVKDGRKRKLVIKDCKVTDAGQFKCT-TNA 1900
Cdd:pfam07679    2 KFTQKPKDVEVQEGESARFTCTV---TGtpdpEVSWFKDGQPLRSSDRFKVTYEGGTYTLTISNVQPDDSGKYTCVaTNS 78
                           90
                   ....*....|..
gi 281359561  1901 ---DTTESEIII 1909
Cdd:pfam07679   79 ageAEASAELTV 90
IgI_Myotilin_C_like cd05744
Immunoglobulin (Ig)-like domain of myotilin, palladin, and myopalladin; member of the I-set of ...
9-102 8.87e-11

Immunoglobulin (Ig)-like domain of myotilin, palladin, and myopalladin; member of the I-set of Ig superfamily (IgSF) domains; The members here are composed of the immunoglobulin (Ig)-like domain in myotilin, palladin, and myopalladin. Myotilin, palladin, and myopalladin function as scaffolds that regulate actin organization. Myotilin and myopalladin are most abundant in skeletal and cardiac muscle; palladin is ubiquitously expressed in the organs of developing vertebrates and plays a key role in cellular morphogenesis. The three family members each interact with specific molecular partners with all three binding to alpha-actinin; In addition, palladin also binds to vasodilator-stimulated phosphoprotein (VASP) and ezrin, myotilin binds to filamin and actin, and myopalladin also binds to nebulin and cardiac ankyrin repeat protein (CARP). This group belongs to the I-set of IgSF domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand, but lack a C" strand.


Pssm-ID: 409405 [Multi-domain]  Cd Length: 91  Bit Score: 62.13  E-value: 8.87e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561    9 PSFVKKPQLHQEDDGNRLIFECQLLSSPKPDIEWFRSDNKVVEDVRTKFKIQPVGenkyTVVLELDDVVETDAGLYKVKA 88
Cdd:cd05744     1 PHFLQAPGDLEVQEGRLCRFDCKVSGLPTPDLFWQLNGKPVRPDSAHKMLVRENG----RHSLIIEPVTKRDAGIYTCIA 76
                          90
                  ....*....|....
gi 281359561   89 KNKSGEVSASINLN 102
Cdd:cd05744    77 RNRAGENSFNAELV 90
I-set pfam07679
Immunoglobulin I-set domain;
1508-1588 9.98e-11

Immunoglobulin I-set domain;


Pssm-ID: 400151 [Multi-domain]  Cd Length: 90  Bit Score: 61.89  E-value: 9.98e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561  1508 VVEDSTAYLTVGVEGSPAPTFKFYKGVSEILEGGRFKFLTDGQTNTITlcMRKCKPNDESKYKIVVSNIHGEDSAEMQLY 1587
Cdd:pfam07679   12 VQEGESARFTCTVTGTPDPEVSWFKDGQPLRSSDRFKVTYEGGTYTLT--ISNVQPDDSGKYTCVATNSAGEAEASAELT 89

                   .
gi 281359561  1588 V 1588
Cdd:pfam07679   90 V 90
IG_like smart00410
Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.
2312-2395 1.10e-10

Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.


Pssm-ID: 214653 [Multi-domain]  Cd Length: 85  Bit Score: 61.37  E-value: 1.10e-10
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561   2312 KNVTVKKGQTIRFDIKYDGEPEPAATWVKGTDNLKFDNQRICLDQLERNSSITIKKSVRKDTGKYKLVLSNSSGTIESEA 2391
Cdd:smart00410    2 PSVTVKEGESVTLSCEASGSPPPEVTWYKQGGKLLAESGRFSVSRSGSTSTLTISNVTPEDSGTYTCAATNSSGSASSGT 81

                    ....
gi 281359561   2392 QVVV 2395
Cdd:smart00410   82 TLTV 85
fn3 pfam00041
Fibronectin type III domain;
3000-3085 1.66e-10

Fibronectin type III domain;


Pssm-ID: 394996 [Multi-domain]  Cd Length: 85  Bit Score: 60.89  E-value: 1.66e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561  3000 SKPRGpLDVKDVTKDSCKLKWKKPEDDGGkPISAYQVEKFDKKQGRWVPLGRTSANDTEFDVKGLQEGHEYQFRVKAINE 3079
Cdd:pfam00041    1 SAPSN-LTVTDVTSTSLTVSWTPPPDGNG-PITGYEVEYRPKNSGEPWNEITVPGTTTSVTLTGLKPGTEYEVRVQAVNG 78

                   ....*.
gi 281359561  3080 EGESDP 3085
Cdd:pfam00041   79 GGEGPP 84
fn3 pfam00041
Fibronectin type III domain;
2102-2187 1.89e-10

Fibronectin type III domain;


Pssm-ID: 394996 [Multi-domain]  Cd Length: 85  Bit Score: 60.89  E-value: 1.89e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561  2102 PPQDVDITDVYQTSCVVSFNPPSDDGGtPITKYVIERQDLSKKHGWESVAEVLPSEPClkKIDDLIPKKQYRFRIRAVNA 2181
Cdd:pfam00041    2 APSNLTVTDVTSTSLTVSWTPPPDGNG-PITGYEVEYRPKNSGEPWNEITVPGTTTSV--TLTGLKPGTEYEVRVQAVNG 78

                   ....*.
gi 281359561  2182 IGQSDP 2187
Cdd:pfam00041   79 GGEGPP 84
fn3 pfam00041
Fibronectin type III domain;
3102-3187 3.05e-10

Fibronectin type III domain;


Pssm-ID: 394996 [Multi-domain]  Cd Length: 85  Bit Score: 60.12  E-value: 3.05e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561  3102 SKPGTPNIVDYNEHMVKLKWEAPRsDGGAPISGYIIEKKDKFSP-IWDEILSTNTSvPEATVEGLVEGNIYQFRVRAVNK 3180
Cdd:pfam00041    1 SAPSNLTVTDVTSTSLTVSWTPPP-DGNGPITGYEVEYRPKNSGePWNEITVPGTT-TSVTLTGLKPGTEYEVRVQAVNG 78

                   ....*..
gi 281359561  3181 AGFSDPS 3187
Cdd:pfam00041   79 GGEGPPS 85
IG_like smart00410
Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.
7758-7833 4.35e-10

Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.


Pssm-ID: 214653 [Multi-domain]  Cd Length: 85  Bit Score: 59.83  E-value: 4.35e-10
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 281359561   7758 GENVVIKIPFTGFPKPRIHWVRDG-ENIESGGHYTVEVKERHAVLIIRDGSHLDSGPYRITAENELGSDTAIIQVQI 7833
Cdd:smart00410    9 GESVTLSCEASGSPPPEVTWYKQGgKLLAESGRFSVSRSGSTSTLTISNVTPEDSGTYTCAATNSSGSASSGTTLTV 85
fn3 pfam00041
Fibronectin type III domain;
4286-4375 4.96e-10

Fibronectin type III domain;


Pssm-ID: 394996 [Multi-domain]  Cd Length: 85  Bit Score: 59.74  E-value: 4.96e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561  4286 GKPGTPEAVDWDKDHVDLVWRPPiNDGGSPITGYVVEKREKGTDKWIKgtEITIPclGEECKATVPTLNENCEYEFRVKA 4365
Cdd:pfam00041    1 SAPSNLTVTDVTSTSLTVSWTPP-PDGNGPITGYEVEYRPKNSGEPWN--EITVP--GTTTSVTLTGLKPGTEYEVRVQA 75
                           90
                   ....*....|
gi 281359561  4366 INAAGPGEPS 4375
Cdd:pfam00041   76 VNGGGEGPPS 85
IG_like smart00410
Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.
133-210 5.04e-10

Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.


Pssm-ID: 214653 [Multi-domain]  Cd Length: 85  Bit Score: 59.83  E-value: 5.04e-10
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 281359561    133 GKRLLFECRVNADPIPAIIWFHNGA-AVKESERHKITVDKDVHsyfaTLEILNVTVEDAGKYKVNAKNELGESNATISL 210
Cdd:smart00410    9 GESVTLSCEASGSPPPEVTWYKQGGkLLAESGRFSVSRSGSTS----TLTISNVTPEDSGTYTCAATNSSGSASSGTTL 83
IgI_Myotilin_C_like cd05744
Immunoglobulin (Ig)-like domain of myotilin, palladin, and myopalladin; member of the I-set of ...
545-636 5.18e-10

Immunoglobulin (Ig)-like domain of myotilin, palladin, and myopalladin; member of the I-set of Ig superfamily (IgSF) domains; The members here are composed of the immunoglobulin (Ig)-like domain in myotilin, palladin, and myopalladin. Myotilin, palladin, and myopalladin function as scaffolds that regulate actin organization. Myotilin and myopalladin are most abundant in skeletal and cardiac muscle; palladin is ubiquitously expressed in the organs of developing vertebrates and plays a key role in cellular morphogenesis. The three family members each interact with specific molecular partners with all three binding to alpha-actinin; In addition, palladin also binds to vasodilator-stimulated phosphoprotein (VASP) and ezrin, myotilin binds to filamin and actin, and myopalladin also binds to nebulin and cardiac ankyrin repeat protein (CARP). This group belongs to the I-set of IgSF domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand, but lack a C" strand.


Pssm-ID: 409405 [Multi-domain]  Cd Length: 91  Bit Score: 59.82  E-value: 5.18e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561  545 FIEKPRIVSENNGKLVIMECKVKADPKPDVIWFRNGEVIKESNKIKTFIEQRGDQyyiKLELLDPQLEDSGLYKCNIKNT 624
Cdd:cd05744     3 FLQAPGDLEVQEGRLCRFDCKVSGLPTPDLFWQLNGKPVRPDSAHKMLVRENGRH---SLIIEPVTKRDAGIYTCIARNR 79
                          90
                  ....*....|..
gi 281359561  625 LGELNANLTLNI 636
Cdd:cd05744    80 AGENSFNAELVV 91
I-set pfam07679
Immunoglobulin I-set domain;
335-425 7.81e-10

Immunoglobulin I-set domain;


Pssm-ID: 400151 [Multi-domain]  Cd Length: 90  Bit Score: 59.19  E-value: 7.81e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561   335 PRFPKKP--TIRQEEDLLIMECVLEAHPVPDIVWYCSEKEICNNQRTKMTrkaitKDSYILTLEIQNPTKEDGGNYRCNA 412
Cdd:pfam07679    1 PKFTQKPkdVEVQEGESARFTCTVTGTPDPEVSWFKDGQPLRSSDRFKVT-----YEGGTYTLTISNVQPDDSGKYTCVA 75
                           90
                   ....*....|...
gi 281359561   413 INMYGESNANIAL 425
Cdd:pfam07679   76 TNSAGEAEASAEL 88
IG_like smart00410
Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.
8455-8525 8.13e-10

Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.


Pssm-ID: 214653 [Multi-domain]  Cd Length: 85  Bit Score: 59.06  E-value: 8.13e-10
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 281359561   8455 KLLCCLSGKPVPNVRWYKDGRELSKYE--YAMTHSDGVVTMEIIDCKPSDSGKYSCKATNCHGTDETDCVVIV 8525
Cdd:smart00410   13 TLSCEASGSPPPEVTWYKQGGKLLAESgrFSVSRSGSTSTLTISNVTPEDSGTYTCAATNSSGSASSGTTLTV 85
fn3 pfam00041
Fibronectin type III domain;
3695-3780 1.03e-09

Fibronectin type III domain;


Pssm-ID: 394996 [Multi-domain]  Cd Length: 85  Bit Score: 58.58  E-value: 1.03e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561  3695 DRPGKPEPTNWDKDFVDLAWDPPKnDGGAPIQKYVIQMRDKSGRAWVDSATVPGDKCNGTVTGVEEGHEYEFRIVAVNKA 3774
Cdd:pfam00041    1 SAPSNLTVTDVTSTSLTVSWTPPP-DGNGPITGYEVEYRPKNSGEPWNEITVPGTTTSVTLTGLKPGTEYEVRVQAVNGG 79

                   ....*.
gi 281359561  3775 GPSDPS 3780
Cdd:pfam00041   80 GEGPPS 85
IgI_Myotilin_C_like cd05744
Immunoglobulin (Ig)-like domain of myotilin, palladin, and myopalladin; member of the I-set of ...
228-320 1.32e-09

Immunoglobulin (Ig)-like domain of myotilin, palladin, and myopalladin; member of the I-set of Ig superfamily (IgSF) domains; The members here are composed of the immunoglobulin (Ig)-like domain in myotilin, palladin, and myopalladin. Myotilin, palladin, and myopalladin function as scaffolds that regulate actin organization. Myotilin and myopalladin are most abundant in skeletal and cardiac muscle; palladin is ubiquitously expressed in the organs of developing vertebrates and plays a key role in cellular morphogenesis. The three family members each interact with specific molecular partners with all three binding to alpha-actinin; In addition, palladin also binds to vasodilator-stimulated phosphoprotein (VASP) and ezrin, myotilin binds to filamin and actin, and myopalladin also binds to nebulin and cardiac ankyrin repeat protein (CARP). This group belongs to the I-set of IgSF domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand, but lack a C" strand.


Pssm-ID: 409405 [Multi-domain]  Cd Length: 91  Bit Score: 58.66  E-value: 1.32e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561  228 PTFTERPVIRQSEDGGNVTFECRCVGDPTPTVTWSHGETELNESNRYKMSLtmDQKLYHiaCLEISSVVSSDQGEYRAQA 307
Cdd:cd05744     1 PHFLQAPGDLEVQEGRLCRFDCKVSGLPTPDLFWQLNGKPVRPDSAHKMLV--RENGRH--SLIIEPVTKRDAGIYTCIA 76
                          90
                  ....*....|...
gi 281359561  308 KNKHgsGVATINL 320
Cdd:cd05744    77 RNRA--GENSFNA 87
IG_like smart00410
Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.
455-532 1.61e-09

Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.


Pssm-ID: 214653 [Multi-domain]  Cd Length: 85  Bit Score: 58.29  E-value: 1.61e-09
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 281359561    455 ITMKCKCKAKPEPTVTWYR-GQDLVEKSKKIKINttviaEDTYELTLEIKDPGATDGGTYRCNVKNEYGESNANLNLNI 532
Cdd:smart00410   12 VTLSCEASGSPPPEVTWYKqGGKLLAESGRFSVS-----RSGSTSTLTISNVTPEDSGTYTCAATNSSGSASSGTTLTV 85
FN3 COG3401
Fibronectin type 3 domain [General function prediction only];
7814-7925 2.34e-09

Fibronectin type 3 domain [General function prediction only];


Pssm-ID: 442628 [Multi-domain]  Cd Length: 603  Bit Score: 64.64  E-value: 2.34e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 7814 YRITAENELGSDTAIIQVQISDRPDPPRFP---LIESIGTESLSLSWKAPvwdGCSDITNYYVERREHPLSSWIRVGNTR 7890
Cdd:COG3401   207 YRVAATDTGGESAPSNEVSVTTPTTPPSAPtglTATADTPGSVTLSWDPV---TESDATGYRVYRSNSGDGPFTKVATVT 283
                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 281359561 7891 FTSMAVSGLTPGKEYDFRIFADNVYG-RSDASDTST 7925
Cdd:COG3401   284 TTSYTDTGLTNGTTYYYRVTAVDAAGnESAPSNVVS 319
fn3 pfam00041
Fibronectin type III domain;
5968-6046 2.74e-09

Fibronectin type III domain;


Pssm-ID: 394996 [Multi-domain]  Cd Length: 85  Bit Score: 57.42  E-value: 2.74e-09
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 281359561  5968 EEITANSVTISWKPPKDnGGSEISSYVIEKRDLTHGGGWVPAVnyVSAKYNHAVVPRLLEGTMYELRVMAENLQGRSDP 6046
Cdd:pfam00041    9 TDVTSTSLTVSWTPPPD-GNGPITGYEVEYRPKNSGEPWNEIT--VPGTTTSVTLTGLKPGTEYEVRVQAVNGGGEGPP 84
fn3 pfam00041
Fibronectin type III domain;
7838-7921 3.60e-09

Fibronectin type III domain;


Pssm-ID: 394996 [Multi-domain]  Cd Length: 85  Bit Score: 57.04  E-value: 3.60e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561  7838 DPPRFPLIESIGTESLSLSWKAPVwDGCSDITNYYVERREH---PLSSWIRVGNTRfTSMAVSGLTPGKEYDFRIFADNV 7914
Cdd:pfam00041    1 SAPSNLTVTDVTSTSLTVSWTPPP-DGNGPITGYEVEYRPKnsgEPWNEITVPGTT-TSVTLTGLKPGTEYEVRVQAVNG 78

                   ....*..
gi 281359561  7915 YGRSDAS 7921
Cdd:pfam00041   79 GGEGPPS 85
IgI_Titin_like cd05747
Immunoglobulin (Ig)-like domain of human titin C terminus and similar proteins; member of the ...
5559-5654 3.69e-09

Immunoglobulin (Ig)-like domain of human titin C terminus and similar proteins; member of the I-set of Ig superfamily (IgSF) domains; The members here are composed of the fifth immunoglobulin (Ig)-like domain from the C-terminus of human titin x and similar proteins. Titin (also called connectin) is a fibrous sarcomeric protein specifically found in vertebrate striated muscle. Titin is gigantic; depending on isoform composition it ranges from 2970 to 3700 kDa, and is of a length that spans half a sarcomere. Titin largely consists of multiple repeats of Ig-like and fibronectin type 3 (FN-III)-like domains. Titin connects the ends of myosin thick filaments to Z disks and extends along the thick filament to the H zone and appears to function similar to an elastic band, keeping the myosin filaments centered in the sarcomere during muscle contraction or stretching. This group belongs to the I-set of IgSF domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand, but lack a C" strand.


Pssm-ID: 143224 [Multi-domain]  Cd Length: 92  Bit Score: 57.37  E-value: 3.69e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 5559 STIICKPRflapffdksllnDITVHAGKRLGWTLPIEASPRPLITWLYNGKEIGSNSRGESGLFQNELTFEIVSSLRSDE 5638
Cdd:cd05747     4 ATILTKPR------------SLTVSEGESARFSCDVDGEPAPTVTWMREGQIIVSSQRHQITSTEYKSTFEISKVQMSDE 71
                          90
                  ....*....|....*.
gi 281359561 5639 GRYTLILKNEHGSFDA 5654
Cdd:cd05747    72 GNYTVVVENSEGKQEA 87
IG_like smart00410
Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.
8318-8401 3.84e-09

Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.


Pssm-ID: 214653 [Multi-domain]  Cd Length: 85  Bit Score: 57.13  E-value: 3.84e-09
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561   8318 PSSQFCYEGQSVKFYCRCIAIATPTLTWSHNNIE-LRQSVKFMKRYVGDDYYFIINRVKLDDRGEYIIRAENHYGSREEV 8396
Cdd:smart00410    1 PPSVTVKEGESVTLSCEASGSPPPEVTWYKQGGKlLAESGRFSVSRSGSTSTLTISNVTPEDSGTYTCAATNSSGSASSG 80

                    ....*
gi 281359561   8397 VFLNV 8401
Cdd:smart00410   81 TTLTV 85
IG_like smart00410
Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.
5284-5366 4.27e-09

Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.


Pssm-ID: 214653 [Multi-domain]  Cd Length: 85  Bit Score: 57.13  E-value: 4.27e-09
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561   5284 SDIKIKAGNVFEFDVPVTGEPLPSKDWTHEG-NMIINTDRVKISNFDDRTKIRILDAKRSDTGVYTLTARNINGTDRHNV 5362
Cdd:smart00410    2 PSVTVKEGESVTLSCEASGSPPPEVTWYKQGgKLLAESGRFSVSRSGSTSTLTISNVTPEDSGTYTCAATNSSGSASSGT 81

                    ....
gi 281359561   5363 KVTI 5366
Cdd:smart00410   82 TLTV 85
IgI_C2_MyBP-C-like cd20967
Domain C2 of human cardiac Myosin Binding Protein C and similar domains; a member of the I-set ...
1842-1896 5.66e-09

Domain C2 of human cardiac Myosin Binding Protein C and similar domains; a member of the I-set of IgSF domains; The members here are composed of the immunoglobulin (Ig) Domain C2 of human cardiac Myosin Binding Protein C (MyBP-C) and similar domains. MyBP-C is a thick filament protein involved in the regulation of muscle contraction. Mutations in cardiac MyBP-C gene are the second most frequent cause of hypertrophic cardiomyopathy. MyBP-C binds to myosin with two binding sites, one at its C-terminus and another at its N-terminus. The N-terminal binding site, consisting of immunoglobulin (lg) domains C1 and C2 connected by a flexible linker, interacts with the S2 segment of myosin in a phosphorylation-regulated manner. The C1 and C2 Ig domains can bind to and activate or inhibit the thin filament. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. Unlike the V-set, one of the distinctive features of I-set domains is the lack of a C" strand. The structures of the Ig domains of MyBP-C lack this strand and thus belong to the I-set of Ig superfamily domains. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors.


Pssm-ID: 409559  Cd Length: 82  Bit Score: 56.48  E-value: 5.66e-09
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 281359561 1842 VTLACEIDDAMGEVQWLRNGEEIKPDKRIQIVKDGRKRKLVIKDCKVTDAGQFKC 1896
Cdd:cd20967    15 IRLTVELADPDAEVKWYKDGQELQSSSKVIFESIGAKRTLTVQQASLADAGEYQC 69
fn3 pfam00041
Fibronectin type III domain;
5381-5454 9.01e-09

Fibronectin type III domain;


Pssm-ID: 394996 [Multi-domain]  Cd Length: 85  Bit Score: 56.27  E-value: 9.01e-09
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 281359561  5381 DVSKNSIVLRWRPPkDDGGSEITHYVVE---KMDNEAMRWVPVgdcTDTEIRAD--NLIENHDYSFRVRAVNKQGQSQP 5454
Cdd:pfam00041   10 DVTSTSLTVSWTPP-PDGNGPITGYEVEyrpKNSGEPWNEITV---PGTTTSVTltGLKPGTEYEVRVQAVNGGGEGPP 84
fn3 pfam00041
Fibronectin type III domain;
3315-3382 1.02e-08

Fibronectin type III domain;


Pssm-ID: 394996 [Multi-domain]  Cd Length: 85  Bit Score: 55.88  E-value: 1.02e-08
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 281359561  3315 LKWRKPKDDGGiPITGYVIEKMDTATGKWVPAGSVDPEKYDIEIKGLDPNHRYQFRVKAVNEEGESEP 3382
Cdd:pfam00041   18 VSWTPPPDGNG-PITGYEVEYRPKNSGEPWNEITVPGTTTSVTLTGLKPGTEYEVRVQAVNGGGEGPP 84
I-set pfam07679
Immunoglobulin I-set domain;
746-835 1.10e-08

Immunoglobulin I-set domain;


Pssm-ID: 400151 [Multi-domain]  Cd Length: 90  Bit Score: 56.11  E-value: 1.10e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561   746 PEISRKLADQKVAESKTFELlvslsqtdrKCK--------VEWYKGSTVIRETKDITTTFDGTTARLTFSSARTEHTSNY 817
Cdd:pfam07679    1 PKFTQKPKDVEVQEGESARF---------TCTvtgtpdpeVSWFKDGQPLRSSDRFKVTYEGGTYTLTISNVQPDDSGKY 71
                           90
                   ....*....|....*...
gi 281359561   818 KVIVTNEVGKDESSCKIT 835
Cdd:pfam07679   72 TCVATNSAGEAEASAELT 89
IgI_Titin_like cd05747
Immunoglobulin (Ig)-like domain of human titin C terminus and similar proteins; member of the ...
436-530 1.36e-08

Immunoglobulin (Ig)-like domain of human titin C terminus and similar proteins; member of the I-set of Ig superfamily (IgSF) domains; The members here are composed of the fifth immunoglobulin (Ig)-like domain from the C-terminus of human titin x and similar proteins. Titin (also called connectin) is a fibrous sarcomeric protein specifically found in vertebrate striated muscle. Titin is gigantic; depending on isoform composition it ranges from 2970 to 3700 kDa, and is of a length that spans half a sarcomere. Titin largely consists of multiple repeats of Ig-like and fibronectin type 3 (FN-III)-like domains. Titin connects the ends of myosin thick filaments to Z disks and extends along the thick filament to the H zone and appears to function similar to an elastic band, keeping the myosin filaments centered in the sarcomere during muscle contraction or stretching. This group belongs to the I-set of IgSF domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand, but lack a C" strand.


Pssm-ID: 143224 [Multi-domain]  Cd Length: 92  Bit Score: 55.82  E-value: 1.36e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561  436 FAPSFIEKPRIIPNESGTLITMKCKCKAKPEPTVTWYRGQDLVEKSKKIKINTTviaedTYELTLEIKDPGATDGGTYRC 515
Cdd:cd05747     2 LPATILTKPRSLTVSEGESARFSCDVDGEPAPTVTWMREGQIIVSSQRHQITST-----EYKSTFEISKVQMSDEGNYTV 76
                          90
                  ....*....|....*
gi 281359561  516 NVKNEYGESNANLNL 530
Cdd:cd05747    77 VVENSEGKQEAQFTL 91
IG_like smart00410
Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.
3810-3885 3.01e-08

Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.


Pssm-ID: 214653 [Multi-domain]  Cd Length: 85  Bit Score: 54.43  E-value: 3.01e-08
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 281359561   3810 GQMLHIDALIKAEPPAKVTWTYNKTE-IKTSDHIKIENEDYKTTFIMPKVKRADRGIYIVTAKNDSGSDTVEVELEV 3885
Cdd:smart00410    9 GESVTLSCEASGSPPPEVTWYKQGGKlLAESGRFSVSRSGSTSTLTISNVTPEDSGTYTCAATNSSGSASSGTTLTV 85
fn3 pfam00041
Fibronectin type III domain;
4780-4863 3.18e-08

Fibronectin type III domain;


Pssm-ID: 394996 [Multi-domain]  Cd Length: 85  Bit Score: 54.34  E-value: 3.18e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561  4780 SPPnGPLQISDVHKEGCHLKWKRPSDDGGtPIEYFQIDKLEPETGCWIPSCR--STEPQVDVTGLSPGNEYKFRVSAVNA 4857
Cdd:pfam00041    1 SAP-SNLTVTDVTSTSLTVSWTPPPDGNG-PITGYEVEYRPKNSGEPWNEITvpGTTTSVTLTGLKPGTEYEVRVQAVNG 78

                   ....*.
gi 281359561  4858 EGESQP 4863
Cdd:pfam00041   79 GGEGPP 84
IG_like smart00410
Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.
557-636 3.92e-08

Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.


Pssm-ID: 214653 [Multi-domain]  Cd Length: 85  Bit Score: 54.43  E-value: 3.92e-08
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561    557 GKLVIMECKVKADPKPDVIWFRNG-EVIKESNKIKtfIEQRGDQYYikLELLDPQLEDSGLYKCNIKNTLGELNANLTLN 635
Cdd:smart00410    9 GESVTLSCEASGSPPPEVTWYKQGgKLLAESGRFS--VSRSGSTST--LTISNVTPEDSGTYTCAATNSSGSASSGTTLT 84

                    .
gi 281359561    636 I 636
Cdd:smart00410   85 V 85
fn3 pfam00041
Fibronectin type III domain;
3599-3677 4.22e-08

Fibronectin type III domain;


Pssm-ID: 394996 [Multi-domain]  Cd Length: 85  Bit Score: 54.34  E-value: 4.22e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561  3599 GPLQVNDITKHSCKLKWEKPDDdGGSPIDYYEIEKLDPHTGQ-WLPC-GKSTEPEAKVIGLHEGKAYKFRVRAVNKEGES 3676
Cdd:pfam00041    4 SNLTVTDVTSTSLTVSWTPPPD-GNGPITGYEVEYRPKNSGEpWNEItVPGTTTSVTLTGLKPGTEYEVRVQAVNGGGEG 82

                   .
gi 281359561  3677 E 3677
Cdd:pfam00041   83 P 83
IG_like smart00410
Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.
1750-1821 4.54e-08

Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.


Pssm-ID: 214653 [Multi-domain]  Cd Length: 85  Bit Score: 54.05  E-value: 4.54e-08
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 281359561   1750 TLECSVSSS-MANVHWFKNNTKLESDDPRYLISKDiNGNLKLIIKDSVLDDAGLYRCQLDKQPDKTECNLKVT 1821
Cdd:smart00410   13 TLSCEASGSpPPEVTWYKQGGKLLAESGRFSVSRS-GSTSTLTISNVTPEDSGTYTCAATNSSGSASSGTTLT 84
fn3 pfam00041
Fibronectin type III domain;
5471-5555 6.94e-08

Fibronectin type III domain;


Pssm-ID: 394996 [Multi-domain]  Cd Length: 85  Bit Score: 53.57  E-value: 6.94e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561  5471 DKPGQPQATDWGKHFVDLEWSTPKrDGGAPISSYIIEKRPKF-GQWERAAVVLGDNCKAHVPELTNGGEYEFRVIAVNRG 5549
Cdd:pfam00041    1 SAPSNLTVTDVTSTSLTVSWTPPP-DGNGPITGYEVEYRPKNsGEPWNEITVPGTTTSVTLTGLKPGTEYEVRVQAVNGG 79

                   ....*.
gi 281359561  5550 GPSDPS 5555
Cdd:pfam00041   80 GEGPPS 85
IG_like smart00410
Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.
1503-1588 8.56e-08

Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.


Pssm-ID: 214653 [Multi-domain]  Cd Length: 85  Bit Score: 53.28  E-value: 8.56e-08
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561   1503 QESYSVVEDSTAYLTVGVEGSPAPTFKFYK-GVSEILEGGRFKFLTDGQTNTITlcMRKCKPNDESKYKIVVSNIHGEDS 1581
Cdd:smart00410    1 PPSVTVKEGESVTLSCEASGSPPPEVTWYKqGGKLLAESGRFSVSRSGSTSTLT--ISNVTPEDSGTYTCAATNSSGSAS 78

                    ....*..
gi 281359561   1582 AEMQLYV 1588
Cdd:smart00410   79 SGTTLTV 85
I-set pfam07679
Immunoglobulin I-set domain;
5570-5660 8.61e-08

Immunoglobulin I-set domain;


Pssm-ID: 400151 [Multi-domain]  Cd Length: 90  Bit Score: 53.42  E-value: 8.61e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561  5570 PFFDKsLLNDITVHAGKRLGWTLPIEASPRPLITWLYNGKEIGSNSRGESGLFQNELTFEIVSSLRSDEGRYTLILKNEH 5649
Cdd:pfam07679    1 PKFTQ-KPKDVEVQEGESARFTCTVTGTPDPEVSWFKDGQPLRSSDRFKVTYEGGTYTLTISNVQPDDSGKYTCVATNSA 79
                           90
                   ....*....|.
gi 281359561  5650 GSfdASAHATV 5660
Cdd:pfam07679   80 GE--AEASAEL 88
I-set pfam07679
Immunoglobulin I-set domain;
656-726 1.01e-07

Immunoglobulin I-set domain;


Pssm-ID: 400151 [Multi-domain]  Cd Length: 90  Bit Score: 53.42  E-value: 1.01e-07
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 281359561   656 TVVIECTVASKFEPKCTWYKETSTVKESKRHVYQVEqtkegEFAVKLEINDVEESDKGAYKLVASNEKGEA 726
Cdd:pfam07679   17 SARFTCTVTGTPDPEVSWFKDGQPLRSSDRFKVTYE-----GGTYTLTISNVQPDDSGKYTCVATNSAGEA 82
IgI_Myotilin_C_like cd05744
Immunoglobulin (Ig)-like domain of myotilin, palladin, and myopalladin; member of the I-set of ...
335-426 1.22e-07

Immunoglobulin (Ig)-like domain of myotilin, palladin, and myopalladin; member of the I-set of Ig superfamily (IgSF) domains; The members here are composed of the immunoglobulin (Ig)-like domain in myotilin, palladin, and myopalladin. Myotilin, palladin, and myopalladin function as scaffolds that regulate actin organization. Myotilin and myopalladin are most abundant in skeletal and cardiac muscle; palladin is ubiquitously expressed in the organs of developing vertebrates and plays a key role in cellular morphogenesis. The three family members each interact with specific molecular partners with all three binding to alpha-actinin; In addition, palladin also binds to vasodilator-stimulated phosphoprotein (VASP) and ezrin, myotilin binds to filamin and actin, and myopalladin also binds to nebulin and cardiac ankyrin repeat protein (CARP). This group belongs to the I-set of IgSF domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand, but lack a C" strand.


Pssm-ID: 409405 [Multi-domain]  Cd Length: 91  Bit Score: 53.27  E-value: 1.22e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561  335 PRFPKKPTIR--QEEDLLIMECVLEAHPVPDIVWYCSEKEICNNQRTKMtrkaITKDSYILTLEIQNPTKEDGGNYRCNA 412
Cdd:cd05744     1 PHFLQAPGDLevQEGRLCRFDCKVSGLPTPDLFWQLNGKPVRPDSAHKM----LVRENGRHSLIIEPVTKRDAGIYTCIA 76
                          90
                  ....*....|....
gi 281359561  413 INMYGESNANIALN 426
Cdd:cd05744    77 RNRAGENSFNAELV 90
IG_like smart00410
Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.
3507-3590 1.55e-07

Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.


Pssm-ID: 214653 [Multi-domain]  Cd Length: 85  Bit Score: 52.51  E-value: 1.55e-07
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561   3507 KPVIVKTGLSISLDINIRGEPAPKVEWFFNNSSVTSDEHSVKIDNVDYNTKFFVMRAQRSQSGKYIIKATNEVGEDEAEL 3586
Cdd:smart00410    2 PSVTVKEGESVTLSCEASGSPPPEVTWYKQGGKLLAESGRFSVSRSGSTSTLTISNVTPEDSGTYTCAATNSSGSASSGT 81

                    ....
gi 281359561   3587 EVTV 3590
Cdd:smart00410   82 TLTV 85
fn3 pfam00041
Fibronectin type III domain;
4186-4269 1.67e-07

Fibronectin type III domain;


Pssm-ID: 394996 [Multi-domain]  Cd Length: 85  Bit Score: 52.42  E-value: 1.67e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561  4186 GPPEGpLRVTDVHKEGCKLKWNAPLDDGGlPIDHYIIEKMDVESGRWLPSGRFK--ESFAELNNLEPSHEYKFRVLAVNT 4263
Cdd:pfam00041    1 SAPSN-LTVTDVTSTSLTVSWTPPPDGNG-PITGYEVEYRPKNSGEPWNEITVPgtTTSVTLTGLKPGTEYEVRVQAVNG 78

                   ....*.
gi 281359561  4264 EGESEP 4269
Cdd:pfam00041   79 GGEGPP 84
IG_like smart00410
Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.
350-425 2.61e-07

Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.


Pssm-ID: 214653 [Multi-domain]  Cd Length: 85  Bit Score: 52.12  E-value: 2.61e-07
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 281359561    350 LIMECVLEAHPVPDIVWYC-SEKEICNNQRTKmtrkaITKDSYILTLEIQNPTKEDGGNYRCNAINMYGESNANIAL 425
Cdd:smart00410   12 VTLSCEASGSPPPEVTWYKqGGKLLAESGRFS-----VSRSGSTSTLTISNVTPEDSGTYTCAATNSSGSASSGTTL 83
IG_like smart00410
Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.
23-101 3.60e-07

Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.


Pssm-ID: 214653 [Multi-domain]  Cd Length: 85  Bit Score: 51.74  E-value: 3.60e-07
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 281359561     23 GNRLIFECQLLSSPKPDIEWFRSDNKVVEDvRTKFKIQpvgENKYTVVLELDDVVETDAGLYKVKAKNKSGEVSASINL 101
Cdd:smart00410    9 GESVTLSCEASGSPPPEVTWYKQGGKLLAE-SGRFSVS---RSGSTSTLTISNVTPEDSGTYTCAATNSSGSASSGTTL 83
I-set pfam07679
Immunoglobulin I-set domain;
5865-5954 8.53e-07

Immunoglobulin I-set domain;


Pssm-ID: 400151 [Multi-domain]  Cd Length: 90  Bit Score: 50.72  E-value: 8.53e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561  5865 PKIITPLNEVRIKCG--LIFhtDIHFIGEPAPEATWTLNSNPLLSNDRSTITSIGHHSVVHTVNCQRSDSGIYHLLLRNS 5942
Cdd:pfam07679    1 PKFTQKPKDVEVQEGesARF--TCTVTGTPDPEVSWFKDGQPLRSSDRFKVTYEGGTYTLTISNVQPDDSGKYTCVATNS 78
                           90
                   ....*....|..
gi 281359561  5943 SGIDEGSFELVV 5954
Cdd:pfam07679   79 AGEAEASAELTV 90
I-set pfam07679
Immunoglobulin I-set domain;
6564-6650 8.96e-07

Immunoglobulin I-set domain;


Pssm-ID: 400151 [Multi-domain]  Cd Length: 90  Bit Score: 50.72  E-value: 8.96e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561  6564 LGKVRDIVCRAGD--DFSIHVpyLAFPKPNAFWYSNDNMLDDNNRVHKHLTDDAASVVVKNSKRADSGQYRLQLKNTSGF 6641
Cdd:pfam07679    4 TQKPKDVEVQEGEsaRFTCTV--TGTPDPEVSWFKDGQPLRSSDRFKVTYEGGTYTLTISNVQPDDSGKYTCVATNSAGE 81

                   ....*....
gi 281359561  6642 DTATINVRV 6650
Cdd:pfam07679   82 AEASAELTV 90
Ig cd00096
Immunoglobulin domain; The members here are composed of the immunoglobulin (Ig) domain found ...
657-731 1.04e-06

Immunoglobulin domain; The members here are composed of the immunoglobulin (Ig) domain found in the Ig superfamily. The Ig superfamily is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. Members of this group are components of immunoglobulin, neuroglia, cell surface glycoproteins, including T-cell receptors, CD2, CD4, CD8, and membrane glycoproteins, including butyrophilin and chondroitin sulfate proteoglycan core protein. A predominant feature of most Ig domains is a disulfide bridge connecting the two beta-sheets with a tryptophan residue packed against the disulfide bond. Ig superfamily (IgSF) domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. Typically, the V-set domains have A, B, E, and D strands in one sheet and A', G, F, C, C' and C" in the other. The structures in C1-set are smaller than those in the V-set; they have one beta sheet that is formed by strands A, B, E, and D and the other by strands G, F, C, and C'. Moreover, a C1-set Ig domain contains a short C' strand (three residues) and lacks A' and C" strand. Unlike other Ig domain sets, C2-set structures do not have a D strand. Like the V-set Ig domains, members of the I-set have a discontinuous A strand, but lack a C" strand.


Pssm-ID: 409353 [Multi-domain]  Cd Length: 70  Bit Score: 49.64  E-value: 1.04e-06
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 281359561  657 VVIECTVASKFEPKCTWYKETSTVKESKRHVYQVEQTKegefaVKLEINDVEESDKGAYKLVASNEKGEAVSQIV 731
Cdd:cd00096     1 VTLTCSASGNPPPTITWYKNGKPLPPSSRDSRRSELGN-----GTLTISNVTLEDSGTYTCVASNSAGGSASASV 70
Ig cd00096
Immunoglobulin domain; The members here are composed of the immunoglobulin (Ig) domain found ...
1750-1806 1.19e-06

Immunoglobulin domain; The members here are composed of the immunoglobulin (Ig) domain found in the Ig superfamily. The Ig superfamily is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. Members of this group are components of immunoglobulin, neuroglia, cell surface glycoproteins, including T-cell receptors, CD2, CD4, CD8, and membrane glycoproteins, including butyrophilin and chondroitin sulfate proteoglycan core protein. A predominant feature of most Ig domains is a disulfide bridge connecting the two beta-sheets with a tryptophan residue packed against the disulfide bond. Ig superfamily (IgSF) domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. Typically, the V-set domains have A, B, E, and D strands in one sheet and A', G, F, C, C' and C" in the other. The structures in C1-set are smaller than those in the V-set; they have one beta sheet that is formed by strands A, B, E, and D and the other by strands G, F, C, and C'. Moreover, a C1-set Ig domain contains a short C' strand (three residues) and lacks A' and C" strand. Unlike other Ig domain sets, C2-set structures do not have a D strand. Like the V-set Ig domains, members of the I-set have a discontinuous A strand, but lack a C" strand.


Pssm-ID: 409353 [Multi-domain]  Cd Length: 70  Bit Score: 49.64  E-value: 1.19e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 281359561 1750 TLECSVSSS-MANVHWFKNNTKLESDDprYLISKDINGNLKLIIKDSVLDDAGLYRCQ 1806
Cdd:cd00096     2 TLTCSASGNpPPTITWYKNGKPLPPSS--RDSRRSELGNGTLTISNVTLEDSGTYTCV 57
I-set pfam07679
Immunoglobulin I-set domain;
1639-1724 2.18e-06

Immunoglobulin I-set domain;


Pssm-ID: 400151 [Multi-domain]  Cd Length: 90  Bit Score: 49.56  E-value: 2.18e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561  1639 SFLSPLIDQFAKEGKDkkVVFEARFS-KPNCKPKWLFRKDEVFTGSKFKFKQENDTYQLIITTPKVEDTGKYTI----EI 1713
Cdd:pfam07679    2 KFTQKPKDVEVQEGES--ARFTCTVTgTPDPEVSWFKDGQPLRSSDRFKVTYEGGTYTLTISNVQPDDSGKYTCvatnSA 79
                           90
                   ....*....|.
gi 281359561  1714 GGVSSTAFLNV 1724
Cdd:pfam07679   80 GEAEASAELTV 90
IG_like smart00410
Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.
5874-5954 3.12e-06

Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.


Pssm-ID: 214653 [Multi-domain]  Cd Length: 85  Bit Score: 49.04  E-value: 3.12e-06
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561   5874 VRIKCglifhtdiHFIGEPAPEATWTLNS-NPLLSNDRSTITSIGHHSVVHTVNCQRSDSGIYHLLLRNSSGIDEGSFEL 5952
Cdd:smart00410   12 VTLSC--------EASGSPPPEVTWYKQGgKLLAESGRFSVSRSGSTSTLTISNVTPEDSGTYTCAATNSSGSASSGTTL 83

                    ..
gi 281359561   5953 VV 5954
Cdd:smart00410   84 TV 85
IgI_Titin_like cd05747
Immunoglobulin (Ig)-like domain of human titin C terminus and similar proteins; member of the ...
8845-8909 7.17e-06

Immunoglobulin (Ig)-like domain of human titin C terminus and similar proteins; member of the I-set of Ig superfamily (IgSF) domains; The members here are composed of the fifth immunoglobulin (Ig)-like domain from the C-terminus of human titin x and similar proteins. Titin (also called connectin) is a fibrous sarcomeric protein specifically found in vertebrate striated muscle. Titin is gigantic; depending on isoform composition it ranges from 2970 to 3700 kDa, and is of a length that spans half a sarcomere. Titin largely consists of multiple repeats of Ig-like and fibronectin type 3 (FN-III)-like domains. Titin connects the ends of myosin thick filaments to Z disks and extends along the thick filament to the H zone and appears to function similar to an elastic band, keeping the myosin filaments centered in the sarcomere during muscle contraction or stretching. This group belongs to the I-set of IgSF domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand, but lack a C" strand.


Pssm-ID: 143224 [Multi-domain]  Cd Length: 92  Bit Score: 48.12  E-value: 7.17e-06
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 281359561 8845 PTSVSVLEGEGTTFECEIDSE-LLNLVWLKDGKPIdETLPRYSFTKDGHRYSFAVAKCNMDDVGQY 8909
Cdd:cd05747    10 PRSLTVSEGESARFSCDVDGEpAPTVTWMREGQII-VSSQRHQITSTEYKSTFEISKVQMSDEGNY 74
IG_like smart00410
Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.
6568-6650 7.98e-06

Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.


Pssm-ID: 214653 [Multi-domain]  Cd Length: 85  Bit Score: 47.89  E-value: 7.98e-06
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561   6568 RDIVCRAGDDFSIHVPYLAFPKPNAFWYSND-NMLDDNNRVHKHLTDDAASVVVKNSKRADSGQYRLQLKNTSGFDTATI 6646
Cdd:smart00410    2 PSVTVKEGESVTLSCEASGSPPPEVTWYKQGgKLLAESGRFSVSRSGSTSTLTISNVTPEDSGTYTCAATNSSGSASSGT 81

                    ....
gi 281359561   6647 NVRV 6650
Cdd:smart00410   82 TLTV 85
COG4733 COG4733
Phage-related protein, tail protein J [Mobilome: prophages, transposons];
2165-2342 1.00e-05

Phage-related protein, tail protein J [Mobilome: prophages, transposons];


Pssm-ID: 443767 [Multi-domain]  Cd Length: 978  Bit Score: 53.03  E-value: 1.00e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 2165 DLIPKKQYRFRIRAVNAIGQSDPATFKNTILAKDPWDEPGKPKAVDLTDwDKDHADLKWEAPEtdgGDPITAYIVEYKEk 2244
Cdd:COG4733   592 PGIYAGDYEVRVRAINALGVSSAWAASSETTVTGKTAPPPAPTGLTATG-GLGGITLSWSFPV---DADTLRTEIRYST- 666
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 2245 fSNDWVSGK--EVDGDARTATVDGLKEGQQYEFRVRAVNRAG-------PGEPSDKTKSIIAkcrfvkpFIVGEGLKNVT 2315
Cdd:COG4733   667 -TGDWASATvaQALYPGNTYTLAGLKAGQTYYYRARAVDRSGnvsawwvSGQASADAAGILD-------AITGQILETEL 738
                         170       180
                  ....*....|....*....|....*..
gi 281359561 2316 VKKGQTIRFDIKYDGEPEPAATWVKGT 2342
Cdd:COG4733   739 GQELDAIIQNATVAEVVAATVTDVTAQ 765
IgI_titin_I1-like cd20951
Immunoglobulin domain I1 of the titin I-band and similar proteins; a member of the I-set of ...
1497-1588 1.16e-05

Immunoglobulin domain I1 of the titin I-band and similar proteins; a member of the I-set of IgSF domains; The members here are composed of the immunoglobulin domain I1 of the titin I-band and similar proteins. Titin is a key component in the assembly and functioning of vertebrate striated muscles. By providing connections at the level of individual microfilaments, it contributes to the fine balance of forces between the two halves of the sarcomere. The Ig superfamily (IgSF) is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. The two sheets are linked together by a conserved disulfide bond between B strand and F strand. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. The Ig I1 domain of the titin I-band is a member of the I-set Ig domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand but lack a C" strand. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors, the hemolymph protein hemolin, the muscle proteins titin, telokin, and twitchin, the neuronal adhesion molecule axonin-1, and the signaling molecule semaphorin 4D that is involved in axonal guidance, immune function and angiogenesis.


Pssm-ID: 409543 [Multi-domain]  Cd Length: 94  Bit Score: 47.42  E-value: 1.16e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 1497 PSIVDVQESYSVVEDSTAYLTVGVEGSPAPTFKFYKG---VSEILEGGRFKFLTDGqtNTITLCMRKCKPNDESKYKIVV 1573
Cdd:cd20951     1 PEFIIRLQSHTVWEKSDAKLRVEVQGKPDPEVKWYKNgvpIDPSSIPGKYKIESEY--GVHVLHIRRVTVEDSAVYSAVA 78
                          90
                  ....*....|....*
gi 281359561 1574 SNIHGEDSAEMQLYV 1588
Cdd:cd20951    79 KNIHGEASSSASVVV 93
COG4733 COG4733
Phage-related protein, tail protein J [Mobilome: prophages, transposons];
3341-3479 1.17e-05

Phage-related protein, tail protein J [Mobilome: prophages, transposons];


Pssm-ID: 443767 [Multi-domain]  Cd Length: 978  Bit Score: 53.03  E-value: 1.17e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 3341 GKWVPAGSVDPEkyDIEIKGLdPNHRYQFRVKAVNEEGESEPLETESAITAKnpFDVSAPPGLPELE----DWdehHVKL 3416
Cdd:COG4733   576 GNWVSVPRTSGT--SFEVPGI-YAGDYEVRVRAINALGVSSAWAASSETTVT--GKTAPPPAPTGLTatggLG---GITL 647
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 281359561 3417 KWEPPIrdgGSPITNYIIEVMDKDSGEFVKAVETDSPVCKGVVKKLEEGQQYKFRVRAVNKAG 3479
Cdd:COG4733   648 SWSFPV---DADTLRTEIRYSTTGDWASATVAQALYPGNTYTLAGLKAGQTYYYRARAVDRSG 707
IG_like smart00410
Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.
1838-1897 1.18e-05

Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.


Pssm-ID: 214653 [Multi-domain]  Cd Length: 85  Bit Score: 47.11  E-value: 1.18e-05
                            10        20        30        40        50        60
                    ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 281359561   1838 EKDTVTLACEI-DDAMGEVQWLRNG-EEIKPDKRIQIVKDGRKRKLVIKDCKVTDAGQFKCT 1897
Cdd:smart00410    8 EGESVTLSCEAsGSPPPEVTWYKQGgKLLAESGRFSVSRSGSTSTLTISNVTPEDSGTYTCA 69
Ig_Titin_like cd05748
Immunoglobulin (Ig)-like domain of titin and similar proteins; The members here are composed ...
2020-2095 1.34e-05

Immunoglobulin (Ig)-like domain of titin and similar proteins; The members here are composed of the immunoglobulin (Ig)-like domain found in titin-like proteins and similar proteins. Titin (also called connectin) is a fibrous sarcomeric protein specifically found in vertebrate striated muscle. Titin is a giant protein; depending on isoform composition, it ranges from 2970 to 3700 kDa, and is of a length that spans half a sarcomere. Titin largely consists of multiple repeats of Ig-like and fibronectin type 3 (FN-III)-like domains. Titin connects the ends of myosin thick filaments to Z disks and extends along the thick filament to the H zone. It appears to function similarly to an elastic band, keeping the myosin filaments centered in the sarcomere during muscle contraction or stretching. Within the sarcomere, titin is also attached to or is associated with myosin binding protein C (MyBP-C). MyBP-C appears to contribute to the generation of passive tension by titin and like titin has repeated Ig-like and FN-III domains. Also included in this group are worm twitchin and insect projectin, thick filament proteins of invertebrate muscle which also have repeated Ig-like and FN-III domains.


Pssm-ID: 409406 [Multi-domain]  Cd Length: 82  Bit Score: 46.81  E-value: 1.34e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 281359561 2020 PVLLEVPFKvsGtKQTPvEAKLFKDGKPLPVKD-VEVAVTDDKVTFKIKKPSRDLSGPYQIKISNGQGEDTKDVQII 2095
Cdd:cd05748     9 SLRLDIPIK--G-RPTP-TVTWSKDGQPLKETGrVQIETTASSTSLVIKNAKRSDSGKYTLTLKNSAGEKSATINVK 81
IG_like smart00410
Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.
3210-3292 1.55e-05

Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.


Pssm-ID: 214653 [Multi-domain]  Cd Length: 85  Bit Score: 46.73  E-value: 1.55e-05
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561   3210 KPIKVRAGQPVKFDVDVKGEPAPSLTWFL-KETELTSTGQVRLENIDYNTKLTLLDTDRKQSGQYKLRAENINGVDEAVV 3288
Cdd:smart00410    2 PSVTVKEGESVTLSCEASGSPPPEVTWYKqGGKLLAESGRFSVSRSGSTSTLTISNVTPEDSGTYTCAATNSSGSASSGT 81

                    ....
gi 281359561   3289 EVII 3292
Cdd:smart00410   82 TLTV 85
I-set pfam07679
Immunoglobulin I-set domain;
1914-1998 3.73e-05

Immunoglobulin I-set domain;


Pssm-ID: 400151 [Multi-domain]  Cd Length: 90  Bit Score: 46.10  E-value: 3.73e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561  1914 RFNKKLKDTEAVEREKLILDIELQDQTAP-CDWKFNGEPIVPSESIEIKNMGGgKHQLIFSSLDMSNEGEITC----ESG 1988
Cdd:pfam07679    2 KFTQKPKDVEVQEGESARFTCTVTGTPDPeVSWFKDGQPLRSSDRFKVTYEGG-TYTLTISNVQPDDSGKYTCvatnSAG 80
                           90
                   ....*....|
gi 281359561  1989 QLSSKCKLSI 1998
Cdd:pfam07679   81 EAEASAELTV 90
IG_like smart00410
Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.
656-730 8.09e-05

Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.


Pssm-ID: 214653 [Multi-domain]  Cd Length: 85  Bit Score: 44.80  E-value: 8.09e-05
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 281359561    656 TVVIECTVASKFEPKCTWYKET-STVKESKRhvYQVEQTKegeFAVKLEINDVEESDKGAYKLVASNEKGEAVSQI 730
Cdd:smart00410   11 SVTLSCEASGSPPPEVTWYKQGgKLLAESGR--FSVSRSG---STSTLTISNVTPEDSGTYTCAATNSSGSASSGT 81
Ig_Titin_like cd05748
Immunoglobulin (Ig)-like domain of titin and similar proteins; The members here are composed ...
7361-7438 9.04e-05

Immunoglobulin (Ig)-like domain of titin and similar proteins; The members here are composed of the immunoglobulin (Ig)-like domain found in titin-like proteins and similar proteins. Titin (also called connectin) is a fibrous sarcomeric protein specifically found in vertebrate striated muscle. Titin is a giant protein; depending on isoform composition, it ranges from 2970 to 3700 kDa, and is of a length that spans half a sarcomere. Titin largely consists of multiple repeats of Ig-like and fibronectin type 3 (FN-III)-like domains. Titin connects the ends of myosin thick filaments to Z disks and extends along the thick filament to the H zone. It appears to function similarly to an elastic band, keeping the myosin filaments centered in the sarcomere during muscle contraction or stretching. Within the sarcomere, titin is also attached to or is associated with myosin binding protein C (MyBP-C). MyBP-C appears to contribute to the generation of passive tension by titin and like titin has repeated Ig-like and FN-III domains. Also included in this group are worm twitchin and insect projectin, thick filament proteins of invertebrate muscle which also have repeated Ig-like and FN-III domains.


Pssm-ID: 409406 [Multi-domain]  Cd Length: 82  Bit Score: 44.50  E-value: 9.04e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 281359561 7361 EGDNSKIKIFYSGDQPLTVILKKNNEVIcdsNDDTHVKVNIFDDYVAIYIRNIVKSDGGPYQIEFTNESGSATGEFYV 7438
Cdd:cd05748     6 AGESLRLDIPIKGRPTPTVTWSKDGQPL---KETGRVQIETTASSTSLVIKNAKRSDSGKYTLTLKNSAGEKSATINV 80
Ig_3 pfam13927
Immunoglobulin domain; This family contains immunoglobulin-like domains.
1750-1806 9.56e-05

Immunoglobulin domain; This family contains immunoglobulin-like domains.


Pssm-ID: 464046 [Multi-domain]  Cd Length: 78  Bit Score: 44.48  E-value: 9.56e-05
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 281359561  1750 TLECSVSSS-MANVHWFKNNTKLESDDPRYLISKDINGNLklIIKDSVLDDAGLYRCQ 1806
Cdd:pfam13927   20 TLTCEATGSpPPTITWYKNGEPISSGSTRSRSLSGSNSTL--TISNVTRSDAGTYTCV 75
IG_like smart00410
Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.
5579-5660 1.84e-04

Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.


Pssm-ID: 214653 [Multi-domain]  Cd Length: 85  Bit Score: 44.03  E-value: 1.84e-04
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561   5579 DITVHAGKRLgwTLPIEAS--PRPLITWLYNGKEIGSNSRGESGLFQ-NELTFEIVSSLRSDEGRYTLILKNEHGSFDAS 5655
Cdd:smart00410    3 SVTVKEGESV--TLSCEASgsPPPEVTWYKQGGKLLAESGRFSVSRSgSTSTLTISNVTPEDSGTYTCAATNSSGSASSG 80

                    ....*
gi 281359561   5656 AHATV 5660
Cdd:smart00410   81 TTLTV 85
fn3 pfam00041
Fibronectin type III domain;
5665-5748 3.23e-04

Fibronectin type III domain;


Pssm-ID: 394996 [Multi-domain]  Cd Length: 85  Bit Score: 43.17  E-value: 3.23e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561  5665 SPPKGpLDITKITRDGCHLTWNVPDDdGGSPILHYIIE---KMDLSRSTWSDAGmSTHIVHDVTRLVHRKEYLFRVKAVN 5741
Cdd:pfam00041    1 SAPSN-LTVTDVTSTSLTVSWTPPPD-GNGPITGYEVEyrpKNSGEPWNEITVP-GTTTSVTLTGLKPGTEYEVRVQAVN 77

                   ....*..
gi 281359561  5742 AIGESDP 5748
Cdd:pfam00041   78 GGGEGPP 84
IG_like smart00410
Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.
778-835 3.51e-04

Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.


Pssm-ID: 214653 [Multi-domain]  Cd Length: 85  Bit Score: 43.26  E-value: 3.51e-04
                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|....*....
gi 281359561    778 VEWYK-GSTVIRETKDITTTFDGTTARLTFSSARTEHTSNYKVIVTNEVGKDESSCKIT 835
Cdd:smart00410   26 VTWYKqGGKLLAESGRFSVSRSGSTSTLTISNVTPEDSGTYTCAATNSSGSASSGTTLT 84
IG_like smart00410
Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.
7354-7440 2.41e-03

Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.


Pssm-ID: 214653 [Multi-domain]  Cd Length: 85  Bit Score: 40.57  E-value: 2.41e-03
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561   7354 PSELKLPEGDNSKIKIFYSGDQPLTVILKKNNEVICDSNDDTHVKVNifDDYVAIYIRNIVKSDGGPYQIEFTNESGSAT 7433
Cdd:smart00410    1 PPSVTVKEGESVTLSCEASGSPPPEVTWYKQGGKLLAESGRFSVSRS--GSTSTLTISNVTPEDSGTYTCAATNSSGSAS 78

                    ....*..
gi 281359561   7434 GEFYVHI 7440
Cdd:smart00410   79 SGTTLTV 85
Ig cd00096
Immunoglobulin domain; The members here are composed of the immunoglobulin (Ig) domain found ...
777-831 7.04e-03

Immunoglobulin domain; The members here are composed of the immunoglobulin (Ig) domain found in the Ig superfamily. The Ig superfamily is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. Members of this group are components of immunoglobulin, neuroglia, cell surface glycoproteins, including T-cell receptors, CD2, CD4, CD8, and membrane glycoproteins, including butyrophilin and chondroitin sulfate proteoglycan core protein. A predominant feature of most Ig domains is a disulfide bridge connecting the two beta-sheets with a tryptophan residue packed against the disulfide bond. Ig superfamily (IgSF) domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. Typically, the V-set domains have A, B, E, and D strands in one sheet and A', G, F, C, C' and C" in the other. The structures in C1-set are smaller than those in the V-set; they have one beta sheet that is formed by strands A, B, E, and D and the other by strands G, F, C, and C'. Moreover, a C1-set Ig domain contains a short C' strand (three residues) and lacks A' and C" strand. Unlike other Ig domain sets, C2-set structures do not have a D strand. Like the V-set Ig domains, members of the I-set have a discontinuous A strand, but lack a C" strand.


Pssm-ID: 409353 [Multi-domain]  Cd Length: 70  Bit Score: 38.85  E-value: 7.04e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 281359561  777 KVEWYKGSTVIRETKDITTTFDGTTARLTFSSARTEHTSNYKVIVTNEVGKDESS 831
Cdd:cd00096    14 TITWYKNGKPLPPSSRDSRRSELGNGTLTISNVTLEDSGTYTCVASNSAGGSASA 68
 
Name Accession Description Interval E-value
STKc_Twitchin_like cd14114
The catalytic domain of the Giant Serine/Threonine Kinases, Twitchin and Projectin; STKs ...
7986-8244 7.64e-177

The catalytic domain of the Giant Serine/Threonine Kinases, Twitchin and Projectin; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily is composed of Caenorhabditis elegans and Aplysia californica Twitchin, Drosophila melanogaster Projectin, and similar proteins. These are very large muscle proteins containing multiple immunoglobulin (Ig)-like and fibronectin type III (FN3) domains and a single kinase domain near the C-terminus. Twitchin and Projectin are both associated with thick filaments. Twitchin is localized in the outer parts of A-bands and is involved in regulating muscle contraction. It interacts with the myofibrillar proteins myosin and actin in a phosphorylation-dependent manner, and may be involved in regulating the myosin cross-bridge cycle. The kinase activity of Twitchen is activated by Ca2+ and the Ca2+ binding protein S100A1. Projectin is associated with the end of thick filaments and is a component of flight muscle connecting filaments. The kinase domain of Projectin may play roles in autophosphorylation and transphosphorylation, which impact the formation of myosin filaments. The Twitchin-like subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271016 [Multi-domain]  Cd Length: 259  Bit Score: 544.49  E-value: 7.64e-177
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 7986 YDRYDILEEIGTGAFGVVHRCRERSTGNIFAAKFIPVSHSVEKDLIRREIDIMNQLHHQKLINLHDAFEDDDEMILILEF 8065
Cdd:cd14114     1 YDHYDILEELGTGAFGVVHRCTERATGNNFAAKFIMTPHESDKETVRKEIQIMNQLHHPKLINLHDAFEDDNEMVLILEF 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 8066 LSGGELFERITAEGYVMTEAEVINYMRQICEGIRHMHEQNIIHLDIKPENIMCQTRSSTNVKLIDFGLATRLDPNEVVKI 8145
Cdd:cd14114    81 LSGGELFERIAAEHYKMSEAEVINYMRQVCEGLCHMHENNIVHLDIKPENIMCTTKRSNEVKLIDFGLATHLDPKESVKV 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 8146 TTGTAEFAAPEIVNREPVGFYTDMWATGVLSYVLLSGLSPFAGDNDVQTLKNVKACDWDFDVESFKYISEEAKDFIRKLL 8225
Cdd:cd14114   161 TTGTAEFAAPEIVEREPVGFYTDMWAVGVLSYVLLSGLSPFAGENDDETLRNVKSCDWNFDDSAFSGISEEAKDFIRKLL 240
                         250
                  ....*....|....*....
gi 281359561 8226 VRNKEKRMTAHECLLHPWL 8244
Cdd:cd14114   241 LADPNKRMTIHQALEHPWL 259
STKc_MLCK cd14103
Catalytic domain of the Serine/Threonine Kinase, Myosin Light Chain Kinase; STKs catalyze the ...
7995-8244 3.69e-138

Catalytic domain of the Serine/Threonine Kinase, Myosin Light Chain Kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MLCK phosphorylates myosin regulatory light chain and controls the contraction of all muscle types. In vertebrates, different MLCKs function in smooth (MLCK1), skeletal (MLCK2), and cardiac (MLCK3) muscles. A fourth protein, MLCK4, has also been identified through comprehensive genome analysis although it has not been biochemically characterized. The MLCK1 gene expresses three transcripts in a cell-specific manner: a short MLCK1 which contains three immunoglobulin (Ig)-like and one fibronectin type III (FN3) domains, PEVK and actin-binding regions, and a kinase domain near the C-terminus; a long MLCK1 containing six additional Ig-like domains at the N-terminus compared to the short MLCK1; and the C-terminal Ig module. MLCK2, MLCK3, and MLCK4 share a simpler domain architecture of a single kinase domain near the C-terminus and the absence of Ig-like or FN3 domains. The MLCK subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271005 [Multi-domain]  Cd Length: 250  Bit Score: 433.19  E-value: 3.69e-138
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 7995 IGTGAFGVVHRCRERSTGNIFAAKFIPVSHSVEKDLIRREIDIMNQLHHQKLINLHDAFEDDDEMILILEFLSGGELFER 8074
Cdd:cd14103     1 LGRGKFGTVYRCVEKATGKELAAKFIKCRKAKDREDVRNEIEIMNQLRHPRLLQLYDAFETPREMVLVMEYVAGGELFER 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 8075 ITAEGYVMTEAEVINYMRQICEGIRHMHEQNIIHLDIKPENIMCQTRSSTNVKLIDFGLATRLDPNEVVKITTGTAEFAA 8154
Cdd:cd14103    81 VVDDDFELTERDCILFMRQICEGVQYMHKQGILHLDLKPENILCVSRTGNQIKIIDFGLARKYDPDKKLKVLFGTPEFVA 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 8155 PEIVNREPVGFYTDMWATGVLSYVLLSGLSPFAGDNDVQTLKNVKACDWDFDVESFKYISEEAKDFIRKLLVRNKEKRMT 8234
Cdd:cd14103   161 PEVVNYEPISYATDMWSVGVICYVLLSGLSPFMGDNDAETLANVTRAKWDFDDEAFDDISDEAKDFISKLLVKDPRKRMS 240
                         250
                  ....*....|
gi 281359561 8235 AHECLLHPWL 8244
Cdd:cd14103   241 AAQCLQHPWL 250
STKc_MLCK-like cd14006
Catalytic kinase domain of Myosin Light Chain Kinase-like Serine/Threonine Kinases; STKs ...
7995-8243 6.78e-129

Catalytic kinase domain of Myosin Light Chain Kinase-like Serine/Threonine Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This family is composed of MLCKs and related MLCK-like kinase domains from giant STKs such as titin, obscurin, SPEG, Unc-89, Trio, kalirin, and Twitchin. Also included in this family are Death-Associated Protein Kinases (DAPKs) and Death-associated protein kinase-Related Apoptosis-inducing protein Kinase (DRAKs). MLCK phosphorylates myosin regulatory light chain and controls the contraction of all muscle types. Titin, obscurin, Twitchin, and SPEG are muscle proteins involved in the contractile apparatus. The giant STKs are multidomain proteins containing immunoglobulin (Ig), fibronectin type III (FN3), SH3, RhoGEF, PH and kinase domains. Titin, obscurin, Twitchin, and SPEG contain many Ig domain repeats at the N-terminus, while Trio and Kalirin contain spectrin-like repeats. The MLCK-like family is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270908 [Multi-domain]  Cd Length: 247  Bit Score: 406.27  E-value: 6.78e-129
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 7995 IGTGAFGVVHRCRERSTGNIFAAKFIPVsHSVEKDLIRREIDIMNQLHHQKLINLHDAFEDDDEMILILEFLSGGELFER 8074
Cdd:cd14006     1 LGRGRFGVVKRCIEKATGREFAAKFIPK-RDKKKEAVLREISILNQLQHPRIIQLHEAYESPTELVLILELCSGGELLDR 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 8075 ItAEGYVMTEAEVINYMRQICEGIRHMHEQNIIHLDIKPENIMCQTRSSTNVKLIDFGLATRLDPNEVVKITTGTAEFAA 8154
Cdd:cd14006    80 L-AERGSLSEEEVRTYMRQLLEGLQYLHNHHILHLDLKPENILLADRPSPQIKIIDFGLARKLNPGEELKEIFGTPEFVA 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 8155 PEIVNREPVGFYTDMWATGVLSYVLLSGLSPFAGDNDVQTLKNVKACDWDFDVESFKYISEEAKDFIRKLLVRNKEKRMT 8234
Cdd:cd14006   159 PEIVNGEPVSLATDMWSIGVLTYVLLSGLSPFLGEDDQETLANISACRVDFSEEYFSSVSQEAKDFIRKLLVKEPRKRPT 238

                  ....*....
gi 281359561 8235 AHECLLHPW 8243
Cdd:cd14006   239 AQEALQHPW 247
STKc_MLCK4 cd14193
Catalytic domain of the Serine/Threonine Kinase, Myosin Light Chain Kinase 4; STKs catalyze ...
7993-8244 3.47e-101

Catalytic domain of the Serine/Threonine Kinase, Myosin Light Chain Kinase 4; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MLCK phosphorylates myosin regulatory light chain and controls the contraction of all muscle types. In vertebrates, different MLCKs function in smooth (MLCK1), skeletal (MLCK2), and cardiac (MLCK3) muscles. A fourth protein, MLCK4, has also been identified through comprehensive genome analysis although it has not been biochemically characterized. MLCK4 (or MYLK4 or SgK085) contains a single kinase domain near the C-terminus. The MLCK4 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271095 [Multi-domain]  Cd Length: 261  Bit Score: 327.64  E-value: 3.47e-101
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 7993 EEIGTGAFGVVHRCRERSTGNIFAAKFIPVSHSVEKDLIRREIDIMNQLHHQKLINLHDAFEDDDEMILILEFLSGGELF 8072
Cdd:cd14193    10 EILGGGRFGQVHKCEEKSSGLKLAAKIIKARSQKEKEEVKNEIEVMNQLNHANLIQLYDAFESRNDIVLVMEYVDGGELF 89
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 8073 ERITAEGYVMTEAEVINYMRQICEGIRHMHEQNIIHLDIKPENIMCQTRSSTNVKLIDFGLATRLDPNEVVKITTGTAEF 8152
Cdd:cd14193    90 DRIIDENYNLTELDTILFIKQICEGIQYMHQMYILHLDLKPENILCVSREANQVKIIDFGLARRYKPREKLRVNFGTPEF 169
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 8153 AAPEIVNREPVGFYTDMWATGVLSYVLLSGLSPFAGDNDVQTLKNVKACDWDFDVESFKYISEEAKDFIRKLLVRNKEKR 8232
Cdd:cd14193   170 LAPEVVNYEFVSFPTDMWSLGVIAYMLLSGLSPFLGEDDNETLNNILACQWDFEDEEFADISEEAKDFISKLLIKEKSWR 249
                         250
                  ....*....|..
gi 281359561 8233 MTAHECLLHPWL 8244
Cdd:cd14193   250 MSASEALKHPWL 261
STKc_CAMK cd05117
The catalytic domain of CAMK family Serine/Threonine Kinases; STKs catalyze the transfer of ...
7988-8243 1.99e-99

The catalytic domain of CAMK family Serine/Threonine Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. CaMKs are multifunctional calcium and calmodulin (CaM) stimulated STKs involved in cell cycle regulation. There are several types of CaMKs including CaMKI, CaMKII, and CaMKIV. CaMKI proteins are monomeric and they play pivotal roles in the nervous system, including long-term potentiation, dendritic arborization, neurite outgrowth, and the formation of spines, synapses, and axons. CaMKII is a signaling molecule that translates upstream calcium and reactive oxygen species (ROS) signals into downstream responses that play important roles in synaptic function and cardiovascular physiology. CAMKIV is implicated in regulating several transcription factors like CREB, MEF2, and retinoid orphan receptors, as well as in T-cell development and signaling. The CAMK family also consists of other related kinases including the Phosphorylase kinase Gamma subunit (PhKG), the C-terminal kinase domains of Ribosomal S6 kinase (RSK) and Mitogen and stress-activated kinase (MSK), Doublecortin-like kinase (DCKL), and the MAPK-activated protein kinases MK2, MK3, and MK5, among others. The CAMK family is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270687 [Multi-domain]  Cd Length: 258  Bit Score: 322.50  E-value: 1.99e-99
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 7988 RYDILEEIGTGAFGVVHRCRERSTGNIFAAKFIPVS--HSVEKDLIRREIDIMNQLHHQKLINLHDAFEDDDEMILILEF 8065
Cdd:cd05117     1 KYELGKVLGRGSFGVVRLAVHKKTGEEYAVKIIDKKklKSEDEEMLRREIEILKRLDHPNIVKLYEVFEDDKNLYLVMEL 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 8066 LSGGELFERITAEGYvMTEAEVINYMRQICEGIRHMHEQNIIHLDIKPENIMCQTRS-STNVKLIDFGLATRLDPNEVVK 8144
Cdd:cd05117    81 CTGGELFDRIVKKGS-FSEREAAKIMKQILSAVAYLHSQGIVHRDLKPENILLASKDpDSPIKIIDFGLAKIFEEGEKLK 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 8145 ITTGTAEFAAPEIVNREPVGFYTDMWATGVLSYVLLSGLSPFAGDNDVQTLKNVKACDWDFDVESFKYISEEAKDFIRKL 8224
Cdd:cd05117   160 TVCGTPYYVAPEVLKGKGYGKKCDIWSLGVILYILLCGYPPFYGETEQELFEKILKGKYSFDSPEWKNVSEEAKDLIKRL 239
                         250
                  ....*....|....*....
gi 281359561 8225 LVRNKEKRMTAHECLLHPW 8243
Cdd:cd05117   240 LVVDPKKRLTAAEALNHPW 258
STKc_MLCK3 cd14192
Catalytic domain of the Serine/Threonine Kinase, Myosin Light Chain Kinase 3; STKs catalyze ...
7993-8244 2.95e-99

Catalytic domain of the Serine/Threonine Kinase, Myosin Light Chain Kinase 3; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MLCK3 (or MYLK3) phosphorylates myosin regulatory light chain 2 and controls the contraction of cardiac muscles. It is expressed specifically in both the atrium and ventricle of the heart and its expression is regulated by the cardiac protein Nkx2-5. MLCK3 plays an important role in cardiogenesis by regulating the assembly of cardiac sarcomeres, the repeating contractile unit of striated muscle. MLCK3 contains a single kinase domain near the C-terminus and a unique N-terminal half, and unlike MLCK1/2, it does not appear to be regulated by Ca2+/calmodulin. The MLCK3 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271094 [Multi-domain]  Cd Length: 261  Bit Score: 322.30  E-value: 2.95e-99
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 7993 EEIGTGAFGVVHRCRERSTGNIFAAKFIPVSHSVEKDLIRREIDIMNQLHHQKLINLHDAFEDDDEMILILEFLSGGELF 8072
Cdd:cd14192    10 EVLGGGRFGQVHKCTELSTGLTLAAKIIKVKGAKEREEVKNEINIMNQLNHVNLIQLYDAFESKTNLTLIMEYVDGGELF 89
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 8073 ERITAEGYVMTEAEVINYMRQICEGIRHMHEQNIIHLDIKPENIMCQTRSSTNVKLIDFGLATRLDPNEVVKITTGTAEF 8152
Cdd:cd14192    90 DRITDESYQLTELDAILFTRQICEGVHYLHQHYILHLDLKPENILCVNSTGNQIKIIDFGLARRYKPREKLKVNFGTPEF 169
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 8153 AAPEIVNREPVGFYTDMWATGVLSYVLLSGLSPFAGDNDVQTLKNVKACDWDFDVESFKYISEEAKDFIRKLLVRNKEKR 8232
Cdd:cd14192   170 LAPEVVNYDFVSFPTDMWSVGVITYMLLSGLSPFLGETDAETMNNIVNCKWDFDAEAFENLSEEAKDFISRLLVKEKSCR 249
                         250
                  ....*....|..
gi 281359561 8233 MTAHECLLHPWL 8244
Cdd:cd14192   250 MSATQCLKHEWL 261
STKc_MLCK2 cd14190
Catalytic domain of the Serine/Threonine Kinase, Myosin Light Chain Kinase 2; STKs catalyze ...
7993-8244 5.02e-99

Catalytic domain of the Serine/Threonine Kinase, Myosin Light Chain Kinase 2; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MLCK2 (or MYLK2) phosphorylates myosin regulatory light chain and controls the contraction of skeletal muscles. MLCK2 contains a single kinase domain near the C-terminus followed by a regulatory segment containing an autoinhibitory Ca2+/calmodulin binding site. The MLCK2 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271092 [Multi-domain]  Cd Length: 261  Bit Score: 321.48  E-value: 5.02e-99
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 7993 EEIGTGAFGVVHRCRERSTGNIFAAKFIPVSHSVEKDLIRREIDIMNQLHHQKLINLHDAFEDDDEMILILEFLSGGELF 8072
Cdd:cd14190    10 EVLGGGKFGKVHTCTEKRTGLKLAAKVINKQNSKDKEMVLLEIQVMNQLNHRNLIQLYEAIETPNEIVLFMEYVEGGELF 89
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 8073 ERITAEGYVMTEAEVINYMRQICEGIRHMHEQNIIHLDIKPENIMCQTRSSTNVKLIDFGLATRLDPNEVVKITTGTAEF 8152
Cdd:cd14190    90 ERIVDEDYHLTEVDAMVFVRQICEGIQFMHQMRVLHLDLKPENILCVNRTGHQVKIIDFGLARRYNPREKLKVNFGTPEF 169
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 8153 AAPEIVNREPVGFYTDMWATGVLSYVLLSGLSPFAGDNDVQTLKNVKACDWDFDVESFKYISEEAKDFIRKLLVRNKEKR 8232
Cdd:cd14190   170 LSPEVVNYDQVSFPTDMWSMGVITYMLLSGLSPFLGDDDTETLNNVLMGNWYFDEETFEHVSDEAKDFVSNLIIKERSAR 249
                         250
                  ....*....|..
gi 281359561 8233 MTAHECLLHPWL 8244
Cdd:cd14190   250 MSATQCLKHPWL 261
STKc_MLCK1 cd14191
Catalytic domain of the Serine/Threonine Kinase, Myosin Light Chain Kinase 1; STKs catalyze ...
7987-8244 2.53e-97

Catalytic domain of the Serine/Threonine Kinase, Myosin Light Chain Kinase 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MLCK1 (or MYLK1) phosphorylates myosin regulatory light chain and controls the contraction of smooth muscles. The MLCK1 gene expresses three transcripts in a cell-specific manner: a short MLCK1 which contains three immunoglobulin (Ig)-like and one fibronectin type III (FN3) domains, PEVK and actin-binding regions, and a kinase domain near the C-terminus followed by a regulatory segment containing an autoinhibitory Ca2+/calmodulin binding site; a long MLCK1 containing six additional Ig-like domains at the N-terminus compared to the short MLCK1; and the C-terminal Ig module which results in the expression of telokin in phasic smooth muscles, leading to Ca2+ desensitization by cyclic nucleotides of smooth muscle force. MLCK1 is also responsible for myosin regulatory light chain phosphorylation in nonmuscle cells and may play a role in regulating myosin II ATPase activity. The MLCK1 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271093 [Multi-domain]  Cd Length: 259  Bit Score: 316.56  E-value: 2.53e-97
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 7987 DRYDILEEIGTGAFGVVHRCRERSTGNIFAAKFIPVSHSVEKDLIRREIDIMNQLHHQKLINLHDAFEDDDEMILILEFL 8066
Cdd:cd14191     2 DFYDIEERLGSGKFGQVFRLVEKKTKKVWAGKFFKAYSAKEKENIRQEISIMNCLHHPKLVQCVDAFEEKANIVMVLEMV 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 8067 SGGELFERITAEGYVMTEAEVINYMRQICEGIRHMHEQNIIHLDIKPENIMCQTRSSTNVKLIDFGLATRLDPNEVVKIT 8146
Cdd:cd14191    82 SGGELFERIIDEDFELTERECIKYMRQISEGVEYIHKQGIVHLDLKPENIMCVNKTGTKIKLIDFGLARRLENAGSLKVL 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 8147 TGTAEFAAPEIVNREPVGFYTDMWATGVLSYVLLSGLSPFAGDNDVQTLKNVKACDWDFDVESFKYISEEAKDFIRKLLV 8226
Cdd:cd14191   162 FGTPEFVAPEVINYEPIGYATDMWSIGVICYILVSGLSPFMGDNDNETLANVTSATWDFDDEAFDEISDDAKDFISNLLK 241
                         250
                  ....*....|....*...
gi 281359561 8227 RNKEKRMTAHECLLHPWL 8244
Cdd:cd14191   242 KDMKARLTCTQCLQHPWL 259
S_TKc smart00220
Serine/Threonine protein kinases, catalytic domain; Phosphotransferases. Serine or ...
7989-8244 1.26e-95

Serine/Threonine protein kinases, catalytic domain; Phosphotransferases. Serine or threonine-specific kinase subfamily.


Pssm-ID: 214567 [Multi-domain]  Cd Length: 254  Bit Score: 311.39  E-value: 1.26e-95
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561   7989 YDILEEIGTGAFGVVHRCRERSTGNIFAAKFIPVSHSVEK-DLIRREIDIMNQLHHQKLINLHDAFEDDDEMILILEFLS 8067
Cdd:smart00220    1 YEILEKLGEGSFGKVYLARDKKTGKLVAIKVIKKKKIKKDrERILREIKILKKLKHPNIVRLYDVFEDEDKLYLVMEYCE 80
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561   8068 GGELFERITAEGYvMTEAEVINYMRQICEGIRHMHEQNIIHLDIKPENIMCQtrSSTNVKLIDFGLATRLDPNEVVKITT 8147
Cdd:smart00220   81 GGDLFDLLKKRGR-LSEDEARFYLRQILSALEYLHSKGIVHRDLKPENILLD--EDGHVKLADFGLARQLDPGEKLTTFV 157
                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561   8148 GTAEFAAPEIVNREPVGFYTDMWATGVLSYVLLSGLSPFAGDNDVQTL-KNVKACDWDFDvESFKYISEEAKDFIRKLLV 8226
Cdd:smart00220  158 GTPEYMAPEVLLGKGYGKAVDIWSLGVILYELLTGKPPFPGDDQLLELfKKIGKPKPPFP-PPEWDISPEAKDLIRKLLV 236
                           250
                    ....*....|....*...
gi 281359561   8227 RNKEKRMTAHECLLHPWL 8244
Cdd:smart00220  237 KDPEKRLTAEEALQHPFF 254
STKc_Titin cd14104
Catalytic domain of the Giant Serine/Threonine Kinase Titin; STKs catalyze the transfer of the ...
7988-8245 3.23e-95

Catalytic domain of the Giant Serine/Threonine Kinase Titin; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Titin, also called connectin, is a muscle-specific elastic protein and is the largest known protein to date. It contains multiple immunoglobulin (Ig)-like and fibronectin type III (FN3) domains, and a single kinase domain near the C-terminus. It spans half of the sarcomere, the repeating contractile unit of striated muscle, and performs mechanical and catalytic functions. Titin contributes to the passive force generated when muscle is stretched during relaxation. Its kinase domain phosphorylates and regulates the muscle protein telethonin, which is required for sarcomere formation in differentiating myocytes. In addition, titin binds many sarcomere proteins and acts as a molecular scaffold for filament formation during myofibrillogenesis. The Titin subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271006 [Multi-domain]  Cd Length: 277  Bit Score: 311.41  E-value: 3.23e-95
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 7988 RYDILEEIGTGAFGVVHRCRERSTGNIFAAKFIPVSHSvEKDLIRREIDIMNQLHHQKLINLHDAFEDDDEMILILEFLS 8067
Cdd:cd14104     1 KYMIAEELGRGQFGIVHRCVETSSKKTYMAKFVKVKGA-DQVLVKKEISILNIARHRNILRLHESFESHEELVMIFEFIS 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 8068 GGELFERITAEGYVMTEAEVINYMRQICEGIRHMHEQNIIHLDIKPENIMCQTRSSTNVKLIDFGLATRLDPNEVVKITT 8147
Cdd:cd14104    80 GVDIFERITTARFELNEREIVSYVRQVCEALEFLHSKNIGHFDIRPENIIYCTRRGSYIKIIEFGQSRQLKPGDKFRLQY 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 8148 GTAEFAAPEIVNREPVGFYTDMWATGVLSYVLLSGLSPFAGDNDVQTLKNVKACDWDFDVESFKYISEEAKDFIRKLLVR 8227
Cdd:cd14104   160 TSAEFYAPEVHQHESVSTATDMWSLGCLVYVLLSGINPFEAETNQQTIENIRNAEYAFDDEAFKNISIEALDFVDRLLVK 239
                         250
                  ....*....|....*...
gi 281359561 8228 NKEKRMTAHECLLHPWLT 8245
Cdd:cd14104   240 ERKSRMTAQEALNHPWLK 257
STKc_DAPK cd14105
Catalytic domain of the Serine/Threonine Kinase, Death-Associated Protein Kinase; STKs ...
7983-8244 4.34e-93

Catalytic domain of the Serine/Threonine Kinase, Death-Associated Protein Kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. DAPKs mediate cell death and act as tumor suppressors. They are necessary to induce cell death and their overexpression leads to death-associated changes including membrane blebbing, cell rounding, and formation of autophagic vesicles. Vertebrates contain three subfamily members with different domain architecture, localization, and function. DAPK1 is the prototypical member of the subfamily and is also simply referred to as DAPK. DAPK2 is also called DAPK-related protein 1 (DRP-1), while DAPK3 has also been named DAP-like kinase (DLK) and zipper-interacting protein kinase (ZIPk). These proteins are ubiquitously expressed in adult tissues, are capable of cross talk with each other, and may act synergistically in regulating cell death. The DAPK subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271007 [Multi-domain]  Cd Length: 269  Bit Score: 304.80  E-value: 4.34e-93
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 7983 QSVYDRYDILEEIGTGAFGVVHRCRERSTGNIFAAKFIPVSHS------VEKDLIRREIDIMNQLHHQKLINLHDAFEDD 8056
Cdd:cd14105     1 ENVEDFYDIGEELGSGQFAVVKKCREKSTGLEYAAKFIKKRRSkasrrgVSREDIEREVSILRQVLHPNIITLHDVFENK 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 8057 DEMILILEFLSGGELFERItAEGYVMTEAEVINYMRQICEGIRHMHEQNIIHLDIKPENIMCQTRSSTN--VKLIDFGLA 8134
Cdd:cd14105    81 TDVVLILELVAGGELFDFL-AEKESLSEEEATEFLKQILDGVNYLHTKNIAHFDLKPENIMLLDKNVPIprIKLIDFGLA 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 8135 TRLDPNEVVKITTGTAEFAAPEIVNREPVGFYTDMWATGVLSYVLLSGLSPFAGDNDVQTLKNVKACDWDFDVESFKYIS 8214
Cdd:cd14105   160 HKIEDGNEFKNIFGTPEFVAPEIVNYEPLGLEADMWSIGVITYILLSGASPFLGDTKQETLANITAVNYDFDDEYFSNTS 239
                         250       260       270
                  ....*....|....*....|....*....|
gi 281359561 8215 EEAKDFIRKLLVRNKEKRMTAHECLLHPWL 8244
Cdd:cd14105   240 ELAKDFIRQLLVKDPRKRMTIQESLRHPWI 269
STKc_DAPK2 cd14196
Catalytic domain of the Serine/Threonine Kinase, Death-Associated Protein Kinase 2; STKs ...
7983-8244 2.22e-86

Catalytic domain of the Serine/Threonine Kinase, Death-Associated Protein Kinase 2; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. DAPKs mediate cell death and act as tumor suppressors. They are necessary to induce cell death and their overexpression leads to death-associated changes including membrane blebbing, cell rounding, and formation of autophagic vesicles. Vertebrates contain three subfamily members with different domain architecture, localization, and function. DAPK2, also called DAPK-related protein 1 (DRP-1), is a Ca2+/calmodulin (CaM)-regulated protein containing an N-terminal kinase domain, a CaM autoinhibitory site and a dimerization module. It lacks the cytoskeletal binding regions of DAPK1 and the exogenous protein has been shown to be soluble and cytoplasmic. FLAG-tagged DAPK2, however, accumulated within membrane-enclosed autophagic vesicles. It is unclear where endogenous DAPK2 is localized. DAPK2 participates in TNF-alpha and FAS-receptor induced cell death and enhances neutrophilic maturation in myeloid leukemic cells. It contributes to the induction of anoikis and its down-regulation is implicated in the beta-catenin induced resistance of malignant epithelial cells to anoikis. The DAPK2 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271098 [Multi-domain]  Cd Length: 269  Bit Score: 285.70  E-value: 2.22e-86
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 7983 QSVYDRYDILEEIGTGAFGVVHRCRERSTGNIFAAKFIPVSHS------VEKDLIRREIDIMNQLHHQKLINLHDAFEDD 8056
Cdd:cd14196     1 QKVEDFYDIGEELGSGQFAIVKKCREKSTGLEYAAKFIKKRQSrasrrgVSREEIEREVSILRQVLHPNIITLHDVYENR 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 8057 DEMILILEFLSGGELFERItAEGYVMTEAEVINYMRQICEGIRHMHEQNIIHLDIKPENIMCQTRSST--NVKLIDFGLA 8134
Cdd:cd14196    81 TDVVLILELVSGGELFDFL-AQKESLSEEEATSFIKQILDGVNYLHTKKIAHFDLKPENIMLLDKNIPipHIKLIDFGLA 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 8135 TRLDPNEVVKITTGTAEFAAPEIVNREPVGFYTDMWATGVLSYVLLSGLSPFAGDNDVQTLKNVKACDWDFDVESFKYIS 8214
Cdd:cd14196   160 HEIEDGVEFKNIFGTPEFVAPEIVNYEPLGLEADMWSIGVITYILLSGASPFLGDTKQETLANITAVSYDFDEEFFSHTS 239
                         250       260       270
                  ....*....|....*....|....*....|
gi 281359561 8215 EEAKDFIRKLLVRNKEKRMTAHECLLHPWL 8244
Cdd:cd14196   240 ELAKDFIRKLLVKETRKRLTIQEALRHPWI 269
STKc_DAPK1 cd14194
Catalytic domain of the Serine/Threonine Kinase, Death-Associated Protein Kinase 1; STKs ...
7983-8244 1.68e-85

Catalytic domain of the Serine/Threonine Kinase, Death-Associated Protein Kinase 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. DAPKs mediate cell death and act as tumor suppressors. They are necessary to induce cell death and their overexpression leads to death-associated changes including membrane blebbing, cell rounding, and formation of autophagic vesicles. Vertebrates contain three subfamily members with different domain architecture, localization, and function. DAPK1 is the prototypical member of the subfamily and is also simply referred to as DAPK. It is Ca2+/calmodulin (CaM)-regulated and actin-associated protein that contains an N-terminal kinase domain followed by an autoinhibitory CaM binding region and a large C-terminal extension with multiple functional domains including ankyrin (ANK) repeats, a cytoskeletal binding domain, a Death domain, and a serine-rich tail. Loss of DAPK1 expression, usually because of DNA methylation, is implicated in many tumor types. DAPK1 is highly abundant in the brain and has also been associated with neurodegeneration. The DAPK1 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271096 [Multi-domain]  Cd Length: 269  Bit Score: 283.06  E-value: 1.68e-85
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 7983 QSVYDRYDILEEIGTGAFGVVHRCRERSTGNIFAAKFIPVSHS------VEKDLIRREIDIMNQLHHQKLINLHDAFEDD 8056
Cdd:cd14194     1 ENVDDYYDTGEELGSGQFAVVKKCREKSTGLQYAAKFIKKRRTkssrrgVSREDIEREVSILKEIQHPNVITLHEVYENK 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 8057 DEMILILEFLSGGELFERItAEGYVMTEAEVINYMRQICEGIRHMHEQNIIHLDIKPENIMCQTRSSTN--VKLIDFGLA 8134
Cdd:cd14194    81 TDVILILELVAGGELFDFL-AEKESLTEEEATEFLKQILNGVYYLHSLQIAHFDLKPENIMLLDRNVPKprIKIIDFGLA 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 8135 TRLDPNEVVKITTGTAEFAAPEIVNREPVGFYTDMWATGVLSYVLLSGLSPFAGDNDVQTLKNVKACDWDFDVESFKYIS 8214
Cdd:cd14194   160 HKIDFGNEFKNIFGTPEFVAPEIVNYEPLGLEADMWSIGVITYILLSGASPFLGDTKQETLANVSAVNYEFEDEYFSNTS 239
                         250       260       270
                  ....*....|....*....|....*....|
gi 281359561 8215 EEAKDFIRKLLVRNKEKRMTAHECLLHPWL 8244
Cdd:cd14194   240 ALAKDFIRRLLVKDPKKRMTIQDSLQHPWI 269
STKc_DRAK cd14106
Catalytic domain of the Serine/Threonine Kinase, Death-associated protein kinase-Related ...
7993-8244 4.80e-81

Catalytic domain of the Serine/Threonine Kinase, Death-associated protein kinase-Related Apoptosis-inducing protein Kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. DRAKs, also called STK17, were named based on their similarity (around 50% identity) to the kinase domain of DAPKs. They contain an N-terminal kinase domain and a C-terminal regulatory domain. Vertebrates contain two subfamily members, DRAK1 and DRAK2. Both DRAKs are localized to the nucleus, autophosphorylate themselves, and phosphorylate myosin light chain as a substrate. They may play a role in apoptotic signaling. The DRAK subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271008 [Multi-domain]  Cd Length: 268  Bit Score: 269.99  E-value: 4.80e-81
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 7993 EEIGTGAFGVVHRCRERSTGNIFAAKFIpvshsvekDLIRREIDIMNQLHHQ-----------KLINLHDAFEDDDEMIL 8061
Cdd:cd14106    14 TPLGRGKFAVVRKCIHKETGKEYAAKFL--------RKRRRGQDCRNEILHEiavlelckdcpRVVNLHEVYETRSELIL 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 8062 ILEFLSGGELFERITAEGyVMTEAEVINYMRQICEGIRHMHEQNIIHLDIKPENIM-CQTRSSTNVKLIDFGLATRLDPN 8140
Cdd:cd14106    86 ILELAAGGELQTLLDEEE-CLTEADVRRLMRQILEGVQYLHERNIVHLDLKPQNILlTSEFPLGDIKLCDFGISRVIGEG 164
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 8141 EVVKITTGTAEFAAPEIVNREPVGFYTDMWATGVLSYVLLSGLSPFAGDNDVQTLKNVKACDWDFDVESFKYISEEAKDF 8220
Cdd:cd14106   165 EEIREILGTPDYVAPEILSYEPISLATDMWSIGVLTYVLLTGHSPFGGDDKQETFLNISQCNLDFPEELFKDVSPLAIDF 244
                         250       260
                  ....*....|....*....|....
gi 281359561 8221 IRKLLVRNKEKRMTAHECLLHPWL 8244
Cdd:cd14106   245 IKRLLVKDPEKRLTAKECLEHPWL 268
STKc_DAPK3 cd14195
Catalytic domain of the Serine/Threonine Kinase, Death-Associated Protein Kinase 3; STKs ...
7983-8244 1.07e-79

Catalytic domain of the Serine/Threonine Kinase, Death-Associated Protein Kinase 3; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. DAPKs mediate cell death and act as tumor suppressors. They are necessary to induce cell death and their overexpression leads to death-associated changes including membrane blebbing, cell rounding, and formation of autophagic vesicles. Vertebrates contain three subfamily members with different domain architecture, localization, and function. DAPK3, also called DAP-like kinase (DLK) and zipper-interacting protein kinase (ZIPk), contains an N-terminal kinase domain and a C-terminal region with nuclear localization signals (NLS) and a leucine zipper motif that mediates homodimerization and interaction with other leucine zipper proteins. It interacts with Par-4, a protein that contains a death domain and interacts with actin filaments. DAPK3 is present in both the cytoplasm and nucleus. Its co-expression with Par-4 results in the co-localization of the two proteins to actin filaments. In addition to cell death, DAPK3 is also implicated in mediating cell motility and the contraction of smooth muscles. The DAPK3 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271097 [Multi-domain]  Cd Length: 271  Bit Score: 266.48  E-value: 1.07e-79
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 7983 QSVYDRYDILEEIGTGAFGVVHRCRERSTGNIFAAKFIP---VSHS---VEKDLIRREIDIMNQLHHQKLINLHDAFEDD 8056
Cdd:cd14195     1 SMVEDHYEMGEELGSGQFAIVRKCREKGTGKEYAAKFIKkrrLSSSrrgVSREEIEREVNILREIQHPNIITLHDIFENK 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 8057 DEMILILEFLSGGELFERItAEGYVMTEAEVINYMRQICEGIRHMHEQNIIHLDIKPENIMCQTRSSTN--VKLIDFGLA 8134
Cdd:cd14195    81 TDVVLILELVSGGELFDFL-AEKESLTEEEATQFLKQILDGVHYLHSKRIAHFDLKPENIMLLDKNVPNprIKLIDFGIA 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 8135 TRLDPNEVVKITTGTAEFAAPEIVNREPVGFYTDMWATGVLSYVLLSGLSPFAGDNDVQTLKNVKACDWDFDVESFKYIS 8214
Cdd:cd14195   160 HKIEAGNEFKNIFGTPEFVAPEIVNYEPLGLEADMWSIGVITYILLSGASPFLGETKQETLTNISAVNYDFDEEYFSNTS 239
                         250       260       270
                  ....*....|....*....|....*....|
gi 281359561 8215 EEAKDFIRKLLVRNKEKRMTAHECLLHPWL 8244
Cdd:cd14195   240 ELAKDFIRRLLVKDPKKRMTIAQSLEHSWI 269
STKc_Aurora cd14007
Catalytic domain of the Serine/Threonine kinase, Aurora kinase; STKs catalyze the transfer of ...
7989-8245 2.68e-74

Catalytic domain of the Serine/Threonine kinase, Aurora kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Aurora kinases are key regulators of mitosis and are essential for the accurate and equal division of genomic material from parent to daughter cells. Yeast contains only one Aurora kinase while most higher eukaryotes have two. Vertebrates contain at least 2 Aurora kinases (A and B); mammals contains a third Aurora kinase gene (C). Aurora-A regulates cell cycle events from the late S-phase through the M-phase including centrosome maturation, mitotic entry, centrosome separation, spindle assembly, chromosome alignment, cytokinesis, and mitotic exit. Aurora-A activation depends on its autophosphorylation and binding to the microtubule-associated protein TPX2. Aurora-B is most active at the transition during metaphase to the end of mitosis. It is critical for accurate chromosomal segregation, cytokinesis, protein localization to the centrosome and kinetochore, correct microtubule-kinetochore attachments, and regulation of the mitotic checkpoint. Aurora-C is mainly expressed in meiotically dividing cells; it was originally discovered in mice as a testis-specific STK called Aie1. Both Aurora-B and -C are chromosomal passenger proteins that can form complexes with INCENP and survivin, and they may have redundant cellular functions. The Aurora subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270909 [Multi-domain]  Cd Length: 253  Bit Score: 250.08  E-value: 2.68e-74
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 7989 YDILEEIGTGAFGVVHRCRERSTGNIFAAKFIP----VSHSVEKDLiRREIDIMNQLHHQKLINLHDAFEDDDEMILILE 8064
Cdd:cd14007     2 FEIGKPLGKGKFGNVYLAREKKSGFIVALKVISksqlQKSGLEHQL-RREIEIQSHLRHPNILRLYGYFEDKKRIYLILE 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 8065 FLSGGELFERITAEGyVMTEAEVINYMRQICEGIRHMHEQNIIHLDIKPENIMCQTRSstNVKLIDFGLATRLDPNevvK 8144
Cdd:cd14007    81 YAPNGELYKELKKQK-RFDEKEAAKYIYQLALALDYLHSKNIIHRDIKPENILLGSNG--ELKLADFGWSVHAPSN---R 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 8145 ITT--GTAEFAAPEIVNREPVGFYTDMWATGVLSYVLLSGLSPFAGDNDVQTLKNVKACDWDFDvesfKYISEEAKDFIR 8222
Cdd:cd14007   155 RKTfcGTLDYLPPEMVEGKEYDYKVDIWSLGVLCYELLVGKPPFESKSHQETYKRIQNVDIKFP----SSVSPEAKDLIS 230
                         250       260
                  ....*....|....*....|...
gi 281359561 8223 KLLVRNKEKRMTAHECLLHPWLT 8245
Cdd:cd14007   231 KLLQKDPSKRLSLEQVLNHPWIK 253
STKc_AMPK-like cd14003
Catalytic domain of AMP-activated protein kinase-like Serine/Threonine Kinases; STKs catalyze ...
7988-8243 2.11e-73

Catalytic domain of AMP-activated protein kinase-like Serine/Threonine Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The AMPK-like subfamily is composed of AMPK, MARK, BRSK, NUAK, MELK, SNRK, TSSK, and SIK, among others. LKB1 serves as a master upstream kinase that activates AMPK and most AMPK-like kinases. AMPK, also called SNF1 (sucrose non-fermenting1) in yeasts and SnRK1 (SNF1-related kinase1) in plants, is a heterotrimeric enzyme composed of a catalytic alpha subunit and two regulatory subunits, beta and gamma. It is a stress-activated kinase that serves as master regulator of glucose and lipid metabolism by monitoring carbon and energy supplies, via sensing the cell's AMP:ATP ratio. MARKs phosphorylate tau and related microtubule-associated proteins (MAPs), and regulates microtubule-based intracellular transport. They are involved in embryogenesis, epithelial cell polarization, cell signaling, and neuronal differentiation. BRSKs play important roles in establishing neuronal polarity. TSSK proteins are almost exclusively expressed postmeiotically in the testis and play important roles in spermatogenesis and/or spermiogenesis. The AMPK-like subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270905 [Multi-domain]  Cd Length: 252  Bit Score: 247.43  E-value: 2.11e-73
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 7988 RYDILEEIGTGAFGVVHRCRERSTGNIFAAKFIPVSHSVEKDL--IRREIDIMNQLHHQKLINLHDAFEDDDEMILILEF 8065
Cdd:cd14003     1 NYELGKTLGEGSFGKVKLARHKLTGEKVAIKIIDKSKLKEEIEekIKREIEIMKLLNHPNIIKLYEVIETENKIYLVMEY 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 8066 LSGGELFERITAEGYvMTEAEVINYMRQICEGIRHMHEQNIIHLDIKPENIMCQtrSSTNVKLIDFGLATRLDPNEVVKI 8145
Cdd:cd14003    81 ASGGELFDYIVNNGR-LSEDEARRFFQQLISAVDYCHSNGIVHRDLKLENILLD--KNGNLKIIDFGLSNEFRGGSLLKT 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 8146 TTGTAEFAAPEIVNREPV-GFYTDMWATGVLSYVLLSGLSPFAGDNDVQTLKNVKACdwDFDVESfkYISEEAKDFIRKL 8224
Cdd:cd14003   158 FCGTPAYAAPEVLLGRKYdGPKADVWSLGVILYAMLTGYLPFDDDNDSKLFRKILKG--KYPIPS--HLSPDARDLIRRM 233
                         250
                  ....*....|....*....
gi 281359561 8225 LVRNKEKRMTAHECLLHPW 8243
Cdd:cd14003   234 LVVDPSKRITIEEILNHPW 252
STKc_SPEG_rpt1 cd14108
Catalytic kinase domain, first repeat, of Giant Serine/Threonine Kinase Striated muscle ...
7987-8244 4.57e-73

Catalytic kinase domain, first repeat, of Giant Serine/Threonine Kinase Striated muscle preferentially expressed protein kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The Striated muscle preferentially expressed gene (SPEG) generates 4 different isoforms through alternative promoter use and splicing in a tissue-specific manner: SPEGalpha and SPEGbeta are expressed in cardiac and skeletal striated muscle; Aortic Preferentially Expressed Protein-1 (APEG-1) is expressed in vascular smooth muscle; and Brain preferentially expressed gene (BPEG) is found in the brain and aorta. SPEG proteins have mutliple immunoglobulin (Ig), 2 fibronectin type III (FN3), and two kinase domains. They are necessary for cardiac development and survival. The SPEG subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271010 [Multi-domain]  Cd Length: 255  Bit Score: 246.74  E-value: 4.57e-73
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 7987 DRYDILEEIGTGAFGVVHRCRERSTGNIFAAKFIPvSHSVEKDLIRREIDIMNQLHHQKLINLHDAFEDDDEMILILEfL 8066
Cdd:cd14108     2 DYYDIHKEIGRGAFSYLRRVKEKSSDLSFAAKFIP-VRAKKKTSARRELALLAELDHKSIVRFHDAFEKRRVVIIVTE-L 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 8067 SGGELFERITAEGYVMtEAEVINYMRQICEGIRHMHEQNIIHLDIKPENIMCQTRSSTNVKLIDFGLATRLDPNEVVKIT 8146
Cdd:cd14108    80 CHEELLERITKRPTVC-ESEVRSYMRQLLEGIEYLHQNDVLHLDLKPENLLMADQKTDQVRICDFGNAQELTPNEPQYCK 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 8147 TGTAEFAAPEIVNREPVGFYTDMWATGVLSYVLLSGLSPFAGDNDVQTLKNVKACDWDFDVESFKYISEEAKDFIRKLLV 8226
Cdd:cd14108   159 YGTPEFVAPEIVNQSPVSKVTDIWPVGVIAYLCLTGISPFVGENDRTTLMNIRNYNVAFEESMFKDLCREAKGFIIKVLV 238
                         250
                  ....*....|....*...
gi 281359561 8227 RNKeKRMTAHECLLHPWL 8244
Cdd:cd14108   239 SDR-LRPDAEETLEHPWF 255
PK_Unc-89_rpt1 cd14109
Pseudokinase domain, first repeat, of the Giant Serine/Threonine Kinase Uncoordinated protein ...
7985-8244 9.30e-72

Pseudokinase domain, first repeat, of the Giant Serine/Threonine Kinase Uncoordinated protein 89; The pseudokinase domain shows similarity to protein kinases but lacks crucial residues for catalytic activity. The nematode Unc-89 gene, through alternative promoter use and splicing, encodes at least six major isoforms (Unc-89A to Unc-89F) of giant muscle proteins that are homologs for the vetebrate obscurin. In flies, five isoforms of Unc-89 have been detected: four in the muscles of adult flies (two in the indirect flight muscle and two in other muscles) and another isoform in the larva. Unc-89 in nematodes is required for normal muscle cell architecture. In flies, it is necessary for the development of a symmetrical sarcomere in the flight muscles. Unc-89 proteins contain several adhesion and signaling domains including multiple copies of the immunoglobulin (Ig) domain, as well as fibronectin type III (FN3), SH3, RhoGEF, and PH domains. The nematode Unc-89 isoforms D, C, D, and F contain two kinase domain with B and F having two complete kinase domains while the first repeat of C and D are partial domains. Homology modeling suggests that the first kinase repeat of Unc-89 may be catalytically inactive, a pseudokinase, while the second kinase repeat may be active. The pseudokinase domain may function as a regulatory domain or a protein interaction domain. The Unc-89 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271011 [Multi-domain]  Cd Length: 255  Bit Score: 242.80  E-value: 9.30e-72
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 7985 VYDRYDILEE-IGTGAFGVVHRCRERSTGNIFAAKFIPVShsvekDLIRREIDIMNQLHHQKLINLHDAFEDDD-EMILI 8062
Cdd:cd14109     1 VRELYEIGEEdEKRAAQGAPFHVTERSTGRNFLAQLRYGD-----PFLMREVDIHNSLDHPNIVQMHDAYDDEKlAVTVI 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 8063 LEFLSGGELFERITAEGY-VMTEAEVINYMRQICEGIRHMHEQNIIHLDIKPENIMCQtrsSTNVKLIDFGLATRLDPNE 8141
Cdd:cd14109    76 DNLASTIELVRDNLLPGKdYYTERQVAVFVRQLLLALKHMHDLGIAHLDLRPEDILLQ---DDKLKLADFGQSRRLLRGK 152
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 8142 VVKITTGTAEFAAPEIVNREPVGFYTDMWATGVLSYVLLSGLSPFAGDNDVQTLKNVKACDWDFDVESFKYISEEAKDFI 8221
Cdd:cd14109   153 LTTLIYGSPEFVSPEIVNSYPVTLATDMWSVGVLTYVLLGGISPFLGDNDRETLTNVRSGKWSFDSSPLGNISDDARDFI 232
                         250       260
                  ....*....|....*....|...
gi 281359561 8222 RKLLVRNKEKRMTAHECLLHPWL 8244
Cdd:cd14109   233 KKLLVYIPESRLTVDEALNHPWF 255
STKc_DRAK2 cd14198
The catalytic domain of the Serine/Threonine Kinase, Death-associated protein kinase-Related ...
7993-8244 5.09e-70

The catalytic domain of the Serine/Threonine Kinase, Death-associated protein kinase-Related Apoptosis-inducing protein Kinase 2; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. DRAKs were named based on their similarity (around 50% identity) to the kinase domain of DAPKs. They contain an N-terminal kinase domain and a C-terminal regulatory domain. Vertebrates contain two subfamily members, DRAK1 and DRAK2 (also called STK17B). Both DRAKs are localized to the nucleus, autophosphorylate themselves, and phosphorylate myosin light chain as a substrate. DRAK2 has been implicated in inducing or enhancing apoptosis in beta cells, fibroblasts, and lymphoid cells, where it is highly expressed. It is involved in regulating many immune processes including the germinal center (GC) reaction, responses to thymus-dependent antigens, activated T cell survival, memory T cell responses. It may be involved in the development of autoimmunity. The DRAK2 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271100 [Multi-domain]  Cd Length: 270  Bit Score: 238.67  E-value: 5.09e-70
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 7993 EEIGTGAFGVVHRCRERSTGNIFAAKFIPVShsvekdliRREIDIMNQLHHQ-----------KLINLHDAFEDDDEMIL 8061
Cdd:cd14198    14 KELGRGKFAVVRQCISKSTGQEYAAKFLKKR--------RRGQDCRAEILHEiavlelaksnpRVVNLHEVYETTSEIIL 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 8062 ILEFLSGGELFER-ITAEGYVMTEAEVINYMRQICEGIRHMHEQNIIHLDIKPENIMCQTRSST-NVKLIDFGLATRLDP 8139
Cdd:cd14198    86 ILEYAAGGEIFNLcVPDLAEMVSENDIIRLIRQILEGVYYLHQNNIVHLDLKPQNILLSSIYPLgDIKIVDFGMSRKIGH 165
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 8140 NEVVKITTGTAEFAAPEIVNREPVGFYTDMWATGVLSYVLLSGLSPFAGDNDVQTLKNVKACDWDFDVESFKYISEEAKD 8219
Cdd:cd14198   166 ACELREIMGTPEYLAPEILNYDPITTATDMWNIGVIAYMLLTHESPFVGEDNQETFLNISQVNVDYSEETFSSVSQLATD 245
                         250       260
                  ....*....|....*....|....*
gi 281359561 8220 FIRKLLVRNKEKRMTAHECLLHPWL 8244
Cdd:cd14198   246 FIQKLLVKNPEKRPTAEICLSHSWL 270
STKc_obscurin_rpt1 cd14107
Catalytic kinase domain, first repeat, of the Giant Serine/Threonine Kinase Obscurin; STKs ...
7989-8244 7.35e-68

Catalytic kinase domain, first repeat, of the Giant Serine/Threonine Kinase Obscurin; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Obscurin, approximately 800 kDa in size, is one of three giant proteins expressed in vetebrate striated muscle, together with titin and nebulin. It is a multidomain protein composed of tandem adhesion and signaling domains, including 49 immunoglobulin (Ig) and 2 fibronectin type III (FN3) domains at the N-terminus followed by a more complex region containing more Ig domains, a conserved SH3 domain near a RhoGEF and PH domains, non-modular regions, as well as IQ and phosphorylation motifs. The obscurin gene also encode two kinase domains, which are not expressed as part of the 800 kDa protein, but as a smaller, alternatively spliced product present mainly in the heart muscle, also called obscurin-MLCK. Obscurin is localized at the peripheries of Z-disks and M-lines, where it is able to communicate with the surrounding myoplasm. It interacts with diverse proteins including sAnk1, myosin, titin, and MyBP-C. It may act as a scaffold for the assembly of elements of the contractile apparatus. The obscurin subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271009 [Multi-domain]  Cd Length: 257  Bit Score: 231.70  E-value: 7.35e-68
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 7989 YDILEEIGTGAFGVVHRCRERSTGNIFAAKFIPVsHSVEKDLIRREIDIMNQLHHQKLINLHDAFEDDDEMILILEFLSG 8068
Cdd:cd14107     4 YEVKEEIGRGTFGFVKRVTHKGNGECCAAKFIPL-RSSTRARAFQERDILARLSHRRLTCLLDQFETRKTLILILELCSS 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 8069 GELFERITAEGyVMTEAEVINYMRQICEGIRHMHEQNIIHLDIKPENIMCQTRSSTNVKLIDFGLATRLDPNEVVKITTG 8148
Cdd:cd14107    83 EELLDRLFLKG-VVTEAEVKLYIQQVLEGIGYLHGMNILHLDIKPDNILMVSPTREDIKICDFGFAQEITPSEHQFSKYG 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 8149 TAEFAAPEIVNREPVGFYTDMWATGVLSYVLLSGLSPFAGDNDVQTLKNVKACDWDFDVESFKYISEEAKDFIRKLLVRN 8228
Cdd:cd14107   162 SPEFVAPEIVHQEPVSAATDIWALGVIAYLSLTCHSPFAGENDRATLLNVAEGVVSWDTPEITHLSEDAKDFIKRVLQPD 241
                         250
                  ....*....|....*.
gi 281359561 8229 KEKRMTAHECLLHPWL 8244
Cdd:cd14107   242 PEKRPSASECLSHEWF 257
STKc_DRAK1 cd14197
Catalytic domain of the Serine/Threonine Kinase, Death-associated protein kinase-Related ...
7987-8244 8.69e-67

Catalytic domain of the Serine/Threonine Kinase, Death-associated protein kinase-Related Apoptosis-inducing protein Kinase 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. DRAKs were named based on their similarity (around 50% identity) to the kinase domain of DAPKs. They contain an N-terminal kinase domain and a C-terminal regulatory domain. Vertebrates contain two subfamily members, DRAK1 (also called STK17A) and DRAK2. Both DRAKs are localized to the nucleus, autophosphorylate themselves, and phosphorylate myosin light chain as a substrate. Rabbit DRAK1 has been shown to induce apoptosis in osteoclasts and overexpressio of human DRAK1 induces apoptosis in cultured fibroblast cells. DRAK1 may be involved in apoptotic signaling. The DRAK1 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271099 [Multi-domain]  Cd Length: 271  Bit Score: 229.44  E-value: 8.69e-67
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 7987 DRYDIL--EEIGTGAFGVVHRCRERSTGNIFAAKFIPVSHSVE--KDLIRREIDIMNQLH-HQKLINLHDAFEDDDEMIL 8061
Cdd:cd14197     7 ERYSLSpgRELGRGKFAVVRKCVEKDSGKEFAAKFMRKRRKGQdcRMEIIHEIAVLELAQaNPWVINLHEVYETASEMIL 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 8062 ILEFLSGGELFERITAE-GYVMTEAEVINYMRQICEGIRHMHEQNIIHLDIKPENIMCQTRSST-NVKLIDFGLATRLDP 8139
Cdd:cd14197    87 VLEYAAGGEIFNQCVADrEEAFKEKDVKRLMKQILEGVSFLHNNNVVHLDLKPQNILLTSESPLgDIKIVDFGLSRILKN 166
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 8140 NEVVKITTGTAEFAAPEIVNREPVGFYTDMWATGVLSYVLLSGLSPFAGDNDVQTLKNVKACDWDFDVESFKYISEEAKD 8219
Cdd:cd14197   167 SEELREIMGTPEYVAPEILSYEPISTATDMWSIGVLAYVMLTGISPFLGDDKQETFLNISQMNVSYSEEEFEHLSESAID 246
                         250       260
                  ....*....|....*....|....*
gi 281359561 8220 FIRKLLVRNKEKRMTAHECLLHPWL 8244
Cdd:cd14197   247 FIKTLLIKKPENRATAEDCLKHPWL 271
STKc_DCKL cd14095
Catalytic domain of the Serine/Threonine Kinase, Doublecortin-like kinase (also called ...
7988-8243 1.85e-62

Catalytic domain of the Serine/Threonine Kinase, Doublecortin-like kinase (also called Doublecortin-like and CAM kinase-like); STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. DCKL (or DCAMKL) proteins belong to the doublecortin (DCX) family of proteins which are involved in neuronal migration, neurogenesis, and eye receptor development, among others. Family members typically contain tandem doublecortin (DCX) domains at the N-terminus; DCX domains can bind microtubules and serve as protein-interaction platforms. In addition, DCKL proteins contain a C-terminal kinase domain with similarity to CAMKs. They are involved in the regulation of cAMP signaling. Vertebrates contain three DCKL proteins (DCKL1-3); DCKL1 and 2 also contain a serine, threonine, and proline rich domain (SP), while DCKL3 contains only a single DCX domain instead of tandem domains. The DCKL subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270997 [Multi-domain]  Cd Length: 258  Bit Score: 216.42  E-value: 1.85e-62
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 7988 RYDILEEIGTGAFGVVHRCRERSTGNIFAAKFIPVSHSVEK-DLIRREIDIMNQLHHQKLINLHDAFEDDDEMILILEFL 8066
Cdd:cd14095     1 KYDIGRVIGDGNFAVVKECRDKATDKEYALKIIDKAKCKGKeHMIENEVAILRRVKHPNIVQLIEEYDTDTELYLVMELV 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 8067 SGGELFERITAEGYVmTEAEVINYMRQICEGIRHMHEQNIIHLDIKPENIMCQTRS--STNVKLIDFGLATRLDpnEVVK 8144
Cdd:cd14095    81 KGGDLFDAITSSTKF-TERDASRMVTDLAQALKYLHSLSIVHRDIKPENLLVVEHEdgSKSLKLADFGLATEVK--EPLF 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 8145 ITTGTAEFAAPEIVNREPVGFYTDMWATGVLSYVLLSGLSPFAGDNDVQT--LKNVKACDWDFDVESFKYISEEAKDFIR 8222
Cdd:cd14095   158 TVCGTPTYVAPEILAETGYGLKVDIWAAGVITYILLCGFPPFRSPDRDQEelFDLILAGEFEFLSPYWDNISDSAKDLIS 237
                         250       260
                  ....*....|....*....|.
gi 281359561 8223 KLLVRNKEKRMTAHECLLHPW 8243
Cdd:cd14095   238 RMLVVDPEKRYSAGQVLDHPW 258
STKc_CaMKII cd14086
Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase ...
7987-8244 2.06e-62

Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase Type II; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. CaMKs are multifunctional calcium and calmodulin (CaM) stimulated STKs involved in cell cycle regulation. There are several types of CaMKs including CaMKI, CaMKII, and CaMKIV. CaMKs contain an N-terminal catalytic domain followed by a regulatory domain that harbors a CaM binding site. In addition, CaMKII contains a C-terminal association domain that facilitates oligomerization. There are four CaMKII proteins (alpha, beta, gamma, delta) encoded by different genes; each gene undergoes alternative splicing to produce more than 30 isoforms. CaMKII-alpha and -beta are enriched in neurons while CaMKII-gamma and -delta are predominant in myocardium. CaMKII is a signaling molecule that translates upstream calcium and reactive oxygen species (ROS) signals into downstream responses that play important roles in synaptic function and cardiovascular physiology. It is a major component of the postsynaptic density and is critical in regulating synaptic plasticity including long-term potentiation. It is critical in regulating ion channels and proteins involved in myocardial excitation-contraction and excitation-transcription coupling. Excessive CaMKII activity promotes processes that contribute to heart failure and arrhythmias. The CaMKII subfamily is part of a larger superfamily that includes the catalytic domains of other protein kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270988 [Multi-domain]  Cd Length: 292  Bit Score: 217.67  E-value: 2.06e-62
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 7987 DRYDILEEIGTGAFGVVHRCRERSTGNIFAAKFIPVSHSVEKDL--IRREIDIMNQLHHQKLINLHDAFEDDDEMILILE 8064
Cdd:cd14086     1 DEYDLKEELGKGAFSVVRRCVQKSTGQEFAAKIINTKKLSARDHqkLEREARICRLLKHPNIVRLHDSISEEGFHYLVFD 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 8065 FLSGGELFERITAEGYvMTEAEVINYMRQICEGIRHMHEQNIIHLDIKPENIMCQTRS-STNVKLIDFGLATRLDPNEVV 8143
Cdd:cd14086    81 LVTGGELFEDIVAREF-YSEADASHCIQQILESVNHCHQNGIVHRDLKPENLLLASKSkGAAVKLADFGLAIEVQGDQQA 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 8144 KIT-TGTAEFAAPEIVNREPVGFYTDMWATGVLSYVLLSGLSPFAGDNDVQTLKNVKACDWDFDVESFKYISEEAKDFIR 8222
Cdd:cd14086   160 WFGfAGTPGYLSPEVLRKDPYGKPVDIWACGVILYILLVGYPPFWDEDQHRLYAQIKAGAYDYPSPEWDTVTPEAKDLIN 239
                         250       260
                  ....*....|....*....|..
gi 281359561 8223 KLLVRNKEKRMTAHECLLHPWL 8244
Cdd:cd14086   240 QMLTVNPAKRITAAEALKHPWI 261
Pkinase pfam00069
Protein kinase domain;
7989-8244 6.14e-61

Protein kinase domain;


Pssm-ID: 459660 [Multi-domain]  Cd Length: 217  Bit Score: 210.18  E-value: 6.14e-61
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561  7989 YDILEEIGTGAFGVVHRCRERSTGNIFAAKFIPVSH--SVEKDLIRREIDIMNQLHHQKLINLHDAFEDDDEMILILEFL 8066
Cdd:pfam00069    1 YEVLRKLGSGSFGTVYKAKHRDTGKIVAIKKIKKEKikKKKDKNILREIKILKKLNHPNIVRLYDAFEDKDNLYLVLEYV 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561  8067 SGGELFERITAEGYvMTEAEVINYMRQICEgirhmheqniihldikpenimcqtrsstnvklidfGLATRLDPNEVVkit 8146
Cdd:pfam00069   81 EGGSLFDLLSEKGA-FSEREAKFIMKQILE-----------------------------------GLESGSSLTTFV--- 121
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561  8147 tGTAEFAAPEIVNREPVGFYTDMWATGVLSYVLLSGLSPFAGDNDVQTLKNVKACDWDFDVEsFKYISEEAKDFIRKLLV 8226
Cdd:pfam00069  122 -GTPWYMAPEVLGGNPYGPKVDVWSLGCILYELLTGKPPFPGINGNEIYELIIDQPYAFPEL-PSNLSEEAKDLLKKLLK 199
                          250
                   ....*....|....*...
gi 281359561  8227 RNKEKRMTAHECLLHPWL 8244
Cdd:pfam00069  200 KDPSKRLTATQALQHPWF 217
PKc cd00180
Catalytic domain of Protein Kinases; PKs catalyze the transfer of the gamma-phosphoryl group ...
7995-8242 4.55e-60

Catalytic domain of Protein Kinases; PKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine or tyrosine residues on protein substrates. PKs make up a large family of serine/threonine kinases (STKs), protein tyrosine kinases (PTKs), and dual-specificity PKs that phosphorylate both serine/threonine and tyrosine residues of target proteins. Majority of protein phosphorylation occurs on serine residues while only 1% occurs on tyrosine residues. Protein phosphorylation is a mechanism by which a wide variety of cellular proteins, such as enzymes and membrane channels, are reversibly regulated in response to certain stimuli. PKs often function as components of signal transduction pathways in which one kinase activates a second kinase, which in turn, may act on other kinases; this sequential action transmits a signal from the cell surface to target proteins, which results in cellular responses. The PK family is one of the largest known protein families with more than 100 homologous yeast enzymes and more than 500 human proteins. A fraction of PK family members are pseudokinases that lack crucial residues for catalytic activity. The mutiplicity of kinases allows for specific regulation according to substrate, tissue distribution, and cellular localization. PKs regulate many cellular processes including proliferation, division, differentiation, motility, survival, metabolism, cell-cycle progression, cytoskeletal rearrangement, immunity, and neuronal functions. Many kinases are implicated in the development of various human diseases including different types of cancer. The PK family is part of a larger superfamily that includes the catalytic domains of RIO kinases, aminoglycoside phosphotransferase, choline kinase, phosphoinositide 3-kinase (PI3K), and actin-fragmin kinase.


Pssm-ID: 270622 [Multi-domain]  Cd Length: 215  Bit Score: 207.89  E-value: 4.55e-60
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 7995 IGTGAFGVVHRCRERSTGNIFAAKFIPVS-HSVEKDLIRREIDIMNQLHHQKLINLHDAFEDDDEMILILEFLSGGELFE 8073
Cdd:cd00180     1 LGKGSFGKVYKARDKETGKKVAVKVIPKEkLKKLLEELLREIEILKKLNHPNIVKLYDVFETENFLYLVMEYCEGGSLKD 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 8074 RITAEGYVMTEAEVINYMRQICEGIRHMHEQNIIHLDIKPENIMCqtRSSTNVKLIDFGLATRLDPNE---VVKITTGTA 8150
Cdd:cd00180    81 LLKENKGPLSEEEALSILRQLLSALEYLHSNGIIHRDLKPENILL--DSDGTVKLADFGLAKDLDSDDsllKTTGGTTPP 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 8151 EFAAPEIVNREPVGFYTDMWATGVLSYVLlsglspfagdndvqtlknvkacdwdfdvesfkyisEEAKDFIRKLLVRNKE 8230
Cdd:cd00180   159 YYAPPELLGGRYYGPKVDIWSLGVILYEL-----------------------------------EELKDLIRRMLQYDPK 203
                         250
                  ....*....|..
gi 281359561 8231 KRMTAHECLLHP 8242
Cdd:cd00180   204 KRPSAKELLEHL 215
STKc_CaMKIV cd14085
Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase ...
7987-8250 1.07e-59

Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase Type IV; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. CaMKs are multifunctional calcium and calmodulin (CaM) stimulated STKs involved in cell cycle regulation. There are several types of CaMKs including CaMKI, CaMKII, and CaMKIV. CaMKs contain an N-terminal catalytic domain and a C-terminal regulatory domain that harbors a CaM binding site. CaMKIV is found predominantly in neurons and immune cells. It is activated by the binding of calcium/CaM and phosphorylation by CaMKK (alpha or beta). The CaMKK-CaMKIV cascade participates in regulating several transcription factors like CREB, MEF2, and retinoid orphan receptors. It also is implicated in T-cell development and signaling, cytokine secretion, and signaling through Toll-like receptors, and is thus, pivotal in immune response and inflammation. The CaMKIV subfamily is part of a larger superfamily that includes the catalytic domains of other protein kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270987 [Multi-domain]  Cd Length: 294  Bit Score: 209.68  E-value: 1.07e-59
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 7987 DRYDILEEIGTGAFGVVHRCRERSTGNIFAAKFipVSHSVEKDLIRREIDIMNQLHHQKLINLHDAFEDDDEMILILEFL 8066
Cdd:cd14085     3 DFFEIESELGRGATSVVYRCRQKGTQKPYAVKK--LKKTVDKKIVRTEIGVLLRLSHPNIIKLKEIFETPTEISLVLELV 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 8067 SGGELFERITAEGYvMTEAEVINYMRQICEGIRHMHEQNIIHLDIKPENIMCQT-RSSTNVKLIDFGLATRLDPNEVVKI 8145
Cdd:cd14085    81 TGGELFDRIVEKGY-YSERDAADAVKQILEAVAYLHENGIVHRDLKPENLLYATpAPDAPLKIADFGLSKIVDQQVTMKT 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 8146 TTGTAEFAAPEIVNREPVGFYTDMWATGVLSYVLLSGLSPFAGDN-DVQTLKNVKACDWDFDVESFKYISEEAKDFIRKL 8224
Cdd:cd14085   160 VCGTPGYCAPEILRGCAYGPEVDMWSVGVITYILLCGFEPFYDERgDQYMFKRILNCDYDFVSPWWDDVSLNAKDLVKKL 239
                         250       260
                  ....*....|....*....|....*.
gi 281359561 8225 LVRNKEKRMTAHECLLHPWLTGDHSA 8250
Cdd:cd14085   240 IVLDPKKRLTTQQALQHPWVTGKAAN 265
STKc_PhKG cd14093
Catalytic domain of the Serine/Threonine Kinase, Phosphorylase kinase Gamma subunit; STKs ...
7986-8244 7.42e-59

Catalytic domain of the Serine/Threonine Kinase, Phosphorylase kinase Gamma subunit; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Phosphorylase kinase (PhK) catalyzes the phosphorylation of inactive phosphorylase b to form the active phosphorylase a. It coordinates hormonal, metabolic, and neuronal signals to initiate the breakdown of glycogen stores, which enables the maintenance of blood-glucose homeostasis during fasting, and is also used as a source of energy for muscle contraction. PhK is one of the largest and most complex protein kinases, composed of a heterotetramer containing four molecules each of four subunit types: one catalytic (gamma) and three regulatory (alpha, beta, and delta). Each subunit has tissue-specific isoforms or splice variants. Vertebrates contain two isoforms of the gamma subunit (gamma 1 and gamma 2). The gamma subunit, when isolated, is constitutively active and does not require phosphorylation of the A-loop for activity. The regulatory subunits restrain this kinase activity until signals are received to relieve this inhibition. For example, the kinase is activated in response to hormonal stimulation, after autophosphorylation or phosphorylation by cAMP-dependent kinase of the alpha and beta subunits. The high-affinity binding of ADP to the beta subunit also stimulates kinase activity, whereas calcium relieves inhibition by binding to the delta (calmodulin) subunit. The PhKG subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270995 [Multi-domain]  Cd Length: 272  Bit Score: 206.44  E-value: 7.42e-59
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 7986 YDRYDILEEIGTGAFGVVHRCRERSTGNIFAAKFIPVS---HSVE-----KDLIRREIDIMNQLH-HQKLINLHDAFEDD 8056
Cdd:cd14093     2 YAKYEPKEILGRGVSSTVRRCIEKETGQEFAVKIIDITgekSSENeaeelREATRREIEILRQVSgHPNIIELHDVFESP 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 8057 DEMILILEFLSGGELFERITaEGYVMTEAEVINYMRQICEGIRHMHEQNIIHLDIKPENIMCQtrSSTNVKLIDFGLATR 8136
Cdd:cd14093    82 TFIFLVFELCRKGELFDYLT-EVVTLSEKKTRRIMRQLFEAVEFLHSLNIVHRDLKPENILLD--DNLNVKISDFGFATR 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 8137 LDPNEVVKITTGTAEFAAPEIV------NREPVGFYTDMWATGVLSYVLLSGLSPFAGDNDVQTLKNVKACDWDFDVESF 8210
Cdd:cd14093   159 LDEGEKLRELCGTPGYLAPEVLkcsmydNAPGYGKEVDMWACGVIMYTLLAGCPPFWHRKQMVMLRNIMEGKYEFGSPEW 238
                         250       260       270
                  ....*....|....*....|....*....|....
gi 281359561 8211 KYISEEAKDFIRKLLVRNKEKRMTAHECLLHPWL 8244
Cdd:cd14093   239 DDISDTAKDLISKLLVVDPKKRLTAEEALEHPFF 272
STKc_CaMKI_gamma cd14166
Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase ...
7989-8271 2.14e-58

Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase Type I gamma; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. CaMKs are multifunctional calcium and calmodulin (CaM) stimulated STKs involved in cell cycle regulation. The CaMK family includes CaMKI, CaMKII, CaMKIV, and CaMK kinase (CaMKK). In vertebrates, there are four CaMKI proteins encoded by different genes (alpha, beta, gamma, and delta), each producing at least one variant. CaMKs contain an N-terminal catalytic domain and a C-terminal regulatory domain that harbors a CaM binding site. CaMKI proteins are monomeric and they play pivotal roles in the nervous system, including long-term potentiation, dendritic arborization, neurite outgrowth, and the formation of spines, synapses, and axons. In addition, they may be involved in osteoclast differentiation and bone resorption. The CaMKI-gamma subfamily is part of a larger superfamily that includes the catalytic domains of other protein kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271068 [Multi-domain]  Cd Length: 285  Bit Score: 205.61  E-value: 2.14e-58
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 7989 YDILEEIGTGAFGVVHRCRERSTGNIFAAKFIPVSHSVEKDLIRREIDIMNQLHHQKLINLHDAFEDDDEMILILEFLSG 8068
Cdd:cd14166     5 FIFMEVLGSGAFSEVYLVKQRSTGKLYALKCIKKSPLSRDSSLENEIAVLKRIKHENIVTLEDIYESTTHYYLVMQLVSG 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 8069 GELFERITAEGyVMTEAEVINYMRQICEGIRHMHEQNIIHLDIKPENIMCQT-RSSTNVKLIDFGLaTRLDPNEVVKITT 8147
Cdd:cd14166    85 GELFDRILERG-VYTEKDASRVINQVLSAVKYLHENGIVHRDLKPENLLYLTpDENSKIMITDFGL-SKMEQNGIMSTAC 162
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 8148 GTAEFAAPEIVNREPVGFYTDMWATGVLSYVLLSGLSPFAGDNDVQTLKNVKACDWDFDVESFKYISEEAKDFIRKLLVR 8227
Cdd:cd14166   163 GTPGYVAPEVLAQKPYSKAVDCWSIGVITYILLCGYPPFYEETESRLFEKIKEGYYEFESPFWDDISESAKDFIRHLLEK 242
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....
gi 281359561 8228 NKEKRMTAHECLLHPWLTGDHSamkqeINRDRYLAYREKLRRKY 8271
Cdd:cd14166   243 NPSKRYTCEKALSHPWIIGNTA-----LHRDIYPSVSEQIQKNF 281
STKc_AGC cd05123
Catalytic domain of AGC family Serine/Threonine Kinases; STKs catalyze the transfer of the ...
7995-8243 4.67e-58

Catalytic domain of AGC family Serine/Threonine Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. AGC kinases regulate many cellular processes including division, growth, survival, metabolism, motility, and differentiation. Many are implicated in the development of various human diseases. Members of this family include cAMP-dependent Protein Kinase (PKA), cGMP-dependent Protein Kinase (PKG), Protein Kinase C (PKC), Protein Kinase B (PKB), G protein-coupled Receptor Kinase (GRK), Serum- and Glucocorticoid-induced Kinase (SGK), and 70 kDa ribosomal Protein S6 Kinase (p70S6K or S6K), among others. AGC kinases share an activation mechanism based on the phosphorylation of up to three sites: the activation loop (A-loop), the hydrophobic motif (HM) and the turn motif. Phosphorylation at the A-loop is required of most AGC kinases, which results in a disorder-to-order transition of the A-loop. The ordered conformation results in the access of substrates and ATP to the active site. A subset of AGC kinases with C-terminal extensions containing the HM also requires phosphorylation at this site. Phosphorylation at the HM allows the C-terminal extension to form an ordered structure that packs into the hydrophobic pocket of the catalytic domain, which then reconfigures the kinase into an active bi-lobed state. In addition, growth factor-activated AGC kinases such as PKB, p70S6K, RSK, MSK, PKC, and SGK, require phosphorylation at the turn motif (also called tail or zipper site), located N-terminal to the HM at the C-terminal extension. The AGC family is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and Phosphoinositide 3-Kinase.


Pssm-ID: 270693 [Multi-domain]  Cd Length: 250  Bit Score: 203.52  E-value: 4.67e-58
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 7995 IGTGAFGVVHRCRERSTGNIFAAKFIPVSHSVEKDLIRR---EIDIMNQLHHQKLINLHDAFEDDDEMILILEFLSGGEL 8071
Cdd:cd05123     1 LGKGSFGKVLLVRKKDTGKLYAMKVLRKKEIIKRKEVEHtlnERNILERVNHPFIVKLHYAFQTEEKLYLVLDYVPGGEL 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 8072 FERITAEGYvMTEAEVINYMRQICEGIRHMHEQNIIHLDIKPENIMCQtrSSTNVKLIDFGLATRLdPNEVVKITT--GT 8149
Cdd:cd05123    81 FSHLSKEGR-FPEERARFYAAEIVLALEYLHSLGIIYRDLKPENILLD--SDGHIKLTDFGLAKEL-SSDGDRTYTfcGT 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 8150 AEFAAPEIVNREPVGFYTDMWATGVLSYVLLSGLSPFAGDNDVQTLKNVKACDWDFDvesfKYISEEAKDFIRKLLVRNK 8229
Cdd:cd05123   157 PEYLAPEVLLGKGYGKAVDWWSLGVLLYEMLTGKPPFYAENRKEIYEKILKSPLKFP----EYVSPEAKSLISGLLQKDP 232
                         250
                  ....*....|....*..
gi 281359561 8230 EKRMTAH--ECLL-HPW 8243
Cdd:cd05123   233 TKRLGSGgaEEIKaHPF 249
STKc_CaMKI cd14083
Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase ...
7985-8243 5.11e-58

Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase Type I; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. CaMKs are multifunctional calcium and calmodulin (CaM) stimulated STKs involved in cell cycle regulation. There are several types of CaMKs including CaMKI, CaMKII, and CaMKIV. In vertebrates, there are four CaMKI proteins encoded by different genes (alpha, beta, gamma, and delta), each producing at least one variant. CaMKs contain an N-terminal catalytic domain and a C-terminal regulatory domain that harbors a CaM binding site. CaMKI proteins are monomeric and they play pivotal roles in the nervous system, including long-term potentiation, dendritic arborization, neurite outgrowth, and the formation of spines, synapses, and axons. In addition, they may be involved in osteoclast differentiation and bone resorption. The CaMKI subfamily is part of a larger superfamily that includes the catalytic domains of other protein kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270985 [Multi-domain]  Cd Length: 259  Bit Score: 203.76  E-value: 5.11e-58
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 7985 VYDRYDILEEIGTGAFGVVHRCRERSTGNIFAAKFIPVSH-SVEKDLIRREIDIMNQLHHQKLINLHDAFEDDDEMILIL 8063
Cdd:cd14083     1 IRDKYEFKEVLGTGAFSEVVLAEDKATGKLVAIKCIDKKAlKGKEDSLENEIAVLRKIKHPNIVQLLDIYESKSHLYLVM 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 8064 EFLSGGELFERITAEGyVMTEAEVINYMRQICEGIRHMHEQNIIHLDIKPENIM-CQTRSSTNVKLIDFGLaTRLDPNEV 8142
Cdd:cd14083    81 ELVTGGELFDRIVEKG-SYTEKDASHLIRQVLEAVDYLHSLGIVHRDLKPENLLyYSPDEDSKIMISDFGL-SKMEDSGV 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 8143 VKITTGTAEFAAPEIVNREPVGFYTDMWATGVLSYVLLSGLSPFAGDNDVQTLKNVKACDWDFDVESFKYISEEAKDFIR 8222
Cdd:cd14083   159 MSTACGTPGYVAPEVLAQKPYGKAVDCWSIGVISYILLCGYPPFYDENDSKLFAQILKAEYEFDSPYWDDISDSAKDFIR 238
                         250       260
                  ....*....|....*....|.
gi 281359561 8223 KLLVRNKEKRMTAHECLLHPW 8243
Cdd:cd14083   239 HLMEKDPNKRYTCEQALEHPW 259
STKc_Rad53_Cds1 cd14098
Catalytic domain of the yeast Serine/Threonine Kinases, Rad53 and Cds1; STKs catalyze the ...
7988-8243 5.92e-58

Catalytic domain of the yeast Serine/Threonine Kinases, Rad53 and Cds1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Rad53 and Cds1 are the checkpoint kinase 2 (Chk2) homologs found in budding and fission yeast, respectively. They play a central role in the cell's response to DNA lesions to prevent genome rearrangements and maintain genome integrity. They are phosphorylated in response to DNA damage and incomplete replication, and are essential for checkpoint control. They help promote DNA repair by stalling the cell cycle prior to mitosis in the presence of DNA damage. The Rad53/Cds1 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271000 [Multi-domain]  Cd Length: 265  Bit Score: 203.86  E-value: 5.92e-58
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 7988 RYDILEEIGTGAFGVVHRCRERSTGNIFAAKFIpVSHSVEK-----DLIRREIDIMNQLHHQKLINLHDAFEDDDEMILI 8062
Cdd:cd14098     1 KYQIIDRLGSGTFAEVKKAVEVETGKMRAIKQI-VKRKVAGndknlQLFQREINILKSLEHPGIVRLIDWYEDDQHIYLV 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 8063 LEFLSGGELFERITAEGYVmTEAEVINYMRQICEGIRHMHEQNIIHLDIKPENIMCQTRSSTNVKLIDFGLATRLDPNEV 8142
Cdd:cd14098    80 MEYVEGGDLMDFIMAWGAI-PEQHARELTKQILEAMAYTHSMGITHRDLKPENILITQDDPVIVKISDFGLAKVIHTGTF 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 8143 VKITTGTAEFAAPEIV---NREPVGFYT---DMWATGVLSYVLLSGLSPFAGDNDVQTLKNVKACDW----DFDVEsfky 8212
Cdd:cd14098   159 LVTFCGTMAYLAPEILmskEQNLQGGYSnlvDMWSVGCLVYVMLTGALPFDGSSQLPVEKRIRKGRYtqppLVDFN---- 234
                         250       260       270
                  ....*....|....*....|....*....|.
gi 281359561 8213 ISEEAKDFIRKLLVRNKEKRMTAHECLLHPW 8243
Cdd:cd14098   235 ISEEAIDFILRLLDVDPEKRMTAAQALDHPW 265
STKc_LKB1_CaMKK cd14008
Catalytic domain of the Serine/Threonine kinases, Liver Kinase B1, Calmodulin Dependent ...
7995-8244 1.84e-57

Catalytic domain of the Serine/Threonine kinases, Liver Kinase B1, Calmodulin Dependent Protein Kinase Kinase, and similar proteins; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Both LKB1 and CaMKKs can phosphorylate and activate AMP-activated protein kinase (AMPK). LKB1, also called STK11, serves as a master upstream kinase that activates AMPK and most AMPK-like kinases. LKB1 and AMPK are part of an energy-sensing pathway that links cell energy to metabolism and cell growth. They play critical roles in the establishment and maintenance of cell polarity, cell proliferation, cytoskeletal organization, as well as T-cell metabolism, including T-cell development, homeostasis, and effector function. CaMKKs are upstream kinases of the CaM kinase cascade that phosphorylate and activate CaMKI and CamKIV. They may also phosphorylate other substrates including PKB and AMPK. Vertebrates contain two CaMKKs, CaMKK1 (or alpha) and CaMKK2 (or beta). CaMKK1 is involved in the regulation of glucose uptake in skeletal muscles. CaMKK2 is involved in regulating energy balance, glucose metabolism, adiposity, hematopoiesis, inflammation, and cancer. The LKB1/CaMKK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270910 [Multi-domain]  Cd Length: 267  Bit Score: 202.40  E-value: 1.84e-57
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 7995 IGTGAFGVVHRCRERSTGNIFAAKFI-----------PVSHSVEKD---LIRREIDIMNQLHHQKLINLHDAFEDD--DE 8058
Cdd:cd14008     1 LGRGSFGKVKLALDTETGQLYAIKIFnksrlrkrregKNDRGKIKNaldDVRREIAIMKKLDHPNIVRLYEVIDDPesDK 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 8059 MILILEFLSGGELFERIT-AEGYVMTEAEVINYMRQICEGIRHMHEQNIIHLDIKPENIMcqtRSSTN-VKLIDFGLATR 8136
Cdd:cd14008    81 LYLVLEYCEGGPVMELDSgDRVPPLPEETARKYFRDLVLGLEYLHENGIVHRDIKPENLL---LTADGtVKISDFGVSEM 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 8137 L-DPNEVVKITTGTAEFAAPEI--VNREPV-GFYTDMWATGVLSYVLLSGLSPFAGDNDVQTLKNVKACDWDFDVEsfKY 8212
Cdd:cd14008   158 FeDGNDTLQKTAGTPAFLAPELcdGDSKTYsGKAADIWALGVTLYCLVFGRLPFNGDNILELYEAIQNQNDEFPIP--PE 235
                         250       260       270
                  ....*....|....*....|....*....|..
gi 281359561 8213 ISEEAKDFIRKLLVRNKEKRMTAHECLLHPWL 8244
Cdd:cd14008   236 LSPELKDLLRRMLEKDPEKRITLKEIKEHPWV 267
STKc_Trio_C cd14113
C-terminal kinase domain of the Large Serine/Threonine Kinase and Rho Guanine Nucleotide ...
7989-8244 3.61e-57

C-terminal kinase domain of the Large Serine/Threonine Kinase and Rho Guanine Nucleotide Exchange Factor, Triple functional domain protein; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Triple functional domain protein (Trio), also called PTPRF-interacting protein, is a large multidomain protein containing a series of spectrin-like repeats, two each of RhoGEF and SH3 domains, an immunoglobulin-like (Ig) domain and a C-terminal kinase. Trio plays important roles in neuronal cell migration and axon guidance. It was originally identified as an interacting partner of the of the receptor-like tyrosine phosphatase (RPTP) LAR (leukocyte-antigen-related protein), a family of receptors that function in the signaling to the actin cytoskeleton during development. Trio functions as a GEF for Rac1, RhoG, and RhoA, and is involved in the regulation of lamellipodia formation, mediating Rac1-dependent cell spreading and migration. The Trio subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271015 [Multi-domain]  Cd Length: 263  Bit Score: 201.36  E-value: 3.61e-57
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 7989 YDILEEIGTGAFGVVHRCRERSTGNIFAAKFIPvSHSVEKDLIRREIDIMNQLHHQKLINLHDAFEDDDEMILILEFLSG 8068
Cdd:cd14113     9 YSEVAELGRGRFSVVKKCDQRGTKRAVATKFVN-KKLMKRDQVTHELGVLQSLQHPQLVGLLDTFETPTSYILVLEMADQ 87
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 8069 GELFERITAEGYvMTEAEVINYMRQICEGIRHMHEQNIIHLDIKPENIMC-QTRSSTNVKLIDFGLATRLDPNEVVKITT 8147
Cdd:cd14113    88 GRLLDYVVRWGN-LTEEKIRFYLREILEALQYLHNCRIAHLDLKPENILVdQSLSKPTIKLADFGDAVQLNTTYYIHQLL 166
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 8148 GTAEFAAPEIVNREPVGFYTDMWATGVLSYVLLSGLSPFAGDNDVQTLKNVKACDWDFDVESFKYISEEAKDFIRKLLVR 8227
Cdd:cd14113   167 GSPEFAAPEIILGNPVSLTSDLWSIGVLTYVLLSGVSPFLDESVEETCLNICRLDFSFPDDYFKGVSQKAKDFVCFLLQM 246
                         250
                  ....*....|....*..
gi 281359561 8228 NKEKRMTAHECLLHPWL 8244
Cdd:cd14113   247 DPAKRPSAALCLQEQWL 263
SPS1 COG0515
Serine/threonine protein kinase [Signal transduction mechanisms];
7987-8232 7.81e-56

Serine/threonine protein kinase [Signal transduction mechanisms];


Pssm-ID: 440281 [Multi-domain]  Cd Length: 482  Bit Score: 205.25  E-value: 7.81e-56
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 7987 DRYDILEEIGTGAFGVVHRCRERSTGNIFAAKFIPVSHSVEKDLI---RREIDIMNQLHHQKLINLHDAFEDDDEMILIL 8063
Cdd:COG0515     7 GRYRILRLLGRGGMGVVYLARDLRLGRPVALKVLRPELAADPEARerfRREARALARLNHPNIVRVYDVGEEDGRPYLVM 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 8064 EFLSGGELFERITAEGyVMTEAEVINYMRQICEGIRHMHEQNIIHLDIKPENIMCqtRSSTNVKLIDFGLATRLDPNEVV 8143
Cdd:COG0515    87 EYVEGESLADLLRRRG-PLPPAEALRILAQLAEALAAAHAAGIVHRDIKPANILL--TPDGRVKLIDFGIARALGGATLT 163
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 8144 KITT--GTAEFAAPEIVNREPVGFYTDMWATGVLSYVLLSGLSPFAGDNDVQTLKNVKACDWDFDVESFKYISEEAKDFI 8221
Cdd:COG0515   164 QTGTvvGTPGYMAPEQARGEPVDPRSDVYSLGVTLYELLTGRPPFDGDSPAELLRAHLREPPPPPSELRPDLPPALDAIV 243
                         250
                  ....*....|.
gi 281359561 8222 RKLLVRNKEKR 8232
Cdd:COG0515   244 LRALAKDPEER 254
STKc_PLK cd14099
Catalytic domain of the Serine/Threonine Kinases, Polo-like kinases; STKs catalyze the ...
7987-8244 9.63e-56

Catalytic domain of the Serine/Threonine Kinases, Polo-like kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PLKs play important roles in cell cycle progression and in DNA damage responses. They regulate mitotic entry, mitotic exit, and cytokinesis. In general PLKs contain an N-terminal catalytic kinase domain and a C-terminal regulatory polo box domain (PBD), which is comprised by two bipartite polo-box motifs (or polo boxes) and is involved in protein interactions. PLKs derive their names from homology to polo, a kinase first identified in Drosophila. There are five mammalian PLKs (PLK1-5) from distinct genes. There is good evidence that PLK1 may function as an oncogene while PLK2-5 have tumor suppressive properties. PLK1 functions as a positive regulator of mitosis, meiosis, and cytokinesis. PLK2 functions in G1 progression, S-phase arrest, and centriole duplication. PLK3 regulates angiogenesis and responses to DNA damage. PLK4 is required for late mitotic progression, cell survival, and embryonic development. PLK5 was first identified as a pseudogene containing a stop codon within the kinase domain, however, both murine and human genes encode expressed proteins. PLK5 functions in cell cycle arrest.


Pssm-ID: 271001 [Multi-domain]  Cd Length: 258  Bit Score: 197.01  E-value: 9.63e-56
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 7987 DRYDILEEIGTGAFGVVHRCRERSTGNIFAAKFIPVS-----HSVEKdlIRREIDIMNQLHHQKLINLHDAFEDDDEMIL 8061
Cdd:cd14099     1 KRYRRGKFLGKGGFAKCYEVTDMSTGKVYAGKVVPKSsltkpKQREK--LKSEIKIHRSLKHPNIVKFHDCFEDEENVYI 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 8062 ILEFLSGGELFERITAEGYvMTEAEVINYMRQICEGIRHMHEQNIIHLDIKPENIMCQtrSSTNVKLIDFGLATRLDPNE 8141
Cdd:cd14099    79 LLELCSNGSLMELLKRRKA-LTEPEVRYFMRQILSGVKYLHSNRIIHRDLKLGNLFLD--ENMNVKIGDFGLAARLEYDG 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 8142 VVKITT-GTAEFAAPEIVNREpVG--FYTDMWATGVLSYVLLSGLSPFAGDNDVQTLKNVKACDWDFdvESFKYISEEAK 8218
Cdd:cd14099   156 ERKKTLcGTPNYIAPEVLEKK-KGhsFEVDIWSLGVILYTLLVGKPPFETSDVKETYKRIKKNEYSF--PSHLSISDEAK 232
                         250       260
                  ....*....|....*....|....*.
gi 281359561 8219 DFIRKLLVRNKEKRMTAHECLLHPWL 8244
Cdd:cd14099   233 DLIRSMLQPDPTKRPSLDEILSHPFF 258
PKc_STE cd05122
Catalytic domain of STE family Protein Kinases; PKs catalyze the transfer of the ...
7989-8244 9.68e-56

Catalytic domain of STE family Protein Kinases; PKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine (ST) or tyrosine residues on protein substrates. This family is composed of STKs, and some dual-specificity PKs that phosphorylate both threonine and tyrosine residues of target proteins. Most members are kinases involved in mitogen-activated protein kinase (MAPK) signaling cascades, acting as MAPK kinases (MAPKKs), MAPKK kinases (MAPKKKs), or MAPKKK kinases (MAP4Ks). The MAPK signaling pathways are important mediators of cellular responses to extracellular signals. The pathways involve a triple kinase core cascade comprising of the MAPK, which is phosphorylated and activated by a MAPKK, which itself is phosphorylated and activated by a MAPKKK. Each MAPK cascade is activated either by a small GTP-binding protein or by an adaptor protein, which transmits the signal either directly to a MAPKKK to start the triple kinase core cascade or indirectly through a mediator kinase, a MAP4K. Other STE family members include p21-activated kinases (PAKs) and class III myosins, among others. PAKs are Rho family GTPase-regulated kinases that serve as important mediators in the function of Cdc42 (cell division cycle 42) and Rac. Class III myosins are motor proteins containing an N-terminal kinase catalytic domain and a C-terminal actin-binding domain, which can phosphorylate several cytoskeletal proteins, conventional myosin regulatory light chains, as well as autophosphorylate the C-terminal motor domain. They play an important role in maintaining the structural integrity of photoreceptor cell microvilli. The STE family is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270692 [Multi-domain]  Cd Length: 254  Bit Score: 197.04  E-value: 9.68e-56
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 7989 YDILEEIGTGAFGVVHRCRERSTGNIFAAKFIPVSHSVEKDLIRREIDIMNQLHHQKLINLHDAFEDDDEMILILEFLSG 8068
Cdd:cd05122     2 FEILEKIGKGGFGVVYKARHKKTGQIVAIKKINLESKEKKESILNEIAILKKCKHPNIVKYYGSYLKKDELWIVMEFCSG 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 8069 GELFERITAEGYVMTEAEVINYMRQICEGIRHMHEQNIIHLDIKPENIMCQTRSStnVKLIDFGLATRLDPNEVVKITTG 8148
Cdd:cd05122    82 GSLKDLLKNTNKTLTEQQIAYVCKEVLKGLEYLHSHGIIHRDIKAANILLTSDGE--VKLIDFGLSAQLSDGKTRNTFVG 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 8149 TAEFAAPEIVNREPVGFYTDMWATGVLSYVLLSGLSPF-----------AGDNDVQTLKNVkacdwdfdvesfKYISEEA 8217
Cdd:cd05122   160 TPYWMAPEVIQGKPYGFKADIWSLGITAIEMAEGKPPYselppmkalflIATNGPPGLRNP------------KKWSKEF 227
                         250       260
                  ....*....|....*....|....*..
gi 281359561 8218 KDFIRKLLVRNKEKRMTAHECLLHPWL 8244
Cdd:cd05122   228 KDFLKKCLQKDPEKRPTAEQLLKHPFI 254
STKc_DCKL3 cd14185
Catalytic domain of the Serine/Threonine Kinase, Doublecortin-like kinase 3 (also called ...
7989-8243 4.01e-55

Catalytic domain of the Serine/Threonine Kinase, Doublecortin-like kinase 3 (also called Doublecortin-like and CAM kinase-like 3); STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. DCKL3 (or DCAMKL3) belongs to the doublecortin (DCX) family of proteins which are involved in neuronal migration, neurogenesis, and eye receptor development, among others. Family members typically contain tandem doublecortin (DCX) domains at the N-terminus; DCX domains can bind microtubules and serve as protein-interaction platforms. DCKL3 contains a single DCX domain (instead of a tandem) and a C-terminal kinase domain with similarity to CAMKs. It has been shown to interact with tubulin and JIP1/2. The DCKL3 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271087 [Multi-domain]  Cd Length: 258  Bit Score: 195.17  E-value: 4.01e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 7989 YDILEEIGTGAFGVVHRCRERSTGNIFAAKFIPVSHSVEK-DLIRREIDIMNQLHHQKLINLHDAFEDDDEMILILEFLS 8067
Cdd:cd14185     2 YEIGRTIGDGNFAVVKECRHWNENQEYAMKIIDKSKLKGKeDMIESEILIIKSLSHPNIVKLFEVYETEKEIYLILEYVR 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 8068 GGELFERITaEGYVMTEAEVINYMRQICEGIRHMHEQNIIHLDIKPENIMCQTRS--STNVKLIDFGLATRLdpNEVVKI 8145
Cdd:cd14185    82 GGDLFDAII-ESVKFTEHDAALMIIDLCEALVYIHSKHIVHRDLKPENLLVQHNPdkSTTLKLADFGLAKYV--TGPIFT 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 8146 TTGTAEFAAPEIVNREPVGFYTDMWATGVLSYVLLSGLSPF-AGDNDVQTLKN-VKACDWDFDVESFKYISEEAKDFIRK 8223
Cdd:cd14185   159 VCGTPTYVAPEILSEKGYGLEVDMWAAGVILYILLCGFPPFrSPERDQEELFQiIQLGHYEFLPPYWDNISEAAKDLISR 238
                         250       260
                  ....*....|....*....|
gi 281359561 8224 LLVRNKEKRMTAHECLLHPW 8243
Cdd:cd14185   239 LLVVDPEKRYTAKQVLQHPW 258
STKc_PDK1 cd05581
Catalytic domain of the Serine/Threonine Kinase, Phosphoinositide-dependent kinase 1; STKs ...
7989-8237 1.07e-54

Catalytic domain of the Serine/Threonine Kinase, Phosphoinositide-dependent kinase 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PDK1 carries an N-terminal catalytic domain and a C-terminal pleckstrin homology (PH) domain that binds phosphoinositides. It phosphorylates the activation loop of AGC kinases that are regulated by PI3K such as PKB, SGK, and PKC, among others, and is crucial for their activation. Thus, it contributes in regulating many processes including metabolism, growth, proliferation, and survival. PDK1 also has the ability to autophosphorylate and is constitutively active in mammalian cells. It is essential for normal embryo development and is important in regulating cell volume. The PDK1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270733 [Multi-domain]  Cd Length: 278  Bit Score: 194.74  E-value: 1.07e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 7989 YDILEEIGTGAFGVVHRCRERSTGNIFAAKFIPVSHSV-EK--DLIRREIDIMNQLHHQKLINLHDAFEDDDEMILILEF 8065
Cdd:cd05581     3 FKFGKPLGEGSYSTVVLAKEKETGKEYAIKVLDKRHIIkEKkvKYVTIEKEVLSRLAHPGIVKLYYTFQDESKLYFVLEY 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 8066 LSGGELFERITAEGYvMTEAEVINYMRQICEGIRHMHEQNIIHLDIKPENIMCQtrSSTNVKLIDFGLATRLDPNEVVKI 8145
Cdd:cd05581    83 APNGDLLEYIRKYGS-LDEKCTRFYTAEIVLALEYLHSKGIIHRDLKPENILLD--EDMHIKITDFGTAKVLGPDSSPES 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 8146 T------------------TGTAEFAAPEIVNREPVGFYTDMWATGVLSYVLLSGLSPFAGDNDVQTLKNVKACDWDFDv 8207
Cdd:cd05581   160 TkgdadsqiaynqaraasfVGTAEYVSPELLNEKPAGKSSDLWALGCIIYQMLTGKPPFRGSNEYLTFQKIVKLEYEFP- 238
                         250       260       270
                  ....*....|....*....|....*....|
gi 281359561 8208 esfKYISEEAKDFIRKLLVRNKEKRMTAHE 8237
Cdd:cd05581   239 ---ENFPPDAKDLIQKLLVLDPSKRLGVNE 265
STKc_CaMKI_alpha cd14167
Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase ...
7985-8246 1.36e-54

Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase Type I alpha; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. CaMKs are multifunctional calcium and calmodulin (CaM) stimulated STKs involved in cell cycle regulation. The CaMK family includes CaMKI, CaMKII, CaMKIV, and CaMK kinase (CaMKK). In vertebrates, there are four CaMKI proteins encoded by different genes (alpha, beta, gamma, and delta), each producing at least one variant. CaMKs contain an N-terminal catalytic domain and a C-terminal regulatory domain that harbors a CaM binding site. CaMKI proteins are monomeric and they play pivotal roles in the nervous system, including long-term potentiation, dendritic arborization, neurite outgrowth, and the formation of spines, synapses, and axons. In addition, they may be involved in osteoclast differentiation and bone resorption. The CaMKI-alpha subfamily is part of a larger superfamily that includes the catalytic domains of other protein kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271069 [Multi-domain]  Cd Length: 263  Bit Score: 194.09  E-value: 1.36e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 7985 VYDRYDILEEIGTGAFGVVHRCRERSTGNIFAAKFIPVSHSVEKDL-IRREIDIMNQLHHQKLINLHDAFEDDDEMILIL 8063
Cdd:cd14167     1 IRDIYDFREVLGTGAFSEVVLAEEKRTQKLVAIKCIAKKALEGKETsIENEIAVLHKIKHPNIVALDDIYESGGHLYLIM 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 8064 EFLSGGELFERITAEGYvMTEAEVINYMRQICEGIRHMHEQNIIHLDIKPENIMCQT-RSSTNVKLIDFGLATRLDPNEV 8142
Cdd:cd14167    81 QLVSGGELFDRIVEKGF-YTERDASKLIFQILDAVKYLHDMGIVHRDLKPENLLYYSlDEDSKIMISDFGLSKIEGSGSV 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 8143 VKITTGTAEFAAPEIVNREPVGFYTDMWATGVLSYVLLSGLSPFAGDNDVQTLKNVKACDWDFDVESFKYISEEAKDFIR 8222
Cdd:cd14167   160 MSTACGTPGYVAPEVLAQKPYSKAVDCWSIGVIAYILLCGYPPFYDENDAKLFEQILKAEYEFDSPYWDDISDSAKDFIQ 239
                         250       260
                  ....*....|....*....|....
gi 281359561 8223 KLLVRNKEKRMTAHECLLHPWLTG 8246
Cdd:cd14167   240 HLMEKDPEKRFTCEQALQHPWIAG 263
STKc_PknB_like cd14014
Catalytic domain of bacterial Serine/Threonine kinases, PknB and similar proteins; STKs ...
7988-8235 1.38e-54

Catalytic domain of bacterial Serine/Threonine kinases, PknB and similar proteins; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily includes many bacterial eukaryotic-type STKs including Staphylococcus aureus PknB (also called PrkC or Stk1), Bacillus subtilis PrkC, and Mycobacterium tuberculosis Pkn proteins (PknB, PknD, PknE, PknF, PknL, and PknH), among others. S. aureus PknB is the only eukaryotic-type STK present in this species, although many microorganisms encode for several such proteins. It is important for the survival and pathogenesis of S. aureus as it is involved in the regulation of purine and pyrimidine biosynthesis, cell wall metabolism, autolysis, virulence, and antibiotic resistance. M. tuberculosis PknB is essential for growth and it acts on diverse substrates including proteins involved in peptidoglycan synthesis, cell division, transcription, stress responses, and metabolic regulation. B. subtilis PrkC is located at the inner membrane of endospores and functions to trigger spore germination. Bacterial STKs in this subfamily show varied domain architectures. The well-characterized members such as S. aureus and M. tuberculosis PknB, and B. subtilis PrkC, contain an N-terminal cytosolic kinase domain, a transmembrane (TM) segment, and mutliple C-terminal extracellular PASTA domains. The PknB subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270916 [Multi-domain]  Cd Length: 260  Bit Score: 193.96  E-value: 1.38e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 7988 RYDILEEIGTGAFGVVHRCRERSTGNIFAAKFIPVSHSVEKDLI---RREIDIMNQLHHQKLINLHDAFEDDDEMILILE 8064
Cdd:cd14014     1 RYRLVRLLGRGGMGEVYRARDTLLGRPVAIKVLRPELAEDEEFRerfLREARALARLSHPNIVRVYDVGEDDGRPYIVME 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 8065 FLSGGELFERITAEGYvMTEAEVINYMRQICEGIRHMHEQNIIHLDIKPENIMCQTRSstNVKLIDFGLATRLDPNEVVK 8144
Cdd:cd14014    81 YVEGGSLADLLRERGP-LPPREALRILAQIADALAAAHRAGIVHRDIKPANILLTEDG--RVKLTDFGIARALGDSGLTQ 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 8145 ITT--GTAEFAAPEIVNREPVGFYTDMWATGVLSYVLLSGLSPFAGDNDVQTLKNVKACDWDFDVESFKYISEEAKDFIR 8222
Cdd:cd14014   158 TGSvlGTPAYMAPEQARGGPVDPRSDIYSLGVVLYELLTGRPPFDGDSPAAVLAKHLQEAPPPPSPLNPDVPPALDAIIL 237
                         250
                  ....*....|...
gi 281359561 8223 KLLVRNKEKRMTA 8235
Cdd:cd14014   238 RALAKDPEERPQS 250
STKc_Chk2 cd14084
Catalytic domain of the Serine/Threonine kinase, Cell cycle Checkpoint Kinase 2; STKs catalyze ...
7977-8244 3.99e-54

Catalytic domain of the Serine/Threonine kinase, Cell cycle Checkpoint Kinase 2; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Checkpoint Kinase 2 (Chk2) plays an important role in cellular responses to DNA double-strand breaks and related lesions. It is phosphorylated and activated by ATM kinase, resulting in its dissociation from sites of damage to phosphorylate downstream targets such as BRCA1, p53, cell cycle transcription factor E2F1, the promyelocytic leukemia protein (PML) involved in apoptosis, and CDC25 phosphatases, among others. Mutations in Chk2 is linked to a variety of cancers including familial breast cancer, myelodysplastic syndromes, prostate cancer, lung cancer, and osteosarcomas. Chk2 contains an N-terminal SQ/TQ cluster domain (SCD), a central forkhead-associated (FHA) domain, and a C-terminal catalytic kinase domain. The Chk2 subfamily is part of a larger superfamily that includes the catalytic domains of other protein kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270986 [Multi-domain]  Cd Length: 275  Bit Score: 192.99  E-value: 3.99e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 7977 PVEISqqsvyDRYDILEEIGTGAFGVVHRCRERSTGNIFAAKFI--------PVSHSVEKDLIRREIDIMNQLHHQKLIN 8048
Cdd:cd14084     1 PKELR-----KKYIMSRTLGSGACGEVKLAYDKSTCKKVAIKIInkrkftigSRREINKPRNIETEIEILKKLSHPCIIK 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 8049 LHDAFEDDDEMILILEFLSGGELFERITAEgYVMTEAEVINYMRQICEGIRHMHEQNIIHLDIKPENIMCQTRSS-TNVK 8127
Cdd:cd14084    76 IEDFFDAEDDYYIVLELMEGGELFDRVVSN-KRLKEAICKLYFYQMLLAVKYLHSNGIIHRDLKPENVLLSSQEEeCLIK 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 8128 LIDFGLATRLDPNEVVKITTGTAEFAAPEIVNREPVGFYT---DMWATGVLSYVLLSGLSPFAGDNDVQTLKN-VKACDW 8203
Cdd:cd14084   155 ITDFGLSKILGETSLMKTLCGTPTYLAPEVLRSFGTEGYTravDCWSLGVILFICLSGYPPFSEEYTQMSLKEqILSGKY 234
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|.
gi 281359561 8204 DFDVESFKYISEEAKDFIRKLLVRNKEKRMTAHECLLHPWL 8244
Cdd:cd14084   235 TFIPKAWKNVSEEAKDLVKKMLVVDPSRRPSIEEALEHPWL 275
STKc_Kalirin_C cd14115
C-terminal kinase domain of the Large Serine/Threonine Kinase and Rho Guanine Nucleotide ...
7995-8243 5.67e-54

C-terminal kinase domain of the Large Serine/Threonine Kinase and Rho Guanine Nucleotide Exchange Factor, Kalirin; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Kalirin, also called Duo or Duet, is a large multidomain protein containing a series of spectrin-like repeats, two each of RhoGEF and SH3 domains, an immunoglobulin-like (Ig) domain and a C-terminal kinase. As a GEF, it activates Rac1, RhoA, and RhoG. It is highly expressed in neurons and is required for spine formation. The kalirin gene produces at least 10 isoforms from alternative promoter use and splicing. Of the major isoforms (Kalirin-7, -9, and -12), only kalirin-12 contains the C-terminal kinase domain. Kalirin-12 is highly expressed during embryonic development and it plays an important role in axon outgrowth. The Kalirin subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271017 [Multi-domain]  Cd Length: 248  Bit Score: 191.71  E-value: 5.67e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 7995 IGTGAFGVVHRCRERSTGNIFAAKFIPVSHSvEKDLIRREIDIMNQLHHQKLINLHDAFEDDDEMILILEFLSGGELFER 8074
Cdd:cd14115     1 IGRGRFSIVKKCLHKATRKDVAVKFVSKKMK-KKEQAAHEAALLQHLQHPQYITLHDTYESPTSYILVLELMDDGRLLDY 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 8075 ITAEGYVMTEaEVINYMRQICEGIRHMHEQNIIHLDIKPENIMCQTRSST-NVKLIDFGLATRLDPNEVVKITTGTAEFA 8153
Cdd:cd14115    80 LMNHDELMEE-KVAFYIRDIMEALQYLHNCRVAHLDIKPENLLIDLRIPVpRVKLIDLEDAVQISGHRHVHHLLGNPEFA 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 8154 APEIVNREPVGFYTDMWATGVLSYVLLSGLSPFAGDNDVQTLKNVKACDWDFDVESFKYISEEAKDFIRKLLVRNKEKRM 8233
Cdd:cd14115   159 APEVIQGTPVSLATDIWSIGVLTYVMLSGVSPFLDESKEETCINVCRVDFSFPDEYFGDVSQAARDFINVILQEDPRRRP 238
                         250
                  ....*....|
gi 281359561 8234 TAHECLLHPW 8243
Cdd:cd14115   239 TAATCLQHPW 248
STKc_RSK_C cd14091
C-terminal catalytic domain of the Serine/Threonine Kinases, Ribosomal S6 kinases; STKs ...
7989-8250 1.13e-53

C-terminal catalytic domain of the Serine/Threonine Kinases, Ribosomal S6 kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. RSKs contain an N-terminal kinase domain (NTD) from the AGC family and a C-terminal kinase domain (CTD) from the CAMK family. They are activated by signaling inputs from extracellular regulated kinase (ERK) and phosphoinositide dependent kinase 1 (PDK1). ERK phosphorylates and activates the CTD of RSK, serving as a docking site for PDK1, which phosphorylates and activates the NTD, which in turn phosphorylates all known RSK substrates. RSKs act as downstream effectors of mitogen-activated protein kinase (MAPK) and play key roles in mitogen-activated cell growth, differentiation, and survival. Mammals possess four RSK isoforms (RSK1-4) from distinct genes. RSK proteins are also referred to as MAP kinase-activated protein kinases (MAPKAPKs), 90 kDa ribosomal protein S6 kinases (p90-RSKs), or p90S6Ks. The RSK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270993 [Multi-domain]  Cd Length: 291  Bit Score: 192.46  E-value: 1.13e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 7989 YDILEEIGTGAFGVVHRCRERSTGNIFAAKFIpvshSVEKDLIRREIDIMNQL-HHQKLINLHDAFEDDDEMILILEFLS 8067
Cdd:cd14091     2 YEIKEEIGKGSYSVCKRCIHKATGKEYAVKII----DKSKRDPSEEIEILLRYgQHPNIITLRDVYDDGNSVYLVTELLR 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 8068 GGELFERITAEGYvMTEAEVINYMRQICEGIRHMHEQNIIHLDIKPENIMCQTRSST--NVKLIDFGLATRL-DPNEVVK 8144
Cdd:cd14091    78 GGELLDRILRQKF-FSEREASAVMKTLTKTVEYLHSQGVVHRDLKPSNILYADESGDpeSLRICDFGFAKQLrAENGLLM 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 8145 ITTGTAEFAAPEIVNREPVGFYTDMWATGVLSYVLLSGLSPFA-GDNDV--QTLKNVKACDWDFDVESFKYISEEAKDFI 8221
Cdd:cd14091   157 TPCYTANFVAPEVLKKQGYDAACDIWSLGVLLYTMLAGYTPFAsGPNDTpeVILARIGSGKIDLSGGNWDHVSDSAKDLV 236
                         250       260
                  ....*....|....*....|....*....
gi 281359561 8222 RKLLVRNKEKRMTAHECLLHPWLTGDHSA 8250
Cdd:cd14091   237 RKMLHVDPSQRPTAAQVLQHPWIRNRDSL 265
STKc_PSKH1 cd14087
Catalytic domain of the Protein Serine/Threonine kinase H1; STKs catalyze the transfer of the ...
7988-8244 1.31e-53

Catalytic domain of the Protein Serine/Threonine kinase H1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PSKH1 is an autophosphorylating STK that is expressed ubiquitously and exhibits multiple intracellular localizations including the centrosome, Golgi apparatus, and splice factor compartments. It contains a catalytic kinase domain and an N-terminal SH4-like motif that is acylated to facilitate membrane attachment. PSKH1 plays a rile in the maintenance of the Golgi apparatus, an important organelle within the secretory pathway. It may also function as a novel splice factor and a regulator of prostate cancer cell growth. The PSKH1 subfamily is part of a larger superfamily that includes the catalytic domains of other protein kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270989 [Multi-domain]  Cd Length: 259  Bit Score: 190.82  E-value: 1.31e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 7988 RYDILEEIGTGAFGVVHRCRERSTGNIFAAKFIPVSHSvEKDLIRREIDIMNQLHHQKLINLHDAFEDDDEMILILEFLS 8067
Cdd:cd14087     2 KYDIKALIGRGSFSRVVRVEHRVTRQPYAIKMIETKCR-GREVCESELNVLRRVRHTNIIQLIEVFETKERVYMVMELAT 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 8068 GGELFERITAEGYvMTEAEVINYMRQICEGIRHMHEQNIIHLDIKPENIM-CQTRSSTNVKLIDFGLAT--RLDPNEVVK 8144
Cdd:cd14087    81 GGELFDRIIAKGS-FTERDATRVLQMVLDGVKYLHGLGITHRDLKPENLLyYHPGPDSKIMITDFGLAStrKKGPNCLMK 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 8145 ITTGTAEFAAPEIVNREPVGFYTDMWATGVLSYVLLSGLSPFAGDNDVQTLKNVKACDWDFDVESFKYISEEAKDFIRKL 8224
Cdd:cd14087   160 TTCGTPEYIAPEILLRKPYTQSVDMWAVGVIAYILLSGTMPFDDDNRTRLYRQILRAKYSYSGEPWPSVSNLAKDFIDRL 239
                         250       260
                  ....*....|....*....|
gi 281359561 8225 LVRNKEKRMTAHECLLHPWL 8244
Cdd:cd14087   240 LTVNPGERLSATQALKHPWI 259
STKc_CaMKI_beta cd14169
Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase ...
7989-8255 1.72e-53

Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase Type I beta; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. CaMKs are multifunctional calcium and calmodulin (CaM) stimulated STKs involved in cell cycle regulation. The CaMK family includes CaMKI, CaMKII, CaMKIV, and CaMK kinase (CaMKK). In vertebrates, there are four CaMKI proteins encoded by different genes (alpha, beta, gamma, and delta), each producing at least one variant. CaMKs contain an N-terminal catalytic domain and a C-terminal regulatory domain that harbors a CaM binding site. CaMKI proteins are monomeric and they play pivotal roles in the nervous system, including long-term potentiation, dendritic arborization, neurite outgrowth, and the formation of spines, synapses, and axons. In addition, they may be involved in osteoclast differentiation and bone resorption. The CaMKI-beta subfamily is part of a larger superfamily that includes the catalytic domains of other protein kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271071 [Multi-domain]  Cd Length: 277  Bit Score: 191.26  E-value: 1.72e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 7989 YDILEEIGTGAFGVVHRCRERSTGNIFAAKFIPVSHSVEKD-LIRREIDIMNQLHHQKLINLHDAFEDDDEMILILEFLS 8067
Cdd:cd14169     5 YELKEKLGEGAFSEVVLAQERGSQRLVALKCIPKKALRGKEaMVENEIAVLRRINHENIVSLEDIYESPTHLYLAMELVT 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 8068 GGELFERITAEGYvMTEAEVINYMRQICEGIRHMHEQNIIHLDIKPENIMCQTR-SSTNVKLIDFGLaTRLDPNEVVKIT 8146
Cdd:cd14169    85 GGELFDRIIERGS-YTEKDASQLIGQVLQAVKYLHQLGIVHRDLKPENLLYATPfEDSKIMISDFGL-SKIEAQGMLSTA 162
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 8147 TGTAEFAAPEIVNREPVGFYTDMWATGVLSYVLLSGLSPFAGDNDVQTLKNVKACDWDFDVESFKYISEEAKDFIRKLLV 8226
Cdd:cd14169   163 CGTPGYVAPELLEQKPYGKAVDVWAIGVISYILLCGYPPFYDENDSELFNQILKAEYEFDSPYWDDISESAKDFIRHLLE 242
                         250       260
                  ....*....|....*....|....*....
gi 281359561 8227 RNKEKRMTAHECLLHPWLTGDhSAMKQEI 8255
Cdd:cd14169   243 RDPEKRFTCEQALQHPWISGD-TALDRDI 270
STKc_MAPKKK cd06606
Catalytic domain of the Serine/Threonine Kinase, Mitogen-Activated Protein Kinase Kinase ...
7993-8244 1.92e-53

Catalytic domain of the Serine/Threonine Kinase, Mitogen-Activated Protein Kinase Kinase Kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MAPKKKs (MKKKs or MAP3Ks) are also called MAP/ERK kinase kinases (MEKKs) in some cases. They phosphorylate and activate MAPK kinases (MAPKKs or MKKs or MAP2Ks), which in turn phosphorylate and activate MAPKs during signaling cascades that are important in mediating cellular responses to extracellular signals. This subfamily is composed of the Apoptosis Signal-regulating Kinases ASK1 (or MAPKKK5) and ASK2 (or MAPKKK6), MEKK1, MEKK2, MEKK3, MEKK4, as well as plant and fungal MAPKKKs. Also included in this subfamily are the cell division control proteins Schizosaccharomyces pombe Cdc7 and Saccharomyces cerevisiae Cdc15. The MAPKKK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270783 [Multi-domain]  Cd Length: 258  Bit Score: 190.42  E-value: 1.92e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 7993 EEIGTGAFGVVHRCRERSTGNIFAAKFIPVSHSVEKDL--IRREIDIMNQLHHQKLINLHDAFEDDDEMILILEFLSGGE 8070
Cdd:cd06606     6 ELLGKGSFGSVYLALNLDTGELMAVKEVELSGDSEEELeaLEREIRILSSLKHPNIVRYLGTERTENTLNIFLEYVPGGS 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 8071 LFERITAEGyVMTEAEVINYMRQICEGIRHMHEQNIIHLDIKPENIMcqTRSSTNVKLIDFGLATRLDPNEVVKITT--- 8147
Cdd:cd06606    86 LASLLKKFG-KLPEPVVRKYTRQILEGLEYLHSNGIVHRDIKGANIL--VDSDGVVKLADFGCAKRLAEIATGEGTKslr 162
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 8148 GTAEFAAPEIVNREPVGFYTDMWATGVLSYVLLSGLSPFAGDNDVQTLknvkacdwDFDVESFK-------YISEEAKDF 8220
Cdd:cd06606   163 GTPYWMAPEVIRGEGYGRAADIWSLGCTVIEMATGKPPWSELGNPVAA--------LFKIGSSGepppipeHLSEEAKDF 234
                         250       260
                  ....*....|....*....|....
gi 281359561 8221 IRKLLVRNKEKRMTAHECLLHPWL 8244
Cdd:cd06606   235 LRKCLQRDPKKRPTADELLQHPFL 258
STKc_CASK cd14094
Catalytic domain of the Serine/Threonine Kinase, Calcium/calmodulin-dependent serine protein ...
7987-8277 3.30e-53

Catalytic domain of the Serine/Threonine Kinase, Calcium/calmodulin-dependent serine protein kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. CASK belongs to the MAGUK (membrane-associated guanylate kinase) protein family, which functions as multiple domain adaptor proteins and is characterized by the presence of a core of three domains: PDZ, SH3, and guanylate kinase (GuK). The enzymatically inactive GuK domain in MAGUK proteins mediates protein-protein interactions and associates intramolecularly with the SH3 domain. In addition, CASK contains a catalytic kinase and two L27 domains. It is highly expressed in the nervous system and plays roles in synaptic protein targeting, neural development, and regulation of gene expression. Binding partners include parkin (a Parkinson's disease molecule), neurexin (adhesion molecule), syndecans, calcium channel proteins, CINAP (nucleosome assembly protein), transcription factor Tbr-1, and the cytoplasmic adaptor proteins Mint1, Veli/mLIN-7/MALS, SAP97, caskin, and CIP98. Deletion or mutations in the CASK gene have been implicated in X-linked mental retardation. The CASK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270996 [Multi-domain]  Cd Length: 300  Bit Score: 191.22  E-value: 3.30e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 7987 DRYDILEEIGTGAFGVVHRCRERSTGNIFAAKFIPVSH-------SVEKdlIRREIDIMNQLHHQKLINLHDAFEDDDEM 8059
Cdd:cd14094     3 DVYELCEVIGKGPFSVVRRCIHRETGQQFAVKIVDVAKftsspglSTED--LKREASICHMLKHPHIVELLETYSSDGML 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 8060 ILILEFLSGGEL-FE--RITAEGYVMTEAEVINYMRQICEGIRHMHEQNIIHLDIKPENIMCQTR-SSTNVKLIDFGLAT 8135
Cdd:cd14094    81 YMVFEFMDGADLcFEivKRADAGFVYSEAVASHYMRQILEALRYCHDNNIIHRDVKPHCVLLASKeNSAPVKLGGFGVAI 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 8136 RL-DPNEVVKITTGTAEFAAPEIVNREPVGFYTDMWATGVLSYVLLSGLSPFAGdNDVQTLKNVKACDWDFDVESFKYIS 8214
Cdd:cd14094   161 QLgESGLVAGGRVGTPHFMAPEVVKREPYGKPVDVWGCGVILFILLSGCLPFYG-TKERLFEGIIKGKYKMNPRQWSHIS 239
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 281359561 8215 EEAKDFIRKLLVRNKEKRMTAHECLLHPWLTgdhsamkqeiNRDRYlAYREKLRRKYEDFERF 8277
Cdd:cd14094   240 ESAKDLVRRMLMLDPAERITVYEALNHPWIK----------ERDRY-AYRIHLPETVEQLRKF 291
STKc_MSK_C cd14092
C-terminal catalytic domain of the Serine/Threonine Kinase, Mitogen and stress-activated ...
7989-8249 2.44e-52

C-terminal catalytic domain of the Serine/Threonine Kinase, Mitogen and stress-activated kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MSKs contain an N-terminal kinase domain (NTD) from the AGC family and a C-terminal kinase domain (CTD) from the CAMK family. MSKs are activated by two major signaling cascades, the Ras-MAPK and p38 stress kinase pathways, in response to various stimuli such as growth factors, hormones, neurotransmitters, cellular stress, and pro-inflammatory cytokines. This triggers phosphorylation in the activation loop (A-loop) of the CTD of MSK. The active CTD phosphorylates the hydrophobic motif (HM) in the C-terminal extension of NTD, which facilitates the phosphorylation of the A-loop and activates the NTD, which in turn phosphorylates downstream targets. MSKs are predominantly nuclear proteins. They are widely expressed in many tissues including heart, brain, lung, liver, kidney, and pancreas. There are two isoforms of MSK, called MSK1 and MSK2. The MSK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270994 [Multi-domain]  Cd Length: 311  Bit Score: 189.43  E-value: 2.44e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 7989 YDI-LEE--IGTGAFGVVHRCRERSTGNIFAAKFIpvshSVEKDlIRREIDIMNQLH-HQKLINLHDAFEDDDEMILILE 8064
Cdd:cd14092     5 YELdLREeaLGDGSFSVCRKCVHKKTGQEFAVKIV----SRRLD-TSREVQLLRLCQgHPNIVKLHEVFQDELHTYLVME 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 8065 FLSGGELFERITAEGYvMTEAEVINYMRQICEGIRHMHEQNIIHLDIKPENIM-CQTRSSTNVKLIDFGLAtRLDPNEVV 8143
Cdd:cd14092    80 LLRGGELLERIRKKKR-FTESEASRIMRQLVSAVSFMHSKGVVHRDLKPENLLfTDEDDDAEIKIVDFGFA-RLKPENQP 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 8144 KITTG-TAEFAAPEIVNR-EPVGFYT---DMWATGVLSYVLLSGLSPFAGDND----VQTLKNVKACDWDFDVESFKYIS 8214
Cdd:cd14092   158 LKTPCfTLPYAAPEVLKQaLSTQGYDescDLWSLGVILYTMLSGQVPFQSPSRnesaAEIMKRIKSGDFSFDGEEWKNVS 237
                         250       260       270
                  ....*....|....*....|....*....|....*
gi 281359561 8215 EEAKDFIRKLLVRNKEKRMTAHECLLHPWLTGDHS 8249
Cdd:cd14092   238 SEAKSLIQGLLTVDPSKRLTMSELRNHPWLQGSSS 272
STKc_Nek cd08215
Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase; ...
7988-8242 4.76e-52

Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The Nek family is composed of 11 different mammalian members (Nek1-11) with similarity to the catalytic domain of Aspergillus nidulans NIMA kinase, the founding member of the Nek family, which was identified in a screen for cell cycle mutants that were prevented from entering mitosis. Neks contain a conserved N-terminal catalytic domain and a more divergent C-terminal regulatory region of various sizes and structures. They are involved in the regulation of downstream processes following the activation of Cdc2, and many of their functions are cell cycle-related. They play critical roles in microtubule dynamics during ciliogenesis and mitosis. The Nek family is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270855 [Multi-domain]  Cd Length: 258  Bit Score: 186.51  E-value: 4.76e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 7988 RYDILEEIGTGAFGVVHRCRERSTGNIFAAKFIPVSH--SVEKDLIRREIDIMNQLHHQKLINLHDAFEDDDEMILILEF 8065
Cdd:cd08215     1 KYEKIRVIGKGSFGSAYLVRRKSDGKLYVLKEIDLSNmsEKEREEALNEVKLLSKLKHPNIVKYYESFEENGKLCIVMEY 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 8066 LSGGELFERITA---EGYVMTEAEVINYMRQICEGIRHMHEQNIIHLDIKPENIMCQTRSstNVKLIDFGLATRLDPNEV 8142
Cdd:cd08215    81 ADGGDLAQKIKKqkkKGQPFPEEQILDWFVQICLALKYLHSRKILHRDLKTQNIFLTKDG--VVKLGDFGISKVLESTTD 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 8143 VKITT-GTAEFAAPEIVNREPVGFYTDMWATGVLSYVLLSGLSPFAGDNDVQTLKNVKACDWDFDVESFkyiSEEAKDFI 8221
Cdd:cd08215   159 LAKTVvGTPYYLSPELCENKPYNYKSDIWALGCVLYELCTLKHPFEANNLPALVYKIVKGQYPPIPSQY---SSELRDLV 235
                         250       260
                  ....*....|....*....|.
gi 281359561 8222 RKLLVRNKEKRMTAHECLLHP 8242
Cdd:cd08215   236 NSMLQKDPEKRPSANEILSSP 256
STKc_SPEG_rpt2 cd14111
Catalytic kinase domain, second repeat, of Giant Serine/Threonine Kinase Striated muscle ...
7989-8244 4.97e-52

Catalytic kinase domain, second repeat, of Giant Serine/Threonine Kinase Striated muscle preferentially expressed protein kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The Striated muscle preferentially expressed gene (SPEG) generates 4 different isoforms through alternative promoter use and splicing in a tissue-specific manner: SPEGalpha and SPEGbeta are expressed in cardiac and skeletal striated muscle; Aortic Preferentially Expressed Protein-1 (APEG-1) is expressed in vascular smooth muscle; and Brain preferentially expressed gene (BPEG) is found in the brain and aorta. SPEG proteins have mutliple immunoglobulin (Ig), 2 fibronectin type III (FN3), and two kinase domains. They are necessary for cardiac development and survival. The SPEG subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271013 [Multi-domain]  Cd Length: 257  Bit Score: 186.18  E-value: 4.97e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 7989 YDILEEIGTGAFGVVHRCRERSTGNIFAAKFIPVSHSvEKDLIRREIDIMNQLHHQKLINLHDAFEDDDEMILILEFLSG 8068
Cdd:cd14111     5 YTFLDEKARGRFGVIRRCRENATGKNFPAKIVPYQAE-EKQGVLQEYEILKSLHHERIMALHEAYITPRYLVLIAEFCSG 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 8069 GELFERITaEGYVMTEAEVINYMRQICEGIRHMHEQNIIHLDIKPENIMCqtrSSTNV-KLIDFGLATRLDPNEVVKIT- 8146
Cdd:cd14111    84 KELLHSLI-DRFRYSEDDVVGYLVQILQGLEYLHGRRVLHLDIKPDNIMV---TNLNAiKIVDFGSAQSFNPLSLRQLGr 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 8147 -TGTAEFAAPEIVNREPVGFYTDMWATGVLSYVLLSGLSPFAGDNDVQTLKNVKACDWDfdveSFKY---ISEEAKDFIR 8222
Cdd:cd14111   160 rTGTLEYMAPEMVKGEPVGPPADIWSIGVLTYIMLSGRSPFEDQDPQETEAKILVAKFD----AFKLypnVSQSASLFLK 235
                         250       260
                  ....*....|....*....|..
gi 281359561 8223 KLLVRNKEKRMTAHECLLHPWL 8244
Cdd:cd14111   236 KVLSSYPWSRPTTKDCFAHAWL 257
STKc_Mnk cd14090
Catalytic domain of the Serine/Threonine kinases, Mitogen-activated protein kinase ...
7987-8243 3.34e-51

Catalytic domain of the Serine/Threonine kinases, Mitogen-activated protein kinase signal-integrating kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MAPK signal-integrating kinases (Mnks) are MAPK-activated protein kinases and is comprised by a group of four proteins, produced by alternative splicing from two genes (Mnk1 and Mnk2). The isoforms of Mnk1 (1a/1b) and Mnk2 (2a/2b) differ at their C-termini, with the a-form having a longer C-terminus containing a MAPK-binding region. All Mnks contain a catalytic kinase domain and a polybasic region at the N-terminus which binds importin and the eukaryotic initiation factor eIF4G. The best characterized Mnk substrate is eIF4G, whose phosphorylation may promote the export of certain mRNAs from the nucleus. Mnk also phosphorylate substrates that bind to AU-rich elements that regulate mRNA stability and translation. Mnks have also been implicated in tyrosine kinase receptor signaling, inflammation, and cell prolieration or survival. The Mnk subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270992 [Multi-domain]  Cd Length: 289  Bit Score: 185.31  E-value: 3.34e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 7987 DRYDILEEI-GTGAFGVVHRCRERSTGNIFAAKFIPVSHSVEKDLIRREIDIMNQLH-HQKLINLHDAFEDDDEMILILE 8064
Cdd:cd14090     1 DLYKLTGELlGEGAYASVQTCINLYTGKEYAVKIIEKHPGHSRSRVFREVETLHQCQgHPNILQLIEYFEDDERFYLVFE 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 8065 FLSGGELFERITAEGYvMTEAEVINYMRQICEGIRHMHEQNIIHLDIKPENIMCQTRSSTN-VKLIDFGLAT--RLDPNE 8141
Cdd:cd14090    81 KMRGGPLLSHIEKRVH-FTEQEASLVVRDIASALDFLHDKGIAHRDLKPENILCESMDKVSpVKICDFDLGSgiKLSSTS 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 8142 VVKITT-------GTAEFAAPEIVN--REPVGFY---TDMWATGVLSYVLLSGLSPFAGD-------------NDVQTL- 8195
Cdd:cd14090   160 MTPVTTpelltpvGSAEYMAPEVVDafVGEALSYdkrCDLWSLGVILYIMLCGYPPFYGRcgedcgwdrgeacQDCQELl 239
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*....
gi 281359561 8196 -KNVKACDWDFDVESFKYISEEAKDFIRKLLVRNKEKRMTAHECLLHPW 8243
Cdd:cd14090   240 fHSIQEGEYEFPEKEWSHISAEAKDLISHLLVRDASQRYTAEQVLQHPW 288
STKc_BRSK1_2 cd14081
Catalytic domain of Brain-specific serine/threonine-protein kinases 1 and 2; STKs catalyze the ...
7995-8244 2.54e-50

Catalytic domain of Brain-specific serine/threonine-protein kinases 1 and 2; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. BRSK1, also called SAD-B or SAD1 (Synapses of Amphids Defective homolog 1), and BRSK2, also called SAD-A, are highly expressed in mammalian forebrain. They play important roles in establishing neuronal polarity. BRSK1/2 double knock-out mice die soon after birth, showing thin cerebral cortices due to disordered subplate layers and neurons that lack distinct axons and dendrites. BRSK1 regulates presynaptic neurotransmitter release. Its activity fluctuates during cell cysle progression and it acts as a regulator of centrosome duplication. BRSK2 is also abundant in pancreatic islets, where it is involved in the regulation of glucose-stimulated insulin secretion. The BRSK1/2 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270983 [Multi-domain]  Cd Length: 255  Bit Score: 181.30  E-value: 2.54e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 7995 IGTGAFGVVHRCRERSTGNIFAAKFIPVSHSVEKDL---IRREIDIMNQLHHQKLINLHDAFEDDDEMILILEFLSGGEL 8071
Cdd:cd14081     9 LGKGQTGLVKLAKHCVTGQKVAIKIVNKEKLSKESVlmkVEREIAIMKLIEHPNVLKLYDVYENKKYLYLVLEYVSGGEL 88
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 8072 FERITAEGyVMTEAEVINYMRQICEGIRHMHEQNIIHLDIKPENIMCqtRSSTNVKLIDFGLATRLDPNEVVKITTGTAE 8151
Cdd:cd14081    89 FDYLVKKG-RLTEKEARKFFRQIISALDYCHSHSICHRDLKPENLLL--DEKNNIKIADFGMASLQPEGSLLETSCGSPH 165
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 8152 FAAPEIVNREPV-GFYTDMWATGVLSYVLLSGLSPFAGDNDVQTLKNVKAcdWDFDVESFkyISEEAKDFIRKLLVRNKE 8230
Cdd:cd14081   166 YACPEVIKGEKYdGRKADIWSCGVILYALLVGALPFDDDNLRQLLEKVKR--GVFHIPHF--ISPDAQDLLRRMLEVNPE 241
                         250
                  ....*....|....
gi 281359561 8231 KRMTAHECLLHPWL 8244
Cdd:cd14081   242 KRITIEEIKKHPWF 255
STKc_STK36 cd14002
Catalytic domain of Serine/Threonine Kinase 36; STKs catalyze the transfer of the ...
7987-8244 1.42e-49

Catalytic domain of Serine/Threonine Kinase 36; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. STK36, also called Fused (or Fu) kinase, is involved in the Hedgehog signaling pathway. It is activated by the Smoothened (SMO) signal transducer, resulting in the stabilization of GLI transcription factors and the phosphorylation of SUFU to facilitate the nuclear accumulation of GLI. In Drosophila, Fused kinase is maternally required for proper segmentation during embryonic development and for the development of legs and wings during the larval stage. In mice, STK36 is not necessary for embryonic development, although mice deficient in STK36 display growth retardation postnatally. The STK36 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270904 [Multi-domain]  Cd Length: 253  Bit Score: 178.98  E-value: 1.42e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 7987 DRYDILEEIGTGAFGVVHRCRERSTGNIFAAKFIPVSHSVEKDL--IRREIDIMNQLHHQKLINLHDAFEDDDEMILILE 8064
Cdd:cd14002     1 ENYHVLELIGEGSFGKVYKGRRKYTGQVVALKFIPKRGKSEKELrnLRQEIEILRKLNHPNIIEMLDSFETKKEFVVVTE 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 8065 FLSgGELFErITAEGYVMTEAEVINYMRQICEGIRHMHEQNIIHLDIKPENIMCQtrSSTNVKLIDFGLATRLDPNEVVk 8144
Cdd:cd14002    81 YAQ-GELFQ-ILEDDGTLPEEEVRSIAKQLVSALHYLHSNRIIHRDMKPQNILIG--KGGVVKLCDFGFARAMSCNTLV- 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 8145 ITT--GTAEFAAPEIVNREPVGFYTDMWATGVLSYVLLSGLSPFAGDNDVQTLKNVKAcDwdfDVESFKYISEEAKDFIR 8222
Cdd:cd14002   156 LTSikGTPLYMAPELVQEQPYDHTADLWSLGCILYELFVGQPPFYTNSIYQLVQMIVK-D---PVKWPSNMSPEFKSFLQ 231
                         250       260
                  ....*....|....*....|..
gi 281359561 8223 KLLVRNKEKRMTAHECLLHPWL 8244
Cdd:cd14002   232 GLLNKDPSKRLSWPDLLEHPFV 253
STKc_ATG1_ULK_like cd14009
Catalytic domain of the Serine/Threonine kinases, Autophagy-related protein 1 and Unc-51-like ...
7995-8243 2.32e-49

Catalytic domain of the Serine/Threonine kinases, Autophagy-related protein 1 and Unc-51-like kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily includes yeast ATG1 and metazoan homologs including vertebrate ULK1-3. The ATG1/ULK complex is conserved from yeast to humans and it plays a critical role in the initiation of autophagy, the intracellular system that leads to the lysosomal degradation of cellular components and their recycling into basic metabolic units. It is involved in nutrient sensing and signaling, the assembly of autophagy factors and the execution of autophagy. In metazoans, ATG1 homologs display additional functions. Unc-51 and ULKs have been implicated in neuronal and axonal development. The ATG1/ULK subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270911 [Multi-domain]  Cd Length: 251  Bit Score: 178.57  E-value: 2.32e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 7995 IGTGAFGVVHRCRERSTGNIFAAKFIPVSHSVEK--DLIRREIDIMNQLHHQKLINLHDAFEDDDEMILILEFLSGGELF 8072
Cdd:cd14009     1 IGRGSFATVWKGRHKQTGEVVAIKEISRKKLNKKlqENLESEIAILKSIKHPNIVRLYDVQKTEDFIYLVLEYCAGGDLS 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 8073 ERITAEGyVMTEAEVINYMRQICEGIRHMHEQNIIHLDIKPENIMCQTRSSTNV-KLIDFGLATRLDPNEVVKITTGTAE 8151
Cdd:cd14009    81 QYIRKRG-RLPEAVARHFMQQLASGLKFLRSKNIIHRDLKPQNLLLSTSGDDPVlKIADFGFARSLQPASMAETLCGSPL 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 8152 FAAPEIVNREPVGFYTDMWATGVLSYVLLSGLSPFAGDNDVQTLKNVKACDWDFDVESFKYISEEAKDFIRKLLVRNKEK 8231
Cdd:cd14009   160 YMAPEILQFQKYDAKADLWSVGAILFEMLVGKPPFRGSNHVQLLRNIERSDAVIPFPIAAQLSPDCKDLLRRLLRRDPAE 239
                         250
                  ....*....|..
gi 281359561 8232 RMTAHECLLHPW 8243
Cdd:cd14009   240 RISFEEFFAHPF 251
STKc_CaMKI_delta cd14168
Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase ...
7989-8252 4.31e-49

Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase Type I delta; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. CaMKs are multifunctional calcium and calmodulin (CaM) stimulated STKs involved in cell cycle regulation. The CaMK family includes CaMKI, CaMKII, CaMKIV, and CaMK kinase (CaMKK). In vertebrates, there are four CaMKI proteins encoded by different genes (alpha, beta, gamma, and delta), each producing at least one variant. CaMKs contain an N-terminal catalytic domain and a C-terminal regulatory domain that harbors a CaM binding site. CaMKI proteins are monomeric and they play pivotal roles in the nervous system, including long-term potentiation, dendritic arborization, neurite outgrowth, and the formation of spines, synapses, and axons. In addition, they may be involved in osteoclast differentiation and bone resorption. The CaMKI-delta subfamily is part of a larger superfamily that includes the catalytic domains of other protein kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271070 [Multi-domain]  Cd Length: 301  Bit Score: 179.47  E-value: 4.31e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 7989 YDILEEIGTGAFGVVHRCRERSTGNIFAAKFIPVSHSVEKDL-IRREIDIMNQLHHQKLINLHDAFEDDDEMILILEFLS 8067
Cdd:cd14168    12 FEFKEVLGTGAFSEVVLAEERATGKLFAVKCIPKKALKGKESsIENEIAVLRKIKHENIVALEDIYESPNHLYLVMQLVS 91
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 8068 GGELFERITAEGYvMTEAEVINYMRQICEGIRHMHEQNIIHLDIKPENIMC-QTRSSTNVKLIDFGLATRLDPNEVVKIT 8146
Cdd:cd14168    92 GGELFDRIVEKGF-YTEKDASTLIRQVLDAVYYLHRMGIVHRDLKPENLLYfSQDEESKIMISDFGLSKMEGKGDVMSTA 170
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 8147 TGTAEFAAPEIVNREPVGFYTDMWATGVLSYVLLSGLSPFAGDNDVQTLKNVKACDWDFDVESFKYISEEAKDFIRKLLV 8226
Cdd:cd14168   171 CGTPGYVAPEVLAQKPYSKAVDCWSIGVIAYILLCGYPPFYDENDSKLFEQILKADYEFDSPYWDDISDSAKDFIRNLME 250
                         250       260
                  ....*....|....*....|....*.
gi 281359561 8227 RNKEKRMTAHECLLHPWLTGDHSAMK 8252
Cdd:cd14168   251 KDPNKRYTCEQALRHPWIAGDTALCK 276
STKc_NUAK cd14073
Catalytic domain of the Serine/Threonine Kinase, novel (nua) kinase family NUAK; STKs catalyze ...
7988-8244 6.36e-49

Catalytic domain of the Serine/Threonine Kinase, novel (nua) kinase family NUAK; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. NUAK proteins are classified as AMP-activated protein kinase (AMPK)-related kinases, which like AMPK are activated by the major tumor suppressor LKB1. Vertebrates contain two NUAK proteins, called NUAK1 and NUAK2. NUAK1, also called ARK5 (AMPK-related protein kinase 5), regulates cell proliferation and displays tumor suppression through direct interaction and phosphorylation of p53. It is also involved in cell senescence and motility. High NUAK1 expression is associated with invasiveness of nonsmall cell lung cancer (NSCLC) and breast cancer cells. NUAK2, also called SNARK (Sucrose, non-fermenting 1/AMP-activated protein kinase-related kinase), is involved in energy metabolism. It is activated by hyperosmotic stress, DNA damage, and nutrients such as glucose and glutamine. NUAK2-knockout mice develop obesity, altered serum lipid profiles, hyperinsulinaemia, hyperglycaemia, and impaired glucose tolerance. The NUAK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270975 [Multi-domain]  Cd Length: 254  Bit Score: 177.20  E-value: 6.36e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 7988 RYDILEEIGTGAFGVVHRCRERSTGNIFAAKFIPVSH-SVEKDL--IRREIDIMNQLHHQKLINLHDAFEDDDEMILILE 8064
Cdd:cd14073     2 RYELLETLGKGTYGKVKLAIERATGREVAIKSIKKDKiEDEQDMvrIRREIEIMSSLNHPHIIRIYEVFENKDKIVIVME 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 8065 FLSGGELFERItAEGYVMTEAEVINYMRQICEGIRHMHEQNIIHLDIKPENIMCQtrSSTNVKLIDFGLATRLDPNEVVK 8144
Cdd:cd14073    82 YASGGELYDYI-SERRRLPEREARRIFRQIVSAVHYCHKNGVVHRDLKLENILLD--QNGNAKIADFGLSNLYSKDKLLQ 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 8145 ITTGTAEFAAPEIVNREP-VGFYTDMWATGVLSYVLLSGLSPFAGDNDVQTLKNVKACDWdFDVESfkyiSEEAKDFIRK 8223
Cdd:cd14073   159 TFCGSPLYASPEIVNGTPyQGPEVDCWSLGVLLYTLVYGTMPFDGSDFKRLVKQISSGDY-REPTQ----PSDASGLIRW 233
                         250       260
                  ....*....|....*....|.
gi 281359561 8224 LLVRNKEKRMTAHECLLHPWL 8244
Cdd:cd14073   234 MLTVNPKRRATIEDIANHWWV 254
STKc_DCKL2 cd14184
Catalytic domain of the Serine/Threonine Kinase, Doublecortin-like kinase 2 (also called ...
7987-8243 2.11e-47

Catalytic domain of the Serine/Threonine Kinase, Doublecortin-like kinase 2 (also called Doublecortin-like and CAM kinase-like 2); STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. DCKL2 (or DCAMKL2) belongs to the doublecortin (DCX) family of proteins which are involved in neuronal migration, neurogenesis, and eye receptor development, among others. Family members typically contain tandem doublecortin (DCX) domains at the N-terminus; DCX domains can bind microtubules and serve as protein-interaction platforms. In addition, DCKL2 contains a serine, threonine, and proline rich domain (SP) and a C-terminal kinase domain with similarity to CAMKs. DCKL2 has been shown to interact with tubulin, JIP1/2, JNK, neurabin 2, and actin. It is associated with the terminal segments of axons and dendrites, and may function as a phosphorylation-dependent switch to control microtubule dynamics in neuronal growth cones. The DCKL2 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271086 [Multi-domain]  Cd Length: 259  Bit Score: 173.29  E-value: 2.11e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 7987 DRYDILEEIGTGAFGVVHRCRERSTGNIFAAKFIPVSHSVEKD-LIRREIDIMNQLHHQKLINLHDAFEDDDEMILILEF 8065
Cdd:cd14184     1 EKYKIGKVIGDGNFAVVKECVERSTGKEFALKIIDKAKCCGKEhLIENEVSILRRVKHPNIIMLIEEMDTPAELYLVMEL 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 8066 LSGGELFERITAE-GYVMTEAEVINYmrQICEGIRHMHEQNIIHLDIKPENIM-CQTRSST-NVKLIDFGLATRLD-PNE 8141
Cdd:cd14184    81 VKGGDLFDAITSStKYTERDASAMVY--NLASALKYLHGLCIVHRDIKPENLLvCEYPDGTkSLKLGDFGLATVVEgPLY 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 8142 VVkitTGTAEFAAPEIVNREPVGFYTDMWATGVLSYVLLSGLSPFAGDNDVQT--LKNVKACDWDFDVESFKYISEEAKD 8219
Cdd:cd14184   159 TV---CGTPTYVAPEIIAETGYGLKVDIWAAGVITYILLCGFPPFRSENNLQEdlFDQILLGKLEFPSPYWDNITDSAKE 235
                         250       260
                  ....*....|....*....|....
gi 281359561 8220 FIRKLLVRNKEKRMTAHECLLHPW 8243
Cdd:cd14184   236 LISHMLQVNVEARYTAEQILSHPW 259
STKc_Yank1 cd05578
Catalytic domain of the Serine/Threonine Kinase, Yank1; STKs catalyze the transfer of the ...
7989-8244 3.29e-46

Catalytic domain of the Serine/Threonine Kinase, Yank1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily contains uncharacterized STKs with similarity to the human protein designated as Yank1 or STK32A. The Yank1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270730 [Multi-domain]  Cd Length: 257  Bit Score: 169.74  E-value: 3.29e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 7989 YDILEEIGTGAFGVVHRCRERSTGNIFAAKFIPVSHSVEKDLIR---REIDIMNQLHHQKLINLHDAFEDDDEMILILEF 8065
Cdd:cd05578     2 FQILRVIGKGSFGKVCIVQKKDTKKMFAMKYMNKQKCIEKDSVRnvlNELEILQELEHPFLVNLWYSFQDEEDMYMVVDL 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 8066 LSGGELFERITAEGyVMTEAEVINYMRQICEGIRHMHEQNIIHLDIKPENIMCQTRSstNVKLIDFGLATRLDPNEVVKI 8145
Cdd:cd05578    82 LLGGDLRYHLQQKV-KFSEETVKFYICEIVLALDYLHSKNIIHRDIKPDNILLDEQG--HVHITDFNIATKLTDGTLATS 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 8146 TTGTAEFAAPEIVNREPVGFYTDMWATGVLSYVLLSGLSPFAGdNDVQTLKNVKACDWDFDVESFKYISEEAKDFIRKLL 8225
Cdd:cd05578   159 TSGTKPYMAPEVFMRAGYSFAVDWWSLGVTAYEMLRGKRPYEI-HSRTSIEEIRAKFETASVLYPAGWSEEAIDLINKLL 237
                         250       260
                  ....*....|....*....|
gi 281359561 8226 VRNKEKRMTAHECLL-HPWL 8244
Cdd:cd05578   238 ERDPQKRLGDLSDLKnHPYF 257
STKc_AMPK_alpha cd14079
Catalytic domain of the Alpha subunit of the Serine/Threonine Kinase, AMP-activated protein ...
7989-8244 4.57e-46

Catalytic domain of the Alpha subunit of the Serine/Threonine Kinase, AMP-activated protein kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. AMPK, also called SNF1 (sucrose non-fermenting1) in yeasts and SnRK1 (SNF1-related kinase1) in plants, is a heterotrimeric enzyme composed of a catalytic alpha subunit and two regulatory subunits, beta and gamma. It is a stress-activated kinase that serves as master regulator of glucose and lipid metabolism by monitoring carbon and energy supplies, via sensing the cell's AMP:ATP ratio. In response to decreased ATP levels, it enhances energy-producing processes and inhibits energy-consuming pathways. Once activated, AMPK phosphorylates a broad range of downstream targets, with effects in carbohydrate metabolism and uptake, lipid and fatty acid biosynthesis, carbon energy storage, and inflammation, among others. Defects in energy homeostasis underlie many human diseases including Type 2 diabetes, obesity, heart disease, and cancer. As a result, AMPK has emerged as a therapeutic target in the treatment of these diseases. The AMPK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270981 [Multi-domain]  Cd Length: 256  Bit Score: 168.99  E-value: 4.57e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 7989 YDILEEIGTGAFGVVHRCRERSTGNIFAAKF-----IPVSHSVEKdlIRREIDIMNQLHHQKLINLHDAFEDDDEMILIL 8063
Cdd:cd14079     4 YILGKTLGVGSFGKVKLAEHELTGHKVAVKIlnrqkIKSLDMEEK--IRREIQILKLFRHPHIIRLYEVIETPTDIFMVM 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 8064 EFLSGGELFERITAEGYvMTEAEVINYMRQICEGIRHMHEQNIIHLDIKPENIMCQTRSstNVKLIDFGLATRLDPNEVV 8143
Cdd:cd14079    82 EYVSGGELFDYIVQKGR-LSEDEARRFFQQIISGVEYCHRHMVVHRDLKPENLLLDSNM--NVKIADFGLSNIMRDGEFL 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 8144 KITTGTAEFAAPEIVN-REPVGFYTDMWATGVLSYVLLSGLSPFaGDNDVQTL-KNVKACdwDFDVESfkYISEEAKDFI 8221
Cdd:cd14079   159 KTSCGSPNYAAPEVISgKLYAGPEVDVWSCGVILYALLCGSLPF-DDEHIPNLfKKIKSG--IYTIPS--HLSPGARDLI 233
                         250       260
                  ....*....|....*....|...
gi 281359561 8222 RKLLVRNKEKRMTAHECLLHPWL 8244
Cdd:cd14079   234 KRMLVVDPLKRITIPEIRQHPWF 256
STKc_PhKG1 cd14182
Catalytic domain of the Serine/Threonine Kinase, Phosphorylase kinase Gamma 1 subunit; STKs ...
7986-8244 4.88e-46

Catalytic domain of the Serine/Threonine Kinase, Phosphorylase kinase Gamma 1 subunit; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Phosphorylase kinase (PhK) catalyzes the phosphorylation of inactive phosphorylase b to form the active phosphorylase a. It coordinates hormonal, metabolic, and neuronal signals to initiate the breakdown of glycogen stores, which enables the maintenance of blood-glucose homeostasis during fasting, and is also used as a source of energy for muscle contraction. PhK is one of the largest and most complex protein kinases, composed of a heterotetramer containing four molecules each of four subunit types: one catalytic (gamma) and three regulatory (alpha, beta, and delta). The gamma 1 subunit (PhKG1) is also referred to as the muscle gamma isoform. The gamma subunit, when isolated, is constitutively active and does not require phosphorylation of the A-loop for activity. The regulatory subunits restrain this kinase activity until signals are received to relieve this inhibition. For example, the kinase is activated in response to hormonal stimulation, after autophosphorylation or phosphorylation by cAMP-dependent kinase of the alpha and beta subunits. The high-affinity binding of ADP to the beta subunit also stimulates kinase activity, whereas calcium relieves inhibition by binding to the delta (calmodulin) subunit. The PhKG1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271084 [Multi-domain]  Cd Length: 276  Bit Score: 169.71  E-value: 4.88e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 7986 YDRYDILEEIGTGAFGVVHRCRERSTGNIFAAKFIPV--SHSVEKDLIR-------REIDIMNQLH-HQKLINLHDAFED 8055
Cdd:cd14182     2 YEKYEPKEILGRGVSSVVRRCIHKPTRQEYAVKIIDItgGGSFSPEEVQelreatlKEIDILRKVSgHPNIIQLKDTYET 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 8056 DDEMILILEFLSGGELFERITaEGYVMTEAEVINYMRQICEGIRHMHEQNIIHLDIKPENIMCQtrSSTNVKLIDFGLAT 8135
Cdd:cd14182    82 NTFFFLVFDLMKKGELFDYLT-EKVTLSEKETRKIMRALLEVICALHKLNIVHRDLKPENILLD--DDMNIKLTDFGFSC 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 8136 RLDPNEVVKITTGTAEFAAPEIV------NREPVGFYTDMWATGVLSYVLLSGLSPFAGDNDVQTLKNVKACDWDFDVES 8209
Cdd:cd14182   159 QLDPGEKLREVCGTPGYLAPEIIecsmddNHPGYGKEVDMWSTGVIMYTLLAGSPPFWHRKQMLMLRMIMSGNYQFGSPE 238
                         250       260       270
                  ....*....|....*....|....*....|....*
gi 281359561 8210 FKYISEEAKDFIRKLLVRNKEKRMTAHECLLHPWL 8244
Cdd:cd14182   239 WDDRSDTVKDLISRFLVVQPQKRYTAEEALAHPFF 273
STKc_MAPKAPK cd14089
Catalytic domain of the Serine/Threonine kinases, Mitogen-activated protein kinase-activated ...
7989-8243 7.40e-46

Catalytic domain of the Serine/Threonine kinases, Mitogen-activated protein kinase-activated protein kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily is composed of the MAPK-activated protein kinases MK2, MK3, MK5 (also called PRAK for p38-regulated/activated protein kinase), and related proteins. These proteins contain a catalytic kinase domain followed by a C-terminal autoinhibitory region that contains nuclear localization (NLS) and nuclear export (NES) signals with a p38 MAPK docking motif that overlaps the NLS. In addition, MK2 and MK3 contain an N-terminal proline-rich region that can bind to SH3 domains. MK2 and MK3 are bonafide substrates for the MAPK p38, while MK5 plays a functional role in the p38 MAPK pathway although their direct interaction has been difficult to detect. MK2 and MK3 are closely related and show, thus far, indistinguishable substrate specificity, while MK5 shows a distinct spectrum of substrates. MK2 and MK3 are mainly involved in the regulation of gene expression and they participate in diverse cellular processes such as endocytosis, cytokine production, cytoskeletal reorganization, cell migration, cell cycle control and chromatin remodeling. They are implicated in inflammation and cance and their substrates include mRNA-AU-rich-element (ARE)-binding proteins (TTP and hnRNP A0), Hsp proteins (Hsp27 and Hsp25) and RSK, among others. MK2/3 are both expressed ubiquitously but MK2 is expressed at significantly higher levels. MK5 is a ubiquitous protein that is implicated in neuronal morphogenesis, cell migration, and tumor angiogenesis. It interacts with PKA, which induces cytoplasmic translocation of MK5. Its substrates includes p53, ERK3/4, Hsp27, and cytosolic phospholipase A2 (cPLA2). The MAPKAPK subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270991 [Multi-domain]  Cd Length: 263  Bit Score: 168.62  E-value: 7.40e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 7989 YDILEEI-GTGAFGVVHRCRERSTGNIFAAKfipVSHSVEKDliRREIDimnqLH-----HQKLINLHDAFE----DDDE 8058
Cdd:cd14089     2 YTISKQVlGLGINGKVLECFHKKTGEKFALK---VLRDNPKA--RREVE----LHwrasgCPHIVRIIDVYEntyqGRKC 72
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 8059 MILILEFLSGGELFERI--TAEGYvMTEAEVINYMRQICEGIRHMHEQNIIHLDIKPENIMCQTRS-STNVKLIDFGLAT 8135
Cdd:cd14089    73 LLVVMECMEGGELFSRIqeRADSA-FTEREAAEIMRQIGSAVAHLHSMNIAHRDLKPENLLYSSKGpNAILKLTDFGFAK 151
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 8136 RLDPNEVVKITTGTAEFAAPEIVNREPVGFYTDMWATGVLSYVLLSGLSPFAGDNDVQ----TLKNVKACDWDFDVESFK 8211
Cdd:cd14089   152 ETTTKKSLQTPCYTPYYVAPEVLGPEKYDKSCDMWSLGVIMYILLCGYPPFYSNHGLAispgMKKRIRNGQYEFPNPEWS 231
                         250       260       270
                  ....*....|....*....|....*....|..
gi 281359561 8212 YISEEAKDFIRKLLVRNKEKRMTAHECLLHPW 8243
Cdd:cd14089   232 NVSEEAKDLIRGLLKTDPSERLTIEEVMNHPW 263
STKc_RCK1-like cd14096
Catalytic domain of RCK1-like Serine/Threonine Kinases; STKs catalyze the transfer of the ...
7988-8244 5.29e-45

Catalytic domain of RCK1-like Serine/Threonine Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily is composed of fungal STKs including Saccharomyces cerevisiae RCK1 and RCK2, Schizosaccharomyces pombe Sty1-regulated kinase 1 (Srk1), and similar proteins. RCK1, RCK2 (or Rck2p), and Srk1 are MAPK-activated protein kinases. RCK1 and RCK2 are involved in oxidative and metal stress resistance in budding yeast. RCK2 also regulates rapamycin sensitivity in both S. cerevisiae and Candida albicans. Srk1 is activated by Sty1/Spc1 and is involved in negatively regulating cell cycle progression by inhibiting Cdc25. The RCK1-like subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270998 [Multi-domain]  Cd Length: 295  Bit Score: 167.61  E-value: 5.29e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 7988 RYDILEEIGTGAFGVVHRCR-ERSTGNIFAAKFIP-------VSHSVEKDLIRREIDIMNQLHHQKLINLHDAFEDDDEM 8059
Cdd:cd14096     2 NYRLINKIGEGAFSNVYKAVpLRNTGKPVAIKVVRkadlssdNLKGSSRANILKEVQIMKRLSHPNIVKLLDFQESDEYY 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 8060 ILILEFLSGGELFERITAEGYvMTEAEVINYMRQICEGIRHMHEQNIIHLDIKPENIMCQT-----------RSSTN--- 8125
Cdd:cd14096    82 YIVLELADGGEIFHQIVRLTY-FSEDLSRHVITQVASAVKYLHEIGVVHRDIKPENLLFEPipfipsivklrKADDDetk 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 8126 -----------------VKLIDFGLATRLDPNEVvKITTGTAEFAAPEIVNREPVGFYTDMWATGVLSYVLLSGLSPFAG 8188
Cdd:cd14096   161 vdegefipgvggggigiVKLADFGLSKQVWDSNT-KTPCGTVGYTAPEVVKDERYSKKVDMWALGCVLYTLLCGFPPFYD 239
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 281359561 8189 DNDVQTLKNVKACDWDFDVESFKYISEEAKDFIRKLLVRNKEKRMTAHECLLHPWL 8244
Cdd:cd14096   240 ESIETLTEKISRGDYTFLSPWWDEISKSAKDLISHLLTVDPAKRYDIDEFLAHPWI 295
STKc_MELK cd14078
Catalytic domain of the Serine/Threonine Kinase, Maternal Embryonic Leucine zipper Kinase; ...
7987-8244 8.67e-45

Catalytic domain of the Serine/Threonine Kinase, Maternal Embryonic Leucine zipper Kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MELK is a cell cycle dependent protein which functions in cytokinesis, cell cycle, apoptosis, cell proliferation, and mRNA processing. It is found upregulated in many types of cancer cells, playing an indispensable role in cancer cell survival. It makes an attractive target in the design of inhibitors for use in the treatment of a wide range of human cancer. The MELK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270980 [Multi-domain]  Cd Length: 257  Bit Score: 165.63  E-value: 8.67e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 7987 DRYDILEEIGTGAFGVVHRCRERSTGNIFAAKfIPVSHSVEKDL--IRREIDIMNQLHHQKLINLHDAFEDDDEMILILE 8064
Cdd:cd14078     3 KYYELHETIGSGGFAKVKLATHILTGEKVAIK-IMDKKALGDDLprVKTEIEALKNLSHQHICRLYHVIETDNKIFMVLE 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 8065 FLSGGELFERITAEGYvMTEAEVINYMRQICEGIRHMHEQNIIHLDIKPENIMCQTRSstNVKLIDFGLATRLDPNEVVK 8144
Cdd:cd14078    82 YCPGGELFDYIVAKDR-LSEDEARVFFRQIVSAVAYVHSQGYAHRDLKPENLLLDEDQ--NLKLIDFGLCAKPKGGMDHH 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 8145 ITT--GTAEFAAPEIVNREP-VGFYTDMWATGVLSYVLLSGLSPFAGDNDVQTLKNVKACDWDFDvesfKYISEEAKDFI 8221
Cdd:cd14078   159 LETccGSPAYAAPELIQGKPyIGSEADVWSMGVLLYALLCGFLPFDDDNVMALYRKIQSGKYEEP----EWLSPSSKLLL 234
                         250       260
                  ....*....|....*....|...
gi 281359561 8222 RKLLVRNKEKRMTAHECLLHPWL 8244
Cdd:cd14078   235 DQMLQVDPKKRITVKELLNHPWV 257
STKc_PAK cd06614
Catalytic domain of the Serine/Threonine Kinase, p21-activated kinase; STKs catalyze the ...
7989-8245 1.29e-44

Catalytic domain of the Serine/Threonine Kinase, p21-activated kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PAKs are Rho family GTPase-regulated kinases that serve as important mediators in the function of Cdc42 (cell division cycle 42) and Rac. PAKs are implicated in the regulation of many cellular processes including growth factor receptor-mediated proliferation, cell polarity, cell motility, cell death and survival, and actin cytoskeleton organization. PAK deregulation is associated with tumor development. PAKs from higher eukaryotes are classified into two groups (I and II), according to their biochemical and structural features. Group I PAKs contain a PBD (p21-binding domain) overlapping with an AID (autoinhibitory domain), a C-terminal catalytic domain, SH3 binding sites and a non-classical SH3 binding site for PIX (PAK-interacting exchange factor). Group II PAKs contain a PBD and a catalytic domain, but lack other motifs found in group I PAKs. Since group II PAKs do not contain an obvious AID, they may be regulated differently from group I PAKs. Group I PAKs interact with the SH3 containing proteins Nck, Grb2 and PIX; no such binding has been demonstrated for group II PAKs. The PAK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270789 [Multi-domain]  Cd Length: 255  Bit Score: 165.08  E-value: 1.29e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 7989 YDILEEIGTGAFGVVHRCRERSTGNIFAAKFIPVShSVEKDLIRREIDIMNQLHHQKLINLHDAFEDDDEMILILEFLSG 8068
Cdd:cd06614     2 YKNLEKIGEGASGEVYKATDRATGKEVAIKKMRLR-KQNKELIINEILIMKECKHPNIVDYYDSYLVGDELWVVMEYMDG 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 8069 GELFERITAEGYVMTEAEVINYMRQICEGIRHMHEQNIIHLDIKPENIMCQtrSSTNVKLIDFGLATRLDPnEVVKITT- 8147
Cdd:cd06614    81 GSLTDIITQNPVRMNESQIAYVCREVLQGLEYLHSQNVIHRDIKSDNILLS--KDGSVKLADFGFAAQLTK-EKSKRNSv 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 8148 -GTAEFAAPEIVNREPVGFYTDMWATGVLSYVLLSGLSPFAGDNDVQTLKNVkACDWDFDVESFKYISEEAKDFIRKLLV 8226
Cdd:cd06614   158 vGTPYWMAPEVIKRKDYGPKVDIWSLGIMCIEMAEGEPPYLEEPPLRALFLI-TTKGIPPLKNPEKWSPEFKDFLNKCLV 236
                         250
                  ....*....|....*....
gi 281359561 8227 RNKEKRMTAHECLLHPWLT 8245
Cdd:cd06614   237 KDPEKRPSAEELLQHPFLK 255
STKc_MSK1_C cd14179
C-terminal catalytic domain of the Serine/Threonine Kinase, Mitogen and stress-activated ...
7986-8247 4.66e-44

C-terminal catalytic domain of the Serine/Threonine Kinase, Mitogen and stress-activated kinase 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MSK1 plays a role in the regulation of translational control and transcriptional activation. It phosphorylates the transcription factors, CREB and NFkB. It also phosphorylates the nucleosomal proteins H3 and HMG-14. Increased phosphorylation of MSK1 is associated with the development of cerebral ischemic/hypoxic preconditioning. MSKs contain an N-terminal kinase domain (NTD) from the AGC family and a C-terminal kinase domain (CTD) from the CAMK family. MSKs are activated by two major signaling cascades, the Ras-MAPK and p38 stress kinase pathways, which trigger phosphorylation in the activation loop (A-loop) of the CTD of MSK. The active CTD phosphorylates the hydrophobic motif (HM) of NTD, which facilitates the phosphorylation of the A-loop and activates the NTD, which in turn phosphorylates downstream targets. The MSK1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271081 [Multi-domain]  Cd Length: 310  Bit Score: 165.21  E-value: 4.66e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 7986 YDRYDI-LEE--IGTGAFGVVHRCRERSTGNIFAAKFIpvSHSVEKDlIRREIDIMNQLH-HQKLINLHDAFEDDDEMIL 8061
Cdd:cd14179     3 YQHYELdLKDkpLGEGSFSICRKCLHKKTNQEYAVKIV--SKRMEAN-TQREIAALKLCEgHPNIVKLHEVYHDQLHTFL 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 8062 ILEFLSGGELFERITAEGYvMTEAEVINYMRQICEGIRHMHEQNIIHLDIKPENIMCQTRS-STNVKLIDFGLAtRLDP- 8139
Cdd:cd14179    80 VMELLKGGELLERIKKKQH-FSETEASHIMRKLVSAVSHMHDVGVVHRDLKPENLLFTDESdNSEIKIIDFGFA-RLKPp 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 8140 -NEVVKITTGTAEFAAPEIVNREPVGFYTDMWATGVLSYVLLSGLSPFAGDND-------VQTLKNVKACDWDFDVESFK 8211
Cdd:cd14179   158 dNQPLKTPCFTLHYAAPELLNYNGYDESCDLWSLGVILYTMLSGQVPFQCHDKsltctsaEEIMKKIKQGDFSFEGEAWK 237
                         250       260       270
                  ....*....|....*....|....*....|....*.
gi 281359561 8212 YISEEAKDFIRKLLVRNKEKRMTAHECLLHPWLTGD 8247
Cdd:cd14179   238 NVSQEAKDLIQGLLTVDPNKRIKMSGLRYNEWLQDG 273
STKc_PhKG2 cd14181
Catalytic domain of the Serine/Threonine Kinase, Phosphorylase kinase Gamma 2 subunit; STKs ...
7986-8244 5.31e-44

Catalytic domain of the Serine/Threonine Kinase, Phosphorylase kinase Gamma 2 subunit; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Phosphorylase kinase (PhK) catalyzes the phosphorylation of inactive phosphorylase b to form the active phosphorylase a. It coordinates hormonal, metabolic, and neuronal signals to initiate the breakdown of glycogen stores, which enables the maintenance of blood-glucose homeostasis during fasting, and is also used as a source of energy for muscle contraction. PhK is one of the largest and most complex protein kinases, composed of a heterotetramer containing four molecules each of four subunit types: one catalytic (gamma) and three regulatory (alpha, beta, and delta). The gamma 2 subunit (PhKG2) is also referred to as the testis/liver gamma isoform. Mutations in its gene cause autosomal-recessive glycogenosis of the liver. The gamma subunit, when isolated, is constitutively active and does not require phosphorylation of the A-loop for activity. The regulatory subunits restrain this kinase activity until signals are received to relieve this inhibition. For example, the kinase is activated in response to hormonal stimulation, after autophosphorylation or phosphorylation by cAMP-dependent kinase of the alpha and beta subunits. The high-affinity binding of ADP to the beta subunit also stimulates kinase activity, whereas calcium relieves inhibition by binding to the delta (calmodulin) subunit. The PhKG2 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271083 [Multi-domain]  Cd Length: 279  Bit Score: 163.99  E-value: 5.31e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 7986 YDRYDILEEIGTGAFGVVHRCRERSTGNIFAAKFIPVS------HSVE--KDLIRREIDIMNQLH-HQKLINLHDAFEDD 8056
Cdd:cd14181     9 YQKYDPKEVIGRGVSSVVRRCVHRHTGQEFAVKIIEVTaerlspEQLEevRSSTLKEIHILRQVSgHPSIITLIDSYESS 88
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 8057 DEMILILEFLSGGELFERITaEGYVMTEAEVINYMRQICEGIRHMHEQNIIHLDIKPENIMCQtrSSTNVKLIDFGLATR 8136
Cdd:cd14181    89 TFIFLVFDLMRRGELFDYLT-EKVTLSEKETRSIMRSLLEAVSYLHANNIVHRDLKPENILLD--DQLHIKLSDFGFSCH 165
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 8137 LDPNEVVKITTGTAEFAAPEIV------NREPVGFYTDMWATGVLSYVLLSGLSPFAGDNDVQTLKNVKACDWDFDVESF 8210
Cdd:cd14181   166 LEPGEKLRELCGTPGYLAPEILkcsmdeTHPGYGKEVDLWACGVILFTLLAGSPPFWHRRQMLMLRMIMEGRYQFSSPEW 245
                         250       260       270
                  ....*....|....*....|....*....|....
gi 281359561 8211 KYISEEAKDFIRKLLVRNKEKRMTAHECLLHPWL 8244
Cdd:cd14181   246 DDRSSTVKDLISRLLVVDPEIRLTAEQALQHPFF 279
STKc_DCKL1 cd14183
Catalytic domain of the Serine/Threonine Kinase, Doublecortin-like kinase 1 (also called ...
7984-8247 1.22e-43

Catalytic domain of the Serine/Threonine Kinase, Doublecortin-like kinase 1 (also called Doublecortin-like and CAM kinase-like 1); STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. DCKL1 (or DCAMKL1) belongs to the doublecortin (DCX) family of proteins which are involved in neuronal migration, neurogenesis, and eye receptor development, among others. Family members typically contain tandem doublecortin (DCX) domains at the N-terminus; DCX domains can bind microtubules and serve as protein-interaction platforms. In addition, DCKL1 contains a serine, threonine, and proline rich domain (SP) and a C-terminal kinase domain with similarity to CAMKs. DCKL1 interacts with tubulin, glucocorticoid receptor, dynein, JIP1/2, caspases (3 and 8), and calpain, among others. It plays roles in neurogenesis, neuronal migration, retrograde transport, and neuronal apoptosis. The DCKL1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271085 [Multi-domain]  Cd Length: 268  Bit Score: 162.47  E-value: 1.22e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 7984 SVYDRYDILEEIGTGAFGVVHRCRERSTGNIFAAKFIPVSHSVEKD-LIRREIDIMNQLHHQKLINLHDAFEDDDEMILI 8062
Cdd:cd14183     3 SISERYKVGRTIGDGNFAVVKECVERSTGREYALKIINKSKCRGKEhMIQNEVSILRRVKHPNIVLLIEEMDMPTELYLV 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 8063 LEFLSGGELFERITAEGYvMTEAEVINYMRQICEGIRHMHEQNIIHLDIKPENIMC--QTRSSTNVKLIDFGLATRLDPN 8140
Cdd:cd14183    83 MELVKGGDLFDAITSTNK-YTERDASGMLYNLASAIKYLHSLNIVHRDIKPENLLVyeHQDGSKSLKLGDFGLATVVDGP 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 8141 evVKITTGTAEFAAPEIVNREPVGFYTDMWATGVLSYVLLSGLSPFAGDNDVQT--LKNVKACDWDFDVESFKYISEEAK 8218
Cdd:cd14183   162 --LYTVCGTPTYVAPEIIAETGYGLKVDIWAAGVITYILLCGFPPFRGSGDDQEvlFDQILMGQVDFPSPYWDNVSDSAK 239
                         250       260
                  ....*....|....*....|....*....
gi 281359561 8219 DFIRKLLVRNKEKRMTAHECLLHPWLTGD 8247
Cdd:cd14183   240 ELITMMLQVDVDQRYSALQVLEHPWVNDD 268
STKc_CMGC cd05118
Catalytic domain of CMGC family Serine/Threonine Kinases; STKs catalyze the transfer of the ...
7989-8244 1.40e-43

Catalytic domain of CMGC family Serine/Threonine Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The CMGC family consists of Cyclin-Dependent protein Kinases (CDKs), Mitogen-activated protein kinases (MAPKs) such as Extracellular signal-regulated kinase (ERKs), c-Jun N-terminal kinases (JNKs), and p38, and other kinases. CDKs belong to a large subfamily of STKs that are regulated by their cognate cyclins. Together, they are involved in the control of cell-cycle progression, transcription, and neuronal function. MAPKs serve as important mediators of cellular responses to extracellular signals. They control critical cellular functions including differentiation, proliferation, migration, and apoptosis. They are also implicated in the pathogenesis of many diseases including multiple types of cancer, stroke, diabetes, and chronic inflammation. Other members of the CMGC family include casein kinase 2 (CK2), Dual-specificity tYrosine-phosphorylated and -Regulated Kinase (DYRK), Glycogen Synthase Kinase 3 (GSK3), among many others. The CMGC family is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270688 [Multi-domain]  Cd Length: 249  Bit Score: 161.63  E-value: 1.40e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 7989 YDILEEIGTGAFGVVHRCRERSTGNIFAAKFIpVSHSVEKDLIRREIDIMNQL----HHQKLINLHDAFEDDDE--MILI 8062
Cdd:cd05118     1 YEVLRKIGEGAFGTVWLARDKVTGEKVAIKKI-KNDFRHPKAALREIKLLKHLndveGHPNIVKLLDVFEHRGGnhLCLV 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 8063 LEFLsGGELFERITAEGYVMTEAEVINYMRQICEGIRHMHEQNIIHLDIKPENIMCQTRSSTnVKLIDFGLATRLDPNEV 8142
Cdd:cd05118    80 FELM-GMNLYELIKDYPRGLPLDLIKSYLYQLLQALDFLHSNGIIHRDLKPENILINLELGQ-LKLADFGLARSFTSPPY 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 8143 VkITTGTAEFAAPE-IVNREPVGFYTDMWATGVLSYVLLSGLSPFAGDNDVQTLKNVkacdwdFDVESfkyiSEEAKDFI 8221
Cdd:cd05118   158 T-PYVATRWYRAPEvLLGAKPYGSSIDIWSLGCILAELLTGRPLFPGDSEVDQLAKI------VRLLG----TPEALDLL 226
                         250       260
                  ....*....|....*....|...
gi 281359561 8222 RKLLVRNKEKRMTAHECLLHPWL 8244
Cdd:cd05118   227 SKMLKYDPAKRITASQALAHPYF 249
STKc_Cdc7_like cd06627
Catalytic domain of Cell division control protein 7-like Serine/Threonine Kinases; STKs ...
7988-8244 3.89e-43

Catalytic domain of Cell division control protein 7-like Serine/Threonine Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Members of this subfamily include Schizosaccharomyces pombe Cdc7, Saccharomyces cerevisiae Cdc15, Arabidopsis thaliana mitogen-activated protein kinase kinase kinase (MAPKKK) epsilon, and related proteins. MAPKKKs phosphorylate and activate MAPK kinases, which in turn phosphorylate and activate MAPKs during signaling cascades that are important in mediating cellular responses to extracellular signals. Fission yeast Cdc7 is essential for cell division by playing a key role in the initiation of septum formation and cytokinesis. Budding yeast Cdc15 functions to coordinate mitotic exit with cytokinesis. Arabidopsis MAPKKK epsilon is required for pollen development in the plasma membrane. The Cdc7-like subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270797 [Multi-domain]  Cd Length: 254  Bit Score: 160.47  E-value: 3.89e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 7988 RYDILEEIGTGAFGVVHRCRERSTGNIFAAKFIPVSHSVEKDL--IRREIDIMNQLHHQKLINLHDAFEDDDEMILILEF 8065
Cdd:cd06627     1 NYQLGDLIGRGAFGSVYKGLNLNTGEFVAIKQISLEKIPKSDLksVMGEIDLLKKLNHPNIVKYIGSVKTKDSLYIILEY 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 8066 LSGGELFERITAEGYvMTEAEVINYMRQICEGIRHMHEQNIIHLDIKPENIMcqTRSSTNVKLIDFGLATRL-----DPN 8140
Cdd:cd06627    81 VENGSLASIIKKFGK-FPESLVAVYIYQVLEGLAYLHEQGVIHRDIKGANIL--TTKDGLVKLADFGVATKLnevekDEN 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 8141 EVVkittGTAEFAAPEIVNREPVGFYTDMWATGVLSYVLLSGLSPFAGDNDVQTLKNVkacdwdfdVESF-----KYISE 8215
Cdd:cd06627   158 SVV----GTPYWMAPEVIEMSGVTTASDIWSVGCTVIELLTGNPPYYDLQPMAALFRI--------VQDDhpplpENISP 225
                         250       260
                  ....*....|....*....|....*....
gi 281359561 8216 EAKDFIRKLLVRNKEKRMTAHECLLHPWL 8244
Cdd:cd06627   226 ELRDFLLQCFQKDPTLRPSAKELLKHPWL 254
STKc_p70S6K cd05584
Catalytic domain of the Serine/Threonine Kinase, 70 kDa ribosomal protein S6 kinase; STKs ...
7992-8264 5.64e-43

Catalytic domain of the Serine/Threonine Kinase, 70 kDa ribosomal protein S6 kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. p70S6K (or S6K) contains only one catalytic kinase domain, unlike p90 ribosomal S6 kinases (RSKs). It acts as a downstream effector of the STK mTOR (mammalian Target of Rapamycin) and plays a role in the regulation of the translation machinery during protein synthesis. p70S6K also plays a pivotal role in regulating cell size and glucose homeostasis. Its targets include S6, the translation initiation factor eIF3, and the insulin receptor substrate IRS-1, among others. Mammals contain two isoforms of p70S6K, named S6K1 and S6K2 (or S6K-beta). The p70S6K subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270736 [Multi-domain]  Cd Length: 323  Bit Score: 162.57  E-value: 5.64e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 7992 LEEIGTGAFGVVHRCRERST---GNIFAAKFIPVSHSV--EKDLI--RREIDIMNQLHHQKLINLHDAFEDDDEMILILE 8064
Cdd:cd05584     1 LKVLGKGGYGKVFQVRKTTGsdkGKIFAMKVLKKASIVrnQKDTAhtKAERNILEAVKHPFIVDLHYAFQTGGKLYLILE 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 8065 FLSGGELFERITAEGYVMtEAEVINYMRQICEGIRHMHEQNIIHLDIKPENIMCQtrSSTNVKLIDFGLAT-RLDPNEVV 8143
Cdd:cd05584    81 YLSGGELFMHLEREGIFM-EDTACFYLAEITLALGHLHSLGIIYRDLKPENILLD--AQGHVKLTDFGLCKeSIHDGTVT 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 8144 KITTGTAEFAAPEIVNREPVGFYTDMWATGVLSYVLLSGLSPFAGDNDVQTLKNVKACDWDFDvesfKYISEEAKDFIRK 8223
Cdd:cd05584   158 HTFCGTIEYMAPEILTRSGHGKAVDWWSLGALMYDMLTGAPPFTAENRKKTIDKILKGKLNLP----PYLTNEARDLLKK 233
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*.
gi 281359561 8224 LLVRNKEKRM-----TAHECLLHPWLtgdhsamkQEINRDRYLAYR 8264
Cdd:cd05584   234 LLKRNVSSRLgsgpgDAEEIKAHPFF--------RHINWDDLLAKK 271
STKc_MAST_like cd05579
Catalytic domain of Microtubule-associated serine/threonine (MAST) kinase-like proteins; STKs ...
7995-8246 6.99e-43

Catalytic domain of Microtubule-associated serine/threonine (MAST) kinase-like proteins; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily includes MAST kinases, MAST-like (MASTL) kinases (also called greatwall kinase or Gwl), and fungal kinases with similarity to Saccharomyces cerevisiae Rim15 and Schizosaccharomyces pombe cek1. MAST kinases contain an N-terminal domain of unknown function, a central catalytic domain, and a C-terminal PDZ domain that mediates protein-protein interactions. MASTL kinases carry only a catalytic domain which contains a long insert relative to other kinases. The fungal kinases in this subfamily harbor other domains in addition to a central catalytic domain, which like in MASTL, also contains an insert relative to MAST kinases. Rim15 contains a C-terminal signal receiver (REC) domain while cek1 contains an N-terminal PAS domain. MAST kinases are cytoskeletal associated kinases of unknown function that are also expressed at neuromuscular junctions and postsynaptic densities. MASTL/Gwl is involved in the regulation of mitotic entry, mRNA stabilization, and DNA checkpoint recovery. The fungal proteins Rim15 and cek1 are involved in the regulation of meiosis and mitosis, respectively. The MAST-like kinase subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270731 [Multi-domain]  Cd Length: 272  Bit Score: 160.46  E-value: 6.99e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 7995 IGTGAFGVVHRCRERSTGNIFAAKFIPVSHSVEKDLIRR---EIDIMNQLHHQKLINLHDAFEDDDEMILILEFLSGGEL 8071
Cdd:cd05579     1 ISRGAYGRVYLAKKKSTGDLYAIKVIKKRDMIRKNQVDSvlaERNILSQAQNPFVVKLYYSFQGKKNLYLVMEYLPGGDL 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 8072 FERITAEGYvMTEAEVINYMRQICEGIRHMHEQNIIHLDIKPENIMCQtrSSTNVKLIDFGL----------------AT 8135
Cdd:cd05579    81 YSLLENVGA-LDEDVARIYIAEIVLALEYLHSHGIIHRDLKPDNILID--ANGHLKLTDFGLskvglvrrqiklsiqkKS 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 8136 RLDPNEVVKITTGTAEFAAPEIVNREPVGFYTDMWATGVLSYVLLSGLSPFAGDNDVQTLKNVkaCDWDFDVESFKYISE 8215
Cdd:cd05579   158 NGAPEKEDRRIVGTPDYLAPEILLGQGHGKTVDWWSLGVILYEFLVGIPPFHAETPEEIFQNI--LNGKIEWPEDPEVSD 235
                         250       260       270
                  ....*....|....*....|....*....|....
gi 281359561 8216 EAKDFIRKLLVRNKEKRM---TAHECLLHPWLTG 8246
Cdd:cd05579   236 EAKDLISKLLTPDPEKRLgakGIEEIKNHPFFKG 269
STKc_Chk1 cd14069
Catalytic domain of the Serine/Threonine kinase, Checkpoint kinase 1; STKs catalyze the ...
7989-8244 2.03e-42

Catalytic domain of the Serine/Threonine kinase, Checkpoint kinase 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Chk1 is implicated in many major checkpoints of the cell cycle, providing a link between upstream sensors and the cell cycle engine. It plays an important role in DNA damage response and maintaining genomic stability. Chk1 acts as an effector of the sensor kinase, ATR (ATM and Rad3-related), a member of the PI3K family, which is activated upon DNA replication stress. Chk1 delays mitotic entry in response to replication blocks by inhibiting cyclin dependent kinase (Cdk) activity. In addition, Chk1 contributes to the function of centrosome and spindle-based checkpoints, inhibits firing of origins of DNA replication (Ori), and represses transcription of cell cycle proteins including cyclin B and Cdk1. The Chk1 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270971 [Multi-domain]  Cd Length: 261  Bit Score: 158.65  E-value: 2.03e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 7989 YDILEEIGTGAFGVVHRCRERSTGNIFAAKFIPVSHSVEKDL--IRREIDIMNQLHHQKLINLHDAFEDDDEMILILEFL 8066
Cdd:cd14069     3 WDLVQTLGEGAFGEVFLAVNRNTEEAVAVKFVDMKRAPGDCPenIKKEVCIQKMLSHKNVVRFYGHRREGEFQYLFLEYA 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 8067 SGGELFERITAEgYVMTEAEVINYMRQICEGIRHMHEQNIIHLDIKPENIMCQtrSSTNVKLIDFGLATRL---DPNEVV 8143
Cdd:cd14069    83 SGGELFDKIEPD-VGMPEDVAQFYFQQLMAGLKYLHSCGITHRDIKPENLLLD--ENDNLKISDFGLATVFrykGKERLL 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 8144 KITTGTAEFAAPEIVNREPV-GFYTDMWATGVLSYVLLSGLSPFagdnDVQTLKNVKACDWDFDvESFKY-----ISEEA 8217
Cdd:cd14069   160 NKMCGTLPYVAPELLAKKKYrAEPVDVWSCGIVLFAMLAGELPW----DQPSDSCQEYSDWKEN-KKTYLtpwkkIDTAA 234
                         250       260
                  ....*....|....*....|....*..
gi 281359561 8218 KDFIRKLLVRNKEKRMTAHECLLHPWL 8244
Cdd:cd14069   235 LSLLRKILTENPNKRITIEDIKKHPWY 261
STKc_PKA_like cd05580
Catalytic subunit of the Serine/Threonine Kinases, cAMP-dependent protein kinases; STKs ...
7989-8232 2.45e-42

Catalytic subunit of the Serine/Threonine Kinases, cAMP-dependent protein kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily is composed of the cAMP-dependent protein kinases, PKA and PRKX, and similar proteins. The inactive PKA holoenzyme is a heterotetramer composed of two phosphorylated and active catalytic subunits with a dimer of regulatory (R) subunits. Activation is achieved through the binding of the important second messenger cAMP to the R subunits, which leads to the dissociation of PKA into the R dimer and two active subunits. PKA is present ubiquitously in cells and interacts with many different downstream targets. It plays a role in the regulation of diverse processes such as growth, development, memory, metabolism, gene expression, immunity, and lipolysis. PRKX is also reulated by the R subunit and is is present in many tissues including fetal and adult brain, kidney, and lung. It is implicated in granulocyte/macrophage lineage differentiation, renal cell epithelial migration, and tubular morphogenesis in the developing kidney. The PKA-like subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270732 [Multi-domain]  Cd Length: 290  Bit Score: 159.67  E-value: 2.45e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 7989 YDILEEIGTGAFGVVHRCRERSTGNIFAAKFI---PVSHSVEKDLIRREIDIMNQLHHQKLINLHDAFEDDDEMILILEF 8065
Cdd:cd05580     3 FEFLKTLGTGSFGRVRLVKHKDSGKYYALKILkkaKIIKLKQVEHVLNEKRILSEVRHPFIVNLLGSFQDDRNLYMVMEY 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 8066 LSGGELFERITAEGYVmtEAEVIN-YMRQICEGIRHMHEQNIIHLDIKPENIMcqTRSSTNVKLIDFGLATRLDPNevVK 8144
Cdd:cd05580    83 VPGGELFSLLRRSGRF--PNDVAKfYAAEVVLALEYLHSLDIVYRDLKPENLL--LDSDGHIKITDFGFAKRVKDR--TY 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 8145 ITTGTAEFAAPEIVNREPVGFYTDMWATGVLSYVLLSGLSPFAGDNDVQTLKNVKACDWDFDvesfKYISEEAKDFIRKL 8224
Cdd:cd05580   157 TLCGTPEYLAPEIILSKGHGKAVDWWALGILIYEMLAGYPPFFDENPMKIYEKILEGKIRFP----SFFDPDAKDLIKRL 232

                  ....*...
gi 281359561 8225 LVRNKEKR 8232
Cdd:cd05580   233 LVVDLTKR 240
STKc_obscurin_rpt2 cd14110
Catalytic kinase domain, second repeat, of the Giant Serine/Threonine Kinase Obscurin; STKs ...
7986-8244 4.89e-42

Catalytic kinase domain, second repeat, of the Giant Serine/Threonine Kinase Obscurin; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Obscurin, approximately 800 kDa in size, is one of three giant proteins expressed in vetebrate striated muscle, together with titin and nebulin. It is a multidomain protein composed of tandem adhesion and signaling domains, including 49 immunoglobulin (Ig) and 2 fibronectin type III (FN3) domains at the N-terminus followed by a more complex region containing more Ig domains, a conserved SH3 domain near a RhoGEF and PH domains, non-modular regions, as well as IQ and phosphorylation motifs. The obscurin gene also encode two kinase domains, which are not expressed as part of the 800 kDa protein, but as a smaller, alternatively spliced product present mainly in the heart muscle, also called obscurin-MLCK. Obscurin is localized at the peripheries of Z-disks and M-lines, where it is able to communicate with the surrounding myoplasm. It interacts with diverse proteins including sAnk1, myosin, titin, and MyBP-C. It may act as a scaffold for the assembly of elements of the contractile apparatus. The obscurin subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271012 [Multi-domain]  Cd Length: 257  Bit Score: 157.77  E-value: 4.89e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 7986 YDRYDILEEIGTGAFGVVHRCRERSTGNIFAAKFIPVsHSVEKDLIRREIDIMNQLHHQKLINLHDAFEDDDEMILILEF 8065
Cdd:cd14110     2 EKTYAFQTEINRGRFSVVRQCEEKRSGQMLAAKIIPY-KPEDKQLVLREYQVLRRLSHPRIAQLHSAYLSPRHLVLIEEL 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 8066 LSGGELFERItAEGYVMTEAEVINYMRQICEGIRHMHEQNIIHLDIKPENIMCQTRSStnVKLIDFGLATRLDPNEVVKI 8145
Cdd:cd14110    81 CSGPELLYNL-AERNSYSEAEVTDYLWQILSAVDYLHSRRILHLDLRSENMIITEKNL--LKIVDLGNAQPFNQGKVLMT 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 8146 TT--GTAEFAAPEIVNREPVGFYTDMWATGVLSYVLLSGLSPFAGDNDVQTLKNVKACDWDFDvESFKYISEEAKDFIRK 8223
Cdd:cd14110   158 DKkgDYVETMAPELLEGQGAGPQTDIWAIGVTAFIMLSADYPVSSDLNWERDRNIRKGKVQLS-RCYAGLSGGAVNFLKS 236
                         250       260
                  ....*....|....*....|.
gi 281359561 8224 LLVRNKEKRMTAHECLLHPWL 8244
Cdd:cd14110   237 TLCAKPWGRPTASECLQNPWL 257
STKc_CaMK_like cd14088
Catalytic domain of an Uncharacterized group of Serine/Threonine kinases with similarity to ...
7987-8244 5.00e-42

Catalytic domain of an Uncharacterized group of Serine/Threonine kinases with similarity to Calcium/calmodulin-dependent protein kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily is composed of uncharacterized STKs with similarity to CaMKs, which are multifunctional calcium and calmodulin (CaM) stimulated STKs involved in cell cycle regulation. The CaMK family includes CaMKI, CaMKII, CaMKIV, and CaMK kinase (CaMKK). CaMKs contain an N-terminal catalytic domain followed by a regulatory domain that harbors a CaM binding site. This uncharacterized subfamily is part of a larger superfamily that includes the catalytic domains of other protein kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270990 [Multi-domain]  Cd Length: 265  Bit Score: 157.88  E-value: 5.00e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 7987 DRYDILEEIGTGAFGVVHRCRERSTGNIFAAK-FIPVSHSVEKDLIRREIDIMNQLHHQKLINLHDAFEDDDEMILILEF 8065
Cdd:cd14088     1 DRYDLGQVIKTEEFCEIFRAKDKTTGKLYTCKkFLKRDGRKVRKAAKNEINILKMVKHPNILQLVDVFETRKEYFIFLEL 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 8066 LSGGELFERITAEGYvMTEAEVINYMRQICEGIRHMHEQNIIHLDIKPENIMCQTR-SSTNVKLIDFGLAtRLDpNEVVK 8144
Cdd:cd14088    81 ATGREVFDWILDQGY-YSERDTSNVIRQVLEAVAYLHSLKIVHRNLKLENLVYYNRlKNSKIVISDFHLA-KLE-NGLIK 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 8145 ITTGTAEFAAPEIVNREPVGFYTDMWATGVLSYVLLSGLSPF---AGDNDVQT-----LKNVKACDWDFDVESFKYISEE 8216
Cdd:cd14088   158 EPCGTPEYLAPEVVGRQRYGRPVDCWAIGVIMYILLSGNPPFydeAEEDDYENhdknlFRKILAGDYEFDSPYWDDISQA 237
                         250       260
                  ....*....|....*....|....*...
gi 281359561 8217 AKDFIRKLLVRNKEKRMTAHECLLHPWL 8244
Cdd:cd14088   238 AKDLVTRLMEVEQDQRITAEEAISHEWI 265
STKc_SIK cd14071
Catalytic domain of the Serine/Threonine Kinases, Salt-Inducible kinases; STKs catalyze the ...
7989-8244 8.60e-42

Catalytic domain of the Serine/Threonine Kinases, Salt-Inducible kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. SIKs are part of a complex network that regulates Na,K-ATPase to maintain sodium homeostasis and blood pressure. Vertebrates contain three forms of SIKs (SIK1-3) from three distinct genes, which display tissue-specific effects. SIK1, also called SNF1LK, controls steroidogenic enzyme production in adrenocortical cells. In the brain, both SIK1 and SIK2 regulate energy metabolism. SIK2, also called QIK or SNF1LK2, is involved in the regulation of gluconeogenesis in the liver and lipogenesis in adipose tissues, where it phosphorylates the insulin receptor substrate-1. In the liver, SIK3 (also called QSK) regulates cholesterol and bile acid metabolism. In addition, SIK2 plays an important role in the initiation of mitosis and regulates the localization of C-Nap1, a centrosome linker protein. The SIK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270973 [Multi-domain]  Cd Length: 253  Bit Score: 156.78  E-value: 8.60e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 7989 YDILEEIGTGAFGVVHRCRERSTGNIFAAKFIPVSHSVEKDL--IRREIDIMNQLHHQKLINLHDAFEDDDEMILILEFL 8066
Cdd:cd14071     2 YDIERTIGKGNFAVVKLARHRITKTEVAIKIIDKSQLDEENLkkIYREVQIMKMLNHPHIIKLYQVMETKDMLYLVTEYA 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 8067 SGGELFERITAEGYvMTEAEVINYMRQICEGIRHMHEQNIIHLDIKPENIMCQtrSSTNVKLIDFGLATRLDPNEVVKIT 8146
Cdd:cd14071    82 SNGEIFDYLAQHGR-MSEKEARKKFWQILSAVEYCHKRHIVHRDLKAENLLLD--ANMNIKIADFGFSNFFKPGELLKTW 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 8147 TGTAEFAAPEIVN-REPVGFYTDMWATGVLSYVLLSGLSPFAGDNdVQTLKNvKACDWDFDVESFkyISEEAKDFIRKLL 8225
Cdd:cd14071   159 CGSPPYAAPEVFEgKEYEGPQLDIWSLGVVLYVLVCGALPFDGST-LQTLRD-RVLSGRFRIPFF--MSTDCEHLIRRML 234
                         250
                  ....*....|....*....
gi 281359561 8226 VRNKEKRMTAHECLLHPWL 8244
Cdd:cd14071   235 VLDPSKRLTIEQIKKHKWM 253
STKc_SnRK3 cd14663
Catalytic domain of the Serine/Threonine Kinases, Sucrose nonfermenting 1-related protein ...
7988-8243 1.12e-41

Catalytic domain of the Serine/Threonine Kinases, Sucrose nonfermenting 1-related protein kinase subfamily 3; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The SnRKs form three different subfamilies designated SnRK1-3. SnRK3 is represented in this cd. The SnRK3 group contains members also known as CBL-interacting protein kinase, salt overly sensitive 2, SOS3-interacting proteins and protein kinase S. These kinases interact with calcium-binding proteins such as SOS3, SCaBPs, and CBL proteins, and are involved in responses to salt stress and in sugar and ABA signaling. The SnRKs belong to a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271133 [Multi-domain]  Cd Length: 256  Bit Score: 156.41  E-value: 1.12e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 7988 RYDILEEIGTGAFGVVHRCRERSTGNIFAAKFIPVSHSVEKDL---IRREIDIMNQLHHQKLINLHDAFEDDDEMILILE 8064
Cdd:cd14663     1 RYELGRTLGEGTFAKVKFARNTKTGESVAIKIIDKEQVAREGMveqIKREIAIMKLLRHPNIVELHEVMATKTKIFFVME 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 8065 FLSGGELFERItAEGYVMTEAEVINYMRQICEGIRHMHEQNIIHLDIKPENIMCQtrSSTNVKLIDFGL---ATRLDPNE 8141
Cdd:cd14663    81 LVTGGELFSKI-AKNGRLKEDKARKYFQQLIDAVDYCHSRGVFHRDLKPENLLLD--EDGNLKISDFGLsalSEQFRQDG 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 8142 VVKITTGTAEFAAPEIV-NREPVGFYTDMWATGVLSYVLLSGLSPFAGDNdVQTLKNvKACDWDFDVESfkYISEEAKDF 8220
Cdd:cd14663   158 LLHTTCGTPNYVAPEVLaRRGYDGAKADIWSCGVILFVLLAGYLPFDDEN-LMALYR-KIMKGEFEYPR--WFSPGAKSL 233
                         250       260
                  ....*....|....*....|...
gi 281359561 8221 IRKLLVRNKEKRMTAHECLLHPW 8243
Cdd:cd14663   234 IKRILDPNPSTRITVEQIMASPW 256
STKc_MSK2_C cd14180
C-terminal catalytic domain of the Serine/Threonine Kinase, Mitogen and stress-activated ...
7986-8246 1.28e-41

C-terminal catalytic domain of the Serine/Threonine Kinase, Mitogen and stress-activated kinase 2; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MSK2 and MSK1 play nonredundant roles in activating histone H3 kinases, which play pivotal roles in compaction of the chromatin fiber. MSK2 is the required H3 kinase in response to stress stimuli and activation of the p38 MAPK pathway. MSK2 also plays a role in the pathogenesis of psoriasis. MSKs contain an N-terminal kinase domain (NTD) from the AGC family and a C-terminal kinase domain (CTD) from the CAMK family, similar to 90 kDa ribosomal protein S6 kinases (RSKs). MSKs are activated by two major signaling cascades, the Ras-MAPK and p38 stress kinase pathways, which trigger phosphorylation in the activation loop (A-loop) of the CTD of MSK. The active CTD phosphorylates the hydrophobic motif (HM) of NTD, which facilitates the phosphorylation of the A-loop and activates the NTD, which in turn phosphorylates downstream targets. The MSK2 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271082 [Multi-domain]  Cd Length: 309  Bit Score: 158.11  E-value: 1.28e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 7986 YDRYDI-LEE--IGTGAFGVVHRCRERSTGNIFAAKFIpvSHSVEKDlIRREIDIMNQLH-HQKLINLHDAFEDDDEMIL 8061
Cdd:cd14180     2 FQCYELdLEEpaLGEGSFSVCRKCRHRQSGQEYAVKII--SRRMEAN-TQREVAALRLCQsHPNIVALHEVLHDQYHTYL 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 8062 ILEFLSGGELFERITAEGYvMTEAEVINYMRQICEGIRHMHEQNIIHLDIKPENIMCQTRS-STNVKLIDFGLAtRLDPN 8140
Cdd:cd14180    79 VMELLRGGELLDRIKKKAR-FSESEASQLMRSLVSAVSFMHEAGVVHRDLKPENILYADESdGAVLKVIDFGFA-RLRPQ 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 8141 EVVKITTG--TAEFAAPEIVNREPVGFYTDMWATGVLSYVLLSGLSPFAGDNDVQT-------LKNVKACDWDFDVESFK 8211
Cdd:cd14180   157 GSRPLQTPcfTLQYAAPELFSNQGYDESCDLWSLGVILYTMLSGQVPFQSKRGKMFhnhaadiMHKIKEGDFSLEGEAWK 236
                         250       260       270
                  ....*....|....*....|....*....|....*
gi 281359561 8212 YISEEAKDFIRKLLVRNKEKRMTAHECLLHPWLTG 8246
Cdd:cd14180   237 GVSEEAKDLVRGLLTVDPAKRLKLSELRESDWLQG 271
STKc_NUAK2 cd14161
Catalytic domain of the Serine/Threonine Kinase, novel (nua) kinase family NUAK 2; STKs ...
7988-8244 4.44e-41

Catalytic domain of the Serine/Threonine Kinase, novel (nua) kinase family NUAK 2; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. NUAK proteins are classified as AMP-activated protein kinase (AMPK)-related kinases, which like AMPK are activated by the major tumor suppressor LKB1. Vertebrates contain two NUAK proteins, called NUAK1 and NUAK2. NUAK2, also called SNARK (Sucrose, non-fermenting 1/AMP-activated protein kinase-related kinase), is involved in energy metabolism. It is activated by hyperosmotic stress, DNA damage, and nutrients such as glucose and glutamine. NUAK2-knockout mice develop obesity, altered serum lipid profiles, hyperinsulinaemia, hyperglycaemia, and impaired glucose tolerance. NUAK2 is implicated in regulating actin stress fiber assembly through its association with myosin phosphatase Rho-interacting protein (MRIP), which leads to an increase in myosin regulatory light chain (MLC) phosphorylation. It is also associated with tumor growth, migration, and oncogenicity of melanoma cells. The NUAK2 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271063 [Multi-domain]  Cd Length: 255  Bit Score: 154.73  E-value: 4.44e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 7988 RYDILEEIGTGAFGVVHRCRERStGNIFAAKFIPVSH-SVEKDL--IRREIDIMNQLHHQKLINLHDAFEDDDEMILILE 8064
Cdd:cd14161     4 RYEFLETLGKGTYGRVKKARDSS-GRLVAIKSIRKDRiKDEQDLlhIRREIEIMSSLNHPHIISVYEVFENSSKIVIVME 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 8065 FLSGGELFERITaEGYVMTEAEVINYMRQICEGIRHMHEQNIIHLDIKPENIMCQtrSSTNVKLIDFGLATRLDPNEVVK 8144
Cdd:cd14161    83 YASRGDLYDYIS-ERQRLSELEARHFFRQIVSAVHYCHANGIVHRDLKLENILLD--ANGNIKIADFGLSNLYNQDKFLQ 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 8145 ITTGTAEFAAPEIVNREP-VGFYTDMWATGVLSYVLLSGLSPFAGDNDVQTLKNVKACDWDfdvESFKyiSEEAKDFIRK 8223
Cdd:cd14161   160 TYCGSPLYASPEIVNGRPyIGPEVDSWSLGVLLYILVHGTMPFDGHDYKILVKQISSGAYR---EPTK--PSDACGLIRW 234
                         250       260
                  ....*....|....*....|.
gi 281359561 8224 LLVRNKEKRMTAHECLLHPWL 8244
Cdd:cd14161   235 LLMVNPERRATLEDVASHWWV 255
STKc_NIM1 cd14075
Catalytic domain of the Serine/Threonine Kinase, NIM1; STKs catalyze the transfer of the ...
7989-8244 5.35e-41

Catalytic domain of the Serine/Threonine Kinase, NIM1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. NIM1 is a widely-expressed kinase belonging to the AMP-activated protein kinase (AMPK) subfamily. Although present in most tissues, NIM1 kinase activity is only observed in the brain and testis. NIM1 is capable of autophosphorylating and activating itself, but may be present in other tissues in the inactive form. The physiological function of NIM1 has yet to be elucidated. The NIM1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270977 [Multi-domain]  Cd Length: 255  Bit Score: 154.42  E-value: 5.35e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 7989 YDILEEIGTGAFGVVHRCRERSTGNIFAAKFIPVSHSVEKD--LIRREIDIMNQLHHQKLINLHDAFEDDDEMILILEFL 8066
Cdd:cd14075     4 YRIRGELGSGNFSQVKLGIHQLTKEKVAIKILDKTKLDQKTqrLLSREISSMEKLHHPNIIRLYEVVETLSKLHLVMEYA 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 8067 SGGELFERITAEGYvMTEAEVINYMRQICEGIRHMHEQNIIHLDIKPENIMCQtrSSTNVKLIDFGLATRLDPNEVVKIT 8146
Cdd:cd14075    84 SGGELYTKISTEGK-LSESEAKPLFAQIVSAVKHMHENNIIHRDLKAENVFYA--SNNCVKVGDFGFSTHAKRGETLNTF 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 8147 TGTAEFAAPEIVNREP-VGFYTDMWATGVLSYVLLSGLSPFAGDndvqTLKNVKAC--DWDFDVESfkYISEEAKDFIRK 8223
Cdd:cd14075   161 CGSPPYAAPELFKDEHyIGIYVDIWALGVLLYFMVTGVMPFRAE----TVAKLKKCilEGTYTIPS--YVSEPCQELIRG 234
                         250       260
                  ....*....|....*....|.
gi 281359561 8224 LLVRNKEKRMTAHECLLHPWL 8244
Cdd:cd14075   235 ILQPVPSDRYSIDEIKNSEWL 255
STKc_Pat1_like cd13993
Catalytic domain of Fungal Pat1-like Serine/Threonine kinases; STKs catalyze the transfer of ...
7988-8237 6.60e-41

Catalytic domain of Fungal Pat1-like Serine/Threonine kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily is composed of Schizosaccharomyces pombe Pat1 (also called Ran1), Saccharomyces cerevisiae VHS1 and KSP1, and similar fungal STKs. Pat1 blocks Mei2, an RNA-binding protein which is indispensable in the initiation of meiosis. Pat1 is inactivated and Mei2 activated, which initiates meiosis, under nutrient-deprived conditions through a signaling cascade involving Ste11. Meiosis induced by Pat1 inactivation may show different characteristics than normal meiosis including aberrant positioning of centromeres. VHS1 was identified in a screen for suppressors of cell cycle arrest at the G1/S transition, while KSP1 may be involved in regulating PRP20, which is required for mRNA export and maintenance of nuclear structure. The Pat1-like subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270895 [Multi-domain]  Cd Length: 267  Bit Score: 154.82  E-value: 6.60e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 7988 RYDILEEIGTGAFGVVHRCRERSTGNIFAAKFIPVSHSVEKDLI-------RREIDIMNQLH-HQKLINLHDAFEDDDEM 8059
Cdd:cd13993     1 RYQLISPIGEGAYGVVYLAVDLRTGRKYAIKCLYKSGPNSKDGNdfqklpqLREIDLHRRVSrHPNIITLHDVFETEVAI 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 8060 ILILEFLSGGELFERITAEGYVMTEAEVI-NYMRQICEGIRHMHEQNIIHLDIKPENIMCQTrSSTNVKLIDFGLATRLD 8138
Cdd:cd13993    81 YIVLEYCPNGDLFEAITENRIYVGKTELIkNVFLQLIDAVKHCHSLGIYHRDIKPENILLSQ-DEGTVKLCDFGLATTEK 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 8139 PNevVKITTGTAEFAAPEI---VNREPVGFYT---DMWATGVLSYVLLSGLSPF--AGDNDVQTLKNVKACDWDFDVesF 8210
Cdd:cd13993   160 IS--MDFGVGSEFYMAPECfdeVGRSLKGYPCaagDIWSLGIILLNLTFGRNPWkiASESDPIFYDYYLNSPNLFDV--I 235
                         250       260
                  ....*....|....*....|....*..
gi 281359561 8211 KYISEEAKDFIRKLLVRNKEKRMTAHE 8237
Cdd:cd13993   236 LPMSDDFYNLLRQIFTVNPNNRILLPE 262
STKc_Unc-89_rpt2 cd14112
Catalytic kinase domain, second repeat, of the Giant Serine/Threonine Kinase Uncoordinated ...
7987-8244 6.61e-41

Catalytic kinase domain, second repeat, of the Giant Serine/Threonine Kinase Uncoordinated protein 89; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The nematode Unc-89 gene, through alternative promoter use and splicing, encodes at least six major isoforms (Unc-89A to Unc-89F) of giant muscle proteins that are homologs for the vetebrate obscurin. In flies, five isoforms of Unc-89 have been detected: four in the muscles of adult flies (two in the indirect flight muscle and two in other muscles) and another isoform in the larva. Unc-89 in nematodes is required for normal muscle cell architecture. In flies, it is necessary for the development of a symmetrical sarcomere in the flight muscles. Unc-89 proteins contain several adhesion and signaling domains including multiple copies of the immunoglobulin (Ig) domain, as well as fibronectin type III (FN3), SH3, RhoGEF, and PH domains. The nematode Unc-89 isoforms D, C, D, and F contain two kinase domain with B and F having two complete kinase domains while the first repeat of C and D are partial domains. Homology modeling suggests that the first kinase repeat of Unc-89 may be catalytically inactive, a pseudokinase, while the second kinase repeat may be active. The Unc-89 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271014 [Multi-domain]  Cd Length: 259  Bit Score: 154.23  E-value: 6.61e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 7987 DRYDILEEIGTGAFGVVHRCRERS--TGNIFAAKFIPVSHsvEKDLIRREIDIMNQLHHQKLINLHDAFEDDDEMILILE 8064
Cdd:cd14112     3 GRFSFGSEIFRGRFSVIVKAVDSTteTDAHCAVKIFEVSD--EASEAVREFESLRTLQHENVQRLIAAFKPSNFAYLVME 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 8065 FLSGgELFERITAEGYvMTEAEVINYMRQICEGIRHMHEQNIIHLDIKPENIMCQTRSSTNVKLIDFGLATRLDPnEVVK 8144
Cdd:cd14112    81 KLQE-DVFTRFSSNDY-YSEEQVATTVRQILDALHYLHFKGIAHLDVQPDNIMFQSVRSWQVKLVDFGRAQKVSK-LGKV 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 8145 ITTGTAEFAAPEIVNRE-PVGFYTDMWATGVLSYVLLSGLSPF--AGDNDVQTLKNVKACDWDFDVeSFKYISEEAKDFI 8221
Cdd:cd14112   158 PVDGDTDWASPEFHNPEtPITVQSDIWGLGVLTFCLLSGFHPFtsEYDDEEETKENVIFVKCRPNL-IFVEATQEALRFA 236
                         250       260
                  ....*....|....*....|...
gi 281359561 8222 RKLLVRNKEKRMTAHECLLHPWL 8244
Cdd:cd14112   237 TWALKKSPTRRMRTDEALEHRWL 259
STKc_PASK cd14004
Catalytic domain of the Serine/Threonine kinase, Per-ARNT-Sim (PAS) domain Kinase; STKs ...
7989-8244 1.08e-40

Catalytic domain of the Serine/Threonine kinase, Per-ARNT-Sim (PAS) domain Kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PASK (or PASKIN) is a nutrient and energy sensor and thus, plays an important role in maintaining cellular energy homeostasis. It coordinates the utilization of glucose in response to metabolic demand. It contains an N-terminal PAS domain which directly interacts and inhibits a C-terminal catalytic kinase domain. The PAS domain serves as a sensory module for different environmental signals such as light, redox state, and various metabolites. Binding of ligands to the PAS domain causes structural changes which leads to kinase activation and the phosphorylation of substrates to trigger the appropriate cellular response. The PASK subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270906 [Multi-domain]  Cd Length: 256  Bit Score: 153.70  E-value: 1.08e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 7989 YDILEEIGTGAFGVVHRCRERSTGNIFAAKFIPVSHSVE------KDL--IRREIDIMNQLH---HQKLINLHDAFEDDD 8057
Cdd:cd14004     2 YTILKEMGEGAYGQVNLAIYKSKGKEVVIKFIFKERILVdtwvrdRKLgtVPLEIHILDTLNkrsHPNIVKLLDFFEDDE 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 8058 EMILILE-FLSGGELFERITAEGyVMTEAEVINYMRQICEGIRHMHEQNIIHLDIKPENIMCQtrSSTNVKLIDFGLATR 8136
Cdd:cd14004    82 FYYLVMEkHGSGMDLFDFIERKP-NMDEKEAKYIFRQVADAVKHLHDQGIVHRDIKDENVILD--GNGTIKLIDFGSAAY 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 8137 LDPNevvKITT--GTAEFAAPEIVNREP-VGFYTDMWATGVLSYVLLSGLSPFAgdNDVQTLknvkacdwDFDVESFKYI 8213
Cdd:cd14004   159 IKSG---PFDTfvGTIDYAAPEVLRGNPyGGKEQDIWALGVLLYTLVFKENPFY--NIEEIL--------EADLRIPYAV 225
                         250       260       270
                  ....*....|....*....|....*....|.
gi 281359561 8214 SEEAKDFIRKLLVRNKEKRMTAHECLLHPWL 8244
Cdd:cd14004   226 SEDLIDLISRMLNRDVGDRPTIEELLTDPWL 256
STKc_cGK cd05572
Catalytic domain of the Serine/Threonine Kinase, cGMP-dependent protein kinase (cGK or PKG); ...
7995-8233 1.13e-40

Catalytic domain of the Serine/Threonine Kinase, cGMP-dependent protein kinase (cGK or PKG); STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Mammals have two cGK isoforms from different genes, cGKI and cGKII. cGKI exists as two splice variants, cGKI-alpha and cGKI-beta. cGK consists of an N-terminal regulatory domain containing a dimerization and an autoinhibitory pseudosubstrate region, two cGMP-binding domains, and a C-terminal catalytic domain. Binding of cGMP to both binding sites releases the inhibition of the catalytic center by the pseudosubstrate region, allowing autophosphorylation and activation of the kinase. cGKI is a soluble protein expressed in all smooth muscles, platelets, cerebellum, and kidney. It is also expressed at lower concentrations in other tissues. cGKII is a membrane-bound protein that is most abundantly expressed in the intestine. It is also present in the brain nuclei, adrenal cortex, kidney, lung, and prostate. cGKI is involved in the regulation of smooth muscle tone, smooth cell proliferation, and platelet activation. cGKII plays a role in the regulation of secretion, such as renin secretion by the kidney and aldosterone secretion by the adrenal. It also regulates bone growth and the circadian rhythm. The cGK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270724 [Multi-domain]  Cd Length: 262  Bit Score: 153.92  E-value: 1.13e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 7995 IGTGAFGVVHRCRERSTGNIFAAKFIPVSHSVEKDL---IRREIDIMNQLHHQKLINLHDAFEDDDEMILILEFLSGGEL 8071
Cdd:cd05572     1 LGVGGFGRVELVQLKSKGRTFALKCVKKRHIVQTRQqehIFSEKEILEECNSPFIVKLYRTFKDKKYLYMLMEYCLGGEL 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 8072 FERITAEGYvMTEAEVINYMRQICEGIRHMHEQNIIHLDIKPENIMCQTRSStnVKLIDFGLATRLDPNEVVKITTGTAE 8151
Cdd:cd05572    81 WTILRDRGL-FDEYTARFYTACVVLAFEYLHSRGIIYRDLKPENLLLDSNGY--VKLVDFGFAKKLGSGRKTWTFCGTPE 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 8152 FAAPEIVNREPVGFYTDMWATGVLSYVLLSGLSPFAGDNDVQ--TLKNVkaCDWDFDVESFKYISEEAKDFIRKLLVRNK 8229
Cdd:cd05572   158 YVAPEIILNKGYDFSVDYWSLGILLYELLTGRPPFGGDDEDPmkIYNII--LKGIDKIEFPKYIDKNAKNLIKQLLRRNP 235

                  ....
gi 281359561 8230 EKRM 8233
Cdd:cd05572   236 EERL 239
STKc_RSK1_C cd14175
C-terminal catalytic domain of the Serine/Threonine Kinase, Ribosomal S6 kinase 1 (also called ...
7987-8257 1.46e-40

C-terminal catalytic domain of the Serine/Threonine Kinase, Ribosomal S6 kinase 1 (also called Ribosomal protein S6 kinase alpha-1 or 90kDa ribosomal protein S6 kinase 1); STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. RSK1 is also called S6K-alpha-1, RPS6KA1, p90RSK1 or MAPK-activated protein kinase 1a (MAPKAPK-1a). It is a component of the insulin transduction pathway, regulating the function of IRS1. It also interacts with PKA and promotes its inactivation. RSK1 is one of four RSK isoforms (RSK1-4) from distinct genes present in vertebrates. RSKs contain an N-terminal kinase domain (NTD) from the AGC family and a C-terminal kinase domain (CTD) from the CAMK family. They are activated by signaling inputs from extracellular regulated kinase (ERK) and phosphoinositide dependent kinase 1 (PDK1). ERK phosphorylates and activates the CTD of RSK, serving as a docking site for PDK1, which phosphorylates and activates the NTD, which in turn phosphorylates all known RSK substrates. RSKs act as downstream effectors of mitogen-activated protein kinase (MAPK) and play key roles in mitogen-activated cell growth, differentiation, and survival. The RSK1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271077 [Multi-domain]  Cd Length: 291  Bit Score: 154.41  E-value: 1.46e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 7987 DRYDILEEIGTGAFGVVHRCRERSTGNIFAAKFIPVSHSVEKDlirrEIDIMNQL-HHQKLINLHDAFEDDDEMILILEF 8065
Cdd:cd14175     1 DGYVVKETIGVGSYSVCKRCVHKATNMEYAVKVIDKSKRDPSE----EIEILLRYgQHPNIITLKDVYDDGKHVYLVTEL 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 8066 LSGGELFERITAEGYvMTEAEVINYMRQICEGIRHMHEQNIIHLDIKPENIMCQTRSST--NVKLIDFGLATRLDP-NEV 8142
Cdd:cd14175    77 MRGGELLDKILRQKF-FSEREASSVLHTICKTVEYLHSQGVVHRDLKPSNILYVDESGNpeSLRICDFGFAKQLRAeNGL 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 8143 VKITTGTAEFAAPEIVNREPVGFYTDMWATGVLSYVLLSGLSPFA---GDNDVQTLKNVKACDWDFDVESFKYISEEAKD 8219
Cdd:cd14175   156 LMTPCYTANFVAPEVLKRQGYDEGCDIWSLGILLYTMLAGYTPFAngpSDTPEEILTRIGSGKFTLSGGNWNTVSDAAKD 235
                         250       260       270
                  ....*....|....*....|....*....|....*...
gi 281359561 8220 FIRKLLVRNKEKRMTAHECLLHPWLTGDHSAMKQEINR 8257
Cdd:cd14175   236 LVSKMLHVDPHQRLTAKQVLQHPWITQKDKLPQSQLNH 273
STKc_CDKL cd07833
Catalytic domain of Cyclin-Dependent protein Kinase Like Serine/Threonine Kinases; STKs ...
7987-8244 1.94e-40

Catalytic domain of Cyclin-Dependent protein Kinase Like Serine/Threonine Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily is composed of CDKL1-5 and similar proteins. Some CDKLs, like CDKL1 and CDKL3, may be implicated in transformation and others, like CDKL3 and CDKL5, are associated with mental retardation when impaired. CDKL2 plays a role in learning and memory. CDKs belong to a large family of STKs that are regulated by their cognate cyclins. Together, they are involved in the control of cell-cycle progression, transcription, and neuronal function. The CDKL subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270827 [Multi-domain]  Cd Length: 288  Bit Score: 154.01  E-value: 1.94e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 7987 DRYDILEEIGTGAFGVVHRCRERSTGNIFAAKFIPVSHSVE--KDLIRREIDIMNQLHHQKLINLHDAFEDDDEMILILE 8064
Cdd:cd07833     1 NKYEVLGVVGEGAYGVVLKCRNKATGEIVAIKKFKESEDDEdvKKTALREVKVLRQLRHENIVNLKEAFRRKGRLYLVFE 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 8065 FLsGGELFERITAEGYVMTEAEVINYMRQICEGIRHMHEQNIIHLDIKPENIMCqTRSSTnVKLIDFGLATRLDPNEVVK 8144
Cdd:cd07833    81 YV-ERTLLELLEASPGGLPPDAVRSYIWQLLQAIAYCHSHNIIHRDIKPENILV-SESGV-LKLCDFGFARALTARPASP 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 8145 ITT--GTAEFAAPEI-VNREPVGFYTDMWATGVLSYVLLSGLSPFAGDNDVQTLKNVKAC--------------DWDFDV 8207
Cdd:cd07833   158 LTDyvATRWYRAPELlVGDTNYGKPVDVWAIGCIMAELLDGEPLFPGDSDIDQLYLIQKClgplppshqelfssNPRFAG 237
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|.
gi 281359561 8208 ESFKYISEE--------------AKDFIRKLLVRNKEKRMTAHECLLHPWL 8244
Cdd:cd07833   238 VAFPEPSQPeslerrypgkvsspALDFLKACLRMDPKERLTCDELLQHPYF 288
STKc_RSK3_C cd14178
C-terminal catalytic domain of the Serine/Threonine Kinase, Ribosomal S6 kinase 3 (also called ...
7987-8271 3.87e-40

C-terminal catalytic domain of the Serine/Threonine Kinase, Ribosomal S6 kinase 3 (also called Ribosomal protein S6 kinase alpha-2 or 90kDa ribosomal protein S6 kinase 2); STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. RSK3 is also called S6K-alpha-2, RPS6KA2, p90RSK2 or MAPK-activated protein kinase 1c (MAPKAPK-1c). RSK3 binds muscle A-kinase anchoring protein (mAKAP)-b directly and regulates concentric cardiac myocyte growth. The RSK3 gene, RPS6KA2, is a putative tumor suppressor gene in sporadic epithelial ovarian cancer and variations to the gene may be associated with rectal cancer risk. RSK3 is one of four RSK isoforms (RSK1-4) from distinct genes present in vertebrates. RSKs contain an N-terminal kinase domain (NTD) from the AGC family and a C-terminal kinase domain (CTD) from the CAMK family. They are activated by signaling inputs from extracellular regulated kinase (ERK) and phosphoinositide dependent kinase 1 (PDK1). ERK phosphorylates and activates the CTD of RSK, serving as a docking site for PDK1, which phosphorylates and activates the NTD, which in turn phosphorylates all known RSK substrates. RSKs act as downstream effectors of mitogen-activated protein kinase (MAPK) and play key roles in mitogen-activated cell growth, differentiation, and survival. The RSK3 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271080 [Multi-domain]  Cd Length: 293  Bit Score: 153.25  E-value: 3.87e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 7987 DRYDILEEIGTGAFGVVHRCRERSTGNIFAAKFIPVShsvEKDlIRREIDIMNQL-HHQKLINLHDAFEDDDEMILILEF 8065
Cdd:cd14178     3 DGYEIKEDIGIGSYSVCKRCVHKATSTEYAVKIIDKS---KRD-PSEEIEILLRYgQHPNIITLKDVYDDGKFVYLVMEL 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 8066 LSGGELFERITAEGYvMTEAEVINYMRQICEGIRHMHEQNIIHLDIKPENI--MCQTRSSTNVKLIDFGLATRLDP-NEV 8142
Cdd:cd14178    79 MRGGELLDRILRQKC-FSEREASAVLCTITKTVEYLHSQGVVHRDLKPSNIlyMDESGNPESIRICDFGFAKQLRAeNGL 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 8143 VKITTGTAEFAAPEIVNREPVGFYTDMWATGVLSYVLLSGLSPFAG---DNDVQTLKNVKACDWDFDVESFKYISEEAKD 8219
Cdd:cd14178   158 LMTPCYTANFVAPEVLKRQGYDAACDIWSLGILLYTMLAGFTPFANgpdDTPEEILARIGSGKYALSGGNWDSISDAAKD 237
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|..
gi 281359561 8220 FIRKLLVRNKEKRMTAHECLLHPWLtgdhsamkqeINRDrYLAYREKLRRKY 8271
Cdd:cd14178   238 IVSKMLHVDPHQRLTAPQVLRHPWI----------VNRE-YLSQNQLSRQDV 278
STKc_Kin1_2 cd14077
Catalytic domain of Kin1, Kin2, and simlar Serine/Threonine Kinases; STKs catalyze the ...
7989-8244 5.62e-40

Catalytic domain of Kin1, Kin2, and simlar Serine/Threonine Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily is composed of yeast Kin1, Kin2, and similar proteins. Fission yeast Kin1 is a membrane-associated kinase that is involved in regulating cell surface cohesiveness during interphase. It also plays a role during mitosis, linking actomyosin ring assembly with septum synthesis and membrane closure to ensure separation of daughter cells. Budding yeast Kin1 and Kin2 act downstream of the Rab-GTPase Sec4 and are associated with the exocytic apparatus; they play roles in the secretory pathway. The Kin1/2 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270979 [Multi-domain]  Cd Length: 267  Bit Score: 151.83  E-value: 5.62e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 7989 YDILEEIGTGAFGVVHRCRERSTGNIFAAKFIPVSH----------SVEKDLIR-----REIDIMNQLHHQKLINLHDAF 8053
Cdd:cd14077     3 WEFVKTIGAGSMGKVKLAKHIRTGEKCAIKIIPRASnaglkkerekRLEKEISRdirtiREAALSSLLNHPHICRLRDFL 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 8054 EDDDEMILILEFLSGGELFERITAEGYvMTEAEVINYMRQICEGIRHMHEQNIIHLDIKPENIMCQtrSSTNVKLIDFGL 8133
Cdd:cd14077    83 RTPNHYYMLFEYVDGGQLLDYIISHGK-LKEKQARKFARQIASALDYLHRNSIVHRDLKIENILIS--KSGNIKIIDFGL 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 8134 ATRLDPNEVVKITTGTAEFAAPEIVNREP-VGFYTDMWATGVLSYVLLSGLSPFaGDNDVQTL-KNVKacdwDFDVESFK 8211
Cdd:cd14077   160 SNLYDPRRLLRTFCGSLYFAAPELLQAQPyTGPEVDVWSFGVVLYVLVCGKVPF-DDENMPALhAKIK----KGKVEYPS 234
                         250       260       270
                  ....*....|....*....|....*....|...
gi 281359561 8212 YISEEAKDFIRKLLVRNKEKRMTAHECLLHPWL 8244
Cdd:cd14077   235 YLSSECKSLISRMLVVDPKKRATLEQVLNHPWM 267
STKc_SNRK cd14074
Catalytic domain of the Serine/Threonine Kinase, SNF1-related kinase; STKs catalyze the ...
7989-8244 8.24e-40

Catalytic domain of the Serine/Threonine Kinase, SNF1-related kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. SNRK is a kinase highly expressed in testis and brain that is found inactive in cells that lack the LKB1 tumour suppressor protein kinase. The regulatory subunits STRAD and MO25 are required for LKB1 to activate SNRK. The SNRK mRNA is increased 3-fold when granule neurons are cultured in low potassium, and may thus play a role in the survival responses in these cells. In some vertebrates, a second SNRK gene (snrkb or snrk-1) has been sequenced and/or identified. Snrk-1 is expressed specifically in embryonic zebrafish vasculature; it plays an essential role in angioblast differentiation, maintenance, and migration. The SNRK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270976 [Multi-domain]  Cd Length: 258  Bit Score: 151.03  E-value: 8.24e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 7989 YDILEEIGTGAFGVVHRCRERSTGNIFAAKFIPVSH--SVEKDLIRREIDIMNQLHHQKLINLHDAFEDDDEMILILEFL 8066
Cdd:cd14074     5 YDLEETLGRGHFAVVKLARHVFTGEKVAVKVIDKTKldDVSKAHLFQEVRCMKLVQHPNVVRLYEVIDTQTKLYLILELG 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 8067 SGGELFERITAEGYVMTEAEVINYMRQICEGIRHMHEQNIIHLDIKPENIM-CQTRSStnVKLIDFGLATRLDPNEVVKI 8145
Cdd:cd14074    85 DGGDMYDYIMKHENGLNEDLARKYFRQIVSAISYCHKLHVVHRDLKPENVVfFEKQGL--VKLTDFGFSNKFQPGEKLET 162
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 8146 TTGTAEFAAPEIVNREpvgFY----TDMWATGVLSYVLLSGLSPFAGDNDVQTLKNVKACdwDFDVESfkYISEEAKDFI 8221
Cdd:cd14074   163 SCGSLAYSAPEILLGD---EYdapaVDIWSLGVILYMLVCGQPPFQEANDSETLTMIMDC--KYTVPA--HVSPECKDLI 235
                         250       260
                  ....*....|....*....|...
gi 281359561 8222 RKLLVRNKEKRMTAHECLLHPWL 8244
Cdd:cd14074   236 RRMLIRDPKKRASLEEIENHPWL 258
STKc_TSSK-like cd14080
Catalytic domain of testis-specific serine/threonine kinases and similar proteins; STKs ...
7989-8244 2.25e-39

Catalytic domain of testis-specific serine/threonine kinases and similar proteins; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. TSSK proteins are almost exclusively expressed postmeiotically in the testis and play important roles in spermatogenesis and/or spermiogenesis. There are five mammalian TSSK proteins which show differences in their localization and timing of expression. TSSK1 and TSSK2 are expressed specifically in meiotic and postmeiotic spermatogenic cells, respectively. TSSK3 has been reported to be expressed in the interstitial Leydig cells of adult testis. TSSK4, also called TSSK5, is expressed in testis from haploid round spermatids to mature spermatozoa. TSSK6, also called SSTK, is expressed at the head of elongated sperm. TSSK1/TSSK2 double knock-out and TSSK6 null mice are sterile without manifesting other defects, making these kinases viable targets for male contraception. The TSSK-like subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270982 [Multi-domain]  Cd Length: 262  Bit Score: 150.03  E-value: 2.25e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 7989 YDILEEIGTGAFGVVHRC--RERSTGNIFAAKFIPVSHSVEKDLIR---REIDIMNQLHHQKLINLHDAFEDDDEMILIL 8063
Cdd:cd14080     2 YRLGKTIGEGSYSKVKLAeyTKSGLKEKVACKIIDKKKAPKDFLEKflpRELEILRKLRHPNIIQVYSIFERGSKVFIFM 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 8064 EFLSGGELFERITAEGYVmTEAEVINYMRQICEGIRHMHEQNIIHLDIKPENIMCQtrSSTNVKLIDFGLATR-LDPNEV 8142
Cdd:cd14080    82 EYAEHGDLLEYIQKRGAL-SESQARIWFRQLALAVQYLHSLDIAHRDLKCENILLD--SNNNVKLSDFGFARLcPDDDGD 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 8143 VKITT--GTAEFAAPEIVNREPV-GFYTDMWATGVLSYVLLSGLSPFAGDNDVQTLKNVKACDWDFDvESFKYISEEAKD 8219
Cdd:cd14080   159 VLSKTfcGSAAYAAPEILQGIPYdPKKYDIWSLGVILYIMLCGSMPFDDSNIKKMLKDQQNRKVRFP-SSVKKLSPECKD 237
                         250       260
                  ....*....|....*....|....*
gi 281359561 8220 FIRKLLVRNKEKRMTAHECLLHPWL 8244
Cdd:cd14080   238 LIDQLLEPDPTKRATIEEILNHPWL 262
STKc_PKD cd14082
Catalytic domain of the Serine/Threonine kinase, Protein Kinase D; STKs catalyze the transfer ...
7989-8243 4.30e-39

Catalytic domain of the Serine/Threonine kinase, Protein Kinase D; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PKDs are important regulators of many intracellular signaling pathways such as ERK and JNK, and cellular processes including the organization of the trans-Golgi network, membrane trafficking, cell proliferation, migration, and apoptosis. They contain N-terminal cysteine-rich zinc binding C1 (PKC conserved region 1), central PH (Pleckstrin Homology), and C-terminal catalytic kinase domains. Mammals harbor three types of PKDs: PKD1 (or PKCmu), PKD2, and PKD3 (or PKCnu). PKDs are activated in a PKC-dependent manner by many agents including diacylglycerol (DAG), PDGF, neuropeptides, oxidative stress, and tumor-promoting phorbol esters, among others. The PKD subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270984 [Multi-domain]  Cd Length: 260  Bit Score: 149.10  E-value: 4.30e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 7989 YDIL--EEIGTGAFGVVHRCRERSTGNIFAAKFIPVSH--SVEKDLIRREIDIMNQLHHQKLINLHDAFEDDDEMILILE 8064
Cdd:cd14082     3 YQIFpdEVLGSGQFGIVYGGKHRKTGRDVAIKVIDKLRfpTKQESQLRNEVAILQQLSHPGVVNLECMFETPERVFVVME 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 8065 FLSG-----------GELFERITAegYVMTeaevinymrQICEGIRHMHEQNIIHLDIKPENIMCQTRSS-TNVKLIDFG 8132
Cdd:cd14082    83 KLHGdmlemilssekGRLPERITK--FLVT---------QILVALRYLHSKNIVHCDLKPENVLLASAEPfPQVKLCDFG 151
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 8133 LATRLDPNEVVKITTGTAEFAAPEIVNREPVGFYTDMWATGVLSYVLLSGLSPFAGDNDVQtlKNVKACDWDFDVESFKY 8212
Cdd:cd14082   152 FARIIGEKSFRRSVVGTPAYLAPEVLRNKGYNRSLDMWSVGVIIYVSLSGTFPFNEDEDIN--DQIQNAAFMYPPNPWKE 229
                         250       260       270
                  ....*....|....*....|....*....|.
gi 281359561 8213 ISEEAKDFIRKLLVRNKEKRMTAHECLLHPW 8243
Cdd:cd14082   230 ISPDAIDLINNLLQVKMRKRYSVDKSLSHPW 260
STKc_Mnk1 cd14174
Catalytic domain of the Serine/Threonine kinase, Mitogen-activated protein kinase ...
7987-8244 4.56e-39

Catalytic domain of the Serine/Threonine kinase, Mitogen-activated protein kinase signal-integrating kinase 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MAPK signal-integrating kinases (Mnks) are MAPK-activated protein kinases and is comprised by a group of four proteins, produced by alternative splicing from two genes (Mnk1 and Mnk2). The isoforms of Mnk1 (1a/1b) and Mnk2 (2a/2b) differ at their C-termini, with the a-form having a longer C-terminus containing a MAPK-binding region. All Mnks contain a catalytic kinase domain and a polybasic region at the N-terminus which binds importin and the eukaryotic initiation factor eIF4G. The best characterized Mnk substrate is eIF4G, whose phosphorylation may promote the export of certain mRNAs from the nucleus. Mnk also phosphorylate substrates that bind to AU-rich elements that regulate mRNA stability and translation. Mnks have also been implicated in tyrosine kinase receptor signaling, inflammation, and cell prolieration or survival. The Mnk subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271076 [Multi-domain]  Cd Length: 289  Bit Score: 150.18  E-value: 4.56e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 7987 DRYDILEEI-GTGAFGVVHRCRERSTGNIFAAKFIPVSHSVEKDLIRREIDIMNQLHHQK-LINLHDAFEDDDEMILILE 8064
Cdd:cd14174     1 DLYRLTDELlGEGAYAKVQGCVSLQNGKEYAVKIIEKNAGHSRSRVFREVETLYQCQGNKnILELIEFFEDDTRFYLVFE 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 8065 FLSGGELFERITAEGYvMTEAEVINYMRQICEGIRHMHEQNIIHLDIKPENIMCQTRSSTN-VKLIDFGLATRLDPNEV- 8142
Cdd:cd14174    81 KLRGGSILAHIQKRKH-FNEREASRVVRDIASALDFLHTKGIAHRDLKPENILCESPDKVSpVKICDFDLGSGVKLNSAc 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 8143 VKITT-------GTAEFAAPEIVN--REPVGFY---TDMWATGVLSYVLLSGLSPFAGDNDV---------------QTL 8195
Cdd:cd14174   160 TPITTpelttpcGSAEYMAPEVVEvfTDEATFYdkrCDLWSLGVILYIMLSGYPPFVGHCGTdcgwdrgevcrvcqnKLF 239
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*....
gi 281359561 8196 KNVKACDWDFDVESFKYISEEAKDFIRKLLVRNKEKRMTAHECLLHPWL 8244
Cdd:cd14174   240 ESIQEGKYEFPDKDWSHISSEAKDLISKLLVRDAKERLSAAQVLQHPWV 288
STKc_MAPKAPK5 cd14171
Catalytic domain of the Serine/Threonine kinase, Mitogen-activated protein kinase-activated ...
7984-8244 8.26e-39

Catalytic domain of the Serine/Threonine kinase, Mitogen-activated protein kinase-activated protein kinase 5; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MAPK-activated protein kinase 5 (MAPKAP5 or MK5) is also called PRAK (p38-regulated/activated protein kinase). It contains a catalytic kinase domain followed by a C-terminal autoinhibitory region that contains nuclear localization (NLS) and nuclear export (NES) signals with a p38 MAPK docking motif that overlaps the NLS. MK5 is a ubiquitous protein that is implicated in neuronal morphogenesis, cell migration, and tumor angiogenesis. It interacts with PKA, which induces cytoplasmic translocation of MK5. Its substrates includes p53, ERK3/4, Hsp27, and cytosolic phospholipase A2 (cPLA2). The MAPKAPK subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271073 [Multi-domain]  Cd Length: 289  Bit Score: 149.53  E-value: 8.26e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 7984 SVYDRYDIL--EEIGTGAFGVVHRCRERSTGNIFAAKFIpvshsVEKDLIRREIdimnQLH-----HQKLINLHDAFEDD 8056
Cdd:cd14171     1 SILEEYEVNwtQKLGTGISGPVRVCVKKSTGERFALKIL-----LDRPKARTEV----RLHmmcsgHPNIVQIYDVYANS 71
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 8057 ----------DEMILILEFLSGGELFERITAEGYvMTEAEVINYMRQICEGIRHMHEQNIIHLDIKPENIMCQTRS-STN 8125
Cdd:cd14171    72 vqfpgessprARLLIVMELMEGGELFDRISQHRH-FTEKQAAQYTKQIALAVQHCHSLNIAHRDLKPENLLLKDNSeDAP 150
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 8126 VKLIDFGLAtRLDpNEVVKITTGTAEFAAPEIV------NREPVGFYT-----------DMWATGVLSYVLLSGLSPFAG 8188
Cdd:cd14171   151 IKLCDFGFA-KVD-QGDLMTPQFTPYYVAPQVLeaqrrhRKERSGIPTsptpytydkscDMWSLGVIIYIMLCGYPPFYS 228
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 281359561 8189 DNDVQTLKN-----VKACDWDFDVESFKYISEEAKDFIRKLLVRNKEKRMTAHECLLHPWL 8244
Cdd:cd14171   229 EHPSRTITKdmkrkIMTGSYEFPEEEWSQISEMAKDIVRKLLCVDPEERMTIEEVLHHPWL 289
STKc_ROCK_NDR_like cd05573
Catalytic domain of Rho-associated coiled-coil containing protein kinase (ROCK)- and Nuclear ...
7987-8247 8.64e-39

Catalytic domain of Rho-associated coiled-coil containing protein kinase (ROCK)- and Nuclear Dbf2-Related (NDR)-like Serine/Threonine Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Members of this subfamily include ROCK and ROCK-like proteins such as DMPK, MRCK, and CRIK, as well as NDR and NDR-like proteins such as LATS, CBK1 and Sid2p. ROCK and CRIK are effectors of the small GTPase Rho, while MRCK is an effector of the small GTPase Cdc42. NDR and NDR-like kinases contain an N-terminal regulatory (NTR) domain and an insert within the catalytic domain that contains an auto-inhibitory sequence. Proteins in this subfamily are involved in regulating many cellular functions including contraction, motility, division, proliferation, apoptosis, morphogenesis, and cytokinesis. The ROCK/NDR-like subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270725 [Multi-domain]  Cd Length: 350  Bit Score: 151.28  E-value: 8.64e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 7987 DRYDILEEIGTGAFGVVHRCRERSTGNIFAAKFIPVSHSVEKD---LIRREIDIMNQLHHQKLINLHDAFEDDDEMILIL 8063
Cdd:cd05573     1 DDFEVIKVIGRGAFGEVWLVRDKDTGQVYAMKILRKSDMLKREqiaHVRAERDILADADSPWIVRLHYAFQDEDHLYLVM 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 8064 EFLSGGELFERITAEGyVMTEAEVINYMRQICEGIRHMHEQNIIHLDIKPENIMCQtrSSTNVKLIDFGLATRL------ 8137
Cdd:cd05573    81 EYMPGGDLMNLLIKYD-VFPEETARFYIAELVLALDSLHKLGFIHRDIKPDNILLD--ADGHIKLADFGLCTKMnksgdr 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 8138 -----------DPNEVVKITT-------------GTAEFAAPEIVNREPVGFYTDMWATGVLSYVLLSGLSPFAGDNDVQ 8193
Cdd:cd05573   158 esylndsvntlFQDNVLARRRphkqrrvraysavGTPDYIAPEVLRGTGYGPECDWWSLGVILYEMLYGFPPFYSDSLVE 237
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 281359561 8194 TLKNVKACDwdfdvESFKY-----ISEEAKDFIRKLLVRNKEKRMTAHECLLHPWLTGD 8247
Cdd:cd05573   238 TYSKIMNWK-----ESLVFpddpdVSPEAIDLIRRLLCDPEDRLGSAEEIKAHPFFKGI 291
STKc_PLK4 cd14186
Catalytic domain of the Serine/Threonine Kinase, Polo-like kinase 4; STKs catalyze the ...
7989-8244 9.92e-39

Catalytic domain of the Serine/Threonine Kinase, Polo-like kinase 4; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PLKs play important roles in cell cycle progression and in DNA damage responses. They regulate mitotic entry, mitotic exit, and cytokinesis. In general PLKs contain an N-terminal catalytic kinase domain and a C-terminal regulatory polo box domain (PBD), which is comprised by two bipartite polo-box motifs (or polo boxes) and is involved in protein interactions. There are five mammalian PLKs (PLK1-5) from distinct genes. PLK4, also called SAK or STK18, is structurally different from other PLKs in that it contains only one polo box that can form two adjacent polo boxes and a functional PDB by homodimerization. It is required for late mitotic progression, cell survival, and embryonic development. It localizes to centrosomes and is required for centriole duplication and chromosomal stability. Overexpression of PLK4 may be associated with colon tumors. The PLK4 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271088 [Multi-domain]  Cd Length: 256  Bit Score: 148.09  E-value: 9.92e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 7989 YDILEEIGTGAFGVVHRCRERSTGNIFAAKFIPVSHSVEKDLIRR---EIDIMNQLHHQKLINLHDAFEDDDEMILILEF 8065
Cdd:cd14186     3 FKVLNLLGKGSFACVYRARSLHTGLEVAIKMIDKKAMQKAGMVQRvrnEVEIHCQLKHPSILELYNYFEDSNYVYLVLEM 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 8066 LSGGELFERITAEGYVMTEAEVINYMRQICEGIRHMHEQNIIHLDIKPENIMCQtrSSTNVKLIDFGLATRLD-PNEVVK 8144
Cdd:cd14186    83 CHNGEMSRYLKNRKKPFTEDEARHFMHQIVTGMLYLHSHGILHRDLTLSNLLLT--RNMNIKIADFGLATQLKmPHEKHF 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 8145 ITTGTAEFAAPEIVNREPVGFYTDMWATGVLSYVLLSGLSPFAGDNDVQTLKNVKACDWdfdvESFKYISEEAKDFIRKL 8224
Cdd:cd14186   161 TMCGTPNYISPEIATRSAHGLESDVWSLGCMFYTLLVGRPPFDTDTVKNTLNKVVLADY----EMPAFLSREAQDLIHQL 236
                         250       260
                  ....*....|....*....|
gi 281359561 8225 LVRNKEKRMTAHECLLHPWL 8244
Cdd:cd14186   237 LRKNPADRLSLSSVLDHPFM 256
STKc_CRIK cd05601
Catalytic domain of the Serine/Threonine Kinase, Citron Rho-interacting kinase; STKs catalyze ...
7995-8246 1.03e-38

Catalytic domain of the Serine/Threonine Kinase, Citron Rho-interacting kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. CRIK (also called citron kinase) is an effector of the small GTPase Rho. It plays an important function during cytokinesis and affects its contractile process. CRIK-deficient mice show severe ataxia and epilepsy as a result of abnormal cytokinesis and massive apoptosis in neuronal precursors. A Down syndrome critical region protein TTC3 interacts with CRIK and inhibits CRIK-dependent neuronal differentiation and neurite extension. CRIK contains a catalytic domain, a central coiled-coil domain, and a C-terminal region containing a Rho-binding domain (RBD), a zinc finger, and a pleckstrin homology (PH) domain, in addition to other motifs. The CRIK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270752 [Multi-domain]  Cd Length: 328  Bit Score: 150.54  E-value: 1.03e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 7995 IGTGAFGVVHRCRERSTGNIFAAKFIPVSHSVEKDLI---RREIDIMNQLHHQKLINLHDAFEDDDEMILILEFLSGGEL 8071
Cdd:cd05601     9 IGRGHFGEVQVVKEKATGDIYAMKVLKKSETLAQEEVsffEEERDIMAKANSPWITKLQYAFQDSENLYLVMEYHPGGDL 88
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 8072 FERITAEGYVMTEAEVINYMRQICEGIRHMHEQNIIHLDIKPENIMCQtrSSTNVKLIDFGLATRLDPNEVV--KITTGT 8149
Cdd:cd05601    89 LSLLSRYDDIFEESMARFYLAELVLAIHSLHSMGYVHRDIKPENILID--RTGHIKLADFGSAAKLSSDKTVtsKMPVGT 166
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 8150 AEFAAPEI---VNREPVGFY---TDMWATGVLSYVLLSGLSPFAGDNDVQTLKNVkacdWDFDvESFKY-----ISEEAK 8218
Cdd:cd05601   167 PDYIAPEVltsMNGGSKGTYgveCDWWSLGIVAYEMLYGKTPFTEDTVIKTYSNI----MNFK-KFLKFpedpkVSESAV 241
                         250       260
                  ....*....|....*....|....*...
gi 281359561 8219 DFIRKLLVrNKEKRMTAHECLLHPWLTG 8246
Cdd:cd05601   242 DLIKGLLT-DAKERLGYEGLCCHPFFSG 268
STKc_CCRK cd07832
Catalytic domain of the Serine/Threonine Kinase, Cell Cycle-Related Kinase; STKs catalyze the ...
7988-8245 1.40e-38

Catalytic domain of the Serine/Threonine Kinase, Cell Cycle-Related Kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. CCRK was previously called p42. It is a Cyclin-Dependent Kinase (CDK)-Activating Kinase (CAK) which is essential for the activation of CDK2. It is indispensable for cell growth and has been implicated in the progression of glioblastoma multiforme. In the heart, a splice variant of CCRK with a different C-terminal half is expressed; this variant promotes cardiac cell growth and survival and is significantly down-regulated during the development of heart failure. The CCRK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270826 [Multi-domain]  Cd Length: 287  Bit Score: 148.63  E-value: 1.40e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 7988 RYDILEEIGTGAFGVVHRCRERSTGNIFAAKFIP---VSHSVEKDLIRrEIDIMNQL-HHQKLINLHDAFEDDDEMILIL 8063
Cdd:cd07832     1 RYKILGRIGEGAHGIVFKAKDRETGETVALKKVAlrkLEGGIPNQALR-EIKALQACqGHPYVVKLRDVFPHGTGFVLVF 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 8064 EFLsGGELFERITAEGYVMTEAEVINYMRQICEGIRHMHEQNIIHLDIKPENIMcqTRSSTNVKLIDFGLAtRLDPNEVV 8143
Cdd:cd07832    80 EYM-LSSLSEVLRDEERPLTEAQVKRYMRMLLKGVAYMHANRIMHRDLKPANLL--ISSTGVLKIADFGLA-RLFSEEDP 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 8144 KITT---GTAEFAAPEIVNREPvgFYT---DMWATGVLSYVLLSGLSPFAGDNDVQTLKNV-------KACDW------- 8203
Cdd:cd07832   156 RLYShqvATRWYRAPELLYGSR--KYDegvDLWAVGCIFAELLNGSPLFPGENDIEQLAIVlrtlgtpNEKTWpeltslp 233
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....
gi 281359561 8204 DFDVESFKY------------ISEEAKDFIRKLLVRNKEKRMTAHECLLHPWLT 8245
Cdd:cd07832   234 DYNKITFPEskgirleeifpdCSPEAIDLLKGLLVYNPKKRLSAEEALRHPYFF 287
STKc_RSK2_C cd14176
C-terminal catalytic domain of the Serine/Threonine Kinase, Ribosomal S6 kinase 2 (also called ...
7987-8293 2.14e-38

C-terminal catalytic domain of the Serine/Threonine Kinase, Ribosomal S6 kinase 2 (also called 90kDa ribosomal protein S6 kinase 3 or Ribosomal protein S6 kinase alpha-3); STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. RSK2 is also called p90RSK3, RPS6KA3, S6K-alpha-3, or MAPK-activated protein kinase 1b (MAPKAPK-1b). RSK2 is expressed highly in the regions of the brain with high synaptic activity. It plays a role in the maintenance and consolidation of excitatory synapses. It is a specific modulator of phospholipase D in calcium-regulated exocytosis. Mutations in the RSK2 gene, RPS6KA3, cause Coffin-Lowry syndrome (CLS), a rare syndromic form of X-linked mental retardation characterized by growth and psychomotor retardation and skeletal abnormalities. RSK2 is one of four RSK isoforms (RSK1-4) from distinct genes present in vertebrates. RSKs contain an N-terminal kinase domain (NTD) from the AGC family and a C-terminal kinase domain (CTD) from the CAMK family. They are activated by signaling inputs from extracellular regulated kinase (ERK) and phosphoinositide dependent kinase 1 (PDK1). ERK phosphorylates and activates the CTD of RSK, serving as a docking site for PDK1, which phosphorylates and activates the NTD, which in turn phosphorylates all known RSK substrates. RSKs act as downstream effectors of mitogen-activated protein kinase (MAPK) and play key roles in mitogen-activated cell growth, differentiation, and survival. The RSK2 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271078 [Multi-domain]  Cd Length: 339  Bit Score: 149.79  E-value: 2.14e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 7987 DRYDILEEIGTGAFGVVHRCRERSTGNIFAAKFIpvshSVEKDLIRREIDIMNQL-HHQKLINLHDAFEDDDEMILILEF 8065
Cdd:cd14176    19 DGYEVKEDIGVGSYSVCKRCIHKATNMEFAVKII----DKSKRDPTEEIEILLRYgQHPNIITLKDVYDDGKYVYVVTEL 94
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 8066 LSGGELFERITAEGYvMTEAEVINYMRQICEGIRHMHEQNIIHLDIKPENIMCQTRSST--NVKLIDFGLATRLDP-NEV 8142
Cdd:cd14176    95 MKGGELLDKILRQKF-FSEREASAVLFTITKTVEYLHAQGVVHRDLKPSNILYVDESGNpeSIRICDFGFAKQLRAeNGL 173
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 8143 VKITTGTAEFAAPEIVNREPVGFYTDMWATGVLSYVLLSGLSPFAG---DNDVQTLKNVKACDWDFDVESFKYISEEAKD 8219
Cdd:cd14176   174 LMTPCYTANFVAPEVLERQGYDAACDIWSLGVLLYTMLTGYTPFANgpdDTPEEILARIGSGKFSLSGGYWNSVSDTAKD 253
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 8220 FIRKLLVRNKEKRMTAHECLLHPWLTGDHSAMKQEINR-DRYLAYREKLRRKYEDFER----FLLPIGR--LSEYSSLRK 8292
Cdd:cd14176   254 LVSKMLHVDPHQRLTAALVLRHPWIVHWDQLPQYQLNRqDAPHLVKGAMAATYSALNRnqspVLEPVGRstLAQRRGIKK 333

                  .
gi 281359561 8293 L 8293
Cdd:cd14176   334 I 334
STKc_LKB1 cd14119
Catalytic domain of the Serine/Threonine kinase, Liver Kinase B1; STKs catalyze the transfer ...
7995-8244 1.05e-37

Catalytic domain of the Serine/Threonine kinase, Liver Kinase B1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. LKB1, also called STK11, was first identified as a tumor suppressor responsible for Peutz-Jeghers syndrome, a disorder that leads to an increased risk of spontaneous epithelial cancer. It serves as a master upstream kinase that activates AMP-activated protein kinase (AMPK) and most AMPK-like kinases. LKB1 and AMPK are part of an energy-sensing pathway that links cell energy to metabolism and cell growth. They play critical roles in the establishment and maintenance of cell polarity, cell proliferation, cytoskeletal organization, as well as T-cell metabolism, including T-cell development, homeostasis, and effector function. To be activated, LKB1 requires the adaptor proteins STe20-Related ADaptor (STRAD) and mouse protein 25 (MO25). The LKB1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271021 [Multi-domain]  Cd Length: 255  Bit Score: 145.09  E-value: 1.05e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 7995 IGTGAFGVVHRCRERSTGNIFAAKFIPvshsvEKDL---------IRREIDIMNQLHHQKLINLHDAFEDDD--EMILIL 8063
Cdd:cd14119     1 LGEGSYGKVKEVLDTETLCRRAVKILK-----KRKLrripngeanVKREIQILRRLNHRNVIKLVDVLYNEEkqKLYMVM 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 8064 EFLSGGELFERITAEGYVMTEAEVINYMRQICEGIRHMHEQNIIHLDIKPENIMCQTRSStnVKLIDFGLATRLD---PN 8140
Cdd:cd14119    76 EYCVGGLQEMLDSAPDKRLPIWQAHGYFVQLIDGLEYLHSQGIIHKDIKPGNLLLTTDGT--LKISDFGVAEALDlfaED 153
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 8141 EVVKITTGTAEFAAPEIVNREPV--GFYTDMWATGVLSYVLLSGLSPFAGDNDVQTLKNVKACDWDFDVEsfkyISEEAK 8218
Cdd:cd14119   154 DTCTTSQGSPAFQPPEIANGQDSfsGFKVDIWSAGVTLYNMTTGKYPFEGDNIYKLFENIGKGEYTIPDD----VDPDLQ 229
                         250       260
                  ....*....|....*....|....*.
gi 281359561 8219 DFIRKLLVRNKEKRMTAHECLLHPWL 8244
Cdd:cd14119   230 DLLRGMLEKDPEKRFTIEQIRQHPWF 255
STKc_MSK_N cd05583
N-terminal catalytic domain of the Serine/Threonine Kinase, Mitogen and stress-activated ...
7995-8246 1.61e-37

N-terminal catalytic domain of the Serine/Threonine Kinase, Mitogen and stress-activated kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MSKs contain an N-terminal kinase domain (NTD) from the AGC family and a C-terminal kinase domain (CTD) from the CAMK family. MSKs are activated by two major signaling cascades, the Ras-MAPK and p38 stress kinase pathways, in response to various stimuli such as growth factors, hormones, neurotransmitters, cellular stress, and pro-inflammatory cytokines. This triggers phosphorylation in the activation loop (A-loop) of the CTD of MSK. The active CTD phosphorylates the hydrophobic motif (HM) in the C-terminal extension of NTD, which facilitates the phosphorylation of the A-loop and activates the NTD, which in turn phosphorylates downstream targets. MSKs are predominantly nuclear proteins. They are widely expressed in many tissues including heart, brain, lung, liver, kidney, and pancreas. There are two isoforms of MSK, called MSK1 and MSK2. The MSK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270735 [Multi-domain]  Cd Length: 268  Bit Score: 144.84  E-value: 1.61e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 7995 IGTGAFGVVHRCRERS---TGNIFAAKFIPVSHSVEK----DLIRREIDIMNQLHHQK-LINLHDAFEDDDEMILILEFL 8066
Cdd:cd05583     2 LGTGAYGKVFLVRKVGghdAGKLYAMKVLKKATIVQKaktaEHTMTERQVLEAVRQSPfLVTLHYAFQTDAKLHLILDYV 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 8067 SGGELFERITAEGYvMTEAEVINYMRQICEGIRHMHEQNIIHLDIKPENIMCQtrSSTNVKLIDFGLATRLDPNEVVKIT 8146
Cdd:cd05583    82 NGGELFTHLYQREH-FTESEVRIYIGEIVLALEHLHKLGIIYRDIKLENILLD--SEGHVVLTDFGLSKEFLPGENDRAY 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 8147 T--GTAEFAAPEIVNREPVG--FYTDMWATGVLSYVLLSGLSPFAGDNDVQTLKNVKACDWDFDVESFKYISEEAKDFIR 8222
Cdd:cd05583   159 SfcGTIEYMAPEVVRGGSDGhdKAVDWWSLGVLTYELLTGASPFTVDGERNSQSEISKRILKSHPPIPKTFSAEAKDFIL 238
                         250       260
                  ....*....|....*....|....*....
gi 281359561 8223 KLLVRNKEKRM-----TAHECLLHPWLTG 8246
Cdd:cd05583   239 KLLEKDPKKRLgagprGAHEIKEHPFFKG 267
STKc_TSSK4-like cd14162
Catalytic domain of testis-specific serine/threonine kinase 4 and similar proteins; STKs ...
7989-8244 1.95e-37

Catalytic domain of testis-specific serine/threonine kinase 4 and similar proteins; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. TSSK proteins are almost exclusively expressed postmeiotically in the testis and play important roles in spermatogenesis and/or spermiogenesis. There are five mammalian TSSK proteins which show differences in their localization and timing of expression. TSSK4, also called TSSK5, is expressed in testis from haploid round spermatids to mature spermatozoa. It phosphorylates Cre-Responsive Element Binding protein (CREB), facilitating the binding of CREB to the specific cis cAMP responsive element (CRE), which is important in activating genes related to germ cell differentiation. Mutations in the human TSSK4 gene is associated with infertile Chinese men with impaired spermatogenesis. The TSSK4-like subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271064 [Multi-domain]  Cd Length: 259  Bit Score: 144.36  E-value: 1.95e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 7989 YDILEEIGTGAFGVV-------HRCR-------ERSTGNIFAAKFIPvshsvekdlirREIDIMNQLHHQKLINLHDAFE 8054
Cdd:cd14162     2 YIVGKTLGHGSYAVVkkaystkHKCKvaikivsKKKAPEDYLQKFLP-----------REIEVIKGLKHPNLICFYEAIE 70
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 8055 DDDEMILILEFLSGGELFERITAEGYVmTEAEVINYMRQICEGIRHMHEQNIIHLDIKPENIMCQTRSstNVKLIDFGLA 8134
Cdd:cd14162    71 TTSRVYIIMELAENGDLLDYIRKNGAL-PEPQARRWFRQLVAGVEYCHSKGVVHRDLKCENLLLDKNN--NLKITDFGFA 147
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 8135 ---TRLDPNEVVKITT--GTAEFAAPEIVNREPV-GFYTDMWATGVLSYVLLSGLSPFAGDNDVQTLKNVkACDWDFdvE 8208
Cdd:cd14162   148 rgvMKTKDGKPKLSETycGSYAYASPEILRGIPYdPFLSDIWSMGVVLYTMVYGRLPFDDSNLKVLLKQV-QRRVVF--P 224
                         250       260       270
                  ....*....|....*....|....*....|....*.
gi 281359561 8209 SFKYISEEAKDFIRKLLVRNKeKRMTAHECLLHPWL 8244
Cdd:cd14162   225 KNPTVSEECKDLILRMLSPVK-KRITIEEIKRDPWF 259
STKc_MAK_like cd07830
Catalytic domain of Male germ cell-Associated Kinase-like Serine/Threonine Kinases; STKs ...
7989-8244 1.98e-37

Catalytic domain of Male germ cell-Associated Kinase-like Serine/Threonine Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily is composed of human MAK and MAK-related kinase (MRK), Saccharomyces cerevisiae Ime2p, Schizosaccharomyces pombe Mei4-dependent protein 3 (Mde3) and Pit1, Caenorhabditis elegans dyf-5, Arabidopsis thaliana MHK, and similar proteins. These proteins play important roles during meiosis. MAK is highly expressed in testicular cells specifically in the meiotic phase, but is not essential for spermatogenesis and fertility. It functions as a coactivator of the androgen receptor in prostate cells. MRK, also called Intestinal Cell Kinase (ICK), is expressed ubiquitously, with highest expression in the ovary and uterus. A missense mutation in MRK causes endocrine-cerebro-osteodysplasia, suggesting that this protein plays an important role in the development of many organs. MAK and MRK may be involved in regulating cell cycle and cell fate. Ime2p is a meiosis-specific kinase that is important during meiotic initiation and during the later stages of meiosis. Mde3 functions downstream of the transcription factor Mei-4 which is essential for meiotic prophase I. The MAK-like subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270824 [Multi-domain]  Cd Length: 283  Bit Score: 144.98  E-value: 1.98e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 7989 YDILEEIGTGAFGVVHRCRERSTGNIFA-----AKFipvsHSVEKDLIRREIDIMNQL-HHQKLINLHDAFEDDDEMILI 8062
Cdd:cd07830     1 YKVIKQLGDGTFGSVYLARNKETGELVAikkmkKKF----YSWEECMNLREVKSLRKLnEHPNIVKLKEVFRENDELYFV 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 8063 LEFLSGgELFERITA-EGYVMTEAEVINYMRQICEGIRHMHEQNIIHLDIKPENIMCqtRSSTNVKLIDFGLATRLDPN- 8140
Cdd:cd07830    77 FEYMEG-NLYQLMKDrKGKPFSESVIRSIIYQILQGLAHIHKHGFFHRDLKPENLLV--SGPEVVKIADFGLAREIRSRp 153
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 8141 ---EVVkittGTAEFAAPEIVNREPvgFYT---DMWATGVLSYVLLSgLSP-FAGDNDV-------QTLKNVKACDWD-- 8204
Cdd:cd07830   154 pytDYV----STRWYRAPEILLRST--SYSspvDIWALGCIMAELYT-LRPlFPGSSEIdqlykicSVLGTPTKQDWPeg 226
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 281359561 8205 -------------FDVESFKYI----SEEAKDFIRKLLVRNKEKRMTAHECLLHPWL 8244
Cdd:cd07830   227 yklasklgfrfpqFAPTSLHQLipnaSPEAIDLIKDMLRWDPKKRPTASQALQHPYF 283
PKc_MAPKK_plant_like cd06623
Catalytic domain of Plant dual-specificity Mitogen-Activated Protein Kinase Kinases and ...
7990-8246 2.15e-37

Catalytic domain of Plant dual-specificity Mitogen-Activated Protein Kinase Kinases and similar proteins; PKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine (ST) or tyrosine residues on protein substrates. Members of this group include MAPKKs from plants, kinetoplastids, alveolates, and mycetozoa. The MAPKK, LmxPK4, from Leishmania mexicana, is important in differentiation and virulence. Dictyostelium discoideum MEK1 is required for proper chemotaxis; MEK1 null mutants display severe defects in cell polarization and directional movement. Plants contain multiple MAPKKs like other eukaryotes. The Arabidopsis genome encodes for 10 MAPKKs while poplar and rice contain 13 MAPKKs each. The functions of these proteins have not been fully elucidated. There is evidence to suggest that MAPK cascades are involved in plant stress responses. In Arabidopsis, MKK3 plays a role in pathogen signaling; MKK2 is involved in cold and salt stress signaling; MKK4/MKK5 participates in innate immunity; and MKK7 regulates basal and systemic acquired resistance. The MAPKK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 132954 [Multi-domain]  Cd Length: 264  Bit Score: 144.27  E-value: 2.15e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 7990 DILEEIGTGAFGVVHRCRERSTGNIFAAKFIPVSHSVEKD-LIRREIDIMNQLHHQKLINLHDAFEDDDEMILILEFLSG 8068
Cdd:cd06623     4 ERVKVLGQGSSGVVYKVRHKPTGKIYALKKIHVDGDEEFRkQLLRELKTLRSCESPYVVKCYGAFYKEGEISIVLEYMDG 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 8069 GELfERITAEGYVMTEaEVINYM-RQICEGIRHMHEQ-NIIHLDIKPENIMCQTRSstNVKLIDFGLATRLDPNEVVKIT 8146
Cdd:cd06623    84 GSL-ADLLKKVGKIPE-PVLAYIaRQILKGLDYLHTKrHIIHRDIKPSNLLINSKG--EVKIADFGISKVLENTLDQCNT 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 8147 -TGTAEFAAPEIVNREPVGFYTDMWATGVLSYVLLSGLSPFAGDND---VQTLKNVkaCDwdFDVESFKY--ISEEAKDF 8220
Cdd:cd06623   160 fVGTVTYMSPERIQGESYSYAADIWSLGLTLLECALGKFPFLPPGQpsfFELMQAI--CD--GPPPSLPAeeFSPEFRDF 235
                         250       260
                  ....*....|....*....|....*.
gi 281359561 8221 IRKLLVRNKEKRMTAHECLLHPWLTG 8246
Cdd:cd06623   236 ISACLQKDPKKRPSAAELLQHPFIKK 261
STKc_MEKK3_like cd06625
Catalytic domain of Mitogen-Activated Protein (MAP)/Extracellular signal-Regulated Kinase (ERK) ...
7995-8243 3.67e-37

Catalytic domain of Mitogen-Activated Protein (MAP)/Extracellular signal-Regulated Kinase (ERK) Kinase Kinase 3-like Serine/Threonine Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily is composed of MEKK3, MEKK2, and related proteins; all contain an N-terminal PB1 domain, which mediates oligomerization, and a C-terminal catalytic domain. MEKK2 and MEKK3 are MAPK kinase kinases (MAPKKKs or MKKK) that activate MEK5 (also called MKK5), which activates ERK5. The ERK5 cascade plays roles in promoting cell proliferation, differentiation, neuronal survival, and neuroprotection. MEKK3 plays an essential role in embryonic angiogenesis and early heart development. MEKK2 and MEKK3 can also activate the MAPKs, c-Jun N-terminal kinase (JNK) and p38, through their respective MAPKKs. The MEKK3-like subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270795 [Multi-domain]  Cd Length: 260  Bit Score: 143.65  E-value: 3.67e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 7995 IGTGAFGVVHRCRERSTGNIFAAKFIPVSH-----SVEKDLIRREIDIMNQLHHQKLINLHDAFEDDDEMILILEFLSGG 8069
Cdd:cd06625     8 LGQGAFGQVYLCYDADTGRELAVKQVEIDPinteaSKEVKALECEIQLLKNLQHERIVQYYGCLQDEKSLSIFMEYMPGG 87
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 8070 ELFERITAEGyVMTEAEVINYMRQICEGIRHMHEQNIIHLDIKPENIMcqtRSST-NVKLIDFGLATRLDP---NEVVKI 8145
Cdd:cd06625    88 SVKDEIKAYG-ALTENVTRKYTRQILEGLAYLHSNMIVHRDIKGANIL---RDSNgNVKLGDFGASKRLQTicsSTGMKS 163
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 8146 TTGTAEFAAPEIVNREPVGFYTDMWATGVLSYVLLSGLSPFAGDNDVQTLKNVKACDWDFDVESfkYISEEAKDFIRKLL 8225
Cdd:cd06625   164 VTGTPYWMSPEVINGEGYGRKADIWSVGCTVVEMLTTKPPWAEFEPMAAIFKIATQPTNPQLPP--HVSEDARDFLSLIF 241
                         250
                  ....*....|....*...
gi 281359561 8226 VRNKEKRMTAHECLLHPW 8243
Cdd:cd06625   242 VRNKKQRPSAEELLSHSF 259
STKc_RSK4_C cd14177
C-terminal catalytic domain of the Serine/Threonine Kinase, Ribosomal S6 kinase 4 (also called ...
7987-8245 4.86e-37

C-terminal catalytic domain of the Serine/Threonine Kinase, Ribosomal S6 kinase 4 (also called Ribosomal protein S6 kinase alpha-6 or 90kDa ribosomal protein S6 kinase 6); STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. RSK4 is also called S6K-alpha-6, RPS6KA6, p90RSK6 or pp90RSK4. RSK4 is a substrate of ERK and is a modulator of p53-dependent proliferation arrest in human cells. Deletion of the RSK4 gene, RPS6KA6, frequently occurs in patients of X-linked deafness type 3, mental retardation and choroideremia. Studies of RSK4 in cancer cells and tissues suggest that it may be oncogenic or tumor suppressive depending on many factors. RSK4 is one of four RSK isoforms (RSK1-4) from distinct genes present in vertebrates. RSKs contain an N-terminal kinase domain (NTD) from the AGC family and a C-terminal kinase domain (CTD) from the CAMK family. They are activated by signaling inputs from extracellular regulated kinase (ERK) and phosphoinositide dependent kinase 1 (PDK1). ERK phosphorylates and activates the CTD of RSK, serving as a docking site for PDK1, which phosphorylates and activates the NTD, which in turn phosphorylates all known RSK substrates. RSKs act as downstream effectors of mitogen-activated protein kinase (MAPK) and play key roles in mitogen-activated cell growth, differentiation, and survival. The RSK4 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271079 [Multi-domain]  Cd Length: 295  Bit Score: 144.39  E-value: 4.86e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 7987 DRYDILEEIGTGAFGVVHRCRERSTGNIFAAKFIPVShsveKDLIRREIDI-MNQLHHQKLINLHDAFEDDDEMILILEF 8065
Cdd:cd14177     4 DVYELKEDIGVGSYSVCKRCIHRATNMEFAVKIIDKS----KRDPSEEIEIlMRYGQHPNIITLKDVYDDGRYVYLVTEL 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 8066 LSGGELFERITAEGYvMTEAEVINYMRQICEGIRHMHEQNIIHLDIKPENI--MCQTRSSTNVKLIDFGLATRLDPNEVV 8143
Cdd:cd14177    80 MKGGELLDRILRQKF-FSEREASAVLYTITKTVDYLHCQGVVHRDLKPSNIlyMDDSANADSIRICDFGFAKQLRGENGL 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 8144 KITTG-TAEFAAPEIVNREPVGFYTDMWATGVLSYVLLSGLSPFA-GDNDV--QTLKNVKACDWDFDVESFKYISEEAKD 8219
Cdd:cd14177   159 LLTPCyTANFVAPEVLMRQGYDAACDIWSLGVLLYTMLAGYTPFAnGPNDTpeEILLRIGSGKFSLSGGNWDTVSDAAKD 238
                         250       260
                  ....*....|....*....|....*.
gi 281359561 8220 FIRKLLVRNKEKRMTAHECLLHPWLT 8245
Cdd:cd14177   239 LLSHMLHVDPHQRYTAEQVLKHSWIA 264
STKc_PLK2 cd14188
Catalytic domain of the Serine/Threonine Kinase, Polo-like kinase 2; STKs catalyze the ...
7995-8241 6.94e-37

Catalytic domain of the Serine/Threonine Kinase, Polo-like kinase 2; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PLKs play important roles in cell cycle progression and in DNA damage responses. They regulate mitotic entry, mitotic exit, and cytokinesis. In general PLKs contain an N-terminal catalytic kinase domain and a C-terminal regulatory polo box domain (PBD), which is comprised by two bipartite polo-box motifs (or polo boxes) and is involved in protein interactions. There are five mammalian PLKs (PLK1-5) from distinct genes. PLK2, also called Snk (serum-inducible kinase), functions in G1 progression, S-phase arrest, and centriole duplication. Its gene is responsive to both growth factors and cellular stress, is a transcriptional target of p53, and activates a G2-M checkpoint. The PLK2 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271090 [Multi-domain]  Cd Length: 255  Bit Score: 142.84  E-value: 6.94e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 7995 IGTGAFGVVHRCRERSTGNIFAAKFIP---VSHSVEKDLIRREIDIMNQLHHQKLINLHDAFEDDDEMILILEFLSGGEL 8071
Cdd:cd14188     9 LGKGGFAKCYEMTDLTTNKVYAAKIIPhsrVSKPHQREKIDKEIELHRILHHKHVVQFYHYFEDKENIYILLEYCSRRSM 88
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 8072 FERITAEGyVMTEAEVINYMRQICEGIRHMHEQNIIHLDIKPENIMcqTRSSTNVKLIDFGLATRLDPNEVVKITT-GTA 8150
Cdd:cd14188    89 AHILKARK-VLTEPEVRYYLRQIVSGLKYLHEQEILHRDLKLGNFF--INENMELKVGDFGLAARLEPLEHRRRTIcGTP 165
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 8151 EFAAPEIVNREPVGFYTDMWATGVLSYVLLSGLSPFAGDNDVQTLKNVKACDWDFDVEsfkyISEEAKDFIRKLLVRNKE 8230
Cdd:cd14188   166 NYLSPEVLNKQGHGCESDIWALGCVMYTMLLGRPPFETTNLKETYRCIREARYSLPSS----LLAPAKHLIASMLSKNPE 241
                         250
                  ....*....|.
gi 281359561 8231 KRMTAHECLLH 8241
Cdd:cd14188   242 DRPSLDEIIRH 252
STKc_STK33 cd14097
Catalytic domain of Serine/Threonine Kinase 33; STKs catalyze the transfer of the ...
7995-8244 1.25e-36

Catalytic domain of Serine/Threonine Kinase 33; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. STK33 is highly expressed in the testis and is present in low levels in most tissues. It may be involved in spermatogenesis and organ ontogenesis. It interacts with and phosphorylates vimentin and may be involved in regulating intermediate filament cytoskeletal dynamics. Its role in promoting the cell viability of KRAS-dependent cancer cells is under debate; some studies have found STK33 to promote cancer cell viability, while other studies have found it to be non-essential. KRAS is the most commonly mutated human oncogene, thus, studies on the role of STK33 in KRAS mutant cancer cells are important. The STK33 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270999 [Multi-domain]  Cd Length: 266  Bit Score: 142.30  E-value: 1.25e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 7995 IGTGAFGVVHRCRERSTGNIFAAKFI--PVSHSVEKDLIRREIDIMNQLHHQKLINLHDAFEDDDEMILILEFLSGGELF 8072
Cdd:cd14097     9 LGQGSFGVVIEATHKETQTKWAIKKInrEKAGSSAVKLLEREVDILKHVNHAHIIHLEEVFETPKRMYLVMELCEDGELK 88
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 8073 ERITAEGyVMTEAEVINYMRQICEGIRHMHEQNIIHLDIKPENIMCQT-----RSSTNVKLIDFGLATRLD--PNEVVKI 8145
Cdd:cd14097    89 ELLLRKG-FFSENETRHIIQSLASAVAYLHKNDIVHRDLKLENILVKSsiidnNDKLNIKVTDFGLSVQKYglGEDMLQE 167
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 8146 TTGTAEFAAPEIVNREPVGFYTDMWATGVLSYVLLSGLSPFAGDNDVQTLKNVKACDWDFDVESFKYISEEAKDFIRKLL 8225
Cdd:cd14097   168 TCGTPIYMAPEVISAHGYSQQCDIWSIGVIMYMLLCGEPPFVAKSEEKLFEEIRKGDLTFTQSVWQSVSDAAKNVLQQLL 247
                         250
                  ....*....|....*....
gi 281359561 8226 VRNKEKRMTAHECLLHPWL 8244
Cdd:cd14097   248 KVDPAHRMTASELLDNPWI 266
STKc_Aurora-A cd14116
Catalytic domain of the Serine/Threonine kinase, Aurora-A kinase; STKs catalyze the transfer ...
7987-8245 1.50e-36

Catalytic domain of the Serine/Threonine kinase, Aurora-A kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Aurora kinases are key regulators of mitosis and are essential for the accurate and equal division of genomic material from parent to daughter cells. Vertebrates contain at least 2 Aurora kinases (A and B); mammals contains a third Aurora kinase gene (C). Aurora-A regulates cell cycle events from the late S-phase through the M-phase including centrosome maturation, mitotic entry, centrosome separation, spindle assembly, chromosome alignment, cytokinesis, and mitotic exit. Aurora-A activation depends on its autophosphorylation and binding to the microtubule-associated protein TPX2, which also localizes the kinase to spindle microtubules. Aurora-A is overexpressed in many cancer types such as prostate, ovarian, breast, bladder, gastric, and pancreatic. The Aurora subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271018 [Multi-domain]  Cd Length: 258  Bit Score: 141.63  E-value: 1.50e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 7987 DRYDILEEIGTGAFGVVHRCRERSTGNIFAAKFIPVSH----SVEKDLiRREIDIMNQLHHQKLINLHDAFEDDDEMILI 8062
Cdd:cd14116     5 EDFEIGRPLGKGKFGNVYLAREKQSKFILALKVLFKAQlekaGVEHQL-RREVEIQSHLRHPNILRLYGYFHDATRVYLI 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 8063 LEFLSGGELFERITAEGyVMTEAEVINYMRQICEGIRHMHEQNIIHLDIKPENIMCQtrSSTNVKLIDFGLATRLdPNEV 8142
Cdd:cd14116    84 LEYAPLGTVYRELQKLS-KFDEQRTATYITELANALSYCHSKRVIHRDIKPENLLLG--SAGELKIADFGWSVHA-PSSR 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 8143 VKITTGTAEFAAPEIVNREPVGFYTDMWATGVLSYVLLSGLSPFAGDNDVQTLKNVKACDWDFDVesfkYISEEAKDFIR 8222
Cdd:cd14116   160 RTTLCGTLDYLPPEMIEGRMHDEKVDLWSLGVLCYEFLVGKPPFEANTYQETYKRISRVEFTFPD----FVTEGARDLIS 235
                         250       260
                  ....*....|....*....|...
gi 281359561 8223 KLLVRNKEKRMTAHECLLHPWLT 8245
Cdd:cd14116   236 RLLKHNPSQRPMLREVLEHPWIT 258
STKc_phototropin_like cd05574
Catalytic domain of Phototropin-like Serine/Threonine Kinases; STKs catalyze the transfer of ...
7987-8246 1.84e-36

Catalytic domain of Phototropin-like Serine/Threonine Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Phototropins are blue-light receptors that control responses such as phototropism, stromatal opening, and chloroplast movement in order to optimize the photosynthetic efficiency of plants. They are light-activated STKs that contain an N-terminal photosensory domain and a C-terminal catalytic domain. The N-terminal domain contains two LOV (Light, Oxygen or Voltage) domains that binds FMN. Photoexcitation of the LOV domains results in autophosphorylation at multiple sites and activation of the catalytic domain. In addition to plant phototropins, included in this subfamily are predominantly uncharacterized fungal STKs whose catalytic domains resemble the phototropin kinase domain. One protein from Neurospora crassa is called nrc-2, which plays a role in growth and development by controlling entry into the conidiation program. The phototropin-like subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270726 [Multi-domain]  Cd Length: 316  Bit Score: 143.53  E-value: 1.84e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 7987 DRYDILEEIGTGAFGVVHRCRERSTGNIFAAKFIPVSHSVEKDLIRR---EIDIMNQLHHQKLINLHDAFEDDDEMILIL 8063
Cdd:cd05574     1 DHFKKIKLLGKGDVGRVYLVRLKGTGKLFAMKVLDKEEMIKRNKVKRvltEREILATLDHPFLPTLYASFQTSTHLCFVM 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 8064 EFLSGGELFE-RITAEGYVMTEAEVINYMRQICEGIRHMHEQNIIHLDIKPENIMcqTRSSTNVKLIDFGLATRLDPNEV 8142
Cdd:cd05574    81 DYCPGGELFRlLQKQPGKRLPEEVARFYAAEVLLALEYLHLLGFVYRDLKPENIL--LHESGHIMLTDFDLSKQSSVTPP 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 8143 VKITT------------------------------GTAEFAAPEIVNREPVGFYTDMWATGVLSYVLLSGLSPFAGDNDV 8192
Cdd:cd05574   159 PVRKSlrkgsrrssvksieketfvaepsarsnsfvGTEEYIAPEVIKGDGHGSAVDWWTLGILLYEMLYGTTPFKGSNRD 238
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 281359561 8193 QTLKNVKACDWDFDveSFKYISEEAKDFIRKLLVRNKEKRM----TAHECLLHPWLTG 8246
Cdd:cd05574   239 ETFSNILKKELTFP--ESPPVSSEAKDLIRKLLVKDPSKRLgskrGASEIKRHPFFRG 294
STKc_Rim15_like cd05611
Catalytic domain of fungal Rim15-like Protein Serine/Threonine Kinases; STKs catalyze the ...
7992-8243 1.89e-36

Catalytic domain of fungal Rim15-like Protein Serine/Threonine Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Members of this group include Saccharomyces cerevisiae Rim15, Schizosaccharomyces pombe cek1, and similar fungal proteins. They contain a central catalytic domain, which contains an insert relative to MAST kinases. In addition, Rim15 contains a C-terminal signal receiver (REC) domain while cek1 contains an N-terminal PAS domain. Rim15 (or Rim15p) functions as a regulator of meiosis. It acts as a downstream effector of PKA and regulates entry into stationary phase (G0). Thus, it plays a crucial role in regulating yeast proliferation, differentiation, and aging. Cek1 may facilitate progression of mitotic anaphase. The Rim15-like subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270762 [Multi-domain]  Cd Length: 263  Bit Score: 141.85  E-value: 1.89e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 7992 LEEIGTGAFGVVHRCRERSTGNIFAAKFIPVSHSVEKDLIR-----REIdIMNQLHHQKLINLHDAFEDDDEMILILEFL 8066
Cdd:cd05611     1 LKPISKGAFGSVYLAKKRSTGDYFAIKVLKKSDMIAKNQVTnvkaeRAI-MMIQGESPYVAKLYYSFQSKDYLYLVMEYL 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 8067 SGGELFERITAEGYvMTEAEVINYMRQICEGIRHMHEQNIIHLDIKPENIMCQTRSstNVKLIDFGLATRLDPNEVVKIT 8146
Cdd:cd05611    80 NGGDCASLIKTLGG-LPEDWAKQYIAEVVLGVEDLHQRGIIHRDIKPENLLIDQTG--HLKLTDFGLSRNGLEKRHNKKF 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 8147 TGTAEFAAPEIVNREPVGFYTDMWATGVLSYVLLSGLSPFAGDNDVQTLKNVKACDWDFDVESFKYISEEAKDFIRKLLV 8226
Cdd:cd05611   157 VGTPDYLAPETILGVGDDKMSDWWSLGCVIFEFLFGYPPFHAETPDAVFDNILSRRINWPEEVKEFCSPEAVDLINRLLC 236
                         250       260
                  ....*....|....*....|
gi 281359561 8227 RNKEKRMTAH---ECLLHPW 8243
Cdd:cd05611   237 MDPAKRLGANgyqEIKSHPF 256
STKc_NDR_like cd05599
Catalytic domain of Nuclear Dbf2-Related kinase-like Protein Serine/Threonine Kinases; STKs ...
7989-8246 2.39e-36

Catalytic domain of Nuclear Dbf2-Related kinase-like Protein Serine/Threonine Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. NDR kinases regulate mitosis, cell growth, embryonic development, and neurological processes. They are also required for proper centrosome duplication. Higher eukaryotes contain two NDR isoforms, NDR1 and NDR2. This subfamily also contains fungal NDR-like kinases. NDR kinase contains an N-terminal regulatory (NTR) domain and an insert within the catalytic domain that contains an auto-inhibitory sequence. Like many other AGC kinases, NDR kinase requires phosphorylation at two sites, the activation loop (A-loop) and the hydrophobic motif (HM), for activity. The NDR kinase subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270750 [Multi-domain]  Cd Length: 324  Bit Score: 143.52  E-value: 2.39e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 7989 YDILEEIGTGAFGVVHRCRERSTGNIFAAKFIPVSHSVEKDL---IRREIDIMNQLHHQKLINLHDAFEDDDEMILILEF 8065
Cdd:cd05599     3 FEPLKVIGRGAFGEVRLVRKKDTGHVYAMKKLRKSEMLEKEQvahVRAERDILAEADNPWVVKLYYSFQDEENLYLIMEF 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 8066 LSGGE----LFERITaegyvMTEAEVINYMRQICEGIRHMHEQNIIHLDIKPENIMCQTRSstNVKLIDFGLATRLDPNE 8141
Cdd:cd05599    83 LPGGDmmtlLMKKDT-----LTEEETRFYIAETVLAIESIHKLGYIHRDIKPDNLLLDARG--HIKLSDFGLCTGLKKSH 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 8142 VVKITTGTAEFAAPEIVNREPVGFYTDMWATGVLSYVLLSGLSPFAGDNDVQTLKnvKACDWDfdvESFKY-----ISEE 8216
Cdd:cd05599   156 LAYSTVGTPDYIAPEVFLQKGYGKECDWWSLGVIMYEMLIGYPPFCSDDPQETCR--KIMNWR---ETLVFppevpISPE 230
                         250       260       270
                  ....*....|....*....|....*....|...
gi 281359561 8217 AKDFIRKLLVrNKEKRMTAH---ECLLHPWLTG 8246
Cdd:cd05599   231 AKDLIERLLC-DAEHRLGANgveEIKSHPFFKG 262
STKc_Mnk2 cd14173
Catalytic domain of the Serine/Threonine kinase, Mitogen-activated protein kinase ...
7987-8244 2.79e-36

Catalytic domain of the Serine/Threonine kinase, Mitogen-activated protein kinase signal-integrating kinase 2; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MAPK signal-integrating kinases (Mnks) are MAPK-activated protein kinases and is comprised by a group of four proteins, produced by alternative splicing from two genes (Mnk1 and Mnk2). The isoforms of Mnk1 (1a/1b) and Mnk2 (2a/2b) differ at their C-termini, with the a-form having a longer C-terminus containing a MAPK-binding region. All Mnks contain a catalytic kinase domain and a polybasic region at the N-terminus which binds importin and the eukaryotic initiation factor eIF4G. The best characterized Mnk substrate is eIF4G, whose phosphorylation may promote the export of certain mRNAs from the nucleus. Mnk also phosphorylate substrates that bind to AU-rich elements that regulate mRNA stability and translation. Mnks have also been implicated in tyrosine kinase receptor signaling, inflammation, and cell prolieration or survival. The Mnk subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271075 [Multi-domain]  Cd Length: 288  Bit Score: 142.09  E-value: 2.79e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 7987 DRYDILEEI-GTGAFGVVHRCRERSTGNIFAAKFIPVSHSVEKDLIRREIDIMNQLH-HQKLINLHDAFEDDDEMILILE 8064
Cdd:cd14173     1 DVYQLQEEVlGEGAYARVQTCINLITNKEYAVKIIEKRPGHSRSRVFREVEMLYQCQgHRNVLELIEFFEEEDKFYLVFE 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 8065 FLSGGELFERITAEGYvMTEAEVINYMRQICEGIRHMHEQNIIHLDIKPENIMCQTRSSTN-VKLIDFGLATRLDPN-EV 8142
Cdd:cd14173    81 KMRGGSILSHIHRRRH-FNELEASVVVQDIASALDFLHNKGIAHRDLKPENILCEHPNQVSpVKICDFDLGSGIKLNsDC 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 8143 VKITT-------GTAEFAAPEIVN--REPVGFY---TDMWATGVLSYVLLSGLSPFAG----DNDVQTLKNVKACD---- 8202
Cdd:cd14173   160 SPISTpelltpcGSAEYMAPEVVEafNEEASIYdkrCDLWSLGVILYIMLSGYPPFVGrcgsDCGWDRGEACPACQnmlf 239
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*....
gi 281359561 8203 -------WDFDVESFKYISEEAKDFIRKLLVRNKEKRMTAHECLLHPWL 8244
Cdd:cd14173   240 esiqegkYEFPEKDWAHISCAAKDLISKLLVRDAKQRLSAAQVLQHPWV 288
STKc_GSK3 cd14137
The catalytic domain of the Serine/Threonine Kinase, Glycogen Synthase Kinase 3; STKs catalyze ...
7988-8242 5.47e-36

The catalytic domain of the Serine/Threonine Kinase, Glycogen Synthase Kinase 3; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. GSK3 is a mutifunctional kinase involved in many cellular processes including cell division, proliferation, differentiation, adhesion, and apoptosis. In plants, GSK3 plays a role in the response to osmotic stress. In Caenorhabditis elegans, it plays a role in regulating normal oocyte-to-embryo transition and response to oxidative stress. In Chlamydomonas reinhardtii, GSK3 regulates flagellar length and assembly. In mammals, there are two isoforms, GSK3alpha and GSK3beta, which show both distinct and redundant functions. The two isoforms differ mainly in their N-termini. They are both involved in axon formation and in Wnt signaling.They play distinct roles in cardiogenesis, with GSKalpha being essential in cardiomyocyte survival, and GSKbeta regulating heart positioning and left-right symmetry. GSK3beta was first identified as a regulator of glycogen synthesis, but has since been determined to play other roles. It regulates the degradation of beta-catenin and IkB. Beta-catenin is the main effector of Wnt, which is involved in normal haematopoiesis and stem cell function. IkB is a central inhibitor of NF-kB, which is critical in maintaining leukemic cell growth. GSK3beta is enriched in the brain and is involved in regulating neuronal signaling pathways. It is implicated in the pathogenesis of many diseases including Type II diabetes, obesity, mood disorders, Alzheimer's disease, osteoporosis, and some types of cancer, among others. The GSK3 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271039 [Multi-domain]  Cd Length: 293  Bit Score: 141.49  E-value: 5.47e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 7988 RYDILEEIGTGAFGVVHRCRERSTGNIFAAKfipvshSVEKD--LIRREIDIMNQLHHQKLINLHDAF----EDDDEMIL 8061
Cdd:cd14137     5 SYTIEKVIGSGSFGVVYQAKLLETGEVVAIK------KVLQDkrYKNRELQIMRRLKHPNIVKLKYFFyssgEKKDEVYL 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 8062 --ILEFLSGgELFERI---TAEGYVMTEAEVINYMRQICEGIRHMHEQNIIHLDIKPENIMCQtRSSTNVKLIDFGLATR 8136
Cdd:cd14137    79 nlVMEYMPE-TLYRVIrhySKNKQTIPIIYVKLYSYQLFRGLAYLHSLGICHRDIKPQNLLVD-PETGVLKLCDFGSAKR 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 8137 LDPNEvvkitTGTAEFA-----APE-IVNREpvgFYT---DMWATG-VLSYVLLsGLSPFAGDNDVQTLK---------- 8196
Cdd:cd14137   157 LVPGE-----PNVSYICsryyrAPElIFGAT---DYTtaiDIWSAGcVLAELLL-GQPLFPGESSVDQLVeiikvlgtpt 227
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 281359561 8197 -----------------NVKACDWDfDVESfKYISEEAKDFIRKLLVRNKEKRMTAHECLLHP 8242
Cdd:cd14137   228 reqikamnpnytefkfpQIKPHPWE-KVFP-KRTPPDAIDLLSKILVYNPSKRLTALEALAHP 288
STKc_CDK_like cd07829
Catalytic domain of Cyclin-Dependent protein Kinase-like Serine/Threonine Kinases; STKs ...
7989-8244 6.03e-36

Catalytic domain of Cyclin-Dependent protein Kinase-like Serine/Threonine Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. CDKs belong to a large family of STKs that are regulated by their cognate cyclins. Together, they are involved in the control of cell-cycle progression, transcription, and neuronal function. CDKs are partly regulated by their subcellular localization, which defines substrate phosphorylation and the resulting specific function. CDK1, CDK2, CDK4, and CDK6 have well-defined functions in the cell cycle, such as the regulation of the early G1 phase by CDK4 or CDK6, the G1/S phase transition by CDK2, or the entry of mitosis by CDK1. They also exhibit overlapping cyclin specificity and functions in certain conditions. Knockout mice with a single CDK deleted remain viable with specific phenotypes, showing that some CDKs can compensate for each other. For example, CDK4 can compensate for the loss of CDK6, however, double knockout mice with both CDK4 and CDK6 deleted die in utero. CDK8 and CDK9 are mainly involved in transcription while CDK5 is implicated in neuronal function. CDK7 plays essential roles in both the cell cycle as a CDK-Activating Kinase (CAK) and in transcription as a component of the general transcription factor TFIIH. The CDK-like subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270823 [Multi-domain]  Cd Length: 282  Bit Score: 140.70  E-value: 6.03e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 7989 YDILEEIGTGAFGVVHRCRERSTGNIFAAKFIPVSHsvEKDLIR----REIDIMNQLHHQKLINLHDAFEDDDEMILILE 8064
Cdd:cd07829     1 YEKLEKLGEGTYGVVYKAKDKKTGEIVALKKIRLDN--EEEGIPstalREISLLKELKHPNIVKLLDVIHTENKLYLVFE 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 8065 FLSGgELFERITAEGYVMTEAEVINYMRQICEGIRHMHEQNIIHLDIKPENIMCqTRSSTnVKLIDFGLA------TRLD 8138
Cdd:cd07829    79 YCDQ-DLKKYLDKRPGPLPPNLIKSIMYQLLRGLAYCHSHRILHRDLKPQNLLI-NRDGV-LKLADFGLArafgipLRTY 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 8139 PNEVVkittgTAEFAAPEIVNREPvgFYT---DMWATGVLSYVLLSGLSPFAGDNDVQTLK---------------NVKA 8200
Cdd:cd07829   156 THEVV-----TLWYRAPEILLGSK--HYStavDIWSVGCIFAELITGKPLFPGDSEIDQLFkifqilgtpteeswpGVTK 228
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....
gi 281359561 8201 -CDWDFDVESFKY---------ISEEAKDFIRKLLVRNKEKRMTAHECLLHPWL 8244
Cdd:cd07829   229 lPDYKPTFPKWPKndlekvlprLDPEGIDLLSKMLQYNPAKRISAKEALKHPYF 282
STKc_SnRK2 cd14662
Catalytic domain of the Serine/Threonine Kinases, Sucrose nonfermenting 1-related protein ...
7988-8243 7.38e-36

Catalytic domain of the Serine/Threonine Kinases, Sucrose nonfermenting 1-related protein kinase subfamily 2; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The SnRKs form three different subfamilies designated SnRK1-3. SnRK2 is represented in this cd. SnRK2s are involved in plant response to abiotic stresses and abscisic acid (ABA)-dependent plant development. The SnRK2s subfamily is in turn classed into three subgroups, all 3 of which are represented in this CD. Group 1 comprises kinases not activated by ABA, group 2 - kinases not activated or activated very weakly by ABA (depending on plant species), and group 3 - kinases strongly activated by ABA. The SnRKs belong to a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271132 [Multi-domain]  Cd Length: 257  Bit Score: 139.90  E-value: 7.38e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 7988 RYDILEEIGTGAFGVVHRCRERSTGNIFAAKFIPVSHSVEKDlIRREIDIMNQLHHQKLINLHDAFEDDDEMILILEFLS 8067
Cdd:cd14662     1 RYELVKDIGSGNFGVARLMRNKETKELVAVKYIERGLKIDEN-VQREIINHRSLRHPNIIRFKEVVLTPTHLAIVMEYAA 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 8068 GGELFERITAEGYvMTEAEVINYMRQICEGIRHMHEQNIIHLDIKPENIMCQTRSSTNVKLIDFGLATRLDPNEVVKITT 8147
Cdd:cd14662    80 GGELFERICNAGR-FSEDEARYFFQQLISGVSYCHSMQICHRDLKLENTLLDGSPAPRLKICDFGYSKSSVLHSQPKSTV 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 8148 GTAEFAAPEIVNR-EPVGFYTDMWATGVLSYVLLSGLSPFAGDNDVQTLKNV--KACDWDFDVESFKYISEEAKDFIRKL 8224
Cdd:cd14662   159 GTPAYIAPEVLSRkEYDGKVADVWSCGVTLYVMLVGAYPFEDPDDPKNFRKTiqRIMSVQYKIPDYVRVSQDCRHLLSRI 238
                         250
                  ....*....|....*....
gi 281359561 8225 LVRNKEKRMTAHECLLHPW 8243
Cdd:cd14662   239 FVANPAKRITIPEIKNHPW 257
STKc_CDK7 cd07841
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 7; STKs ...
7988-8245 7.90e-36

Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 7; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. CDK7 plays essential roles in the cell cycle and in transcription. It associates with cyclin H and MAT1 and acts as a CDK-Activating Kinase (CAK) by phosphorylating and activating cell cycle CDKs (CDK1/2/4/6). In the brain, it activates CDK5. CDK7 is also a component of the general transcription factor TFIIH, which phosphorylates the C-terminal domain (CTD) of RNA polymerase II when it is bound with unphosphorylated DNA, as present in the pre-initiation complex. Following phosphorylation, the CTD dissociates from the DNA which allows transcription initiation. CDKs belong to a large family of STKs that are regulated by their cognate cyclins. Together, they are involved in the control of cell-cycle progression, transcription, and neuronal function. The CDK7 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270833 [Multi-domain]  Cd Length: 298  Bit Score: 141.17  E-value: 7.90e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 7988 RYDILEEIGTGAFGVVHRCRERSTGNIFAAKFIPVSH-SVEKDLIR----REIDIMNQLHHQKLINLHDAFEDDDEMILI 8062
Cdd:cd07841     1 RYEKGKKLGEGTYAVVYKARDKETGRIVAIKKIKLGErKEAKDGINftalREIKLLQELKHPNIIGLLDVFGHKSNINLV 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 8063 LEFLSGgELFERITAEGYVMTEAEVINYMRQICEGIRHMHEQNIIHLDIKPENIMCqtrsSTN--VKLIDFGLATRL-DP 8139
Cdd:cd07841    81 FEFMET-DLEKVIKDKSIVLTPADIKSYMLMTLRGLEYLHSNWILHRDLKPNNLLI----ASDgvLKLADFGLARSFgSP 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 8140 NEVVKITTGTAEFAAPEIV-NREPVGFYTDMWATGVLSYVLLSGLSPFAGDNDVQTLKNV-KAC------DW-------- 8203
Cdd:cd07841   156 NRKMTHQVVTRWYRAPELLfGARHYGVGVDMWSVGCIFAELLLRVPFLPGDSDIDQLGKIfEALgtpteeNWpgvtslpd 235
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|.
gi 281359561 8204 -----DFDVESFKYI----SEEAKDFIRKLLVRNKEKRMTAHECLLHPWLT 8245
Cdd:cd07841   236 yvefkPFPPTPLKQIfpaaSDDALDLLQRLLTLNPNKRITARQALEHPYFS 286
STKc_PKC cd05570
Catalytic domain of the Serine/Threonine Kinase, Protein Kinase C; STKs catalyze the transfer ...
7995-8233 1.05e-35

Catalytic domain of the Serine/Threonine Kinase, Protein Kinase C; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PKCs are classified into three groups (classical, atypical, and novel) depending on their mode of activation and the structural characteristics of their regulatory domain. PKCs undergo three phosphorylations in order to take mature forms. In addition, classical PKCs depend on calcium, DAG (1,2-diacylglycerol), and in most cases, phosphatidylserine (PS) for activation. Novel PKCs are calcium-independent, but require DAG and PS for activity, while atypical PKCs only require PS. PKCs phosphorylate and modify the activities of a wide variety of cellular proteins including receptors, enzymes, cytoskeletal proteins, transcription factors, and other kinases. They play a central role in signal transduction pathways that regulate cell migration and polarity, proliferation, differentiation, and apoptosis. Also included in this subfamily are the PKC-like proteins, called PKNs. The PKC subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270722 [Multi-domain]  Cd Length: 318  Bit Score: 141.20  E-value: 1.05e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 7995 IGTGAFGVVHRCRERSTGNIFAAKfipvshSVEKDLIRREIDI---MNQ-------LHHQKLINLHDAFEDDDEMILILE 8064
Cdd:cd05570     3 LGKGSFGKVMLAERKKTDELYAIK------VLKKEVIIEDDDVectMTEkrvlalaNRHPFLTGLHACFQTEDRLYFVME 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 8065 FLSGGELFERITAEGyVMTEAEVINYMRQICEGIRHMHEQNIIHLDIKPENIMCQTRSstNVKLIDFGLAtRLDPNEVVK 8144
Cdd:cd05570    77 YVNGGDLMFHIQRAR-RFTEERARFYAAEICLALQFLHERGIIYRDLKLDNVLLDAEG--HIKIADFGMC-KEGIWGGNT 152
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 8145 ITT--GTAEFAAPEIVNREPVGFYTDMWATGVLSYVLLSGLSPFAGDNDVQTLKNVKacdwDFDVESFKYISEEAKDFIR 8222
Cdd:cd05570   153 TSTfcGTPDYIAPEILREQDYGFSVDWWALGVLLYEMLAGQSPFEGDDEDELFEAIL----NDEVLYPRWLSREAVSILK 228
                         250
                  ....*....|.
gi 281359561 8223 KLLVRNKEKRM 8233
Cdd:cd05570   229 GLLTKDPARRL 239
STKc_MAPKAPK3 cd14172
Catalytic domain of the Serine/Threonine kinase, Mitogen-activated protein kinase-activated ...
7985-8244 3.10e-35

Catalytic domain of the Serine/Threonine kinase, Mitogen-activated protein kinase-activated protein kinase 3; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MAPK-activated protein kinase 3 (MAPKAP3 or MK3) contains an N-terminal proline-rich region that can bind to SH3 domains, a catalytic kinase domain followed by a C-terminal autoinhibitory region that contains nuclear localization (NLS) and nuclear export (NES) signals with a p38 MAPK docking motif that overlaps the NLS. MK3 is a bonafide substrate for the MAPK p38. It is closely related to MK2 and thus far, MK2/3 show indistinguishable substrate specificity. They are mainly involved in the regulation of gene expression and they participate in diverse cellular processes such as endocytosis, cytokine production, cytoskeletal reorganization, cell migration, cell cycle control and chromatin remodeling. They are implicated in inflammation and cance and their substrates include mRNA-AU-rich-element (ARE)-binding proteins (TTP and hnRNP A0), Hsp proteins (Hsp27 and Hsp25) and RSK, among others. MK2/3 are both expressed ubiquitously but MK2 is expressed at significantly higher levels. MK3 activity is only significant when MK2 is absent. The MK3 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271074 [Multi-domain]  Cd Length: 267  Bit Score: 138.20  E-value: 3.10e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 7985 VYDRYDILEEI-GTGAFGVVHRCRERSTGNIFAAKFIpvshsVEKDLIRREIDimnqlHH------QKLINLHDAFEDDD 8057
Cdd:cd14172     1 VTDDYKLSKQVlGLGVNGKVLECFHRRTGQKCALKLL-----YDSPKARREVE-----HHwrasggPHIVHILDVYENMH 70
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 8058 E----MILILEFLSGGELFERITAEG-YVMTEAEVINYMRQICEGIRHMHEQNIIHLDIKPENIMCQTRSSTNV-KLIDF 8131
Cdd:cd14172    71 HgkrcLLIIMECMEGGELFSRIQERGdQAFTEREASEIMRDIGTAIQYLHSMNIAHRDVKPENLLYTSKEKDAVlKLTDF 150
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 8132 GLATRLDPNEVVKITTGTAEFAAPEIVNREPVGFYTDMWATGVLSYVLLSGLSPFAgDNDVQTL-----KNVKACDWDFD 8206
Cdd:cd14172   151 GFAKETTVQNALQTPCYTPYYVAPEVLGPEKYDKSCDMWSLGVIMYILLCGFPPFY-SNTGQAIspgmkRRIRMGQYGFP 229
                         250       260       270
                  ....*....|....*....|....*....|....*...
gi 281359561 8207 VESFKYISEEAKDFIRKLLVRNKEKRMTAHECLLHPWL 8244
Cdd:cd14172   230 NPEWAEVSEEAKQLIRHLLKTDPTERMTITQFMNHPWI 267
STKc_MEKK1_plant cd06632
Catalytic domain of the Serine/Threonine Kinase, Plant Mitogen-Activated Protein (MAP) ...
7995-8244 4.98e-35

Catalytic domain of the Serine/Threonine Kinase, Plant Mitogen-Activated Protein (MAP)/Extracellular signal-Regulated Kinase (ERK) Kinase Kinase 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily is composed of plant MAPK kinase kinases (MAPKKKs) including Arabidopsis thaliana MEKK1 and MAPKKK3. Arabidopsis thaliana MEKK1 activates MPK4, a MAPK that regulates systemic acquired resistance. MEKK1 also participates in the regulation of temperature-sensitive and tissue-specific cell death. MAPKKKs phosphorylate and activate MAPK kinases, which in turn phosphorylate and activate MAPKs during signaling cascades that are important in mediating cellular responses to extracellular signals. The plant MEKK1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270802 [Multi-domain]  Cd Length: 259  Bit Score: 137.53  E-value: 4.98e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 7995 IGTGAFGVVHRCRERSTGNIFAAKFIPV----SHSVE--KDLiRREIDIMNQLHHQKLINLHDAFEDDDEMILILEFLSG 8068
Cdd:cd06632     8 LGSGSFGSVYEGFNGDTGDFFAVKEVSLvdddKKSREsvKQL-EQEIALLSKLRHPNIVQYYGTEREEDNLYIFLEYVPG 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 8069 GELfERITAEGYVMTEAEVINYMRQICEGIRHMHEQNIIHLDIKPENIMCQTrsSTNVKLIDFGLATRLDPNEVVKITTG 8148
Cdd:cd06632    87 GSI-HKLLQRYGAFEEPVIRLYTRQILSGLAYLHSRNTVHRDIKGANILVDT--NGVVKLADFGMAKHVEAFSFAKSFKG 163
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 8149 TAEFAAPEIVNRE--PVGFYTDMWATGVLSYVLLSGLSPFAGDNDVQTLknvkacdwdFDVESFK-------YISEEAKD 8219
Cdd:cd06632   164 SPYWMAPEVIMQKnsGYGLAVDIWSLGCTVLEMATGKPPWSQYEGVAAI---------FKIGNSGelppipdHLSPDAKD 234
                         250       260
                  ....*....|....*....|....*
gi 281359561 8220 FIRKLLVRNKEKRMTAHECLLHPWL 8244
Cdd:cd06632   235 FIRLCLQRDPEDRPTASQLLEHPFV 259
STKc_Aurora-B_like cd14117
Catalytic domain of the Serine/Threonine kinase, Aurora-B kinase and similar proteins; STKs ...
7987-8244 5.17e-35

Catalytic domain of the Serine/Threonine kinase, Aurora-B kinase and similar proteins; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Aurora kinases are key regulators of mitosis and are essential for the accurate and equal division of genomic material from parent to daughter cells. Vertebrates contain at least 2 Aurora kinases (A and B); mammals contains a third Aurora kinase gene (C). This subfamily includes Aurora-B and Aurora-C. Aurora-B is most active at the transition during metaphase to the end of mitosis. It associates with centromeres, relocates to the midzone of the central spindle, and concentrates at the midbody during cell division. It is critical for accurate chromosomal segregation, cytokinesis, protein localization to the centrosome and kinetochore, correct microtubule-kinetochore attachments, and regulation of the mitotic checkpoint. Aurora-C is mainly expressed in meiotically dividing cells; it was originally discovered in mice as a testis-specific STK called Aie1. Both Aurora-B and -C are chromosomal passenger proteins that can form complexes with INCENP and survivin, and they may have redundant cellular functions. INCENP participates in the activation of Aurora-B in a two-step process: first by binding to form an intermediate state of activation and the phosphorylation of its C-terminal TSS motif to generate the fully active kinase. The Aurora-B subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271019 [Multi-domain]  Cd Length: 270  Bit Score: 137.69  E-value: 5.17e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 7987 DRYDILEEIGTGAFGVVHRCRERSTGNIFAAKFIPVSHsVEKD----LIRREIDIMNQLHHQKLINLHDAFEDDDEMILI 8062
Cdd:cd14117     6 DDFDIGRPLGKGKFGNVYLAREKQSKFIVALKVLFKSQ-IEKEgvehQLRREIEIQSHLRHPNILRLYNYFHDRKRIYLI 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 8063 LEFLSGGELFERITAEGYvMTEAEVINYMRQICEGIRHMHEQNIIHLDIKPENIMCQTRSStnVKLIDFGLATRLdPNEV 8142
Cdd:cd14117    85 LEYAPRGELYKELQKHGR-FDEQRTATFMEELADALHYCHEKKVIHRDIKPENLLMGYKGE--LKIADFGWSVHA-PSLR 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 8143 VKITTGTAEFAAPEIVNREPVGFYTDMWATGVLSYVLLSGLSPFAGDNDVQTLKNVKACDWDFDvesfKYISEEAKDFIR 8222
Cdd:cd14117   161 RRTMCGTLDYLPPEMIEGRTHDEKVDLWCIGVLCYELLVGMPPFESASHTETYRRIVKVDLKFP----PFLSDGSRDLIS 236
                         250       260
                  ....*....|....*....|..
gi 281359561 8223 KLLVRNKEKRMTAHECLLHPWL 8244
Cdd:cd14117   237 KLLRYHPSERLPLKGVMEHPWV 258
STKc_SnRK2-3 cd14665
Catalytic domain of the Serine/Threonine Kinases, Sucrose nonfermenting 1-related protein ...
7988-8243 5.40e-35

Catalytic domain of the Serine/Threonine Kinases, Sucrose nonfermenting 1-related protein kinase subfamily 2, group 3; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The SnRKs form three different subfamilies designated SnRK1-3. SnRK2 is represented in this cd. SnRK2s are involved in plant response to abiotic stresses and abscisic acid (ABA)-dependent plant development. The SnRK2s subfamily is in turn classed into three subgroups, all 3 of which are represented in this CD. Group 1 comprises kinases not activated by ABA, group 2 - kinases not activated or activated very weakly by ABA (depending on plant species), and group 3 - kinases strongly activated by ABA. The SnRKs belong to a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271135 [Multi-domain]  Cd Length: 257  Bit Score: 137.42  E-value: 5.40e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 7988 RYDILEEIGTGAFGVVHRCRERSTGNIFAAKFIPVSHSVEKDlIRREIDIMNQLHHQKLINLHDAFEDDDEMILILEFLS 8067
Cdd:cd14665     1 RYELVKDIGSGNFGVARLMRDKQTKELVAVKYIERGEKIDEN-VQREIINHRSLRHPNIVRFKEVILTPTHLAIVMEYAA 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 8068 GGELFERITAEGYvMTEAEVINYMRQICEGIRHMHEQNIIHLDIKPENIMCQTRSSTNVKLIDFGLATRLDPNEVVKITT 8147
Cdd:cd14665    80 GGELFERICNAGR-FSEDEARFFFQQLISGVSYCHSMQICHRDLKLENTLLDGSPAPRLKICDFGYSKSSVLHSQPKSTV 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 8148 GTAEFAAPEIVNR-EPVGFYTDMWATGVLSYVLLSGLSPFAGDNDVQTLKNV--KACDWDFDVESFKYISEEAKDFIRKL 8224
Cdd:cd14665   159 GTPAYIAPEVLLKkEYDGKIADVWSCGVTLYVMLVGAYPFEDPEEPRNFRKTiqRILSVQYSIPDYVHISPECRHLISRI 238
                         250
                  ....*....|....*....
gi 281359561 8225 LVRNKEKRMTAHECLLHPW 8243
Cdd:cd14665   239 FVADPATRITIPEIRNHEW 257
STKc_MARK cd14072
Catalytic domain of the Serine/Threonine Kinases, MAP/microtubule affinity-regulating kinases; ...
7988-8244 5.94e-35

Catalytic domain of the Serine/Threonine Kinases, MAP/microtubule affinity-regulating kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MARKs, also called Partitioning-defective 1 (Par1) proteins, function as regulators of diverse cellular processes in nematodes, Drosophila, yeast, and vertebrates. They are involved in embryogenesis, epithelial cell polarization, cell signaling, and neuronal differentiation. MARKs phosphorylate tau and related microtubule-associated proteins (MAPs), and regulates microtubule-based intracellular transport. Vertebrates contain four isoforms, namely MARK1 (or Par1c), MARK2 (or Par1b), MARK3 (Par1a), and MARK4 (or MARKL1). Known substrates of MARKs include the cell cycle-regulating phosphatase Cdc25, tyrosine phosphatase PTPH1, MAPK scaffolding protein KSR1, class IIa histone deacetylases, and plakophilin 2. The MARK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270974 [Multi-domain]  Cd Length: 253  Bit Score: 136.88  E-value: 5.94e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 7988 RYDILEEIGTGAFGVVHRCRERSTGNIFAAKFIPVSH----SVEKdlIRREIDIMNQLHHQKLINLHDAFEDDDEMILIL 8063
Cdd:cd14072     1 NYRLLKTIGKGNFAKVKLARHVLTGREVAIKIIDKTQlnpsSLQK--LFREVRIMKILNHPNIVKLFEVIETEKTLYLVM 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 8064 EFLSGGELFERITAEGYvMTEAEVINYMRQICEGIRHMHEQNIIHLDIKPENIMCQtrSSTNVKLIDFGLATRLDPNEVV 8143
Cdd:cd14072    79 EYASGGEVFDYLVAHGR-MKEKEARAKFRQIVSAVQYCHQKRIVHRDLKAENLLLD--ADMNIKIADFGFSNEFTPGNKL 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 8144 KITTGTAEFAAPEIVN-REPVGFYTDMWATGVLSYVLLSGLSPFAGdndvQTLKNVKAcdwdfDVESFKY-----ISEEA 8217
Cdd:cd14072   156 DTFCGSPPYAAPELFQgKKYDGPEVDVWSLGVILYTLVSGSLPFDG----QNLKELRE-----RVLRGKYripfyMSTDC 226
                         250       260
                  ....*....|....*....|....*..
gi 281359561 8218 KDFIRKLLVRNKEKRMTAHECLLHPWL 8244
Cdd:cd14072   227 ENLLKKFLVLNPSKRGTLEQIMKDRWM 253
STKc_PAK_I cd06647
Catalytic domain of the Serine/Threonine Kinase, Group I p21-activated kinase; STKs catalyze ...
7988-8244 7.82e-35

Catalytic domain of the Serine/Threonine Kinase, Group I p21-activated kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Group I PAKs, also called conventional PAKs, include PAK1, PAK2, and PAK3. Group I PAKs contain a PBD (p21-binding domain) overlapping with an AID (autoinhibitory domain), a C-terminal catalytic domain, SH3 binding sites and a non-classical SH3 binding site for PIX (PAK-interacting exchange factor). They interact with the SH3 domain containing proteins Nck, Grb2 and PIX. Binding of group I PAKs to activated GTPases leads to conformational changes that destabilize the AID, allowing autophosphorylation and full activation of the kinase domain. Known group I PAK substrates include MLCK, Bad, Raf, MEK1, LIMK, Merlin, Vimentin, Myc, Stat5a, and Aurora A, among others. PAKs are Rho family GTPase-regulated kinases that serve as important mediators in the function of Cdc42 (cell division cycle 42) and Rac. PAKs are implicated in the regulation of many cellular processes including growth factor receptor-mediated proliferation, cell polarity, cell motility, cell death and survival, and actin cytoskeleton organization. The PAK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270814 [Multi-domain]  Cd Length: 261  Bit Score: 136.98  E-value: 7.82e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 7988 RYDILEEIGTGAFGVVHRCRERSTGNIFAAKFIPVSHSVEKDLIRREIDIMNQLHHQKLINLHDAFEDDDEMILILEFLS 8067
Cdd:cd06647     8 KYTRFEKIGQGASGTVYTAIDVATGQEVAIKQMNLQQQPKKELIINEILVMRENKNPNIVNYLDSYLVGDELWVVMEYLA 87
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 8068 GGELFERITAEgyVMTEAEVINYMRQICEGIRHMHEQNIIHLDIKPENIMCQTRSStnVKLIDFGLATRLDPNEVVKIT- 8146
Cdd:cd06647    88 GGSLTDVVTET--CMDEGQIAAVCRECLQALEFLHSNQVIHRDIKSDNILLGMDGS--VKLTDFGFCAQITPEQSKRSTm 163
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 8147 TGTAEFAAPEIVNREPVGFYTDMWATGVLSYVLLSGLSPFAGDNDVQTLKNVkACDWDFDVESFKYISEEAKDFIRKLLV 8226
Cdd:cd06647   164 VGTPYWMAPEVVTRKAYGPKVDIWSLGIMAIEMVEGEPPYLNENPLRALYLI-ATNGTPELQNPEKLSAIFRDFLNRCLE 242
                         250
                  ....*....|....*...
gi 281359561 8227 RNKEKRMTAHECLLHPWL 8244
Cdd:cd06647   243 MDVEKRGSAKELLQHPFL 260
STKc_PIM cd14005
Catalytic domain of the Serine/Threonine kinase, Proviral Integration Moloney virus (PIM) ...
7988-8244 1.01e-34

Catalytic domain of the Serine/Threonine kinase, Proviral Integration Moloney virus (PIM) kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The PIM gene locus was discovered as a result of the cloning of retroviral intergration sites in murine Moloney leukemia virus, leading to the identification of PIM kinases. They are constitutively active STKs with a broad range of cellular targets and are overexpressed in many haematopoietic malignancies and solid cancers. Vertebrates contain three distinct PIM kinase genes (PIM1-3); each gene may result in mutliple protein isoforms. There are two PIM1 and three PIM2 isoforms as a result of alternative translation initiation sites, while there is only one PIM3 protein. Compound knockout mice deficient of all three PIM kinases that survive the perinatal period show a profound reduction in body size, indicating that PIMs are important for body growth. The PIM subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270907 [Multi-domain]  Cd Length: 255  Bit Score: 136.21  E-value: 1.01e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 7988 RYDILEEIGTGAFGVVHRCRERSTGNIFAAKFIPVSHSVEKDLIRR------EIDIM---NQLHHQKLINLHDAFEDDDE 8058
Cdd:cd14005     1 QYEVGDLLGKGGFGTVYSGVRIRDGLPVAVKFVPKSRVTEWAMINGpvpvplEIALLlkaSKPGVPGVIRLLDWYERPDG 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 8059 MILILEFLSGGE-LFERITAEGyVMTEAEVINYMRQICEGIRHMHEQNIIHLDIKPENIMCQTRSStNVKLIDFGLATRL 8137
Cdd:cd14005    81 FLLIMERPEPCQdLFDFITERG-ALSENLARIIFRQVVEAVRHCHQRGVLHRDIKDENLLINLRTG-EVKLIDFGCGALL 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 8138 DpNEVVKITTGTAEFAAPE-IVNREPVGFYTDMWATGVLSYVLLSGLSPFAGDNDVQTLKNVKACDWdfdvesfkyiSEE 8216
Cdd:cd14005   159 K-DSVYTDFDGTRVYSPPEwIRHGRYHGRPATVWSLGILLYDMLCGDIPFENDEQILRGNVLFRPRL----------SKE 227
                         250       260
                  ....*....|....*....|....*...
gi 281359561 8217 AKDFIRKLLVRNKEKRMTAHECLLHPWL 8244
Cdd:cd14005   228 CCDLISRCLQFDPSKRPSLEQILSHPWF 255
STKc_PKA cd14209
Catalytic subunit of the Serine/Threonine Kinase, cAMP-dependent protein kinase; STKs catalyze ...
7987-8246 1.90e-34

Catalytic subunit of the Serine/Threonine Kinase, cAMP-dependent protein kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The inactive PKA holoenzyme is a heterotetramer composed of two phosphorylated and active catalytic subunits with a dimer of regulatory (R) subunits. Activation is achieved through the binding of the important second messenger cAMP to the R subunits, which leads to the dissociation of PKA into the R dimer and two active subunits. PKA is present ubiquitously in cells and interacts with many different downstream targets. It plays a role in the regulation of diverse processes such as growth, development, memory, metabolism, gene expression, immunity, and lipolysis. The PKA subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271111 [Multi-domain]  Cd Length: 290  Bit Score: 136.76  E-value: 1.90e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 7987 DRYDILEEIGTGAFGVVHRCRERSTGNIFAAKFIP----VSH-SVEKDLirREIDIMNQLHHQKLINLHDAFEDDDEMIL 8061
Cdd:cd14209     1 DDFDRIKTLGTGSFGRVMLVRHKETGNYYAMKILDkqkvVKLkQVEHTL--NEKRILQAINFPFLVKLEYSFKDNSNLYM 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 8062 ILEFLSGGELFERITAEGYvMTEAEVINYMRQICEGIRHMHEQNIIHLDIKPENIMCQTRSStnVKLIDFGLATRldpne 8141
Cdd:cd14209    79 VMEYVPGGEMFSHLRRIGR-FSEPHARFYAAQIVLAFEYLHSLDLIYRDLKPENLLIDQQGY--IKVTDFGFAKR----- 150
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 8142 vVKITT----GTAEFAAPEIVNREPVGFYTDMWATGVLSYVLLSGLSPFAGDNDVQTLKNVKACDWDFDvesfKYISEEA 8217
Cdd:cd14209   151 -VKGRTwtlcGTPEYLAPEIILSKGYNKAVDWWALGVLIYEMAAGYPPFFADQPIQIYEKIVSGKVRFP----SHFSSDL 225
                         250       260       270
                  ....*....|....*....|....*....|....
gi 281359561 8218 KDFIRKLLVRNKEKRM-----TAHECLLHPWLTG 8246
Cdd:cd14209   226 KDLLRNLLQVDLTKRFgnlknGVNDIKNHKWFAT 259
STKc_RSK_N cd05582
N-terminal catalytic domain of the Serine/Threonine Kinase, 90 kDa ribosomal protein S6 kinase; ...
7995-8235 3.20e-34

N-terminal catalytic domain of the Serine/Threonine Kinase, 90 kDa ribosomal protein S6 kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. RSKs contain an N-terminal kinase domain (NTD) from the AGC family and a C-terminal kinase domain (CTD) from the CAMK family. They are activated by signaling inputs from extracellular regulated kinase (ERK) and phosphoinositide dependent kinase 1 (PDK1). ERK phosphorylates and activates the CTD of RSK, serving as a docking site for PDK1, which phosphorylates and activates the NTD, which in turn phosphorylates all known RSK substrates. RSKs act as downstream effectors of mitogen-activated protein kinase (MAPK) and play key roles in mitogen-activated cell growth, differentiation, and survival. Mammals possess four RSK isoforms (RSK1-4) from distinct genes. RSK proteins are also referred to as MAP kinase-activated protein kinases (MAPKAPKs), p90-RSKs, or p90S6Ks. The RSK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270734 [Multi-domain]  Cd Length: 317  Bit Score: 137.15  E-value: 3.20e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 7995 IGTGAFGVVHRCRERS---TGNIFAAKFIPVSHSVEKDLIRR--EIDIMNQLHHQKLINLHDAFEDDDEMILILEFLSGG 8069
Cdd:cd05582     3 LGQGSFGKVFLVRKITgpdAGTLYAMKVLKKATLKVRDRVRTkmERDILADVNHPFIVKLHYAFQTEGKLYLILDFLRGG 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 8070 ELFERITAEgyVM-TEAEVINYMRQICEGIRHMHEQNIIHLDIKPENIMCQtrSSTNVKLIDFGLATR-LDPNEVVKITT 8147
Cdd:cd05582    83 DLFTRLSKE--VMfTEEDVKFYLAELALALDHLHSLGIIYRDLKPENILLD--EDGHIKLTDFGLSKEsIDHEKKAYSFC 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 8148 GTAEFAAPEIVNREPVGFYTDMWATGVLSYVLLSGLSPFAGDNDVQTLKNV-KAcdwdfDVESFKYISEEAKDFIRKLLV 8226
Cdd:cd05582   159 GTVEYMAPEVVNRRGHTQSADWWSFGVLMFEMLTGSLPFQGKDRKETMTMIlKA-----KLGMPQFLSPEAQSLLRALFK 233

                  ....*....
gi 281359561 8227 RNKEKRMTA 8235
Cdd:cd05582   234 RNPANRLGA 242
STKc_PAK_II cd06648
Catalytic domain of the Serine/Threonine Kinase, Group II p21-activated kinase; STKs catalyze ...
7994-8244 4.18e-34

Catalytic domain of the Serine/Threonine Kinase, Group II p21-activated kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Group II PAKs, also called non-conventional PAKs, include PAK4, PAK5, and PAK6. Group II PAKs contain PBD (p21-binding domain) and catalytic domains, but lack other motifs found in group I PAKs, such as an AID (autoinhibitory domain) and SH3 binding sites. Since group II PAKs do not contain an obvious AID, they may be regulated differently from group I PAKs. While group I PAKs interact with the SH3 containing proteins Nck, Grb2 and PIX, no such binding has been demonstrated for group II PAKs. Some known substrates of group II PAKs are also substrates of group I PAKs such as Raf, BAD, LIMK and GEFH1. Unique group II substrates include MARK/Par-1 and PDZ-RhoGEF. Group II PAKs play important roles in filopodia formation, neuron extension, cytoskeletal organization, and cell survival. PAKs are Rho family GTPase-regulated kinases that serve as important mediators in the function of Cdc42 (cell division cycle 42) and Rac. The PAK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270815 [Multi-domain]  Cd Length: 261  Bit Score: 134.88  E-value: 4.18e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 7994 EIGTGAFGVVHRCRERSTGNIFAAKFIPVSHSVEKDLIRREIDIMNQLHHQKLINLHDAFEDDDEMILILEFLSGGELFE 8073
Cdd:cd06648    14 KIGEGSTGIVCIATDKSTGRQVAVKKMDLRKQQRRELLFNEVVIMRDYQHPNIVEMYSSYLVGDELWVVMEFLEGGALTD 93
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 8074 RITAEGyvMTEAEVINYMRQICEGIRHMHEQNIIHLDIKPENIMcqTRSSTNVKLIDFGLATRLDpNEVV--KITTGTAE 8151
Cdd:cd06648    94 IVTHTR--MNEEQIATVCRAVLKALSFLHSQGVIHRDIKSDSIL--LTSDGRVKLSDFGFCAQVS-KEVPrrKSLVGTPY 168
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 8152 FAAPEIVNREPVGFYTDMWATGVLSYVLLSGLSPFAGDNDVQTLKNVKACDWDFDVESFKyISEEAKDFIRKLLVRNKEK 8231
Cdd:cd06648   169 WMAPEVISRLPYGTEVDIWSLGIMVIEMVDGEPPYFNEPPLQAMKRIRDNEPPKLKNLHK-VSPRLRSFLDRMLVRDPAQ 247
                         250
                  ....*....|...
gi 281359561 8232 RMTAHECLLHPWL 8244
Cdd:cd06648   248 RATAAELLNHPFL 260
STKc_MST3_like cd06609
Catalytic domain of Mammalian Ste20-like protein kinase 3-like Serine/Threonine Kinases; STKs ...
7987-8245 5.13e-34

Catalytic domain of Mammalian Ste20-like protein kinase 3-like Serine/Threonine Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily is composed of MST3, MST4, STK25, Schizosaccharomyces pombe Nak1 and Sid1, Saccharomyces cerevisiae sporulation-specific protein 1 (SPS1), and related proteins. Nak1 is required by fission yeast for polarizing the tips of actin cytoskeleton and is involved in cell growth, cell separation, cell morphology and cell-cycle progression. Sid1 is a component in the septation initiation network (SIN) signaling pathway, and plays a role in cytokinesis. SPS1 plays a role in regulating proteins required for spore wall formation. MST4 plays a role in mitogen-activated protein kinase (MAPK) signaling during cytoskeletal rearrangement, morphogenesis, and apoptosis. MST3 phosphorylates the STK NDR and may play a role in cell cycle progression and cell morphology. STK25 may play a role in the regulation of cell migration and polarization. The MST3-like subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270786 [Multi-domain]  Cd Length: 274  Bit Score: 135.06  E-value: 5.13e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 7987 DRYDILEEIGTGAFGVVHRCRERSTGNIFAAKFIPVSHSVEK-DLIRREIDIMNQLHHQKLINLHDAFEDDDEMILILEF 8065
Cdd:cd06609     1 ELFTLLERIGKGSFGEVYKGIDKRTNQVVAIKVIDLEEAEDEiEDIQQEIQFLSQCDSPYITKYYGSFLKGSKLWIIMEY 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 8066 LSGGELFERItaEGYVMTEAEVINYMRQICEGIRHMHEQNIIHLDIKPENIMcqTRSSTNVKLIDFGLATRLDPNEVVKI 8145
Cdd:cd06609    81 CGGGSVLDLL--KPGPLDETYIAFILREVLLGLEYLHSEGKIHRDIKAANIL--LSEEGDVKLADFGVSGQLTSTMSKRN 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 8146 T-TGTAEFAAPEIVNREPVGFYTDMWATGVLSYVLLSGLSPFAGDNDVQTLKNVKACDWDfDVESFKYiSEEAKDFIRKL 8224
Cdd:cd06609   157 TfVGTPFWMAPEVIKQSGYDEKADIWSLGITAIELAKGEPPLSDLHPMRVLFLIPKNNPP-SLEGNKF-SKPFKDFVELC 234
                         250       260
                  ....*....|....*....|.
gi 281359561 8225 LVRNKEKRMTAHECLLHPWLT 8245
Cdd:cd06609   235 LNKDPKERPSAKELLKHKFIK 255
STKc_FA2-like cd08529
Catalytic domain of the Serine/Threonine Kinases, Chlamydomonas reinhardtii FA2 and similar ...
7989-8244 5.17e-34

Catalytic domain of the Serine/Threonine Kinases, Chlamydomonas reinhardtii FA2 and similar proteins; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Chlamydomonas reinhardtii FA2 was discovered in a genetic screen for deflagellation-defective mutants. It is essential for basal-body/centriole-associated microtubule severing, and plays a role in cell cycle progression. No cellular function has yet been ascribed to CNK4. The Chlamydomonas reinhardtii FA2-like subfamily belongs to the (NIMA)-related kinase (Nek) family, which includes seven different Chlamydomonas Neks (CNKs 1-6 and Fa2). This subfamily contains FA2 and CNK4. The Nek family is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270868 [Multi-domain]  Cd Length: 256  Bit Score: 134.46  E-value: 5.17e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 7989 YDILEEIGTGAFGVVHRCRERSTGNIFAAKFIPVS--HSVEKDLIRREIDIMNQLHHQKLINLHDAFEDDDEMILILEFL 8066
Cdd:cd08529     2 FEILNKLGKGSFGVVYKVVRKVDGRVYALKQIDISrmSRKMREEAIDEARVLSKLNSPYVIKYYDSFVDKGKLNIVMEYA 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 8067 SGGELFERITAE-GYVMTEAEVINYMRQICEGIRHMHEQNIIHLDIKPENIMCQtrSSTNVKLIDFGLATRLDPNEVVKI 8145
Cdd:cd08529    82 ENGDLHSLIKSQrGRPLPEDQIWKFFIQTLLGLSHLHSKKILHRDIKSMNIFLD--KGDNVKIGDLGVAKILSDTTNFAQ 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 8146 T-TGTAEFAAPEIVNREPVGFYTDMWATGVLSYVLLSGLSPFAGDNDVQ-TLKNVKAcdwDFDVESFKYiSEEAKDFIRK 8223
Cdd:cd08529   160 TiVGTPYYLSPELCEDKPYNEKSDVWALGCVLYELCTGKHPFEAQNQGAlILKIVRG---KYPPISASY-SQDLSQLIDS 235
                         250       260
                  ....*....|....*....|.
gi 281359561 8224 LLVRNKEKRMTAHECLLHPWL 8244
Cdd:cd08529   236 CLTKDYRQRPDTTELLRNPSL 256
STKc_MAPK cd07834
Catalytic domain of the Serine/Threonine Kinase, Mitogen-Activated Protein Kinase; STKs ...
7988-8249 1.07e-33

Catalytic domain of the Serine/Threonine Kinase, Mitogen-Activated Protein Kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MAPKs serve as important mediators of cellular responses to extracellular signals. They control critical cellular functions including differentiation, proliferation, migration, and apoptosis. They are also implicated in the pathogenesis of many diseases including multiple types of cancer, stroke, diabetes, and chronic inflammation. Typical MAPK pathways involve a triple kinase core cascade comprising of the MAPK, which is phosphorylated and activated by a MAPK kinase (MAP2K or MKK), which itself is phosphorylated and activated by a MAPK kinase kinase (MAP3K or MKKK). Each cascade is activated either by a small GTP-binding protein or by an adaptor protein, which transmits the signal either directly to a MAP3K to start the triple kinase core cascade or indirectly through a mediator kinase, a MAP4K. There are three typical MAPK subfamilies: Extracellular signal-Regulated Kinase (ERK), c-Jun N-terminal Kinase (JNK), and p38. Some MAPKs are atypical in that they are not regulated by MAP2Ks. These include MAPK4, MAPK6, NLK, and ERK7. The MAPK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270828 [Multi-domain]  Cd Length: 329  Bit Score: 135.73  E-value: 1.07e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 7988 RYDILEEIGTGAFGVVHRCRERSTGNIFAAKFIPvshSVEKDLI---R--REIDIMNQLHHQKLINLHDAF-----EDDD 8057
Cdd:cd07834     1 RYELLKPIGSGAYGVVCSAYDKRTGRKVAIKKIS---NVFDDLIdakRilREIKILRHLKHENIIGLLDILrppspEEFN 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 8058 EMILILEflsggeLFE----RITAEGYVMTEAEVINYMRQICEGIRHMHEQNIIHLDIKPENIMcqTRSSTNVKLIDFGL 8133
Cdd:cd07834    78 DVYIVTE------LMEtdlhKVIKSPQPLTDDHIQYFLYQILRGLKYLHSAGVIHRDLKPSNIL--VNSNCDLKICDFGL 149
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 8134 ATRLDPNEVVKITTG---TAEFAAPEIVnrepVGF--YT---DMWATGVL--------------SYV------------- 8178
Cdd:cd07834   150 ARGVDPDEDKGFLTEyvvTRWYRAPELL----LSSkkYTkaiDIWSVGCIfaelltrkplfpgrDYIdqlnlivevlgtp 225
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 281359561 8179 ----LLSGLSPFAgDNDVQTLKNVKACDWDfdvESFKYISEEAKDFIRKLLVRNKEKRMTAHECLLHPWLTGDHS 8249
Cdd:cd07834   226 seedLKFISSEKA-RNYLKSLPKKPKKPLS---EVFPGASPEAIDLLEKMLVFNPKKRITADEALAHPYLAQLHD 296
STKc_SLK_like cd06611
Catalytic domain of Ste20-Like Kinase-like Serine/Threonine Kinases; STKs catalyze the ...
7987-8252 1.10e-33

Catalytic domain of Ste20-Like Kinase-like Serine/Threonine Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Members of the subfamily include SLK, STK10 (also called LOK for Lymphocyte-Oriented Kinase), SmSLK (Schistosoma mansoni SLK), and related proteins. SLK promotes apoptosis through apoptosis signal-regulating kinase 1 (ASK1) and the mitogen-activated protein kinase (MAPK) p38. It also plays a role in mediating actin reorganization. STK10 is responsible in regulating the CD28 responsive element in T cells, as well as leukocyte function associated antigen (LFA-1)-mediated lymphocyte adhesion. SmSLK is capable of activating the MAPK Jun N-terminal kinase (JNK) pathway in human embryonic kidney cells as well as in Xenopus oocytes. It may participate in regulating MAPK cascades during host-parasite interactions. The SLK-like subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 132942 [Multi-domain]  Cd Length: 280  Bit Score: 134.10  E-value: 1.10e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 7987 DRYDILEEIGTGAFGVVHRCRERSTGNIFAAKFIPVSHSVEKDLIRREIDIMNQLHHQKLINLHDAFEDDDEMILILEFL 8066
Cdd:cd06611     5 DIWEIIGELGDGAFGKVYKAQHKETGLFAAAKIIQIESEEELEDFMVEIDILSECKHPNIVGLYEAYFYENKLWILIEFC 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 8067 SGGELFERITAEGYVMTEAEVINYMRQICEGIRHMHEQNIIHLDIKPENIMCqTRSStNVKLIDFGLATRLDpNEVVKIT 8146
Cdd:cd06611    85 DGGALDSIMLELERGLTEPQIRYVCRQMLEALNFLHSHKVIHRDLKAGNILL-TLDG-DVKLADFGVSAKNK-STLQKRD 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 8147 T--GTAEFAAPEIVNRE-----PVGFYTDMWATGVLSYVLLSGLSPFAGDNDVQTLKNVKACDWDFDVESFKYiSEEAKD 8219
Cdd:cd06611   162 TfiGTPYWMAPEVVACEtfkdnPYDYKADIWSLGITLIELAQMEPPHHELNPMRVLLKILKSEPPTLDQPSKW-SSSFND 240
                         250       260       270
                  ....*....|....*....|....*....|....*
gi 281359561 8220 FIRKLLVRNKEKRMTAHECLLHPWLT--GDHSAMK 8252
Cdd:cd06611   241 FLKSCLVKDPDDRPTAAELLKHPFVSdqSDNKAIK 275
STKc_Nek6_7 cd08224
Catalytic domain of the Serine/Threonine Kinases, Never In Mitosis gene A (NIMA)-related ...
7988-8235 1.10e-33

Catalytic domain of the Serine/Threonine Kinases, Never In Mitosis gene A (NIMA)-related kinase 6 and 7; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Nek6 and Nek7 are the shortest Neks, consisting only of the catalytic domain and a very short N-terminal extension. They show distinct expression patterns and both appear to be downstream substrates of Nek9. They are required for mitotic spindle formation and cytokinesis. They may also be regulators of the p70 ribosomal S6 kinase. Nek6/7 is part of a family of 11 different Neks (Nek1-11) that are involved in cell cycle control. The Nek family is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270863 [Multi-domain]  Cd Length: 262  Bit Score: 133.55  E-value: 1.10e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 7988 RYDILEEIGTGAFGVVHRCRERSTGNIFAAKFIPV---SHSVEKDLIRREIDIMNQLHHQKLINLHDAFEDDDEMILILE 8064
Cdd:cd08224     1 NYEIEKKIGKGQFSVVYRARCLLDGRLVALKKVQIfemMDAKARQDCLKEIDLLQQLNHPNIIKYLASFIENNELNIVLE 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 8065 FLSGGELFERI---TAEGYVMTEAEVINYMRQICEGIRHMHEQNIIHLDIKPENIMCQTRSStnVKLIDFGLATRLDPNE 8141
Cdd:cd08224    81 LADAGDLSRLIkhfKKQKRLIPERTIWKYFVQLCSALEHMHSKRIMHRDIKPANVFITANGV--VKLGDLGLGRFFSSKT 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 8142 VVKITT-GTAEFAAPEIVNREPVGFYTDMWATGVLSYVLLSGLSPFAGDN-DVQTL-KNVKACDWDfDVESFKYiSEEAK 8218
Cdd:cd08224   159 TAAHSLvGTPYYMSPERIREQGYDFKSDIWSLGCLLYEMAALQSPFYGEKmNLYSLcKKIEKCEYP-PLPADLY-SQELR 236
                         250
                  ....*....|....*..
gi 281359561 8219 DFIRKLLVRNKEKRMTA 8235
Cdd:cd08224   237 DLVAACIQPDPEKRPDI 253
STKc_MST1_2 cd06612
Catalytic domain of the Serine/Threonine Kinases, Mammalian STe20-like protein kinase 1 and 2; ...
7989-8244 1.14e-33

Catalytic domain of the Serine/Threonine Kinases, Mammalian STe20-like protein kinase 1 and 2; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily is composed of MST1, MST2, and related proteins including Drosophila Hippo and Dictyostelium discoideum Krs1 (kinase responsive to stress 1). MST1/2 and Hippo are involved in a conserved pathway that governs cell contact inhibition, organ size control, and tumor development. MST1 activates the mitogen-activated protein kinases (MAPKs) p38 and c-Jun N-terminal kinase (JNK) through MKK7 and MEKK1 by acting as a MAPK kinase kinase kinase. Activation of JNK by MST1 leads to caspase activation and apoptosis. MST1 has also been implicated in cell proliferation and differentiation. Krs1 may regulate cell growth arrest and apoptosis in response to cellular stress. The MST1/2 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 132943 [Multi-domain]  Cd Length: 256  Bit Score: 133.55  E-value: 1.14e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 7989 YDILEEIGTGAFGVVHRCRERSTGNIFAAKFIPVSHSVEKdlIRREIDIMNQLHHQKLINLHDAFEDDDEMILILEFLSG 8068
Cdd:cd06612     5 FDILEKLGEGSYGSVYKAIHKETGQVVAIKVVPVEEDLQE--IIKEISILKQCDSPYIVKYYGSYFKNTDLWIVMEYCGA 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 8069 GELFERITAEGYVMTEAEVINYMRQICEGIRHMHEQNIIHLDIKPENIMCQTRSstNVKLIDFGLATRL-----DPNEVV 8143
Cdd:cd06612    83 GSVSDIMKITNKTLTEEEIAAILYQTLKGLEYLHSNKKIHRDIKAGNILLNEEG--QAKLADFGVSGQLtdtmaKRNTVI 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 8144 kittGTAEFAAPEIVNREPVGFYTDMWATGVLSYVLLSGLSPFAGDNDV-----------QTLKNVKacDWdfdvesfky 8212
Cdd:cd06612   161 ----GTPFWMAPEVIQEIGYNNKADIWSLGITAIEMAEGKPPYSDIHPMraifmipnkppPTLSDPE--KW--------- 225
                         250       260       270
                  ....*....|....*....|....*....|..
gi 281359561 8213 iSEEAKDFIRKLLVRNKEKRMTAHECLLHPWL 8244
Cdd:cd06612   226 -SPEFNDFVKKCLVKDPEERPSAIQLLQHPFI 256
STKc_MSK1_N cd05613
N-terminal catalytic domain of the Serine/Threonine Kinase, Mitogen and stress-activated ...
7989-8233 1.37e-33

N-terminal catalytic domain of the Serine/Threonine Kinase, Mitogen and stress-activated kinase 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MSK1 plays a role in the regulation of translational control and transcriptional activation. It phosphorylates the transcription factors, CREB and NFkB. It also phosphorylates the nucleosomal proteins H3 and HMG-14. Increased phosphorylation of MSK1 is associated with the development of cerebral ischemic/hypoxic preconditioning. MSKs contain an N-terminal kinase domain (NTD) from the AGC family and a C-terminal kinase domain (CTD) from the CAMK family. MSKs are activated by two major signaling cascades, the Ras-MAPK and p38 stress kinase pathways, which trigger phosphorylation in the activation loop (A-loop) of the CTD of MSK. The active CTD phosphorylates the hydrophobic motif (HM) of NTD, which facilitates the phosphorylation of the A-loop and activates the NTD, which in turn phosphorylates downstream targets. The MSK1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270764 [Multi-domain]  Cd Length: 290  Bit Score: 134.36  E-value: 1.37e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 7989 YDILEEIGTGAFGVVHRCRERS---TGNIFAAKFIPVSHSVEK----DLIRREIDIMNQLHHQK-LINLHDAFEDDDEMI 8060
Cdd:cd05613     2 FELLKVLGTGAYGKVFLVRKVSghdAGKLYAMKVLKKATIVQKaktaEHTRTERQVLEHIRQSPfLVTLHYAFQTDTKLH 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 8061 LILEFLSGGELFERITaEGYVMTEAEVINYMRQICEGIRHMHEQNIIHLDIKPENIMCQtrSSTNVKLIDFGLATR--LD 8138
Cdd:cd05613    82 LILDYINGGELFTHLS-QRERFTENEVQIYIGEIVLALEHLHKLGIIYRDIKLENILLD--SSGHVVLTDFGLSKEflLD 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 8139 PNEVVKITTGTAEFAAPEIVNREPVGF--YTDMWATGVLSYVLLSGLSPFAGDNDVQTLKNVKACDWDFDVESFKYISEE 8216
Cdd:cd05613   159 ENERAYSFCGTIEYMAPEIVRGGDSGHdkAVDWWSLGVLMYELLTGASPFTVDGEKNSQAEISRRILKSEPPYPQEMSAL 238
                         250
                  ....*....|....*..
gi 281359561 8217 AKDFIRKLLVRNKEKRM 8233
Cdd:cd05613   239 AKDIIQRLLMKDPKKRL 255
STKc_CNK2-like cd08530
Catalytic domain of the Serine/Threonine Kinases, Chlamydomonas reinhardtii CNK2 and similar ...
7988-8242 1.55e-33

Catalytic domain of the Serine/Threonine Kinases, Chlamydomonas reinhardtii CNK2 and similar proteins; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Chlamydomonas reinhardtii CNK2 has both cilliary and cell cycle functions. It influences flagellar length through promoting flagellar disassembly, and it regulates cell size, through influencing the size threshold at which cells commit to mitosis. This subfamily belongs to the (NIMA)-related kinase (Nek) family, which includes seven different Chlamydomonas Neks (CNKs 1-6 and Fa2). This subfamily includes CNK1, and -2. The Nek family is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270869 [Multi-domain]  Cd Length: 256  Bit Score: 132.90  E-value: 1.55e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 7988 RYDILEEIGTGAFGVVHRCRERSTGNIFAAKFIPV---SHSVEKDLIRrEIDIMNQLHHQKLINLHDAFEDDDEMILILE 8064
Cdd:cd08530     1 DFKVLKKLGKGSYGSVYKVKRLSDNQVYALKEVNLgslSQKEREDSVN-EIRLLASVNHPNIIRYKEAFLDGNRLCIVME 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 8065 FLSGGELFERIT---AEGYVMTEAEVINYMRQICEGIRHMHEQNIIHLDIKPENIMcqTRSSTNVKLIDFGLATRLDPNe 8141
Cdd:cd08530    80 YAPFGDLSKLISkrkKKRRLFPEDDIWRIFIQMLRGLKALHDQKILHRDLKSANIL--LSAGDLVKIGDLGISKVLKKN- 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 8142 VVKITTGTAEFAAPEIVNREPVGFYTDMWATGVLSYVLLSGLSPFAGDnDVQTLkNVKACDWDFDVESFKYiSEEAKDFI 8221
Cdd:cd08530   157 LAKTQIGTPLYAAPEVWKGRPYDYKSDIWSLGCLLYEMATFRPPFEAR-TMQEL-RYKVCRGKFPPIPPVY-SQDLQQII 233
                         250       260
                  ....*....|....*....|.
gi 281359561 8222 RKLLVRNKEKRMTAHECLLHP 8242
Cdd:cd08530   234 RSLLQVNPKKRPSCDKLLQSP 254
STKc_PLK3 cd14189
Catalytic domain of the Serine/Threonine Kinase, Polo-like kinase 3; STKs catalyze the ...
7995-8241 1.94e-33

Catalytic domain of the Serine/Threonine Kinase, Polo-like kinase 3; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PLKs play important roles in cell cycle progression and in DNA damage responses. They regulate mitotic entry, mitotic exit, and cytokinesis. In general PLKs contain an N-terminal catalytic kinase domain and a C-terminal regulatory polo box domain (PBD), which is comprised by two bipartite polo-box motifs (or polo boxes) and is involved in protein interactions. There are five mammalian PLKs (PLK1-5) from distinct genes. PLK3, also called Prk or Fnk (FGF-inducible kinase), regulates angiogenesis and responses to DNA damage. Activated PLK3 mediates Chk2 phosphorylation by ATM and the resulting checkpoint activation. PLK3 phosphorylates DNA polymerase delta and may be involved in DNA repair. It also inhibits Cdc25c, thereby regulating the onset of mitosis. The PLK3 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271091 [Multi-domain]  Cd Length: 255  Bit Score: 132.74  E-value: 1.94e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 7995 IGTGAFGVVHRCRERSTGNIFAAKFIPVS-----HSVEKdlIRREIDIMNQLHHQKLINLHDAFEDDDEMILILEFLSGG 8069
Cdd:cd14189     9 LGKGGFARCYEMTDLATNKTYAVKVIPHSrvakpHQREK--IVNEIELHRDLHHKHVVKFSHHFEDAENIYIFLELCSRK 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 8070 ELfERITAEGYVMTEAEVINYMRQICEGIRHMHEQNIIHLDIKPENIMcqTRSSTNVKLIDFGLATRLDPNEVVKITT-G 8148
Cdd:cd14189    87 SL-AHIWKARHTLLEPEVRYYLKQIISGLKYLHLKGILHRDLKLGNFF--INENMELKVGDFGLAARLEPPEQRKKTIcG 163
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 8149 TAEFAAPEIVNREPVGFYTDMWATGVLSYVLLSGLSPFAGDNDVQTLKNVKACDWDFDVesfkYISEEAKDFIRKLLVRN 8228
Cdd:cd14189   164 TPNYLAPEVLLRQGHGPESDVWSLGCVMYTLLCGNPPFETLDLKETYRCIKQVKYTLPA----SLSLPARHLLAGILKRN 239
                         250
                  ....*....|...
gi 281359561 8229 KEKRMTAHECLLH 8241
Cdd:cd14189   240 PGDRLTLDQILEH 252
STKc_GAK_like cd13985
Catalytic domain of cyclin G-Associated Kinase-like proteins; STKs catalyze the transfer of ...
7988-8232 2.22e-33

Catalytic domain of cyclin G-Associated Kinase-like proteins; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily includes cyclin G-Associated Kinase (GAK), Drosophila melanogaster Numb-Associated Kinase (NAK)-like proteins, and similar protein kinases. GAK plays regulatory roles in clathrin-mediated membrane trafficking, the maintenance of centrosome integrity and chromosome congression, neural patterning, survival of neurons, and immune responses. NAK plays a role in asymmetric cell division through its association with Numb. It also regulates the localization of Dlg, a protein essential for septate junction formation. The GAK-like subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270887 [Multi-domain]  Cd Length: 272  Bit Score: 133.23  E-value: 2.22e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 7988 RYDILEEIGTGAFGVVHRCRERSTGNIFAAKFIPVSHSVEKDLIRREIDIMNQL-HHQKLINLHDAFEDDD----EMILI 8062
Cdd:cd13985     1 RYQVTKQLGEGGFSYVYLAHDVNTGRRYALKRMYFNDEEQLRVAIKEIEIMKRLcGHPNIVQYYDSAILSSegrkEVLLL 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 8063 LEFlSGGELFERI--TAEGYvMTEAEVINYMRQICEGIRHMHEQN--IIHLDIKPENIMCQtrSSTNVKLIDFGLATRLD 8138
Cdd:cd13985    81 MEY-CPGSLVDILekSPPSP-LSEEEVLRIFYQICQAVGHLHSQSppIIHRDIKIENILFS--NTGRFKLCDFGSATTEH 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 8139 P------------NEVVKITtgTAEFAAPEIVN---REPVGFYTDMWATGVLSYVLLSGLSPFaGDNDVqtlknVKACDW 8203
Cdd:cd13985   157 YpleraeevniieEEIQKNT--TPMYRAPEMIDlysKKPIGEKADIWALGCLLYKLCFFKLPF-DESSK-----LAIVAG 228
                         250       260
                  ....*....|....*....|....*....
gi 281359561 8204 DFDVESFKYISEEAKDFIRKLLVRNKEKR 8232
Cdd:cd13985   229 KYSIPEQPRYSPELHDLIRHMLTPDPAER 257
STKc_PAK2 cd06655
Catalytic domain of the Serine/Threonine Kinase, p21-activated kinase 2; STKs catalyze the ...
7986-8244 2.77e-33

Catalytic domain of the Serine/Threonine Kinase, p21-activated kinase 2; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PAK2 plays a role in pro-apoptotic signaling. It is cleaved and activated by caspases leading to morphological changes during apoptosis. PAK2 is also activated in response to a variety of stresses including DNA damage, hyperosmolarity, serum starvation, and contact inhibition, and may play a role in coordinating the stress response. PAK2 also contributes to cancer cell invasion through a mechanism distinct from that of PAK1. It belongs to the group I PAKs, which contain a PBD (p21-binding domain) overlapping with an AID (autoinhibitory domain), a C-terminal catalytic domain, SH3 binding sites and a non-classical SH3 binding site for PIX (PAK-interacting exchange factor). PAKs are Rho family GTPase-regulated kinases that serve as important mediators in the function of Cdc42 (cell division cycle 42) and Rac. The PAK subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 132986 [Multi-domain]  Cd Length: 296  Bit Score: 133.70  E-value: 2.77e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 7986 YDRYdilEEIGTGAFGVVHRCRERSTGNIFAAKFIPVSHSVEKDLIRREIDIMNQLHHQKLINLHDAFEDDDEMILILEF 8065
Cdd:cd06655    21 YTRY---EKIGQGASGTVFTAIDVATGQEVAIKQINLQKQPKKELIINEILVMKELKNPNIVNFLDSFLVGDELFVVMEY 97
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 8066 LSGGELFERITAEgyVMTEAEVINYMRQICEGIRHMHEQNIIHLDIKPENIMCQTRSStnVKLIDFGLATRLDPNEVVKI 8145
Cdd:cd06655    98 LAGGSLTDVVTET--CMDEAQIAAVCRECLQALEFLHANQVIHRDIKSDNVLLGMDGS--VKLTDFGFCAQITPEQSKRS 173
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 8146 T-TGTAEFAAPEIVNREPVGFYTDMWATGVLSYVLLSGLSPFAGDNDVQTLKNVkACDWDFDVESFKYISEEAKDFIRKL 8224
Cdd:cd06655   174 TmVGTPYWMAPEVVTRKAYGPKVDIWSLGIMAIEMVEGEPPYLNENPLRALYLI-ATNGTPELQNPEKLSPIFRDFLNRC 252
                         250       260
                  ....*....|....*....|
gi 281359561 8225 LVRNKEKRMTAHECLLHPWL 8244
Cdd:cd06655   253 LEMDVEKRGSAKELLQHPFL 272
STKc_MAP4K3_like cd06613
Catalytic domain of Mitogen-activated protein kinase kinase kinase kinase (MAP4K) 3-like ...
7989-8242 3.05e-33

Catalytic domain of Mitogen-activated protein kinase kinase kinase kinase (MAP4K) 3-like Serine/Threonine Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily includes MAP4K3, MAP4K1, MAP4K2, MAP4K5, and related proteins. Vertebrate members contain an N-terminal catalytic domain and a C-terminal citron homology (CNH) regulatory domain. MAP4K1, also called haematopoietic progenitor kinase 1 (HPK1), is a hematopoietic-specific STK involved in many cellular signaling cascades including MAPK, antigen receptor, apoptosis, growth factor, and cytokine signaling. It participates in the regulation of T cell receptor signaling and T cell-mediated immune responses. MAP4K2 was referred to as germinal center (GC) kinase because of its preferred location in GC B cells. MAP4K3 plays a role in the nutrient-responsive pathway of mTOR (mammalian target of rapamycin) signaling. It is required in the activation of S6 kinase by amino acids and for the phosphorylation of the mTOR-regulated inhibitor of eukaryotic initiation factor 4E. MAP4K5, also called germinal center kinase-related enzyme (GCKR), has been shown to activate the MAPK c-Jun N-terminal kinase (JNK). The MAP4K3-like subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270788 [Multi-domain]  Cd Length: 259  Bit Score: 132.43  E-value: 3.05e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 7989 YDILEEIGTGAFGVVHRCRERSTGNIFAAKFIPVSHSVEKDLIRREIDIMNQLHHQKLINLHDAFEDDDEMILILEFLSG 8068
Cdd:cd06613     2 YELIQRIGSGTYGDVYKARNIATGELAAVKVIKLEPGDDFEIIQQEISMLKECRHPNIVAYFGSYLRRDKLWIVMEYCGG 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 8069 GELferitAEGYVMTEA---EVINYM-RQICEGIRHMHEQNIIHLDIKPENIMCQTRSstNVKLIDFGLATRLDpNEVVK 8144
Cdd:cd06613    82 GSL-----QDIYQVTGPlseLQIAYVcRETLKGLAYLHSTGKIHRDIKGANILLTEDG--DVKLADFGVSAQLT-ATIAK 153
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 8145 ITT--GTAEFAAPEIVNREPVGFYT---DMWATGVLSYVLLSGLSPFAG-------------DNDVQTLKNVKacDWdfd 8206
Cdd:cd06613   154 RKSfiGTPYWMAPEVAAVERKGGYDgkcDIWALGITAIELAELQPPMFDlhpmralflipksNFDPPKLKDKE--KW--- 228
                         250       260       270
                  ....*....|....*....|....*....|....*.
gi 281359561 8207 vesfkyiSEEAKDFIRKLLVRNKEKRMTAHECLLHP 8242
Cdd:cd06613   229 -------SPDFHDFIKKCLTKNPKKRPTATKLLQHP 257
STKc_MEKK4 cd06626
Catalytic domain of the Protein Serine/Threonine Kinase, Mitogen-Activated Protein (MAP) ...
7995-8244 3.83e-33

Catalytic domain of the Protein Serine/Threonine Kinase, Mitogen-Activated Protein (MAP)/Extracellular signal-Regulated Kinase (ERK) Kinase Kinase 4; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MEKK4 is a MAPK kinase kinase that phosphorylates and activates the c-Jun N-terminal kinase (JNK) and p38 MAPK signaling pathways by directly activating their respective MAPKKs, MKK4/MKK7 and MKK3/MKK6. JNK and p38 are collectively known as stress-activated MAPKs, as they are activated in response to a variety of environmental stresses and pro-inflammatory cytokines. MEKK4 also plays roles in the re-polarization of the actin cytoskeleton in response to osmotic stress, in the proper closure of the neural tube, in cardiovascular development, and in immune responses. The MEKK4 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270796 [Multi-domain]  Cd Length: 265  Bit Score: 132.04  E-value: 3.83e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 7995 IGTGAFGVVHRCRERSTGNIFAAKFIPVSHSVEK--DLIRREIDIMNQLHHQKLINLHDAFEDDDEMILILEFLSGGELF 8072
Cdd:cd06626     8 IGEGTFGKVYTAVNLDTGELMAMKEIRFQDNDPKtiKEIADEMKVLEGLDHPNLVRYYGVEVHREEVYIFMEYCQEGTLE 87
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 8073 ErITAEGYVMTEAEVINYMRQICEGIRHMHEQNIIHLDIKPENIMCQTRSStnVKLIDFGLATRLDPN------EVVKIT 8146
Cdd:cd06626    88 E-LLRHGRILDEAVIRVYTLQLLEGLAYLHENGIVHRDIKPANIFLDSNGL--IKLGDFGSAVKLKNNtttmapGEVNSL 164
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 8147 TGTAEFAAPEIVNREPV---GFYTDMWATGVLSYVLLSGLSPFAG-DNDVQTLKNVKACDWDFDVESFKyISEEAKDFIR 8222
Cdd:cd06626   165 VGTPAYMAPEVITGNKGeghGRAADIWSLGCVVLEMATGKRPWSElDNEWAIMYHVGMGHKPPIPDSLQ-LSPEGKDFLS 243
                         250       260
                  ....*....|....*....|..
gi 281359561 8223 KLLVRNKEKRMTAHECLLHPWL 8244
Cdd:cd06626   244 RCLESDPKKRPTASELLDHPFI 265
STKc_GRK cd05577
Catalytic domain of the Serine/Threonine Kinase, G protein-coupled Receptor Kinase; STKs ...
7995-8233 1.10e-32

Catalytic domain of the Serine/Threonine Kinase, G protein-coupled Receptor Kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. GRKs phosphorylate and regulate G protein-coupled receptors (GPCRs), the largest superfamily of cell surface receptors, which regulate some part of nearly all physiological functions. Phosphorylated GPCRs bind to arrestins, which prevents further G protein signaling despite the presence of activating ligand. GRKs play important roles in the cardiovascular, immune, respiratory, skeletal, and nervous systems. They contain a central catalytic domain, flanked by N- and C-terminal extensions. The N-terminus contains an RGS (regulator of G protein signaling) homology (RH) domain and several motifs. The C-terminus diverges among different groups of GRKs. There are seven types of GRKs, named GRK1 to GRK7, which are subdivided into three main groups: visual (GRK1/7); beta-adrenergic receptor kinases (GRK2/3); and GRK4-like (GRK4/5/6). Expression of GRK2/3/5/6 is widespread while GRK1/4/7 show a limited tissue distribution. The substrate spectrum of the widely expressed GRKs partially overlaps. The GRK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270729 [Multi-domain]  Cd Length: 278  Bit Score: 131.11  E-value: 1.10e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 7995 IGTGAFGVVHRCRERSTGNIFAAKfipvshSVEKDLIRR---------EIDIMNQLHHQKLINLHDAFEDDDEMILILEF 8065
Cdd:cd05577     1 LGRGGFGEVCACQVKATGKMYACK------KLDKKRIKKkkgetmalnEKIILEKVSSPFIVSLAYAFETKDKLCLVLTL 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 8066 LSGGELFERITAEGY-VMTEAEVINYMRQICEGIRHMHEQNIIHLDIKPENIMCQTRSstNVKLIDFGLATRLDPNEVVK 8144
Cdd:cd05577    75 MNGGDLKYHIYNVGTrGFSEARAIFYAAEIICGLEHLHNRFIVYRDLKPENILLDDHG--HVRISDLGLAVEFKGGKKIK 152
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 8145 ITTGTAEFAAPEIV-NREPVGFYTDMWATGVLSYVLLSGLSPFAGDNDVQTLKNVKACDWDFDVESFKYISEEAKDFIRK 8223
Cdd:cd05577   153 GRVGTHGYMAPEVLqKEVAYDFSVDWFALGCMLYEMIAGRSPFRQRKEKVDKEELKRRTLEMAVEYPDSFSPEARSLCEG 232
                         250
                  ....*....|
gi 281359561 8224 LLVRNKEKRM 8233
Cdd:cd05577   233 LLQKDPERRL 242
STKc_MAP3K-like cd13999
Catalytic domain of Mitogen-Activated Protein Kinase (MAPK) Kinase Kinase-like Serine ...
7995-8193 1.16e-32

Catalytic domain of Mitogen-Activated Protein Kinase (MAPK) Kinase Kinase-like Serine/Threonine kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily is composed mainly of MAP3Ks and similar proteins, including TGF-beta Activated Kinase-1 (TAK1, also called MAP3K7), MAP3K12, MAP3K13, Mixed lineage kinase (MLK), MLK-Like mitogen-activated protein Triple Kinase (MLTK), and Raf (Rapidly Accelerated Fibrosarcoma) kinases. MAP3Ks (MKKKs or MAPKKKs) phosphorylate and activate MAPK kinases (MAPKKs or MKKs or MAP2Ks), which in turn phosphorylate and activate MAPKs during signaling cascades that are important in mediating cellular responses to extracellular signals. Also included in this subfamily is the pseudokinase Kinase Suppressor of Ras (KSR), which is a scaffold protein that functions downstream of Ras and upstream of Raf in the Extracellular signal-Regulated Kinase (ERK) pathway.


Pssm-ID: 270901 [Multi-domain]  Cd Length: 245  Bit Score: 129.97  E-value: 1.16e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 7995 IGTGAFGVVHRCRERstGNIFAAKFIPVSHSVEKDL--IRREIDIMNQLHHQKLINLHDAFEDDDEMILILEFLSGGELF 8072
Cdd:cd13999     1 IGSGSFGEVYKGKWR--GTDVAIKKLKVEDDNDELLkeFRREVSILSKLRHPNIVQFIGACLSPPPLCIVTEYMPGGSLY 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 8073 ERITAEGYVMTEAEVINYMRQICEGIRHMHEQNIIHLDIKPENIMcqTRSSTNVKLIDFGLATRLDPNEVVKIT-TGTAE 8151
Cdd:cd13999    79 DLLHKKKIPLSWSLRLKIALDIARGMNYLHSPPIIHRDLKSLNIL--LDENFTVKIADFGLSRIKNSTTEKMTGvVGTPR 156
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|..
gi 281359561 8152 FAAPEIVNREPVGFYTDMWATGVLSYVLLSGLSPFAGDNDVQ 8193
Cdd:cd13999   157 WMAPEVLRGEPYTEKADVYSFGIVLWELLTGEVPFKELSPIQ 198
pk1 PHA03390
serine/threonine-protein kinase 1; Provisional
7998-8244 1.21e-32

serine/threonine-protein kinase 1; Provisional


Pssm-ID: 223069 [Multi-domain]  Cd Length: 267  Bit Score: 130.75  E-value: 1.21e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 7998 GAFGVVHRCRERSTGNIFAAKFIPVSHSvekdlirREIDIM-NQL--HHQKLINLHDAFEDDDEMILILEFLSGGELFER 8074
Cdd:PHA03390   27 GKFGKVSVLKHKPTQKLFVQKIIKAKNF-------NAIEPMvHQLmkDNPNFIKLYYSVTTLKGHVLIMDYIKDGDLFDL 99
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 8075 ITAEGYVmTEAEVINYMRQICEGIRHMHEQNIIHLDIKPENIMCqTRSSTNVKLIDFGLATRLDpneVVKITTGTAEFAA 8154
Cdd:PHA03390  100 LKKEGKL-SEAEVKKIIRQLVEALNDLHKHNIIHNDIKLENVLY-DRAKDRIYLCDYGLCKIIG---TPSCYDGTLDYFS 174
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 8155 PEIVNREPVGFYTDMWATGVLSYVLLSGLSPFAGDND----VQTLKNVKAcdwdFDVESFKYISEEAKDFIRKLLVRNKE 8230
Cdd:PHA03390  175 PEKIKGHNYDVSFDWWAVGVLTYELLTGKHPFKEDEDeeldLESLLKRQQ----KKLPFIKNVSKNANDFVQSMLKYNIN 250
                         250
                  ....*....|....*
gi 281359561 8231 KRMTAHECLL-HPWL 8244
Cdd:PHA03390  251 YRLTNYNEIIkHPFL 265
STKc_MAPKAPK2 cd14170
Catalytic domain of the Serine/Threonine kinase, Mitogen-activated protein kinase-activated ...
7987-8261 1.59e-32

Catalytic domain of the Serine/Threonine kinase, Mitogen-activated protein kinase-activated protein kinase 2; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MAPK-activated protein kinase 2 (MAPKAP2 or MK2) contains an N-terminal proline-rich region that can bind to SH3 domains, a catalytic kinase domain followed by a C-terminal autoinhibitory region that contains nuclear localization (NLS) and nuclear export (NES) signals with a p38 MAPK docking motif that overlaps the NLS. MK2 is a bonafide substrate for the MAPK p38. It is closely related to MK3 and thus far, MK2/3 show indistinguishable substrate specificity. They are mainly involved in the regulation of gene expression and they participate in diverse cellular processes such as endocytosis, cytokine production, cytoskeletal reorganization, cell migration, cell cycle control and chromatin remodeling. They are implicated in inflammation and cance and their substrates include mRNA-AU-rich-element (ARE)-binding proteins (TTP and hnRNP A0), Hsp proteins (Hsp27 and Hsp25) and RSK, among others. MK2/3 are both expressed ubiquitously but MK2 is expressed at significantly higher levels. The MK2 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271072 [Multi-domain]  Cd Length: 303  Bit Score: 131.70  E-value: 1.59e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 7987 DRYDILEEI-GTGAFGVVHRCRERSTGNIFAAKFIpvsHSVEKdlIRREIDI---MNQLHH-QKLINLHD-AFEDDDEMI 8060
Cdd:cd14170     1 DDYKVTSQVlGLGINGKVLQIFNKRTQEKFALKML---QDCPK--ARREVELhwrASQCPHiVRIVDVYEnLYAGRKCLL 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 8061 LILEFLSGGELFERITAEG-YVMTEAEVINYMRQICEGIRHMHEQNIIHLDIKPENIM-CQTRSSTNVKLIDFGLATRLD 8138
Cdd:cd14170    76 IVMECLDGGELFSRIQDRGdQAFTEREASEIMKSIGEAIQYLHSINIAHRDVKPENLLyTSKRPNAILKLTDFGFAKETT 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 8139 PNEVVKITTGTAEFAAPEIVNREPVGFYTDMWATGVLSYVLLSGLSPFAGDNDVQ----TLKNVKACDWDFDVESFKYIS 8214
Cdd:cd14170   156 SHNSLTTPCYTPYYVAPEVLGPEKYDKSCDMWSLGVIMYILLCGYPPFYSNHGLAispgMKTRIRMGQYEFPNPEWSEVS 235
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*..
gi 281359561 8215 EEAKDFIRKLLVRNKEKRMTAHECLLHPWLTGDHSAMKQEINRDRYL 8261
Cdd:cd14170   236 EEVKMLIRNLLKTEPTQRMTITEFMNHPWIMQSTKVPQTPLHTSRVL 282
STKc_myosinIII_N_like cd06608
N-terminal Catalytic domain of Class III myosin-like Serine/Threonine Kinases; STKs catalyze ...
7987-8244 3.06e-32

N-terminal Catalytic domain of Class III myosin-like Serine/Threonine Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Class III myosins are motor proteins with an N-terminal kinase catalytic domain and a C-terminal actin-binding motor domain. Class III myosins are present in the photoreceptors of invertebrates and vertebrates and in the auditory hair cells of mammals. The kinase domain of myosin III can phosphorylate several cytoskeletal proteins, conventional myosin regulatory light chains, and can autophosphorylate the C-terminal motor domain. Myosin III may play an important role in maintaining the structural integrity of photoreceptor cell microvilli. It may also function as a cargo carrier during light-dependent translocation, in photoreceptor cells, of proteins such as transducin and arrestin. The Drosophila class III myosin, called NinaC (Neither inactivation nor afterpotential protein C), is critical in normal adaptation and termination of photoresponse. Vertebrates contain two isoforms of class III myosin, IIIA and IIIB. This subfamily also includes mammalian NIK-like embryo-specific kinase (NESK), Traf2- and Nck-interacting kinase (TNIK), and mitogen-activated protein kinase (MAPK) kinase kinase kinase 4/6. MAP4Ks are involved in some MAPK signaling pathways by activating a MAPK kinase kinase. MAPK signaling cascades are important in mediating cellular responses to extracellular signals. The class III myosin-like subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270785 [Multi-domain]  Cd Length: 275  Bit Score: 129.73  E-value: 3.06e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 7987 DRYDILEEIGTGAFGVVHRCRERSTGNIFAAKFIPVSHSvEKDLIRREIDIMNQL-HHQKLINLHDAF------EDDDEM 8059
Cdd:cd06608     6 GIFELVEVIGEGTYGKVYKARHKKTGQLAAIKIMDIIED-EEEEIKLEINILRKFsNHPNIATFYGAFikkdppGGDDQL 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 8060 ILILEFLSGG---ELFERITAEGYVMTEaEVINY-MRQICEGIRHMHEQNIIHLDIKPENIMCQTrsSTNVKLIDFGLAT 8135
Cdd:cd06608    85 WLVMEYCGGGsvtDLVKGLRKKGKRLKE-EWIAYiLRETLRGLAYLHENKVIHRDIKGQNILLTE--EAEVKLVDFGVSA 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 8136 RLDpNEVVKITT--GTAEFAAPEIV----NREPVgfYT---DMWATGVLSYVLLSGLSPFAG-----------DNDVQTL 8195
Cdd:cd06608   162 QLD-STLGRRNTfiGTPYWMAPEVIacdqQPDAS--YDarcDVWSLGITAIELADGKPPLCDmhpmralfkipRNPPPTL 238
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*....
gi 281359561 8196 KNVKacDWdfdvesfkyiSEEAKDFIRKLLVRNKEKRMTAHECLLHPWL 8244
Cdd:cd06608   239 KSPE--KW----------SKEFNDFISECLIKNYEQRPFTEELLEHPFI 275
PKc_Wee1_like cd13997
Catalytic domain of the Wee1-like Protein Kinases; PKs catalyze the transfer of the ...
7988-8242 5.50e-32

Catalytic domain of the Wee1-like Protein Kinases; PKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine or tyrosine residues on protein substrates. This subfamily is composed of the dual-specificity kinase Myt1, the protein tyrosine kinase Wee1, and similar proteins. These proteins are cell cycle checkpoint kinases that are involved in the regulation of cyclin-dependent kinase CDK1, the master engine for mitosis. CDK1 is kept inactivated through phosphorylation of N-terminal thr (T14 by Myt1) and tyr (Y15 by Myt1 and Wee1) residues. Mitosis progression is ensured through activation of CDK1 by dephoshorylation and inactivation of Myt1/Wee1. The Wee1-like subfamily is part of a larger superfamily that includes the catalytic domains of other protein serine/threonine PKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270899 [Multi-domain]  Cd Length: 252  Bit Score: 128.27  E-value: 5.50e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 7988 RYDILEEIGTGAFGVVHRCRERSTGNIFAAK--FIPVSHSVEKDLIRREIDIMNQL-HHQKLINLHDAFEDDDEMILILE 8064
Cdd:cd13997     1 HFHELEQIGSGSFSEVFKVRSKVDGCLYAVKksKKPFRGPKERARALREVEAHAALgQHPNIVRYYSSWEEGGHLYIQME 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 8065 FLSGGEL---FERITAEGYVmTEAEVINYMRQICEGIRHMHEQNIIHLDIKPENIMcqTRSSTNVKLIDFGLATRLDPNE 8141
Cdd:cd13997    81 LCENGSLqdaLEELSPISKL-SEAEVWDLLLQVALGLAFIHSKGIVHLDIKPDNIF--ISNKGTCKIGDFGLATRLETSG 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 8142 VVKitTGTAEFAAPEIVNrepvGFYT-----DMWATGVLSYVLLSGLSPFAGDNDVQTLKNVKACDWDFDVesfkyISEE 8216
Cdd:cd13997   158 DVE--EGDSRYLAPELLN----ENYThlpkaDIFSLGVTVYEAATGEPLPRNGQQWQQLRQGKLPLPPGLV-----LSQE 226
                         250       260
                  ....*....|....*....|....*.
gi 281359561 8217 AKDFIRKLLVRNKEKRMTAHECLLHP 8242
Cdd:cd13997   227 LTRLLKVMLDPDPTRRPTADQLLAHD 252
STKc_Nek2 cd08217
Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase ...
7989-8242 6.68e-32

Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase 2; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The Nek2 subfamily includes Aspergillus nidulans NIMA kinase, the founding member of the Nek family, which was identified in a screen for cell cycle mutants prevented from entering mitosis. NIMA is essential for mitotic entry and progression through mitosis, and its degradation is essential for mitotic exit. NIMA is involved in nuclear membrane fission. Vertebrate Nek2 is a cell cycle-regulated STK, localized in centrosomes and kinetochores, that regulates centrosome splitting at the G2/M phase. It also interacts with other mitotic kinases such as Polo-like kinase 1 and may play a role in spindle checkpoint. An increase in the expression of the human NEK2 gene is strongly associated with the progression of non-Hodgkin lymphoma. Nek2 is one in a family of 11 different Neks (Nek1-11) that are involved in cell cycle control. It The Nek family is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270857 [Multi-domain]  Cd Length: 265  Bit Score: 128.43  E-value: 6.68e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 7989 YDILEEIGTGAFGVVHRCRERSTGNIFAAKFIPVSH--SVEKDLIRREIDIMNQLHHQKLINLHDAFEDDDE--MILILE 8064
Cdd:cd08217     2 YEVLETIGKGSFGTVRKVRRKSDGKILVWKEIDYGKmsEKEKQQLVSEVNILRELKHPNIVRYYDRIVDRANttLYIVME 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 8065 FLSGGEL---FERITAEGYVMTEAEVINYMRQICEGIRHMH-----EQNIIHLDIKPENIMCQtrSSTNVKLIDFGLATR 8136
Cdd:cd08217    82 YCEGGDLaqlIKKCKKENQYIPEEFIWKIFTQLLLALYECHnrsvgGGKILHRDLKPANIFLD--SDNNVKLGDFGLARV 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 8137 LDPNEVVKIT-TGTAEFAAPEIVNREPvgfYT---DMWATGVLSYVLLSGLSPFAGDNDVQTLKNVKAcdwdfdvESFKY 8212
Cdd:cd08217   160 LSHDSSFAKTyVGTPYYMSPELLNEQS---YDeksDIWSLGCLIYELCALHPPFQAANQLELAKKIKE-------GKFPR 229
                         250       260       270
                  ....*....|....*....|....*....|....
gi 281359561 8213 I----SEEAKDFIRKLLVRNKEKRMTAHECLLHP 8242
Cdd:cd08217   230 IpsrySSELNEVIKSMLNVDPDKRPSVEELLQLP 263
STKc_PRKX_like cd05612
Catalytic domain of PRKX-like Protein Serine/Threonine Kinases; STKs catalyze the transfer of ...
7987-8233 1.04e-31

Catalytic domain of PRKX-like Protein Serine/Threonine Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Members of this group include human PRKX (X chromosome-encoded protein kinase), Drosophila DC2, and similar proteins. PRKX is present in many tissues including fetal and adult brain, kidney, and lung. The PRKX gene is located in the Xp22.3 subregion and has a homolog called PRKY on the Y chromosome. An abnormal interchange between PRKX aand PRKY leads to the sex reversal disorder of XX males and XY females. PRKX is implicated in granulocyte/macrophage lineage differentiation, renal cell epithelial migration, and tubular morphogenesis in the developing kidney. The PRKX-like subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270763 [Multi-domain]  Cd Length: 292  Bit Score: 128.71  E-value: 1.04e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 7987 DRYDILEEIGTGAFGVVHRCRERSTGNIFAAKFIPVSHSV---EKDLIRREIDIMNQLHHQKLINLHDAFEDDDEMILIL 8063
Cdd:cd05612     1 DDFERIKTIGTGTFGRVHLVRDRISEHYYALKVMAIPEVIrlkQEQHVHNEKRVLKEVSHPFIIRLFWTEHDQRFLYMLM 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 8064 EFLSGGELFERITAEGYvMTEAEVINYMRQICEGIRHMHEQNIIHLDIKPENIMCQtrSSTNVKLIDFGLATRLdpneVV 8143
Cdd:cd05612    81 EYVPGGELFSYLRNSGR-FSNSTGLFYASEIVCALEYLHSKEIVYRDLKPENILLD--KEGHIKLTDFGFAKKL----RD 153
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 8144 KITT--GTAEFAAPEIVNREPVGFYTDMWATGVLSYVLLSGLSPFAGDNDVQTLKNVKACDWDFDvesfKYISEEAKDFI 8221
Cdd:cd05612   154 RTWTlcGTPEYLAPEVIQSKGHNKAVDWWALGILIYEMLVGYPPFFDDNPFGIYEKILAGKLEFP----RHLDLYAKDLI 229
                         250
                  ....*....|..
gi 281359561 8222 RKLLVRNKEKRM 8233
Cdd:cd05612   230 KKLLVVDRTRRL 241
STKc_EIF2AK cd13996
Catalytic domain of the Serine/Threonine kinase, eukaryotic translation Initiation Factor ...
7983-8239 1.65e-31

Catalytic domain of the Serine/Threonine kinase, eukaryotic translation Initiation Factor 2-Alpha Kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. EIF2AKs phosphorylate the alpha subunit of eIF-2, resulting in the downregulation of protein synthesis. eIF-2 phosphorylation is induced in response to cellular stresses including virus infection, heat shock, nutrient deficiency, and the accummulation of unfolded proteins, among others. There are four distinct kinases that phosphorylate eIF-2 and control protein synthesis under different stress conditions: General Control Non-derepressible-2 (GCN2) which is activated during amino acid or serum starvation; protein kinase regulated by RNA (PKR) which is activated by double stranded RNA; heme-regulated inhibitor kinase (HRI) which is activated under heme-deficient conditions; and PKR-like endoplasmic reticulum kinase (PERK) which is activated when misfolded proteins accumulate in the ER. The EIF2AK subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270898 [Multi-domain]  Cd Length: 273  Bit Score: 127.79  E-value: 1.65e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 7983 QSVYDR-YDILEEIGTGAFGVVHRCRERSTGNIFAAKFIPV---SHSVEKdlIRREIDIMNQLHHQKLINLHDAFEDDDE 8058
Cdd:cd13996     1 NSRYLNdFEEIELLGSGGFGSVYKVRNKVDGVTYAIKKIRLtekSSASEK--VLREVKALAKLNHPNIVRYYTAWVEEPP 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 8059 MILILEFLSGGEL---FERITAEGYVMtEAEVINYMRQICEGIRHMHEQNIIHLDIKPENIMCQTRSSTnVKLIDFGLAT 8135
Cdd:cd13996    79 LYIQMELCEGGTLrdwIDRRNSSSKND-RKLALELFKQILKGVSYIHSKGIVHRDLKPSNIFLDNDDLQ-VKIGDFGLAT 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 8136 RL-----------------DPNEVVKIttGTAEFAAPEIVNREPVGFYTDMWATGVlsyVLLSGLSPFAGDND-VQTLKN 8197
Cdd:cd13996   157 SIgnqkrelnnlnnnnngnTSNNSVGI--GTPLYASPEQLDGENYNEKADIYSLGI---ILFEMLHPFKTAMErSTILTD 231
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|...
gi 281359561 8198 VkacdWDFDV-ESFKYISEEAKDFIRKLLVRNKEKRMTAHECL 8239
Cdd:cd13996   232 L----RNGILpESFKAKHPKEADLIQSLLSKNPEERPSAEQLL 270
STKc_HAL4_like cd13994
Catalytic domain of Fungal Halotolerance protein 4-like Serine/Threonine kinases; STKs ...
7995-8244 2.09e-31

Catalytic domain of Fungal Halotolerance protein 4-like Serine/Threonine kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily is composed of HAL4, Saccharomyces cerevisiae Ptk2/Stk2, and similar fungal proteins. Proteins in this subfamily are involved in regulating ion transporters. In budding and fission yeast, HAL4 promotes potassium ion uptake, which increases cellular resistance to other cations such as sodium, lithium, and calcium ions. HAL4 stabilizes the major high-affinity K+ transporter Trk1 at the plasma membrane under low K+ conditions, which prevents endocytosis and vacuolar degradation. Budding yeast Ptk2 phosphorylates and regulates the plasma membrane H+ ATPase, Pma1. The HAL4-like subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270896 [Multi-domain]  Cd Length: 265  Bit Score: 127.04  E-value: 2.09e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 7995 IGTGAFGVVHRC--RERSTGNIFAAKFI--PVSHSVEKDLIRR---EIDIMNQLHHQKLINLHDAFED-DDEMILILEFL 8066
Cdd:cd13994     1 IGKGATSVVRIVtkKNPRSGVLYAVKEYrrRDDESKRKDYVKRltsEYIISSKLHHPNIVKVLDLCQDlHGKWCLVMEYC 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 8067 SGGELFERITAEGyVMTEAEVINYMRQICEGIRHMHEQNIIHLDIKPENIMCQTRSstNVKLIDFGLA-TRLDPNEVVKI 8145
Cdd:cd13994    81 PGGDLFTLIEKAD-SLSLEEKDCFFKQILRGVAYLHSHGIAHRDLKPENILLDEDG--VLKLTDFGTAeVFGMPAEKESP 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 8146 TT----GTAEFAAPEIVNREPV-GFYTDMWATGVLSYVLLSGLSPF--AGDNDVQTLKNVKACD--WDFDVESFKYISEE 8216
Cdd:cd13994   158 MSaglcGSEPYMAPEVFTSGSYdGRAVDVWSCGIVLFALFTGRFPWrsAKKSDSAYKAYEKSGDftNGPYEPIENLLPSE 237
                         250       260
                  ....*....|....*....|....*...
gi 281359561 8217 AKDFIRKLLVRNKEKRMTAHECLLHPWL 8244
Cdd:cd13994   238 CRRLIYRMLHPDPEKRITIDEALNDPWV 265
I-set pfam07679
Immunoglobulin I-set domain;
8632-8721 2.67e-31

Immunoglobulin I-set domain;


Pssm-ID: 400151 [Multi-domain]  Cd Length: 90  Bit Score: 120.44  E-value: 2.67e-31
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561  8632 PEFTKPLHDLTIHDGEQLILTCYVKGDPEPQISWSKNGKSLSSSDILDLRYKNGIATLTINEVFPEDEGVITCTATNSVG 8711
Cdd:pfam07679    1 PKFTQKPKDVEVQEGESARFTCTVTGTPDPEVSWFKDGQPLRSSDRFKVTYEGGTYTLTISNVQPDDSGKYTCVATNSAG 80
                           90
                   ....*....|
gi 281359561  8712 AVETKCKLTI 8721
Cdd:pfam07679   81 EAEASAELTV 90
STKc_PAK3 cd06656
Catalytic domain of the Protein Serine/Threonine Kinase, p21-activated kinase 3; Serine ...
7988-8244 3.47e-31

Catalytic domain of the Protein Serine/Threonine Kinase, p21-activated kinase 3; Serine/threonine kinases (STKs), p21-activated kinase (PAK) 3, catalytic (c) domain. STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The PAK subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase. PAKs are Rho family GTPase-regulated kinases that serve as important mediators in the function of Cdc42 (cell division cycle 42) and Rac. PAKs from higher eukaryotes are classified into two groups (I and II), according to their biochemical and structural features. PAK3 belongs to group I. Group I PAKs contain a PBD (p21-binding domain) overlapping with an AID (autoinhibitory domain), a C-terminal catalytic domain, SH3 binding sites and a non-classical SH3 binding site for PIX (PAK-interacting exchange factor). PAK3 is highly expressed in the brain. It is implicated in neuronal plasticity, synapse formation, dendritic spine morphogenesis, cell cycle progression, neuronal migration, and apoptosis. Inactivating mutations in the PAK3 gene cause X-linked non-syndromic mental retardation, the severity of which depends on the site of the mutation.


Pssm-ID: 132987 [Multi-domain]  Cd Length: 297  Bit Score: 127.53  E-value: 3.47e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 7988 RYDILEEIGTGAFGVVHRCRERSTGNIFAAKFIPVSHSVEKDLIRREIDIMNQLHHQKLINLHDAFEDDDEMILILEFLS 8067
Cdd:cd06656    20 KYTRFEKIGQGASGTVYTAIDIATGQEVAIKQMNLQQQPKKELIINEILVMRENKNPNIVNYLDSYLVGDELWVVMEYLA 99
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 8068 GGELFERITAEgyVMTEAEVINYMRQICEGIRHMHEQNIIHLDIKPENIMCQTRSStnVKLIDFGLATRLDPNEVVKIT- 8146
Cdd:cd06656   100 GGSLTDVVTET--CMDEGQIAAVCRECLQALDFLHSNQVIHRDIKSDNILLGMDGS--VKLTDFGFCAQITPEQSKRSTm 175
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 8147 TGTAEFAAPEIVNREPVGFYTDMWATGVLSYVLLSGLSPFAGDNDVQTLKNVkACDWDFDVESFKYISEEAKDFIRKLLV 8226
Cdd:cd06656   176 VGTPYWMAPEVVTRKAYGPKVDIWSLGIMAIEMVEGEPPYLNENPLRALYLI-ATNGTPELQNPERLSAVFRDFLNRCLE 254
                         250
                  ....*....|....*...
gi 281359561 8227 RNKEKRMTAHECLLHPWL 8244
Cdd:cd06656   255 MDVDRRGSAKELLQHPFL 272
STKc_Kin4 cd14076
Catalytic domain of the yeast Serine/Threonine Kinase, Kin4; STKs catalyze the transfer of the ...
7989-8244 3.95e-31

Catalytic domain of the yeast Serine/Threonine Kinase, Kin4; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Kin4 is a central component of the spindle position checkpoint (SPOC), which monitors spindle position and regulates the mitotic exit network (MEN). Kin4 associates with spindle pole bodies in mother cells to inhibit MEN signaling and delay mitosis until the anaphase nucleus is properly positioned along the mother-bud axis. Kin4 activity is regulated by both the bud neck-associated kinase Elm1 and protein phosphatase 2A. The Kin4 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270978 [Multi-domain]  Cd Length: 270  Bit Score: 126.44  E-value: 3.95e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 7989 YDILEEIGTGAFGVVH------RCRERSTGNIfAAKFI---PVSHSVEKDLIRREIDIMNQLHHQKLINLHDAFEDDDEM 8059
Cdd:cd14076     3 YILGRTLGEGEFGKVKlgwplpKANHRSGVQV-AIKLIrrdTQQENCQTSKIMREINILKGLTHPNIVRLLDVLKTKKYI 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 8060 ILILEFLSGGELFERITAEGYvMTEAEVINYMRQICEGIRHMHEQNIIHLDIKPENIMCQTrsSTNVKLIDFGLATRLDP 8139
Cdd:cd14076    82 GIVLEFVSGGELFDYILARRR-LKDSVACRLFAQLISGVAYLHKKGVVHRDLKLENLLLDK--NRNLVITDFGFANTFDH 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 8140 --NEVVKITTGTAEFAAPEIVNREPV--GFYTDMWATGVLSYVLLSGLSPFAGDNDVQTLKNVkacdwdfdVESFKYI-- 8213
Cdd:cd14076   159 fnGDLMSTSCGSPCYAAPELVVSDSMyaGRKADIWSCGVILYAMLAGYLPFDDDPHNPNGDNV--------PRLYRYIcn 230
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|
gi 281359561 8214 ---------SEEAKDFIRKLLVRNKEKRMTAHECLLHPWL 8244
Cdd:cd14076   231 tplifpeyvTPKARDLLRRILVPNPRKRIRLSAIMRHAWL 270
STKc_GRK5 cd05632
Catalytic domain of the Serine/Threonine Kinase, G protein-coupled Receptor Kinase 5; STKs ...
7983-8248 5.01e-31

Catalytic domain of the Serine/Threonine Kinase, G protein-coupled Receptor Kinase 5; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. GRK5 is widely expressed in many tissues. It associates with the membrane though an N-terminal PIP2 binding domain and also binds phospholipids via its C-terminus. GRK5 deficiency is associated with early Alzheimer's disease in humans and mouse models. GRK5 also plays a crucial role in the pathogenesis of sporadic Parkinson's disease. It participates in the regulation and desensitization of PDGFRbeta, a receptor tyrosine kinase involved in a variety of downstream cellular effects including cell growth, chemotaxis, apoptosis, and angiogenesis. GRK5 also regulates Toll-like receptor 4, which is involved in innate and adaptive immunity. GRKs phosphorylate and regulate G protein-coupled receptors (GPCRs), the largest superfamily of cell surface receptors which regulate some part of nearly all physiological functions. Phosphorylated GPCRs bind to arrestins, which prevents further G protein signaling despite the presence of activating ligand. The GRK5 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270780 [Multi-domain]  Cd Length: 313  Bit Score: 127.40  E-value: 5.01e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 7983 QSVYDRYDILeeiGTGAFGVVHRCRERSTGNIFAAKfipvshSVEKDLIRR---------EIDIMNQLHHQKLINLHDAF 8053
Cdd:cd05632     1 KNTFRQYRVL---GKGGFGEVCACQVRATGKMYACK------RLEKKRIKKrkgesmalnEKQILEKVNSQFVVNLAYAY 71
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 8054 EDDDEMILILEFLSGGELFERITAEGYVMTEAE-VINYMRQICEGIRHMHEQNIIHLDIKPENIMCQtrSSTNVKLIDFG 8132
Cdd:cd05632    72 ETKDALCLVLTIMNGGDLKFHIYNMGNPGFEEErALFYAAEILCGLEDLHRENTVYRDLKPENILLD--DYGHIRISDLG 149
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 8133 LATRLDPNEVVKITTGTAEFAAPEIVNREPVGFYTDMWATGVLSYVLLSGLSPFAGDNDVQTLKNV-KACDWDFDVESFK 8211
Cdd:cd05632   150 LAVKIPEGESIRGRVGTVGYMAPEVLNNQRYTLSPDYWGLGCLIYEMIEGQSPFRGRKEKVKREEVdRRVLETEEVYSAK 229
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|..
gi 281359561 8212 YiSEEAKDFIRKLLVRNKEKRM-----TAHECLLHPWLTGDH 8248
Cdd:cd05632   230 F-SEEAKSICKMLLTKDPKQRLgcqeeGAGEVKRHPFFRNMN 270
STKc_ULK3 cd14121
Catalytic domain of the Serine/Threonine kinase, Unc-51-like kinase 3; STKs catalyze the ...
7993-8243 5.22e-31

Catalytic domain of the Serine/Threonine kinase, Unc-51-like kinase 3; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The ATG1/ULK complex is conserved from yeast to humans and it plays a critical role in the initiation of autophagy, the intracellular system that leads to the lysosomal degradation of cellular components and their recycling into basic metabolic units. ULK3 mRNA is up-regulated in fibroblasts after Ras-induced senescence, and its overexpression induces both autophagy and senescence in a fibroblast cell line. ULK3, through its kinase activity, positively regulates Gli proteins, mediators of the Sonic hedgehog (Shh) signaling pathway that is implicated in tissue homeostasis maintenance and neurogenesis. It is inhibited by binding to Suppressor of Fused (Sufu). The ULK3 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271023 [Multi-domain]  Cd Length: 252  Bit Score: 125.48  E-value: 5.22e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 7993 EEIGTGAFGVVHRC-RERSTGNIFAAKFI---PVSHSVEKDLIRrEIDIMNQLHHQKLINLHDAFEDDDEMILILEFLSG 8068
Cdd:cd14121     1 EKLGSGTYATVYKAyRKSGAREVVAVKCVsksSLNKASTENLLT-EIELLKKLKHPHIVELKDFQWDEEHIYLIMEYCSG 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 8069 GELFERITAEGyVMTEAEVINYMRQICEGIRHMHEQNIIHLDIKPENIMCQTRSSTNVKLIDFGLATRLDPNEVVKITTG 8148
Cdd:cd14121    80 GDLSRFIRSRR-TLPESTVRRFLQQLASALQFLREHNISHMDLKPQNLLLSSRYNPVLKLADFGFAQHLKPNDEAHSLRG 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 8149 TAEFAAPEIVNREPVGFYTDMWATGVLSYVLLSGLSPFAGdndvQTLKNVKACDWDFD---VESFKYISEEAKDFIRKLL 8225
Cdd:cd14121   159 SPLYMAPEMILKKKYDARVDLWSVGVILYECLFGRAPFAS----RSFEELEEKIRSSKpieIPTRPELSADCRDLLLRLL 234
                         250
                  ....*....|....*...
gi 281359561 8226 VRNKEKRMTAHECLLHPW 8243
Cdd:cd14121   235 QRDPDRRISFEEFFAHPF 252
STKc_GRK4_like cd05605
Catalytic domain of G protein-coupled Receptor Kinase 4-like Serine/Threonine Kinases; STKs ...
7995-8243 5.40e-31

Catalytic domain of G protein-coupled Receptor Kinase 4-like Serine/Threonine Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Members of the GRK4-like group include GRK4, GRK5, GRK6, and similar GRKs. They contain an N-terminal RGS homology (RH) domain and a catalytic domain, but lack a G protein betagamma-subunit binding domain. They are localized to the plasma membrane through post-translational lipid modification or direct binding to PIP2. GRKs phosphorylate and regulate G protein-coupled receptors (GPCRs), the largest superfamily of cell surface receptors which regulate some part of nearly all physiological functions. Phosphorylated GPCRs bind to arrestins, which prevents further G protein signaling despite the presence of activating ligand. The GRK4-like subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270756 [Multi-domain]  Cd Length: 285  Bit Score: 126.70  E-value: 5.40e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 7995 IGTGAFGVVHRCRERSTGNIFAAKfipvshSVEKDLIRR---------EIDIMNQLHHQKLINLHDAFEDDDEMILILEF 8065
Cdd:cd05605     8 LGKGGFGEVCACQVRATGKMYACK------KLEKKRIKKrkgeamalnEKQILEKVNSRFVVSLAYAYETKDALCLVLTI 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 8066 LSGGELFERItaegYVM-----TEAEVINYMRQICEGIRHMHEQNIIHLDIKPENIMCQTRSstNVKLIDFGLATRLDPN 8140
Cdd:cd05605    82 MNGGDLKFHI----YNMgnpgfEEERAVFYAAEITCGLEHLHSERIVYRDLKPENILLDDHG--HVRISDLGLAVEIPEG 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 8141 EVVKITTGTAEFAAPEIVNREPVGFYTDMWATGVLSYVLLSGLSPF-AGDNDVQTLKNVKACDWDFDVESFKYiSEEAKD 8219
Cdd:cd05605   156 ETIRGRVGTVGYMAPEVVKNERYTFSPDWWGLGCLIYEMIEGQAPFrARKEKVKREEVDRRVKEDQEEYSEKF-SEEAKS 234
                         250       260
                  ....*....|....*....|....*....
gi 281359561 8220 FIRKLLVRNKEKRM-----TAHECLLHPW 8243
Cdd:cd05605   235 ICSQLLQKDPKTRLgcrgeGAEDVKSHPF 263
STKc_Cdc7 cd14019
Catalytic domain of the Serine/Threonine Kinase, Cell Division Cycle 7 kinase; STKs catalyze ...
7989-8244 5.47e-31

Catalytic domain of the Serine/Threonine Kinase, Cell Division Cycle 7 kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Cdc7 kinase (or Hsk1 in fission yeast) is a critical regulator in the initiation of DNA replication. It forms a complex with a Dbf4-related regulatory subunit, a cyclin-like molecule that activates the kinase in late G1 phase, and is also referred to as Dbf4-dependent kinase (DDK). Its main targets are mini-chromosome maintenance (MCM) proteins. Cdc7 kinase may also have additional roles in meiosis, checkpoint responses, the maintenance and repair of chromosome structures, and cancer progression. The Cdc7 kinase subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270921 [Multi-domain]  Cd Length: 252  Bit Score: 125.41  E-value: 5.47e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 7989 YDILEEIGTGAFGVVHRCRERST-------GNIFAAKFI-PVSHSVEkdlIRREIDIMNQLHHQK-LINLHDAFEDDDEM 8059
Cdd:cd14019     3 YRIIEKIGEGTFSSVYKAEDKLHdlydrnkGRLVALKHIyPTSSPSR---ILNELECLERLGGSNnVSGLITAFRNEDQV 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 8060 ILILEFlsggelFERITAEGYV--MTEAEVINYMRQICEGIRHMHEQNIIHLDIKPENIMCQTRSSTNVkLIDFGLATRL 8137
Cdd:cd14019    80 VAVLPY------IEHDDFRDFYrkMSLTDIRIYLRNLFKALKHVHSFGIIHRDVKPGNFLYNRETGKGV-LVDFGLAQRE 152
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 8138 -DPNEVVKITTGTAEFAAPEIVNREP-VGFYTDMWATGVLSYVLLSGLSPFAGDNDvqtlknvkacdwdfDVESFKYI-- 8213
Cdd:cd14019   153 eDRPEQRAPRAGTRGFRAPEVLFKCPhQTTAIDIWSAGVILLSILSGRFPFFFSSD--------------DIDALAEIat 218
                         250       260       270
                  ....*....|....*....|....*....|....
gi 281359561 8214 ---SEEAKDFIRKLLVRNKEKRMTAHECLLHPWL 8244
Cdd:cd14019   219 ifgSDEAYDLLDKLLELDPSKRITAEEALKHPFF 252
STKc_MSK2_N cd05614
N-terminal catalytic domain of the Serine/Threonine Kinase, Mitogen and stress-activated ...
7989-8246 7.29e-31

N-terminal catalytic domain of the Serine/Threonine Kinase, Mitogen and stress-activated kinase 2; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MSK2 and MSK1 play nonredundant roles in activating histone H3 kinases, which play pivotal roles in compaction of the chromatin fiber. MSK2 is the required H3 kinase in response to stress stimuli and activation of the p38 MAPK pathway. MSK2 also plays a role in the pathogenesis of psoriasis. MSKs contain an N-terminal kinase domain (NTD) from the AGC family and a C-terminal kinase domain (CTD) from the CAMK family, similar to 90 kDa ribosomal protein S6 kinases (RSKs). MSKs are activated by two major signaling cascades, the Ras-MAPK and p38 stress kinase pathways, which trigger phosphorylation in the activation loop (A-loop) of the CTD of MSK. The active CTD phosphorylates the hydrophobic motif (HM) of NTD, which facilitates the phosphorylation of the A-loop and activates the NTD, which in turn phosphorylates downstream targets. The MSK2 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270765 [Multi-domain]  Cd Length: 332  Bit Score: 127.73  E-value: 7.29e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 7989 YDILEEIGTGAFGVVHRCRERS---TGNIFAAKFIPVSHSVEK----DLIRREIDIMNQLHHQK-LINLHDAFEDDDEMI 8060
Cdd:cd05614     2 FELLKVLGTGAYGKVFLVRKVSghdANKLYAMKVLRKAALVQKaktvEHTRTERNVLEHVRQSPfLVTLHYAFQTDAKLH 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 8061 LILEFLSGGELFERITAEGYvMTEAEVINYMRQICEGIRHMHEQNIIHLDIKPENIMCQtrSSTNVKLIDFGLATRLDPN 8140
Cdd:cd05614    82 LILDYVSGGELFTHLYQRDH-FSEDEVRFYSGEIILALEHLHKLGIVYRDIKLENILLD--SEGHVVLTDFGLSKEFLTE 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 8141 EVVKITT--GTAEFAAPEIV-NREPVGFYTDMWATGVLSYVLLSGLSPFA--GDNDVQT--LKNVKACDWDFDvesfKYI 8213
Cdd:cd05614   159 EKERTYSfcGTIEYMAPEIIrGKSGHGKAVDWWSLGILMFELLTGASPFTleGEKNTQSevSRRILKCDPPFP----SFI 234
                         250       260       270
                  ....*....|....*....|....*....|....*...
gi 281359561 8214 SEEAKDFIRKLLVRNKEKRM-----TAHECLLHPWLTG 8246
Cdd:cd05614   235 GPVARDLLQKLLCKDPKKRLgagpqGAQEIKEHPFFKG 272
STKc_PAK1 cd06654
Catalytic domain of the Serine/Threonine Kinase, p21-activated kinase 1; STKs catalyze the ...
7988-8244 8.27e-31

Catalytic domain of the Serine/Threonine Kinase, p21-activated kinase 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PAK1 is important in the regulation of many cellular processes including cytoskeletal dynamics, cell motility, growth, and proliferation. Although PAK1 has been regarded mainly as a cytosolic protein, recent reports indicate that PAK1 also exists in significant amounts in the nucleus, where it is involved in transcription modulation and in cell cycle regulatory events. PAK1 is also involved in transformation and tumorigenesis. Its overexpression, hyperactivation and increased nuclear accumulation is correlated to breast cancer invasiveness and progression. Nuclear accumulation is also linked to tamoxifen resistance in breast cancer cells. PAK1 belongs to the group I PAKs, which contain a PBD (p21-binding domain) overlapping with an AID (autoinhibitory domain), a C-terminal catalytic domain, SH3 binding sites and a non-classical SH3 binding site for PIX (PAK-interacting exchange factor). PAKs are Rho family GTPase-regulated kinases that serve as important mediators in the function of Cdc42 (cell division cycle 42) and Rac. The PAK subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270820 [Multi-domain]  Cd Length: 296  Bit Score: 126.38  E-value: 8.27e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 7988 RYDILEEIGTGAFGVVHRCRERSTGNIFAAKFIPVSHSVEKDLIRREIDIMNQLHHQKLINLHDAFEDDDEMILILEFLS 8067
Cdd:cd06654    21 KYTRFEKIGQGASGTVYTAMDVATGQEVAIRQMNLQQQPKKELIINEILVMRENKNPNIVNYLDSYLVGDELWVVMEYLA 100
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 8068 GGELFERITAEgyVMTEAEVINYMRQICEGIRHMHEQNIIHLDIKPENIMCQTRSStnVKLIDFGLATRLDPNEVVKIT- 8146
Cdd:cd06654   101 GGSLTDVVTET--CMDEGQIAAVCRECLQALEFLHSNQVIHRDIKSDNILLGMDGS--VKLTDFGFCAQITPEQSKRSTm 176
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 8147 TGTAEFAAPEIVNREPVGFYTDMWATGVLSYVLLSGLSPFAGDNDVQTLKNVkACDWDFDVESFKYISEEAKDFIRKLLV 8226
Cdd:cd06654   177 VGTPYWMAPEVVTRKAYGPKVDIWSLGIMAIEMIEGEPPYLNENPLRALYLI-ATNGTPELQNPEKLSAIFRDFLNRCLE 255
                         250
                  ....*....|....*...
gi 281359561 8227 RNKEKRMTAHECLLHPWL 8244
Cdd:cd06654   256 MDVEKRGSAKELLQHQFL 273
STKc_GRK4 cd05631
Catalytic domain of the Serine/Threonine Kinase, G protein-coupled Receptor Kinase 4; STKs ...
7995-8242 8.38e-31

Catalytic domain of the Serine/Threonine Kinase, G protein-coupled Receptor Kinase 4; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. GRK4 has a limited tissue distribution. It is mainly found in the testis, but is also present in the cerebellum and kidney. It is expressed as multiple splice variants with different domain architectures and is post-translationally palmitoylated and localized in the membrane. GRK4 polymorphisms are associated with hypertension and salt sensitivity, as they cause hyperphosphorylation, desensitization, and internalization of the dopamine 1 (D1) receptor while increasing the expression of the angiotensin II type 1 receptor. GRK4 plays a crucial role in the D1 receptor regulation of sodium excretion and blood pressure. GRKs phosphorylate and regulate G protein-coupled receptors (GPCRs), the largest superfamily of cell surface receptors which regulate some part of nearly all physiological functions. Phosphorylated GPCRs bind to arrestins, which prevents further G protein signaling despite the presence of activating ligand. The GRK4 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 173720 [Multi-domain]  Cd Length: 285  Bit Score: 126.26  E-value: 8.38e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 7995 IGTGAFGVVHRCRERSTGNIFAAKfipvshSVEKDLIRR---------EIDIMNQLHHQKLINLHDAFEDDDEMILILEF 8065
Cdd:cd05631     8 LGKGGFGEVCACQVRATGKMYACK------KLEKKRIKKrkgeamalnEKRILEKVNSRFVVSLAYAYETKDALCLVLTI 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 8066 LSGGELFERITAEGYV-MTEAEVINYMRQICEGIRHMHEQNIIHLDIKPENIMCQTRSstNVKLIDFGLATRLDPNEVVK 8144
Cdd:cd05631    82 MNGGDLKFHIYNMGNPgFDEQRAIFYAAELCCGLEDLQRERIVYRDLKPENILLDDRG--HIRISDLGLAVQIPEGETVR 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 8145 ITTGTAEFAAPEIVNREPVGFYTDMWATGVLSYVLLSGLSPFAGDNDVQTLKNV--KACDwdfDVESF-KYISEEAKDFI 8221
Cdd:cd05631   160 GRVGTVGYMAPEVINNEKYTFSPDWWGLGCLIYEMIQGQSPFRKRKERVKREEVdrRVKE---DQEEYsEKFSEDAKSIC 236
                         250       260
                  ....*....|....*....|....*.
gi 281359561 8222 RKLLVRNKEKRM-----TAHECLLHP 8242
Cdd:cd05631   237 RMLLTKNPKERLgcrgnGAAGVKQHP 262
Ig_Titin_like cd05748
Immunoglobulin (Ig)-like domain of titin and similar proteins; The members here are composed ...
6174-6255 1.01e-30

Immunoglobulin (Ig)-like domain of titin and similar proteins; The members here are composed of the immunoglobulin (Ig)-like domain found in titin-like proteins and similar proteins. Titin (also called connectin) is a fibrous sarcomeric protein specifically found in vertebrate striated muscle. Titin is a giant protein; depending on isoform composition, it ranges from 2970 to 3700 kDa, and is of a length that spans half a sarcomere. Titin largely consists of multiple repeats of Ig-like and fibronectin type 3 (FN-III)-like domains. Titin connects the ends of myosin thick filaments to Z disks and extends along the thick filament to the H zone. It appears to function similarly to an elastic band, keeping the myosin filaments centered in the sarcomere during muscle contraction or stretching. Within the sarcomere, titin is also attached to or is associated with myosin binding protein C (MyBP-C). MyBP-C appears to contribute to the generation of passive tension by titin and like titin has repeated Ig-like and FN-III domains. Also included in this group are worm twitchin and insect projectin, thick filament proteins of invertebrate muscle which also have repeated Ig-like and FN-III domains.


Pssm-ID: 409406 [Multi-domain]  Cd Length: 82  Bit Score: 118.46  E-value: 1.01e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 6174 RIKVRAGEPVNLNIPISGAPTPTIEWKRGDLKLEEGKRISYETNSERTLFRIDDSNRRDSGKYTVTAANEFGKDTADIEV 6253
Cdd:cd05748     1 TIVVRAGESLRLDIPIKGRPTPTVTWSKDGQPLKETGRVQIETTASSTSLVIKNAKRSDSGKYTLTLKNSAGEKSATINV 80

                  ..
gi 281359561 6254 IV 6255
Cdd:cd05748    81 KV 82
STKc_TLK cd13990
Catalytic domain of the Serine/Threonine kinase, Tousled-Like Kinase; STKs catalyze the ...
7988-8243 1.02e-30

Catalytic domain of the Serine/Threonine kinase, Tousled-Like Kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. TLKs play important functions during the cell cycle and are implicated in chromatin remodeling, DNA replication and repair, and mitosis. They phosphorylate and regulate Anti-silencing function 1 protein (Asf1), a histone H3/H4 chaperone that helps facilitate the assembly of chromatin following DNA replication during S phase. TLKs also phosphorylate the H3 histone tail and are essential in transcription. Vertebrates contain two subfamily members, TLK1 and TLK2. The TLK subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270892 [Multi-domain]  Cd Length: 279  Bit Score: 125.51  E-value: 1.02e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 7988 RYDILEEIGTGAFGVVHRCRERSTGNIFAAKFipvsHSVEKDL--------IR---REIDIMNQLHHQKLINLHDAFE-D 8055
Cdd:cd13990     1 RYLLLNLLGKGGFSEVYKAFDLVEQRYVACKI----HQLNKDWseekkqnyIKhalREYEIHKSLDHPRIVKLYDVFEiD 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 8056 DDEMILILEFLSGGELFERITAEGYvMTEAEVINYMRQICEGIRHMHE--QNIIHLDIKPENIM-CQTRSSTNVKLIDFG 8132
Cdd:cd13990    77 TDSFCTVLEYCDGNDLDFYLKQHKS-IPEREARSIIMQVVSALKYLNEikPPIIHYDLKPGNILlHSGNVSGEIKITDFG 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 8133 LATRLDPN-------EVVKITTGTAEFAAPEI--VNREP--VGFYTDMWATGVLSYVLLSGLSPFA-GDNDVQTLKN--- 8197
Cdd:cd13990   156 LSKIMDDEsynsdgmELTSQGAGTYWYLPPECfvVGKTPpkISSKVDVWSVGVIFYQMLYGRKPFGhNQSQEAILEEnti 235
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*.
gi 281359561 8198 VKACDWDFDVESfkYISEEAKDFIRKLLVRNKEKRMTAHECLLHPW 8243
Cdd:cd13990   236 LKATEVEFPSKP--VVSSEAKDFIRRCLTYRKEDRPDVLQLANDPY 279
STKc_Nek1 cd08218
Catalytic domain of the Protein Serine/Threonine Kinase, Never In Mitosis gene A (NIMA) ...
7988-8244 1.09e-30

Catalytic domain of the Protein Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Nek1 is associated with centrosomes throughout the cell cycle. It is involved in the formation of primary cilium and in the maintenance of centrosomes. It cycles through the nucleus and may be capable of relaying signals between the cilium and the nucleus. Nek1 is implicated in the development of polycystic kidney disease, which is characterized by benign polycystic tumors formed by abnormal overgrowth of renal epithelial cells. It appears also to be involved in DNA damage response, and may be important for both correct DNA damage checkpoint activation and DNA repair. Nek1 is one in a family of 11 different Neks (Nek1-11) that are involved in cell cycle control. The Nek family is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270858 [Multi-domain]  Cd Length: 256  Bit Score: 124.92  E-value: 1.09e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 7988 RYDILEEIGTGAFGVVHRCRERSTGNIFAAKFIPVS--HSVEKDLIRREIDIMNQLHHQKLINLHDAFEDDDEMILILEF 8065
Cdd:cd08218     1 KYVRIKKIGEGSFGKALLVKSKEDGKQYVIKEINISkmSPKEREESRKEVAVLSKMKHPNIVQYQESFEENGNLYIVMDY 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 8066 LSGGELFERITAE-GYVMTEAEVINYMRQICEGIRHMHEQNIIHLDIKPENIMCqTRSSTnVKLIDFGLATRLDPN-EVV 8143
Cdd:cd08218    81 CDGGDLYKRINAQrGVLFPEDQILDWFVQLCLALKHVHDRKILHRDIKSQNIFL-TKDGI-IKLGDFGIARVLNSTvELA 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 8144 KITTGTAEFAAPEIVNREPVGFYTDMWATGVLSYVLLSGLSPFAGDNdvqtLKN--VKACDWDFDVESFKYiSEEAKDFI 8221
Cdd:cd08218   159 RTCIGTPYYLSPEICENKPYNNKSDIWALGCVLYEMCTLKHAFEAGN----MKNlvLKIIRGSYPPVPSRY-SYDLRSLV 233
                         250       260
                  ....*....|....*....|...
gi 281359561 8222 RKLLVRNKEKRMTAHECLLHPWL 8244
Cdd:cd08218   234 SQLFKRNPRDRPSINSILEKPFI 256
PTZ00263 PTZ00263
protein kinase A catalytic subunit; Provisional
7989-8233 1.35e-30

protein kinase A catalytic subunit; Provisional


Pssm-ID: 140289 [Multi-domain]  Cd Length: 329  Bit Score: 126.86  E-value: 1.35e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 7989 YDILEEIGTGAFGVVHRCRERSTGNIFAAKFIPvSHSVEK----DLIRREIDIMNQLHHQKLINLHDAFEDDDEMILILE 8064
Cdd:PTZ00263   20 FEMGETLGTGSFGRVRIAKHKGTGEYYAIKCLK-KREILKmkqvQHVAQEKSILMELSHPFIVNMMCSFQDENRVYFLLE 98
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 8065 FLSGGELFERITAEGYVMTEAEVInYMRQICEGIRHMHEQNIIHLDIKPENIMCQTRSstNVKLIDFGLATRLdpNEVVK 8144
Cdd:PTZ00263   99 FVVGGELFTHLRKAGRFPNDVAKF-YHAELVLAFEYLHSKDIIYRDLKPENLLLDNKG--HVKVTDFGFAKKV--PDRTF 173
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 8145 ITTGTAEFAAPEIVNREPVGFYTDMWATGVLSYVLLSGLSPFAGDNDVQTLKNVKACDWDFDvesfKYISEEAKDFIRKL 8224
Cdd:PTZ00263  174 TLCGTPEYLAPEVIQSKGHGKAVDWWTMGVLLYEFIAGYPPFFDDTPFRIYEKILAGRLKFP----NWFDGRARDLVKGL 249

                  ....*....
gi 281359561 8225 LVRNKEKRM 8233
Cdd:PTZ00263  250 LQTDHTKRL 258
STKc_Nek5 cd08225
Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase ...
7988-8244 2.43e-30

Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase 5; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Neks are involved in the regulation of downstream processes following the activation of Cdc2, and many of their functions are cell cycle-related. They play critical roles in microtubule dynamics during ciliogenesis and mitosis. The specific function of Nek5 is unknown. Nek5 is one in a family of 11 different Neks (Nek1-11). The Nek family is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 173765 [Multi-domain]  Cd Length: 257  Bit Score: 123.91  E-value: 2.43e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 7988 RYDILEEIGTGAFGVVHRCRERSTGNIFAAKFIPVSHSV--EKDLIRREIDIMNQLHHQKLINLHDAFEDDDEMILILEF 8065
Cdd:cd08225     1 RYEIIKKIGEGSFGKIYLAKAKSDSEHCVIKEIDLTKMPvkEKEASKKEVILLAKMKHPNIVTFFASFQENGRLFIVMEY 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 8066 LSGGELFERITAE-GYVMTEAEVINYMRQICEGIRHMHEQNIIHLDIKPENIMCqTRSSTNVKLIDFGLATRL-DPNEVV 8143
Cdd:cd08225    81 CDGGDLMKRINRQrGVLFSEDQILSWFVQISLGLKHIHDRKILHRDIKSQNIFL-SKNGMVAKLGDFGIARQLnDSMELA 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 8144 KITTGTAEFAAPEIVNREPVGFYTDMWATGVLSYVLLSGLSPFAGDNDVQTLknVKACDWDFDVESFKYiSEEAKDFIRK 8223
Cdd:cd08225   160 YTCVGTPYYLSPEICQNRPYNNKTDIWSLGCVLYELCTLKHPFEGNNLHQLV--LKICQGYFAPISPNF-SRDLRSLISQ 236
                         250       260
                  ....*....|....*....|.
gi 281359561 8224 LLVRNKEKRMTAHECLLHPWL 8244
Cdd:cd08225   237 LFKVSPRDRPSITSILKRPFL 257
STKc_CDKL2_3 cd07846
Catalytic domain of the Serine/Threonine Kinases, Cyclin-Dependent protein Kinase Like 2 and 3; ...
7987-8201 3.23e-30

Catalytic domain of the Serine/Threonine Kinases, Cyclin-Dependent protein Kinase Like 2 and 3; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. CDKL2, also called p56 KKIAMRE, is expressed in testis, kidney, lung, and brain. It functions mainly in mature neurons and plays an important role in learning and memory. Inactivation of CDKL3, also called NKIAMRE (NKIATRE in rat), by translocation is associated with mild mental retardation. It has been reported that CDKL3 is lost in leukemic cells having a chromosome arm 5q deletion, and may contribute to the transformed phenotype. CDKs belong to a large family of STKs that are regulated by their cognate cyclins. Together, they are involved in the control of cell-cycle progression, transcription, and neuronal function. The CDKL2/3 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270836 [Multi-domain]  Cd Length: 286  Bit Score: 124.46  E-value: 3.23e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 7987 DRYDILEEIGTGAFGVVHRCRERSTGNIFAAK-FIpvsHSVEKDLIR----REIDIMNQLHHQKLINLHDAFEDDDEMIL 8061
Cdd:cd07846     1 EKYENLGLVGEGSYGMVMKCRHKETGQIVAIKkFL---ESEDDKMVKkiamREIKMLKQLRHENLVNLIEVFRRKKRWYL 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 8062 ILEFLSGGELFERITAEGYvMTEAEVINYMRQICEGIRHMHEQNIIHLDIKPENIMcqTRSSTNVKLIDFGLATRLD-PN 8140
Cdd:cd07846    78 VFEFVDHTVLDDLEKYPNG-LDESRVRKYLFQILRGIDFCHSHNIIHRDIKPENIL--VSQSGVVKLCDFGFARTLAaPG 154
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 281359561 8141 EVVKITTGTAEFAAPEIVNREP-VGFYTDMWATGVLSYVLLSGLSPFAGDNDVQTLKNVKAC 8201
Cdd:cd07846   155 EVYTDYVATRWYRAPELLVGDTkYGKAVDVWAVGCLVTEMLTGEPLFPGDSDIDQLYHIIKC 216
STKc_CDK9_like cd07840
Catalytic domain of Cyclin-Dependent protein Kinase 9-like Serine/Threonine Kinases; STKs ...
7989-8243 3.31e-30

Catalytic domain of Cyclin-Dependent protein Kinase 9-like Serine/Threonine Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily is composed of CDK9 and CDK12 from higher eukaryotes, yeast BUR1, C-type plant CDKs (CdkC), and similar proteins. CDK9, BUR1, and CdkC are functionally equivalent. They act as a kinase for the C-terminal domain of RNA polymerase II and participate in regulating mutliple steps of gene expression including transcription elongation and RNA processing. CDK9 and CdkC associate with T-type cyclins while BUR1 associates with the cyclin BUR2. CDK12 is a unique CDK that contains an arginine/serine-rich (RS) domain, which is predominantly found in splicing factors. CDK12 interacts with cyclins L1 and L2, and participates in regulating transcription and alternative splicing. CDKs belong to a large family of STKs that are regulated by their cognate cyclins. Together, they are involved in the control of cell-cycle progression, transcription, and neuronal function. The CDK9-like subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270832 [Multi-domain]  Cd Length: 291  Bit Score: 124.60  E-value: 3.31e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 7989 YDILEEIGTGAFGVVHRCRERSTGNIFAAKFIPVSHsvEKD----LIRREIDIMNQLHHQKLINLHD------AFEDDDE 8058
Cdd:cd07840     1 YEKIAQIGEGTYGQVYKARNKKTGELVALKKIRMEN--EKEgfpiTAIREIKLLQKLDHPNVVRLKEivtskgSAKYKGS 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 8059 MILILEF----LSGgeLFERitaEGYVMTEAEVINYMRQICEGIRHMHEQNIIHLDIKPENIMCQTRSstNVKLIDFGLA 8134
Cdd:cd07840    79 IYMVFEYmdhdLTG--LLDN---PEVKFTESQIKCYMKQLLEGLQYLHSNGILHRDIKGSNILINNDG--VLKLADFGLA 151
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 8135 TRLDPNEVVKITTG--TAEFAAPEIVNREP-VGFYTDMWATGVLSYVLLSGLSPFAGDNDVQTLKNV-KAC------DW- 8203
Cdd:cd07840   152 RPYTKENNADYTNRviTLWYRPPELLLGATrYGPEVDMWSVGCILAELFTGKPIFQGKTELEQLEKIfELCgspteeNWp 231
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 281359561 8204 DFD------------------VESFK-YISEEAKDFIRKLLVRNKEKRMTAHECLLHPW 8243
Cdd:cd07840   232 GVSdlpwfenlkpkkpykrrlREVFKnVIDPSALDLLDKLLTLDPKKRISADQALQHEY 290
STKc_TSSK1_2-like cd14165
Catalytic domain of testis-specific serine/threonine kinase 1, TSSK2, and similar proteins; ...
7989-8244 3.92e-30

Catalytic domain of testis-specific serine/threonine kinase 1, TSSK2, and similar proteins; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. TSSK proteins are almost exclusively expressed postmeiotically in the testis and play important roles in spermatogenesis and/or spermiogenesis. There are five mammalian TSSK proteins which show differences in their localization and timing of expression. TSSK1 and TSSK2 are expressed specifically in meiotic and postmeiotic spermatogenic cells, respectively. TSSK2 is localized in the sperm neck, equatorial segment, and mid-piece of the sperm tail. Both TSSK1 and TSSK2 phosphorylate their common substrate TSKS (testis-specific-kinase-substrate). TSSK1/TSSK2 double knock-out mice are sterile without manifesting other defects, making these kinases viable targets for male contraception. The TSSK1/2-like subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271067 [Multi-domain]  Cd Length: 263  Bit Score: 123.35  E-value: 3.92e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 7989 YDILEEIGTGAFGVV-----HRCRERSTGNIFAAKFIPvSHSVEKdLIRREIDIMNQLHHQKLINLHDAFEDDDEMILI- 8062
Cdd:cd14165     3 YILGINLGEGSYAKVksaysERLKCNVAIKIIDKKKAP-DDFVEK-FLPRELEILARLNHKSIIKTYEIFETSDGKVYIv 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 8063 LEFLSGGELFERITAEGyVMTEAEVINYMRQICEGIRHMHEQNIIHLDIKPENIMCQtrSSTNVKLIDFGLATRLDPNEV 8142
Cdd:cd14165    81 MELGVQGDLLEFIKLRG-ALPEDVARKMFHQLSSAIKYCHELDIVHRDLKCENLLLD--KDFNIKLTDFGFSKRCLRDEN 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 8143 VKIT-----TGTAEFAAPEIVNREPvgfY----TDMWATGVLSYVLLSGLSPFAGDNDVQTLKNVKACDWDFdvESFKYI 8213
Cdd:cd14165   158 GRIVlsktfCGSAAYAAPEVLQGIP---YdpriYDIWSLGVILYIMVCGSMPYDDSNVKKMLKIQKEHRVRF--PRSKNL 232
                         250       260       270
                  ....*....|....*....|....*....|.
gi 281359561 8214 SEEAKDFIRKLLVRNKEKRMTAHECLLHPWL 8244
Cdd:cd14165   233 TSECKDLIYRLLQPDVSQRLCIDEVLSHPWL 263
STKc_YSK4 cd06631
Catalytic domain of the Serine/Threonine Kinase, Yeast Sps1/Ste20-related Kinase 4; STKs ...
7993-8244 4.55e-30

Catalytic domain of the Serine/Threonine Kinase, Yeast Sps1/Ste20-related Kinase 4; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. YSK4 is a putative MAPKKK, whose mammalian gene has been isolated. MAPKKKs phosphorylate and activate MAPK kinases, which in turn phosphorylate and activate MAPKs during signaling cascades that are important in mediating cellular responses to extracellular signals. The YSK4 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270801 [Multi-domain]  Cd Length: 266  Bit Score: 123.32  E-value: 4.55e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 7993 EEIGTGAFGVVHrCRERSTGNIFAAKFIPVSHS------VEKDLIRREIDIMNQLHHQKLINLHDAFEDDDEMILILEFL 8066
Cdd:cd06631     7 NVLGKGAYGTVY-CGLTSTGQLIAVKQVELDTSdkekaeKEYEKLQEEVDLLKTLKHVNIVGYLGTCLEDNVVSIFMEFV 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 8067 SGGELfERITAEGYVMTEAEVINYMRQICEGIRHMHEQNIIHLDIKPENIMCQTRSStnVKLIDFGLATRL-------DP 8139
Cdd:cd06631    86 PGGSI-ASILARFGALEEPVFCRYTKQILEGVAYLHNNNVIHRDIKGNNIMLMPNGV--IKLIDFGCAKRLcinlssgSQ 162
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 8140 NEVVKITTGTAEFAAPEIVNREPVGFYTDMWATGVLSYVLLSGLSPFAGDNDVQTL-------KNVKACDWDFdvesfky 8212
Cdd:cd06631   163 SQLLKSMRGTPYWMAPEVINETGHGRKSDIWSIGCTVFEMATGKPPWADMNPMAAIfaigsgrKPVPRLPDKF------- 235
                         250       260       270
                  ....*....|....*....|....*....|..
gi 281359561 8213 iSEEAKDFIRKLLVRNKEKRMTAHECLLHPWL 8244
Cdd:cd06631   236 -SPEARDFVHACLTRDQDERPSAEQLLKHPFI 266
STKc_GRK6 cd05630
Catalytic domain of the Serine/Threonine Kinase, G protein-coupled Receptor Kinase 6; STKs ...
7995-8242 5.42e-30

Catalytic domain of the Serine/Threonine Kinase, G protein-coupled Receptor Kinase 6; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. GRK6 is widely expressed in many tissues and is expressed as multiple splice variants with different domain architectures. It is post-translationally palmitoylated and localized in the membrane. GRK6 plays important roles in the regulation of dopamine, M3 muscarinic, opioid, and chemokine receptor signaling. It also plays maladaptive roles in addiction and Parkinson's disease. GRK6-deficient mice exhibit altered dopamine receptor regulation, decreased lymphocyte chemotaxis, and increased acute inflammation and neutrophil chemotaxis. GRKs phosphorylate and regulate G protein-coupled receptors (GPCRs), the largest superfamily of cell surface receptors which regulate some part of nearly all physiological functions. Phosphorylated GPCRs bind to arrestins, which prevents further G protein signaling despite the presence of activating ligand. The GRK6 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270779 [Multi-domain]  Cd Length: 285  Bit Score: 123.59  E-value: 5.42e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 7995 IGTGAFGVVHRCRERSTGNIFAAKfipvshSVEKDLIRR---------EIDIMNQLHHQKLINLHDAFEDDDEMILILEF 8065
Cdd:cd05630     8 LGKGGFGEVCACQVRATGKMYACK------KLEKKRIKKrkgeamalnEKQILEKVNSRFVVSLAYAYETKDALCLVLTL 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 8066 LSGGELFERITAEGYV-MTEAEVINYMRQICEGIRHMHEQNIIHLDIKPENIMCQTRSstNVKLIDFGLATRLDPNEVVK 8144
Cdd:cd05630    82 MNGGDLKFHIYHMGQAgFPEARAVFYAAEICCGLEDLHRERIVYRDLKPENILLDDHG--HIRISDLGLAVHVPEGQTIK 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 8145 ITTGTAEFAAPEIVNREPVGFYTDMWATGVLSYVLLSGLSPFAGDNDVQTLKNVKACDWDFDVESFKYISEEAKDFIRKL 8224
Cdd:cd05630   160 GRVGTVGYMAPEVVKNERYTFSPDWWALGCLLYEMIAGQSPFQQRKKKIKREEVERLVKEVPEEYSEKFSPQARSLCSML 239
                         250       260
                  ....*....|....*....|...
gi 281359561 8225 LVRNKEKRM-----TAHECLLHP 8242
Cdd:cd05630   240 LCKDPAERLgcrggGAREVKEHP 262
PKc_MAPKK cd06605
Catalytic domain of the dual-specificity Protein Kinase, Mitogen-Activated Protein Kinase ...
7987-8245 6.48e-30

Catalytic domain of the dual-specificity Protein Kinase, Mitogen-Activated Protein Kinase Kinase; PKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine (ST) or tyrosine residues on protein substrates. MAPKKs are dual-specificity PKs that phosphorylate their downstream targets, MAPKs, at specific threonine and tyrosine residues. The MAPK signaling pathways are important mediators of cellular responses to extracellular signals. The pathways involve a triple kinase core cascade comprising the MAPK, which is phosphorylated and activated by a MAPK kinase (MAPKK or MKK or MAP2K), which itself is phosphorylated and activated by a MAPKK kinase (MAPKKK or MKKK or MAP3K). There are three MAPK subfamilies: extracellular signal-regulated kinase (ERK), c-Jun N-terminal kinase (JNK), and p38. In mammalian cells, there are seven MAPKKs (named MKK1-7) and 20 MAPKKKs. Each MAPK subfamily can be activated by at least two cognate MAPKKs and by multiple MAPKKKs. The MAPKK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270782 [Multi-domain]  Cd Length: 265  Bit Score: 122.84  E-value: 6.48e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 7987 DRYDILEEIGTGAFGVVHRCRERSTGNIFAAKFIPVS-HSVEKDLIRREIDIMNQLHHQKLINLHDAFEDDDEMILILEF 8065
Cdd:cd06605     1 DDLEYLGELGEGNGGVVSKVRHRPSGQIMAVKVIRLEiDEALQKQILRELDVLHKCNSPYIVGFYGAFYSEGDISICMEY 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 8066 LSGGELfERITAEGYVMTEAEVINYMRQICEGIRHMHEQ-NIIHLDIKPENIMCQTRSstNVKLIDFGLATRLdPNEVVK 8144
Cdd:cd06605    81 MDGGSL-DKILKEVGRIPERILGKIAVAVVKGLIYLHEKhKIIHRDVKPSNILVNSRG--QVKLCDFGVSGQL-VDSLAK 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 8145 ITTGTAEFAAPEIVNREPVGFYTDMWATGVLSYVLLSGLSPFAGDNdvqtlknvkACDWDFDVESFKYI----------- 8213
Cdd:cd06605   157 TFVGTRSYMAPERISGGKYTVKSDIWSLGLSLVELATGRFPYPPPN---------AKPSMMIFELLSYIvdepppllpsg 227
                         250       260       270
                  ....*....|....*....|....*....|....
gi 281359561 8214 --SEEAKDFIRKLLVRNKEKRMTAHECLLHPWLT 8245
Cdd:cd06605   228 kfSPDFQDFVSQCLQKDPTERPSYKELMEHPFIK 261
STKc_OSR1_SPAK cd06610
Catalytic domain of the Serine/Threonine Kinases, Oxidative stress response kinase and ...
7987-8242 1.14e-29

Catalytic domain of the Serine/Threonine Kinases, Oxidative stress response kinase and Ste20-related proline alanine-rich kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. SPAK is also referred to as STK39 or PASK (proline-alanine-rich STE20-related kinase). OSR1 and SPAK regulate the activity of cation-chloride cotransporters through direct interaction and phosphorylation. They are also implicated in cytoskeletal rearrangement, cell differentiation, transformation and proliferation. OSR1 and SPAK contain a conserved C-terminal (CCT) domain, which recognizes a unique motif ([RK]FX[VI]) present in their activating kinases (WNK1/WNK4) and their substrates. The OSR1 and SPAK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270787 [Multi-domain]  Cd Length: 267  Bit Score: 122.08  E-value: 1.14e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 7987 DRYDILEEIGTGAFGVVHRCRERSTGNIFAAKFIPVSH-SVEKDLIRREIDIMNQLHHQKLINLHDAFEDDDEMILILEF 8065
Cdd:cd06610     1 DDYELIEVIGSGATAVVYAAYCLPKKEKVAIKRIDLEKcQTSMDELRKEIQAMSQCNHPNVVSYYTSFVVGDELWLVMPL 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 8066 LSGGELFErITAEGY---VMTEAEVINYMRQICEGIRHMHEQNIIHLDIKPENIMCQTRSStnVKLIDFGLATRLDPN-- 8140
Cdd:cd06610    81 LSGGSLLD-IMKSSYprgGLDEAIIATVLKEVLKGLEYLHSNGQIHRDVKAGNILLGEDGS--VKIADFGVSASLATGgd 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 8141 ---EVVKITTGTAEFAAPEIVnrEPVGFYT---DMWATGVLSYVLLSGLSPFAG----DNDVQTLKNVKACdWDFDVESF 8210
Cdd:cd06610   158 rtrKVRKTFVGTPCWMAPEVM--EQVRGYDfkaDIWSFGITAIELATGAAPYSKyppmKVLMLTLQNDPPS-LETGADYK 234
                         250       260       270
                  ....*....|....*....|....*....|..
gi 281359561 8211 KYiSEEAKDFIRKLLVRNKEKRMTAHECLLHP 8242
Cdd:cd06610   235 KY-SKSFRKMISLCLQKDPSKRPTAEELLKHK 265
PKc_DYRK_like cd14133
Catalytic domain of Dual-specificity tYrosine-phosphorylated and -Regulated Kinase-like ...
7989-8244 1.15e-29

Catalytic domain of Dual-specificity tYrosine-phosphorylated and -Regulated Kinase-like protein kinases; Dual-specificity PKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine (S/T) as well as tyrosine residues on protein substrates. This subfamily is composed of the dual-specificity DYRKs and YAK1, as well as the S/T kinases (STKs), HIPKs. DYRKs and YAK1 autophosphorylate themselves on tyrosine residues and phosphorylate their substrates exclusively on S/T residues. Proteins in this subfamily play important roles in cell proliferation, differentiation, survival, growth, and development. The DYRK-like subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271035 [Multi-domain]  Cd Length: 262  Bit Score: 121.99  E-value: 1.15e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 7989 YDILEEIGTGAFGVVHRCRERSTGNIFAAKFIPVShsveKDLIRREIDIMNQLH---------HQKLINLHDAFEDDDEM 8059
Cdd:cd14133     1 YEVLEVLGKGTFGQVVKCYDLLTGEEVALKIIKNN----KDYLDQSLDEIRLLEllnkkdkadKYHIVRLKDVFYFKNHL 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 8060 ILILEFLsGGELFE--RITAEGYVmTEAEVINYMRQICEGIRHMHEQNIIHLDIKPENIMCQTRSSTNVKLIDFGLATRL 8137
Cdd:cd14133    77 CIVFELL-SQNLYEflKQNKFQYL-SLPRIRKIAQQILEALVFLHSLGLIHCDLKPENILLASYSRCQIKIIDFGSSCFL 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 8138 dpNEVVKITTGTAEFAAPEIVNREPVGFYTDMWATGVLSYVLLSGLSPFAGDNDVQTLKNVKACDWDFDvesFKYIS--- 8214
Cdd:cd14133   155 --TQRLYSYIQSRYYRAPEVILGLPYDEKIDMWSLGCILAELYTGEPLFPGASEVDQLARIIGTIGIPP---AHMLDqgk 229
                         250       260       270
                  ....*....|....*....|....*....|...
gi 281359561 8215 ---EEAKDFIRKLLVRNKEKRMTAHECLLHPWL 8244
Cdd:cd14133   230 addELFVDFLKKLLEIDPKERPTASQALSHPWL 262
STKc_SGK cd05575
Catalytic domain of the Serine/Threonine Kinase, Serum- and Glucocorticoid-induced Kinase; ...
7995-8235 1.19e-29

Catalytic domain of the Serine/Threonine Kinase, Serum- and Glucocorticoid-induced Kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. SGKs are activated by insulin and growth factors via phosphoinositide 3-kinase and PDK1. They activate ion channels, ion carriers, and the Na-K-ATPase, as well as regulate the activity of enzymes and transcription factors. SGKs play important roles in transport, hormone release, neuroexcitability, cell proliferation, and apoptosis. There are three isoforms of SGK, named SGK1, SGK2, and SGK3 (also called cytokine-independent survival kinase CISK). The SGK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270727 [Multi-domain]  Cd Length: 323  Bit Score: 123.97  E-value: 1.19e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 7995 IGTGAFGVVHRCRERSTGNIFAAKFIpvshsvEKDLI--RREID-IM-------NQLHHQKLINLHDAFEDDDEMILILE 8064
Cdd:cd05575     3 IGKGSFGKVLLARHKAEGKLYAVKVL------QKKAIlkRNEVKhIMaernvllKNVKHPFLVGLHYSFQTKDKLYFVLD 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 8065 FLSGGELFERITAEGYvMTEAEVINYMRQICEGIRHMHEQNIIHLDIKPENIMCQtrSSTNVKLIDFGLATR-LDPNEVV 8143
Cdd:cd05575    77 YVNGGELFFHLQRERH-FPEPRARFYAAEIASALGYLHSLNIIYRDLKPENILLD--SQGHVVLTDFGLCKEgIEPSDTT 153
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 8144 KITTGTAEFAAPEIVNREPVGFYTDMWATGVLSYVLLSGLSPFAGDNDVQTLKNVKacdwdFDVESFK-YISEEAKDFIR 8222
Cdd:cd05575   154 STFCGTPEYLAPEVLRKQPYDRTVDWWCLGAVLYEMLYGLPPFYSRDTAEMYDNIL-----HKPLRLRtNVSPSARDLLE 228
                         250
                  ....*....|...
gi 281359561 8223 KLLVRNKEKRMTA 8235
Cdd:cd05575   229 GLLQKDRTKRLGS 241
STKc_SBK1 cd13987
Catalytic domain of the Serine/Threonine kinase, SH3 Binding Kinase 1; STKs catalyze the ...
7995-8243 1.35e-29

Catalytic domain of the Serine/Threonine kinase, SH3 Binding Kinase 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. SBK1, also called BSK146, is predominantly expressed in the brain. Its expression is increased in the developing brain during the late embryonic stage, coinciding with dramatic neuronal proliferation, migration, and maturation. SBK1 may play an important role in regulating brain development. The SBK1 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270889 [Multi-domain]  Cd Length: 259  Bit Score: 121.66  E-value: 1.35e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 7995 IGTGAFGVVHRCRERSTGNIFAAKFIPVSHSVEKDLIRrEIDIMNQL-HHQKLINLHD-AFEDDDEMILILEFLSGGELF 8072
Cdd:cd13987     1 LGEGTYGKVLLAVHKGSGTKMALKFVPKPSTKLKDFLR-EYNISLELsVHPHIIKTYDvAFETEDYYVFAQEYAPYGDLF 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 8073 ERITAEGYVmTEAEVINYMRQICEGIRHMHEQNIIHLDIKPENIMCQTRSSTNVKLIDFGLATRLDpnEVVKITTGTAEF 8152
Cdd:cd13987    80 SIIPPQVGL-PEERVKRCAAQLASALDFMHSKNLVHRDIKPENVLLFDKDCRRVKLCDFGLTRRVG--STVKRVSGTIPY 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 8153 AAPEIVNREPVGFY-----TDMWATGVLSYVLLSGLSPF---AGDND-----VQTLKNVKACdwdfdVES-FKYISEEAK 8218
Cdd:cd13987   157 TAPEVCEAKKNEGFvvdpsIDVWAFGVLLFCCLTGNFPWekaDSDDQfyeefVRWQKRKNTA-----VPSqWRRFTPKAL 231
                         250       260
                  ....*....|....*....|....*...
gi 281359561 8219 DFIRKLLVRNKEKRMTA---HECLLHPW 8243
Cdd:cd13987   232 RMFKKLLAPEPERRCSIkevFKYLGDRW 259
STKc_DMPK_like cd05597
Catalytic domain of Myotonic Dystrophy protein kinase (DMPK)-like Serine/Threonine Kinases; ...
7987-8246 1.65e-29

Catalytic domain of Myotonic Dystrophy protein kinase (DMPK)-like Serine/Threonine Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The DMPK-like subfamily is composed of DMPK and DMPK-related cell division control protein 42 (Cdc42) binding kinase (MRCK). DMPK is expressed in skeletal and cardiac muscles, and in central nervous tissues. The functional role of DMPK is not fully understood. It may play a role in the signal transduction and homeostasis of calcium. The DMPK gene is implicated in myotonic dystrophy 1 (DM1), an inherited multisystemic disorder with symptoms that include muscle hyperexcitability, progressive muscle weakness and wasting, cataract development, testicular atrophy, and cardiac conduction defects. The genetic basis for DM1 is the mutational expansion of a CTG repeat in the 3'-UTR of DMPK. MRCK is activated via interaction with the small GTPase Cdc42. MRCK/Cdc42 signaling mediates myosin-dependent cell motility. Three isoforms of MRCK are known, named alpha, beta and gamma. MRCKgamma is expressed in heart and skeletal muscles, unlike MRCKalpha and MRCKbeta, which are expressed ubiquitously. The DMPK-like subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270748 [Multi-domain]  Cd Length: 331  Bit Score: 123.61  E-value: 1.65e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 7987 DRYDILEEIGTGAFGVVHRCRERSTGNIFAAKFI---PVSHSVEKDLIRREIDIMNQLHHQKLINLHDAFEDDDEMILIL 8063
Cdd:cd05597     1 DDFEILKVIGRGAFGEVAVVKLKSTEKVYAMKILnkwEMLKRAETACFREERDVLVNGDRRWITKLHYAFQDENYLYLVM 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 8064 EFLSGGELFERITAEGYVMTEAEVINYMRQICEGIRHMHEQNIIHLDIKPENIMCQtrSSTNVKLIDFGLATRLDPNEVV 8143
Cdd:cd05597    81 DYYCGGDLLTLLSKFEDRLPEEMARFYLAEMVLAIDSIHQLGYVHRDIKPDNVLLD--RNGHIRLADFGSCLKLREDGTV 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 8144 KITT--GTAEFAAPEIV--NREPVGFY---TDMWATGVLSYVLLSGLSPFAGDNDVQT---LKNVKACdWDF--DVESfk 8211
Cdd:cd05597   159 QSSVavGTPDYISPEILqaMEDGKGRYgpeCDWWSLGVCMYEMLYGETPFYAESLVETygkIMNHKEH-FSFpdDEDD-- 235
                         250       260       270
                  ....*....|....*....|....*....|....*..
gi 281359561 8212 yISEEAKDFIRKLLVRNKEK--RMTAHECLLHPWLTG 8246
Cdd:cd05597   236 -VSEEAKDLIRRLICSRERRlgQNGIDDFKKHPFFEG 271
STKc_MOK cd07831
Catalytic domain of the Serine/Threonine Kinase, MAPK/MAK/MRK Overlapping Kinase; STKs ...
7989-8243 2.50e-29

Catalytic domain of the Serine/Threonine Kinase, MAPK/MAK/MRK Overlapping Kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MOK, also called Renal tumor antigen 1 (RAGE-1), is widely expressed and is enriched in testis, kidney, lung, and brain. It is expressed in approximately 50% of renal cell carcinomas (RCC) and is a potential target for immunotherapy. MOK is stabilized by its association with the HSP90 molecular chaperone. It is induced by the transcription factor Cdx2 and may be involved in regulating intestinal epithelial development and differentiation. The MOK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270825 [Multi-domain]  Cd Length: 282  Bit Score: 121.61  E-value: 2.50e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 7989 YDILEEIGTGAFGVVHRCRERSTGNIFAAK-FIPVSHSVEKDLIRREIDIMNQL-HHQKLINLHDAFEDDDE--MILILE 8064
Cdd:cd07831     1 YKILGKIGEGTFSEVLKAQSRKTGKYYAIKcMKKHFKSLEQVNNLREIQALRRLsPHPNILRLIEVLFDRKTgrLALVFE 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 8065 fLSGGELFERITAEGYVMTEAEVINYMRQICEGIRHMHEQNIIHLDIKPENIMCQtrsSTNVKLIDFGLATRLDPNEVVK 8144
Cdd:cd07831    81 -LMDMNLYELIKGRKRPLPEKRVKNYMYQLLKSLDHMHRNGIFHRDIKPENILIK---DDILKLADFGSCRGIYSKPPYT 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 8145 ITTGTAEFAAPEIVNREpvGFYT---DMWATGVLSYVLLSgLSP-FAGDNDVQTLK---NV---------------KACD 8202
Cdd:cd07831   157 EYISTRWYRAPECLLTD--GYYGpkmDIWAVGCVFFEILS-LFPlFPGTNELDQIAkihDVlgtpdaevlkkfrksRHMN 233
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*...
gi 281359561 8203 WDFDVESFKYI-------SEEAKDFIRKLLVRNKEKRMTAHECLLHPW 8243
Cdd:cd07831   234 YNFPSKKGTGLrkllpnaSAEGLDLLKKLLAYDPDERITAKQALRHPY 281
STKc_PKB cd05571
Catalytic domain of the Serine/Threonine Kinase, Protein Kinase B; STKs catalyze the transfer ...
7995-8243 4.12e-29

Catalytic domain of the Serine/Threonine Kinase, Protein Kinase B; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. There are three PKB isoforms from different genes, PKB-alpha (or Akt1), PKB-beta (or Akt2), and PKB-gamma (or Akt3). PKB contains an N-terminal pleckstrin homology (PH) domain and a C-terminal catalytic domain. It is activated downstream of phosphoinositide 3-kinase (PI3K) and plays important roles in diverse cellular functions including cell survival, growth, proliferation, angiogenesis, motility, and migration. PKB also has a central role in a variety of human cancers, having been implicated in tumor initiation, progression, and metastasis. The PKB subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and PI3K.


Pssm-ID: 270723 [Multi-domain]  Cd Length: 322  Bit Score: 122.08  E-value: 4.12e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 7995 IGTGAFGVVHRCRERSTGNIFAAKFIPVSHSVEKDLIRR---EIDIMNQLHHQKLINLHDAFEDDDEMILILEFLSGGEL 8071
Cdd:cd05571     3 LGKGTFGKVILCREKATGELYAIKILKKEVIIAKDEVAHtltENRVLQNTRHPFLTSLKYSFQTNDRLCFVMEYVNGGEL 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 8072 FERITAEGyVMTEAEVINYMRQICEGIRHMHEQNIIHLDIKPENIMCQtrSSTNVKLIDFGLATR-LDPNEVVKITTGTA 8150
Cdd:cd05571    83 FFHLSRER-VFSEDRTRFYGAEIVLALGYLHSQGIVYRDLKLENLLLD--KDGHIKITDFGLCKEeISYGATTKTFCGTP 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 8151 EFAAPEIVNREPVGFYTDMWATGVLSYVLLSGLSPF-AGDNDVQtlknvkacdwdFD---VESFKY---ISEEAKDFIRK 8223
Cdd:cd05571   160 EYLAPEVLEDNDYGRAVDWWGLGVVMYEMMCGRLPFyNRDHEVL-----------FElilMEEVRFpstLSPEAKSLLAG 228
                         250       260
                  ....*....|....*....|....*
gi 281359561 8224 LLVRNKEKRM-----TAHECLLHPW 8243
Cdd:cd05571   229 LLKKDPKKRLgggprDAKEIMEHPF 253
STKc_Nek8 cd08220
Catalytic domain of the Protein Serine/Threonine Kinase, Never In Mitosis gene A (NIMA) ...
7988-8242 4.31e-29

Catalytic domain of the Protein Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase 8; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Nek8 contains an N-terminal kinase catalytic domain and a C-terminal RCC1 (regulator of chromosome condensation) domain. A double point mutation in Nek8 causes cystic kidney disease in mice that genetically resembles human autosomal recessive polycystic kidney disease (ARPKD). Nek8 is also associated with a rare form of juvenile renal cystic disease, nephronophthisis type 9. It has been suggested that a defect in the ciliary localization of Nek8 contributes to the development of cysts manifested by these diseases. Nek8 is one in a family of 11 different Neks (Nek1-11) that are involved in cell cycle control. The Nek family is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270859 [Multi-domain]  Cd Length: 256  Bit Score: 120.22  E-value: 4.31e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 7988 RYDILEEIGTGAFGVVHRCRERSTGNIFAAKFIPVSHSV--EKDLIRREIDIMNQLHHQKLINLHDAFEDDDEMILILEF 8065
Cdd:cd08220     1 KYEKIRVVGRGAYGTVYLCRRKDDNKLVIIKQIPVEQMTkeERQAALNEVKVLSMLHHPNIIEYYESFLEDKALMIVMEY 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 8066 LSGGELFERITAE-GYVMTEAEVINYMRQICEGIRHMHEQNIIHLDIKPENIMCQtRSSTNVKLIDFGLATRLDPNEVVK 8144
Cdd:cd08220    81 APGGTLFEYIQQRkGSLLSEEEILHFFVQILLALHHVHSKQILHRDLKTQNILLN-KKRTVVKIGDFGISKILSSKSKAY 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 8145 ITTGTAEFAAPEIVNREPVGFYTDMWATGVLSYVLLSGLSPFAGDN-DVQTLKNVKAcdwDFDVESFKYiSEEAKDFIRK 8223
Cdd:cd08220   160 TVVGTPCYISPELCEGKPYNQKSDIWALGCVLYELASLKRAFEAANlPALVLKIMRG---TFAPISDRY-SEELRHLILS 235
                         250
                  ....*....|....*....
gi 281359561 8224 LLVRNKEKRMTAHECLLHP 8242
Cdd:cd08220   236 MLHLDPNKRPTLSEIMAQP 254
STKc_WNK cd13983
Catalytic domain of the Serine/Threonine kinase, With No Lysine (WNK) kinase; STKs catalyze ...
7986-8244 4.69e-29

Catalytic domain of the Serine/Threonine kinase, With No Lysine (WNK) kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. WNKs comprise a subfamily of STKs with an unusual placement of a catalytic lysine relative to all other protein kinases. They are critical in regulating ion balance and are thus, important components in the control of blood pressure. They are also involved in cell signaling, survival, proliferation, and organ development. WNKs are activated by hyperosmotic or low-chloride hypotonic stress and they function upstream of SPAK and OSR1 kinases, which regulate the activity of cation-chloride cotransporters through direct interaction and phosphorylation. There are four vertebrate WNKs which show varying expression patterns. WNK1 and WNK2 are widely expressed while WNK3 and WNK4 show a more restricted expression pattern. Because mutations in human WNK1 and WNK4 cause PseudoHypoAldosteronism type II (PHAII), characterized by hypertension (due to increased sodium reabsorption) and hyperkalemia (due to impaired renal potassium secretion), there are more studies conducted on these two proteins, compared to WNK2 and WNK3. The WNK subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270885 [Multi-domain]  Cd Length: 258  Bit Score: 120.02  E-value: 4.69e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 7986 YDRYDilEEIGTGAFGVVHRCRERSTGNIFAAKFIPVSH--SVEKDLIRREIDIMNQLHHQKLINLHDAFEDD--DEMIL 8061
Cdd:cd13983     2 YLKFN--EVLGRGSFKTVYRAFDTEEGIEVAWNEIKLRKlpKAERQRFKQEIEILKSLKHPNIIKFYDSWESKskKEVIF 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 8062 ILEFLSGGELFERITAEGyVMTEAEVINYMRQICEGIRHMHEQN--IIHLDIKPENIMCqTRSSTNVKLIDFGLATRLDP 8139
Cdd:cd13983    80 ITELMTSGTLKQYLKRFK-RLKLKVIKSWCRQILEGLNYLHTRDppIIHRDLKCDNIFI-NGNTGEVKIGDLGLATLLRQ 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 8140 NEVVKItTGTAEFAAPEIVNREpvgfYT---DMWATGVLSYVLLSGLSPFAG-DNDVQTLKNVKAcdwDFDVESFKYI-S 8214
Cdd:cd13983   158 SFAKSV-IGTPEFMAPEMYEEH----YDekvDIYAFGMCLLEMATGEYPYSEcTNAAQIYKKVTS---GIKPESLSKVkD 229
                         250       260       270
                  ....*....|....*....|....*....|
gi 281359561 8215 EEAKDFIRKLLvRNKEKRMTAHECLLHPWL 8244
Cdd:cd13983   230 PELKDFIEKCL-KPPDERPSARELLEHPFF 258
STKc_PAK6 cd06659
Catalytic domain of the Serine/Threonine Kinase, p21-activated kinase 6; STKs catalyze the ...
7994-8244 4.92e-29

Catalytic domain of the Serine/Threonine Kinase, p21-activated kinase 6; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PAK6 may play a role in stress responses through its activation by the mitogen-activated protein kinase (MAPK) p38 and MAPK kinase 6 (MKK6) pathway. PAK6 is highly expressed in the brain. It is not required for viability, but together with PAK5, it is required for normal levels of locomotion and activity, and for learning and memory. Increased expression of PAK6 is found in primary and metastatic prostate cancer. PAK6 may play a role in the regulation of motility. PAK6 belongs to the group II PAKs, which contain a PBD (p21-binding domain) and a C-terminal catalytic domain, but do not harbor an AID (autoinhibitory domain) or SH3 binding sites. PAKs are Rho family GTPase-regulated kinases that serve as important mediators in the function of Cdc42 (cell division cycle 42) and Rac. The PAK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270821 [Multi-domain]  Cd Length: 297  Bit Score: 121.25  E-value: 4.92e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 7994 EIGTGAFGVVHRCRERSTGNIFAAKFIPVSHSVEKDLIRREIDIMNQLHHQKLINLHDAFEDDDEMILILEFLSGGELFE 8073
Cdd:cd06659    28 KIGEGSTGVVCIAREKHSGRQVAVKMMDLRKQQRRELLFNEVVIMRDYQHPNVVEMYKSYLVGEELWVLMEYLQGGALTD 107
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 8074 RITAEGYvmTEAEVINYMRQICEGIRHMHEQNIIHLDIKPENIMCQTrsSTNVKLIDFGLATRLD---PNEvvKITTGTA 8150
Cdd:cd06659   108 IVSQTRL--NEEQIATVCEAVLQALAYLHSQGVIHRDIKSDSILLTL--DGRVKLSDFGFCAQISkdvPKR--KSLVGTP 181
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 8151 EFAAPEIVNREPVGFYTDMWATGVLSYVLLSGLSPFAGDNDVQTLKNVKACDwDFDVESFKYISEEAKDFIRKLLVRNKE 8230
Cdd:cd06659   182 YWMAPEVISRCPYGTEVDIWSLGIMVIEMVDGEPPYFSDSPVQAMKRLRDSP-PPKLKNSHKASPVLRDFLERMLVRDPQ 260
                         250
                  ....*....|....
gi 281359561 8231 KRMTAHECLLHPWL 8244
Cdd:cd06659   261 ERATAQELLDHPFL 274
STKc_ROCK cd05596
Catalytic domain of the Serine/Threonine Kinase, Rho-associated coiled-coil containing protein ...
7959-8247 5.26e-29

Catalytic domain of the Serine/Threonine Kinase, Rho-associated coiled-coil containing protein kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. ROCK is also referred to as Rho-associated kinase or simply as Rho kinase. It contains an N-terminal extension, a catalytic kinase domain, and a long C-terminal extension, which contains a coiled-coil region encompassing a Rho-binding domain (RBD) and a pleckstrin homology (PH) domain. ROCK is auto-inhibited by the RBD and PH domain interacting with the catalytic domain. It is activated via interaction with Rho GTPases and is involved in many cellular functions including contraction, adhesion, migration, motility, proliferation, and apoptosis. The ROCK subfamily consists of two isoforms, ROCK1 and ROCK2, which may be functionally redundant in some systems, but exhibit different tissue distributions. Both isoforms are ubiquitously expressed in most tissues, but ROCK2 is more prominent in brain and skeletal muscle while ROCK1 is more pronounced in the liver, testes, and kidney. Studies in knockout mice result in different phenotypes, suggesting that the two isoforms do not compensate for each other during embryonic development. The ROCK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270747 [Multi-domain]  Cd Length: 352  Bit Score: 122.87  E-value: 5.26e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 7959 VKDYDSYVfDIYSKFVPQpVEISQQSVYDrYDILEEIGTGAFGVVHRCRERSTGNIFAAKFIPvshsvEKDLIRR----- 8033
Cdd:cd05596     1 NKNIENFL-NRYEKPVNE-ITKLRMNAED-FDVIKVIGRGAFGEVQLVRHKSTKKVYAMKLLS-----KFEMIKRsdsaf 72
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 8034 ---EIDIMNQLHHQKLINLHDAFEDDDEMILILEFLSGGELFERItaEGYVMTEAEVINYMRQICEGIRHMHEQNIIHLD 8110
Cdd:cd05596    73 fweERDIMAHANSEWIVQLHYAFQDDKYLYMVMDYMPGGDLVNLM--SNYDVPEKWARFYTAEVVLALDAIHSMGFVHRD 150
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 8111 IKPENIMCQtrSSTNVKLIDFGLATRLDPNEVVKITT--GTAEFAAPEIVNREPV-GFY---TDMWATGVLSYVLLSGLS 8184
Cdd:cd05596   151 VKPDNMLLD--ASGHLKLADFGTCMKMDKDGLVRSDTavGTPDYISPEVLKSQGGdGVYgreCDWWSVGVFLYEMLVGDT 228
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 8185 PFAGDNDVQTLKNV----KACDWDFDVEsfkyISEEAKDFIRKLLVrNKEKRMTAH---ECLLHPWLTGD 8247
Cdd:cd05596   229 PFYADSLVGTYGKImnhkNSLQFPDDVE----ISKDAKSLICAFLT-DREVRLGRNgieEIKAHPFFKND 293
STKc_ULK2 cd14201
Catalytic domain of the Serine/Threonine kinase, Unc-51-like kinase 2; STKs catalyze the ...
7986-8244 5.29e-29

Catalytic domain of the Serine/Threonine kinase, Unc-51-like kinase 2; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The ATG1/ULK complex is conserved from yeast to humans and it plays a critical role in the initiation of autophagy, the intracellular system that leads to the lysosomal degradation of cellular components and their recycling into basic metabolic units. ULK2 is ubiquitously expressed and is essential in autophagy induction. It displays partially redundant functions with ULK1 and is able to compensate for the loss of ULK1 in non-selective autophagy. It also displays neuron-specific functions and is important in axon development. The ULK2 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271103 [Multi-domain]  Cd Length: 271  Bit Score: 120.50  E-value: 5.29e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 7986 YDRYDIleeIGTGAFGVVHRCRERS-TGNIFAAKFIPVSH-SVEKDLIRREIDIMNQLHHQKLINLHDAFEDDDEMILIL 8063
Cdd:cd14201     8 YSRKDL---VGHGAFAVVFKGRHRKkTDWEVAIKSINKKNlSKSQILLGKEIKILKELQHENIVALYDVQEMPNSVFLVM 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 8064 EFLSGGELFERITAEGyVMTEAEVINYMRQICEGIRHMHEQNIIHLDIKPENIMCQ-------TRSSTNVKLIDFGLATR 8136
Cdd:cd14201    85 EYCNGGDLADYLQAKG-TLSEDTIRVFLQQIAAAMRILHSKGIIHRDLKPQNILLSyasrkksSVSGIRIKIADFGFARY 163
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 8137 LDPNEVVKITTGTAEFAAPEIVNREPVGFYTDMWATGVLSYVLLSGLSPFAGdNDVQTLKNVKACDWDFDVESFKYISEE 8216
Cdd:cd14201   164 LQSNMMAATLCGSPMYMAPEVIMSQHYDAKADLWSIGTVIYQCLVGKPPFQA-NSPQDLRMFYEKNKNLQPSIPRETSPY 242
                         250       260
                  ....*....|....*....|....*...
gi 281359561 8217 AKDFIRKLLVRNKEKRMTAHECLLHPWL 8244
Cdd:cd14201   243 LADLLLGLLQRNQKDRMDFEAFFSHPFL 270
STKc_Nek9 cd08221
Catalytic domain of the Protein Serine/Threonine Kinase, Never In Mitosis gene A (NIMA) ...
7995-8244 6.68e-29

Catalytic domain of the Protein Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase 9; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Nek9, also called Nercc1, is primarily a cytoplasmic protein but can also localize in the nucleus. It is involved in modulating chromosome alignment and splitting during mitosis. It interacts with the gamma-tubulin ring complex and the Ran GTPase, and is implicated in microtubule organization. Nek9 associates with FACT (FAcilitates Chromatin Transcription) and modulates interphase progression. It also interacts with Nek6, and Nek7, during mitosis, resulting in their activation. Nek9 is one in a family of 11 different Neks (Nek1-11) that are involved in cell cycle control. The Nek family is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270860 [Multi-domain]  Cd Length: 256  Bit Score: 119.46  E-value: 6.68e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 7995 IGTGAFGVVHRCRERSTGNIFAAKFIPVSHSVEKDliRR----EIDIMNQLHHQKLINLHDAFEDDDEMILILEFLSGGE 8070
Cdd:cd08221     8 LGRGAFGEAVLYRKTEDNSLVVWKEVNLSRLSEKE--RRdalnEIDILSLLNHDNIITYYNHFLDGESLFIEMEYCNGGN 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 8071 LFERITAE-GYVMTEAEVINYMRQICEGIRHMHEQNIIHLDIKPENIMCqTRSSTnVKLIDFGLATRLDP-NEVVKITTG 8148
Cdd:cd08221    86 LHDKIAQQkNQLFPEEVVLWYLYQIVSAVSHIHKAGILHRDIKTLNIFL-TKADL-VKLGDFGISKVLDSeSSMAESIVG 163
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 8149 TAEFAAPEIVNREPVGFYTDMWATGVLSYVLLSGLSPFAGDNDVQTLKNVKACDWDFDVESFkyiSEEAKDFIRKLLVRN 8228
Cdd:cd08221   164 TPYYMSPELVQGVKYNFKSDIWAVGCVLYELLTLKRTFDATNPLRLAVKIVQGEYEDIDEQY---SEEIIQLVHDCLHQD 240
                         250
                  ....*....|....*.
gi 281359561 8229 KEKRMTAHECLLHPWL 8244
Cdd:cd08221   241 PEDRPTAEELLERPLL 256
STKc_Byr2_like cd06628
Catalytic domain of the Serine/Threonine Kinases, fungal Byr2-like Mitogen-Activated Protein ...
7995-8244 7.96e-29

Catalytic domain of the Serine/Threonine Kinases, fungal Byr2-like Mitogen-Activated Protein Kinase Kinase Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Members of this group include the MAPKKKs Schizosaccharomyces pombe Byr2, Saccharomyces cerevisiae and Cryptococcus neoformans Ste11, and related proteins. They contain an N-terminal SAM (sterile alpha-motif) domain, which mediates protein-protein interaction, and a C-terminal catalytic domain. MAPKKKs phosphorylate and activate MAPK kinases, which in turn phosphorylate and activate MAPKs during signaling cascades that are important in mediating cellular responses to extracellular signals. Fission yeast Byr2 is regulated by Ras1. It responds to pheromone signaling and controls mating through the MAPK pathway. Budding yeast Ste11 functions in MAPK cascades that regulate mating, high osmolarity glycerol, and filamentous growth responses. The Byr2 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270798 [Multi-domain]  Cd Length: 267  Bit Score: 119.56  E-value: 7.96e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 7995 IGTGAFGVVHRCRERSTGNIFAAKFIPVSHSVEK---------DLIRREIDIMNQLHHQKLINLHDAFEDDDEMILILEF 8065
Cdd:cd06628     8 IGSGSFGSVYLGMNASSGELMAVKQVELPSVSAEnkdrkksmlDALQREIALLRELQHENIVQYLGSSSDANHLNIFLEY 87
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 8066 LSGGELFERITAEGyVMTEAEVINYMRQICEGIRHMHEQNIIHLDIKPENIMCQTRSStnVKLIDFGLATRLDPNEVVKI 8145
Cdd:cd06628    88 VPGGSVATLLNNYG-AFEESLVRNFVRQILKGLNYLHNRGIIHRDIKGANILVDNKGG--IKISDFGISKKLEANSLSTK 164
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 8146 TT-------GTAEFAAPEIVNREPVGFYTDMWATGVLSYVLLSGLSPFAGDNDVQTLknvkacdwdFDVESF------KY 8212
Cdd:cd06628   165 NNgarpslqGSVFWMAPEVVKQTSYTRKADIWSLGCLVVEMLTGTHPFPDCTQMQAI---------FKIGENasptipSN 235
                         250       260       270
                  ....*....|....*....|....*....|..
gi 281359561 8213 ISEEAKDFIRKLLVRNKEKRMTAHECLLHPWL 8244
Cdd:cd06628   236 ISSEARDFLEKTFEIDHNKRPTADELLKHPFL 267
TyrKc smart00219
Tyrosine kinase, catalytic domain; Phosphotransferases. Tyrosine-specific kinase subfamily.
7991-8200 1.06e-28

Tyrosine kinase, catalytic domain; Phosphotransferases. Tyrosine-specific kinase subfamily.


Pssm-ID: 197581 [Multi-domain]  Cd Length: 257  Bit Score: 119.17  E-value: 1.06e-28
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561   7991 ILEEIGTGAFGVVHRCRERSTGNIF----AAKFIPVSHS-VEKDLIRREIDIMNQLHHQKLINLHDAFEDDDEMILILEF 8065
Cdd:smart00219    3 LGKKLGEGAFGEVYKGKLKGKGGKKkvevAVKTLKEDASeQQIEEFLREARIMRKLDHPNVVKLLGVCTEEEPLYIVMEY 82
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561   8066 LSGGELFERITAEGYVMTEAEVINYMRQICEGIRHMHEQNIIHLDIKPENIMCQTRssTNVKLIDFGLATRLDPNEVVKI 8145
Cdd:smart00219   83 MEGGDLLSYLRKNRPKLSLSDLLSFALQIARGMEYLESKNFIHRDLAARNCLVGEN--LVVKISDFGLSRDLYDDDYYRK 160
                           170       180       190       200       210       220
                    ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 281359561   8146 TTGTAEFA--APEIVNRepvGFYT---DMWATGVLSYVLLS-GLSPFAGDNDVQTLKNVKA 8200
Cdd:smart00219  161 RGGKLPIRwmAPESLKE---GKFTsksDVWSFGVLLWEIFTlGEQPYPGMSNEEVLEYLKN 218
STKc_SLK cd06643
Catalytic domain of the Serine/Threonine Kinase, Ste20-Like Kinase; STKs catalyze the transfer ...
7987-8245 1.13e-28

Catalytic domain of the Serine/Threonine Kinase, Ste20-Like Kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. SLK promotes apoptosis through apoptosis signal-regulating kinase 1 (ASK1) and the mitogen-activated protein kinase (MAPK) p38. It acts as a MAPK kinase kinase by phosphorylating ASK1, resulting in the phosphorylation of p38. SLK also plays a role in mediating actin reorganization. It is part of a microtubule-associated complex that is targeted at adhesion sites, and is required in focal adhesion turnover and in regulating cell migration. The SLK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270811 [Multi-domain]  Cd Length: 283  Bit Score: 119.75  E-value: 1.13e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 7987 DRYDILEEIGTGAFGVVHRCRERSTGNIFAAKFIPVSHSVEKDLIRREIDIMNQLHHQKLINLHDAFEDDDEMILILEFL 8066
Cdd:cd06643     5 DFWEIVGELGDGAFGKVYKAQNKETGILAAAKVIDTKSEEELEDYMVEIDILASCDHPNIVKLLDAFYYENNLWILIEFC 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 8067 SGGELFERITAEGYVMTEAEVINYMRQICEGIRHMHEQNIIHLDIKPENIMCQtrSSTNVKLIDFGLATRlDPNEVVKIT 8146
Cdd:cd06643    85 AGGAVDAVMLELERPLTEPQIRVVCKQTLEALVYLHENKIIHRDLKAGNILFT--LDGDIKLADFGVSAK-NTRTLQRRD 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 8147 T--GTAEFAAPEIVNRE-----PVGFYTDMWATGVLSYVLLSGLSPFAGDNDVQTLKNVKACDWDFDVESFKYiSEEAKD 8219
Cdd:cd06643   162 SfiGTPYWMAPEVVMCEtskdrPYDYKADVWSLGVTLIEMAQIEPPHHELNPMRVLLKIAKSEPPTLAQPSRW-SPEFKD 240
                         250       260
                  ....*....|....*....|....*.
gi 281359561 8220 FIRKLLVRNKEKRMTAHECLLHPWLT 8245
Cdd:cd06643   241 FLRKCLEKNVDARWTTSQLLQHPFVS 266
STKc_CAMKK cd14118
Catalytic domain of the Serine/Threonine kinase, Calmodulin Dependent Protein Kinase Kinase; ...
7994-8245 1.22e-28

Catalytic domain of the Serine/Threonine kinase, Calmodulin Dependent Protein Kinase Kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. CaMKKs are upstream kinases of the CaM kinase cascade that phosphorylate and activate CaMKI and CamKIV. They may also phosphorylate other substrates including PKB and AMP-activated protein kinase (AMPK). Vertebrates contain two CaMKKs, CaMKK1 (or alpha) and CaMKK2 (or beta). CaMKK1 is involved in the regulation of glucose uptake in skeletal muscles. CaMKK2 is involved in regulating energy balance, glucose metabolism, adiposity, hematopoiesis, inflammation, and cancer. The CaMKK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271020 [Multi-domain]  Cd Length: 275  Bit Score: 119.39  E-value: 1.22e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 7994 EIGTGAFGVVHRCRERSTGNIFAAKFI--------------PVSHSVEK---------DLIRREIDIMNQLHHQKLINLH 8050
Cdd:cd14118     1 EIGKGSYGIVKLAYNEEDNTLYAMKILskkkllkqagffrrPPPRRKPGalgkpldplDRVYREIAILKKLDHPNVVKLV 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 8051 DAFED--DDEMILILEFLSGGELFERITAEgyVMTEAEVINYMRQICEGIRHMHEQNIIHLDIKPENIMCQtrSSTNVKL 8128
Cdd:cd14118    81 EVLDDpnEDNLYMVFELVDKGAVMEVPTDN--PLSEETARSYFRDIVLGIEYLHYQKIIHRDIKPSNLLLG--DDGHVKI 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 8129 IDFGLATRLDPNEVVKITT-GTAEFAAPEIVNREPVGFY---TDMWATGVLSYVLLSGLSPFAGDNDVQTLKNVKACDWD 8204
Cdd:cd14118   157 ADFGVSNEFEGDDALLSSTaGTPAFMAPEALSESRKKFSgkaLDIWAMGVTLYCFVFGRCPFEDDHILGLHEKIKTDPVV 236
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|.
gi 281359561 8205 FDvESFkYISEEAKDFIRKLLVRNKEKRMTAHECLLHPWLT 8245
Cdd:cd14118   237 FP-DDP-VVSEQLKDLILRMLDKNPSERITLPEIKEHPWVT 275
STKc_PLK1 cd14187
Catalytic domain of the Serine/Threonine Kinase, Polo-like kinase 1; STKs catalyze the ...
7995-8245 1.33e-28

Catalytic domain of the Serine/Threonine Kinase, Polo-like kinase 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PLKs play important roles in cell cycle progression and in DNA damage responses. They regulate mitotic entry, mitotic exit, and cytokinesis. In general PLKs contain an N-terminal catalytic kinase domain and a C-terminal regulatory polo box domain (PBD), which is comprised by two bipartite polo-box motifs (or polo boxes) and is involved in protein interactions. There are five mammalian PLKs (PLK1-5) from distinct genes. PLK1 functions as a positive regulator of mitosis, meiosis, and cytokinesis. Its localization changes during mitotic progression; associating first with centrosomes in prophase, with kinetochores in prometaphase and metaphase, at the central spindle in anaphase, and in the midbody during telophase. It carries multiple functions throughout the cell cycle through interactions with differrent substrates at these specific subcellular locations. PLK1 is overexpressed in many human cancers and is associated with poor prognosis. The PLK1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271089 [Multi-domain]  Cd Length: 265  Bit Score: 118.88  E-value: 1.33e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 7995 IGTGAFGVVHRCRERSTGNIFAAKFIPVSHSV---EKDLIRREIDIMNQLHHQKLINLHDAFEDDDEMILILEFLSGGEL 8071
Cdd:cd14187    15 LGKGGFAKCYEITDADTKEVFAGKIVPKSLLLkphQKEKMSMEIAIHRSLAHQHVVGFHGFFEDNDFVYVVLELCRRRSL 94
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 8072 FErITAEGYVMTEAEVINYMRQICEGIRHMHEQNIIHLDIKPENIMCQtrSSTNVKLIDFGLATRLDPN-EVVKITTGTA 8150
Cdd:cd14187    95 LE-LHKRRKALTEPEARYYLRQIILGCQYLHRNRVIHRDLKLGNLFLN--DDMEVKIGDFGLATKVEYDgERKKTLCGTP 171
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 8151 EFAAPEIVNREPVGFYTDMWATGVLSYVLLSGLSPFAGDNDVQTLKNVKACDWDFDvesfKYISEEAKDFIRKLLVRNKE 8230
Cdd:cd14187   172 NYIAPEVLSKKGHSFEVDIWSIGCIMYTLLVGKPPFETSCLKETYLRIKKNEYSIP----KHINPVAASLIQKMLQTDPT 247
                         250
                  ....*....|....*
gi 281359561 8231 KRMTAHECLLHPWLT 8245
Cdd:cd14187   248 ARPTINELLNDEFFT 262
FN3 COG3401
Fibronectin type 3 domain [General function prediction only];
6236-6552 1.54e-28

Fibronectin type 3 domain [General function prediction only];


Pssm-ID: 442628 [Multi-domain]  Cd Length: 603  Bit Score: 125.89  E-value: 1.54e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 6236 YTVTAANEFGKDTADIEVIVVDKPSPPEGP--LSYTETAPDHISLHWYSPKDdggSDITGYIIEFTEFGVDDWKPVpGTC 6313
Cdd:COG3401   207 YRVAATDTGGESAPSNEVSVTTPTTPPSAPtgLTATADTPGSVTLSWDPVTE---SDATGYRVYRSNSGDGPFTKV-ATV 282
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 6314 PNTNFTVKNLVEGKKYVFRIRAENIYG----ASEALEGKPVLAkspfdPPGAPSQPTISAYTPNSANLEWHPPDDcggKP 6389
Cdd:COG3401   283 TTTSYTDTGLTNGTTYYYRVTAVDAAGnesaPSNVVSVTTDLT-----PPAAPSGLTATAVGSSSITLSWTASSD---AD 354
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 6390 ITGYIVERRER-GGEWIKCNNYPTpNTSYTVSNLRDGARYEFRVLAVNEAGPGhpSKPSDPMTAEHQRYRPDPPEPPKPD 6468
Cdd:COG3401   355 VTGYNVYRSTSgGGTYTKIAETVT-TTSYTDTGLTPGTTYYYKVTAVDAAGNE--SAPSEEVSATTASAASGESLTASVD 431
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 6469 RITRNGV------TLSWRPPRTDGKSRIKGYYVEMRPKNGKDWKTVNDiPINSTVYTVPSLKEGEEYSFRVVAENEVGRS 6542
Cdd:COG3401   432 AVPLTDVagataaASAASNPGVSAAVLADGGDTGNAVPFTTTSSTVTA-TTTDTTTANLSVTTGSLVGGSGASSVTNSVS 510
                         330
                  ....*....|
gi 281359561 6543 DPSKPSQPIT 6552
Cdd:COG3401   511 VIGASAAAAV 520
STKc_CaMKK1 cd14200
Catalytic domain of the Serine/Threonine kinase, Calmodulin Dependent Protein Kinase Kinase 1; ...
7988-8245 1.59e-28

Catalytic domain of the Serine/Threonine kinase, Calmodulin Dependent Protein Kinase Kinase 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. CaMKKs are upstream kinases of the CaM kinase cascade that phosphorylate and activate CaMKI and CamKIV. They may also phosphorylate other substrates including PKB and AMP-activated protein kinase (AMPK). CaMKK1, also called CaMKK alpha, is involved in the regulation of glucose uptake in skeletal muscles, independently of AMPK and PKB activation. It also play roles in learning and memory. Studies on CaMKK1 knockout mice reveal deficits in fear conditioning. The CaMKK1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271102 [Multi-domain]  Cd Length: 284  Bit Score: 119.28  E-value: 1.59e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 7988 RYDILEEIGTGAFGVVHRCRERSTGNIFAAKFIPVSHSVEK--------------------------DLIRREIDIMNQL 8041
Cdd:cd14200     1 QYKLQSEIGKGSYGVVKLAYNESDDKYYAMKVLSKKKLLKQygfprrppprgskaaqgeqakplaplERVYQEIAILKKL 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 8042 HHQKLINLHDAFED--DDEMILILEFLSGGELFERITAEGYVMTEAEVinYMRQICEGIRHMHEQNIIHLDIKPENIMCQ 8119
Cdd:cd14200    81 DHVNIVKLIEVLDDpaEDNLYMVFDLLRKGPVMEVPSDKPFSEDQARL--YFRDIVLGIEYLHYQKIVHRDIKPSNLLLG 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 8120 trSSTNVKLIDFGLATRLDPNEV-VKITTGTAEFAAPEIVNREPVGFY---TDMWATGVLSYVLLSGLSPFAgDNDVQTL 8195
Cdd:cd14200   159 --DDGHVKIADFGVSNQFEGNDAlLSSTAGTPAFMAPETLSDSGQSFSgkaLDVWAMGVTLYCFVYGKCPFI-DEFILAL 235
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|.
gi 281359561 8196 KN-VKACDWDFDVESfkYISEEAKDFIRKLLVRNKEKRMTAHECLLHPWLT 8245
Cdd:cd14200   236 HNkIKNKPVEFPEEP--EISEELKDLILKMLDKNPETRITVPEIKVHPWVT 284
STKc_ULK1 cd14202
Catalytic domain of the Serine/Threonine kinase, Unc-51-like kinase 1; STKs catalyze the ...
7986-8244 1.93e-28

Catalytic domain of the Serine/Threonine kinase, Unc-51-like kinase 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The ATG1/ULK complex is conserved from yeast to humans and it plays a critical role in the initiation of autophagy, the intracellular system that leads to the lysosomal degradation of cellular components and their recycling into basic metabolic units. ULK1 is required for efficient amino acid starvation-induced autophagy and mitochondrial clearance. It associates with three autophagy-related proteins (Atg13, FIP200 amd Atg101) to form the ULK1 complex. All fours proteins are essential for autophagosome formation. ULK1 is regulated by both mammalian target-of rapamycin complex 1 (mTORC1) and AMP-activated protein kinase (AMPK). mTORC1 negatively regulates the ULK1 complex in a nutrient-dependent manner while AMPK stimulates autophagy by inhibiting mTORC1. ULK1 also plays neuron-specific roles and is involved in non-clathrin-coated endocytosis in growth cones, filopodia extension, neurite extension, and axon branching. The ULK1 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271104 [Multi-domain]  Cd Length: 267  Bit Score: 118.57  E-value: 1.93e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 7986 YDRYDIleeIGTGAFGVVHRCRERSTGNI-FAAKFIPVSH-SVEKDLIRREIDIMNQLHHQKLINLHDAFEDDDEMILIL 8063
Cdd:cd14202     4 FSRKDL---IGHGAFAVVFKGRHKEKHDLeVAVKCINKKNlAKSQTLLGKEIKILKELKHENIVALYDFQEIANSVYLVM 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 8064 EFLSGGELFERITAEGyVMTEAEVINYMRQICEGIRHMHEQNIIHLDIKPENIM--CQTRSSTN-----VKLIDFGLATR 8136
Cdd:cd14202    81 EYCNGGDLADYLHTMR-TLSEDTIRLFLQQIAGAMKMLHSKGIIHRDLKPQNILlsYSGGRKSNpnnirIKIADFGFARY 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 8137 LDPNEVVKITTGTAEFAAPEIVNREPVGFYTDMWATGVLSYVLLSGLSPFAGDNDvQTLKNVKACDWDFDVESFKYISEE 8216
Cdd:cd14202   160 LQNNMMAATLCGSPMYMAPEVIMSQHYDAKADLWSIGTIIYQCLTGKAPFQASSP-QDLRLFYEKNKSLSPNIPRETSSH 238
                         250       260
                  ....*....|....*....|....*...
gi 281359561 8217 AKDFIRKLLVRNKEKRMTAHECLLHPWL 8244
Cdd:cd14202   239 LRQLLLGLLQRNQKDRMDFDEFFHHPFL 266
STKc_MAPK15-like cd07852
Catalytic domain of the Serine/Threonine Kinase, Mitogen-Activated Protein Kinase 15 and ...
7985-8267 1.97e-28

Catalytic domain of the Serine/Threonine Kinase, Mitogen-Activated Protein Kinase 15 and similar MAPKs; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Human MAPK15 is also called Extracellular signal Regulated Kinase 8 (ERK8) while the rat protein is called ERK7. ERK7 and ERK8 display both similar and different biochemical properties. They autophosphorylate and activate themselves and do not require upstream activating kinases. ERK7 is constitutively active and is not affected by extracellular stimuli whereas ERK8 shows low basal activity and is activated by DNA-damaging agents. ERK7 and ERK8 also have different substrate profiles. Genome analysis shows that they are orthologs with similar gene structures. ERK7 and ERK 8 may be involved in the signaling of some nuclear receptor transcription factors. ERK7 regulates hormone-dependent degradation of estrogen receptor alpha while ERK8 down-regulates the transcriptional co-activation androgen and glucocorticoid receptors. MAPKs are important mediators of cellular responses to extracellular signals. The MAPK15 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270841 [Multi-domain]  Cd Length: 337  Bit Score: 120.74  E-value: 1.97e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 7985 VYDRYDILEEIGTGAFGVVHRCRERSTGNIFAAKFIPVSHSVEKDLIR--REIDIMNQL-HHQKLINLHDAF--EDDDEM 8059
Cdd:cd07852     5 ILRRYEILKKLGKGAYGIVWKAIDKKTGEVVALKKIFDAFRNATDAQRtfREIMFLQELnDHPNIIKLLNVIraENDKDI 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 8060 ILILEFLSgGELFERITAEgyVMTEAEVINYMRQICEGIRHMHEQNIIHLDIKPENIMCQtrSSTNVKLIDFGLA---TR 8136
Cdd:cd07852    85 YLVFEYME-TDLHAVIRAN--ILEDIHKQYIMYQLLKALKYLHSGGVIHRDLKPSNILLN--SDCRVKLADFGLArslSQ 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 8137 LDPNEVVKITT---GTAEFAAPEIVnrepVG--FYT---DMWATGVLSYVLLSGLSPFAGDN------------------ 8190
Cdd:cd07852   160 LEEDDENPVLTdyvATRWYRAPEIL----LGstRYTkgvDMWSVGCILGEMLLGKPLFPGTStlnqlekiievigrpsae 235
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 8191 DVQT---------LKNVKACDWDFDVESFKYISEEAKDFIRKLLVRNKEKRMTAHECLLHPWLTGDHSAmKQEINRDRYL 8261
Cdd:cd07852   236 DIESiqspfaatmLESLPPSRPKSLDELFPKASPDALDLLKKLLVFNPNKRLTAEEALRHPYVAQFHNP-ADEPSLPGPI 314
                         330
                  ....*....|....*....
gi 281359561 8262 -------------AYREKL 8267
Cdd:cd07852   315 viplddnkkltvdEYRNRL 333
STKc_CDKL1_4 cd07847
Catalytic domain of the Serine/Threonine Kinases, Cyclin-Dependent protein Kinase Like 1 and 4; ...
7987-8243 6.48e-28

Catalytic domain of the Serine/Threonine Kinases, Cyclin-Dependent protein Kinase Like 1 and 4; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. CDKL1, also called p42 KKIALRE, is a glial protein that is upregulated in gliosis. It is present in neuroblastoma and A431 human carcinoma cells, and may be implicated in neoplastic transformation. The function of CDKL4 is unknown. CDKs belong to a large family of STKs that are regulated by their cognate cyclins. Together, they are involved in the control of cell-cycle progression, transcription, and neuronal function. The CDKL1/4 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270837 [Multi-domain]  Cd Length: 286  Bit Score: 117.47  E-value: 6.48e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 7987 DRYDILEEIGTGAFGVVHRCRERSTGNIFAAK-FIpvsHSVEKDLIR----REIDIMNQLHHQKLINLHDAFEDDDEMIL 8061
Cdd:cd07847     1 EKYEKLSKIGEGSYGVVFKCRNRETGQIVAIKkFV---ESEDDPVIKkialREIRMLKQLKHPNLVNLIEVFRRKRKLHL 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 8062 ILEFLSGGELFErITAEGYVMTEAEVINYMRQICEGIRHMHEQNIIHLDIKPENIMCqTRSSTnVKLIDFGLATRLDPNE 8141
Cdd:cd07847    78 VFEYCDHTVLNE-LEKNPRGVPEHLIKKIIWQTLQAVNFCHKHNCIHRDVKPENILI-TKQGQ-IKLCDFGFARILTGPG 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 8142 VVKIT-TGTAEFAAPE-IVNREPVGFYTDMWATGVLSYVLLSGLSPFAGDNDVQTLKNVKACDWDF-------------- 8205
Cdd:cd07847   155 DDYTDyVATRWYRAPElLVGDTQYGPPVDVWAIGCVFAELLTGQPLWPGKSDVDQLYLIRKTLGDLiprhqqifstnqff 234
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|.
gi 281359561 8206 ------------DVES-FKYISEEAKDFIRKLLVRNKEKRMTAHECLLHPW 8243
Cdd:cd07847   235 kglsipepetrePLESkFPNISSPALSFLKGCLQMDPTERLSCEELLEHPY 285
STYKc smart00221
Protein kinase; unclassified specificity; Phosphotransferases. The specificity of this class ...
7991-8200 6.53e-28

Protein kinase; unclassified specificity; Phosphotransferases. The specificity of this class of kinases can not be predicted. Possible dual-specificity Ser/Thr/Tyr kinase.


Pssm-ID: 214568 [Multi-domain]  Cd Length: 258  Bit Score: 116.88  E-value: 6.53e-28
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561   7991 ILEEIGTGAFGVVHRCRERSTGNIF----AAKFIPVSHS-VEKDLIRREIDIMNQLHHQKLINLHDAFEDDDEMILILEF 8065
Cdd:smart00221    3 LGKKLGEGAFGEVYKGTLKGKGDGKevevAVKTLKEDASeQQIEEFLREARIMRKLDHPNIVKLLGVCTEEEPLMIVMEY 82
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561   8066 LSGGELFERI-TAEGYVMTEAEVINYMRQICEGIRHMHEQNIIHLDIKPENIMCQTRssTNVKLIDFGLATRLDPNEVVK 8144
Cdd:smart00221   83 MPGGDLLDYLrKNRPKELSLSDLLSFALQIARGMEYLESKNFIHRDLAARNCLVGEN--LVVKISDFGLSRDLYDDDYYK 160
                           170       180       190       200       210       220
                    ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 281359561   8145 ITTGTAEFA--APEIVNRepvGFYT---DMWATGVLSYVLLS-GLSPFAGDNDVQTLKNVKA 8200
Cdd:smart00221  161 VKGGKLPIRwmAPESLKE---GKFTsksDVWSFGVLLWEIFTlGEEPYPGMSNAEVLEYLKK 219
STKc_PAK5 cd06658
Catalytic domain of the Serine/Threonine Kinase, p21-activated kinase 5; STKs catalyze the ...
7994-8244 6.97e-28

Catalytic domain of the Serine/Threonine Kinase, p21-activated kinase 5; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PAK5 is mainly expressed in the brain. It is not required for viability, but together with PAK6, it is required for normal levels of locomotion and activity, and for learning and memory. PAK5 cooperates with Inca (induced in neural crest by AP2) in the regulation of cell adhesion and cytoskeletal organization in the embryo and in neural crest cells during craniofacial development. PAK5 may also play a role in controlling the signaling of Raf-1, an effector of Ras, at the mitochondria. PAK5 belongs to the group II PAKs, which contain a PBD (p21-binding domain) and a C-terminal catalytic domain, but do not harbor an AID (autoinhibitory domain) or SH3 binding sites. PAKs are Rho family GTPase-regulated kinases that serve as important mediators in the function of Cdc42 (cell division cycle 42) and Rac. The PAK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 132989 [Multi-domain]  Cd Length: 292  Bit Score: 117.83  E-value: 6.97e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 7994 EIGTGAFGVVHRCRERSTGNIFAAKFIPVSHSVEKDLIRREIDIMNQLHHQKLINLHDAFEDDDEMILILEFLSGGELFE 8073
Cdd:cd06658    29 KIGEGSTGIVCIATEKHTGKQVAVKKMDLRKQQRRELLFNEVVIMRDYHHENVVDMYNSYLVGDELWVVMEFLEGGALTD 108
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 8074 RITAEGyvMTEAEVINYMRQICEGIRHMHEQNIIHLDIKPENIMCQtrSSTNVKLIDFGLATRLDpNEVV--KITTGTAE 8151
Cdd:cd06658   109 IVTHTR--MNEEQIATVCLSVLRALSYLHNQGVIHRDIKSDSILLT--SDGRIKLSDFGFCAQVS-KEVPkrKSLVGTPY 183
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 8152 FAAPEIVNREPVGFYTDMWATGVLSYVLLSGLSPFAGDNDVQTLKNVKAcDWDFDVESFKYISEEAKDFIRKLLVRNKEK 8231
Cdd:cd06658   184 WMAPEVISRLPYGTEVDIWSLGIMVIEMIDGEPPYFNEPPLQAMRRIRD-NLPPRVKDSHKVSSVLRGFLDLMLVREPSQ 262
                         250
                  ....*....|...
gi 281359561 8232 RMTAHECLLHPWL 8244
Cdd:cd06658   263 RATAQELLQHPFL 275
STKc_MEKK3 cd06651
Catalytic domain of the Serine/Threonine Kinase, Mitogen-Activated Protein (MAP)/Extracellular ...
7995-8243 7.27e-28

Catalytic domain of the Serine/Threonine Kinase, Mitogen-Activated Protein (MAP)/Extracellular signal-Regulated Kinase (ERK) Kinase Kinase 3; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MEKK3 is a MAPK kinase kinase (MAPKKK or MKKK), that phosphorylates and activates the MAPK kinase MEK5 (or MKK5), which in turn phosphorylates and activates ERK5. The ERK5 cascade plays roles in promoting cell proliferation, differentiation, neuronal survival, and neuroprotection. MEKK3 plays an essential role in embryonic angiogenesis and early heart development. In addition, MEKK3 is involved in interleukin-1 receptor and Toll-like receptor 4 signaling. It is also a specific regulator of the proinflammatory cytokines IL-6 and GM-CSF in some immune cells. MEKK3 also regulates calcineurin, which plays a critical role in T cell activation, apoptosis, skeletal myocyte differentiation, and cardiac hypertrophy. The MEKK3 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270817 [Multi-domain]  Cd Length: 271  Bit Score: 117.11  E-value: 7.27e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 7995 IGTGAFGVVHRCRERSTGNIFAAK---FIPVSHSVEKDL--IRREIDIMNQLHHQKLINLHDAFEDDDE--MILILEFLS 8067
Cdd:cd06651    15 LGQGAFGRVYLCYDVDTGRELAAKqvqFDPESPETSKEVsaLECEIQLLKNLQHERIVQYYGCLRDRAEktLTIFMEYMP 94
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 8068 GGELFERITAEGyVMTEAEVINYMRQICEGIRHMHEQNIIHLDIKPENIMcqTRSSTNVKLIDFGLATRLD----PNEVV 8143
Cdd:cd06651    95 GGSVKDQLKAYG-ALTESVTRKYTRQILEGMSYLHSNMIVHRDIKGANIL--RDSAGNVKLGDFGASKRLQticmSGTGI 171
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 8144 KITTGTAEFAAPEIVNREPVGFYTDMWATGVLSYVLLSGLSPFAGDNDVQTLKNVKACDWDFDVESfkYISEEAKDFIRK 8223
Cdd:cd06651   172 RSVTGTPYWMSPEVISGEGYGRKADVWSLGCTVVEMLTEKPPWAEYEAMAAIFKIATQPTNPQLPS--HISEHARDFLGC 249
                         250       260
                  ....*....|....*....|
gi 281359561 8224 LLVRNKEkRMTAHECLLHPW 8243
Cdd:cd06651   250 IFVEARH-RPSAEELLRHPF 268
PKc_CLK cd14134
Catalytic domain of the Dual-specificity protein kinases, CDC-like kinases; Dual-specificity ...
7987-8244 8.13e-28

Catalytic domain of the Dual-specificity protein kinases, CDC-like kinases; Dual-specificity PKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine (S/T) as well as tyrosine residues on protein substrates. CLKs are involved in the phosphorylation and regulation of serine/arginine-rich (SR) proteins, which play a crucial role in pre-mRNA splicing by directing splice site selection. SR proteins are phosphorylated first by SR protein kinases (SRPKs) at the N-terminus, which leads to its assembly into nuclear speckles where splicing factors are stored. CLKs phosphorylate the C-terminal part of SR proteins, causing the nuclear speckles to dissolve and splicing factors to be recruited at sites of active transcription. Based on a conserved "EHLAMMERILG" signature motif which may be crucial for substrate specificity, CLKs are also referred to as LAMMER kinases. CLKs autophosphorylate at tyrosine residues and phosphorylate their substrates exclusively on S/T residues. In Drosophila, the CLK homolog DOA (Darkener of apricot) is essential for embryogenesis and its mutation leads to defects in sexual differentiation, eye formation, and neuronal development. In fission yeast, the CLK homolog Lkh1 is a negative regulator of filamentous growth and asexual flocculation, and is also involved in oxidative stress response. Vertebrates contain mutliple CLK proteins and mammals have four (CLK1-4). The CLK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271036 [Multi-domain]  Cd Length: 332  Bit Score: 118.82  E-value: 8.13e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 7987 DRYDILEEIGTGAFGVVHRCRERSTGNIFAAKFIpvsHSVEK--DLIRREIDIMNQLHHQ------KLINLHDAFEDDDE 8058
Cdd:cd14134    12 NRYKILRLLGEGTFGKVLECWDRKRKRYVAVKII---RNVEKyrEAAKIEIDVLETLAEKdpngksHCVQLRDWFDYRGH 88
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 8059 MILILEFLsGGELFERITAEGY-VMTEAEVINYMRQICEGIRHMHEQNIIHLDIKPENIM---------------CQTRS 8122
Cdd:cd14134    89 MCIVFELL-GPSLYDFLKKNNYgPFPLEHVQHIAKQLLEAVAFLHDLKLTHTDLKPENILlvdsdyvkvynpkkkRQIRV 167
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 8123 --STNVKLIDFGLAT--RLDPNEVVKittgTAEFAAPEIVNREPVGFYTDMWATGVLSYVLLSGLSPFAGDNDVQTL--- 8195
Cdd:cd14134   168 pkSTDIKLIDFGSATfdDEYHSSIVS----TRHYRAPEVILGLGWSYPCDVWSIGCILVELYTGELLFQTHDNLEHLamm 243
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 8196 ------------KNVKAC-----------DWDFDVESFKYISEEAK-----------------DFIRKLLVRNKEKRMTA 8235
Cdd:cd14134   244 erilgplpkrmiRRAKKGakyfyfyhgrlDWPEGSSSGRSIKRVCKplkrlmllvdpehrllfDLIRKMLEYDPSKRITA 323

                  ....*....
gi 281359561 8236 HECLLHPWL 8244
Cdd:cd14134   324 KEALKHPFF 332
PLN00034 PLN00034
mitogen-activated protein kinase kinase; Provisional
7980-8262 8.57e-28

mitogen-activated protein kinase kinase; Provisional


Pssm-ID: 215036 [Multi-domain]  Cd Length: 353  Bit Score: 119.16  E-value: 8.57e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 7980 ISQQSVYDRYDILEEIGTGAFGVVHRCRERSTGNIFAAKFIPVSH--SVEKDlIRREIDIMNQLHHQKLINLHDAFEDDD 8057
Cdd:PLN00034   67 PSAAKSLSELERVNRIGSGAGGTVYKVIHRPTGRLYALKVIYGNHedTVRRQ-ICREIEILRDVNHPNVVKCHDMFDHNG 145
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 8058 EMILILEFLSGGELferitaEG-YVMTEAEVINYMRQICEGIRHMHEQNIIHLDIKPENIMCQtrSSTNVKLIDFG---- 8132
Cdd:PLN00034  146 EIQVLLEFMDGGSL------EGtHIADEQFLADVARQILSGIAYLHRRHIVHRDIKPSNLLIN--SAKNVKIADFGvsri 217
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 8133 LATRLDP-NEVVkittGTAEFAAPEIVNREPV-----GFYTDMWATGV--LSYVLlsGLSPFAGDndvqtlknvKACDWD 8204
Cdd:PLN00034  218 LAQTMDPcNSSV----GTIAYMSPERINTDLNhgaydGYAGDIWSLGVsiLEFYL--GRFPFGVG---------RQGDWA 282
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 281359561 8205 FDV---------ESFKYISEEAKDFIRKLLVRNKEKRMTAHECLLHPWLTGDHSAMKQEINRDRYLA 8262
Cdd:PLN00034  283 SLMcaicmsqppEAPATASREFRHFISCCLQREPAKRWSAMQLLQHPFILRAQPGQGQGGPNLHQLL 349
STKc_SGK1 cd05602
Catalytic domain of the Protein Serine/Threonine Kinase, Serum- and Glucocorticoid-induced ...
7989-8235 8.89e-28

Catalytic domain of the Protein Serine/Threonine Kinase, Serum- and Glucocorticoid-induced Kinase 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. SGK1 is ubiquitously expressed and is under transcriptional control of numerous stimuli including cell stress (cell shrinkage), serum, hormones (gluco- and mineralocorticoids), gonadotropins, growth factors, interleukin-6, and other cytokines. It plays roles in sodium retention and potassium elimination in the kidney, nutrient transport, salt sensitivity, memory consolidation, and cardiac repolarization. A common SGK1 variant is associated with increased blood pressure and body weight. SGK1 may also contribute to tumor growth, neurodegeneration, fibrosing disease, and ischemia. The SGK1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270753 [Multi-domain]  Cd Length: 339  Bit Score: 118.97  E-value: 8.89e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 7989 YDILEEIGTGAFGVVHRCRERSTGNIFAAKFIP----VSHSVEKDLIRREIDIMNQLHHQKLINLHDAFEDDDEMILILE 8064
Cdd:cd05602     9 FHFLKVIGKGSFGKVLLARHKSDEKFYAVKVLQkkaiLKKKEEKHIMSERNVLLKNVKHPFLVGLHFSFQTTDKLYFVLD 88
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 8065 FLSGGELFERITAEGYVMtEAEVINYMRQICEGIRHMHEQNIIHLDIKPENIMCQtrSSTNVKLIDFGLATR-LDPNEVV 8143
Cdd:cd05602    89 YINGGELFYHLQRERCFL-EPRARFYAAEIASALGYLHSLNIVYRDLKPENILLD--SQGHIVLTDFGLCKEnIEPNGTT 165
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 8144 KITTGTAEFAAPEIVNREPVGFYTDMWATGVLSYVLLSGLSPFAGDNDVQTLKNVkacdWDFDVESFKYISEEAKDFIRK 8223
Cdd:cd05602   166 STFCGTPEYLAPEVLHKQPYDRTVDWWCLGAVLYEMLYGLPPFYSRNTAEMYDNI----LNKPLQLKPNITNSARHLLEG 241
                         250
                  ....*....|..
gi 281359561 8224 LLVRNKEKRMTA 8235
Cdd:cd05602   242 LLQKDRTKRLGA 253
STKc_CDK4_6_like cd07838
Catalytic domain of Cyclin-Dependent protein Kinase 4 and 6-like Serine/Threonine Kinases; ...
7989-8244 9.35e-28

Catalytic domain of Cyclin-Dependent protein Kinase 4 and 6-like Serine/Threonine Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. CDK4 and CDK6 partner with D-type cyclins to regulate the early G1 phase of the cell cycle. They are the first kinases activated by mitogenic signals to release cells from the G0 arrested state. CDK4 and CDK6 are both expressed ubiquitously, associate with all three D cyclins (D1, D2 and D3), and phosphorylate the retinoblastoma (pRb) protein. They are also regulated by the INK4 family of inhibitors which associate with either the CDK alone or the CDK/cyclin complex. CDK4 and CDK6 show differences in subcellular localization, sensitivity to some inhibitors, timing in activation, tumor selectivity, and possibly substrate profiles. Although CDK4 and CDK6 seem to show some redundancy, they also have discrete, nonoverlapping functions. CDK6 plays an important role in cell differentiation. CDKs belong to a large family of STKs that are regulated by their cognate cyclins. Together, they are involved in the control of cell-cycle progression, transcription, and neuronal function. The CDK4/6-like subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270831 [Multi-domain]  Cd Length: 287  Bit Score: 117.38  E-value: 9.35e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 7989 YDILEEIGTGAFGVVHRCRERSTGNIFAAKFIPVSHSvEKDL---IRREIDIMNQL---HHQKLINLHDAF---EDDDEM 8059
Cdd:cd07838     1 YEEVAEIGEGAYGTVYKARDLQDGRFVALKKVRVPLS-EEGIplsTIREIALLKQLesfEHPNVVRLLDVChgpRTDREL 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 8060 ILILEF------LSGgeLFERITAEGyvMTEAEVINYMRQICEGIRHMHEQNIIHLDIKPENIMCqTRSSTnVKLIDFGL 8133
Cdd:cd07838    80 KLTLVFehvdqdLAT--YLDKCPKPG--LPPETIKDLMRQLLRGLDFLHSHRIVHRDLKPQNILV-TSDGQ-VKLADFGL 153
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 8134 ATRLDPNevVKITT--GTAEFAAPEIVNREPVGFYTDMWATGVLSYVLLSgLSP-FAGDNDVQTLKNV-------KACDW 8203
Cdd:cd07838   154 ARIYSFE--MALTSvvVTLWYRAPEVLLQSSYATPVDMWSVGCIFAELFN-RRPlFRGSSEADQLGKIfdviglpSEEEW 230
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 281359561 8204 DFDV----ESF------------KYISEEAKDFIRKLLVRNKEKRMTAHECLLHPWL 8244
Cdd:cd07838   231 PRNSalprSSFpsytprpfksfvPEIDEEGLDLLKKMLTFNPHKRISAFEALQHPYF 287
PKc_Pek1_like cd06621
Catalytic domain of fungal Pek1-like dual-specificity Mitogen-Activated Protein Kinase Kinases; ...
7992-8262 9.92e-28

Catalytic domain of fungal Pek1-like dual-specificity Mitogen-Activated Protein Kinase Kinases; PKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine (ST) or tyrosine residues on protein substrates. Members of this group include the MAPKKs Pek1/Skh1 from Schizosaccharomyces pombe and MKK2 from Saccharomyces cerevisiae, and related proteins. Both fission yeast Pek1 and baker's yeast MKK2 are components of the cell integrity MAPK pathway. In fission yeast, Pek1 phosphorylates and activates Pmk1/Spm1 and is regulated by the MAPKK kinase Mkh1. In baker's yeast, the pathway involves the MAPK Slt2, the MAPKKs MKK1 and MKK2, and the MAPKK kinase Bck1. The cell integrity MAPK cascade is activated by multiple stress conditions, and is essential in cell wall construction, morphogenesis, cytokinesis, and ion homeostasis. MAPK signaling pathways are important mediators of cellular responses to extracellular signals. The MAPKK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270793 [Multi-domain]  Cd Length: 287  Bit Score: 117.14  E-value: 9.92e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 7992 LEEIGTGAFGVVHRCRERSTGNIFAAKFIPVSHSVE-KDLIRREIDIMNQLHHQKLINLHDAFEDD-DEMILI-LEFLSG 8068
Cdd:cd06621     6 LSSLGEGAGGSVTKCRLRNTKTIFALKTITTDPNPDvQKQILRELEINKSCASPYIVKYYGAFLDEqDSSIGIaMEYCEG 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 8069 GEL---FERITAEGYVMTEAEVINYMRQICEGIRHMHEQNIIHLDIKPENIMCQTRSstNVKLIDFGLATRLdPNEVVKI 8145
Cdd:cd06621    86 GSLdsiYKKVKKKGGRIGEKVLGKIAESVLKGLSYLHSRKIIHRDIKPSNILLTRKG--QVKLCDFGVSGEL-VNSLAGT 162
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 8146 TTGTAEFAAPEIVNREPVGFYTDMWATGVLSYVLLSGLSPFAGD-----------NDVQTLKNVKACDwdfDVESFKYIS 8214
Cdd:cd06621   163 FTGTSYYMAPERIQGGPYSITSDVWSLGLTLLEVAQNRFPFPPEgepplgpiellSYIVNMPNPELKD---EPENGIKWS 239
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*...
gi 281359561 8215 EEAKDFIRKLLVRNKEKRMTAHECLLHPWLTGdhsAMKQEINRDRYLA 8262
Cdd:cd06621   240 ESFKDFIEKCLEKDGTRRPGPWQMLAHPWIKA---QEKKKVNMAKFVK 284
STKc_Nek3 cd08219
Catalytic domain of the Protein Serine/Threonine Kinase, Never In Mitosis gene A (NIMA) ...
7988-8239 1.81e-27

Catalytic domain of the Protein Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase 3; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Nek3 is primarily localized in the cytoplasm and shows no cell cycle-dependent changes in its activity. It is present in the axons of neurons and affects morphogenesis and polarity through its regulation of microtubule acetylation. Nek3 modulates the signaling of the prolactin receptor through its activation of Vav2 and contributes to prolactin-mediated motility of breast cancer cells. It is one in a family of 11 different Neks (Nek1-11) that are involved in cell cycle control. The Nek family is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 173759 [Multi-domain]  Cd Length: 255  Bit Score: 115.46  E-value: 1.81e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 7988 RYDILEEIGTGAFGVVHRCRERSTGNIFAAKFI--PVS-HSVEKDliRREIDIMNQLHHQKLINLHDAFEDDDEMILILE 8064
Cdd:cd08219     1 QYNVLRVVGEGSFGRALLVQHVNSDQKYAMKEIrlPKSsSAVEDS--RKEAVLLAKMKHPNIVAFKESFEADGHLYIVME 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 8065 FLSGGELFERITAE-GYVMTEAEVINYMRQICEGIRHMHEQNIIHLDIKPENIMCQtrSSTNVKLIDFGLATRL-DPNEV 8142
Cdd:cd08219    79 YCDGGDLMQKIKLQrGKLFPEDTILQWFVQMCLGVQHIHEKRVLHRDIKSKNIFLT--QNGKVKLGDFGSARLLtSPGAY 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 8143 VKITTGTAEFAAPEIVNREPVGFYTDMWATGVLSYVLLSGLSPFAGDndvqTLKN--VKACDWDFDVESFKYiSEEAKDF 8220
Cdd:cd08219   157 ACTYVGTPYYVPPEIWENMPYNNKSDIWSLGCILYELCTLKHPFQAN----SWKNliLKVCQGSYKPLPSHY-SYELRSL 231
                         250
                  ....*....|....*....
gi 281359561 8221 IRKLLVRNKEKRMTAHECL 8239
Cdd:cd08219   232 IKQMFKRNPRSRPSATTIL 250
STKc_nPKC_theta_like cd05592
Catalytic domain of the Serine/Threonine Kinases, Novel Protein Kinase C theta, delta, and ...
7995-8238 3.23e-27

Catalytic domain of the Serine/Threonine Kinases, Novel Protein Kinase C theta, delta, and similar proteins; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PKC-theta is selectively expressed in T-cells and plays an important and non-redundant role in several aspects of T-cell biology. PKC-delta plays a role in cell cycle regulation and programmed cell death in many cell types. PKCs are classified into three groups (classical, atypical, and novel) depending on their mode of activation and the structural characteristics of their regulatory domain. nPKCs are calcium-independent, but require DAG (1,2-diacylglycerol) and phosphatidylserine (PS) for activity. There are four nPKC isoforms, delta, epsilon, eta, and theta. The nPKC-theta-like subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270744 [Multi-domain]  Cd Length: 320  Bit Score: 116.72  E-value: 3.23e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 7995 IGTGAFGVVHRCRERSTGNIFAAK-----FIPVSHSVEKDLIRREIDIMNQlHHQKLINLHDAFEDDDEMILILEFLSGG 8069
Cdd:cd05592     3 LGKGSFGKVMLAELKGTNQYFAIKalkkdVVLEDDDVECTMIERRVLALAS-QHPFLTHLFCTFQTESHLFFVMEYLNGG 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 8070 ELFERITAEGYvMTEAEVINYMRQICEGIRHMHEQNIIHLDIKPENIMCQTRSstNVKLIDFGLAtRLDPNEVVKITT-- 8147
Cdd:cd05592    82 DLMFHIQQSGR-FDEDRARFYGAEIICGLQFLHSRGIIYRDLKLDNVLLDREG--HIKIADFGMC-KENIYGENKASTfc 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 8148 GTAEFAAPEIVNREPVGFYTDMWATGVLSYVLLSGLSPFAGDNDVQTLKNVkaCDwdfDVESF-KYISEEAKDFIRKLLV 8226
Cdd:cd05592   158 GTPDYIAPEILKGQKYNQSVDWWSFGVLLYEMLIGQSPFHGEDEDELFWSI--CN---DTPHYpRWLTKEAASCLSLLLE 232
                         250
                  ....*....|..
gi 281359561 8227 RNKEKRMTAHEC 8238
Cdd:cd05592   233 RNPEKRLGVPEC 244
STKc_ASK cd06624
Catalytic domain of the Serine/Threonine Kinase, Apoptosis signal-regulating kinase; STKs ...
7995-8244 3.31e-27

Catalytic domain of the Serine/Threonine Kinase, Apoptosis signal-regulating kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Members of this subfamily are mitogen-activated protein kinase (MAPK) kinase kinases (MAPKKKs or MKKKs) and include ASK1, ASK2, and MAPKKK15. ASK1 (also called MAPKKK5) functions in the c-Jun N-terminal kinase (JNK) and p38 MAPK signaling pathways by directly activating their respective MAPKKs, MKK4/MKK7 and MKK3/MKK6. It plays important roles in cytokine and stress responses, as well as in reactive oxygen species-mediated cellular responses. ASK1 is implicated in various diseases mediated by oxidative stress including inschemic heart disease, hypertension, vessel injury, brain ischemia, Fanconi anemia, asthma, and pulmonary edema, among others. ASK2 (also called MAPKKK6) functions only in a heteromeric complex with ASK1, and can activate ASK1 by direct phosphorylation. The function of MAPKKK15 is still unknown. The ASK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270794 [Multi-domain]  Cd Length: 268  Bit Score: 115.20  E-value: 3.31e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 7995 IGTGAFGVVHRCRERSTGNIFAAKFIPVSHSVEKDLIRREIDIMNQLHHQKLINLHDAFEDDDEMILILEFLSGGELFER 8074
Cdd:cd06624    16 LGKGTFGVVYAARDLSTQVRIAIKEIPERDSREVQPLHEEIALHSRLSHKNIVQYLGSVSEDGFFKIFMEQVPGGSLSAL 95
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 8075 ITAE-GYVMT-EAEVINYMRQICEGIRHMHEQNIIHLDIKPENIMCQTRSSTnVKLIDFGLATRLDP-NEVVKITTGTAE 8151
Cdd:cd06624    96 LRSKwGPLKDnENTIGYYTKQILEGLKYLHDNKIVHRDIKGDNVLVNTYSGV-VKISDFGTSKRLAGiNPCTETFTGTLQ 174
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 8152 FAAPEIVNREPVGF--YTDMWATGVLSYVLLSGLSPFAgdndvqTLKNVKACdwDFDVESFKY-------ISEEAKDFIR 8222
Cdd:cd06624   175 YMAPEVIDKGQRGYgpPADIWSLGCTIIEMATGKPPFI------ELGEPQAA--MFKVGMFKIhpeipesLSEEAKSFIL 246
                         250       260
                  ....*....|....*....|..
gi 281359561 8223 KLLVRNKEKRMTAHECLLHPWL 8244
Cdd:cd06624   247 RCFEPDPDKRATASDLLQDPFL 268
STKc_MRCK_beta cd05624
Catalytic domain of the Protein Serine/Threonine Kinase, DMPK-related cell division control ...
7963-8246 4.31e-27

Catalytic domain of the Protein Serine/Threonine Kinase, DMPK-related cell division control protein 42 binding kinase (MRCK) beta; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MRCK-beta is expressed ubiquitously in many tissues. MRCK is activated via interaction with the small GTPase Cdc42. MRCK/Cdc42 signaling mediates myosin-dependent cell motility. The MRCK-beta subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase. This alignment model includes the dimerization domain.


Pssm-ID: 270774 [Multi-domain]  Cd Length: 409  Bit Score: 118.57  E-value: 4.31e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 7963 DSYVFDIYSKFVPQPVEISQQSVY-DRYDILEEIGTGAFGVVHRCRERSTGNIFAAKFI---PVSHSVEKDLIRREIDIM 8038
Cdd:cd05624    47 DKYVSEFLEWAKPFTQLVKEMQLHrDDFEIIKVIGRGAFGEVAVVKMKNTERIYAMKILnkwEMLKRAETACFREERNVL 126
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 8039 NQLHHQKLINLHDAFEDDDEMILILEFLSGGELFERITAEGYVMTEAEVINYMRQICEGIRHMHEQNIIHLDIKPENIMC 8118
Cdd:cd05624   127 VNGDCQWITTLHYAFQDENYLYLVMDYYVGGDLLTLLSKFEDKLPEDMARFYIGEMVLAIHSIHQLHYVHRDIKPDNVLL 206
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 8119 QTRSstNVKLIDFGLATRLDPNEVVK--ITTGTAEFAAPEIVN--REPVGFY---TDMWATGVLSYVLLSGLSPFAGDND 8191
Cdd:cd05624   207 DMNG--HIRLADFGSCLKMNDDGTVQssVAVGTPDYISPEILQamEDGMGKYgpeCDWWSLGVCMYEMLYGETPFYAESL 284
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 281359561 8192 VQTLKNVKACDWDFDVES-FKYISEEAKDFIRKLLVrNKEKRMTAH---ECLLHPWLTG 8246
Cdd:cd05624   285 VETYGKIMNHEERFQFPShVTDVSEEAKDLIQRLIC-SRERRLGQNgieDFKKHAFFEG 342
STKc_PAK4 cd06657
Catalytic domain of the Serine/Threonine Kinase, p21-activated kinase 4; STKs catalyze the ...
7994-8245 4.79e-27

Catalytic domain of the Serine/Threonine Kinase, p21-activated kinase 4; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PAK4 regulates cell morphology and cytoskeletal organization. It is essential for embryonic viability and proper neural development. Mice lacking PAK4 die due to defects in the fetal heart. In addition, their spinal cord motor neurons showed failure to differentiate and migrate. PAK4 also plays a role in cell survival and tumorigenesis. It is overexpressed in many primary tumors including colon, esophageal, and mammary tumors. PAK4 has also been implicated in viral and bacterial infection pathways. PAK4 belongs to the group II PAKs, which contain a PBD (p21-binding domain) and a C-terminal catalytic domain, but do not harbor an AID (autoinhibitory domain) or SH3 binding sites. PAKs are Rho family GTPase-regulated kinases that serve as important mediators in the function of Cdc42 (cell division cycle 42) and Rac. The PAK subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 132988 [Multi-domain]  Cd Length: 292  Bit Score: 115.51  E-value: 4.79e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 7994 EIGTGAFGVVHRCRERSTGNIFAAKFIPVSHSVEKDLIRREIDIMNQLHHQKLINLHDAFEDDDEMILILEFLSGGELFE 8073
Cdd:cd06657    27 KIGEGSTGIVCIATVKSSGKLVAVKKMDLRKQQRRELLFNEVVIMRDYQHENVVEMYNSYLVGDELWVVMEFLEGGALTD 106
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 8074 RITAEGyvMTEAEVINYMRQICEGIRHMHEQNIIHLDIKPENIMCQtrSSTNVKLIDFGLATRLDpNEVV--KITTGTAE 8151
Cdd:cd06657   107 IVTHTR--MNEEQIAAVCLAVLKALSVLHAQGVIHRDIKSDSILLT--HDGRVKLSDFGFCAQVS-KEVPrrKSLVGTPY 181
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 8152 FAAPEIVNREPVGFYTDMWATGVLSYVLLSGLSPFAGDNDVQTLKNVKAcDWDFDVESFKYISEEAKDFIRKLLVRNKEK 8231
Cdd:cd06657   182 WMAPELISRLPYGPEVDIWSLGIMVIEMVDGEPPYFNEPPLKAMKMIRD-NLPPKLKNLHKVSPSLKGFLDRLLVRDPAQ 260
                         250
                  ....*....|....
gi 281359561 8232 RMTAHECLLHPWLT 8245
Cdd:cd06657   261 RATAAELLKHPFLA 274
STKc_MEKK3_like_u1 cd06653
Catalytic domain of an Uncharacterized subfamily of Mitogen-Activated Protein (MAP) ...
7995-8243 4.87e-27

Catalytic domain of an Uncharacterized subfamily of Mitogen-Activated Protein (MAP)/Extracellular signal-Regulated Kinase (ERK) Kinase Kinase 3-like Serine/Threonine Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily is composed of uncharacterized proteins with similarity to MEKK3, MEKK2, and related proteins; they contain an N-terminal PB1 domain, which mediates oligomerization, and a C-terminal catalytic domain. MEKK2 and MEKK3 are MAPK kinase kinases (MAPKKKs or MKKKs), proteins that phosphorylate and activate MAPK kinases (MAPKKs or MKKs), which in turn phosphorylate and activate MAPKs during signaling cascades that are important in mediating cellular responses to extracellular signals. MEKK2 and MEKK3 activate MEK5 (also called MKK5), which activates ERK5. The ERK5 cascade plays roles in promoting cell proliferation, differentiation, neuronal survival, and neuroprotection. MEKK3 plays an essential role in embryonic angiogenesis and early heart development. MEKK2 and MEKK3 can also activate the MAPKs, c-Jun N-terminal kinase (JNK) and p38, through their respective MAPKKs. The MEKK3-like subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270819 [Multi-domain]  Cd Length: 264  Bit Score: 114.35  E-value: 4.87e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 7995 IGTGAFGVVHRCRERSTGNIFAAK---FIPVSHSVEKDL--IRREIDIMNQLHHQKLINLHDAFEDDDE--MILILEFLS 8067
Cdd:cd06653    10 LGRGAFGEVYLCYDADTGRELAVKqvpFDPDSQETSKEVnaLECEIQLLKNLRHDRIVQYYGCLRDPEEkkLSIFVEYMP 89
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 8068 GGELFERITAEGyVMTEAEVINYMRQICEGIRHMHEQNIIHLDIKPENIMcqTRSSTNVKLIDFGLATRLD----PNEVV 8143
Cdd:cd06653    90 GGSVKDQLKAYG-ALTENVTRRYTRQILQGVSYLHSNMIVHRDIKGANIL--RDSAGNVKLGDFGASKRIQticmSGTGI 166
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 8144 KITTGTAEFAAPEIVNREPVGFYTDMWATGVLSYVLLSGLSPFAgdnDVQTLKNV-KACDWDFDVESFKYISEEAKDFIR 8222
Cdd:cd06653   167 KSVTGTPYWMSPEVISGEGYGRKADVWSVACTVVEMLTEKPPWA---EYEAMAAIfKIATQPTKPQLPDGVSDACRDFLR 243
                         250       260
                  ....*....|....*....|.
gi 281359561 8223 KLLVRNKeKRMTAHECLLHPW 8243
Cdd:cd06653   244 QIFVEEK-RRPTAEFLLRHPF 263
STKc_Sck1_like cd05586
Catalytic domain of Suppressor of loss of cAMP-dependent protein kinase-like Serine/Threonine ...
7995-8237 6.41e-27

Catalytic domain of Suppressor of loss of cAMP-dependent protein kinase-like Serine/Threonine Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily is composed of Schizosaccharomyces pombe Sck1 and similar fungal proteins. Sck1 plays a role in trehalase activation triggered by glucose and a nitrogen source. Trehalase catalyzes the cleavage of the disaccharide trehalose to glucose. Trehalose, as a carbohydrate reserve and stress metabolite, plays an important role in the response of yeast to environmental changes. The Sck1-like subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270738 [Multi-domain]  Cd Length: 330  Bit Score: 116.13  E-value: 6.41e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 7995 IGTGAFGVVHRCRERSTGNIFAAKFIPVSHSVEKDLIRREIDIMNQLHHQK------LINLHDAFEDDDEMILILEFLSG 8068
Cdd:cd05586     1 IGKGTFGQVYQVRKKDTRRIYAMKVLSKKVIVAKKEVAHTIGERNILVRTAldespfIVGLKFSFQTPTDLYLVTDYMSG 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 8069 GELFERITAEGYvMTEAEVINYMRQICEGIRHMHEQNIIHLDIKPENIMCQtrSSTNVKLIDFGLA-TRLDPNEVVKITT 8147
Cdd:cd05586    81 GELFWHLQKEGR-FSEDRAKFYIAELVLALEHLHKNDIVYRDLKPENILLD--ANGHIALCDFGLSkADLTDNKTTNTFC 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 8148 GTAEFAAPEIVNREP-VGFYTDMWATGVLSYVLLSGLSPFAGDNDVQTLKNVKACDWDFDVESfkyISEEAKDFIRKLLV 8226
Cdd:cd05586   158 GTTEYLAPEVLLDEKgYTKMVDFWSLGVLVFEMCCGWSPFYAEDTQQMYRNIAFGKVRFPKDV---LSDEGRSFVKGLLN 234
                         250
                  ....*....|.
gi 281359561 8227 RNKEKRMTAHE 8237
Cdd:cd05586   235 RNPKHRLGAHD 245
STKc_ULK1_2-like cd14120
Catalytic domain of the Serine/Threonine kinases, Unc-51-like kinases 1 and 2, and similar ...
7995-8242 7.32e-27

Catalytic domain of the Serine/Threonine kinases, Unc-51-like kinases 1 and 2, and similar proteins; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The ATG1/ULK complex is conserved from yeast to humans and it plays a critical role in the initiation of autophagy, the intracellular system that leads to the lysosomal degradation of cellular components and their recycling into basic metabolic units. ULK1 is required for efficient amino acid starvation-induced autophagy and mitochondrial clearance. ULK2 is ubiquitously expressed and is essential in autophagy induction. ULK1 and ULK2 have unique and cell-type specific roles, but also display partially redundant roles in starvation-induced autophagy. They both display neuron-specific functions: ULK1 is involved in non-clathrin-coated endocytosis in growth cones, filopodia extension, and axon branching; ULK2 plays a role in axon development. The ULK1/2 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271022 [Multi-domain]  Cd Length: 256  Bit Score: 113.62  E-value: 7.32e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 7995 IGTGAFGVVHRCRER-STGNIFAAKFIPVSH-SVEKDLIRREIDIMNQLHHQKLINLHDAFEDDDEMILILEFLSGGELF 8072
Cdd:cd14120     1 IGHGAFAVVFKGRHRkKPDLPVAIKCITKKNlSKSQNLLGKEIKILKELSHENVVALLDCQETSSSVYLVMEYCNGGDLA 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 8073 ERITAEGyVMTEAEVINYMRQICEGIRHMHEQNIIHLDIKPENIM----CQTRSSTN---VKLIDFGLATRLDPNEVVKI 8145
Cdd:cd14120    81 DYLQAKG-TLSEDTIRVFLQQIAAAMKALHSKGIVHRDLKPQNILlshnSGRKPSPNdirLKIADFGFARFLQDGMMAAT 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 8146 TTGTAEFAAPEIVNREPVGFYTDMWATGVLSYVLLSGLSPFAGdNDVQTLKNVKACDWDFDVESFKYISEEAKDFIRKLL 8225
Cdd:cd14120   160 LCGSPMYMAPEVIMSLQYDAKADLWSIGTIVYQCLTGKAPFQA-QTPQELKAFYEKNANLRPNIPSGTSPALKDLLLGLL 238
                         250
                  ....*....|....*..
gi 281359561 8226 VRNKEKRMTAHECLLHP 8242
Cdd:cd14120   239 KRNPKDRIDFEDFFSHP 255
STKc_GRK7 cd05607
Catalytic domain of the Protein Serine/Threonine Kinase, G protein-coupled Receptor Kinase 7; ...
7995-8237 9.43e-27

Catalytic domain of the Protein Serine/Threonine Kinase, G protein-coupled Receptor Kinase 7; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. GRK7 (also called iodopsin kinase) belongs to the visual group of GRKs. It is primarily found in the retina and plays a role in the regulation of opsin light receptors. GRK7 is located in retinal cone outer segments and plays an important role in regulating photoresponse of the cones. GRKs phosphorylate and regulate G protein-coupled receptors (GPCRs), the largest superfamily of cell surface receptors, which regulate some part of nearly all physiological functions. Phosphorylated GPCRs bind to arrestins, which prevents further G protein signaling despite the presence of activating ligand. The GRK7 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270758 [Multi-domain]  Cd Length: 286  Bit Score: 114.23  E-value: 9.43e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 7995 IGTGAFGVVHRCRERSTGNIFAAKFIPVSHSVEKD---LIRREIDIMNQLHHQKLINLHDAFEDDDEMILILEFLSGGEL 8071
Cdd:cd05607    10 LGKGGFGEVCAVQVKNTGQMYACKKLDKKRLKKKSgekMALLEKEILEKVNSPFIVSLAYAFETKTHLCLVMSLMNGGDL 89
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 8072 FERITAEGYVMTEAE-VINYMRQICEGIRHMHEQNIIHLDIKPENIMCQTRSstNVKLIDFGLATRLDPNEVVKITTGTA 8150
Cdd:cd05607    90 KYHIYNVGERGIEMErVIFYSAQITCGILHLHSLKIVYRDMKPENVLLDDNG--NCRLSDLGLAVEVKEGKPITQRAGTN 167
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 8151 EFAAPEIVNREPVGFYTDMWATGVLSYVLLSGLSPFAGDNDVQTLKNVKACDWDFDVEsFKY--ISEEAKDFIRKLLVRN 8228
Cdd:cd05607   168 GYMAPEILKEESYSYPVDWFAMGCSIYEMVAGRTPFRDHKEKVSKEELKRRTLEDEVK-FEHqnFTEEAKDICRLFLAKK 246

                  ....*....
gi 281359561 8229 KEKRMTAHE 8237
Cdd:cd05607   247 PENRLGSRT 255
STKc_MEKK2 cd06652
Catalytic domain of the Serine/Threonine Kinase, Mitogen-Activated Protein (MAP)/Extracellular ...
7995-8241 1.26e-26

Catalytic domain of the Serine/Threonine Kinase, Mitogen-Activated Protein (MAP)/Extracellular signal-Regulated Kinase (ERK) Kinase Kinase 2; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MEKK2 is a MAPK kinase kinase (MAPKKK or MKKK), that phosphorylates and activates the MAPK kinase MEK5 (or MKK5), which in turn phosphorylates and activates ERK5. The ERK5 cascade plays roles in promoting cell proliferation, differentiation, neuronal survival, and neuroprotection. MEKK2 also activates ERK1/2, c-Jun N-terminal kinase (JNK) and p38 through their respective MAPKKs MEK1/2, JNK-activating kinase 2 (JNKK2), and MKK3/6. MEKK2 plays roles in T cell receptor signaling, immune synapse formation, cytokine gene expression, as well as in EGF and FGF receptor signaling. The MEKK2 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270818 [Multi-domain]  Cd Length: 264  Bit Score: 113.22  E-value: 1.26e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 7995 IGTGAFGVVHRCRERSTGNIFAAK---FIPVSHSVEKDL--IRREIDIMNQLHHQKLINLHDAFEDDDEMIL--ILEFLS 8067
Cdd:cd06652    10 LGQGAFGRVYLCYDADTGRELAVKqvqFDPESPETSKEVnaLECEIQLLKNLLHERIVQYYGCLRDPQERTLsiFMEYMP 89
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 8068 GGELFERITAEGyVMTEAEVINYMRQICEGIRHMHEQNIIHLDIKPENIMcqTRSSTNVKLIDFGLATRLD----PNEVV 8143
Cdd:cd06652    90 GGSIKDQLKSYG-ALTENVTRKYTRQILEGVHYLHSNMIVHRDIKGANIL--RDSVGNVKLGDFGASKRLQticlSGTGM 166
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 8144 KITTGTAEFAAPEIVNREPVGFYTDMWATGVLSYVLLSGLSPFAgdnDVQTLKNV-KACDWDFDVESFKYISEEAKDFIR 8222
Cdd:cd06652   167 KSVTGTPYWMSPEVISGEGYGRKADIWSVGCTVVEMLTEKPPWA---EFEAMAAIfKIATQPTNPQLPAHVSDHCRDFLK 243
                         250
                  ....*....|....*....
gi 281359561 8223 KLLVRNKEkRMTAHECLLH 8241
Cdd:cd06652   244 RIFVEAKL-RPSADELLRH 261
STKc_IKK cd13989
Catalytic domain of the Serine/Threonine kinase, Inhibitor of Nuclear Factor-KappaB Kinase ...
7995-8186 1.78e-26

Catalytic domain of the Serine/Threonine kinase, Inhibitor of Nuclear Factor-KappaB Kinase (IKK); STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The IKK complex functions as a master regulator of Nuclear Factor-KappaB (NF-kB) proteins, a family of transcription factors which are critical in many cellular functions including inflammatory responses, immune development, cell survival, and cell proliferation, among others. It is composed of two kinases, IKKalpha and IKKbeta, and the regulatory subunit IKKgamma or NEMO (NF-kB Essential MOdulator). IKKs facilitate the release of NF-kB dimers from an inactive state, allowing them to migrate to the nucleus where they regulate gene transcription. There are two IKK pathways that regulate NF-kB signaling, called the classical (involving IKKbeta and NEMO) and non-canonical (involving IKKalpha) pathways. The classical pathway regulates the majority of genes activated by NF-kB. The IKK subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase (PI3K).


Pssm-ID: 270891 [Multi-domain]  Cd Length: 289  Bit Score: 113.70  E-value: 1.78e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 7995 IGTGAFGVVHRCRERSTGNIFAAK---FIPVSHSVEKDLIRREIDIMNQLHHQKLINLHD------AFEDDDEMILILEF 8065
Cdd:cd13989     1 LGSGGFGYVTLWKHQDTGEYVAIKkcrQELSPSDKNRERWCLEVQIMKKLNHPNVVSARDvppeleKLSPNDLPLLAMEY 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 8066 LSGGELFERIT-AEGYV-MTEAEVINYMRQICEGIRHMHEQNIIHLDIKPENIMCQTRSSTNV-KLIDFGLATRLDPNEV 8142
Cdd:cd13989    81 CSGGDLRKVLNqPENCCgLKESEVRTLLSDISSAISYLHENRIIHRDLKPENIVLQQGGGRVIyKLIDLGYAKELDQGSL 160
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....
gi 281359561 8143 VKITTGTAEFAAPEIVNREPVGFYTDMWATGVLSYVLLSGLSPF 8186
Cdd:cd13989   161 CTSFVGTLQYLAPELFESKKYTCTVDYWSFGTLAFECITGYRPF 204
FN3 COG3401
Fibronectin type 3 domain [General function prediction only];
3866-4181 1.85e-26

Fibronectin type 3 domain [General function prediction only];


Pssm-ID: 442628 [Multi-domain]  Cd Length: 603  Bit Score: 119.34  E-value: 1.85e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 3866 YIVTAKNDSG----SDTVEVeLEVLCKPSKPKGpLAVSNVTAETLHLKWEKPEDDGgdpIEQYLVERMDTETGRWVPVLT 3941
Cdd:COG3401   207 YRVAATDTGGesapSNEVSV-TTPTTPPSAPTG-LTATADTPGSVTLSWDPVTESD---ATGYRVYRSNSGDGPFTKVAT 281
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 3942 TKTPEADVTGLTEGKEYLFRVKAVNSEG-ESEPLVTDIPTKAKNPfdaadtPGKPQIVD---WSGNHCDLKWRAPEDDGg 4017
Cdd:COG3401   282 VTTTSYTDTGLTNGTTYYYRVTAVDAAGnESAPSNVVSVTTDLTP------PAAPSGLTataVGSSSITLSWTASSDAD- 354
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 4018 asITGYIVERKDPNTGKWQKALETSTpDCKARVNDLIAGNKYQFRIMAVNKAG-KSKPSEPSDQMTAKDRFAPPKIDRTN 4096
Cdd:COG3401   355 --VTGYNVYRSTSGGGTYTKIAETVT-TTSYTDTGLTPGTTYYYKVTAVDAAGnESAPSEEVSATTASAASGESLTASVD 431
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 4097 IKDITIKAGQHIRfdIKVSGEPPATKVWLHNKARLENDDSNYNIDMESYRTKLTVPIS-KRFHSGKYTLKAENESGRDEA 4175
Cdd:COG3401   432 AVPLTDVAGATAA--ASAASNPGVSAAVLADGGDTGNAVPFTTTSSTVTATTTDTTTAnLSVTTGSLVGGSGASSVTNSV 509

                  ....*.
gi 281359561 4176 SFEVIV 4181
Cdd:COG3401   510 SVIGAS 515
STKc_CDK12 cd07864
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 12; STKs ...
7987-8244 2.53e-26

Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 12; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. CDK12 is also called Cdc2-related protein kinase 7 (CRK7) or Cdc2-related kinase arginine/serine-rich (CrkRS). It is a unique CDK that contains an RS domain, which is predominantly found in splicing factors. CDK12 is widely expressed in tissues. It interacts with cyclins L1 and L2, and plays roles in regulating transcription and alternative splicing. CDKs belong to a large family of STKs that are regulated by their cognate cyclins. Together, they are involved in the control of cell-cycle progression, transcription, and neuronal function. The CDK12 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270847 [Multi-domain]  Cd Length: 302  Bit Score: 113.36  E-value: 2.53e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 7987 DRYDILEEIGTGAFGVVHRCRERSTGNIFAAKFIPVSHSVEKDLIR--REIDIMNQLHHQKLINLHDAFEDDDEMI---- 8060
Cdd:cd07864     7 DKFDIIGIIGEGTYGQVYKAKDKDTGELVALKKVRLDNEKEGFPITaiREIKILRQLNHRSVVNLKEIVTDKQDALdfkk 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 8061 ------LILEFLSGgELFERITAEGYVMTEAEVINYMRQICEGIRHMHEQNIIHLDIKPENIMCQTRSstNVKLIDFGLA 8134
Cdd:cd07864    87 dkgafyLVFEYMDH-DLMGLLESGLVHFSEDHIKSFMKQLLEGLNYCHKKNFLHRDIKCSNILLNNKG--QIKLADFGLA 163
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 8135 -------TRLDPNEVVkittgTAEFAAPE-IVNREPVGFYTDMWATGVLSYVLLSGLSPFAGDNDVQTLKNV-KAC---- 8201
Cdd:cd07864   164 rlynseeSRPYTNKVI-----TLWYRPPElLLGEERYGPAIDVWSCGCILGELFTKKPIFQANQELAQLELIsRLCgspc 238
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 281359561 8202 --DWDfDV--------------------ESFKYISEEAKDFIRKLLVRNKEKRMTAHECLLHPWL 8244
Cdd:cd07864   239 paVWP-DViklpyfntmkpkkqyrrrlrEEFSFIPTPALDLLDHMLTLDPSKRCTAEQALNSPWL 302
STKc_SGK2 cd05603
Catalytic domain of the Serine/Threonine Kinase, Serum- and Glucocorticoid-induced Kinase 2; ...
7995-8235 3.02e-26

Catalytic domain of the Serine/Threonine Kinase, Serum- and Glucocorticoid-induced Kinase 2; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. SGK2 shows a more restricted distribution than SGK1 and is most abundantly expressed in epithelial tissues including kidney, liver, pancreas, and the choroid plexus of the brain. In vitro cellular assays show that SGK2 can stimulate the activity of ion channels, the glutamate transporter EEAT4, and the glutamate receptors, GluR6 and GLUR1. The SGK2 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270754 [Multi-domain]  Cd Length: 321  Bit Score: 113.91  E-value: 3.02e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 7995 IGTGAFGVVHRCRERSTGNIFAAKFI---PVSHSVEKDLIRREIDIM-NQLHHQKLINLHDAFEDDDEMILILEFLSGGE 8070
Cdd:cd05603     3 IGKGSFGKVLLAKRKCDGKFYAVKVLqkkTILKKKEQNHIMAERNVLlKNLKHPFLVGLHYSFQTSEKLYFVLDYVNGGE 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 8071 LFERITAEgYVMTEAEVINYMRQICEGIRHMHEQNIIHLDIKPENIMCQTRSstNVKLIDFGLATR-LDPNEVVKITTGT 8149
Cdd:cd05603    83 LFFHLQRE-RCFLEPRARFYAAEVASAIGYLHSLNIIYRDLKPENILLDCQG--HVVLTDFGLCKEgMEPEETTSTFCGT 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 8150 AEFAAPEIVNREPVGFYTDMWATGVLSYVLLSGLSPFAGDNDVQTLKNVkaCDWDFDVESFKyiSEEAKDFIRKLLVRNK 8229
Cdd:cd05603   160 PEYLAPEVLRKEPYDRTVDWWCLGAVLYEMLYGLPPFYSRDVSQMYDNI--LHKPLHLPGGK--TVAACDLLQGLLHKDQ 235

                  ....*.
gi 281359561 8230 EKRMTA 8235
Cdd:cd05603   236 RRRLGA 241
STKc_ULK4 cd14010
Catalytic domain of the Serine/Threonine kinase, Unc-51-like kinase 4; STKs catalyze the ...
7988-8243 4.81e-26

Catalytic domain of the Serine/Threonine kinase, Unc-51-like kinase 4; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. ULK4 is a functionally uncharacterized kinase that shows similarity to ATG1/ULKs. The ATG1/ULK complex is conserved from yeast to humans and it plays a critical role in the initiation of autophagy, the intracellular system that leads to the lysosomal degradation of cellular components and their recycling into basic metabolic units. The ULK4 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270912 [Multi-domain]  Cd Length: 269  Bit Score: 111.62  E-value: 4.81e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 7988 RYDILEEIGTGAFGVVHRCRERSTGNIFAAkfipvsHSVEK---DLIRREIDIMNQLHHQKLINLHDAFEDDDEMILILE 8064
Cdd:cd14010     1 NYVLYDEIGRGKHSVVYKGRRKGTIEFVAI------KCVDKskrPEVLNEVRLTHELKHPNVLKFYEWYETSNHLWLVVE 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 8065 FLSGGELFERITAEGYvMTEAEVINYMRQICEGIRHMHEQNIIHLDIKPENIMCQtrSSTNVKLIDFGLATRLD------ 8138
Cdd:cd14010    75 YCTGGDLETLLRQDGN-LPESSVRKFGRDLVRGLHYIHSKGIIYCDLKPSNILLD--GNGTLKLSDFGLARREGeilkel 151
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 8139 -----------PNEVVKITTGTAEFAAPEIVNREPVGFYTDMWATGVLSYVLLSGLSPFAGDNDVQTLKNVKACDWDF-D 8206
Cdd:cd14010   152 fgqfsdegnvnKVSKKQAKRGTPYYMAPELFQGGVHSFASDLWALGCVLYEMFTGKPPFVAESFTELVEKILNEDPPPpP 231
                         250       260       270
                  ....*....|....*....|....*....|....*...
gi 281359561 8207 VESFKYISEEAKDFIRKLLVRNKEKRMTAHECLLHP-W 8243
Cdd:cd14010   232 PKVSSKPSPDFKSLLKGLLEKDPAKRLSWDELVKHPfW 269
STKc_NAK_like cd14037
Catalytic domain of Numb-Associated Kinase (NAK)-like Serine/Threonine kinases; STKs catalyze ...
7991-8232 6.31e-26

Catalytic domain of Numb-Associated Kinase (NAK)-like Serine/Threonine kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily is composed of Drosophila melanogaster NAK, human BMP-2-inducible protein kinase (BMP2K or BIKe) and similar vertebrate proteins, as well as the Saccharomyces cerevisiae proteins Prk1, Actin-regulating kinase 1 (Ark1), and Akl1. NAK was the first characterized member of this subfamily. It plays a role in asymmetric cell division through its association with Numb. It also regulates the localization of Dlg, a protein essential for septate junction formation. BMP2K contains a nuclear localization signal and a kinase domain that is capable of phosphorylating itself and myelin basic protein. The expression of the BMP2K gene is increase during BMP-2-induced osteoblast differentiation. It may function to control the rate of differentiation. Prk1, Ark1, and Akl1 comprise a subfamily of yeast proteins that are important regulators of the actin cytoskeleton and endocytosis. They share an N-terminal kinase domain but no significant homology in other regions of their sequences. The NAK-like subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270939 [Multi-domain]  Cd Length: 277  Bit Score: 111.61  E-value: 6.31e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 7991 ILEEIGTGAFGVVHRCRERSTGNIFAAKFIPVSHSVEKDLIRREIDIMNQLH-HQKLINLHDAF-----EDDDEMILILE 8064
Cdd:cd14037     7 IEKYLAEGGFAHVYLVKTSNGGNRAALKRVYVNDEHDLNVCKREIEIMKRLSgHKNIVGYIDSSanrsgNGVYEVLLLME 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 8065 FLSGGELF----ERITAEgyvMTEAEVINYMRQICEGIRHMHEQN--IIHLDIKPENIMCQtrSSTNVKLIDFGLATRLD 8138
Cdd:cd14037    87 YCKGGGVIdlmnQRLQTG---LTESEILKIFCDVCEAVAAMHYLKppLIHRDLKVENVLIS--DSGNYKLCDFGSATTKI 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 8139 PN------------EVVKITtgTAEFAAPEIVN---REPVGFYTDMWATGVLSYVLLSGLSPFaGDNDvqtlkNVKACDW 8203
Cdd:cd14037   162 LPpqtkqgvtyveeDIKKYT--TLQYRAPEMIDlyrGKPITEKSDIWALGCLLYKLCFYTTPF-EESG-----QLAILNG 233
                         250       260
                  ....*....|....*....|....*....
gi 281359561 8204 DFDVESFKYISEEAKDFIRKLLVRNKEKR 8232
Cdd:cd14037   234 NFTFPDNSRYSKRLHKLIRYMLEEDPEKR 262
STKc_Nek10 cd08528
Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase ...
7989-8232 7.13e-26

Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase 10; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. No function has yet been ascribed to Nek10. The gene encoding Nek10 is a putative causative gene for breast cancer; it is located within a breast cancer susceptibility loci on chromosome 3p24. Nek10 is one in a family of 11 different Neks (Nek1-11) that are involved in cell cycle control. The Nek family is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270867 [Multi-domain]  Cd Length: 270  Bit Score: 111.44  E-value: 7.13e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 7989 YDILEEIGTGAFGVVHR-CRERSTGNIFAAKFIPVSH------SVEKDL----IRREIDIM-NQLHHQKLINLHDAFEDD 8056
Cdd:cd08528     2 YAVLELLGSGAFGCVYKvRKKSNGQTLLALKEINMTNpafgrtEQERDKsvgdIISEVNIIkEQLRHPNIVRYYKTFLEN 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 8057 DEMILILEFLSG---GELFERITAEGYVMTEAEVINYMRQICEGIRHMH-EQNIIHLDIKPENIMCQTRSstNVKLIDFG 8132
Cdd:cd08528    82 DRLYIVMELIEGaplGEHFSSLKEKNEHFTEDRIWNIFVQMVLALRYLHkEKQIVHRDLKPNNIMLGEDD--KVTITDFG 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 8133 LATRLDPNEVvKITT--GTAEFAAPEIVNREPVGFYTDMWATGVLSYVLLSGLSPFAGDNdVQTLKNvKACDWDFDVESF 8210
Cdd:cd08528   160 LAKQKGPESS-KMTSvvGTILYSCPEIVQNEPYGEKADIWALGCILYQMCTLQPPFYSTN-MLTLAT-KIVEAEYEPLPE 236
                         250       260
                  ....*....|....*....|..
gi 281359561 8211 KYISEEAKDFIRKLLVRNKEKR 8232
Cdd:cd08528   237 GMYSDDITFVIRSCLTPDPEAR 258
STKc_STK10 cd06644
Catalytic domain of the Serine/Threonine Kinase, STK10 (also called Lymphocyte-Oriented Kinase ...
7987-8245 8.36e-26

Catalytic domain of the Serine/Threonine Kinase, STK10 (also called Lymphocyte-Oriented Kinase or LOK); STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. STK10/LOK is also called polo-like kinase kinase 1 in Xenopus (xPlkk1). It is highly expressed in lymphocytes and is responsible in regulating leukocyte function associated antigen (LFA-1)-mediated lymphocyte adhesion. It plays a role in regulating the CD28 responsive element in T cells, and may also function as a regulator of polo-like kinase 1 (Plk1), a protein which is overexpressed in multiple tumor types. The STK10 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 132975 [Multi-domain]  Cd Length: 292  Bit Score: 111.66  E-value: 8.36e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 7987 DRYDILEEIGTGAFGVVHRCRERSTGNIFAAKFIPVSHSVEKDLIRREIDIMNQLHHQKLINLHDAFEDDDEMILILEFL 8066
Cdd:cd06644    12 EVWEIIGELGDGAFGKVYKAKNKETGALAAAKVIETKSEEELEDYMVEIEILATCNHPYIVKLLGAFYWDGKLWIMIEFC 91
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 8067 SGGELFERITAEGYVMTEAEVINYMRQICEGIRHMHEQNIIHLDIKPENIMCQTRSstNVKLIDFGL-ATRLDPNEVVKI 8145
Cdd:cd06644    92 PGGAVDAIMLELDRGLTEPQIQVICRQMLEALQYLHSMKIIHRDLKAGNVLLTLDG--DIKLADFGVsAKNVKTLQRRDS 169
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 8146 TTGTAEFAAPEIVNRE-----PVGFYTDMWATGVLSYVLLSGLSPFAGDNDVQTLKNVKACDWDFDVESFKYiSEEAKDF 8220
Cdd:cd06644   170 FIGTPYWMAPEVVMCEtmkdtPYDYKADIWSLGITLIEMAQIEPPHHELNPMRVLLKIAKSEPPTLSQPSKW-SMEFRDF 248
                         250       260
                  ....*....|....*....|....*
gi 281359561 8221 IRKLLVRNKEKRMTAHECLLHPWLT 8245
Cdd:cd06644   249 LKTALDKHPETRPSAAQLLEHPFVS 273
STKc_YPK1_like cd05585
Catalytic domain of Yeast Protein Kinase 1-like Serine/Threonine Kinases; STKs catalyze the ...
7995-8244 1.13e-25

Catalytic domain of Yeast Protein Kinase 1-like Serine/Threonine Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily is composed of fungal proteins with similarity to the AGC STKs, Saccharomyces cerevisiae YPK1 and Schizosaccharomyces pombe Gad8p. YPK1 is required for cell growth and acts as a downstream kinase in the sphingolipid-mediated signaling pathway of yeast. It also plays a role in efficient endocytosis and in the maintenance of cell wall integrity. Gad8p is a downstream target of Tor1p, the fission yeast homolog of mTOR. It plays a role in cell growth and sexual development. The YPK1-like subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270737 [Multi-domain]  Cd Length: 313  Bit Score: 111.89  E-value: 1.13e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 7995 IGTGAFGVVHRCRERSTGNIFAAKFIPVSHSVEKDLIRR---EIDIMNQLHHQKLINLHDAFEDDDEMILILEFLSGGEL 8071
Cdd:cd05585     2 IGKGSFGKVMQVRKKDTSRIYALKTIRKAHIVSRSEVTHtlaERTVLAQVDCPFIVPLKFSFQSPEKLYLVLAFINGGEL 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 8072 FERITAEG-YVMTEAEVinYMRQICEGIRHMHEQNIIHLDIKPENIMCQTrsSTNVKLIDFGLAtRLDPNEVVKITT--G 8148
Cdd:cd05585    82 FHHLQREGrFDLSRARF--YTAELLCALECLHKFNVIYRDLKPENILLDY--TGHIALCDFGLC-KLNMKDDDKTNTfcG 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 8149 TAEFAAPEIVNREPVGFYTDMWATGVLSYVLLSGLSPFAGDNDVQTLKNVKACDWDFDvesfKYISEEAKDFIRKLLVRN 8228
Cdd:cd05585   157 TPEYLAPELLLGHGYTKAVDWWTLGVLLYEMLTGLPPFYDENTNEMYRKILQEPLRFP----DGFDRDAKDLLIGLLNRD 232
                         250
                  ....*....|....*....
gi 281359561 8229 KEKRM---TAHECLLHPWL 8244
Cdd:cd05585   233 PTKRLgynGAQEIKNHPFF 251
STKc_PKB_beta cd05595
Catalytic domain of the Serine/Threonine Kinase, Protein Kinase B beta (also called Akt2); ...
7995-8246 1.18e-25

Catalytic domain of the Serine/Threonine Kinase, Protein Kinase B beta (also called Akt2); STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PKB-beta is the predominant PKB isoform expressed in insulin-responsive tissues. It plays a critical role in the regulation of glucose homeostasis. It is also implicated in muscle cell differentiation. Mice deficient in PKB-beta display normal growth weights but exhibit severe insulin resistance and diabetes, accompanied by lipoatrophy and B-cell failure. PKB contains an N-terminal pleckstrin homology (PH) domain and a C-terminal catalytic domain.The PKB-beta subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 173686 [Multi-domain]  Cd Length: 323  Bit Score: 112.02  E-value: 1.18e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 7995 IGTGAFGVVHRCRERSTGNIFAAKFIPVSHSVEKDLIRR---EIDIMNQLHHQKLINLHDAFEDDDEMILILEFLSGGEL 8071
Cdd:cd05595     3 LGKGTFGKVILVREKATGRYYAMKILRKEVIIAKDEVAHtvtESRVLQNTRHPFLTALKYAFQTHDRLCFVMEYANGGEL 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 8072 FERITAEgYVMTEAEVINYMRQICEGIRHMHEQNIIHLDIKPENIMCQtrSSTNVKLIDFGLATRLDPNE-VVKITTGTA 8150
Cdd:cd05595    83 FFHLSRE-RVFTEDRARFYGAEIVSALEYLHSRDVVYRDIKLENLMLD--KDGHIKITDFGLCKEGITDGaTMKTFCGTP 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 8151 EFAAPEIVNREPVGFYTDMWATGVLSYVLLSGLSPFAGDNDVQTLKNVKACDWDFDvesfKYISEEAKDFIRKLLVRNKE 8230
Cdd:cd05595   160 EYLAPEVLEDNDYGRAVDWWGLGVVMYEMMCGRLPFYNQDHERLFELILMEEIRFP----RTLSPEAKSLLAGLLKKDPK 235
                         250       260
                  ....*....|....*....|.
gi 281359561 8231 KRM-----TAHECLLHPWLTG 8246
Cdd:cd05595   236 QRLgggpsDAKEVMEHRFFLS 256
PK_Tyr_Ser-Thr pfam07714
Protein tyrosine and serine/threonine kinase; Protein phosphorylation, which plays a key role ...
7991-8216 1.30e-25

Protein tyrosine and serine/threonine kinase; Protein phosphorylation, which plays a key role in most cellular activities, is a reversible process mediated by protein kinases and phosphoprotein phosphatases. Protein kinases catalyze the transfer of the gamma phosphate from nucleotide triphosphates (often ATP) to one or more amino acid residues in a protein substrate side chain, resulting in a conformational change affecting protein function. Phosphoprotein phosphatases catalyze the reverse process. Protein kinases fall into three broad classes, characterized with respect to substrate specificity; Serine/threonine-protein kinases, tyrosine-protein kinases, and dual specificity protein kinases (e.g. MEK - phosphorylates both Thr and Tyr on target proteins). This entry represents the catalytic domain found in a number of serine/threonine- and tyrosine-protein kinases. It does not include the catalytic domain of dual specificity kinases.


Pssm-ID: 462242 [Multi-domain]  Cd Length: 258  Bit Score: 109.89  E-value: 1.30e-25
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561  7991 ILEEIGTGAFGVVHRCRERSTGNifaAKFIPV--------SHSVEKDLIRREIDIMNQLHHQKLINLHDAFEDDDEMILI 8062
Cdd:pfam07714    3 LGEKLGEGAFGEVYKGTLKGEGE---NTKIKVavktlkegADEEEREDFLEEASIMKKLDHPNIVKLLGVCTQGEPLYIV 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561  8063 LEFLSGGELFERITAEGYVMTEAEVINYMRQICEGIRHMHEQNIIHLDIKPENIMCQtrSSTNVKLIDFGLATRLDPNEV 8142
Cdd:pfam07714   80 TEYMPGGDLLDFLRKHKRKLTLKDLLSMALQIAKGMEYLESKNFVHRDLAARNCLVS--ENLVVKISDFGLSRDIYDDDY 157
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561  8143 VKITTGTAE---FAAPE-IVNREpvgfYT---DMWATGVLSYVLLS-GLSPFAGDNDVQTLKNVKA-------------- 8200
Cdd:pfam07714  158 YRKRGGGKLpikWMAPEsLKDGK----FTsksDVWSFGVLLWEIFTlGEQPYPGMSNEEVLEFLEDgyrlpqpencpdel 233
                          250       260
                   ....*....|....*....|....*
gi 281359561  8201 ------CdWDFDVE---SFKYISEE 8216
Cdd:pfam07714  234 ydlmkqC-WAYDPEdrpTFSELVED 257
STKc_TBK1 cd13988
Catalytic domain of the Serine/Threonine kinase, TANK Binding Kinase 1; STKs catalyze the ...
7995-8186 1.43e-25

Catalytic domain of the Serine/Threonine kinase, TANK Binding Kinase 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. TBK1 is also called T2K and NF-kB-activating kinase. It is widely expressed in most cell types and acts as an IkappaB kinase (IKK)-activating kinase responsible for NF-kB activation in response to growth factors. It plays a role in modulating inflammatory responses through the NF-kB pathway. TKB1 is also a major player in innate immune responses since it functions as a virus-activated kinase necessary for establishing an antiviral state. It phosphorylates IRF-3 and IRF-7, which are important transcription factors for inducing type I interferon during viral infection. In addition, TBK1 may also play roles in cell transformation and oncogenesis. The TBK1 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270890 [Multi-domain]  Cd Length: 316  Bit Score: 111.81  E-value: 1.43e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 7995 IGTGAFGVVHRCRERSTGNIFAAK-FIPVSHSVEKDLIRREIDIMNQLHHQKLINLhdaFEDDDEM-----ILILEFLSG 8068
Cdd:cd13988     1 LGQGATANVFRGRHKKTGDLYAVKvFNNLSFMRPLDVQMREFEVLKKLNHKNIVKL---FAIEEELttrhkVLVMELCPC 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 8069 GELFERIT--AEGYVMTEAEVINYMRQICEGIRHMHEQNIIHLDIKPENIMCQTRS--STNVKLIDFGLATRLDPNEVVK 8144
Cdd:cd13988    78 GSLYTVLEepSNAYGLPESEFLIVLRDVVAGMNHLRENGIVHRDIKPGNIMRVIGEdgQSVYKLTDFGAARELEDDEQFV 157
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|
gi 281359561 8145 ITTGTAEFAAPEIVNR--------EPVGFYTDMWATGVLSYVLLSGLSPF 8186
Cdd:cd13988   158 SLYGTEEYLHPDMYERavlrkdhqKKYGATVDLWSIGVTFYHAATGSLPF 207
STKc_PKN cd05589
Catalytic domain of the Serine/Threonine Kinase, Protein Kinase N; STKs catalyze the transfer ...
7995-8237 1.51e-25

Catalytic domain of the Serine/Threonine Kinase, Protein Kinase N; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PKN has a C-terminal catalytic domain that is highly homologous to PKCs. Its unique N-terminal regulatory region contains antiparallel coiled-coil (ACC) domains. In mammals, there are three PKN isoforms from different genes (designated PKN-alpha, beta, and gamma), which show different enzymatic properties, tissue distribution, and varied functions. PKN can be activated by the small GTPase Rho, and by fatty acids such as arachidonic and linoleic acids. It is involved in many biological processes including cytokeletal regulation, cell adhesion, vesicle transport, glucose transport, regulation of meiotic maturation and embryonic cell cycles, signaling to the nucleus, and tumorigenesis. The PKN subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270741 [Multi-domain]  Cd Length: 326  Bit Score: 112.01  E-value: 1.51e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 7995 IGTGAFGVVHRCRERSTGNIFAAKFIPVSHSVEKDLI------RREIDIMNQLHHQKLINLHDAFEDDDEMILILEFLSG 8068
Cdd:cd05589     7 LGRGHFGKVLLAEYKPTGELFAIKALKKGDIIARDEVeslmceKRIFETVNSARHPFLVNLFACFQTPEHVCFVMEYAAG 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 8069 GELFERITAEgyVMTEAEVINYMRQICEGIRHMHEQNIIHLDIKPENIMCQTRSStnVKLIDFGLATR-LDPNEVVKITT 8147
Cdd:cd05589    87 GDLMMHIHED--VFSEPRAVFYAACVVLGLQFLHEHKIVYRDLKLDNLLLDTEGY--VKIADFGLCKEgMGFGDRTSTFC 162
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 8148 GTAEFAAPEIVNREpvgFYT---DMWATGVLSYVLLSGLSPFAGDNDVQTLKNVKacdwDFDVESFKYISEEAKDFIRKL 8224
Cdd:cd05589   163 GTPEFLAPEVLTDT---SYTravDWWGLGVLIYEMLVGESPFPGDDEEEVFDSIV----NDEVRYPRFLSTEAISIMRRL 235
                         250
                  ....*....|...
gi 281359561 8225 LVRNKEKRMTAHE 8237
Cdd:cd05589   236 LRKNPERRLGASE 248
STKc_ERK1_2_like cd07849
Catalytic domain of Extracellular signal-Regulated Kinase 1 and 2-like Serine/Threonine ...
7985-8244 1.73e-25

Catalytic domain of Extracellular signal-Regulated Kinase 1 and 2-like Serine/Threonine Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily is composed of the mitogen-activated protein kinases (MAPKs) ERK1, ERK2, baker's yeast Fus3, and similar proteins. MAPK pathways are important mediators of cellular responses to extracellular signals. ERK1/2 activation is preferentially by mitogenic factors, differentiation stimuli, and cytokines, through a kinase cascade involving the MAPK kinases MEK1/2 and a MAPK kinase kinase from the Raf family. ERK1/2 have numerous substrates, many of which are nuclear and participate in transcriptional regulation of many cellular processes. They regulate cell growth, cell proliferation, and cell cycle progression from G1 to S phase. Although the distinct roles of ERK1 and ERK2 have not been fully determined, it is known that ERK2 can maintain most functions in the absence of ERK1, and that the deletion of ERK2 is embryonically lethal. The MAPK, Fus3, regulates yeast mating processes including mating-specific gene expression, G1 arrest, mating projection, and cell fusion. This ERK1/2-like subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270839 [Multi-domain]  Cd Length: 336  Bit Score: 112.01  E-value: 1.73e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 7985 VYDRYDILEEIGTGAFGVVHRCRERSTGNIFAAKFI-PVSHSVEKDLIRREIDIMNQLHHQKLINLHD-----AFEDDDE 8058
Cdd:cd07849     3 VGPRYQNLSYIGEGAYGMVCSAVHKPTGQKVAIKKIsPFEHQTYCLRTLREIKILLRFKHENIIGILDiqrppTFESFKD 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 8059 MILILEFLSGgELFERITAEgyVMTEAEVINYMRQICEGIRHMHEQNIIHLDIKPENIMCQTrsSTNVKLIDFGLATRLD 8138
Cdd:cd07849    83 VYIVQELMET-DLYKLIKTQ--HLSNDHIQYFLYQILRGLKYIHSANVLHRDLKPSNLLLNT--NCDLKICDFGLARIAD 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 8139 PNEVVKIT----TGTAEFAAPEIV--NREpvgfYT---DMWATGVLSYVLLSGLSPFAG------------------DND 8191
Cdd:cd07849   158 PEHDHTGFlteyVATRWYRAPEIMlnSKG----YTkaiDIWSVGCILAEMLSNRPLFPGkdylhqlnlilgilgtpsQED 233
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 281359561 8192 VQTLKNVKACDWdfdVES------------FKYISEEAKDFIRKLLVRNKEKRMTAHECLLHPWL 8244
Cdd:cd07849   234 LNCIISLKARNY---IKSlpfkpkvpwnklFPNADPKALDLLDKMLTFNPHKRITVEEALAHPYL 295
STKc_IKK_alpha cd14039
Catalytic domain of the Serine/Threonine kinase, Inhibitor of Nuclear Factor-KappaB Kinase ...
7995-8186 2.19e-25

Catalytic domain of the Serine/Threonine kinase, Inhibitor of Nuclear Factor-KappaB Kinase (IKK) alpha; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. IKKalpha is involved in the non-canonical or alternative pathway of regulating Nuclear Factor-KappaB (NF-kB) proteins, a family of transcription factors which are critical in many cellular functions including inflammatory responses, immune development, cell survival, and cell proliferation, among others. The non-canonical pathway functions in cells lacking NEMO (NF-kB Essential MOdulator) and IKKbeta. It is induced by a subset of TNFR family members including CD40, RANK, and B cell-activating factor receptor. IKKalpha processes the Inhibitor of NF-kB (IkB)-like C-terminus of NF-kB2/p100 to produce p52, allowing the p52/RelB dimer to migrate to the nucleus. This pathway is dependent on NIK (NF-kB Inducing Kinase) which phosphorylates and activates IKKalpha. The IKKalpha subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270941 [Multi-domain]  Cd Length: 289  Bit Score: 110.39  E-value: 2.19e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 7995 IGTGAFGVVHRCRERSTGNIFAAKFIPVSHSVE-KDLIRREIDIMNQLHHQKLINLHDAFED-----DDEMILILEFLSG 8068
Cdd:cd14039     1 LGTGGFGNVCLYQNQETGEKIAIKSCRLELSVKnKDRWCHEIQIMKKLNHPNVVKACDVPEEmnflvNDVPLLAMEYCSG 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 8069 GELFERITAEGYV--MTEAEVINYMRQICEGIRHMHEQNIIHLDIKPENIMCQTRSSTNV-KLIDFGLATRLDPNEVVKI 8145
Cdd:cd14039    81 GDLRKLLNKPENCcgLKESQVLSLLSDIGSGIQYLHENKIIHRDLKPENIVLQEINGKIVhKIIDLGYAKDLDQGSLCTS 160
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|.
gi 281359561 8146 TTGTAEFAAPEIVNREPVGFYTDMWATGVLSYVLLSGLSPF 8186
Cdd:cd14039   161 FVGTLQYLAPELFENKSYTVTVDYWSFGTMVFECIAGFRPF 201
STKc_GRK1 cd05608
Catalytic domain of the Serine/Threonine Kinase, G protein-coupled Receptor Kinase 1; STKs ...
7995-8233 2.48e-25

Catalytic domain of the Serine/Threonine Kinase, G protein-coupled Receptor Kinase 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. GRK1 (also called rhodopsin kinase) belongs to the visual group of GRKs and is expressed in retinal cells. It phosphorylates rhodopsin in rod cells, which leads to termination of the phototransduction cascade. Mutations in GRK1 are associated to a recessively inherited form of stationary nightblindness called Oguchi disease. GRKs phosphorylate and regulate G protein-coupled receptors (GPCRs), the largest superfamily of cell surface receptors, which regulate some part of nearly all physiological functions. Phosphorylated GPCRs bind to arrestins, which prevents further G protein signaling despite the presence of activating ligand. The GRK1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270759 [Multi-domain]  Cd Length: 288  Bit Score: 110.36  E-value: 2.48e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 7995 IGTGAFGVVHRCRERSTGNIFAAKFIPvshsvEKDLIRR--------EIDIMNQLHHQKLINLHDAFEDDDEMILILEFL 8066
Cdd:cd05608     9 LGKGGFGEVSACQMRATGKLYACKKLN-----KKRLKKRkgyegamvEKRILAKVHSRFIVSLAYAFQTKTDLCLVMTIM 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 8067 SGGEL---FERITAEGYVMTEAEVINYMRQICEGIRHMHEQNIIHLDIKPENIMCQtrSSTNVKLIDFGLATRL-DPNEV 8142
Cdd:cd05608    84 NGGDLryhIYNVDEENPGFQEPRACFYTAQIISGLEHLHQRRIIYRDLKPENVLLD--DDGNVRISDLGLAVELkDGQTK 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 8143 VKITTGTAEFAAPEIVNREPVGFYTDMWATGVLSYVLLSGLSPFAGDNDVQTLKNVKACDWDFDVESFKYISEEAKDFIR 8222
Cdd:cd05608   162 TKGYAGTPGFMAPELLLGEEYDYSVDYFTLGVTLYEMIAARGPFRARGEKVENKELKQRILNDSVTYSEKFSPASKSICE 241
                         250
                  ....*....|.
gi 281359561 8223 KLLVRNKEKRM 8233
Cdd:cd05608   242 ALLAKDPEKRL 252
STKc_CDK1_CdkB_like cd07835
Catalytic domain of Cyclin-Dependent protein Kinase 1-like Serine/Threonine Kinases and of ...
7989-8244 3.11e-25

Catalytic domain of Cyclin-Dependent protein Kinase 1-like Serine/Threonine Kinases and of Plant B-type Cyclin-Dependent protein Kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily is composed of CDK, CDK2, and CDK3. CDK1 is also called Cell division control protein 2 (Cdc2) or p34 protein kinase, and is regulated by cyclins A, B, and E. The CDK1/cyclin A complex controls G2 phase entry and progression while the CDK1/cyclin B complex is critical for G2 to M phase transition. CDK2 is regulated by cyclin E or cyclin A. Upon activation by cyclin E, it phosphorylates the retinoblastoma (pRb) protein which activates E2F mediated transcription and allows cells to move into S phase. The CDK2/cyclin A complex plays a role in regulating DNA replication. Studies in knockout mice revealed that CDK1 can compensate for the loss of the cdk2 gene as it can also bind cyclin E and drive G1 to S phase transition. CDK3 is regulated by cyclin C and it phosphorylates pRB specifically during the G0/G1 transition. This phosphorylation is required for cells to exit G0 efficiently and enter the G1 phase. The plant-specific B-type CDKs are expressed from the late S to the M phase of the cell cycle. They are characterized by the cyclin binding motif PPT[A/T]LRE. They play a role in controlling mitosis and integrating developmental pathways, such as stomata and leaf development. CdkB has been shown to associate with both cyclin B, which controls G2/M transition, and cyclin D, which acts as a mediator in linking extracellular signals to the cell cycle. CDKs belong to a large family of STKs that are regulated by their cognate cyclins. Together, they are involved in the control of cell-cycle progression, transcription, and neuronal function. The CDK1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270829 [Multi-domain]  Cd Length: 283  Bit Score: 109.69  E-value: 3.11e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 7989 YDILEEIGTGAFGVVHRCRERSTGNIFAAKFIPVSHS---VEKDLIRrEIDIMNQLHHQKLINLHDAFEDDDEMILILEF 8065
Cdd:cd07835     1 YQKLEKIGEGTYGVVYKARDKLTGEIVALKKIRLETEdegVPSTAIR-EISLLKELNHPNIVRLLDVVHSENKLYLVFEF 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 8066 LSGgELFERITAEGYVMTEAEVI-NYMRQICEGIRHMHEQNIIHLDIKPENIMCQTRSstNVKLIDFGLA------TRLD 8138
Cdd:cd07835    80 LDL-DLKKYMDSSPLTGLDPPLIkSYLYQLLQGIAFCHSHRVLHRDLKPQNLLIDTEG--ALKLADFGLArafgvpVRTY 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 8139 PNEVVkittgTAEFAAPEIVnrepVG--FYT---DMWATGVLSYVLLSGLSPFAGDN---------------------DV 8192
Cdd:cd07835   157 THEVV-----TLWYRAPEIL----LGskHYStpvDIWSVGCIFAEMVTRRPLFPGDSeidqlfrifrtlgtpdedvwpGV 227
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 281359561 8193 QTLKNVKAC-------DWDFDVESFkyiSEEAKDFIRKLLVRNKEKRMTAHECLLHPWL 8244
Cdd:cd07835   228 TSLPDYKPTfpkwarqDLSKVVPSL---DEDGLDLLSQMLVYDPAKRISAKAALQHPYF 283
STKc_CK2_alpha cd14132
Catalytic subunit (alpha) of the Serine/Threonine Kinase, Casein Kinase 2; STKs catalyze the ...
7961-8242 5.03e-25

Catalytic subunit (alpha) of the Serine/Threonine Kinase, Casein Kinase 2; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. CK2 is a tetrameric protein with two catalytic (alpha) and two regulatory (beta) subunits. It is constitutively active and ubiquitously expressed, and is found in the cytoplasm, nucleus, as well as in the plasma membrane. It phosphorylates a wide variety of substrates including gylcogen synthase, cell cycle proteins, nuclear proteins (e.g. DNA topoisomerase II), and ion channels (e.g. ENaC), among others. It may be considered a master kinase controlling the activity or lifespan of many other kinases and exerting its effect over cell fate, gene expression, protein synthesis and degradation, and viral infection. CK2 is implicated in every stage of the cell cycle and is required for cell cycle progression. It plays crucial roles in cell differentiation, proliferation, and survival, and is thus implicated in cancer. CK2 is not an oncogene by itself but elevated CK2 levels create an environment that enhances the survival of tumor cells. The CK2 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271034 [Multi-domain]  Cd Length: 306  Bit Score: 109.94  E-value: 5.03e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 7961 DYDSYVFdiyskfvpqpveisQQSVYDRYDILEEIGTGAFGVVHRCRERSTGNIFAAKfipVSHSVEKDLIRREIDIMNQ 8040
Cdd:cd14132     6 DYENLNV--------------EWGSQDDYEIIRKIGRGKYSEVFEGINIGNNEKVVIK---VLKPVKKKKIKREIKILQN 68
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 8041 LH-HQKLINLHDAFEDDDEMI--LILEFLSGGELFERItaegYVMTEAEVINYMRQICEGIRHMHEQNIIHLDIKPENIM 8117
Cdd:cd14132    69 LRgGPNIVKLLDVVKDPQSKTpsLIFEYVNNTDFKTLY----PTLTDYDIRYYMYELLKALDYCHSKGIMHRDVKPHNIM 144
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 8118 C-QTRSStnVKLIDFGLATRLDPNEVVKITTGTAEFAAPEI-VNrepVGFYT---DMWATGVLSYVLLSGLSPF--AGDN 8190
Cdd:cd14132   145 IdHEKRK--LRLIDWGLAEFYHPGQEYNVRVASRYYKGPELlVD---YQYYDyslDMWSLGCMLASMIFRKEPFfhGHDN 219
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 8191 DVQTLKNVKAC------------------------------DWDFDV--ESFKYISEEAKDFIRKLLVRNKEKRMTAHEC 8238
Cdd:cd14132   220 YDQLVKIAKVLgtddlyayldkygielpprlndilgrhskkPWERFVnsENQHLVTPEALDLLDKLLRYDHQERITAKEA 299

                  ....
gi 281359561 8239 LLHP 8242
Cdd:cd14132   300 MQHP 303
STKc_cPKC_beta cd05616
Catalytic domain of the Serine/Threonine Kinase, Classical Protein Kinase C beta; STKs ...
7989-8233 5.06e-25

Catalytic domain of the Serine/Threonine Kinase, Classical Protein Kinase C beta; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The PKC beta isoforms (I and II), generated by alternative splicing of a single gene, are preferentially activated by hyperglycemia-induced DAG (1,2-diacylglycerol) in retinal tissues. This is implicated in diabetic microangiopathy such as ischemia, neovascularization, and abnormal vasodilator function. PKC-beta also plays an important role in VEGF signaling. In addition, glucose regulates proliferation in retinal endothelial cells via PKC-betaI. PKC-beta is also being explored as a therapeutic target in cancer. It contributes to tumor formation and is involved in the tumor host mechanisms of inflammation and angiogenesis. PKCs are classified into three groups (classical, atypical, and novel) depending on their mode of activation and the structural characteristics of their regulatory domain. PKCs undergo three phosphorylations in order to take mature forms. In addition, cPKCs depend on calcium, DAG, and in most cases, phosphatidylserine (PS) for activation. The cPKC-beta subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270767 [Multi-domain]  Cd Length: 323  Bit Score: 110.09  E-value: 5.06e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 7989 YDILEEIGTGAFGVVHRCRERSTGNIFAAKFIpvshsvEKDLIRREIDIMNQLHHQK----------LINLHDAFEDDDE 8058
Cdd:cd05616     2 FNFLMVLGKGSFGKVMLAERKGTDELYAVKIL------KKDVVIQDDDVECTMVEKRvlalsgkppfLTQLHSCFQTMDR 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 8059 MILILEFLSGGELFERITAEGYvMTEAEVINYMRQICEGIRHMHEQNIIHLDIKPENIMCQtrSSTNVKLIDFGLATRld 8138
Cdd:cd05616    76 LYFVMEYVNGGDLMYHIQQVGR-FKEPHAVFYAAEIAIGLFFLQSKGIIYRDLKLDNVMLD--SEGHIKIADFGMCKE-- 150
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 8139 pNEVVKITT----GTAEFAAPEIVNREPVGFYTDMWATGVLSYVLLSGLSPFAGDNDVQTLKNVKacdwDFDVESFKYIS 8214
Cdd:cd05616   151 -NIWDGVTTktfcGTPDYIAPEIIAYQPYGKSVDWWAFGVLLYEMLAGQAPFEGEDEDELFQSIM----EHNVAYPKSMS 225
                         250
                  ....*....|....*....
gi 281359561 8215 EEAKDFIRKLLVRNKEKRM 8233
Cdd:cd05616   226 KEAVAICKGLMTKHPGKRL 244
STKc_CDK1_euk cd07861
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 1 from higher ...
7989-8244 5.21e-25

Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 1 from higher eukaryotes; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. CDK1 is also called Cell division control protein 2 (Cdc2) or p34 protein kinase, and is regulated by cyclins A, B, and E. The CDK1/cyclin A complex controls G2 phase entry and progression. CDK1/cyclin A2 has also been implicated as an important regulator of S phase events. The CDK1/cyclin B complex is critical for G2 to M phase transition. It induces mitosis by activating nuclear enzymes that regulate chromatin condensation, nuclear membrane degradation, mitosis-specific microtubule and cytoskeletal reorganization. CDK1 also associates with cyclin E and plays a role in the entry into S phase. CDK1 transcription is stable throughout the cell cycle but is modulated in some pathological conditions. It may play a role in regulating apoptosis under these conditions. In breast cancer cells, HER2 can mediate apoptosis by inactivating CDK1. Activation of CDK1 may contribute to HIV-1 induced apoptosis as well as neuronal apoptosis in neurodegenerative diseases. CDKs belong to a large family of STKs that are regulated by their cognate cyclins. Together, they are involved in the control of cell-cycle progression, transcription, and neuronal function. The CDK1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270845 [Multi-domain]  Cd Length: 285  Bit Score: 109.05  E-value: 5.21e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 7989 YDILEEIGTGAFGVVHRCRERSTGNIFAAKFIPVSHSVE--KDLIRREIDIMNQLHHQKLINLHDAFEDDDEMILILEFL 8066
Cdd:cd07861     2 YTKIEKIGEGTYGVVYKGRNKKTGQIVAMKKIRLESEEEgvPSTAIREISLLKELQHPNIVCLEDVLMQENRLYLVFEFL 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 8067 SGG--ELFERITAEGYvMTEAEVINYMRQICEGIRHMHEQNIIHLDIKPENIMCQtrSSTNVKLIDFGLA------TRLD 8138
Cdd:cd07861    82 SMDlkKYLDSLPKGKY-MDAELVKSYLYQILQGILFCHSRRVLHRDLKPQNLLID--NKGVIKLADFGLArafgipVRVY 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 8139 PNEVVkittgTAEFAAPEIVNREPVgfYT---DMWATGVLSYVLLSGLSPFAGD---------------------NDVQT 8194
Cdd:cd07861   159 THEVV-----TLWYRAPEVLLGSPR--YStpvDIWSIGTIFAEMATKKPLFHGDseidqlfrifrilgtptediwPGVTS 231
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....
gi 281359561 8195 LKNVKAC--DW--DFDVESFKYISEEAKDFIRKLLVRNKEKRMTAHECLLHPWL 8244
Cdd:cd07861   232 LPDYKNTfpKWkkGSLRTAVKNLDEDGLDLLEKMLIYDPAKRISAKKALVHPYF 285
STKc_Sid2p_like cd05600
Catalytic domain of Fungal Sid2p-like Protein Serine/Threonine Kinases; STKs catalyze the ...
7989-8225 6.08e-25

Catalytic domain of Fungal Sid2p-like Protein Serine/Threonine Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This group contains fungal kinases including Schizosaccharomyces pombe Sid2p and Saccharomyces cerevisiae Dbf2p. Group members show similarity to NDR kinases in that they contain an N-terminal regulatory (NTR) domain and an insert within the catalytic domain that contains an auto-inhibitory sequence. Sid2p plays a crucial role in the septum initiation network (SIN) and in the initiation of cytokinesis. Dbf2p is important in regulating the mitotic exit network (MEN) and in cytokinesis. The Sid2p-like group is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270751 [Multi-domain]  Cd Length: 386  Bit Score: 111.28  E-value: 6.08e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 7989 YDILEEIGTGAFGVVHRCRERSTGNIFAAKFIPVSHSVEKDLIRR---EIDIMNQLHHQKLINLHDAFEDDDEMILILEF 8065
Cdd:cd05600    13 FQILTQVGQGGYGSVFLARKKDTGEICALKIMKKKVLFKLNEVNHvltERDILTTTNSPWLVKLLYAFQDPENVYLAMEY 92
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 8066 LSGGELFERITAEGyVMTEAEVINYMRQICEGIRHMHEQNIIHLDIKPENIMCQtrSSTNVKLIDFGLAT---------- 8135
Cdd:cd05600    93 VPGGDFRTLLNNSG-ILSEEHARFYIAEMFAAISSLHQLGYIHRDLKPENFLID--SSGHIKLTDFGLASgtlspkkies 169
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 8136 -RLDPNEVVKITT---------------------------GTAEFAAPEIVNREPVGFYTDMWATGVLSYVLLSGLSPFA 8187
Cdd:cd05600   170 mKIRLEEVKNTAFleltakerrniyramrkedqnyansvvGSPDYMAPEVLRGEGYDLTVDYWSLGCILFECLVGFPPFS 249
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*...
gi 281359561 8188 GDNDVQTLKNVKacDW----------DFDVESFkyISEEAKDFIRKLL 8225
Cdd:cd05600   250 GSTPNETWANLY--HWkktlqrpvytDPDLEFN--LSDEAWDLITKLI 293
STKc_BUR1 cd07866
Catalytic domain of the Serine/Threonine Kinase, Fungal Cyclin-Dependent protein Kinase (CDK), ...
7984-8243 7.73e-25

Catalytic domain of the Serine/Threonine Kinase, Fungal Cyclin-Dependent protein Kinase (CDK), Bypass UAS Requirement 1, and similar proteins; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. BUR1, also called SGV1, is a yeast CDK that is functionally equivalent to mammalian CDK9. It associates with the cyclin BUR2. BUR genes were orginally identified in a genetic screen as factors involved in general transcription. The BUR1/BUR2 complex phosphorylates the C-terminal domain of RNA polymerase II. In addition, this complex regulates histone modification by phosporylating Rad6 and mediating the association of the Paf1 complex with chromatin. CDKs belong to a large family of STKs that are regulated by their cognate cyclins. Together, they are involved in the control of cell-cycle progression, transcription, and neuronal function. The BUR1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270849 [Multi-domain]  Cd Length: 311  Bit Score: 109.33  E-value: 7.73e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 7984 SVYDRYDILEEIGTGAFGVVHRCRERSTGNIFAAKFIPVSHsvEKDLI----RREIDIMNQLHHQKLINLHD-AFEDDDE 8058
Cdd:cd07866     5 SKLRDYEILGKLGEGTFGEVYKARQIKTGRVVALKKILMHN--EKDGFpitaLREIKILKKLKHPNVVPLIDmAVERPDK 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 8059 -------MILILEF----LSGgeLFE--RITaegyvMTEAEVINYMRQICEGIRHMHEQNIIHLDIKPENIMCQtrSSTN 8125
Cdd:cd07866    83 skrkrgsVYMVTPYmdhdLSG--LLEnpSVK-----LTESQIKCYMLQLLEGINYLHENHILHRDIKAANILID--NQGI 153
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 8126 VKLIDFGLATRLD---PNEVVKITTGTAEFA---------APEIVNREPVgfYT---DMWATGVLSYVLLSGLSPFAGDN 8190
Cdd:cd07866   154 LKIADFGLARPYDgppPNPKGGGGGGTRKYTnlvvtrwyrPPELLLGERR--YTtavDIWGIGCVFAEMFTRRPILQGKS 231
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 281359561 8191 DV---------------------QTLKNVKACDWDFDV-----ESFKYISEEAKDFIRKLLVRNKEKRMTAHECLLHPW 8243
Cdd:cd07866   232 DIdqlhlifklcgtpteetwpgwRSLPGCEGVHSFTNYprtleERFGKLGPEGLDLLSKLLSLDPYKRLTASDALEHPY 310
STKc_PKB_gamma cd05593
Catalytic domain of the Serine/Threonine Kinase, Protein Kinase B gamma (also called Akt3); ...
7982-8246 1.81e-24

Catalytic domain of the Serine/Threonine Kinase, Protein Kinase B gamma (also called Akt3); STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PKB-gamma is predominantly expressed in neuronal tissues. Mice deficient in PKB-gamma show a reduction in brain weight due to the decreases in cell size and cell number. PKB-gamma has also been shown to be upregulated in estrogen-deficient breast cancer cells, androgen-independent prostate cancer cells, and primary ovarian tumors. It acts as a key mediator in the genesis of ovarian cancer. PKB contains an N-terminal pleckstrin homology (PH) domain and a C-terminal catalytic domain. The PKB-gamma subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270745 [Multi-domain]  Cd Length: 348  Bit Score: 109.40  E-value: 1.81e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 7982 QQSVYDRYDILEEIGTGAFGVVHRCRERSTGNIFAAKFIPVSHSVEKDLIRR---EIDIMNQLHHQKLINLHDAFEDDDE 8058
Cdd:cd05593    10 KRKTMNDFDYLKLLGKGTFGKVILVREKASGKYYAMKILKKEVIIAKDEVAHtltESRVLKNTRHPFLTSLKYSFQTKDR 89
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 8059 MILILEFLSGGELFERITAEgYVMTEAEVINYMRQICEGIRHMHEQNIIHLDIKPENIMCQtrSSTNVKLIDFGLATR-L 8137
Cdd:cd05593    90 LCFVMEYVNGGELFFHLSRE-RVFSEDRTRFYGAEIVSALDYLHSGKIVYRDLKLENLMLD--KDGHIKITDFGLCKEgI 166
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 8138 DPNEVVKITTGTAEFAAPEIVNREPVGFYTDMWATGVLSYVLLSGLSPFAGDNDVQTLKNVKACDWDFDvesfKYISEEA 8217
Cdd:cd05593   167 TDAATMKTFCGTPEYLAPEVLEDNDYGRAVDWWGLGVVMYEMMCGRLPFYNQDHEKLFELILMEDIKFP----RTLSADA 242
                         250       260       270
                  ....*....|....*....|....*....|....
gi 281359561 8218 KDFIRKLLVRNKEKRM-----TAHECLLHPWLTG 8246
Cdd:cd05593   243 KSLLSGLLIKDPNKRLgggpdDAKEIMRHSFFTG 276
STKc_MEKK1 cd06630
Catalytic domain of the Protein Serine/Threonine Kinase, Mitogen-Activated Protein (MAP) ...
7995-8245 2.06e-24

Catalytic domain of the Protein Serine/Threonine Kinase, Mitogen-Activated Protein (MAP)/Extracellular signal-Regulated Kinase (ERK) Kinase Kinase 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MEKK1 is a MAPK kinase kinase (MAPKKK or MKKK) that phosphorylates and activates activates the ERK1/2 and c-Jun N-terminal kinase (JNK) pathways by activating their respective MAPKKs, MEK1/2 and MKK4/MKK7, respectively. MEKK1 is important in regulating cell survival and apoptosis. MEKK1 also plays a role in cell migration, tissue maintenance and homeostasis, and wound healing. The MEKK1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270800 [Multi-domain]  Cd Length: 268  Bit Score: 106.74  E-value: 2.06e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 7995 IGTGAFGVVHRCRERSTGNIFAAK---FIPVSHSVEKDL---IRREIDIMNQLHHQKLINLHDAFEDDDEMILILEFLSG 8068
Cdd:cd06630     8 LGTGAFSSCYQARDVKTGTLMAVKqvsFCRNSSSEQEEVveaIREEIRMMARLNHPNIVRMLGATQHKSHFNIFVEWMAG 87
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 8069 GE---LFERITAegyvMTEAEVINYMRQICEGIRHMHEQNIIHLDIKPENIMCQTrSSTNVKLIDFGLATRLdpneVVKI 8145
Cdd:cd06630    88 GSvasLLSKYGA----FSENVIINYTLQILRGLAYLHDNQIIHRDLKGANLLVDS-TGQRLRIADFGAAARL----ASKG 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 8146 T---------TGTAEFAAPEIVNREPVGFYTDMWATGVLSYVLLSGLSPFAGDNDVQTLKNVkacdwdFDVESF------ 8210
Cdd:cd06630   159 TgagefqgqlLGTIAFMAPEVLRGEQYGRSCDVWSVGCVIIEMATAKPPWNAEKISNHLALI------FKIASAttpppi 232
                         250       260       270
                  ....*....|....*....|....*....|....*.
gi 281359561 8211 -KYISEEAKDFIRKLLVRNKEKRMTAHECLLHPWLT 8245
Cdd:cd06630   233 pEHLSPGLRDVTLRCLELQPEDRPPARELLKHPVFT 268
Ig_Titin_like cd05748
Immunoglobulin (Ig)-like domain of titin and similar proteins; The members here are composed ...
6570-6650 2.18e-24

Immunoglobulin (Ig)-like domain of titin and similar proteins; The members here are composed of the immunoglobulin (Ig)-like domain found in titin-like proteins and similar proteins. Titin (also called connectin) is a fibrous sarcomeric protein specifically found in vertebrate striated muscle. Titin is a giant protein; depending on isoform composition, it ranges from 2970 to 3700 kDa, and is of a length that spans half a sarcomere. Titin largely consists of multiple repeats of Ig-like and fibronectin type 3 (FN-III)-like domains. Titin connects the ends of myosin thick filaments to Z disks and extends along the thick filament to the H zone. It appears to function similarly to an elastic band, keeping the myosin filaments centered in the sarcomere during muscle contraction or stretching. Within the sarcomere, titin is also attached to or is associated with myosin binding protein C (MyBP-C). MyBP-C appears to contribute to the generation of passive tension by titin and like titin has repeated Ig-like and FN-III domains. Also included in this group are worm twitchin and insect projectin, thick filament proteins of invertebrate muscle which also have repeated Ig-like and FN-III domains.


Pssm-ID: 409406 [Multi-domain]  Cd Length: 82  Bit Score: 100.36  E-value: 2.18e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 6570 IVCRAGDDFSIHVPYLAFPKPNAFWYSNDNMLDDNNRVHKHLTDDAASVVVKNSKRADSGQYRLQLKNTSGFDTATINVR 6649
Cdd:cd05748     2 IVVRAGESLRLDIPIKGRPTPTVTWSKDGQPLKETGRVQIETTASSTSLVIKNAKRSDSGKYTLTLKNSAGEKSATINVK 81

                  .
gi 281359561 6650 V 6650
Cdd:cd05748    82 V 82
PKc_PBS2_like cd06622
Catalytic domain of fungal PBS2-like dual-specificity Mitogen-Activated Protein Kinase Kinases; ...
7987-8250 2.57e-24

Catalytic domain of fungal PBS2-like dual-specificity Mitogen-Activated Protein Kinase Kinases; PKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine (ST) or tyrosine residues on protein substrates. Members of this group include the MAPKKs Polymyxin B resistance protein 2 (PBS2) from Saccharomyces cerevisiae, Wis1 from Schizosaccharomyces pombe, and related proteins. PBS2 and Wis1 are components of stress-activated MAPK cascades in budding and fission yeast, respectively. PBS2 is the specific activator of the MAPK Hog1, which plays a central role in the response of budding yeast to stress including exposure to arsenite and hyperosmotic environments. Wis1 phosphorylates and activates the MAPK Sty1 (also called Spc1 or Phh1), which stimulates a transcriptional response to a wide range of cellular insults through the bZip transcription factors Atf1, Pcr1, and Pap1. The PBS2 subfamily is part of a larger superfamily that includes the catalytic domains of STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 132953 [Multi-domain]  Cd Length: 286  Bit Score: 107.24  E-value: 2.57e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 7987 DRYDILEEIGTGAFGVVHRCRERSTGNIFAAKFIPVSHSVEK-DLIRREIDIMNQLHHQKLINLHDAFEDDDEMILILEF 8065
Cdd:cd06622     1 DEIEVLDELGKGNYGSVYKVLHRPTGVTMAMKEIRLELDESKfNQIIMELDILHKAVSPYIVDFYGAFFIEGAVYMCMEY 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 8066 LSGGELfERITAEGyVMTEAEVINYMRQIC----EGIRHMHEQ-NIIHLDIKPENIMCQTRSStnVKLIDFGLATRLDPN 8140
Cdd:cd06622    81 MDAGSL-DKLYAGG-VATEGIPEDVLRRITyavvKGLKFLKEEhNIIHRDVKPTNVLVNGNGQ--VKLCDFGVSGNLVAS 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 8141 eVVKITTGTAEFAAPEIV---NREPVGFYT---DMWATGVLSYVLLSGLSPFAGDNDVQTLKNVKA-CDWDFDVESFKYi 8213
Cdd:cd06622   157 -LAKTNIGCQSYMAPERIksgGPNQNPTYTvqsDVWSLGLSILEMALGRYPYPPETYANIFAQLSAiVDGDPPTLPSGY- 234
                         250       260       270
                  ....*....|....*....|....*....|....*..
gi 281359561 8214 SEEAKDFIRKLLVRNKEKRMTAHECLLHPWLTGDHSA 8250
Cdd:cd06622   235 SDDAQDFVAKCLNKIPNRRPTYAQLLEHPWLVKYKNA 271
STKc_EIF2AK4_GCN2_rpt2 cd14046
Catalytic domain, repeat 2, of the Serine/Threonine kinase, eukaryotic translation Initiation ...
7989-8241 2.67e-24

Catalytic domain, repeat 2, of the Serine/Threonine kinase, eukaryotic translation Initiation Factor 2-Alpha Kinase 4 or General Control Non-derepressible-2; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. GCN2 (or EIF2AK4) is activated by amino acid or serum starvation and UV irradiation. It induces GCN4, a transcriptional activator of amino acid biosynthetic genes, leading to increased production of amino acids under amino acid-deficient conditions. In serum-starved cells, GCN2 activation induces translation of the stress-responsive transcription factor ATF4, while under UV stress, GCN2 triggers transcriptional rescue via NF-kB signaling. GCN2 contains an N-terminal RWD, a degenerate kinase-like (repeat 1), the catalytic kinase (repeat 2), a histidyl-tRNA synthetase (HisRS)-like, and a C-terminal ribosome-binding and dimerization (RB/DD) domains. Its kinase domain is activated via conformational changes as a result of the binding of uncharged tRNA to the HisRS-like domain. EIF2AKs phosphorylate the alpha subunit of eIF-2, resulting in the overall downregulation of protein synthesis. The GCN2 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270948 [Multi-domain]  Cd Length: 278  Bit Score: 107.07  E-value: 2.67e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 7989 YDILEEIGTGAFGVVHRCRERSTGNIFAAKFIPV-SHSVEKDLIRREIDIMNQLHHQKLINLHDAFEDDDEMILILEFLS 8067
Cdd:cd14046     8 FEELQVLGKGAFGQVVKVRNKLDGRYYAIKKIKLrSESKNNSRILREVMLLSRLNHQHVVRYYQAWIERANLYIQMEYCE 87
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 8068 GGELFERITAEGYVMTEaEVINYMRQICEGIRHMHEQNIIHLDIKPENIMCQtrSSTNVKLIDFGLAT------RLDPNE 8141
Cdd:cd14046    88 KSTLRDLIDSGLFQDTD-RLWRLFRQILEGLAYIHSQGIIHRDLKPVNIFLD--SNGNVKIGDFGLATsnklnvELATQD 164
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 8142 VVKITT-------------GTAEFAAPEIVNREPVGF--YTDMWATGV----LSYVLLSGLSpfagdnDVQTLKNVKACD 8202
Cdd:cd14046   165 INKSTSaalgssgdltgnvGTALYVAPEVQSGTKSTYneKVDMYSLGIiffeMCYPFSTGME------RVQILTALRSVS 238
                         250       260       270
                  ....*....|....*....|....*....|....*....
gi 281359561 8203 WDFDVESFKYISEEAKDFIRKLLVRNKEKRMTAHECLLH 8241
Cdd:cd14046   239 IEFPPDFDDNKHSKQAKLIRWLLNHDPAKRPSAQELLKS 277
STKc_TSSK3-like cd14163
Catalytic domain of testis-specific serine/threonine kinase 3 and similar proteins; STKs ...
7989-8244 2.68e-24

Catalytic domain of testis-specific serine/threonine kinase 3 and similar proteins; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. TSSK proteins are almost exclusively expressed postmeiotically in the testis and play important roles in spermatogenesis and/or spermiogenesis. There are five mammalian TSSK proteins which show differences in their localization and timing of expression. TSSK3 has been reported to be expressed in the interstitial Leydig cells of adult testis. Its mRNA levels is low at birth, increases at puberty, and remains high throughout adulthood. The TSSK3-like subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271065 [Multi-domain]  Cd Length: 257  Bit Score: 106.23  E-value: 2.68e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 7989 YDILEEIGTGAFGVVHRCRERSTGNIFAAKFIPVSHSVEKDLIR---REIDIMNQLHHQKLINLHDAFEDDDEMI-LILE 8064
Cdd:cd14163     2 YQLGKTIGEGTYSKVKEAFSKKHQRKVAIKIIDKSGGPEEFIQRflpRELQIVERLDHKNIIHVYEMLESADGKIyLVME 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 8065 FLSGGELFERITAEGyVMTEAEVINYMRQICEGIRHMHEQNIIHLDIKPENIMCQTRsstNVKLIDFGLATRLDPN--EV 8142
Cdd:cd14163    82 LAEDGDVFDCVLHGG-PLPEHRAKALFRQLVEAIRYCHGCGVAHRDLKCENALLQGF---TLKLTDFGFAKQLPKGgrEL 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 8143 VKITTGTAEFAAPEIVNREPVGFYT-DMWATGVLSYVLLSGLSPFaGDNDV-----QTLKNVKacdwdfdVESFKYISEE 8216
Cdd:cd14163   158 SQTFCGSTAYAAPEVLQGVPHDSRKgDIWSMGVVLYVMLCAQLPF-DDTDIpkmlcQQQKGVS-------LPGHLGVSRT 229
                         250       260
                  ....*....|....*....|....*...
gi 281359561 8217 AKDFIRKLLVRNKEKRMTAHECLLHPWL 8244
Cdd:cd14163   230 CQDLLKRLLEPDMVLRPSIEEVSWHPWL 257
PKc_Mps1 cd14131
Catalytic domain of the Dual-specificity Mitotic checkpoint protein kinase, Monopolar spindle ...
7988-8244 3.41e-24

Catalytic domain of the Dual-specificity Mitotic checkpoint protein kinase, Monopolar spindle 1 (also called TTK); Dual-specificity PKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine as well as tyrosine residues on protein substrates. TTK/Mps1 is a spindle checkpoint kinase that was first discovered due to its necessity in centrosome duplication in budding yeast. It was later found to function in the spindle assembly checkpoint, which monitors the proper attachment of chromosomes to the mitotic spindle. In yeast, substrates of Mps1 include the spindle pole body components Spc98p, Spc110p, and Spc42p. The TTK/Mps1 subfamily is part of a larger superfamily that includes the catalytic domains of other protein serine/threonine PKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271033 [Multi-domain]  Cd Length: 271  Bit Score: 106.53  E-value: 3.41e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 7988 RYDILEEIGTGAFGVVHRCReRSTGNIFAAK---FIPVSHSVEKDLIRrEIDIMNQLHHQK-LINLHDA--FEDDDEMIL 8061
Cdd:cd14131     2 PYEILKQLGKGGSSKVYKVL-NPKKKIYALKrvdLEGADEQTLQSYKN-EIELLKKLKGSDrIIQLYDYevTDEDDYLYM 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 8062 ILEFlsgGEL-FERITAE--GYVMTEAEVINYMRQICEGIRHMHEQNIIHLDIKPENIMCqtrSSTNVKLIDFGLATRLd 8138
Cdd:cd14131    80 VMEC---GEIdLATILKKkrPKPIDPNFIRYYWKQMLEAVHTIHEEGIVHSDLKPANFLL---VKGRLKLIDFGIAKAI- 152
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 8139 PNEVVKIT----TGTAEFAAPE----------IVNREPVGFYTDMWATGVLSYVLLSGLSPFAgdNDVQTLKNVKA-CDW 8203
Cdd:cd14131   153 QNDTTSIVrdsqVGTLNYMSPEaikdtsasgeGKPKSKIGRPSDVWSLGCILYQMVYGKTPFQ--HITNPIAKLQAiIDP 230
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|..
gi 281359561 8204 DFDVEsFKYISE-EAKDFIRKLLVRNKEKRMTAHECLLHPWL 8244
Cdd:cd14131   231 NHEIE-FPDIPNpDLIDVMKRCLQRDPKKRPSIPELLNHPFL 271
STKc_MRCK_alpha cd05623
Catalytic domain of the Serine/Threonine Kinase, DMPK-related cell division control protein 42 ...
7975-8246 4.00e-24

Catalytic domain of the Serine/Threonine Kinase, DMPK-related cell division control protein 42 binding kinase (MRCK) alpha; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MRCK-alpha is expressed ubiquitously in many tissues. It plays a role in the regulation of peripheral actin reorganization and neurite outgrowth. It may also play a role in the transferrin iron uptake pathway. MRCK is activated via interaction with the small GTPase Cdc42. MRCK/Cdc42 signaling mediates myosin-dependent cell motility. The MRCK-alpha subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase. This alignment model includes the dimerization domain.


Pssm-ID: 270773 [Multi-domain]  Cd Length: 409  Bit Score: 109.33  E-value: 4.00e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 7975 PQPVEISQQSVY-DRYDILEEIGTGAFGVVHRCRERSTGNIFAAKFI---PVSHSVEKDLIRREIDIMNQLHHQKLINLH 8050
Cdd:cd05623    59 PFTSKVKQMRLHkEDFEILKVIGRGAFGEVAVVKLKNADKVFAMKILnkwEMLKRAETACFREERDVLVNGDSQWITTLH 138
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 8051 DAFEDDDEMILILEFLSGGELFERITAEGYVMTEAEVINYMRQICEGIRHMHEQNIIHLDIKPENIMCQTRSstNVKLID 8130
Cdd:cd05623   139 YAFQDDNNLYLVMDYYVGGDLLTLLSKFEDRLPEDMARFYLAEMVLAIDSVHQLHYVHRDIKPDNILMDMNG--HIRLAD 216
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 8131 FGLATRLDPNEVVK--ITTGTAEFAAPEIVN-----REPVGFYTDMWATGVLSYVLLSGLSPFAGDNDVQTLKNVKAcdw 8203
Cdd:cd05623   217 FGSCLKLMEDGTVQssVAVGTPDYISPEILQamedgKGKYGPECDWWSLGVCMYEMLYGETPFYAESLVETYGKIMN--- 293
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|..
gi 281359561 8204 dfDVESFKY------ISEEAKDFIRKLLVrNKEKRMTAH---ECLLHPWLTG 8246
Cdd:cd05623   294 --HKERFQFptqvtdVSENAKDLIRRLIC-SREHRLGQNgieDFKNHPFFVG 342
STKc_CaMKK2 cd14199
Catalytic domain of the Serine/Threonine kinase, Calmodulin Dependent Protein Kinase Kinase 2; ...
7987-8245 5.01e-24

Catalytic domain of the Serine/Threonine kinase, Calmodulin Dependent Protein Kinase Kinase 2; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. CaMKKs are upstream kinases of the CaM kinase cascade that phosphorylate and activate CaMKI and CamKIV. They may also phosphorylate other substrates including PKB and AMP-activated protein kinase (AMPK). CaMKK2, also called CaMKK beta, is one of the most versatile CaMKs. It is involved in regulating energy balance, glucose metabolism, adiposity, hematopoiesis, inflammation, and cancer. CaMKK2 contains unique N- and C-terminal domains and a central catalytic kinase domain that is followed by a regulatory domain that bears overlapping autoinhibitory and CaM-binding regions. It can be activated by signaling through G-coupled receptors, IP3 receptors, plasma membrane ion channels, and Toll-like receptors. Thus, CaMKK2 acts as a molecular hub that is capable of receiving and decoding signals from diverse pathways. The CaMKK2 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271101 [Multi-domain]  Cd Length: 286  Bit Score: 106.20  E-value: 5.01e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 7987 DRYDILEEIGTGAFGVVHRCRERSTGNIFAAKFIPvshsvEKDLIRR-------------------------------EI 8035
Cdd:cd14199     2 NQYKLKDEIGKGSYGVVKLAYNEDDNTYYAMKVLS-----KKKLMRQagfprrppprgaraapegctqprgpiervyqEI 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 8036 DIMNQLHHQKLINLHDAFED--DDEMILILEFLSGGELFERITAEGyvMTEAEVINYMRQICEGIRHMHEQNIIHLDIKP 8113
Cdd:cd14199    77 AILKKLDHPNVVKLVEVLDDpsEDHLYMVFELVKQGPVMEVPTLKP--LSEDQARFYFQDLIKGIEYLHYQKIIHRDVKP 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 8114 ENIMcqTRSSTNVKLIDFGLATRLDPNE-VVKITTGTAEFAAPEIVNREPVGFY---TDMWATGVLSYVLLSGLSPFAGD 8189
Cdd:cd14199   155 SNLL--VGEDGHIKIADFGVSNEFEGSDaLLTNTVGTPAFMAPETLSETRKIFSgkaLDVWAMGVTLYCFVFGQCPFMDE 232
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 281359561 8190 NDVQTLKNVKACDWDFDVESfkYISEEAKDFIRKLLVRNKEKRMTAHECLLHPWLT 8245
Cdd:cd14199   233 RILSLHSKIKTQPLEFPDQP--DISDDLKDLLFRMLDKNPESRISVPEIKLHPWVT 286
STKc_NDR_like_fungal cd05629
Catalytic domain of Fungal Nuclear Dbf2-Related kinase-like Serine/Threonine Kinases; STKs ...
7987-8246 9.48e-24

Catalytic domain of Fungal Nuclear Dbf2-Related kinase-like Serine/Threonine Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This group is composed of fungal NDR-like proteins including Saccharomyces cerevisiae CBK1 (or CBK1p), Schizosaccharomyces pombe Orb6 (or Orb6p), Ustilago maydis Ukc1 (or Ukc1p), and Neurospora crassa Cot1. Like NDR kinase, group members contain an N-terminal regulatory (NTR) domain and an insert within the catalytic domain that contains an auto-inhibitory sequence. CBK1 is an essential component in the RAM (regulation of Ace2p activity and cellular morphogenesis) network. CBK1 and Orb6 play similar roles in coordinating cell morphology with cell cycle progression. Ukc1 is involved in morphogenesis, pathogenicity, and pigment formation. Cot1 plays a role in polar tip extension.The fungal NDR subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270778 [Multi-domain]  Cd Length: 377  Bit Score: 107.63  E-value: 9.48e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 7987 DRYDILEEIGTGAFGVVHRCRERSTGNIFAAKFIPVSHSVEKDL---IRREIDIMNQLHHQKLINLHDAFEDDDEMILIL 8063
Cdd:cd05629     1 EDFHTVKVIGKGAFGEVRLVQKKDTGKIYAMKTLLKSEMFKKDQlahVKAERDVLAESDSPWVVSLYYSFQDAQYLYLIM 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 8064 EFLSGGELFERITAEGyVMTEAEVINYMRQICEGIRHMHEQNIIHLDIKPENIMCQTRSstNVKLIDFGLAT-------- 8135
Cdd:cd05629    81 EFLPGGDLMTMLIKYD-TFSEDVTRFYMAECVLAIEAVHKLGFIHRDIKPDNILIDRGG--HIKLSDFGLSTgfhkqhds 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 8136 --------------RLDPNEVVKI--------------------------TTGTAEFAAPEIVNREPVGFYTDMWATGVL 8175
Cdd:cd05629   158 ayyqkllqgksnknRIDNRNSVAVdsinltmsskdqiatwkknrrlmaysTVGTPDYIAPEIFLQQGYGQECDWWSLGAI 237
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 281359561 8176 SYVLLSGLSPFAGDNDVQTLKnvKACDWDfdvESFKY-----ISEEAKDFIRKLLV--RNKEKRMTAHECLLHPWLTG 8246
Cdd:cd05629   238 MFECLIGWPPFCSENSHETYR--KIINWR---ETLYFpddihLSVEAEDLIRRLITnaENRLGRGGAHEIKSHPFFRG 310
FN3 COG3401
Fibronectin type 3 domain [General function prediction only];
6905-7189 1.11e-23

Fibronectin type 3 domain [General function prediction only];


Pssm-ID: 442628 [Multi-domain]  Cd Length: 603  Bit Score: 110.48  E-value: 1.11e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 6905 FDSNDYASMYYNKSAKRDETGSYTITLTNNKGSDTASCHVTVVDRPLPPQGP--LNAYDITPDTCTLAWKTPLDDGgspI 6982
Cdd:COG3401   185 LTVTSTTLVDGGGDIEPGTTYYYRVAATDTGGESAPSNEVSVTTPTTPPSAPtgLTATADTPGSVTLSWDPVTESD---A 261
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 6983 TNYVVE-KLDNSGSWVKISSfVRNTHYDVMGLEPHYKYNFRVRAENQYGL-SDPLDIIEPIVAKhqfTVPDEPGQPKVID 7060
Cdd:COG3401   262 TGYRVYrSNSGDGPFTKVAT-VTTTSYTDTGLTNGTTYYYRVTAVDAAGNeSAPSNVVSVTTDL---TPPAAPSGLTATA 337
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 7061 WDSGNVTLIWTRPLSDGgsrIQGYQIeYRDILNDSSWNAYDYIIKDTKYQLYNLINGSEYEFRIKAKNAAGLSKPSSPSL 7140
Cdd:COG3401   338 VGSSSITLSWTASSDAD---VTGYNV-YRSTSGGGTYTKIAETVTTTSYTDTGLTPGTTYYYKVTAVDAAGNESAPSEEV 413
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*....
gi 281359561 7141 RFKlkgKFTVPSPPGAPQVTRVGKNYVDLKWEKPLRDGGSRITGYIIER 7189
Cdd:COG3401   414 SAT---TASAASGESLTASVDAVPLTDVAGATAAASAASNPGVSAAVLA 459
STKc_TNIK cd06637
Catalytic domain of the Serine/Threonine Kinase, Traf2- and Nck-Interacting Kinase; STKs ...
7989-8244 1.13e-23

Catalytic domain of the Serine/Threonine Kinase, Traf2- and Nck-Interacting Kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. TNIK is an effector of Rap2, a small GTP-binding protein from the Ras family. TNIK specifically activates the c-Jun N-terminal kinase (JNK) pathway and plays a role in regulating the actin cytoskeleton. The TNIK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270807 [Multi-domain]  Cd Length: 296  Bit Score: 105.57  E-value: 1.13e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 7989 YDILEEIGTGAFGVVHRCRERSTGNIFAAKFIPVSHSVEKDlIRREIDIMNQL-HHQKLINLHDAFED------DDEMIL 8061
Cdd:cd06637     8 FELVELVGNGTYGQVYKGRHVKTGQLAAIKVMDVTGDEEEE-IKQEINMLKKYsHHRNIATYYGAFIKknppgmDDQLWL 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 8062 ILEFLSGGELFERI-TAEGYVMTEAEVINYMRQICEGIRHMHEQNIIHLDIKPENIMCQtrSSTNVKLIDFGLATRLDPN 8140
Cdd:cd06637    87 VMEFCGAGSVTDLIkNTKGNTLKEEWIAYICREILRGLSHLHQHKVIHRDIKGQNVLLT--ENAEVKLVDFGVSAQLDRT 164
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 8141 EVVKIT-TGTAEFAAPEIV--NREP---VGFYTDMWATGVLSYVLLSGLSPFAGDNDVQTL--------KNVKACDWdfd 8206
Cdd:cd06637   165 VGRRNTfIGTPYWMAPEVIacDENPdatYDFKSDLWSLGITAIEMAEGAPPLCDMHPMRALfliprnpaPRLKSKKW--- 241
                         250       260       270
                  ....*....|....*....|....*....|....*...
gi 281359561 8207 vesfkyiSEEAKDFIRKLLVRNKEKRMTAHECLLHPWL 8244
Cdd:cd06637   242 -------SKKFQSFIESCLVKNHSQRPSTEQLMKHPFI 272
STKc_SGK3 cd05604
Catalytic domain of the Protein Serine/Threonine Kinase, Serum- and Glucocorticoid-induced ...
7992-8198 1.14e-23

Catalytic domain of the Protein Serine/Threonine Kinase, Serum- and Glucocorticoid-induced Kinase 3; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. SGK3 (also called cytokine-independent survival kinase or CISK) is expressed in most tissues and is most abundant in the embryo and adult heart and spleen. It was originally discovered in a screen for antiapoptotic genes. It phosphorylates and inhibits the proapoptotic proteins, Bad and FKHRL1. SGK3 also regulates many transporters, ion channels, and receptors. It plays a critical role in hair follicle morphogenesis and hair cycling. The SGK3 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270755 [Multi-domain]  Cd Length: 326  Bit Score: 106.20  E-value: 1.14e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 7992 LEEIGTGAFGVVHRCRERSTGNIFAAKF----IPVSHSVEKDLIRREIDIMNQLHHQKLINLHDAFEDDDEMILILEFLS 8067
Cdd:cd05604     1 LKVIGKGSFGKVLLAKRKRDGKYYAVKVlqkkVILNRKEQKHIMAERNVLLKNVKHPFLVGLHYSFQTTDKLYFVLDFVN 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 8068 GGELFERITAEGYvMTEAEVINYMRQICEGIRHMHEQNIIHLDIKPENIMCQtrSSTNVKLIDFGLATRLDPNEVVKIT- 8146
Cdd:cd05604    81 GGELFFHLQRERS-FPEPRARFYAAEIASALGYLHSINIVYRDLKPENILLD--SQGHIVLTDFGLCKEGISNSDTTTTf 157
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 281359561 8147 TGTAEFAAPEIVNREPVGFYTDMWATGVLSYVLLSGLSPFAGDNDVQTLKNV 8198
Cdd:cd05604   158 CGTPEYLAPEVIRKQPYDNTVDWWCLGSVLYEMLYGLPPFYCRDTAEMYENI 209
STKc_Sty1_Hog1 cd07856
Catalytic domain of the Serine/Threonine Kinases, Fungal Mitogen-Activated Protein Kinases ...
7985-8248 1.21e-23

Catalytic domain of the Serine/Threonine Kinases, Fungal Mitogen-Activated Protein Kinases Sty1 and Hog1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily is composed of the MAPKs Sty1 from Schizosaccharomyces pombe, Hog1 from Saccharomyces cerevisiae, and similar proteins. Sty1 and Hog1 are stress-activated MAPKs that partipate in transcriptional regulation in response to stress. Sty1 is activated in response to oxidative stress, osmotic stress, and UV radiation. It is regulated by the MAP2K Wis1, which is activated by the MAP3Ks Wis4 and Win1, which receive signals of the stress condition from membrane-spanning histidine kinases Mak1-3. Activated Sty1 stabilizes the Atf1 transcription factor and induces transcription of Atf1-dependent genes of the core environmetal stress response. Hog1 is the key element in the high osmolarity glycerol (HOG) pathway and is activated upon hyperosmotic stress. Activated Hog1 accumulates in the nucleus and regulates stress-induced transcription. The HOG pathway is mediated by two transmembrane osmosensors, Sln1 and Sho1. MAPKs are important mediators of cellular responses to extracellular signals. The Sty1/Hog1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270843 [Multi-domain]  Cd Length: 328  Bit Score: 106.12  E-value: 1.21e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 7985 VYDRYDILEEIGTGAFGVVHRCRERSTGNIFAAKFI--PVSHSVEKDLIRREIDIMNQLHHQKLINLHDAFEDDDEMILI 8062
Cdd:cd07856     8 ITTRYSDLQPVGMGAFGLVCSARDQLTGQNVAVKKImkPFSTPVLAKRTYRELKLLKHLRHENIISLSDIFISPLEDIYF 87
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 8063 LEFLSGGELFERITAEgyvMTEAEVINY-MRQICEGIRHMHEQNIIHLDIKPENIMcqTRSSTNVKLIDFGLATRLDPNE 8141
Cdd:cd07856    88 VTELLGTDLHRLLTSR---PLEKQFIQYfLYQILRGLKYVHSAGVIHRDLKPSNIL--VNENCDLKICDFGLARIQDPQM 162
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 8142 VVKITtgTAEFAAPEI-VNREPVGFYTDMWATGVLSYVLLSGLSPFAGDNDVQ------------------------TLK 8196
Cdd:cd07856   163 TGYVS--TRYYRAPEImLTWQKYDVEVDIWSAGCIFAEMLEGKPLFPGKDHVNqfsiitellgtppddvinticsenTLR 240
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 281359561 8197 NVKACDWDFDV---ESFKYISEEAKDFIRKLLVRNKEKRMTAHECLLHPWLTGDH 8248
Cdd:cd07856   241 FVQSLPKRERVpfsEKFKNADPDAIDLLEKMLVFDPKKRISAAEALAHPYLAPYH 295
PTKc cd00192
Catalytic domain of Protein Tyrosine Kinases; PTKs catalyze the transfer of the ...
7993-8200 1.25e-23

Catalytic domain of Protein Tyrosine Kinases; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. They can be classified into receptor and non-receptor tyr kinases. PTKs play important roles in many cellular processes including, lymphocyte activation, epithelium growth and maintenance, metabolism control, organogenesis regulation, survival, proliferation, differentiation, migration, adhesion, motility, and morphogenesis. Receptor tyr kinases (RTKs) are integral membrane proteins which contain an extracellular ligand-binding region, a transmembrane segment, and an intracellular tyr kinase domain. RTKs are usually activated through ligand binding, which causes dimerization and autophosphorylation of the intracellular tyr kinase catalytic domain, leading to intracellular signaling. Some RTKs are orphan receptors with no known ligands. Non-receptor (or cytoplasmic) tyr kinases are distributed in different intracellular compartments and are usually multi-domain proteins containing a catalytic tyr kinase domain as well as various regulatory domains such as SH3 and SH2. PTKs are usually autoinhibited and require a mechanism for activation. In many PTKs, the phosphorylation of tyr residues in the activation loop is essential for optimal activity. Aberrant expression of PTKs is associated with many development abnormalities and cancers.The PTK family is part of a larger superfamily that includes the catalytic domains of serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270623 [Multi-domain]  Cd Length: 262  Bit Score: 104.54  E-value: 1.25e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 7993 EEIGTGAFGVVHRCRERSTGNIF---AAKFIPVSHS-VEKDLIRREIDIMNQLHHQKLINLHDAFEDDDEMILILEFLSG 8068
Cdd:cd00192     1 KKLGEGAFGEVYKGKLKGGDGKTvdvAVKTLKEDASeSERKDFLKEARVMKKLGHPNVVRLLGVCTEEEPLYLVMEYMEG 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 8069 GEL--------FERITAEGYVMTEAEVINYMRQICEGIRHMHEQNIIHLDIKPENIMCqtrSSTN-VKLIDFGLATRLDP 8139
Cdd:cd00192    81 GDLldflrksrPVFPSPEPSTLSLKDLLSFAIQIAKGMEYLASKKFVHRDLAARNCLV---GEDLvVKISDFGLSRDIYD 157
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 281359561 8140 NEVVKITTGTAE---FAAPEIVNRepvGFYT---DMWATGVLSYVLLS-GLSPFAGDNDVQTLKNVKA 8200
Cdd:cd00192   158 DDYYRKKTGGKLpirWMAPESLKD---GIFTsksDVWSFGVLLWEIFTlGATPYPGLSNEEVLEYLRK 222
STKc_HUNK cd14070
Catalytic domain of the Serine/Threonine Kinase, Hormonally up-regulated Neu-associated kinase ...
7989-8186 1.34e-23

Catalytic domain of the Serine/Threonine Kinase, Hormonally up-regulated Neu-associated kinase (also called MAK-V); STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. HUNK/MAK-V was identified from a mammary tumor in an MMTV-neu transgenic mouse. It is required for the metastasis of c-myc-induced mammary tumors, but is not necessary for c-myc-induced primary tumor formation or normal development. It is required for HER2/neu-induced tumor formation and maintenance of the cells' tumorigenic phenotype. It is over-expressed in aggressive subsets of ovary, colon, and breast carcinomas. HUNK interacts with synaptopodin, and may also play a role in synaptic plasticity. The HUNK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270972 [Multi-domain]  Cd Length: 262  Bit Score: 104.51  E-value: 1.34e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 7989 YDILEEIGTGAFGVVHRCRERSTGNIFAAKFIPVSHS-----VEKDLiRREIDIMNQLHHQKLINLHDAFEDDDEMILIL 8063
Cdd:cd14070     4 YLIGRKLGEGSFAKVREGLHAVTGEKVAIKVIDKKKAkkdsyVTKNL-RREGRIQQMIRHPNITQLLDILETENSYYLVM 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 8064 EFLSGGELFERItAEGYVMTEAEVINYMRQICEGIRHMHEQNIIHLDIKPENIMCQtrSSTNVKLIDFGL---ATRLDPN 8140
Cdd:cd14070    83 ELCPGGNLMHRI-YDKKRLEEREARRYIRQLVSAVEHLHRAGVVHRDLKIENLLLD--ENDNIKLIDFGLsncAGILGYS 159
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*.
gi 281359561 8141 EVVKITTGTAEFAAPEIVNREPVGFYTDMWATGVLSYVLLSGLSPF 8186
Cdd:cd14070   160 DPFSTQCGSPAYAAPELLARKKYGPKVDVWSIGVNMYAMLTGTLPF 205
STKc_cPKC_alpha cd05615
Catalytic domain of the Serine/Threonine Kinase, Classical Protein Kinase C alpha; STKs ...
7989-8233 1.55e-23

Catalytic domain of the Serine/Threonine Kinase, Classical Protein Kinase C alpha; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PKC-alpha is expressed in many tissues and is associated with cell proliferation, apoptosis, and cell motility. It plays a role in the signaling of the growth factors PDGF, VEGF, EGF, and FGF. Abnormal levels of PKC-alpha have been detected in many transformed cell lines and several human tumors. In addition, PKC-alpha is required for HER2 dependent breast cancer invasion. PKCs are classified into three groups (classical, atypical, and novel) depending on their mode of activation and the structural characteristics of their regulatory domain. PKCs undergo three phosphorylations in order to take mature forms. In addition, cPKCs depend on calcium, DAG (1,2-diacylglycerol), and in most cases, phosphatidylserine (PS) for activation. The cPKC-alpha subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270766 [Multi-domain]  Cd Length: 341  Bit Score: 106.23  E-value: 1.55e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 7989 YDILEEIGTGAFGVVHRCRERSTGNIFAAKFIpvshsvEKDLIRREIDIMNQLHHQK----------LINLHDAFEDDDE 8058
Cdd:cd05615    12 FNFLMVLGKGSFGKVMLAERKGSDELYAIKIL------KKDVVIQDDDVECTMVEKRvlalqdkppfLTQLHSCFQTVDR 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 8059 MILILEFLSGGELFERITAEGYvMTEAEVINYMRQICEGIRHMHEQNIIHLDIKPENIMCQtrSSTNVKLIDFGLATRld 8138
Cdd:cd05615    86 LYFVMEYVNGGDLMYHIQQVGK-FKEPQAVFYAAEISVGLFFLHKKGIIYRDLKLDNVMLD--SEGHIKIADFGMCKE-- 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 8139 pNEVVKITT----GTAEFAAPEIVNREPVGFYTDMWATGVLSYVLLSGLSPFAGDNDVQTLKNVKacdwDFDVESFKYIS 8214
Cdd:cd05615   161 -HMVEGVTTrtfcGTPDYIAPEIIAYQPYGRSVDWWAYGVLLYEMLAGQPPFDGEDEDELFQSIM----EHNVSYPKSLS 235
                         250
                  ....*....|....*....
gi 281359561 8215 EEAKDFIRKLLVRNKEKRM 8233
Cdd:cd05615   236 KEAVSICKGLMTKHPAKRL 254
STKc_IRAK cd14066
Catalytic domain of the Serine/Threonine kinases, Interleukin-1 Receptor Associated Kinases ...
7995-8240 2.11e-23

Catalytic domain of the Serine/Threonine kinases, Interleukin-1 Receptor Associated Kinases and related STKs; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. IRAKs are involved in Toll-like receptor (TLR) and interleukin-1 (IL-1) signalling pathways, and are thus critical in regulating innate immune responses and inflammation. Some IRAKs may also play roles in T- and B-cell signaling, and adaptive immunity. Vertebrates contain four IRAKs (IRAK-1, -2, -3 (or -M), and -4) that display distinct functions and patterns of expression and subcellular distribution, and can differentially mediate TLR signaling. IRAK-1, -2, and -4 are ubiquitously expressed and are active kinases, while IRAK-M is only induced in monocytes and macrophages and is an inactive kinase. Variations in IRAK genes are linked to diverse diseases including infection, sepsis, cancer, and autoimmune diseases. IRAKs contain an N-terminal Death domain (DD), a proST region (rich in serines, prolines, and threonines), a central kinase domain (a pseudokinase domain in the case of IRAK3), and a C-terminal domain; IRAK-4 lacks the C-terminal domain. This subfamily includes plant receptor-like kinases (RLKs) including Arabidopsis thaliana BAK1 and CLAVATA1 (CLV1). BAK1 functions in BR (brassinosteroid)-regulated plant development and in pathways involved in plant resistance to pathogen infection and herbivore attack. CLV1, directly binds small signaling peptides, CLAVATA3 (CLV3) and CLAVATA3/EMBRYO SURROUNDING REGI0N (CLE), to restrict stem cell proliferation: the CLV3-CLV1-WUS (WUSCHEL) module influences stem cell maintenance in the shoot apical meristem, and the CLE40 (CLAVATA3/EMBRYO SURROUNDING REGION40) -ACR4 (CRINKLY4) -CLV1- WOX5 (WUSCHEL-RELATED HOMEOBOX5) module at the root apical meristem. The IRAK subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270968 [Multi-domain]  Cd Length: 272  Bit Score: 103.89  E-value: 2.11e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 7995 IGTGAFGVVHRCReRSTGNIFAAKFIPVS--HSVEKDLiRREIDIMNQLHHQKLINLHDAFEDDDEMILILEFLSGGELF 8072
Cdd:cd14066     1 IGSGGFGTVYKGV-LENGTVVAVKRLNEMncAASKKEF-LTELEMLGRLRHPNLVRLLGYCLESDEKLLVYEYMPNGSLE 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 8073 ERITA--EGYVMTEAEVINYMRQICEGIRHMHEQN---IIHLDIKPENIMCQtrSSTNVKLIDFGLATRLDPNEVVKITT 8147
Cdd:cd14066    79 DRLHChkGSPPLPWPQRLKIAKGIARGLEYLHEECpppIIHGDIKSSNILLD--EDFEPKLTDFGLARLIPPSESVSKTS 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 8148 ---GTAEFAAPEIVNREPVGFYTDMWATGVLSYVLLSGLSPFAGDNDVQTLKNVKacDWdfdVESFKyiSEEAKDFIRKL 8224
Cdd:cd14066   157 avkGTIGYLAPEYIRTGRVSTKSDVYSFGVVLLELLTGKPAVDENRENASRKDLV--EW---VESKG--KEELEDILDKR 229
                         250
                  ....*....|....*.
gi 281359561 8225 LVRNKEKRMTAHECLL 8240
Cdd:cd14066   230 LVDDDGVEEEEVEALL 245
STKc_CDC2L1 cd07843
Catalytic domain of the Serine/Threonine Kinase, Cell Division Cycle 2-like 1; STKs catalyze ...
7984-8243 2.31e-23

Catalytic domain of the Serine/Threonine Kinase, Cell Division Cycle 2-like 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. CDC2L1, also called PITSLRE, exists in different isoforms which are named using the alias CDK11(p). The CDC2L1 gene produces two protein products, CDK11(p110) and CDK11(p58). CDC2L1 is also represented by the caspase-processed CDK11(p46). CDK11(p110), the major isoform, associates with cyclin L and is expressed throughout the cell cycle. It is involved in RNA processing and the regulation of transcription. CDK11(p58) associates with cyclin D3 and is expressed during the G2/M phase of the cell cycle. It plays roles in spindle morphogenesis, centrosome maturation, sister chromatid cohesion, and the completion of mitosis. CDK11(p46) is formed from the larger isoforms by caspases during TNFalpha- and Fas-induced apoptosis. It functions as a downstream effector kinase in apoptotic signaling pathways and interacts with eukaryotic initiation factor 3f (eIF3f), p21-activated kinase (PAK1), and Ran-binding protein (RanBPM). CDKs belong to a large family of STKs that are regulated by their cognate cyclins. Together, they are involved in the control of cell-cycle progression, transcription, and neuronal function. The CDC2L1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 173741 [Multi-domain]  Cd Length: 293  Bit Score: 104.61  E-value: 2.31e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 7984 SVYDrYDILEEIGTGAFGVVHRCRERSTGNIFAAKFIPVSHSVEKDLIR--REIDIMNQLHHQKLINLHDAF--EDDDEM 8059
Cdd:cd07843     3 SVDE-YEKLNRIEEGTYGVVYRARDKKTGEIVALKKLKMEKEKEGFPITslREINILLKLQHPNIVTVKEVVvgSNLDKI 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 8060 ILILEF----LSGgeLFERITAEgyvMTEAEVINYMRQICEGIRHMHEQNIIHLDIKPENIMCQTRSStnVKLIDFGLAT 8135
Cdd:cd07843    82 YMVMEYvehdLKS--LMETMKQP---FLQSEVKCLMLQLLSGVAHLHDNWILHRDLKTSNLLLNNRGI--LKICDFGLAR 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 8136 RL-DP-----NEVVkittgTAEFAAPEIVNREPVgfYT---DMWATGVLSYVLLSGLSPFAGDNDVQT------------ 8194
Cdd:cd07843   155 EYgSPlkpytQLVV-----TLWYRAPELLLGAKE--YStaiDMWSVGCIFAELLTKKPLFPGKSEIDQlnkifkllgtpt 227
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 281359561 8195 ---------LKNVKACDWDFDVES-----FK--YISEEAKDFIRKLLVRNKEKRMTAHECLLHPW 8243
Cdd:cd07843   228 ekiwpgfseLPGAKKKTFTKYPYNqlrkkFPalSLSDNGFDLLNRLLTYDPAKRISAEDALKHPY 292
STKc_nPKC_eta cd05590
Catalytic domain of the Serine/Threonine Kinase, Novel Protein Kinase C eta; STKs catalyze the ...
7995-8246 2.67e-23

Catalytic domain of the Serine/Threonine Kinase, Novel Protein Kinase C eta; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PKC-eta is predominantly expressed in squamous epithelia, where it plays a crucial role in the signaling of cell-type specific differentiation. It is also expressed in pro-B cells and early-stage thymocytes, and acts as a key regulator in early B-cell development. PKC-eta increases glioblastoma multiforme (GBM) proliferation and resistance to radiation, and is being developed as a therapeutic target for the management of GBM. PKCs are classified into three groups (classical, atypical, and novel) depending on their mode of activation and the structural characteristics of their regulatory domain. nPKCs are calcium-independent, but require DAG (1,2-diacylglycerol) and phosphatidylserine (PS) for activity. The nPKC-eta subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270742 [Multi-domain]  Cd Length: 323  Bit Score: 104.99  E-value: 2.67e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 7995 IGTGAFGVVHRCRERSTGNIFAAKFIpvshsvEKDLIRREIDIMNQL----------HHQKLINLHDAFEDDDEMILILE 8064
Cdd:cd05590     3 LGKGSFGKVMLARLKESGRLYAVKVL------KKDVILQDDDVECTMtekrilslarNHPFLTQLYCCFQTPDRLFFVME 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 8065 FLSGGELFERITaEGYVMTEAEVINYMRQICEGIRHMHEQNIIHLDIKPENIMCQTRSstNVKLIDFGLATRLDPNEVVK 8144
Cdd:cd05590    77 FVNGGDLMFHIQ-KSRRFDEARARFYAAEITSALMFLHDKGIIYRDLKLDNVLLDHEG--HCKLADFGMCKEGIFNGKTT 153
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 8145 IT-TGTAEFAAPEIVNREPVGFYTDMWATGVLSYVLLSGLSPFAGDNDvqtlKNVKACDWDFDVESFKYISEEAKDFIRK 8223
Cdd:cd05590   154 STfCGTPDYIAPEILQEMLYGPSVDWWAMGVLLYEMLCGHAPFEAENE----DDLFEAILNDEVVYPTWLSQDAVDILKA 229
                         250       260
                  ....*....|....*....|....*....
gi 281359561 8224 LLVRNKEKRMTA------HECLLHPWLTG 8246
Cdd:cd05590   230 FMTKNPTMRLGSltlggeEAILRHPFFKE 258
FN3 COG3401
Fibronectin type 3 domain [General function prediction only];
6854-7237 3.33e-23

Fibronectin type 3 domain [General function prediction only];


Pssm-ID: 442628 [Multi-domain]  Cd Length: 603  Bit Score: 109.32  E-value: 3.33e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 6854 APKITSDLSIRDMTVIAGDEFRITVPYHASPRPTASWSLNGLEVIPGERIKFDSNDYAS-MYYNKSAKRDETGSYTITLT 6932
Cdd:COG3401    51 SPGTLLVAAGLSSGGGLGTGGRAGTTSGVAAVAVAAAPPTATGLTTLTGSGSVGGATNTgLTSSDEVPSPAVGTATTATA 130
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 6933 NNKGSDTASCHVTVVDRPLPPQGPLNAYDITPDTCTLAWKTPLDDGGSPITNYVVEKLDNSGSWVKIssfvrnthydvmG 7012
Cdd:COG3401   131 VAGGAATAGTYALGAGLYGVDGANASGTTASSVAGAGVVVSPDTSATAAVATTSLTVTSTTLVDGGG------------D 198
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 7013 LEPHYKYNFRVRAENQYGLSDPLDIIEPIVAKhqfTVPDEPGQPKVIDWDSGNVTLIWTrplSDGGSRIQGYQIeYRDIL 7092
Cdd:COG3401   199 IEPGTTYYYRVAATDTGGESAPSNEVSVTTPT---TPPSAPTGLTATADTPGSVTLSWD---PVTESDATGYRV-YRSNS 271
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 7093 NDSSWNAYDYIiKDTKYQLYNLINGSEYEFRIKAKNAAGL-SKPSSPSlrfKLKGKFTVPSPPGAPQVTRVGKNYVDLKW 7171
Cdd:COG3401   272 GDGPFTKVATV-TTTSYTDTGLTNGTTYYYRVTAVDAAGNeSAPSNVV---SVTTDLTPPAAPSGLTATAVGSSSITLSW 347
                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 281359561 7172 EKPLrdgGSRITGYIIERRDIGGAVWVKCNDyNVLDTEYTVMNLIEMGDYEFRVFAVNSAGR-SEPS 7237
Cdd:COG3401   348 TASS---DADVTGYNVYRSTSGGGTYTKIAE-TVTTTSYTDTGLTPGTTYYYKVTAVDAAGNeSAPS 410
STKc_MAP4K4_6_N cd06636
N-terminal Catalytic domain of the Serine/Threonine Kinases, Mitogen-Activated Protein Kinase ...
7989-8244 5.09e-23

N-terminal Catalytic domain of the Serine/Threonine Kinases, Mitogen-Activated Protein Kinase Kinase Kinase Kinase 4 and 6; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Members of this subfamily contain an N-terminal catalytic domain and a C-terminal citron homology (CNH) regulatory domain. MAP4K4 is also called Nck Interacting kinase (NIK). It facilitates the activation of the MAPKs, extracellular signal-regulated kinase (ERK) 1, ERK2, and c-Jun N-terminal kinase (JNK), by phosphorylating and activating MEKK1. MAP4K4 plays a role in tumor necrosis factor (TNF) alpha-induced insulin resistance. MAP4K4 silencing in skeletal muscle cells from type II diabetic patients restores insulin-mediated glucose uptake. MAP4K4, through JNK, also plays a broad role in cell motility, which impacts inflammation, homeostasis, as well as the invasion and spread of cancer. MAP4K4 is found to be highly expressed in most tumor cell lines relative to normal tissue. MAP4K6 (also called MINK for Misshapen/NIKs-related kinase) is activated after Ras induction and mediates activation of p38 MAPK. MAP4K6 plays a role in cell cycle arrest, cytoskeleton organization, cell adhesion, and cell motility. The MAP4K4/6 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270806 [Multi-domain]  Cd Length: 282  Bit Score: 103.16  E-value: 5.09e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 7989 YDILEEIGTGAFGVVHRCRERSTGNIFAAKFIPVSHSVEKDlIRREIDIMNQL-HHQKLINLHDAF------EDDDEMIL 8061
Cdd:cd06636    18 FELVEVVGNGTYGQVYKGRHVKTGQLAAIKVMDVTEDEEEE-IKLEINMLKKYsHHRNIATYYGAFikksppGHDDQLWL 96
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 8062 ILEFLSGGELFERI-TAEGYVMTEAEVINYMRQICEGIRHMHEQNIIHLDIKPENIMCQtrSSTNVKLIDFGLATRLDPN 8140
Cdd:cd06636    97 VMEFCGAGSVTDLVkNTKGNALKEDWIAYICREILRGLAHLHAHKVIHRDIKGQNVLLT--ENAEVKLVDFGVSAQLDRT 174
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 8141 EVVKIT-TGTAEFAAPEIV--NREPVGFY---TDMWATGVLSYVLLSGLSPFAGDNDVQTL--------KNVKACDWdfd 8206
Cdd:cd06636   175 VGRRNTfIGTPYWMAPEVIacDENPDATYdyrSDIWSLGITAIEMAEGAPPLCDMHPMRALfliprnppPKLKSKKW--- 251
                         250       260       270
                  ....*....|....*....|....*....|....*...
gi 281359561 8207 veSFKYIseeakDFIRKLLVRNKEKRMTAHECLLHPWL 8244
Cdd:cd06636   252 --SKKFI-----DFIEGCLVKNYLSRPSTEQLLKHPFI 282
PKc_DYRK cd14210
Catalytic domain of the protein kinase, Dual-specificity tYrosine-phosphorylated and ...
7988-8244 5.70e-23

Catalytic domain of the protein kinase, Dual-specificity tYrosine-phosphorylated and -Regulated Kinase; Protein Kinases (PKs), Dual-specificity tYrosine-phosphorylated and -Regulated Kinase (DYRK) subfamily, catalytic (c) domain. Dual-specificity PKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine (S/T) as well as tyrosine residues on protein substrates. The DYRK subfamily is part of a larger superfamily that includes the catalytic domains of other protein S/T PKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase (PI3K). DYRKs autophosphorylate themselves on tyrosine residues and phosphorylate their substrates exclusively on S/T residues. They play important roles in cell proliferation, differentiation, survival, and development. Vertebrates contain multiple DYRKs (DYRK1-4) and mammals contain two types of DYRK1 proteins, DYRK1A and DYRK1B. DYRK1A is involved in neuronal differentiation and is implicated in the pathogenesis of DS (Down syndrome). DYRK1B plays a critical role in muscle differentiation by regulating transcription, cell motility, survival, and cell cycle progression. It is overexpressed in many solid tumors where it acts as a tumor survival factor. DYRK2 promotes apoptosis in response to DNA damage by phosphorylating the tumor suppressor p53, while DYRK3 promotes cell survival by phosphorylating SIRT1 and promoting p53 deacetylation. DYRK4 is a testis-specific kinase that may function during spermiogenesis.


Pssm-ID: 271112 [Multi-domain]  Cd Length: 311  Bit Score: 103.78  E-value: 5.70e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 7988 RYDILEEIGTGAFGVVHRCRERSTGNIFAAKFIpvshsveKDLIR------REIDIMNQLHHQK------LINLHDAFED 8055
Cdd:cd14210    14 RYEVLSVLGKGSFGQVVKCLDHKTGQLVAIKII-------RNKKRfhqqalVEVKILKHLNDNDpddkhnIVRYKDSFIF 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 8056 DDEMILILEFLSGgELFERITAEGYVMTEAEVINYM-RQICEGIRHMHEQNIIHLDIKPENIMCQTRSSTNVKLIDFG-- 8132
Cdd:cd14210    87 RGHLCIVFELLSI-NLYELLKSNNFQGLSLSLIRKFaKQILQALQFLHKLNIIHCDLKPENILLKQPSKSSIKVIDFGss 165
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 8133 ----------LATRLdpnevvkittgtaeFAAPEIVNREPVGFYTDMWATGVLSYVLLSGLSPFAGDN------------ 8190
Cdd:cd14210   166 cfegekvytyIQSRF--------------YRAPEVILGLPYDTAIDMWSLGCILAELYTGYPLFPGENeeeqlacimevl 231
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 8191 ---DVQTLKNVKACDWDFDvESFK---YISEEAK---------------------DFIRKLLVRNKEKRMTAHECLLHPW 8243
Cdd:cd14210   232 gvpPKSLIDKASRRKKFFD-SNGKprpTTNSKGKkrrpgskslaqvlkcddpsflDFLKKCLRWDPSERMTPEEALQHPW 310

                  .
gi 281359561 8244 L 8244
Cdd:cd14210   311 I 311
FN3 cd00063
Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein ...
6359-6451 6.78e-23

Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein fibronectin. Its tenth fibronectin type III repeat contains an RGD cell recognition sequence in a flexible loop between 2 strands. Approximately 2% of all animal proteins contain the FN3 repeat; including extracellular and intracellular proteins, membrane spanning cytokine receptors, growth hormone receptors, tyrosine phosphatase receptors, and adhesion molecules. FN3-like domains are also found in bacterial glycosyl hydrolases.


Pssm-ID: 238020 [Multi-domain]  Cd Length: 93  Bit Score: 96.41  E-value: 6.78e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 6359 PGAPSQPTISAYTPNSANLEWHPPDDCGGkPITGYIVERRERG-GEWIKCNNYPTPNTSYTVSNLRDGARYEFRVLAVNE 6437
Cdd:cd00063     1 PSPPTNLRVTDVTSTSVTLSWTPPEDDGG-PITGYVVEYREKGsGDWKEVEVTPGSETSYTLTGLKPGTEYEFRVRAVNG 79
                          90
                  ....*....|....
gi 281359561 6438 AGPGHPSKPSDPMT 6451
Cdd:cd00063    80 GGESPPSESVTVTT 93
STKc_Nek6 cd08228
Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase ...
7989-8203 6.92e-23

Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase 6; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Nek6 is required for the transition from metaphase to anaphase. It also plays important roles in mitotic spindle formation and cytokinesis. Activated by Nek9 during mitosis, Nek6 phosphorylates Eg5, a kinesin that is important for spindle bipolarity. Nek6 localizes to spindle microtubules during metaphase and anaphase, and to the midbody during cytokinesis. It is one in a family of 11 different Neks (Nek1-11) that are involved in cell cycle control. The Nek family is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270865 [Multi-domain]  Cd Length: 268  Bit Score: 102.41  E-value: 6.92e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 7989 YDILEEIGTGAFGVVHRCRERSTGNIFAAK----FIPVSHSVEKDLIRrEIDIMNQLHHQKLINLHDAFEDDDEMILILE 8064
Cdd:cd08228     4 FQIEKKIGRGQFSEVYRATCLLDRKPVALKkvqiFEMMDAKARQDCVK-EIDLLKQLNHPNVIKYLDSFIEDNELNIVLE 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 8065 FLSGGELFERIT---AEGYVMTEAEVINYMRQICEGIRHMHEQNIIHLDIKPENIMcqTRSSTNVKLIDFGLAtRLDPNE 8141
Cdd:cd08228    83 LADAGDLSQMIKyfkKQKRLIPERTVWKYFVQLCSAVEHMHSRRVMHRDIKPANVF--ITATGVVKLGDLGLG-RFFSSK 159
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 281359561 8142 VVKITT--GTAEFAAPEIVNREPVGFYTDMWATGVLSYVLLSGLSPFAGD--NDVQTLKNVKACDW 8203
Cdd:cd08228   160 TTAAHSlvGTPYYMSPERIHENGYNFKSDIWSLGCLLYEMAALQSPFYGDkmNLFSLCQKIEQCDY 225
STKc_cPKC cd05587
Catalytic domain of the Serine/Threonine Kinase, Classical (or Conventional) Protein Kinase C; ...
7995-8233 6.96e-23

Catalytic domain of the Serine/Threonine Kinase, Classical (or Conventional) Protein Kinase C; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. cPKCs are potent kinases for histones, myelin basic protein, and protamine. They depend on calcium, DAG (1,2-diacylglycerol), and in most cases, phosphatidylserine (PS) for activation. cPKCs contain a calcium-binding C2 region in their regulatory domain. There are four cPKC isoforms, named alpha, betaI, betaII, and gamma. PKC-gamma is mainly expressed in neuronal tissues. It plays a role in protection from ischemia. PKCs are classified into three groups (classical, atypical, and novel) depending on their mode of activation and the structural characteristics of their regulatory domain. The cPKC subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270739 [Multi-domain]  Cd Length: 320  Bit Score: 104.01  E-value: 6.96e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 7995 IGTGAFGVVHRCRERSTGNIFAAKFIpvshsvEKDLIRREIDIMNQLHHQK----------LINLHDAFEDDDEMILILE 8064
Cdd:cd05587     4 LGKGSFGKVMLAERKGTDELYAIKIL------KKDVIIQDDDVECTMVEKRvlalsgkppfLTQLHSCFQTMDRLYFVME 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 8065 FLSGGELFERITAEGYvMTEAEVINYMRQICEGIRHMHEQNIIHLDIKPENIMCQtrSSTNVKLIDFGLAT-RLDPNEVV 8143
Cdd:cd05587    78 YVNGGDLMYHIQQVGK-FKEPVAVFYAAEIAVGLFFLHSKGIIYRDLKLDNVMLD--AEGHIKIADFGMCKeGIFGGKTT 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 8144 KITTGTAEFAAPEIVNREPVGFYTDMWATGVLSYVLLSGLSPFAGDNDVQTLKNVKacdwDFDVESFKYISEEAKDFIRK 8223
Cdd:cd05587   155 RTFCGTPDYIAPEIIAYQPYGKSVDWWAYGVLLYEMLAGQPPFDGEDEDELFQSIM----EHNVSYPKSLSKEAVSICKG 230
                         250
                  ....*....|
gi 281359561 8224 LLVRNKEKRM 8233
Cdd:cd05587   231 LLTKHPAKRL 240
STKc_Nek11 cd08222
Catalytic domain of the Protein Serine/Threonine Kinase, Never In Mitosis gene A (NIMA) ...
7988-8244 7.95e-23

Catalytic domain of the Protein Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase 11; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Nek11 is involved, through direct phosphorylation, in regulating the degradation of Cdc25A (Cell Division Cycle 25 homolog A), which plays a role in cell cycle progression and in activating cyclin dependent kinases. Nek11 is activated by CHK1 (CHeckpoint Kinase 1) and may be involved in the G2/M checkpoint. Nek11 may also play a role in the S-phase checkpoint as well as in DNA replication and genotoxic stress responses. It is one in a family of 11 different Neks (Nek1-11) that are involved in cell cycle control. The Nek family is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270861 [Multi-domain]  Cd Length: 260  Bit Score: 102.12  E-value: 7.95e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 7988 RYDILEEIGTGAFGVVHRCRERST---GNIFAAKFIPVSHSVEKDLIR--REIDIMNQLHHQKLINLHDAFEDDDEMILI 8062
Cdd:cd08222     1 RYRVVRKLGSGNFGTVYLVSDLKAtadEELKVLKEISVGELQPDETVDanREAKLLSKLDHPAIVKFHDSFVEKESFCIV 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 8063 LEFLSGGELFERITA---EGYVMTEAEVINYMRQICEGIRHMHEQNIIHLDIKPENIMCQtrsSTNVKLIDFGLATRLDP 8139
Cdd:cd08222    81 TEYCEGGDLDDKISEykkSGTTIDENQILDWFIQLLLAVQYMHERRILHRDLKAKNIFLK---NNVIKVGDFGISRILMG 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 8140 NEVVKIT-TGTAEFAAPEIVNREPVGFYTDMWATGVLSYVLLSGLSPFAGdndvQTLKNV--KACDWDFDVESFKYiSEE 8216
Cdd:cd08222   158 TSDLATTfTGTPYYMSPEVLKHEGYNSKSDIWSLGCILYEMCCLKHAFDG----QNLLSVmyKIVEGETPSLPDKY-SKE 232
                         250       260
                  ....*....|....*....|....*...
gi 281359561 8217 AKDFIRKLLVRNKEKRMTAHECLLHPWL 8244
Cdd:cd08222   233 LNAIYSRMLNKDPALRPSAAEILKIPFI 260
STKc_nPKC_delta cd05620
Catalytic domain of the Serine/Threonine Kinase, Novel Protein Kinase C delta; STKs catalyze ...
7995-8285 8.39e-23

Catalytic domain of the Serine/Threonine Kinase, Novel Protein Kinase C delta; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PKC-delta plays a role in cell cycle regulation and programmed cell death in many cell types. It slows down cell proliferation, inducing cell cycle arrest and enhancing cell differentiation. PKC-delta is also involved in the regulation of transcription as well as immune and inflammatory responses. It plays a central role in the genotoxic stress response that leads to DNA damaged-induced apoptosis. PKCs are classified into three groups (classical, atypical, and novel) depending on their mode of activation and the structural characteristics of their regulatory domain. nPKCs are calcium-independent, but require DAG (1,2-diacylglycerol) and phosphatidylserine (PS) for activity. The nPKC-delta subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 173710 [Multi-domain]  Cd Length: 316  Bit Score: 103.49  E-value: 8.39e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 7995 IGTGAFGVVHRCRERSTGNIFAAKfipvshSVEKDLIRREIDIMNQLHHQK----------LINLHDAFEDDDEMILILE 8064
Cdd:cd05620     3 LGKGSFGKVLLAELKGKGEYFAVK------ALKKDVVLIDDDVECTMVEKRvlalawenpfLTHLYCTFQTKEHLFFVME 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 8065 FLSGGELFERITAEG-YVMTEAEVinYMRQICEGIRHMHEQNIIHLDIKPENIMCQtrSSTNVKLIDFGLATRLDPNEVV 8143
Cdd:cd05620    77 FLNGGDLMFHIQDKGrFDLYRATF--YAAEIVCGLQFLHSKGIIYRDLKLDNVMLD--RDGHIKIADFGMCKENVFGDNR 152
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 8144 KIT-TGTAEFAAPEIVNREPVGFYTDMWATGVLSYVLLSGLSPFAGDNDVQTLKNVKAcdwdfDVESF-KYISEEAKDFI 8221
Cdd:cd05620   153 ASTfCGTPDYIAPEILQGLKYTFSVDWWSFGVLLYEMLIGQSPFHGDDEDELFESIRV-----DTPHYpRWITKESKDIL 227
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 281359561 8222 RKLLVRNKEKRM-TAHECLLHPWLTGDHSAMKQEINRDRYLAYREKLRRKYEDFER-FLLPIGRLS 8285
Cdd:cd05620   228 EKLFERDPTRRLgVVGNIRGHPFFKTINWTALEKRELDPPFKPKVKSPSDYSNFDReFLSEKPRLS 293
STKc_CDK2_3 cd07860
Catalytic domain of the Serine/Threonine Kinases, Cyclin-Dependent protein Kinase 2 and 3; ...
7992-8243 9.95e-23

Catalytic domain of the Serine/Threonine Kinases, Cyclin-Dependent protein Kinase 2 and 3; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. CDK2 is regulated by cyclin E or cyclin A. Upon activation by cyclin E, it phosphorylates the retinoblastoma (pRb) protein which activates E2F mediated transcription and allows cells to move into S phase. The CDK2/cyclin A complex plays a role in regulating DNA replication. CDK2, together with CDK4, also regulates embryonic cell proliferation. Despite these important roles, mice deleted for the cdk2 gene are viable and normal except for being sterile. This may be due to compensation provided by CDK1 (also called Cdc2), which can also bind cyclin E and drive the G1 to S phase transition. CDK3 is regulated by cyclin C and it phosphorylates pRB specifically during the G0/G1 transition. This phosphorylation is required for cells to exit G0 efficiently and enter the G1 phase. CDKs belong to a large family of STKs that are regulated by their cognate cyclins. Together, they are involved in the control of cell-cycle progression, transcription, and neuronal function. The CDK2/3 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270844 [Multi-domain]  Cd Length: 284  Bit Score: 102.58  E-value: 9.95e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 7992 LEEIGTGAFGVVHRCRERSTGNIFAAKFIPV---SHSVEKDLIRrEIDIMNQLHHQKLINLHDAFEDDDEMILILEFLSG 8068
Cdd:cd07860     5 VEKIGEGTYGVVYKARNKLTGEVVALKKIRLdteTEGVPSTAIR-EISLLKELNHPNIVKLLDVIHTENKLYLVFEFLHQ 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 8069 G-ELFERITAEGYVMTeAEVINYMRQICEGIRHMHEQNIIHLDIKPENIMCQTRSStnVKLIDFGLA------TRLDPNE 8141
Cdd:cd07860    84 DlKKFMDASALTGIPL-PLIKSYLFQLLQGLAFCHSHRVLHRDLKPQNLLINTEGA--IKLADFGLArafgvpVRTYTHE 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 8142 VVkittgTAEFAAPEIVnrepVG--FYT---DMWATGVLSYVLLSGLSPFAGDND---------------------VQTL 8195
Cdd:cd07860   161 VV-----TLWYRAPEIL----LGckYYStavDIWSLGCIFAEMVTRRALFPGDSEidqlfrifrtlgtpdevvwpgVTSM 231
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|..
gi 281359561 8196 KNVKACDWDFDVESFKYI----SEEAKDFIRKLLVRNKEKRMTAHECLLHPW 8243
Cdd:cd07860   232 PDYKPSFPKWARQDFSKVvpplDEDGRDLLSQMLHYDPNKRISAKAALAHPF 283
STKc_Nek4 cd08223
Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase ...
7988-8244 1.20e-22

Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase 4; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Nek4 is highly abundant in the testis. Its specific function is unknown. Neks are involved in the regulation of downstream processes following the activation of Cdc2, and many of their functions are cell cycle-related. They play critical roles in microtubule dynamics during ciliogenesis and mitosis. Nek4 is one in a family of 11 different Neks (Nek1-11). The Nek family is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270862 [Multi-domain]  Cd Length: 257  Bit Score: 101.36  E-value: 1.20e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 7988 RYDILEEIGTGAFGVVHRCRERSTGNIFAAKFIPVSHSV--EKDLIRREIDIMNQLHHQKLINLHDAFEDDDEMILI-LE 8064
Cdd:cd08223     1 EYQFLRVIGKGSYGEVWLVRHKRDRKQYVIKKLNLKNASkrERKAAEQEAKLLSKLKHPNIVSYKESFEGEDGFLYIvMG 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 8065 FLSGGELFERITAE-GYVMTEAEVINYMRQICEGIRHMHEQNIIHLDIKPENIMCqTRSSTnVKLIDFGLATRLD-PNEV 8142
Cdd:cd08223    81 FCEGGDLYTRLKEQkGVLLEERQVVEWFVQIAMALQYMHERNILHRDLKTQNIFL-TKSNI-IKVGDLGIARVLEsSSDM 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 8143 VKITTGTAEFAAPEIVNREPVGFYTDMWATGVLSYvllsglspfagdnDVQTLK---NVKacdwDFDVESFKYI------ 8213
Cdd:cd08223   159 ATTLIGTPYYMSPELFSNKPYNHKSDVWALGCCVY-------------EMATLKhafNAK----DMNSLVYKILegklpp 221
                         250       260       270
                  ....*....|....*....|....*....|....*.
gi 281359561 8214 -----SEEAKDFIRKLLVRNKEKRMTAHECLLHPWL 8244
Cdd:cd08223   222 mpkqySPELGELIKAMLHQDPEKRPSVKRILRQPYI 257
I-set pfam07679
Immunoglobulin I-set domain;
3494-3590 1.25e-22

Immunoglobulin I-set domain;


Pssm-ID: 400151 [Multi-domain]  Cd Length: 90  Bit Score: 95.79  E-value: 1.25e-22
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561  3494 PRFLKPhidrvnLKPVIVKTGLSISLDINIRGEPAPKVEWFFNNSSVTSDEHsVKIDNVDYNTKFFVMRAQRSQSGKYII 3573
Cdd:pfam07679    1 PKFTQK------PKDVEVQEGESARFTCTVTGTPDPEVSWFKDGQPLRSSDR-FKVTYEGGTYTLTISNVQPDDSGKYTC 73
                           90
                   ....*....|....*..
gi 281359561  3574 KATNEVGEDEAELEVTV 3590
Cdd:pfam07679   74 VATNSAGEAEASAELTV 90
STKc_ERK5 cd07855
Catalytic domain of the Serine/Threonine Kinase, Extracellular signal-Regulated Kinase 5; ...
7985-8250 1.37e-22

Catalytic domain of the Serine/Threonine Kinase, Extracellular signal-Regulated Kinase 5; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. ERK5 (also called Big MAPK1 (BMK1) or MAPK7) has a unique C-terminal extension, making it approximately twice as big as other MAPKs. This extension contains transcriptional activation capability which is inhibited by the N-terminal half. ERK5 is activated in response to growth factors and stress by a cascade that leads to its phosphorylation by the MAP2K MEK5, which in turn is regulated by the MAP3Ks MEKK2 and MEKK3. Activated ERK5 phosphorylates its targets including myocyte enhancer factor 2 (MEF2), Sap1a, c-Myc, and RSK. It plays a role in EGF-induced cell proliferation during the G1/S phase transition. Studies on knockout mice revealed that ERK5 is essential for cardiovascular development and plays an important role in angiogenesis. It is also critical for neural differentiation and survival. The ERK5 pathway has been implicated in the pathogenesis of many diseases including cancer, cardiac hypertrophy, and atherosclerosis. MAPKs are important mediators of cellular responses to extracellular signals. The ERK5 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270842 [Multi-domain]  Cd Length: 336  Bit Score: 103.21  E-value: 1.37e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 7985 VYDRYDILEEIGTGAFGVVHRCRERSTGNIFAAKFIPVSHSVEKDLIR--REIDIMNQLHHQKLINLHDAF------EDD 8056
Cdd:cd07855     3 VGDRYEPIETIGSGAYGVVCSAIDTKSGQKVAIKKIPNAFDVVTTAKRtlRELKILRHFKHDNIIAIRDILrpkvpyADF 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 8057 DEMILILEFLSGGelFERITAEGYVMTEAEVINYMRQICEGIRHMHEQNIIHLDIKPENIMcqTRSSTNVKLIDFGLATR 8136
Cdd:cd07855    83 KDVYVVLDLMESD--LHHIIHSDQPLTLEHIRYFLYQLLRGLKYIHSANVIHRDLKPSNLL--VNENCELKIGDFGMARG 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 8137 LDPNEVVKITTGTAEFA-----APEIVNREPVgfYT---DMWATGVL--------------SYV-----LLSGLSPFAGD 8189
Cdd:cd07855   159 LCTSPEEHKYFMTEYVAtrwyrAPELMLSLPE--YTqaiDMWSVGCIfaemlgrrqlfpgkNYVhqlqlILTVLGTPSQA 236
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 281359561 8190 -----------NDVQTLKNVKACDWDfdvESFKYISEEAKDFIRKLLVRNKEKRMTAHECLLHPWLTGDHSA 8250
Cdd:cd07855   237 vinaigadrvrRYIQNLPNKQPVPWE---TLYPKADQQALDLLSQMLRFDPSERITVAEALQHPFLAKYHDP 305
STKc_ROCK2 cd05621
Catalytic domain of the Serine/Threonine Kinase, Rho-associated coiled-coil containing protein ...
7960-8248 1.39e-22

Catalytic domain of the Serine/Threonine Kinase, Rho-associated coiled-coil containing protein kinase 2; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. ROCK2 was the first identified target of activated RhoA, and was found to play a role in stress fiber and focal adhesion formation. It is prominently expressed in the brain, heart, and skeletal muscles. It is implicated in vascular and neurological disorders, such as hypertension and vasospasm of the coronary and cerebral arteries. ROCK2 is also activated by caspase-2 cleavage, resulting in thrombin-induced microparticle generation in response to cell activation. Mice deficient in ROCK2 show intrauterine growth retardation and embryonic lethality because of placental dysfunction. ROCK contains an N-terminal extension, a catalytic kinase domain, and a C-terminal extension, which contains a coiled-coil region encompassing a Rho-binding domain (RBD) and a pleckstrin homology (PH) domain. ROCK is auto-inhibited by the RBD and PH domain interacting with the catalytic domain, and is activated via interaction with Rho GTPases. The ROCK2 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270771 [Multi-domain]  Cd Length: 379  Bit Score: 104.31  E-value: 1.39e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 7960 KDYDSYVfDIYSKFVPQPVEISQQSvyDRYDILEEIGTGAFGVVHRCRERSTGNIFAAKFIPVSHSVEKD---LIRREID 8036
Cdd:cd05621    28 KNIDNFL-NRYEKIVNKIRELQMKA--EDYDVVKVIGRGAFGEVQLVRHKASQKVYAMKLLSKFEMIKRSdsaFFWEERD 104
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 8037 IMNQLHHQKLINLHDAFEDDDEMILILEFLSGGELFERITaeGYVMTEAEVINYMRQICEGIRHMHEQNIIHLDIKPENI 8116
Cdd:cd05621   105 IMAFANSPWVVQLFCAFQDDKYLYMVMEYMPGGDLVNLMS--NYDVPEKWAKFYTAEVVLALDAIHSMGLIHRDVKPDNM 182
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 8117 MCQTRSstNVKLIDFGLATRLDPNEVVKITT--GTAEFAAPEIVNRE-PVGFY---TDMWATGVLSYVLLSGLSPFAGDN 8190
Cdd:cd05621   183 LLDKYG--HLKLADFGTCMKMDETGMVHCDTavGTPDYISPEVLKSQgGDGYYgreCDWWSVGVFLFEMLVGDTPFYADS 260
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 281359561 8191 DVQTLKNV----KACDWDFDVEsfkyISEEAKDFIRKLLVrNKEKRM---TAHECLLHPWLTGDH 8248
Cdd:cd05621   261 LVGTYSKImdhkNSLNFPDDVE----ISKHAKNLICAFLT-DREVRLgrnGVEEIKQHPFFRNDQ 320
STKc_CDK10 cd07845
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 10; STKs ...
7989-8243 1.40e-22

Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 10; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. CDK10, also called PISSLRE, is essential for cell growth and proliferation, and acts through the G2/M phase of the cell cycle. CDK10 has also been identified as an important factor in endocrine therapy resistance in breast cancer. CDK10 silencing increases the transcription of c-RAF and the activation of the p42/p44 MAPK pathway, which leads to antiestrogen resistance. Patients who express low levels of CDK10 relapse early on tamoxifen. CDKs belong to a large family of STKs that are regulated by their cognate cyclins. Together, they are involved in the control of cell-cycle progression, transcription, and neuronal function. The CDK10 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 173742 [Multi-domain]  Cd Length: 309  Bit Score: 102.83  E-value: 1.40e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 7989 YDILEEIGTGAFGVVHRCRERSTGNIFAAKfiPVSHSVEKDLIR----REIDIMNQLHHQKLINLHDAFEDD--DEMILI 8062
Cdd:cd07845     9 FEKLNRIGEGTYGIVYRARDTTSGEIVALK--KVRMDNERDGIPisslREITLLLNLRHPNIVELKEVVVGKhlDSIFLV 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 8063 LEFLSG--GELFERITAEgyvMTEAEVINYMRQICEGIRHMHEQNIIHLDIKPENIMCQTRSStnVKLIDFGLATRL-DP 8139
Cdd:cd07845    87 MEYCEQdlASLLDNMPTP---FSESQVKCLMLQLLRGLQYLHENFIIHRDLKVSNLLLTDKGC--LKIADFGLARTYgLP 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 8140 NEVVKITTGTAEFAAPEIVnrepVGF--YT---DMWATGVLSYVLLSGLSPFAGDNDVQTLK------------------ 8196
Cdd:cd07845   162 AKPMTPKVVTLWYRAPELL----LGCttYTtaiDMWAVGCILAELLAHKPLLPGKSEIEQLDliiqllgtpnesiwpgfs 237
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 281359561 8197 --------NVKACDWDFDVESFKYISEEAKDFIRKLLVRNKEKRMTAHECLLHPW 8243
Cdd:cd07845   238 dlplvgkfTLPKQPYNNLKHKFPWLSEAGLRLLNFLLMYDPKKRATAEEALESSY 292
STKc_PIM2 cd14101
Catalytic domain of the Serine/Threonine kinase, Proviral Integration Moloney virus (PIM) ...
7995-8244 1.42e-22

Catalytic domain of the Serine/Threonine kinase, Proviral Integration Moloney virus (PIM) kinase 2; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The PIM gene locus was discovered as a result of the cloning of retroviral intergration sites in murine Moloney leukemia virus, leading to the identification of PIM kinases. They are constitutively active STKs with a broad range of cellular targets and are overexpressed in many haematopoietic malignancies and solid cancers. Vertebrates contain three distinct PIM kinase genes (PIM1-3); each gene may result in mutliple protein isoforms. There are three PIM2 isoforms resulting from alternative translation initiation sites. PIM2 is highly expressed in leukemia and lymphomas and has been shown to promote the survival and proliferation of tumor cells. The PIM2 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271003 [Multi-domain]  Cd Length: 257  Bit Score: 101.08  E-value: 1.42e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 7995 IGTGAFGVVHRCRERSTGNIFAAKFIPVSHSVE------KDLIRREIDIMNQL----HHQKLINLHDAFEDDDEMILILE 8064
Cdd:cd14101     8 LGKGGFGTVYAGHRISDGLQVAIKQISRNRVQQwsklpgVNPVPNEVALLQSVgggpGHRGVIRLLDWFEIPEGFLLVLE 87
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 8065 F-LSGGELFERITAEGyVMTEAEVINYMRQICEGIRHMHEQNIIHLDIKPENIMCQTRSStNVKLIDFGLATRLDpNEVV 8143
Cdd:cd14101    88 RpQHCQDLFDYITERG-ALDESLARRFFKQVVEAVQHCHSKGVVHRDIKDENILVDLRTG-DIKLIDFGSGATLK-DSMY 164
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 8144 KITTGTAEFAAPEIVNREPV-GFYTDMWATGVLSYVLLSGLSPFAGDNDVqtlknVKAcdwdfDVESFKYISEEAKDFIR 8222
Cdd:cd14101   165 TDFDGTRVYSPPEWILYHQYhALPATVWSLGILLYDMVCGDIPFERDTDI-----LKA-----KPSFNKRVSNDCRSLIR 234
                         250       260
                  ....*....|....*....|..
gi 281359561 8223 KLLVRNKEKRMTAHECLLHPWL 8244
Cdd:cd14101   235 SCLAYNPSDRPSLEQILLHPWM 256
STKc_IKK_beta cd14038
Catalytic domain of the Serine/Threonine kinase, Inhibitor of Nuclear Factor-KappaB Kinase ...
7995-8186 1.63e-22

Catalytic domain of the Serine/Threonine kinase, Inhibitor of Nuclear Factor-KappaB Kinase (IKK) beta; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. IKKbeta is involved in the classical pathway of regulating Nuclear Factor-KappaB (NF-kB) proteins, a family of transcription factors which are critical in many cellular functions including inflammatory responses, immune development, cell survival, and cell proliferation, among others. The classical pathway regulates the majority of genes activated by NF-kB including those encoding cytokines, chemokines, leukocyte adhesion molecules, and anti-apoptotic factors. It involves NEMO (NF-kB Essential MOdulator)- and IKKbeta-dependent phosphorylation and degradation of the Inhibitor of NF-kB (IkB), which liberates NF-kB dimers (typified by the p50-p65 heterodimer) from an inactive IkB/dimeric NF-kB complex, enabling them to migrate to the nucleus where they regulate gene transcription. The IKKbeta subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270940 [Multi-domain]  Cd Length: 290  Bit Score: 101.96  E-value: 1.63e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 7995 IGTGAFGVVHRCRERSTGNIFAAKFIPVSHSVE-KDLIRREIDIMNQLHHQKLINLHDAFED------DDEMILILEFLS 8067
Cdd:cd14038     2 LGTGGFGNVLRWINQETGEQVAIKQCRQELSPKnRERWCLEIQIMKRLNHPNVVAARDVPEGlqklapNDLPLLAMEYCQ 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 8068 GGEL------FERITAegyvMTEAEVINYMRQICEGIRHMHEQNIIHLDIKPENIMCQTRSSTNV-KLIDFGLATRLDPN 8140
Cdd:cd14038    82 GGDLrkylnqFENCCG----LREGAILTLLSDISSALRYLHENRIIHRDLKPENIVLQQGEQRLIhKIIDLGYAKELDQG 157
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*.
gi 281359561 8141 EVVKITTGTAEFAAPEIVNREPVGFYTDMWATGVLSYVLLSGLSPF 8186
Cdd:cd14038   158 SLCTSFVGTLQYLAPELLEQQKYTVTVDYWSFGTLAFECITGFRPF 203
PKc_Byr1_like cd06620
Catalytic domain of fungal Byr1-like dual-specificity Mitogen-activated protein Kinase Kinases; ...
7991-8242 1.97e-22

Catalytic domain of fungal Byr1-like dual-specificity Mitogen-activated protein Kinase Kinases; PKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine (ST) or tyrosine residues on protein substrates. Members of this group include the MAPKKs Byr1 from Schizosaccharomyces pombe, FUZ7 from Ustilago maydis, and related proteins. Byr1 phosphorylates its downstream target, the MAPK Spk1, and is regulated by the MAPKK kinase Byr2. The Spk1 cascade is pheromone-responsive and is essential for sporulation and sexual differentiation in fission yeast. FUZ7 phosphorylates and activates its target, the MAPK Crk1, which is required in mating and virulence in U. maydis. MAPK signaling pathways are important mediators of cellular responses to extracellular signals. The Byr-1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270792 [Multi-domain]  Cd Length: 286  Bit Score: 101.75  E-value: 1.97e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 7991 ILEEIGTGAFGVVHRCRERSTGNIFAAKFIPV-SHSVEKDLIRREIDIMNQLHHQKLINLHDAF-EDDDEMILILEFLSG 8068
Cdd:cd06620     9 TLKDLGAGNGGSVSKVLHIPTGTIMAKKVIHIdAKSSVRKQILRELQILHECHSPYIVSFYGAFlNENNNIIICMEYMDC 88
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 8069 GELfERITAEGYVMTEAEVINYMRQICEGIRHMHEQ-NIIHLDIKPENIMCQTRSstNVKLIDFGLATRLdPNEVVKITT 8147
Cdd:cd06620    89 GSL-DKILKKKGPFPEEVLGKIAVAVLEGLTYLYNVhRIIHRDIKPSNILVNSKG--QIKLCDFGVSGEL-INSIADTFV 164
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 8148 GTAEFAAPEIVNREPVGFYTDMWATGVLSYVLLSGLSPFAGDNDVQTLKNVKACDWDF----------DVESFKYISEEA 8217
Cdd:cd06620   165 GTSTYMSPERIQGGKYSVKSDVWSLGLSIIELALGEFPFAGSNDDDDGYNGPMGILDLlqrivnepppRLPKDRIFPKDL 244
                         250       260
                  ....*....|....*....|....*
gi 281359561 8218 KDFIRKLLVRNKEKRMTAHECLLHP 8242
Cdd:cd06620   245 RDFVDRCLLKDPRERPSPQLLLDHD 269
FN3 cd00063
Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein ...
2203-2292 2.49e-22

Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein fibronectin. Its tenth fibronectin type III repeat contains an RGD cell recognition sequence in a flexible loop between 2 strands. Approximately 2% of all animal proteins contain the FN3 repeat; including extracellular and intracellular proteins, membrane spanning cytokine receptors, growth hormone receptors, tyrosine phosphatase receptors, and adhesion molecules. FN3-like domains are also found in bacterial glycosyl hydrolases.


Pssm-ID: 238020 [Multi-domain]  Cd Length: 93  Bit Score: 94.87  E-value: 2.49e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 2203 PGKPKAVDLTDWDKDHADLKWEAPETDGGdPITAYIVEYKEKFSNDWVSGKEVDGDARTATVDGLKEGQQYEFRVRAVNR 2282
Cdd:cd00063     1 PSPPTNLRVTDVTSTSVTLSWTPPEDDGG-PITGYVVEYREKGSGDWKEVEVTPGSETSYTLTGLKPGTEYEFRVRAVNG 79
                          90
                  ....*....|
gi 281359561 2283 AGPGEPSDKT 2292
Cdd:cd00063    80 GGESPPSESV 89
STKc_myosinIIIB_N cd06639
N-terminal Catalytic domain of the Serine/Threonine Kinase, Class IIIB myosin; STKs catalyze ...
7987-8244 3.13e-22

N-terminal Catalytic domain of the Serine/Threonine Kinase, Class IIIB myosin; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Class IIIB myosin is expressed highly in retina. It is also present in the brain and testis. The human class IIIB myosin gene maps to a region that overlaps the locus for Bardet-Biedl syndrome, which is characterized by dysmorphic extremities, retinal dystrophy, obesity, male hypogenitalism, and renal abnormalities. Class III myosins are motor proteins containing an N-terminal kinase catalytic domain and a C-terminal actin-binding domain. They may play an important role in maintaining the structural integrity of photoreceptor cell microvilli. They may also function as cargo carriers during light-dependent translocation, in photoreceptor cells, of proteins such as transducin and arrestin. The class III myosin subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270808 [Multi-domain]  Cd Length: 291  Bit Score: 101.22  E-value: 3.13e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 7987 DRYDILEEIGTGAFGVVHRCRERSTGNIFAAKFI-PVSHSVEKdlIRREIDIMNQL-HHQKLINLHDAFEDDDEMI---- 8060
Cdd:cd06639    22 DTWDIIETIGKGTYGKVYKVTNKKDGSLAAVKILdPISDVDEE--IEAEYNILRSLpNHPNVVKFYGMFYKADQYVggql 99
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 8061 -LILEFLSGG---ELFERITAEGYVMTEAEVINYMRQICEGIRHMHEQNIIHLDIKPENIMCQTRSStnVKLIDFGLATR 8136
Cdd:cd06639   100 wLVLELCNGGsvtELVKGLLKCGQRLDEAMISYILYGALLGLQHLHNNRIIHRDVKGNNILLTTEGG--VKLVDFGVSAQ 177
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 8137 LDPNEVVKITT-GTAEFAAPEIVNREPVGFYT-----DMWATGVLSYVLLSGLSPFAGDNDVQTLKNVKACDWDFDVESF 8210
Cdd:cd06639   178 LTSARLRRNTSvGTPFWMAPEVIACEQQYDYSydarcDVWSLGITAIELADGDPPLFDMHPVKALFKIPRNPPPTLLNPE 257
                         250       260       270
                  ....*....|....*....|....*....|....
gi 281359561 8211 KYiSEEAKDFIRKLLVRNKEKRMTAHECLLHPWL 8244
Cdd:cd06639   258 KW-CRGFSHFISQCLIKDFEKRPSVTHLLEHPFI 290
STKc_myosinIIIA_N cd06638
N-terminal Catalytic domain of the Serine/Threonine Kinase, Class IIIA myosin; STKs catalyze ...
7987-8244 3.27e-22

N-terminal Catalytic domain of the Serine/Threonine Kinase, Class IIIA myosin; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Class IIIA myosin is highly expressed in retina and in inner ear hair cells. It is localized to the distal ends of actin-bundled structures. Mutations in human myosin IIIA are responsible for progressive nonsyndromic hearing loss. Human myosin IIIA possesses ATPase and kinase activities, and the ability to move actin filaments in a motility assay. It may function as a cellular transporter capable of moving along actin bundles in sensory cells. Class III myosins are motor proteins containing an N-terminal kinase catalytic domain and a C-terminal actin-binding domain. Class III myosins may play an important role in maintaining the structural integrity of photoreceptor cell microvilli. In photoreceptor cells, they may also function as cargo carriers during light-dependent translocation of proteins such as transducin and arrestin. The class III myosin subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 132969 [Multi-domain]  Cd Length: 286  Bit Score: 100.86  E-value: 3.27e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 7987 DRYDILEEIGTGAFGVVHRCRERSTGNIFAAKFIPVSHSVEKDlIRREIDIMNQLH-HQKLINLHDAF-----EDDDEMI 8060
Cdd:cd06638    18 DTWEIIETIGKGTYGKVFKVLNKKNGSKAAVKILDPIHDIDEE-IEAEYNILKALSdHPNVVKFYGMYykkdvKNGDQLW 96
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 8061 LILEFLSGG---ELFERITAEGYVMTEAEVINYMRQICEGIRHMHEQNIIHLDIKPENIMCQTRSStnVKLIDFGLATRL 8137
Cdd:cd06638    97 LVLELCNGGsvtDLVKGFLKRGERMEEPIIAYILHEALMGLQHLHVNKTIHRDVKGNNILLTTEGG--VKLVDFGVSAQL 174
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 8138 DPNEVVKITT-GTAEFAAPEIVNREPVGFYT-----DMWATGVLSYVLLSGLSPFAGDNDVQTLKNVKAcDWDFDVESFK 8211
Cdd:cd06638   175 TSTRLRRNTSvGTPFWMAPEVIACEQQLDSTydarcDVWSLGITAIELGDGDPPLADLHPMRALFKIPR-NPPPTLHQPE 253
                         250       260       270
                  ....*....|....*....|....*....|...
gi 281359561 8212 YISEEAKDFIRKLLVRNKEKRMTAHECLLHPWL 8244
Cdd:cd06638   254 LWSNEFNDFIRKCLTKDYEKRPTVSDLLQHVFI 286
STKc_NDR2 cd05627
Catalytic domain of the Serine/Threonine Kinase, Nuclear Dbf2-Related kinase 2; STKs catalyze ...
7987-8246 4.06e-22

Catalytic domain of the Serine/Threonine Kinase, Nuclear Dbf2-Related kinase 2; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. NDR2 (also called STK38-like) plays a role in proper centrosome duplication. In addition, it is involved in regulating neuronal growth and differentiation, as well as in facilitating neurite outgrowth. NDR2 is also implicated in fear conditioning as it contributes to the coupling of neuronal morphological changes with fear-memory consolidation. NDR kinase contains an N-terminal regulatory (NTR) domain and an insert within the catalytic domain that contains an auto-inhibitory sequence. Like many other AGC kinases, NDR kinase requires phosphorylation at two sites, the activation loop (A-loop) and the hydrophobic motif (HM), for activity. The NDR2 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270776 [Multi-domain]  Cd Length: 366  Bit Score: 102.44  E-value: 4.06e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 7987 DRYDILEEIGTGAFGVVHRCRERSTGNIFAAKFIPVSHSVEKDL---IRREIDIMNQLHHQKLINLHDAFEDDDEMILIL 8063
Cdd:cd05627     2 DDFESLKVIGRGAFGEVRLVQKKDTGHIYAMKILRKADMLEKEQvahIRAERDILVEADGAWVVKMFYSFQDKRNLYLIM 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 8064 EFLSGGELFERITAEGyVMTEAEVINYMRQICEGIRHMHEQNIIHLDIKPENIMCQTRSstNVKLIDFGLATRL------ 8137
Cdd:cd05627    82 EFLPGGDMMTLLMKKD-TLSEEATQFYIAETVLAIDAIHQLGFIHRDIKPDNLLLDAKG--HVKLSDFGLCTGLkkahrt 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 8138 ------------------------------DPNEVVKITTGTAEFAAPEIVNREPVGFYTDMWATGVLSYVLLSGLSPFA 8187
Cdd:cd05627   159 efyrnlthnppsdfsfqnmnskrkaetwkkNRRQLAYSTVGTPDYIAPEVFMQTGYNKLCDWWSLGVIMYEMLIGYPPFC 238
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 281359561 8188 GDNDVQTLKnvKACDWDfdvESFKY-----ISEEAKDFIRKLLV--RNKEKRMTAHECLLHPWLTG 8246
Cdd:cd05627   239 SETPQETYR--KVMNWK---ETLVFppevpISEKAKDLILRFCTdaENRIGSNGVEEIKSHPFFEG 299
I-set pfam07679
Immunoglobulin I-set domain;
6173-6255 4.42e-22

Immunoglobulin I-set domain;


Pssm-ID: 400151 [Multi-domain]  Cd Length: 90  Bit Score: 94.25  E-value: 4.42e-22
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561  6173 KRIKVRAGEPVNLNIPISGAPTPTIEWKRGDLKLEEGKRISYETNSERTLFRIDDSNRRDSGKYTVTAANEFGKDTADIE 6252
Cdd:pfam07679    8 KDVEVQEGESARFTCTVTGTPDPEVSWFKDGQPLRSSDRFKVTYEGGTYTLTISNVQPDDSGKYTCVATNSAGEAEASAE 87

                   ...
gi 281359561  6253 VIV 6255
Cdd:pfam07679   88 LTV 90
PKc_Myt1 cd14050
Catalytic domain of the Dual-specificity protein kinase, Myt1; Dual-specificity PKs catalyze ...
7989-8242 5.08e-22

Catalytic domain of the Dual-specificity protein kinase, Myt1; Dual-specificity PKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine as well as tyrosine residues on protein substrates. Myt1 is a cytoplasmic cell cycle checkpoint kinase that can keep the cyclin-dependent kinase CDK1 in an inactive state through phosphorylation of N-terminal thr (T14) and tyr (Y15) residues, leading to the delay of meiosis I entry. Meiotic progression is ensured by a two-step inhibition and downregulation of Myt1 by CDK1/XRINGO and p90Rsk during oocyte maturation. In addition, Myt1 targets cyclin B1/B2 and is essential for Golgi and ER assembly during telophase. In Drosophila, Myt1 may be a downstream target of Notch during eye development. The Myt1 subfamily is part of a larger superfamily that includes the catalytic domains of other protein serine/threonine PKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270952 [Multi-domain]  Cd Length: 249  Bit Score: 99.31  E-value: 5.08e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 7989 YDILEEIGTGAFGVVHRCRERSTGNIFAAKFIPVSHSVEKDLIR--REIDIMNQLH-HQKLINLHDAFEDDDEMILILEf 8065
Cdd:cd14050     3 FTILSKLGEGSFGEVFKVRSREDGKLYAVKRSRSRFRGEKDRKRklEEVERHEKLGeHPNCVRFIKAWEEKGILYIQTE- 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 8066 LSGGELfERITAEGYVMTEAEVINYMRQICEGIRHMHEQNIIHLDIKPENIMCqTRSSTnVKLIDFGLATRLDPNEVVKI 8145
Cdd:cd14050    82 LCDTSL-QQYCEETHSLPESEVWNILLDLLKGLKHLHDHGLIHLDIKPANIFL-SKDGV-CKLGDFGLVVELDKEDIHDA 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 8146 TTGTAEFAAPEIVNrepvGFYT---DMWATGVLSYVLLSGLS-PFAGDnDVQTLKNvkacdWDFDVESFKYISEEAKDFI 8221
Cdd:cd14050   159 QEGDPRYMAPELLQ----GSFTkaaDIFSLGITILELACNLElPSGGD-GWHQLRQ-----GYLPEEFTAGLSPELRSII 228
                         250       260
                  ....*....|....*....|.
gi 281359561 8222 RKLLVRNKEKRMTAHECLLHP 8242
Cdd:cd14050   229 KLMMDPDPERRPTAEDLLALP 249
STKc_MAST cd05609
Catalytic domain of the Protein Serine/Threonine Kinase, Microtubule-associated serine ...
7989-8246 5.18e-22

Catalytic domain of the Protein Serine/Threonine Kinase, Microtubule-associated serine/threonine kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MAST kinases contain an N-terminal domain of unknown function, a central catalytic domain, and a C-terminal PDZ domain that mediates protein-protein interactions. There are four mammalian MAST kinases, named MAST1-MAST4. MAST1 is also called syntrophin-associated STK (SAST) while MAST2 is also called MAST205. MAST kinases are cytoskeletal associated kinases of unknown function that are also expressed at neuromuscular junctions and postsynaptic densities. MAST1, MAST2, and MAST3 bind and phosphorylate the tumor suppressor PTEN, and may contribute to the regulation and stabilization of PTEN. MAST2 is involved in the regulation of the Fc-gamma receptor of the innate immune response in macrophages, and may also be involved in the regulation of the Na+/H+ exchanger NHE3. The MAST kinase subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270760 [Multi-domain]  Cd Length: 280  Bit Score: 100.17  E-value: 5.18e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 7989 YDILEEIGTGAFGVVHRCRERSTGNIFAAKFIPVSHSVEKDLIRR---EIDIMNQLHHQKLINLHDAFEDDDEMILILEF 8065
Cdd:cd05609     2 FETIKLISNGAYGAVYLVRHRETRQRFAMKKINKQNLILRNQIQQvfvERDILTFAENPFVVSMYCSFETKRHLCMVMEY 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 8066 LSGGE---LFERITAEGYVMTEAevinYMRQICEGIRHMHEQNIIHLDIKPENIMcqTRSSTNVKLIDFGL--------A 8134
Cdd:cd05609    82 VEGGDcatLLKNIGPLPVDMARM----YFAETVLALEYLHSYGIVHRDLKPDNLL--ITSMGHIKLTDFGLskiglmslT 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 8135 TRL-------DPNEVV-KITTGTAEFAAPEIVNREPVGFYTDMWATGVLSYVLLSGLSPFAGDNDVQTLKNVKACDWDFd 8206
Cdd:cd05609   156 TNLyeghiekDTREFLdKQVCGTPEYIAPEVILRQGYGKPVDWWAMGIILYEFLVGCVPFFGDTPEELFGQVISDEIEW- 234
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|...
gi 281359561 8207 VESFKYISEEAKDFIRKLLVRNKEKRM---TAHECLLHPWLTG 8246
Cdd:cd05609   235 PEGDDALPDDAQDLITRLLQQNPLERLgtgGAEEVKQHPFFQD 277
STKc_Pho85 cd07836
Catalytic domain of the Serine/Threonine Kinase, Fungal Cyclin-Dependent protein Kinase Pho85; ...
7989-8243 5.60e-22

Catalytic domain of the Serine/Threonine Kinase, Fungal Cyclin-Dependent protein Kinase Pho85; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Pho85 is a multifunctional CDK in yeast. It is regulated by 10 different cyclins (Pcls) and plays a role in G1 progression, cell polarity, phosphate and glycogen metabolism, gene expression, and in signaling changes in the environment. It is not essential for yeast viability and is the functional homolog of mammalian CDK5, which plays a role in central nervous system development. CDKs belong to a large family of STKs that are regulated by their cognate cyclins. Together, they are involved in the control of cell-cycle progression, transcription, and neuronal function. The Pho85 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 143341 [Multi-domain]  Cd Length: 284  Bit Score: 100.25  E-value: 5.60e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 7989 YDILEEIGTGAFGVVHRCRERSTGNIFAAKFIPV-SHSVEKDLIRREIDIMNQLHHQKLINLHDAFEDDDEMILILEFLS 8067
Cdd:cd07836     2 FKQLEKLGEGTYATVYKGRNRTTGEIVALKEIHLdAEEGTPSTAIREISLMKELKHENIVRLHDVIHTENKLMLVFEYMD 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 8068 gGELFERITAEGY--VMTEAEVINYMRQICEGIRHMHEQNIIHLDIKPENIMCQTRSstNVKLIDFGLATRLD------P 8139
Cdd:cd07836    82 -KDLKKYMDTHGVrgALDPNTVKSFTYQLLKGIAFCHENRVLHRDLKPQNLLINKRG--ELKLADFGLARAFGipvntfS 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 8140 NEVVkittgTAEFAAPEIVnrepVGFYT-----DMWATGVLSYVLLSGLSPFAGDNDVQTLKNV-------KACDWDFDV 8207
Cdd:cd07836   159 NEVV-----TLWYRAPDVL----LGSRTystsiDIWSVGCIMAEMITGRPLFPGTNNEDQLLKIfrimgtpTESTWPGIS 229
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....
gi 281359561 8208 ESFKY------------------ISEEAKDFIRKLLVRNKEKRMTAHECLLHPW 8243
Cdd:cd07836   230 QLPEYkptfpryppqdlqqlfphADPLGIDLLHRLLQLNPELRISAHDALQHPW 283
FN3 cd00063
Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein ...
5764-5853 6.16e-22

Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein fibronectin. Its tenth fibronectin type III repeat contains an RGD cell recognition sequence in a flexible loop between 2 strands. Approximately 2% of all animal proteins contain the FN3 repeat; including extracellular and intracellular proteins, membrane spanning cytokine receptors, growth hormone receptors, tyrosine phosphatase receptors, and adhesion molecules. FN3-like domains are also found in bacterial glycosyl hydrolases.


Pssm-ID: 238020 [Multi-domain]  Cd Length: 93  Bit Score: 93.72  E-value: 6.16e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 5764 PDAPGKPIITDWDRDHIDLQWAVPKSDGGaPISEYIIQKKEKGSPYWTNVRHVPSNKNTTTIPELTEGQEYEFRVIAVNQ 5843
Cdd:cd00063     1 PSPPTNLRVTDVTSTSVTLSWTPPEDDGG-PITGYVVEYREKGSGDWKEVEVTPGSETSYTLTGLKPGTEYEFRVRAVNG 79
                          90
                  ....*....|
gi 281359561 5844 AGQSEPSEPS 5853
Cdd:cd00063    80 GGESPPSESV 89
STKc_ROCK1 cd05622
Catalytic domain of the Serine/Threonine Kinase, Rho-associated coiled-coil containing protein ...
7987-8250 6.35e-22

Catalytic domain of the Serine/Threonine Kinase, Rho-associated coiled-coil containing protein kinase 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. ROCK1 is preferentially expressed in the liver, lung, spleen, testes, and kidney. It mediates signaling from Rho to the actin cytoskeleton. It is implicated in the development of cardiac fibrosis, cardiomyocyte apoptosis, and hyperglycemia. Mice deficient with ROCK1 display eyelids open at birth (EOB) and omphalocele phenotypes due to the disorganization of actin filaments in the eyelids and the umbilical ring. ROCK contains an N-terminal extension, a catalytic kinase domain, and a C-terminal extension, which contains a coiled-coil region encompassing a Rho-binding domain (RBD) and a pleckstrin homology (PH) domain. ROCK is auto-inhibited by the RBD and PH domain interacting with the catalytic domain, and is activated via interaction with Rho GTPases. The ROCK1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270772 [Multi-domain]  Cd Length: 405  Bit Score: 102.78  E-value: 6.35e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 7987 DRYDILEEIGTGAFGVVHRCRERSTGNIFAAKFIPVSHSVEKD---LIRREIDIMNQLHHQKLINLHDAFEDDDEMILIL 8063
Cdd:cd05622    73 EDYEVVKVIGRGAFGEVQLVRHKSTRKVYAMKLLSKFEMIKRSdsaFFWEERDIMAFANSPWVVQLFYAFQDDRYLYMVM 152
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 8064 EFLSGGELFERITaeGYVMTEAEVINYMRQICEGIRHMHEQNIIHLDIKPENIMCQtrSSTNVKLIDFGLATRLDPNEVV 8143
Cdd:cd05622   153 EYMPGGDLVNLMS--NYDVPEKWARFYTAEVVLALDAIHSMGFIHRDVKPDNMLLD--KSGHLKLADFGTCMKMNKEGMV 228
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 8144 KITT--GTAEFAAPEIVNRE-PVGFY---TDMWATGVLSYVLLSGLSPFAGDNDVQTLKNVKACDWDFDVESFKYISEEA 8217
Cdd:cd05622   229 RCDTavGTPDYISPEVLKSQgGDGYYgreCDWWSVGVFLYEMLVGDTPFYADSLVGTYSKIMNHKNSLTFPDDNDISKEA 308
                         250       260       270
                  ....*....|....*....|....*....|....*.
gi 281359561 8218 KDFIRKLLVrNKEKRM---TAHECLLHPWLTGDHSA 8250
Cdd:cd05622   309 KNLICAFLT-DREVRLgrnGVEEIKRHLFFKNDQWA 343
STKc_16 cd13986
Catalytic domain of Serine/Threonine Kinase 16; STKs catalyze the transfer of the ...
7988-8241 7.74e-22

Catalytic domain of Serine/Threonine Kinase 16; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. STK16 is associated with many names including Myristylated and Palmitylated Serine/threonine Kinase 1 (MPSK1), Kinase related to cerevisiae and thaliana (Krct), and Protein Kinase expressed in day 12 fetal liver (PKL12). It is widely expressed in mammals with highest levels found in liver, testis, and kidney. It is localized in the Golgi but is translocated to the nucleus upon disorganization of the Golgi. STK16 is constitutively active and is capable of phosphorylating itself and other substrates. It may be involved in regulating stromal-epithelial interactions during mammary gland ductal morphogenesis. It may also function as a transcriptional co-activator of type-C natriuretic peptide and VEGF. The STK16 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270888 [Multi-domain]  Cd Length: 282  Bit Score: 99.68  E-value: 7.74e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 7988 RYDILEEIGTGAFGVVHRCRERSTGNIFAAKFIPVsHSVE-KDLIRREIDIMNQLHHQKLINLHDA----FEDDDEMI-L 8061
Cdd:cd13986     1 RYRIQRLLGEGGFSFVYLVEDLSTGRLYALKKILC-HSKEdVKEAMREIENYRLFNHPNILRLLDSqivkEAGGKKEVyL 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 8062 ILEFLSGGEL---FERITAEGYVMTEAEVINYMRQICEGIRHMHEQNII---HLDIKPENIMCqTRSSTNVkLIDFGlAT 8135
Cdd:cd13986    80 LLPYYKRGSLqdeIERRLVKGTFFPEDRILHIFLGICRGLKAMHEPELVpyaHRDIKPGNVLL-SEDDEPI-LMDLG-SM 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 8136 RLDPNEVVKITT-----------GTAEFAAPEIVNREP---VGFYTDMWATGVLSYVLLSGLSPFagDNDVQTLKNVKAC 8201
Cdd:cd13986   157 NPARIEIEGRREalalqdwaaehCTMPYRAPELFDVKShctIDEKTDIWSLGCTLYALMYGESPF--ERIFQKGDSLALA 234
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....
gi 281359561 8202 ----DWDFDVESfkYISEEAKDFIRKLLVRNKEKRMTAHECLLH 8241
Cdd:cd13986   235 vlsgNYSFPDNS--RYSEELHQLVKSMLVVNPAERPSIDDLLSR 276
IgI_Twitchin_like cd20949
C-terminal immunoglobulin-like domain of the myosin-associated giant protein kinase Twitchin, ...
8313-8401 7.94e-22

C-terminal immunoglobulin-like domain of the myosin-associated giant protein kinase Twitchin, and similar domains; member of the I-set IgSF domains; The members here are composed of the C-terminal immunoglobulin-like domain of the myosin-associated giant protein kinase Twitchin and similar proteins, including Caenorhabditis elegans and Aplysia californica Twitchin, Drosophila melanogaster Projectin, and similar proteins. These are very large muscle proteins containing multiple immunoglobulin (Ig)-like and fibronectin type III (FN3) domains and a single kinase domain near the C-terminus. In humans these proteins are called Titin. The Ig superfamily (IgSF) is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. The Ig-like domain of the Twitchin is a member of the I-set IgSF domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand but lack a C" strand. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors, the hemolymph protein hemolin, the muscle proteins (titin, telokin, and twitchin), the neuronal adhesion molecule axonin-1, and the signaling molecule semaphorin 4D.


Pssm-ID: 409541 [Multi-domain]  Cd Length: 89  Bit Score: 93.55  E-value: 7.94e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 8313 RFVIRPSSQFCYEGQSVKFYCRCIAIATPTLTWSHNNIELRQSVKFMKRYVGDDYYFIINRVKLDDRGEYIIRAENHYGS 8392
Cdd:cd20949     1 TFTENAYVTTVKEGQSATILCEVKGEPQPNVTWHFNGQPISASVADMSKYRILADGLLINKVTQDDTGEYTCRAYQVNSI 80

                  ....*....
gi 281359561 8393 REEVVFLNV 8401
Cdd:cd20949    81 ASDMQERTV 89
STKc_CDK5 cd07839
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 5; STKs ...
7988-8243 9.56e-22

Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 5; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. CDK5 is unusual in that it is regulated by non-cyclin proteins, p35 and p39. It is highly expressed in the nervous system and is critical in normal neural development and function. It plays a role in neuronal migration and differentiation, and is also important in synaptic plasticity and learning. CDK5 also participates in protecting against cell death and promoting angiogenesis. Impaired CDK5 activity is implicated in Alzheimer's disease, amyotrophic lateral sclerosis, Parkinson's disease, Huntington's disease and acute neuronal injury. CDKs belong to a large family of STKs that are regulated by their cognate cyclins. Together, they are involved in the control of cell-cycle progression, transcription, and neuronal function. The CDK5 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 143344 [Multi-domain]  Cd Length: 284  Bit Score: 99.43  E-value: 9.56e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 7988 RYDILEEIGTGAFGVVHRCRERSTGNIFAAKFIPVSHSVE--KDLIRREIDIMNQLHHQKLINLHDAFEDDDEMILILEF 8065
Cdd:cd07839     1 KYEKLEKIGEGTYGTVFKAKNRETHEIVALKRVRLDDDDEgvPSSALREICLLKELKHKNIVRLYDVLHSDKKLTLVFEY 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 8066 LSGG--ELFERITAEgyvMTEAEVINYMRQICEGIRHMHEQNIIHLDIKPENIMCQTRSstNVKLIDFGLA------TRL 8137
Cdd:cd07839    81 CDQDlkKYFDSCNGD---IDPEIVKSFMFQLLKGLAFCHSHNVLHRDLKPQNLLINKNG--ELKLADFGLArafgipVRC 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 8138 DPNEVVkittgTAEFAAPEIVnrepVG--FYT---DMWATGVLSYVLLSGLSPFAGDNDVQ-TLKNV-------KACDWD 8204
Cdd:cd07839   156 YSAEVV-----TLWYRPPDVL----FGakLYStsiDMWSAGCIFAELANAGRPLFPGNDVDdQLKRIfrllgtpTEESWP 226
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 281359561 8205 FDVESFKY------------------ISEEAKDFIRKLLVRNKEKRMTAHECLLHPW 8243
Cdd:cd07839   227 GVSKLPDYkpypmypattslvnvvpkLNSTGRDLLQNLLVCNPVQRISAEEALQHPY 283
STKc_Nek7 cd08229
Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase ...
7989-8232 1.09e-21

Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase 7; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Nek7 is required for mitotic spindle formation and cytokinesis. It is enriched in the centrosome and is critical for microtubule nucleation. Nek7 is activated by Nek9 during mitosis, and may regulate the p70 ribosomal S6 kinase. It is one in a family of 11 different Neks (Nek1-11) that are involved in cell cycle control. The Nek family is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270866 [Multi-domain]  Cd Length: 292  Bit Score: 99.72  E-value: 1.09e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 7989 YDILEEIGTGAFGVVHRCRERSTGNIFAAKFIPV----SHSVEKDLIRrEIDIMNQLHHQKLINLHDAFEDDDEMILILE 8064
Cdd:cd08229    26 FRIEKKIGRGQFSEVYRATCLLDGVPVALKKVQIfdlmDAKARADCIK-EIDLLKQLNHPNVIKYYASFIEDNELNIVLE 104
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 8065 FLSGGELFERI---TAEGYVMTEAEVINYMRQICEGIRHMHEQNIIHLDIKPENIMcqTRSSTNVKLIDFGLATRLDPNE 8141
Cdd:cd08229   105 LADAGDLSRMIkhfKKQKRLIPEKTVWKYFVQLCSALEHMHSRRVMHRDIKPANVF--ITATGVVKLGDLGLGRFFSSKT 182
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 8142 VVKIT-TGTAEFAAPEIVNREPVGFYTDMWATGVLSYVLLSGLSPFAGD--NDVQTLKNVKACDWDfDVESFKYiSEEAK 8218
Cdd:cd08229   183 TAAHSlVGTPYYMSPERIHENGYNFKSDIWSLGCLLYEMAALQSPFYGDkmNLYSLCKKIEQCDYP-PLPSDHY-SEELR 260
                         250
                  ....*....|....
gi 281359561 8219 DFIRKLLVRNKEKR 8232
Cdd:cd08229   261 QLVNMCINPDPEKR 274
STKc_LATS cd05598
Catalytic domain of the Serine/Threonine Kinase, Large Tumor Suppressor; STKs catalyze the ...
7987-8246 1.26e-21

Catalytic domain of the Serine/Threonine Kinase, Large Tumor Suppressor; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. LATS was originally identified in Drosophila using a screen for genes whose inactivation led to overproliferation of cells. In tetrapods, there are two LATS isoforms, LATS1 and LATS2. Inactivation of LATS1 in mice results in the development of various tumors, including sarcomas and ovarian cancer. LATS functions as a tumor suppressor and is implicated in cell cycle regulation. The LATS subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270749 [Multi-domain]  Cd Length: 333  Bit Score: 100.47  E-value: 1.26e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 7987 DRYDILEEIGTGAFGVVHRCRERSTGNIFAAKFIPvshsvEKDLIRR--------EIDIMNQLHHQKLINLHDAFEDDDE 8058
Cdd:cd05598     1 SMFEKIKTIGVGAFGEVSLVRKKDTNALYAMKTLR-----KKDVLKRnqvahvkaERDILAEADNEWVVKLYYSFQDKEN 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 8059 MILILEFLSGGEL---------FERITAEGYVmteAEVInymrqiCeGIRHMHEQNIIHLDIKPENIMCQtrSSTNVKLI 8129
Cdd:cd05598    76 LYFVMDYIPGGDLmsllikkgiFEEDLARFYI---AELV------C-AIESVHKMGFIHRDIKPDNILID--RDGHIKLT 143
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 8130 DFGLAT--RLDPNE---VVKITTGTAEFAAPEIVNREPVGFYTDMWATGVLSYVLLSGLSPFAGDNDVQTLKNVKACDWD 8204
Cdd:cd05598   144 DFGLCTgfRWTHDSkyyLAHSLVGTPNYIAPEVLLRTGYTQLCDWWSVGVILYEMLVGQPPFLAQTPAETQLKVINWRTT 223
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*
gi 281359561 8205 FDVESFKYISEEAKDFIRKLLvRNKEKRM---TAHECLLHPWLTG 8246
Cdd:cd05598   224 LKIPHEANLSPEAKDLILRLC-CDAEDRLgrnGADEIKAHPFFAG 267
FN3 cd00063
Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein ...
5073-5166 1.28e-21

Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein fibronectin. Its tenth fibronectin type III repeat contains an RGD cell recognition sequence in a flexible loop between 2 strands. Approximately 2% of all animal proteins contain the FN3 repeat; including extracellular and intracellular proteins, membrane spanning cytokine receptors, growth hormone receptors, tyrosine phosphatase receptors, and adhesion molecules. FN3-like domains are also found in bacterial glycosyl hydrolases.


Pssm-ID: 238020 [Multi-domain]  Cd Length: 93  Bit Score: 92.94  E-value: 1.28e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 5073 PAPPNGpLKVDEINSESCTLHWNPPDDDGGqPIDNYVVEKLDETTGRWIPAGETDGPVTALKVGGLTPGHKYKFRVRAKN 5152
Cdd:cd00063     1 PSPPTN-LRVTDVTSTSVTLSWTPPEDDGG-PITGYVVEYREKGSGDWKEVEVTPGSETSYTLTGLKPGTEYEFRVRAVN 78
                          90
                  ....*....|....
gi 281359561 5153 RQGTSEPLTTAQAI 5166
Cdd:cd00063    79 GGGESPPSESVTVT 92
STKc_PCTAIRE3 cd07871
Catalytic domain of the Serine/Threonine Kinase, PCTAIRE-3 kinase; STKs catalyze the transfer ...
7987-8188 1.49e-21

Catalytic domain of the Serine/Threonine Kinase, PCTAIRE-3 kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PCTAIRE-3 shows a restricted pattern of expression and is present in brain, kidney, and intestine. It is elevated in Alzheimer's disease (AD) and has been shown to associate with paired helical filaments (PHFs) and stimulate Tau phosphorylation. As AD progresses, phosphorylated Tau aggregates and forms PHFs, which leads to the formation of neurofibrillary tangles. In human glioma cells, PCTAIRE-3 induces cell cycle arrest and cell death. PCTAIRE-3 shares sequence similarity with Cyclin-Dependent Kinases (CDKs), which belong to a large family of STKs that are regulated by their cognate cyclins. Together, CDKs and cyclins are involved in the control of cell-cycle progression, transcription, and neuronal function. The PCTAIRE-3 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270853 [Multi-domain]  Cd Length: 288  Bit Score: 99.31  E-value: 1.49e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 7987 DRYDILEEIGTGAFGVVHRCRERSTGNIFAAKFIPVSHSVEKDLIR-REIDIMNQLHHQKLINLHDAFEDDDEMILILEF 8065
Cdd:cd07871     5 ETYVKLDKLGEGTYATVFKGRSKLTENLVALKEIRLEHEEGAPCTAiREVSLLKNLKHANIVTLHDIIHTERCLTLVFEY 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 8066 LSGgELFERITAEGYVMTEAEVINYMRQICEGIRHMHEQNIIHLDIKPENIMCQTRSStnVKLIDFGLA------TRLDP 8139
Cdd:cd07871    85 LDS-DLKQYLDNCGNLMSMHNVKIFMFQLLRGLSYCHKRKILHRDLKPQNLLINEKGE--LKLADFGLAraksvpTKTYS 161
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 281359561 8140 NEVVK-------ITTGTAEFAAPeivnrepvgfyTDMWATGVLSYVLLSGLSPFAG 8188
Cdd:cd07871   162 NEVVTlwyrppdVLLGSTEYSTP-----------IDMWGVGCILYEMATGRPMFPG 206
PTKc_Wee1_fungi cd14052
Catalytic domain of the Protein Tyrosine Kinases, Fungal Wee1 proteins; PTKs catalyze the ...
7988-8175 1.92e-21

Catalytic domain of the Protein Tyrosine Kinases, Fungal Wee1 proteins; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. This subfamily is composed of fungal Wee1 proteins, also called Swe1 in budding yeast and Mik1 in fission yeast. Yeast Wee1 is required to control cell size. Wee1 is a cell cycle checkpoint kinase that helps keep the cyclin-dependent kinase CDK1 in an inactive state through phosphorylation of an N-terminal tyr (Y15) residue. During the late G2 phase, CDK1 is activated and mitotic entry is promoted by the removal of this inhibitory phosphorylation by the phosphatase Cdc25. Although Wee1 is functionally a tyr kinase, it is more closely related to serine/threonine kinases (STKs). It contains a catalytic kinase domain sandwiched in between N- and C-terminal regulatory domains. It is regulated by phosphorylation and degradation, and its expression levels are also controlled by circadian clock proteins. The fungal Wee1 subfamily is part of a larger superfamily that includes the catalytic domains of STKs, other PTKs, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270954 [Multi-domain]  Cd Length: 278  Bit Score: 98.65  E-value: 1.92e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 7988 RYDILEEIGTGAFGVVHRCRERS-TGNIFAAKFIPVSHSVEKDLIRR--EIDIMNQLH---HQKLINLHDAFEDDDEMIL 8061
Cdd:cd14052     1 RFANVELIGSGEFSQVYKVSERVpTGKVYAVKKLKPNYAGAKDRLRRleEVSILRELTldgHDNIVQLIDSWEYHGHLYI 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 8062 ILEFLSGGEL--FERITAEGYVMTEAEVINYMRQICEGIRHMHEQNIIHLDIKPENIMcqTRSSTNVKLIDFGLATRLdP 8139
Cdd:cd14052    81 QTELCENGSLdvFLSELGLLGRLDEFRVWKILVELSLGLRFIHDHHFVHLDLKPANVL--ITFEGTLKIGDFGMATVW-P 157
                         170       180       190
                  ....*....|....*....|....*....|....*.
gi 281359561 8140 NEVVKITTGTAEFAAPEIVNREPVGFYTDMWATGVL 8175
Cdd:cd14052   158 LIRGIEREGDREYIAPEILSEHMYDKPADIFSLGLI 193
FN3 COG3401
Fibronectin type 3 domain [General function prediction only];
6630-7006 2.27e-21

Fibronectin type 3 domain [General function prediction only];


Pssm-ID: 442628 [Multi-domain]  Cd Length: 603  Bit Score: 103.16  E-value: 2.27e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 6630 QYRLQLKNTSGFDTATINVRVLDR---PSPPTRLRADEFSGDSLTLYWNPPNDDGgsaIQNYIIEKKEARSSTWSKVSSF 6706
Cdd:COG3401   206 YYRVAATDTGGESAPSNEVSVTTPttpPSAPTGLTATADTPGSVTLSWDPVTESD---ATGYRVYRSNSGDGPFTKVATV 282
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 6707 CTVPFVrIRNLVLNKEYDFRVIAENKYG-QSDPANTSEPILARHPfdiPNTPGIPHGIDSTEDSITIAWTKPKhdgGSPI 6785
Cdd:COG3401   283 TTTSYT-DTGLTNGTTYYYRVTAVDAAGnESAPSNVVSVTTDLTP---PAAPSGLTATAVGSSSITLSWTASS---DADV 355
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 6786 TGYIIEKRLLSDDKWTKaVHALCPDLSCKIPNLIENAEYEFRVAAVNAAGqsAYSGSSDLIFCRRPPHAPKITSDLSIRD 6865
Cdd:COG3401   356 TGYNVYRSTSGGGTYTK-IAETVTTTSYTDTGLTPGTTYYYKVTAVDAAG--NESAPSEEVSATTASAASGESLTASVDA 432
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 6866 MTVIAGDefRITVPYHASPRPTASWSLNGLEVIPGERIKFDSNDYASMYYNKSAKRDETGSYTITLTNNKGSDTASCHVT 6945
Cdd:COG3401   433 VPLTDVA--GATAAASAASNPGVSAAVLADGGDTGNAVPFTTTSSTVTATTTDTTTANLSVTTGSLVGGSGASSVTNSVS 510
                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 281359561 6946 VVDRPLPPQGPLNAYDITPDTC--TLAWKTPLDDGGSPITNYVVEKLDNSGSWVKISSFVRNT 7006
Cdd:COG3401   511 VIGASAAAAVGGAPDGTPNVTGasPVTVGASTGDVLITDLVSLTTSASSSVSGAGLGSGNLYL 573
FN3 cd00063
Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein ...
2999-3088 2.31e-21

Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein fibronectin. Its tenth fibronectin type III repeat contains an RGD cell recognition sequence in a flexible loop between 2 strands. Approximately 2% of all animal proteins contain the FN3 repeat; including extracellular and intracellular proteins, membrane spanning cytokine receptors, growth hormone receptors, tyrosine phosphatase receptors, and adhesion molecules. FN3-like domains are also found in bacterial glycosyl hydrolases.


Pssm-ID: 238020 [Multi-domain]  Cd Length: 93  Bit Score: 92.17  E-value: 2.31e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 2999 PSKPRGpLDVKDVTKDSCKLKWKKPEDDGGkPISAYQVEKFDKKQGRWVPLGRTSANDTEFDVKGLQEGHEYQFRVKAIN 3078
Cdd:cd00063     1 PSPPTN-LRVTDVTSTSVTLSWTPPEDDGG-PITGYVVEYREKGSGDWKEVEVTPGSETSYTLTGLKPGTEYEFRVRAVN 78
                          90
                  ....*....|
gi 281359561 3079 EEGESDPLDS 3088
Cdd:cd00063    79 GGGESPPSES 88
FN3 cd00063
Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein ...
2501-2590 2.43e-21

Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein fibronectin. Its tenth fibronectin type III repeat contains an RGD cell recognition sequence in a flexible loop between 2 strands. Approximately 2% of all animal proteins contain the FN3 repeat; including extracellular and intracellular proteins, membrane spanning cytokine receptors, growth hormone receptors, tyrosine phosphatase receptors, and adhesion molecules. FN3-like domains are also found in bacterial glycosyl hydrolases.


Pssm-ID: 238020 [Multi-domain]  Cd Length: 93  Bit Score: 92.17  E-value: 2.43e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 2501 PSPPSQPVIDDYDNKSVLLKWKRPPSDGGrPITHYIVEIKDKFAPSWSEVAKTDDPNPECNVEGLKEKMVYQFRVRAVNK 2580
Cdd:cd00063     1 PSPPTNLRVTDVTSTSVTLSWTPPEDDGG-PITGYVVEYREKGSGDWKEVEVTPGSETSYTLTGLKPGTEYEFRVRAVNG 79
                          90
                  ....*....|
gi 281359561 2581 AGPSEPSQPT 2590
Cdd:cd00063    80 GGESPPSESV 89
STKc_p38 cd07851
Catalytic domain of the Serine/Threonine Kinase, p38 Mitogen-Activated Protein Kinase; STKs ...
7973-8244 2.70e-21

Catalytic domain of the Serine/Threonine Kinase, p38 Mitogen-Activated Protein Kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. p38 kinases are mitogen-activated protein kinases (MAPKs), serving as important mediators of cellular responses to extracellular signals. They function in the regulation of the cell cycle, cell development, cell differentiation, senescence, tumorigenesis, apoptosis, pain development and pain progression, and immune responses. p38 kinases are activated by the MAPK kinases MKK3 and MKK6, which in turn are activated by upstream MAPK kinase kinases including TAK1, ASK1, and MLK3, in response to cellular stresses or inflammatory cytokines. p38 substrates include other protein kinases and factors that regulate transcription, nuclear export, mRNA stability and translation. p38 kinases are drug targets for the inflammatory diseases psoriasis, rheumatoid arthritis, and chronic pulmonary disease. Vertebrates contain four isoforms of p38, named alpha, beta, gamma, and delta, which show varying substrate specificity and expression patterns. p38alpha and p38beta are ubiquitously expressed, p38gamma is predominantly found in skeletal muscle, and p38delta is found in the heart, lung, testis, pancreas, and small intestine. The p38 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 143356 [Multi-domain]  Cd Length: 343  Bit Score: 99.68  E-value: 2.70e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 7973 FVPQPVEISQQSVYDRYDILEEIGTGAFGVVHRCRERSTGNIFAAKFI--PVSHSVEKDLIRREIDIMNQLHHQKLINLH 8050
Cdd:cd07851     1 FYRQELNKTVWEVPDRYQNLSPVGSGAYGQVCSAFDTKTGRKVAIKKLsrPFQSAIHAKRTYRELRLLKHMKHENVIGLL 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 8051 DAF------EDDDEMILILEFLsGGELFERITAEgyVMTEAEVINYMRQICEGIRHMHEQNIIHLDIKPENImcQTRSST 8124
Cdd:cd07851    81 DVFtpasslEDFQDVYLVTHLM-GADLNNIVKCQ--KLSDDHIQFLVYQILRGLKYIHSAGIIHRDLKPSNL--AVNEDC 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 8125 NVKLIDFGLATRLDpnevVKITT--GTAEFAAPEIV-NRepvGFYT---DMWATGVLSYVLLSGLSPFAGDNDVQTLKNV 8198
Cdd:cd07851   156 ELKILDFGLARHTD----DEMTGyvATRWYRAPEIMlNW---MHYNqtvDIWSVGCIMAELLTGKTLFPGSDHIDQLKRI 228
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 281359561 8199 kacdwdFDV-----ESF--KYISEEAKDFIR--------------------------KLLVRNKEKRMTAHECLLHPWL 8244
Cdd:cd07851   229 ------MNLvgtpdEELlkKISSESARNYIQslpqmpkkdfkevfsganplaidlleKMLVLDPDKRITAAEALAHPYL 301
STKc_CDKL5 cd07848
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase Like 5; STKs ...
7987-8242 3.22e-21

Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase Like 5; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Mutations in the gene encoding CDKL5, previously called STK9, are associated with early onset epilepsy and severe mental retardation [X-linked infantile spasm syndrome (ISSX) or West syndrome]. In addition, CDKL5 mutations also sometimes cause a phenotype similar to Rett syndrome (RTT), a progressive neurodevelopmental disorder. These pathogenic mutations are located in the N-terminal portion of the protein within the kinase domain. CDKs belong to a large family of STKs that are regulated by their cognate cyclins. Together, they are involved in the control of cell-cycle progression, transcription, and neuronal function. The CDKL5 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270838 [Multi-domain]  Cd Length: 287  Bit Score: 98.14  E-value: 3.22e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 7987 DRYDILEEIGTGAFGVVHRCRERSTGNIFAAKFIPVSHSVE--KDLIRREIDIMNQLHHQKLINLHDAFEDDDEMILILE 8064
Cdd:cd07848     1 NKFEVLGVVGEGAYGVVLKCRHKETKEIVAIKKFKDSEENEevKETTLRELKMLRTLKQENIVELKEAFRRRGKLYLVFE 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 8065 FLSGG--ELFERITAEgyvMTEAEVINYMRQICEGIRHMHEQNIIHLDIKPENIMCQtrSSTNVKLIDFGLATRLDPNEV 8142
Cdd:cd07848    81 YVEKNmlELLEEMPNG---VPPEKVRSYIYQLIKAIHWCHKNDIVHRDIKPENLLIS--HNDVLKLCDFGFARNLSEGSN 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 8143 VKIT--TGTAEFAAPEIVNREPVGFYTDMWATGVLSYVLLSGLSPFAGDNDVQTLKNVKACDWDFDVESFKYISEEAK-- 8218
Cdd:cd07848   156 ANYTeyVATRWYRSPELLLGAPYGKAVDMWSVGCILGELSDGQPLFPGESEIDQLFTIQKVLGPLPAEQMKLFYSNPRfh 235
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|
gi 281359561 8219 --------------------------DFIRKLLVRNKEKRMTAHECLLHP 8242
Cdd:cd07848   236 glrfpavnhpqslerrylgilsgvllDLMKNLLKLNPTDRYLTEQCLNHP 285
FN3 COG3401
Fibronectin type 3 domain [General function prediction only];
5972-6384 3.24e-21

Fibronectin type 3 domain [General function prediction only];


Pssm-ID: 442628 [Multi-domain]  Cd Length: 603  Bit Score: 102.77  E-value: 3.24e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 5972 ANSVTISWKPPKDNGGSEISSYVIEKRDLTHGGGWVPAVNYVSAKYNHAVVPRLLEGTMYELRVMAENLQGRSDPltsDQ 6051
Cdd:COG3401   146 GLYGVDGANASGTTASSVAGAGVVVSPDTSATAAVATTSLTVTSTTLVDGGGDIEPGTTYYYRVAATDTGGESAP---SN 222
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 6052 PVVAKSQYTVPGAPGKPELTDSDKNHITIKWKqpiSNGGSPIIGYDIERRDVNTGRWIKINGqpVPTAEYQDDRVTSNHQ 6131
Cdd:COG3401   223 EVSVTTPTTPPSAPTGLTATADTPGSVTLSWD---PVTESDATGYRVYRSNSGDGPFTKVAT--VTTTSYTDTGLTNGTT 297
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 6132 YQYRISAVNAAGNgkTSEPSAifnarplrekprfyfdgligkrikvragepvnlnipisgaptptiewkrgdlkleegkr 6211
Cdd:COG3401   298 YYYRVTAVDAAGN--ESAPSN----------------------------------------------------------- 316
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 6212 isyetnsertlfriddsnrrdsgkyTVTAanefgkdTADIEvivvdKPSPPEGpLSYTETAPDHISLHWYSPKDdggSDI 6291
Cdd:COG3401   317 -------------------------VVSV-------TTDLT-----PPAAPSG-LTATAVGSSSITLSWTASSD---ADV 355
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 6292 TGYIIEFTEFGVDDWKPVPGTCPNTNFTVKNLVEGKKYVFRIRAENIYG----ASEALEGKPVLAKSPFDPPGAPSQPTI 6367
Cdd:COG3401   356 TGYNVYRSTSGGGTYTKIAETVTTTSYTDTGLTPGTTYYYKVTAVDAAGnesaPSEEVSATTASAASGESLTASVDAVPL 435
                         410
                  ....*....|....*..
gi 281359561 6368 SAYTPNSANLEWHPPDD 6384
Cdd:COG3401   436 TDVAGATAAASAASNPG 452
STKc_p38alpha cd07877
Catalytic domain of the Serine/Threonine Kinase, p38alpha Mitogen-Activated Protein Kinase ...
7973-8277 3.43e-21

Catalytic domain of the Serine/Threonine Kinase, p38alpha Mitogen-Activated Protein Kinase (also called MAPK14); STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. p38alpha/MAPK14 is expressed in most tissues and is the major isoform involved in the immune and inflammatory response. It is the central p38 MAPK involved in myogenesis. It plays a role in regulating cell cycle check-point transition and promoting cell differentiation. p38alpha also regulates cell proliferation and death through crosstalk with the JNK pathway. Its substrates include MAPK activated protein kinase 2 (MK2), MK5, and the transcription factors ATF2 and Mitf. p38 kinases MAPKs, serving as important mediators of cellular responses to extracellular signals. They are activated by the MAPK kinases MKK3 and MKK6, which in turn are activated by upstream MAPK kinase kinases including TAK1, ASK1, and MLK3, in response to cellular stresses or inflammatory cytokines. The p38alpha subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 143382 [Multi-domain]  Cd Length: 345  Bit Score: 99.34  E-value: 3.43e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 7973 FVPQPVEISQQSVYDRYDILEEIGTGAFGVVHRCRERSTGNIFAAKFI--PVSHSVEKDLIRREIDIMNQLHHQKLINLH 8050
Cdd:cd07877     3 FYRQELNKTIWEVPERYQNLSPVGSGAYGSVCAAFDTKTGLRVAVKKLsrPFQSIIHAKRTYRELRLLKHMKHENVIGLL 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 8051 DAF------EDDDEMILILEfLSGGELFERITAEGyvMTEAEVINYMRQICEGIRHMHEQNIIHLDIKPENImcQTRSST 8124
Cdd:cd07877    83 DVFtparslEEFNDVYLVTH-LMGADLNNIVKCQK--LTDDHVQFLIYQILRGLKYIHSADIIHRDLKPSNL--AVNEDC 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 8125 NVKLIDFGLATRLDpnEVVKITTGTAEFAAPEI-VNREPVGFYTDMWATGVLSYVLLSGLSPFAGDNDVQTLKNVKACDW 8203
Cdd:cd07877   158 ELKILDFGLARHTD--DEMTGYVATRWYRAPEImLNWMHYNQTVDIWSVGCIMAELLTGRTLFPGTDHIDQLKLILRLVG 235
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 8204 DFDVESFKYISEE---------------------------AKDFIRKLLVRNKEKRMTAHECLLHPWLTGDHSAMKQEIN 8256
Cdd:cd07877   236 TPGAELLKKISSEsarnyiqsltqmpkmnfanvfiganplAVDLLEKMLVLDSDKRITAAQALAHAYFAQYHDPDDEPVA 315
                         330       340
                  ....*....|....*....|....*...
gi 281359561 8257 R--DRYLAYREKL-----RRKYEDFERF 8277
Cdd:cd07877   316 DpyDQSFESRDLLidewkSLTYDEVISF 343
FN3 cd00063
Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein ...
6470-6552 3.62e-21

Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein fibronectin. Its tenth fibronectin type III repeat contains an RGD cell recognition sequence in a flexible loop between 2 strands. Approximately 2% of all animal proteins contain the FN3 repeat; including extracellular and intracellular proteins, membrane spanning cytokine receptors, growth hormone receptors, tyrosine phosphatase receptors, and adhesion molecules. FN3-like domains are also found in bacterial glycosyl hydrolases.


Pssm-ID: 238020 [Multi-domain]  Cd Length: 93  Bit Score: 91.79  E-value: 3.62e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 6470 ITRNGVTLSWRPPRTDGkSRIKGYYVEMRPKNGKDWKTVNDIPINSTVYTVPSLKEGEEYSFRVVAENEVGRSDPSKPSQ 6549
Cdd:cd00063    12 VTSTSVTLSWTPPEDDG-GPITGYVVEYREKGSGDWKEVEVTPGSETSYTLTGLKPGTEYEFRVRAVNGGGESPPSESVT 90

                  ...
gi 281359561 6550 PIT 6552
Cdd:cd00063    91 VTT 93
STKc_CDK4 cd07863
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 4; STKs ...
7988-8244 3.63e-21

Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 4; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. CDK4 partners with all three D-type cyclins (D1, D2, and D3) and is also regulated by INK4 inhibitors. It is active towards the retinoblastoma (pRb) protein and plays a role in regulating the early G1 phase of the cell cycle. It is expressed ubiquitously and is localized in the nucleus. CDK4 also shows kinase activity towards Smad3, a signal transducer of TGF-beta signaling which modulates transcription and plays a role in cell proliferation and apoptosis. CDK4 is inhibited by the p21 inhibitor and is specifically mutated in human melanoma. CDKs belong to a large family of STKs that are regulated by their cognate cyclins. Together, they are involved in the control of cell-cycle progression, transcription, and neuronal function. The CDK4 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 143368 [Multi-domain]  Cd Length: 288  Bit Score: 98.11  E-value: 3.63e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 7988 RYDILEEIGTGAFGVVHRCRERSTGNIFAAKFI---------PVSHSVEKDLIRReidiMNQLHHQKLINLHD---AFED 8055
Cdd:cd07863     1 QYEPVAEIGVGAYGTVYKARDPHSGHFVALKSVrvqtnedglPLSTVREVALLKR----LEAFDHPNIVRLMDvcaTSRT 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 8056 DDEMILILEFLSGGE----LFERITAEGYvmtEAEVI-NYMRQICEGIRHMHEQNIIHLDIKPENIMCQTRSStnVKLID 8130
Cdd:cd07863    77 DRETKVTLVFEHVDQdlrtYLDKVPPPGL---PAETIkDLMRQFLRGLDFLHANCIVHRDLKPENILVTSGGQ--VKLAD 151
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 8131 FGLA------TRLDPNEVvkittgTAEFAAPEIVNREPVGFYTDMWATGVLSYVLLSGLSPFAGDNDVQTLKNVKAC--- 8201
Cdd:cd07863   152 FGLAriyscqMALTPVVV------TLWYRAPEVLLQSTYATPVDMWSVGCIFAEMFRRKPLFCGNSEADQLGKIFDLigl 225
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 281359561 8202 ----DWDFDV----------------ESFKYISEEAKDFIRKLLVRNKEKRMTAHECLLHPWL 8244
Cdd:cd07863   226 ppedDWPRDVtlprgafsprgprpvqSVVPEIEESGAQLLLEMLTFNPHKRISAFRALQHPFF 288
STKc_NDR1 cd05628
Catalytic domain of the Serine/Threonine Kinase, Nuclear Dbf2-Related kinase 1; STKs catalyze ...
7989-8224 4.96e-21

Catalytic domain of the Serine/Threonine Kinase, Nuclear Dbf2-Related kinase 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. NDR1 (also called STK38) plays a role in proper centrosome duplication. It is highly expressed in thymus, muscle, lung and spleen. It is not an essential protein because mice deficient of NDR1 remain viable and fertile. However, these mice develop T-cell lymphomas and appear to be hypersenstive to carcinogenic treatment. NDR1 appears to also act as a tumor suppressor. NDR kinase contains an N-terminal regulatory (NTR) domain and an insert within the catalytic domain that contains an auto-inhibitory sequence. Like many other AGC kinases, NDR kinase requires phosphorylation at two sites, the activation loop (A-loop) and the hydrophobic motif (HM), for activity. The NDR1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270777 [Multi-domain]  Cd Length: 376  Bit Score: 99.73  E-value: 4.96e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 7989 YDILEEIGTGAFGVVHRCRERSTGNIFAAKFIPVSHSVEKDL---IRREIDIMNQLHHQKLINLHDAFEDDDEMILILEF 8065
Cdd:cd05628     3 FESLKVIGRGAFGEVRLVQKKDTGHVYAMKILRKADMLEKEQvghIRAERDILVEADSLWVVKMFYSFQDKLNLYLIMEF 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 8066 LSGGELFERITAEGyVMTEAEVINYMRQICEGIRHMHEQNIIHLDIKPENIMCQTRSstNVKLIDFGLATRL-------- 8137
Cdd:cd05628    83 LPGGDMMTLLMKKD-TLTEEETQFYIAETVLAIDSIHQLGFIHRDIKPDNLLLDSKG--HVKLSDFGLCTGLkkahrtef 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 8138 ----------------------------DPNEVVKITTGTAEFAAPEIVNREPVGFYTDMWATGVLSYVLLSGLSPFAGD 8189
Cdd:cd05628   160 yrnlnhslpsdftfqnmnskrkaetwkrNRRQLAFSTVGTPDYIAPEVFMQTGYNKLCDWWSLGVIMYEMLIGYPPFCSE 239
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|
gi 281359561 8190 NDVQTLKnvKACDWDfdvESFKY-----ISEEAKDFIRKL 8224
Cdd:cd05628   240 TPQETYK--KVMNWK---ETLIFppevpISEKAKDLILRF 274
FN3 COG3401
Fibronectin type 3 domain [General function prediction only];
4356-4776 6.18e-21

Fibronectin type 3 domain [General function prediction only];


Pssm-ID: 442628 [Multi-domain]  Cd Length: 603  Bit Score: 102.00  E-value: 6.18e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 4356 NCEYEFRVKAINAAGPGEPSDASKPIITKPRKLAPKIDRKNIRTYNFKSGEPIFLDINISGEPAPDVTWNQNNKSVQTTS 4435
Cdd:COG3401   108 NTGLTSSDEVPSPAVGTATTATAVAGGAATAGTYALGAGLYGVDGANASGTTASSVAGAGVVVSPDTSATAAVATTSLTV 187
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 4436 fshienLPYNTKYINNNPERKDTGLYKISAHNFYGQ----DQVEFqINIITKPGKPEGpLEVSEVHKDGCKLKWKKPKDD 4511
Cdd:COG3401   188 ------TSTTLVDGGGDIEPGTTYYYRVAATDTGGEsapsNEVSV-TTPTTPPSAPTG-LTATADTPGSVTLSWDPVTES 259
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 4512 GgepVESYLVEKFDPDTGIWLPVGRSDGPEYNVDGLVPGHDYKFRVKAVNKEG-ESEPLETLgsiiakdpfSVPTKPGVP 4590
Cdd:COG3401   260 D---ATGYRVYRSNSGDGPFTKVATVTTTSYTDTGLTNGTTYYYRVTAVDAAGnESAPSNVV---------SVTTDLTPP 327
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 4591 EP------TDWTANKVELAWpEPASDGGspIQGYIVEVKDKYSPLWEKALETNSpTPTATVQGLIEGNEYQFRVVALNKG 4664
Cdd:COG3401   328 AApsgltaTAVGSSSITLSW-TASSDAD--VTGYNVYRSTSGGGTYTKIAETVT-TTSYTDTGLTPGTTYYYKVTAVDAA 403
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 4665 GL-SEPSDPSKIFTAKPRYLAPKIDRRNLRNITLSSG-TALKLDANITGEPAPKVEWKLSNYHLQSGKNVTIETPDYYTk 4742
Cdd:COG3401   404 GNeSAPSEEVSATTASAASGESLTASVDAVPLTDVAGaTAAASAASNPGVSAAVLADGGDTGNAVPFTTTSSTVTATTT- 482
                         410       420       430
                  ....*....|....*....|....*....|....
gi 281359561 4743 LVIRPTQRSDSGEYLVTATNTSGKDSVLVNVVIT 4776
Cdd:COG3401   483 DTTTANLSVTTGSLVGGSGASSVTNSVSVIGASA 516
I-set pfam07679
Immunoglobulin I-set domain;
8740-8831 6.23e-21

Immunoglobulin I-set domain;


Pssm-ID: 400151 [Multi-domain]  Cd Length: 90  Bit Score: 90.78  E-value: 6.23e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561  8740 PKIVSHLESRFVRDGDAVNLACRIIGAQHFDVVWLHNNKEIKPSKDFQYTNEANIYRLQIAEIFPEDGGTYTCEAFNDIG 8819
Cdd:pfam07679    1 PKFTQKPKDVEVQEGESARFTCTVTGTPDPEVSWFKDGQPLRSSDRFKVTYEGGTYTLTISNVQPDDSGKYTCVATNSAG 80
                           90
                   ....*....|..
gi 281359561  8820 EsfSTCTINVTV 8831
Cdd:pfam07679   81 E--AEASAELTV 90
FN3 cd00063
Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein ...
4879-4970 9.76e-21

Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein fibronectin. Its tenth fibronectin type III repeat contains an RGD cell recognition sequence in a flexible loop between 2 strands. Approximately 2% of all animal proteins contain the FN3 repeat; including extracellular and intracellular proteins, membrane spanning cytokine receptors, growth hormone receptors, tyrosine phosphatase receptors, and adhesion molecules. FN3-like domains are also found in bacterial glycosyl hydrolases.


Pssm-ID: 238020 [Multi-domain]  Cd Length: 93  Bit Score: 90.25  E-value: 9.76e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 4879 PGKPENLKATDWDKDHVDLAWTPPLiDGGSPISCYIIEKQDKY-GKWERALDVPADQCKATIPDLVEGQTYKFRVSAVNA 4957
Cdd:cd00063     1 PSPPTNLRVTDVTSTSVTLSWTPPE-DDGGPITGYVVEYREKGsGDWKEVEVTPGSETSYTLTGLKPGTEYEFRVRAVNG 79
                          90
                  ....*....|...
gi 281359561 4958 AGTGEPSDSTPPI 4970
Cdd:cd00063    80 GGESPPSESVTVT 92
STKc_MAP4K3 cd06645
Catalytic domain of the Serine/Threonine Kinase, Mitogen-activated protein kinase kinase ...
7978-8245 1.06e-20

Catalytic domain of the Serine/Threonine Kinase, Mitogen-activated protein kinase kinase kinase kinase 3; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MAP4K3 plays a role in the nutrient-responsive pathway of mTOR (mammalian target of rapamycin) signaling. MAP4K3 is required in the activation of S6 kinase by amino acids and for the phosphorylation of the mTOR-regulated inhibitor of eukaryotic initiation factor 4E. mTOR regulates ribosome biogenesis and protein translation, and is frequently deregulated in cancer. MAP4Ks are involved in MAPK signaling pathways by activating a MAPK kinase kinase. Each MAPK cascade is activated either by a small GTP-binding protein or by an adaptor protein, which transmits the signal either directly to a MAP3K to start the triple kinase core cascade or indirectly through a mediator kinase, a MAP4K. Members of this subfamily contain an N-terminal catalytic domain and a C-terminal citron homology (CNH) regulatory domain. The MAP4K3 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270812 [Multi-domain]  Cd Length: 272  Bit Score: 96.27  E-value: 1.06e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 7978 VEISQQSVYDRYDILEEIGTGAFGVVHRCRERSTGNIFAAKFIPVSHSVEKDLIRREIDIMNQLHHQKLINLHDAFEDDD 8057
Cdd:cd06645     2 LDLSRRNPQEDFELIQRIGSGTYGDVYKARNVNTGELAAIKVIKLEPGEDFAVVQQEIIMMKDCKHSNIVAYFGSYLRRD 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 8058 EMILILEFLSGGELFERITAEGyVMTEAEVINYMRQICEGIRHMHEQNIIHLDIKPENIMCQtrSSTNVKLIDFGLATRL 8137
Cdd:cd06645    82 KLWICMEFCGGGSLQDIYHVTG-PLSESQIAYVSRETLQGLYYLHSKGKMHRDIKGANILLT--DNGHVKLADFGVSAQI 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 8138 DPNEVVKIT-TGTAEFAAPEIVNREPVGFYT---DMWATGVLSyVLLSGLSPFAGDndvqtLKNVKACdwdFDVESFKYI 8213
Cdd:cd06645   159 TATIAKRKSfIGTPYWMAPEVAAVERKGGYNqlcDIWAVGITA-IELAELQPPMFD-----LHPMRAL---FLMTKSNFQ 229
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|..
gi 281359561 8214 SEEAKD----------FIRKLLVRNKEKRMTAHECLLHPWLT 8245
Cdd:cd06645   230 PPKLKDkmkwsnsfhhFVKMALTKNPKKRPTAEKLLQHPFVT 271
STKc_nPKC_theta cd05619
Catalytic domain of the Serine/Threonine Kinase, Novel Protein Kinase C theta; STKs catalyze ...
7995-8233 1.07e-20

Catalytic domain of the Serine/Threonine Kinase, Novel Protein Kinase C theta; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PKC-theta is selectively expressed in T-cells and plays an important and non-redundant role in several aspects of T-cell biology. Although T-cells also express other PKC isoforms, PKC-theta is unique in that upon antigen stimulation, it is translocated to the plasma membrane at the immunological synapse, where it mediates signals essential for T-cell activation. It is essential for TCR-induced proliferation, cytokine production, T-cell survival, and the differentiation and effector function of T-helper (Th) cells, particularly Th2 and Th17. PKC-theta is being developed as a therapeutic target for Th2-mediated allergic inflammation and Th17-mediated autoimmune diseases. PKCs are classified into three groups (classical, atypical, and novel) depending on their mode of activation and the structural characteristics of their regulatory domain. nPKCs are calcium-independent, but require DAG (1,2-diacylglycerol) and phosphatidylserine (PS) for activity. The nPKC subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270770 [Multi-domain]  Cd Length: 331  Bit Score: 97.69  E-value: 1.07e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 7995 IGTGAFGVVHRCRERSTGNIFAAKfipvshSVEKDLIRREIDIMNQL----------HHQKLINLHDAFEDDDEMILILE 8064
Cdd:cd05619    13 LGKGSFGKVFLAELKGTNQFFAIK------ALKKDVVLMDDDVECTMvekrvlslawEHPFLTHLFCTFQTKENLFFVME 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 8065 FLSGGELFERI-TAEGYVMTEAEVinYMRQICEGIRHMHEQNIIHLDIKPENIMCQTRSstNVKLIDFGLATRLDPNEVV 8143
Cdd:cd05619    87 YLNGGDLMFHIqSCHKFDLPRATF--YAAEIICGLQFLHSKGIVYRDLKLDNILLDKDG--HIKIADFGMCKENMLGDAK 162
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 8144 KIT-TGTAEFAAPEIVNREPVGFYTDMWATGVLSYVLLSGLSPFAGDNDVQTLKNVKACDWDFDvesfKYISEEAKDFIR 8222
Cdd:cd05619   163 TSTfCGTPDYIAPEILLGQKYNTSVDWWSFGVLLYEMLIGQSPFHGQDEEELFQSIRMDNPFYP----RWLEKEAKDILV 238
                         250
                  ....*....|.
gi 281359561 8223 KLLVRNKEKRM 8233
Cdd:cd05619   239 KLFVREPERRL 249
FN3 cd00063
Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein ...
4584-4677 1.09e-20

Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein fibronectin. Its tenth fibronectin type III repeat contains an RGD cell recognition sequence in a flexible loop between 2 strands. Approximately 2% of all animal proteins contain the FN3 repeat; including extracellular and intracellular proteins, membrane spanning cytokine receptors, growth hormone receptors, tyrosine phosphatase receptors, and adhesion molecules. FN3-like domains are also found in bacterial glycosyl hydrolases.


Pssm-ID: 238020 [Multi-domain]  Cd Length: 93  Bit Score: 90.25  E-value: 1.09e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 4584 PTKPGVPEPTDWTANKVELAWpEPASDGGSPIQGYIVEVKDKYSPLWEKALETNSPTPTATVQGLIEGNEYQFRVVALNK 4663
Cdd:cd00063     1 PSPPTNLRVTDVTSTSVTLSW-TPPEDDGGPITGYVVEYREKGSGDWKEVEVTPGSETSYTLTGLKPGTEYEFRVRAVNG 79
                          90
                  ....*....|....
gi 281359561 4664 GGLSEPSDPSKIFT 4677
Cdd:cd00063    80 GGESPPSESVTVTT 93
STKc_CK1 cd14016
Catalytic domain of the Serine/Threonine protein kinase, Casein Kinase 1; STKs catalyze the ...
7988-8153 1.22e-20

Catalytic domain of the Serine/Threonine protein kinase, Casein Kinase 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. CK1 phosphorylates a variety of substrates including enzymes, transcription and splice factors, cytoskeletal proteins, viral oncogenes, receptors, and membrane-associated proteins. There are mutliple isoforms of CK1 and in mammals, seven isoforms (alpha, beta, gamma1-3, delta, and epsilon) have been characterized. These isoforms differ mainly in the length and structure of their C-terminal non-catalytic region. Some isoforms have several splice variants such as the long (L) and short (S) variants of CK1alpha. CK1 proteins are involved in the regulation of many cellular processes including membrane transport processes, circadian rhythm, cell division, apoptosis, and the development of cancer and neurodegenerative diseases. The CK1 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270918 [Multi-domain]  Cd Length: 266  Bit Score: 95.99  E-value: 1.22e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 7988 RYDILEEIGTGAFGVVHRCRERSTGNIFAAKFIPVSHsvEKDLIRREIDIMNQLHHQKLI-NLHDAFEDDDEMILILEFL 8066
Cdd:cd14016     1 RYKLVKKIGSGSFGEVYLGIDLKTGEEVAIKIEKKDS--KHPQLEYEAKVYKLLQGGPGIpRLYWFGQEGDYNVMVMDLL 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 8067 --SGGELFERItaeGYVMTEAEVINYMRQICEGIRHMHEQNIIHLDIKPENIMC-QTRSSTNVKLIDFGLATR-LDPNEV 8142
Cdd:cd14016    79 gpSLEDLFNKC---GRKFSLKTVLMLADQMISRLEYLHSKGYIHRDIKPENFLMgLGKNSNKVYLIDFGLAKKyRDPRTG 155
                         170
                  ....*....|....*...
gi 281359561 8143 VKIT-------TGTAEFA 8153
Cdd:cd14016   156 KHIPyregkslTGTARYA 173
FN3 cd00063
Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein ...
7151-7237 1.31e-20

Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein fibronectin. Its tenth fibronectin type III repeat contains an RGD cell recognition sequence in a flexible loop between 2 strands. Approximately 2% of all animal proteins contain the FN3 repeat; including extracellular and intracellular proteins, membrane spanning cytokine receptors, growth hormone receptors, tyrosine phosphatase receptors, and adhesion molecules. FN3-like domains are also found in bacterial glycosyl hydrolases.


Pssm-ID: 238020 [Multi-domain]  Cd Length: 93  Bit Score: 90.25  E-value: 1.31e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 7151 PSPPGAPQVTRVGKNYVDLKWEKPlRDGGSRITGYIIERRDIGGAVWVKCNDYNVLDTEYTVMNLIEMGDYEFRVFAVNS 7230
Cdd:cd00063     1 PSPPTNLRVTDVTSTSVTLSWTPP-EDDGGPITGYVVEYREKGSGDWKEVEVTPGSETSYTLTGLKPGTEYEFRVRAVNG 79

                  ....*..
gi 281359561 7231 AGRSEPS 7237
Cdd:cd00063    80 GGESPPS 86
STKc_PKB_alpha cd05594
Catalytic domain of the Serine/Threonine Kinase, Protein Kinase B alpha (also called Akt1); ...
7989-8246 1.31e-20

Catalytic domain of the Serine/Threonine Kinase, Protein Kinase B alpha (also called Akt1); STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PKB-alpha is predominantly expressed in endothelial cells. It is critical for the regulation of angiogenesis and the maintenance of vascular integrity. It also plays a role in adipocyte differentiation. Mice deficient in PKB-alpha exhibit perinatal morbidity, growth retardation, reduction in body weight accompanied by reduced sizes of multiple organs, and enhanced apoptosis in some cell types. PKB-alpha activity has been reported to be frequently elevated in breast and prostate cancers. In some cancer cells, PKB-alpha may act as a suppressor of metastasis. PKB contains an N-terminal pleckstrin homology (PH) domain and a C-terminal catalytic domain. The PKB-alpha subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270746 [Multi-domain]  Cd Length: 356  Bit Score: 97.79  E-value: 1.31e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 7989 YDILEEIGTGAFGVVHRCRERSTGNIFAAKFIPVSHSVEKDLIRR---EIDIMNQLHHQKLINLHDAFEDDDEMILILEF 8065
Cdd:cd05594    27 FEYLKLLGKGTFGKVILVKEKATGRYYAMKILKKEVIVAKDEVAHtltENRVLQNSRHPFLTALKYSFQTHDRLCFVMEY 106
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 8066 LSGGELFERITAEgYVMTEAEVINYMRQICEGIRHMH-EQNIIHLDIKPENIMCQtrSSTNVKLIDFGLATR-LDPNEVV 8143
Cdd:cd05594   107 ANGGELFFHLSRE-RVFSEDRARFYGAEIVSALDYLHsEKNVVYRDLKLENLMLD--KDGHIKITDFGLCKEgIKDGATM 183
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 8144 KITTGTAEFAAPEIVNREPVGFYTDMWATGVLSYVLLSGLSPFAGDNDVQTLKNVKACDWDFDvesfKYISEEAKDFIRK 8223
Cdd:cd05594   184 KTFCGTPEYLAPEVLEDNDYGRAVDWWGLGVVMYEMMCGRLPFYNQDHEKLFELILMEEIRFP----RTLSPEAKSLLSG 259
                         250       260
                  ....*....|....*....|....*...
gi 281359561 8224 LLVRNKEKRM-----TAHECLLHPWLTG 8246
Cdd:cd05594   260 LLKKDPKQRLgggpdDAKEIMQHKFFAG 287
STKc_IRE1 cd13982
Catalytic domain of the Serine/Threonine kinase, Inositol-requiring protein 1; STKs catalyze ...
8048-8242 1.40e-20

Catalytic domain of the Serine/Threonine kinase, Inositol-requiring protein 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. IRE1, also called Endoplasmic reticulum (ER)-to-nucleus signaling protein (or ERN), is an ER-localized type I transmembrane protein with kinase and endoribonuclease domains in the cytoplasmic side. It acts as an ER stress sensor and is the oldest and most conserved component of the unfolded protein response (UPR) in eukaryotes. The UPR is activated when protein misfolding is detected in the ER in order to decrease the synthesis of new proteins and increase the capacity of the ER to cope with the stress. During ER stress, IRE1 dimerizes and forms oligomers, allowing the kinase domain to undergo trans-autophosphorylation. This leads to a conformational change that stimulates its endoribonuclease activity and results in the cleavage of its mRNA substrate, HAC1 in yeast and XBP1 in metazoans, promoting a splicing event that enables translation into a transcription factor which activates the UPR. Mammals contain two IRE1 proteins, IRE1alpha (or ERN1) and IRE1beta (or ERN2). The Ire1 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270884 [Multi-domain]  Cd Length: 269  Bit Score: 95.80  E-value: 1.40e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 8048 NLHDAFEDDDEmilileflsgGELFERItaegyvmtEAEVINYMRQICEGIRHMHEQNIIHLDIKPENIMCQTRSSTN-- 8125
Cdd:cd13982    80 SLQDLVESPRE----------SKLFLRP--------GLEPVRLLRQIASGLAHLHSLNIVHRDLKPQNILISTPNAHGnv 141
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 8126 -VKLIDFGLATRLDPNE----VVKITTGTAEFAAPEIVNREPVGFYT---DMWATG-VLSYVLLSGLSPFaGDN---DVQ 8193
Cdd:cd13982   142 rAMISDFGLCKKLDVGRssfsRRSGVAGTSGWIAPEMLSGSTKRRQTravDIFSLGcVFYYVLSGGSHPF-GDKlerEAN 220
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*....
gi 281359561 8194 TLKNVKACDWDFDVESFkyiSEEAKDFIRKLLVRNKEKRMTAHECLLHP 8242
Cdd:cd13982   221 ILKGKYSLDKLLSLGEH---GPEAQDLIERMIDFDPEKRPSAEEVLNHP 266
STKc_NAK1_like cd06917
Catalytic domain of Fungal Nak1-like Serine/Threonine Kinases; STKs catalyze the transfer of ...
7984-8257 1.50e-20

Catalytic domain of Fungal Nak1-like Serine/Threonine Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily is composed of Schizosaccharomyces pombe Nak1, Saccharomyces cerevisiae Kic1p (kinase that interacts with Cdc31p) and related proteins. Nak1 (also called N-rich kinase 1), is required by fission yeast for polarizing the tips of actin cytoskeleton and is involved in cell growth, cell separation, cell morphology and cell-cycle progression. Kic1p is required by budding yeast for cell integrity and morphogenesis. Kic1p interacts with Cdc31p, the yeast homologue of centrin, and phosphorylates substrates in a Cdc31p-dependent manner. The Nak1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270822 [Multi-domain]  Cd Length: 277  Bit Score: 96.00  E-value: 1.50e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 7984 SVYDRYDIleeIGTGAFGVVHRCRERSTGNIFAAKFIPV-SHSVEKDLIRREIDIMNQLHHQKLINL---HDAFEDDDEM 8059
Cdd:cd06917     1 SLYRRLEL---VGRGSYGAVYRGYHVKTGRVVALKVLNLdTDDDDVSDIQKEVALLSQLKLGQPKNIikyYGSYLKGPSL 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 8060 ILILEFLSGGELfeRITAEGYVMTEAEVINYMRQICEGIRHMHEQNIIHLDIKPENIMCQTrsSTNVKLIDFGLATRLDP 8139
Cdd:cd06917    78 WIIMDYCEGGSI--RTLMRAGPIAERYIAVIMREVLVALKFIHKDGIIHRDIKAANILVTN--TGNVKLCDFGVAASLNQ 153
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 8140 NEVVKIT-TGTAEFAAPEIVnREPVGFYT--DMWATGVLSYVLLSGLSPFAGDNDVQTLKNV-KACDWDFDVESFkyiSE 8215
Cdd:cd06917   154 NSSKRSTfVGTPYWMAPEVI-TEGKYYDTkaDIWSLGITTYEMATGNPPYSDVDALRAVMLIpKSKPPRLEGNGY---SP 229
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*.
gi 281359561 8216 EAKDFIRKLLVRNKEKRMTAHECLLHPWL----TGDHSAMKQEINR 8257
Cdd:cd06917   230 LLKEFVAACLDEEPKDRLSADELLKSKWIkqhsKTPTSVLKELISR 275
FN3 COG3401
Fibronectin type 3 domain [General function prediction only];
2673-2891 1.71e-20

Fibronectin type 3 domain [General function prediction only];


Pssm-ID: 442628 [Multi-domain]  Cd Length: 603  Bit Score: 100.46  E-value: 1.71e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 2673 FYTLKAEN--RNGIDRETVELVVLGKPSSPKGPLAVSDVTASGCKLQWKKPEDDGgvpIKEYVVEKMDTATGKWVRVGRS 2750
Cdd:COG3401   206 YYRVAATDtgGESAPSNEVSVTTPTTPPSAPTGLTATADTPGSVTLSWDPVTESD---ATGYRVYRSNSGDGPFTKVATV 282
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 2751 PGekepPSFDVTGLSLGSEYMFRVSAVNEEG-ESEPLTTLVGVVAKDPfdePNKPGTPEVTDYDNQSISLKWAAPnndGG 2829
Cdd:COG3401   283 TT----TSYTDTGLTNGTTYYYRVTAVDAAGnESAPSNVVSVTTDLTP---PAAPSGLTATAVGSSSITLSWTAS---SD 352
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 281359561 2830 APIQKYIIEKKNKNKTEWEKaLEIPGDQLEATVAGLQEYGEYQFRVIAVNKAGLSPPSDASV 2891
Cdd:COG3401   353 ADVTGYNVYRSTSGGGTYTK-IAETVTTTSYTDTGLTPGTTYYYKVTAVDAAGNESAPSEEV 413
FN3 COG3401
Fibronectin type 3 domain [General function prediction only];
2957-3191 1.93e-20

Fibronectin type 3 domain [General function prediction only];


Pssm-ID: 442628 [Multi-domain]  Cd Length: 603  Bit Score: 100.46  E-value: 1.93e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 2957 IPYNTKISIIETVRKHTGIYKIIAVNEHGQDEATVEVNILA---PPSKPRGpLDVKDVTKDSCKLKWKKPEDDGgkpISA 3033
Cdd:COG3401   188 TSTTLVDGGGDIEPGTTYYYRVAATDTGGESAPSNEVSVTTpttPPSAPTG-LTATADTPGSVTLSWDPVTESD---ATG 263
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 3034 YQVEKFDKKQGRWVPLGRTsaNDTEFDVKGLQEGHEYQFRVKAINEEG-ESDPLDSDDSIIAKNPydaaskPGTPNIVDY 3112
Cdd:COG3401   264 YRVYRSNSGDGPFTKVATV--TTTSYTDTGLTNGTTYYYRVTAVDAAGnESAPSNVVSVTTDLTP------PAAPSGLTA 335
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 3113 NEHM---VKLKWEAPrSDGGApiSGYIIEKKDKFSPIWDEILSTNTSvPEATVEGLVEGNIYQFRVRAVNKAG-FSDPSD 3188
Cdd:COG3401   336 TAVGsssITLSWTAS-SDADV--TGYNVYRSTSGGGTYTKIAETVTT-TSYTDTGLTPGTTYYYKVTAVDAAGnESAPSE 411

                  ...
gi 281359561 3189 ATE 3191
Cdd:COG3401   412 EVS 414
I-set pfam07679
Immunoglobulin I-set domain;
8312-8401 2.68e-20

Immunoglobulin I-set domain;


Pssm-ID: 400151 [Multi-domain]  Cd Length: 90  Bit Score: 88.85  E-value: 2.68e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561  8312 PRFVIRPSSQFCYEGQSVKFYCRCIAIATPTLTWSHNNIELRQSVKFMKRYVGDDYYFIINRVKLDDRGEYIIRAENHYG 8391
Cdd:pfam07679    1 PKFTQKPKDVEVQEGESARFTCTVTGTPDPEVSWFKDGQPLRSSDRFKVTYEGGTYTLTISNVQPDDSGKYTCVATNSAG 80
                           90
                   ....*....|
gi 281359561  8392 SREEVVFLNV 8401
Cdd:pfam07679   81 EAEASAELTV 90
I-set pfam07679
Immunoglobulin I-set domain;
7648-7737 2.95e-20

Immunoglobulin I-set domain;


Pssm-ID: 400151 [Multi-domain]  Cd Length: 90  Bit Score: 88.85  E-value: 2.95e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561  7648 PLIVKPLRDANCIQNHNAQFTCTINGVPKPTISWYKGAREISNGARYHMYSEGDNHFLNINDVFGEDADEYVCRAVNKAG 7727
Cdd:pfam07679    1 PKFTQKPKDVEVQEGESARFTCTVTGTPDPEVSWFKDGQPLRSSDRFKVTYEGGTYTLTISNVQPDDSGKYTCVATNSAG 80
                           90
                   ....*....|
gi 281359561  7728 AKSTRATLAI 7737
Cdd:pfam07679   81 EAEASAELTV 90
STKc_aPKC_zeta cd05617
Catalytic domain of the Serine/Threonine Kinase, Atypical Protein Kinase C zeta; STKs catalyze ...
7978-8186 3.14e-20

Catalytic domain of the Serine/Threonine Kinase, Atypical Protein Kinase C zeta; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PKC-zeta plays a critical role in activating the glucose transport response. It is activated by glucose, insulin, and exercise through diverse pathways. PKC-zeta also plays a central role in maintaining cell polarity in yeast and mammalian cells. In addition, it affects actin remodeling in muscle cells. PKCs are classified into three groups (classical, atypical, and novel) depending on their mode of activation and the structural characteristics of their regulatory domain. aPKCs only require phosphatidylserine (PS) for activation. The aPKC-zeta subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270768 [Multi-domain]  Cd Length: 357  Bit Score: 96.63  E-value: 3.14e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 7978 VEISQQSVYDRYDILEEIGTGAFGVVHRCRERSTGNIFAAKFIP---VSHSVEKDLIRREIDIMNQLHHQK-LINLHDAF 8053
Cdd:cd05617     6 IKISQGLGLQDFDLIRVIGRGSYAKVLLVRLKKNDQIYAMKVVKkelVHDDEDIDWVQTEKHVFEQASSNPfLVGLHSCF 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 8054 EDDDEMILILEFLSGGELFERITAEgYVMTEAEVINYMRQICEGIRHMHEQNIIHLDIKPENIMCQtrSSTNVKLIDFGL 8133
Cdd:cd05617    86 QTTSRLFLVIEYVNGGDLMFHMQRQ-RKLPEEHARFYAAEICIALNFLHERGIIYRDLKLDNVLLD--ADGHIKLTDYGM 162
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....
gi 281359561 8134 ATR-LDPNEVVKITTGTAEFAAPEIVNREPVGFYTDMWATGVLSYVLLSGLSPF 8186
Cdd:cd05617   163 CKEgLGPGDTTSTFCGTPNYIAPEILRGEEYGFSVDWWALGVLMFEMMAGRSPF 216
STKc_aPKC_iota cd05618
Catalytic domain of the Serine/Threonine Kinase, Atypical Protein Kinase C iota; STKs catalyze ...
7989-8236 3.21e-20

Catalytic domain of the Serine/Threonine Kinase, Atypical Protein Kinase C iota; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PKC-iota is directly implicated in carcinogenesis. It is critical to oncogenic signaling mediated by Ras and Bcr-Abl. The PKC-iota gene is the target of tumor-specific gene amplification in many human cancers, and has been identified as a human oncogene. In addition to its role in transformed growth, PKC-iota also promotes invasion, chemoresistance, and tumor cell survival. Expression profiling of PKC-iota is a prognostic marker of poor clinical outcome in several human cancers. PKC-iota also plays a role in establishing cell polarity, and has critical embryonic functions. PKCs are classified into three groups (classical, atypical, and novel) depending on their mode of activation and the structural characteristics of their regulatory domain. aPKCs only require phosphatidylserine (PS) for activation. The aPKC subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270769 [Multi-domain]  Cd Length: 364  Bit Score: 97.03  E-value: 3.21e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 7989 YDILEEIGTGAFGVVHRCRERSTGNIFAAKFIP---VSHSVEKDLIRREIDIMNQL-HHQKLINLHDAFEDDDEMILILE 8064
Cdd:cd05618    22 FDLLRVIGRGSYAKVLLVRLKKTERIYAMKVVKkelVNDDEDIDWVQTEKHVFEQAsNHPFLVGLHSCFQTESRLFFVIE 101
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 8065 FLSGGELFERITAEgYVMTEAEVINYMRQICEGIRHMHEQNIIHLDIKPENIMCQtrSSTNVKLIDFGLATR-LDPNEVV 8143
Cdd:cd05618   102 YVNGGDLMFHMQRQ-RKLPEEHARFYSAEISLALNYLHERGIIYRDLKLDNVLLD--SEGHIKLTDYGMCKEgLRPGDTT 178
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 8144 KITTGTAEFAAPEIVNREPVGFYTDMWATGVLSYVLLSGLSPF----AGDNDVQTLKnvkacDWDFDVESFKYI------ 8213
Cdd:cd05618   179 STFCGTPNYIAPEILRGEDYGFSVDWWALGVLMFEMMAGRSPFdivgSSDNPDQNTE-----DYLFQVILEKQIriprsl 253
                         250       260
                  ....*....|....*....|...
gi 281359561 8214 SEEAKDFIRKLLVRNKEKRMTAH 8236
Cdd:cd05618   254 SVKAASVLKSFLNKDPKERLGCH 276
PTKc_Wee1 cd14051
Catalytic domain of the Protein Tyrosine Kinase, Wee1; PTKs catalyze the transfer of the ...
7992-8123 3.42e-20

Catalytic domain of the Protein Tyrosine Kinase, Wee1; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Wee1 is a nuclear cell cycle checkpoint kinase that helps keep the cyclin-dependent kinase CDK1 in an inactive state through phosphorylation of an N-terminal tyr (Y15) residue. During the late G2 phase, CDK1 is activated and mitotic entry is promoted by the removal of this inhibitory phosphorylation by the phosphatase Cdc25. Although Wee1 is functionally a tyr kinase, it is more closely related to serine/threonine kinases (STKs). It contains a catalytic kinase domain sandwiched in between N- and C-terminal regulatory domains. It is regulated by phosphorylation and degradation, and its expression levels are also controlled by circadian clock proteins. There are two distinct Wee1 proteins in vertebrates showing different expression patterns, called Wee1a and Wee1b. They are functionally dstinct and are implicated in different steps of egg maturation and embryo development. The Wee1 subfamily is part of a larger superfamily that includes the catalytic domains of STKs, other PTKs, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270953 [Multi-domain]  Cd Length: 275  Bit Score: 94.78  E-value: 3.42e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 7992 LEEIGTGAFGVVHRCRERSTGNIFAAK--FIPVSHSVEKDLIRREIDIMNQL-HHQKLINLHDAFEDDDEMILILEFLSG 8068
Cdd:cd14051     5 VEKIGSGEFGSVYKCINRLDGCVYAIKksKKPVAGSVDEQNALNEVYAHAVLgKHPHVVRYYSAWAEDDHMIIQNEYCNG 84
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 281359561 8069 GELFERITA---EGYVMTEAEVINYMRQICEGIRHMHEQNIIHLDIKPENI-MCQTRSS 8123
Cdd:cd14051    85 GSLADAISEnekAGERFSEAELKDLLLQVAQGLKYIHSQNLVHMDIKPGNIfISRTPNP 143
FN3 cd00063
Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein ...
6754-6840 3.42e-20

Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein fibronectin. Its tenth fibronectin type III repeat contains an RGD cell recognition sequence in a flexible loop between 2 strands. Approximately 2% of all animal proteins contain the FN3 repeat; including extracellular and intracellular proteins, membrane spanning cytokine receptors, growth hormone receptors, tyrosine phosphatase receptors, and adhesion molecules. FN3-like domains are also found in bacterial glycosyl hydrolases.


Pssm-ID: 238020 [Multi-domain]  Cd Length: 93  Bit Score: 88.71  E-value: 3.42e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 6754 PNTPGIPHGIDSTEDSITIAWTKPKHDGGsPITGYIIEKRLLSDDKWTKAVHALCPDLSCKIPNLIENAEYEFRVAAVNA 6833
Cdd:cd00063     1 PSPPTNLRVTDVTSTSVTLSWTPPEDDGG-PITGYVVEYREKGSGDWKEVEVTPGSETSYTLTGLKPGTEYEFRVRAVNG 79

                  ....*..
gi 281359561 6834 AGQSAYS 6840
Cdd:cd00063    80 GGESPPS 86
PKc_DYRK4 cd14225
Catalytic domain of the protein kinase, Dual-specificity tYrosine-phosphorylated and ...
7988-8244 3.48e-20

Catalytic domain of the protein kinase, Dual-specificity tYrosine-phosphorylated and -Regulated Kinase 4; Dual-specificity PKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine (S/T) as well as tyrosine residues on protein substrates. DYRK4 is a testis-specific kinase with restricted expression to postmeiotic spermatids. It may function during spermiogenesis, however, it is not required for male fertility. DYRK4 has also been detected in a human teratocarcinoma cell line induced to produce postmitotic neurons. It may have a role in neuronal differentiation. DYRKs autophosphorylate themselves on tyrosine residues and phosphorylate their substrates exclusively on S/T residues. They play important roles in cell proliferation, differentiation, survival, and development. The DYRK4 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271127 [Multi-domain]  Cd Length: 341  Bit Score: 96.31  E-value: 3.48e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 7988 RYDILEEIGTGAFGVVHRCRERSTGNIFAAKfipvshsvekdLIRREidimNQLHHQKLINLH--DAFEDDDE-----MI 8060
Cdd:cd14225    44 RYEILEVIGKGSFGQVVKALDHKTNEHVAIK-----------IIRNK----KRFHHQALVEVKilDALRRKDRdnshnVI 108
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 8061 LILEF------------LSGGELFERITAEGYVMTEAEVInymRQICEGI----RHMHEQNIIHLDIKPENIMCQTRSST 8124
Cdd:cd14225   109 HMKEYfyfrnhlcitfeLLGMNLYELIKKNNFQGFSLSLI---RRFAISLlqclRLLYRERIIHCDLKPENILLRQRGQS 185
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 8125 NVKLIDFGlaTRLDPNEVVKITTGTAEFAAPEIVNREPVGFYTDMWATGVLSYVLLSGLSPFAGDNDVQTLknvkACDWD 8204
Cdd:cd14225   186 SIKVIDFG--SSCYEHQRVYTYIQSRFYRSPEVILGLPYSMAIDMWSLGCILAELYTGYPLFPGENEVEQL----ACIME 259
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 8205 -FDVESFKYISEEAK-----------------------------------------DFIRKLLVRNKEKRMTAHECLLHP 8242
Cdd:cd14225   260 vLGLPPPELIENAQRrrlffdskgnprcitnskgkkrrpnskdlasalktsdplflDFIRRCLEWDPSKRMTPDEALQHE 339

                  ..
gi 281359561 8243 WL 8244
Cdd:cd14225   340 WI 341
STKc_TLK1 cd14040
Catalytic domain of the Serine/Threonine kinase, Tousled-Like Kinase 1; STKs catalyze the ...
7984-8244 4.38e-20

Catalytic domain of the Serine/Threonine kinase, Tousled-Like Kinase 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. A splice variant of TLK1, called TLK1B, is expressed in the presence of double strand breaks (DSBs). It lacks the N-terminal part of TLK1, but is expected to phosphorylate the same substrates. TLK1/1B interacts with Rad9, which is critical in DNA damage-activated checkpoint response, and plays a role in the repair of linearized DNA with incompatible ends. TLKs play important functions during the cell cycle and are implicated in chromatin remodeling, DNA replication and repair, and mitosis. The TLK1 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270942 [Multi-domain]  Cd Length: 299  Bit Score: 95.12  E-value: 4.38e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 7984 SVYDRYDILEEIGTGAFGVVHRCRERSTGNIFAAKFIPVSHSVEKDLIR-------REIDIMNQLHHQKLINLHDAFE-D 8055
Cdd:cd14040     3 TLNERYLLLHLLGRGGFSEVYKAFDLYEQRYAAVKIHQLNKSWRDEKKEnyhkhacREYRIHKELDHPRIVKLYDYFSlD 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 8056 DDEMILILEFLSGGELfERITAEGYVMTEAEVINYMRQICEGIRHMHEQN--IIHLDIKPENIM-CQTRSSTNVKLIDFG 8132
Cdd:cd14040    83 TDTFCTVLEYCEGNDL-DFYLKQHKLMSEKEARSIVMQIVNALRYLNEIKppIIHYDLKPGNILlVDGTACGEIKITDFG 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 8133 LATRLDPN-------EVVKITTGTAEFAAPE--IVNREP--VGFYTDMWATGVLSYVLLSGLSPFAGDNDVQTLKN---- 8197
Cdd:cd14040   162 LSKIMDDDsygvdgmDLTSQGAGTYWYLPPEcfVVGKEPpkISNKVDVWSVGVIFFQCLYGRKPFGHNQSQQDILQenti 241
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*..
gi 281359561 8198 VKACDWDFDVESFkyISEEAKDFIRKLLVRNKEKRMTAHECLLHPWL 8244
Cdd:cd14040   242 LKATEVQFPVKPV--VSNEAKAFIRRCLAYRKEDRFDVHQLASDPYL 286
FN3 COG3401
Fibronectin type 3 domain [General function prediction only];
5958-6312 4.53e-20

Fibronectin type 3 domain [General function prediction only];


Pssm-ID: 442628 [Multi-domain]  Cd Length: 603  Bit Score: 99.31  E-value: 4.53e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 5958 PGPPEGpMEYEEITANSVTISWKPPKDNGgseISSYVIEkRDLTHGGGWVPAVNYVSAKYnhaVVPRLLEGTMYELRVMA 6037
Cdd:COG3401   233 PSAPTG-LTATADTPGSVTLSWDPVTESD---ATGYRVY-RSNSGDGPFTKVATVTTTSY---TDTGLTNGTTYYYRVTA 304
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 6038 ENLQG-RSDPltSDqPVVAKSQYTVPGAPGKPELTDSDKNHITIKWKqpiSNGGSPIIGYDIERRDVNTGRWIKInGQPV 6116
Cdd:COG3401   305 VDAAGnESAP--SN-VVSVTTDLTPPAAPSGLTATAVGSSSITLSWT---ASSDADVTGYNVYRSTSGGGTYTKI-AETV 377
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 6117 PTAEYQDDRVTSNHQYQYRISAVNAAGNgkTSEPSAIFNARPLREKPRFYFDGLIgkrIKVRAGEPVNLNIPISGAPTPT 6196
Cdd:COG3401   378 TTTSYTDTGLTPGTTYYYKVTAVDAAGN--ESAPSEEVSATTASAASGESLTASV---DAVPLTDVAGATAAASAASNPG 452
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 6197 IEWKRGDLKLEEGKRISYETNSERTLFRIDDSNRRDSGKYTVTAANEFGKDTADIEVIVVDKPSPPEGPLSYTETAPDhi 6276
Cdd:COG3401   453 VSAAVLADGGDTGNAVPFTTTSSTVTATTTDTTTANLSVTTGSLVGGSGASSVTNSVSVIGASAAAAVGGAPDGTPNV-- 530
                         330       340       350
                  ....*....|....*....|....*....|....*.
gi 281359561 6277 slhWYSPKDDGGSDITGYIIEFTEFGVDDWKPVPGT 6312
Cdd:COG3401   531 ---TGASPVTVGASTGDVLITDLVSLTTSASSSVSG 563
STKc_NIK cd13991
Catalytic domain of the Serine/Threonine kinase, NF-kappaB Inducing Kinase (NIK); STKs ...
7995-8186 5.22e-20

Catalytic domain of the Serine/Threonine kinase, NF-kappaB Inducing Kinase (NIK); STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. NIK, also called mitogen activated protein kinase kinase kinase 14 (MAP3K14), phosphorylates and activates Inhibitor of NF-KappaB Kinase (IKK) alpha, which is a regulator of NF-kB proteins, a family of transcription factors which are critical in many cellular functions including inflammatory responses, immune development, cell survival, and cell proliferation, among others. NIK is essential in the IKKalpha-mediated non-canonical NF-kB signaling pathway, in which IKKalpha processes the IkB-like C-terminus of NF-kB2/p100 to produce p52, allowing the p52/RelB dimer to migrate to the nucleus where it regulates gene transcription. NIK also plays an important role in Toll-like receptor 7/9 signaling cascades. The NIK subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270893 [Multi-domain]  Cd Length: 268  Bit Score: 94.11  E-value: 5.22e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 7995 IGTGAFGVVHRCRERSTGNIFAAKFIPVSH-SVEkdlirrEIDIMNQLHHQKLINLHDAFEDDDEMILILEFLSGGELFE 8073
Cdd:cd13991    14 IGRGSFGEVHRMEDKQTGFQCAVKKVRLEVfRAE------ELMACAGLTSPRVVPLYGAVREGPWVNIFMDLKEGGSLGQ 87
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 8074 RITAEGyVMTEAEVINYMRQICEGIRHMHEQNIIHLDIKPENIMCQTRSStNVKLIDFGLATRLDPNEVVK------ITT 8147
Cdd:cd13991    88 LIKEQG-CLPEDRALHYLGQALEGLEYLHSRKILHGDVKADNVLLSSDGS-DAFLCDFGHAECLDPDGLGKslftgdYIP 165
                         170       180       190
                  ....*....|....*....|....*....|....*....
gi 281359561 8148 GTAEFAAPEIVNREPVGFYTDMWATGVLSYVLLSGLSPF 8186
Cdd:cd13991   166 GTETHMAPEVVLGKPCDAKVDVWSSCCMMLHMLNGCHPW 204
FN3 cd00063
Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein ...
3296-3390 5.46e-20

Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein fibronectin. Its tenth fibronectin type III repeat contains an RGD cell recognition sequence in a flexible loop between 2 strands. Approximately 2% of all animal proteins contain the FN3 repeat; including extracellular and intracellular proteins, membrane spanning cytokine receptors, growth hormone receptors, tyrosine phosphatase receptors, and adhesion molecules. FN3-like domains are also found in bacterial glycosyl hydrolases.


Pssm-ID: 238020 [Multi-domain]  Cd Length: 93  Bit Score: 88.32  E-value: 5.46e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 3296 PSKPEGpIEVSDIHKEGCKLKWRKPKDDGGiPITGYVIEKMDTATGKWVPAGSVDPEKYDIEIKGLDPNHRYQFRVKAVN 3375
Cdd:cd00063     1 PSPPTN-LRVTDVTSTSVTLSWTPPEDDGG-PITGYVVEYREKGSGDWKEVEVTPGSETSYTLTGLKPGTEYEFRVRAVN 78
                          90
                  ....*....|....*
gi 281359561 3376 EEGESEPLETESAIT 3390
Cdd:cd00063    79 GGGESPPSESVTVTT 93
STKc_TAO cd06607
Catalytic domain of the Serine/Threonine Kinases, Thousand-and-One Amino acids proteins; STKs ...
7988-8245 5.98e-20

Catalytic domain of the Serine/Threonine Kinases, Thousand-and-One Amino acids proteins; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. TAO proteins possess mitogen-activated protein kinase (MAPK) kinase kinase activity. They activate the MAPKs, p38 and c-Jun N-terminal kinase (JNK), by phosphorylating and activating the respective MAP/ERK kinases (MEKs, also known as MKKs or MAPKKs), MEK3/MEK6 and MKK4/MKK7. MAPK signaling cascades are important in mediating cellular responses to extracellular signals. Vertebrates contain three TAO subfamily members, named TAO1, TAO2, and TAO3. The TAO subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270784 [Multi-domain]  Cd Length: 258  Bit Score: 93.67  E-value: 5.98e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 7988 RYDILEEIGTGAFGVVHRCRERSTGNIFAAKFIPVS--HSVEK--DLIRrEIDIMNQLHHQKLINLHDAFEDDDEMILIL 8063
Cdd:cd06607     2 IFEDLREIGHGSFGAVYYARNKRTSEVVAIKKMSYSgkQSTEKwqDIIK-EVKFLRQLRHPNTIEYKGCYLREHTAWLVM 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 8064 EFL--SGGELFEritAEGYVMTEAEVINYMRQICEGIRHMHEQNIIHLDIKPENIMCqTRSSTnVKLIDFGLATRLDP-N 8140
Cdd:cd06607    81 EYClgSASDIVE---VHKKPLQEVEIAAICHGALQGLAYLHSHNRIHRDVKAGNILL-TEPGT-VKLADFGSASLVCPaN 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 8141 EVVkittGTAEFAAPEIVNREPVGFYT---DMWATGVLSYVL------------LSGLSPFAgDNDVQTLKNVkacDWdf 8205
Cdd:cd06607   156 SFV----GTPYWMAPEVILAMDEGQYDgkvDVWSLGITCIELaerkpplfnmnaMSALYHIA-QNDSPTLSSG---EW-- 225
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|
gi 281359561 8206 dvesfkyiSEEAKDFIRKLLVRNKEKRMTAHECLLHPWLT 8245
Cdd:cd06607   226 --------SDDFRNFVDSCLQKIPQDRPSAEDLLKHPFVT 257
STKc_p38beta cd07878
Catalytic domain of the Serine/Threonine Kinase, p38beta Mitogen-Activated Protein Kinase ...
7973-8248 5.99e-20

Catalytic domain of the Serine/Threonine Kinase, p38beta Mitogen-Activated Protein Kinase (also called MAPK11); STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. p38beta/MAPK11 is widely expressed in tissues and shows more similarity with p38alpha than with the other isoforms. Both are sensitive to pyridinylimidazoles and share some common substrates such as MAPK activated protein kinase 2 (MK2) and the transcription factors ATF2, c-Fos and, ELK-1. p38beta is involved in regulating the activation of the cyclooxygenase-2 promoter and the expression of TGFbeta-induced alpha-smooth muscle cell actin. p38 kinases are mitogen-activated protein kinases (MAPKs), serving as important mediators of cellular responses to extracellular signals. They are activated by the MAPK kinases MKK3 and MKK6, which in turn are activated by upstream MAPK kinase kinases including TAK1, ASK1, and MLK3, in response to cellular stresses or inflammatory cytokines. The p38beta subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 143383 [Multi-domain]  Cd Length: 343  Bit Score: 95.50  E-value: 5.99e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 7973 FVPQPVEISQQSVYDRYDILEEIGTGAFGVVHRCRERSTGNIFAAKFI--PVSHSVEKDLIRREIDIMNQLHHQKLINLH 8050
Cdd:cd07878     1 FYRQELNKTVWEVPERYQNLTPVGSGAYGSVCSAYDTRLRQKVAVKKLsrPFQSLIHARRTYRELRLLKHMKHENVIGLL 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 8051 DAF------EDDDEMILILEfLSGGELFERITAEGyvMTEAEVINYMRQICEGIRHMHEQNIIHLDIKPENImcQTRSST 8124
Cdd:cd07878    81 DVFtpatsiENFNEVYLVTN-LMGADLNNIVKCQK--LSDEHVQFLIYQLLRGLKYIHSAGIIHRDLKPSNV--AVNEDC 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 8125 NVKLIDFGLATRLDpnEVVKITTGTAEFAAPEI-VNREPVGFYTDMWATGVLSYVLLSGLSPFAGDNDVQTLKNVKACDW 8203
Cdd:cd07878   156 ELRILDFGLARQAD--DEMTGYVATRWYRAPEImLNWMHYNQTVDIWSVGCIMAELLKGKALFPGNDYIDQLKRIMEVVG 233
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 281359561 8204 DFDVESFKYISEE---------------------------AKDFIRKLLVRNKEKRMTAHECLLHPWLTGDH 8248
Cdd:cd07878   234 TPSPEVLKKISSEharkyiqslphmpqqdlkkifrganplAIDLLEKMLVLDSDKRISASEALAHPYFSQYH 305
STKc_beta_ARK cd05606
Catalytic domain of the Serine/Threonine Kinase, beta-adrenergic receptor kinase; STKs ...
7995-8246 6.02e-20

Catalytic domain of the Serine/Threonine Kinase, beta-adrenergic receptor kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The beta-ARK group is composed of GRK2, GRK3, and similar proteins. GRK2 and GRK3 are both widely expressed in many tissues, although GRK2 is present at higher levels. They contain an N-terminal RGS homology (RH) domain, a central catalytic domain, and C-terminal pleckstrin homology (PH) domain that mediates PIP2 and G protein betagamma-subunit translocation to the membrane. GRK2 (also called beta-ARK or beta-ARK1) is important in regulating several cardiac receptor responses. It plays a role in cardiac development and in hypertension. Deletion of GRK2 in mice results in embryonic lethality, caused by hypoplasia of the ventricular myocardium. GRK2 also plays important roles in the liver (as a regulator of portal blood pressure), in immune cells, and in the nervous system. Altered GRK2 expression has been reported in several disorders including major depression, schizophrenia, bipolar disorder, and Parkinsonism. GRKs phosphorylate and regulate G protein-coupled receptors (GPCRs), the largest superfamily of cell surface receptors which regulate some part of nearly all physiological functions. Phosphorylated GPCRs bind to arrestins, which prevents further G protein signaling despite the presence of activating ligand. The beta-ARK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270757 [Multi-domain]  Cd Length: 279  Bit Score: 94.04  E-value: 6.02e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 7995 IGTGAFGVVHRCRERSTGNIFAAKfipvshSVEKDLIRREID--------IMNQLHHQK-----LINLHDAFEDDDEMIL 8061
Cdd:cd05606     2 IGRGGFGEVYGCRKADTGKMYAMK------CLDKKRIKMKQGetlalnerIMLSLVSTGgdcpfIVCMTYAFQTPDKLCF 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 8062 ILEFLSGGELFERITAEGyVMTEAEVINYMRQICEGIRHMHEQNIIHLDIKPENIMCQtrSSTNVKLIDFGLA---TRLD 8138
Cdd:cd05606    76 ILDLMNGGDLHYHLSQHG-VFSEAEMRFYAAEVILGLEHMHNRFIVYRDLKPANILLD--EHGHVRISDLGLAcdfSKKK 152
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 8139 PNEVVkittGTAEFAAPEIVNR-EPVGFYTDMWATGVLSYVLLSGLSPFAGDN-------DVQTLKnvkacdwdFDVESF 8210
Cdd:cd05606   153 PHASV----GTHGYMAPEVLQKgVAYDSSADWFSLGCMLYKLLKGHSPFRQHKtkdkheiDRMTLT--------MNVELP 220
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|.
gi 281359561 8211 KYISEEAKDFIRKLLVRNKEKRM-----TAHECLLHPWLTG 8246
Cdd:cd05606   221 DSFSPELKSLLEGLLQRDVSKRLgclgrGATEVKEHPFFKG 261
K-ycf53 COG5752
Signaling protein combining a Ser/Thr protein kinase domain and the GUN4/Ycf53 ...
7987-8186 6.19e-20

Signaling protein combining a Ser/Thr protein kinase domain and the GUN4/Ycf53 porphyrin-binding domain [Signal transduction mechanisms];


Pssm-ID: 444462 [Multi-domain]  Cd Length: 466  Bit Score: 97.38  E-value: 6.19e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 7987 DRYDILEEIGTGAFGvvhrcreRStgniFAAK---------------FIPV--SHSVEK--DLIRREIDIMNQL-HHQKL 8046
Cdd:COG5752    32 ERYRAIKPLGQGGFG-------RT----FLAVdedipshphcvikqfYFPEqgPSSFQKavELFRQEAVRLDELgKHPQI 100
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 8047 INLHDAFEDDDEMILILEFLSGGELFERITAEGyVMTEAEVINYMRQICEGIRHMHEQNIIHLDIKPENIMcQTRSSTNV 8126
Cdd:COG5752   101 PELLAYFEQDQRLYLVQEFIEGQTLAQELEKKG-VFSESQIWQLLKDLLPVLQFIHSRNVIHRDIKPANII-RRRSDGKL 178
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 281359561 8127 KLIDFGLATRLDPNEVVKITT--GTAEFAAPEIVnREPVGFYTDMWATGVLSYVLLSGLSPF 8186
Cdd:COG5752   179 VLIDFGVAKLLTITALLQTGTiiGTPEYMAPEQL-RGKVFPASDLYSLGVTCIYLLTGVSPF 239
FN3 COG3401
Fibronectin type 3 domain [General function prediction only];
5021-5264 7.24e-20

Fibronectin type 3 domain [General function prediction only];


Pssm-ID: 442628 [Multi-domain]  Cd Length: 603  Bit Score: 98.54  E-value: 7.24e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 5021 YSKDNVKVTNVDYNTKLKVNSATRSDSGI---YTVFAENANGEDSADVKVTVIDKPAPPNGP--LKVDEINSESCTLHWN 5095
Cdd:COG3401   175 SATAAVATTSLTVTSTTLVDGGGDIEPGTtyyYRVAATDTGGESAPSNEVSVTTPTTPPSAPtgLTATADTPGSVTLSWD 254
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 5096 PPDDDGgqpIDNYVVEKLDETTGRWIPAGETDGpvTALKVGGLTPGHKYKFRVRAKNRQGT-SEPLTTAQAIIAKNPfdv 5174
Cdd:COG3401   255 PVTESD---ATGYRVYRSNSGDGPFTKVATVTT--TSYTDTGLTNGTTYYYRVTAVDAAGNeSAPSNVVSVTTDLTP--- 326
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 5175 PTKPGTPTIKDFDKEFVDLEWTrpeADGGSPITGYVVEKRDKFSPDWEKCAEISDDiTNAHVPDLIEGLKYEFRVRAVNK 5254
Cdd:COG3401   327 PAAPSGLTATAVGSSSITLSWT---ASSDADVTGYNVYRSTSGGGTYTKIAETVTT-TSYTDTGLTPGTTYYYKVTAVDA 402
                         250
                  ....*....|
gi 281359561 5255 AGPGSPSDAT 5264
Cdd:COG3401   403 AGNESAPSEE 412
STKc_TLK2 cd14041
Catalytic domain of the Serine/Threonine kinase, Tousled-Like Kinase 2; STKs catalyze the ...
7987-8244 7.34e-20

Catalytic domain of the Serine/Threonine kinase, Tousled-Like Kinase 2; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. TLKs play important functions during the cell cycle and are implicated in chromatin remodeling, DNA replication and repair, and mitosis. They phosphorylate and regulate Anti-silencing function 1 protein (Asf1), a histone H3/H4 chaperone that helps facilitate the assembly of chromatin following DNA replication during S phase. TLKs also phosphorylate the H3 histone tail and are essential in transcription. Vertebrates contain two subfamily members, TLK1 and TLK2. The TLK2 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase (PI3K).


Pssm-ID: 270943 [Multi-domain]  Cd Length: 309  Bit Score: 94.74  E-value: 7.34e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 7987 DRYDILEEIGTGAFGVVHRCRERSTGNIFAAKFipvsHSVEKDLIR-----------REIDIMNQLHHQKLINLHDAFE- 8054
Cdd:cd14041     6 DRYLLLHLLGRGGFSEVYKAFDLTEQRYVAVKI----HQLNKNWRDekkenyhkhacREYRIHKELDHPRIVKLYDYFSl 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 8055 DDDEMILILEFLSGGELfERITAEGYVMTEAEVINYMRQICEGIRHMHEQN--IIHLDIKPENIMCQTRSST-NVKLIDF 8131
Cdd:cd14041    82 DTDSFCTVLEYCEGNDL-DFYLKQHKLMSEKEARSIIMQIVNALKYLNEIKppIIHYDLKPGNILLVNGTACgEIKITDF 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 8132 GLATRLDPN--------EVVKITTGTAEFAAPE--IVNREP--VGFYTDMWATGVLSYVLLSGLSPFAGDNDVQTLKN-- 8197
Cdd:cd14041   161 GLSKIMDDDsynsvdgmELTSQGAGTYWYLPPEcfVVGKEPpkISNKVDVWSVGVIFYQCLYGRKPFGHNQSQQDILQen 240
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*....
gi 281359561 8198 --VKACDWDFDVESFkyISEEAKDFIRKLLVRNKEKRMTAHECLLHPWL 8244
Cdd:cd14041   241 tiLKATEVQFPPKPV--VTPEAKAFIRRCLAYRKEDRIDVQQLACDPYL 287
PLN00009 PLN00009
cyclin-dependent kinase A; Provisional
7987-8243 8.50e-20

cyclin-dependent kinase A; Provisional


Pssm-ID: 177649 [Multi-domain]  Cd Length: 294  Bit Score: 94.11  E-value: 8.50e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 7987 DRYDILEEIGTGAFGVVHRCRERSTGNIFAAKFIPVSHSVE--KDLIRREIDIMNQLHHQKLINLHDAFEDDDEMILILE 8064
Cdd:PLN00009    2 DQYEKVEKIGEGTYGVVYKARDRVTNETIALKKIRLEQEDEgvPSTAIREISLLKEMQHGNIVRLQDVVHSEKRLYLVFE 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 8065 FLSGGELFERITAEGYVMTEAEVINYMRQICEGIRHMHEQNIIHLDIKPENIMCQtRSSTNVKLIDFGLA------TRLD 8138
Cdd:PLN00009   82 YLDLDLKKHMDSSPDFAKNPRLIKTYLYQILRGIAYCHSHRVLHRDLKPQNLLID-RRTNALKLADFGLArafgipVRTF 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 8139 PNEVVkittgTAEFAAPEIV-----NREPVgfytDMWATGVLSYVLLSGLSPFAGDNDVQTLKNV-------KACDW--- 8203
Cdd:PLN00009  161 THEVV-----TLWYRAPEILlgsrhYSTPV----DIWSVGCIFAEMVNQKPLFPGDSEIDELFKIfrilgtpNEETWpgv 231
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 281359561 8204 ----DF----------DVESF-KYISEEAKDFIRKLLVRNKEKRMTAHECLLHPW 8243
Cdd:PLN00009  232 tslpDYksafpkwppkDLATVvPTLEPAGVDLLSKMLRLDPSKRITARAALEHEY 286
FN3 cd00063
Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein ...
5175-5265 1.12e-19

Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein fibronectin. Its tenth fibronectin type III repeat contains an RGD cell recognition sequence in a flexible loop between 2 strands. Approximately 2% of all animal proteins contain the FN3 repeat; including extracellular and intracellular proteins, membrane spanning cytokine receptors, growth hormone receptors, tyrosine phosphatase receptors, and adhesion molecules. FN3-like domains are also found in bacterial glycosyl hydrolases.


Pssm-ID: 238020 [Multi-domain]  Cd Length: 93  Bit Score: 87.55  E-value: 1.12e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 5175 PTKPGTPTIKDFDKEFVDLEWTRPEADGGsPITGYVVEKRDKFSPDWEKCAEISDDITNAHVPDLIEGLKYEFRVRAVNK 5254
Cdd:cd00063     1 PSPPTNLRVTDVTSTSVTLSWTPPEDDGG-PITGYVVEYREKGSGDWKEVEVTPGSETSYTLTGLKPGTEYEFRVRAVNG 79
                          90
                  ....*....|.
gi 281359561 5255 AGPGSPSDATE 5265
Cdd:cd00063    80 GGESPPSESVT 90
FN3 COG3401
Fibronectin type 3 domain [General function prediction only];
7421-7762 1.31e-19

Fibronectin type 3 domain [General function prediction only];


Pssm-ID: 442628 [Multi-domain]  Cd Length: 603  Bit Score: 97.77  E-value: 1.31e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 7421 YQIEFTNESGSATGEFYVHITGMPSAPTGPMGISYINK--NSCMLNWRPPSYDGglkVSHYVIERKDVSSPHWITVSSTc 7498
Cdd:COG3401   207 YRVAATDTGGESAPSNEVSVTTPTTPPSAPTGLTATADtpGSVTLSWDPVTESD---ATGYRVYRSNSGDGPFTKVATV- 282
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 7499 KDTAFNVQGLIENQEYIFRVMAVNENG-MGPPlegLNPIRAKDPIDPPSPPGSPQITEIGGDFVHLEWEKPESdggAHIQ 7577
Cdd:COG3401   283 TTTSYTDTGLTNGTTYYYRVTAVDAAGnESAP---SNVVSVTTDLTPPAAPSGLTATAVGSSSITLSWTASSD---ADVT 356
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 7578 GYWIDKREVGSNTWQRVNATICAANQINcINLIEGRQYEFRIFAQNVAGLstESSASQAVKIIDPQAASPPLIVKPLRDA 7657
Cdd:COG3401   357 GYNVYRSTSGGGTYTKIAETVTTTSYTD-TGLTPGTTYYYKVTAVDAAGN--ESAPSEEVSATTASAASGESLTASVDAV 433
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 7658 NCIQNHNAQFTCTINGVPKPTISWYKGAREISNGARYHMYSEGDNHFLNINDVFGEDADEYVcrAVNKAGAKSTRATLAI 7737
Cdd:COG3401   434 PLTDVAGATAAASAASNPGVSAAVLADGGDTGNAVPFTTTSSTVTATTTDTTTANLSVTTGS--LVGGSGASSVTNSVSV 511
                         330       340
                  ....*....|....*....|....*
gi 281359561 7738 MTAPKLNVPPRFRDTAYFDKGENVV 7762
Cdd:COG3401   512 IGASAAAAVGGAPDGTPNVTGASPV 536
STKc_p38gamma cd07880
Catalytic domain of the Serine/Threonine Kinase, p38gamma Mitogen-Activated Protein Kinase ...
7973-8248 1.71e-19

Catalytic domain of the Serine/Threonine Kinase, p38gamma Mitogen-Activated Protein Kinase (also called MAPK12); STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. p38gamma/MAPK12 is predominantly expressed in skeletal muscle. Unlike p38alpha and p38beta, p38gamma is insensitive to pyridinylimidazoles. It displays an antagonizing function compared to p38alpha. p38gamma inhibits, while p38alpha stimulates, c-Jun phosphorylation and AP-1 mediated transcription. p38gamma also plays a role in the signaling between Ras and the estrogen receptor and has been implicated to increase cell invasion and breast cancer progression. In Xenopus, p38gamma is critical in the meiotic maturation of oocytes. p38 kinases are MAPKs, serving as important mediators of cellular responses to extracellular signals. They are activated by the MAPK kinases MKK3 and MKK6, which in turn are activated by upstream MAPK kinase kinases including TAK1, ASK1, and MLK3, in response to cellular stresses or inflammatory cytokines. The p38gamma subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 143385 [Multi-domain]  Cd Length: 343  Bit Score: 94.25  E-value: 1.71e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 7973 FVPQPVEISQQSVYDRYDILEEIGTGAFGVVHRCRERSTGNIFAAK--FIPVSHSVEKDLIRREIDIMNQLHHQKLINLH 8050
Cdd:cd07880     1 YYRQEVNKTIWEVPDRYRDLKQVGSGAYGTVCSALDRRTGAKVAIKklYRPFQSELFAKRAYRELRLLKHMKHENVIGLL 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 8051 DAFEDD------DEMILILEFLsGGELFERITAEGyvMTEAEVINYMRQICEGIRHMHEQNIIHLDIKPENImcQTRSST 8124
Cdd:cd07880    81 DVFTPDlsldrfHDFYLVMPFM-GTDLGKLMKHEK--LSEDRIQFLVYQMLKGLKYIHAAGIIHRDLKPGNL--AVNEDC 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 8125 NVKLIDFGLATRLDPNEVVKITtgTAEFAAPE-IVNREPVGFYTDMWATGVLSYVLLSGLSPFAGDNDVQTLKNVKACDW 8203
Cdd:cd07880   156 ELKILDFGLARQTDSEMTGYVV--TRWYRAPEvILNWMHYTQTVDIWSVGCIMAEMLTGKPLFKGHDHLDQLMEIMKVTG 233
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 281359561 8204 DFDVE-SFKYISEEAKDFIRKL--------------------------LVRNKEKRMTAHECLLHPWLTGDH 8248
Cdd:cd07880   234 TPSKEfVQKLQSEDAKNYVKKLprfrkkdfrsllpnanplavnvlekmLVLDAESRITAAEALAHPYFEEFH 305
STKc_STK25 cd06642
Catalytic domain of Serine/Threonine Kinase 25 (also called Yeast Sps1/Ste20-related kinase 1); ...
7992-8245 1.75e-19

Catalytic domain of Serine/Threonine Kinase 25 (also called Yeast Sps1/Ste20-related kinase 1); STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. STK25 is also called Ste20/oxidant stress response kinase 1 (SOK1) or yeast Sps1/Ste20-related kinase 1 (YSK1). It is localized in the Golgi apparatus through its interaction with the Golgi matrix protein GM130. It may be involved in the regulation of cell migration and polarization. STK25 binds and phosphorylates CCM3 (cerebral cavernous malformation 3), also called PCD10 (programmed cell death 10), and may play a role in apoptosis. Human STK25 is a candidate gene responsible for pseudopseudohypoparathyroidism (PPHP), a disease that shares features with the Albright hereditary osteodystrophy (AHO) phenotype. The STK25 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270810 [Multi-domain]  Cd Length: 277  Bit Score: 92.81  E-value: 1.75e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 7992 LEEIGTGAFGVVHRCRERSTGNIFAAKFIPVSHSV-EKDLIRREIDIMNQLHHQKLINLHDAFEDDDEMILILEFLSGGE 8070
Cdd:cd06642     9 LERIGKGSFGEVYKGIDNRTKEVVAIKIIDLEEAEdEIEDIQQEITVLSQCDSPYITRYYGSYLKGTKLWIIMEYLGGGS 88
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 8071 LFERITAEGyvMTEAEVINYMRQICEGIRHMHEQNIIHLDIKPENIMCQTRSstNVKLIDFGLATRLDPNEVVKIT-TGT 8149
Cdd:cd06642    89 ALDLLKPGP--LEETYIATILREILKGLDYLHSERKIHRDIKAANVLLSEQG--DVKLADFGVAGQLTDTQIKRNTfVGT 164
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 8150 AEFAAPEIVNREPVGFYTDMWATGVLSYVLLSGLSPFAgdnDVQTLKNVKACDWDFDVESFKYISEEAKDFIRKLLVRNK 8229
Cdd:cd06642   165 PFWMAPEVIKQSAYDFKADIWSLGITAIELAKGEPPNS---DLHPMRVLFLIPKNSPPTLEGQHSKPFKEFVEACLNKDP 241
                         250
                  ....*....|....*.
gi 281359561 8230 EKRMTAHECLLHPWLT 8245
Cdd:cd06642   242 RFRPTAKELLKHKFIT 257
FN3 cd00063
Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein ...
2801-2893 2.03e-19

Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein fibronectin. Its tenth fibronectin type III repeat contains an RGD cell recognition sequence in a flexible loop between 2 strands. Approximately 2% of all animal proteins contain the FN3 repeat; including extracellular and intracellular proteins, membrane spanning cytokine receptors, growth hormone receptors, tyrosine phosphatase receptors, and adhesion molecules. FN3-like domains are also found in bacterial glycosyl hydrolases.


Pssm-ID: 238020 [Multi-domain]  Cd Length: 93  Bit Score: 86.78  E-value: 2.03e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 2801 PNKPGTPEVTDYDNQSISLKWAAPNNDGGaPIQKYIIEKKNKNKTEWEKALEIPGDQLEATVAGLQEYGEYQFRVIAVNK 2880
Cdd:cd00063     1 PSPPTNLRVTDVTSTSVTLSWTPPEDDGG-PITGYVVEYREKGSGDWKEVEVTPGSETSYTLTGLKPGTEYEFRVRAVNG 79
                          90
                  ....*....|...
gi 281359561 2881 AGLSPPSDASVPQ 2893
Cdd:cd00063    80 GGESPPSESVTVT 92
STKc_MAP4K5 cd06646
Catalytic domain of the Serine/Threonine Kinase, Mitogen-activated protein kinase kinase ...
7979-8241 2.09e-19

Catalytic domain of the Serine/Threonine Kinase, Mitogen-activated protein kinase kinase kinase kinase 5; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MAP4K5, also called germinal center kinase-related enzyme (GCKR), has been shown to activate the MAPK c-Jun N-terminal kinase (JNK). MAP4K5 also facilitates Wnt signaling in B cells, and may therefore be implicated in the control of cell fate, proliferation, and polarity. MAP4Ks are involved in some MAPK signaling pathways by activating a MAPK kinase kinase. Each MAPK cascade is activated either by a small GTP-binding protein or by an adaptor protein, which transmits the signal either directly to a MAP3K to start the triple kinase core cascade or indirectly through a mediator kinase, a MAP4K. Members of this subfamily contain an N-terminal catalytic domain and a C-terminal citron homology (CNH) regulatory domain. The MAP4K5 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270813 [Multi-domain]  Cd Length: 268  Bit Score: 92.40  E-value: 2.09e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 7979 EISQQSVYDRYDILEEIGTGAFGVVHRCRERSTGNIFAAKFIPVSHSVEKDLIRREIDIMNQLHHQKLINLHDAFEDDDE 8058
Cdd:cd06646     1 DILRRNPQHDYELIQRVGSGTYGDVYKARNLHTGELAAVKIIKLEPGDDFSLIQQEIFMVKECKHCNIVAYFGSYLSREK 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 8059 MILILEFLSGGELFERITAEGyVMTEAEVINYMRQICEGIRHMHEQNIIHLDIKPENIMCQtrSSTNVKLIDFGLATRLD 8138
Cdd:cd06646    81 LWICMEYCGGGSLQDIYHVTG-PLSELQIAYVCRETLQGLAYLHSKGKMHRDIKGANILLT--DNGDVKLADFGVAAKIT 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 8139 PNEVVKIT-TGTAEFAAPEIVNREPVGFYT---DMWATGVLSyVLLSGLSP------------FAGDNDVQTLKNVKACD 8202
Cdd:cd06646   158 ATIAKRKSfIGTPYWMAPEVAAVEKNGGYNqlcDIWAVGITA-IELAELQPpmfdlhpmralfLMSKSNFQPPKLKDKTK 236
                         250       260       270
                  ....*....|....*....|....*....|....*....
gi 281359561 8203 WdfdvesfkyiSEEAKDFIRKLLVRNKEKRMTAHECLLH 8241
Cdd:cd06646   237 W----------SSTFHNFVKISLTKNPKKRPTAERLLTH 265
FN3 cd00063
Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein ...
3990-4082 2.72e-19

Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein fibronectin. Its tenth fibronectin type III repeat contains an RGD cell recognition sequence in a flexible loop between 2 strands. Approximately 2% of all animal proteins contain the FN3 repeat; including extracellular and intracellular proteins, membrane spanning cytokine receptors, growth hormone receptors, tyrosine phosphatase receptors, and adhesion molecules. FN3-like domains are also found in bacterial glycosyl hydrolases.


Pssm-ID: 238020 [Multi-domain]  Cd Length: 93  Bit Score: 86.40  E-value: 2.72e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 3990 DTPGKPQIVDWSGNHCDLKWRAPEDDGGAsITGYIVERKDPNTGKWQKALETSTPDCKARVNDLIAGNKYQFRIMAVNKA 4069
Cdd:cd00063     2 SPPTNLRVTDVTSTSVTLSWTPPEDDGGP-ITGYVVEYREKGSGDWKEVEVTPGSETSYTLTGLKPGTEYEFRVRAVNGG 80
                          90
                  ....*....|...
gi 281359561 4070 GKSKPSEPSDQMT 4082
Cdd:cd00063    81 GESPPSESVTVTT 93
FN3 smart00060
Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, ...
6359-6441 3.06e-19

Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, fibronectin. The tenth fibronectin type III repeat contains a RGD cell recognition sequence in a flexible loop between 2 strands. Type III modules are present in both extracellular and intracellular proteins.


Pssm-ID: 214495 [Multi-domain]  Cd Length: 83  Bit Score: 85.74  E-value: 3.06e-19
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561   6359 PGAPSQPTISAYTPNSANLEWHPP-DDCGGKPITGYIVERRERGGEWIKCNNyPTPNTSYTVSNLRDGARYEFRVLAVNE 6437
Cdd:smart00060    1 PSPPSNLRVTDVTSTSVTLSWEPPpDDGITGYIVGYRVEYREEGSEWKEVNV-TPSSTSYTLTGLKPGTEYEFRVRAVNG 79

                    ....
gi 281359561   6438 AGPG 6441
Cdd:smart00060   80 AGEG 83
PknB_PASTA_kin NF033483
Stk1 family PASTA domain-containing Ser/Thr kinase;
7987-8193 3.71e-19

Stk1 family PASTA domain-containing Ser/Thr kinase;


Pssm-ID: 468045 [Multi-domain]  Cd Length: 563  Bit Score: 96.02  E-value: 3.71e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 7987 DRYDILEEIGTGAFGVVHRCR----ER-----------STGNIFAAKFipvshsvekdliRREIDIMNQLHHQKLINLHD 8051
Cdd:NF033483    7 GRYEIGERIGRGGMAEVYLAKdtrlDRdvavkvlrpdlARDPEFVARF------------RREAQSAASLSHPNIVSVYD 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 8052 AFEDDDEMILILEFLSGGELFERITAEGyVMTEAEVINYMRQICEGIRHMHEQNIIHLDIKPENIMCqTRSStNVKLIDF 8131
Cdd:NF033483   75 VGEDGGIPYIVMEYVDGRTLKDYIREHG-PLSPEEAVEIMIQILSALEHAHRNGIVHRDIKPQNILI-TKDG-RVKVTDF 151
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 281359561 8132 GLATRLDpneVVKITT-----GTAEFAAPEIVNREPVGFYTDMWATGVLSYVLLSGLSPFAGDNDVQ 8193
Cdd:NF033483  152 GIARALS---STTMTQtnsvlGTVHYLSPEQARGGTVDARSDIYSLGIVLYEMLTGRPPFDGDSPVS 215
FN3 cd00063
Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein ...
3400-3489 4.38e-19

Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein fibronectin. Its tenth fibronectin type III repeat contains an RGD cell recognition sequence in a flexible loop between 2 strands. Approximately 2% of all animal proteins contain the FN3 repeat; including extracellular and intracellular proteins, membrane spanning cytokine receptors, growth hormone receptors, tyrosine phosphatase receptors, and adhesion molecules. FN3-like domains are also found in bacterial glycosyl hydrolases.


Pssm-ID: 238020 [Multi-domain]  Cd Length: 93  Bit Score: 85.63  E-value: 4.38e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 3400 PPGLPELEDWDEHHVKLKWEPPiRDGGSPITNYIIEVMDKDSGEFVKAVETDSPVCKGVVKKLEEGQQYKFRVRAVNKAG 3479
Cdd:cd00063     3 PPTNLRVTDVTSTSVTLSWTPP-EDDGGPITGYVVEYREKGSGDWKEVEVTPGSETSYTLTGLKPGTEYEFRVRAVNGGG 81
                          90
                  ....*....|
gi 281359561 3480 PSDPSEQTNW 3489
Cdd:cd00063    82 ESPPSESVTV 91
PTKc_Srm_Brk cd05148
Catalytic domain of the Protein Tyrosine Kinases, Src-related kinase lacking C-terminal ...
7989-8200 5.22e-19

Catalytic domain of the Protein Tyrosine Kinases, Src-related kinase lacking C-terminal regulatory tyrosine and N-terminal myristylation sites (Srm) and Breast tumor kinase (Brk); PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Srm and Brk (also called protein tyrosine kinase 6) are members of the Src subfamily of proteins, which are cytoplasmic (or non-receptor) PTKs. Brk has been found to be overexpressed in a majority of breast tumors. Src kinases in general contain an N-terminal SH4 domain with a myristoylation site, followed by SH3 and SH2 domains, a tyr kinase domain, and a regulatory C-terminal region containing a conserved tyr; they are activated by autophosphorylation at the tyr kinase domain, but are negatively regulated by phosphorylation at the C-terminal tyr by Csk (C-terminal Src Kinase). Srm and Brk however, lack the N-terminal myristylation sites. Src proteins are involved in signaling pathways that regulate cytokine and growth factor responses, cytoskeleton dynamics, cell proliferation, survival, and differentiation. The Srm/Brk subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 133248 [Multi-domain]  Cd Length: 261  Bit Score: 90.96  E-value: 5.22e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 7989 YDILEEIGTGAFGVVHRCRERSTGNIfAAKFIPVSHSVEKDLIRREIDIMNQLHHQKLINLHDAFEDDDEMILILEFLSG 8068
Cdd:cd05148     8 FTLERKLGSGYFGEVWEGLWKNRVRV-AIKILKSDDLLKQQDFQKEVQALKRLRHKHLISLFAVCSVGEPVYIITELMEK 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 8069 GELFERI-TAEGYVMTEAEVINYMRQICEGIRHMHEQNIIHLDIKPENIMcqTRSSTNVKLIDFGLATRLdpNEVVKITT 8147
Cdd:cd05148    87 GSLLAFLrSPEGQVLPVASLIDMACQVAEGMAYLEEQNSIHRDLAARNIL--VGEDLVCKVADFGLARLI--KEDVYLSS 162
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 281359561 8148 GTA---EFAAPEIVNREPVGFYTDMWATGVLSYVLLS-GLSPFAGDNDVQTLKNVKA 8200
Cdd:cd05148   163 DKKipyKWTAPEAASHGTFSTKSDVWSFGILLYEMFTyGQVPYPGMNNHEVYDQITA 219
PTKc_Wee1a cd14138
Catalytic domain of the Protein Tyrosine Kinase, Wee1a; PTKs catalyze the transfer of the ...
7992-8242 5.28e-19

Catalytic domain of the Protein Tyrosine Kinase, Wee1a; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. This subfamily is composed of human Wee1a, Xenopus laevis Wee1b (XeWee1b) and similar vertebrate proteins. Members of this subfamily show a wide expression pattern. XeWee1b functions after the first zygotic cell divisions. It is expressed in all tissues and is also present after the gastrulation stage of embryos. Wee1 is a cell cycle checkpoint kinase that helps keep the cyclin-dependent kinase CDK1 in an inactive state through phosphorylation of an N-terminal tyr (Y15) residue. During the late G2 phase, CDK1 is activated and mitotic entry is promoted by the removal of this inhibitory phosphorylation by the phosphatase Cdc25. Although Wee1 is functionally a tyr kinase, it is more closely related to serine/threonine kinases (STKs). It contains a catalytic kinase domain sandwiched in between N- and C-terminal regulatory domains. It is regulated by phosphorylation and degradation, and its expression levels are also controlled by circadian clock proteins. The Wee1a subfamily is part of a larger superfamily that includes the catalytic domains of STKs, other PTKs, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271040 [Multi-domain]  Cd Length: 276  Bit Score: 91.24  E-value: 5.28e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 7992 LEEIGTGAFGVVHRCRERSTGNIFAAKFI--PVSHSVEKDLIRREI---DIMNQlhHQKLINLHDAFEDDDEMILILEFL 8066
Cdd:cd14138    10 LEKIGSGEFGSVFKCVKRLDGCIYAIKRSkkPLAGSVDEQNALREVyahAVLGQ--HSHVVRYYSAWAEDDHMLIQNEYC 87
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 8067 SGGELFERITAEGYVM---TEAEVINYMRQICEGIRHMHEQNIIHLDIKPENIMCQTRSSTNV----------------- 8126
Cdd:cd14138    88 NGGSLADAISENYRIMsyfTEPELKDLLLQVARGLKYIHSMSLVHMDIKPSNIFISRTSIPNAaseegdedewasnkvif 167
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 8127 KLIDFGLATRLDPNEVVKittGTAEFAAPEIVNREpvgfYT-----DMWATGvLSYVLLSGLSPFAGDNDvqtlknvkac 8201
Cdd:cd14138   168 KIGDLGHVTRVSSPQVEE---GDSRFLANEVLQEN----YThlpkaDIFALA-LTVVCAAGAEPLPTNGD---------- 229
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*..
gi 281359561 8202 DWDfDVESFKY------ISEEAKDFIRKLLVRNKEKRMTAHECLLHP 8242
Cdd:cd14138   230 QWH-EIRQGKLpripqvLSQEFLDLLKVMIHPDPERRPSAVALVKHS 275
STKc_A-Raf cd14150
Catalytic domain of the Serine/Threonine Kinase, A-Raf (Rapidly Accelerated Fibrosarcoma) ...
7991-8191 5.29e-19

Catalytic domain of the Serine/Threonine Kinase, A-Raf (Rapidly Accelerated Fibrosarcoma) kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. A-Raf cooperates with C-Raf in regulating ERK transient phosphorylation that is associated with cyclin D expression and cell cycle progression. Mice deficient in A-Raf are born alive but show neurological and intestinal defects. A-Raf demonstrates low kinase activity to MEK, compared with B- and C-Raf, and may also have alternative functions other than in the ERK signaling cascade. It regulates the M2 type pyruvate kinase, a key glycolytic enzyme. It also plays a role in endocytic membrane trafficking. A-Raf is a mitogen-activated protein kinase kinase kinase (MAP3K, MKKK, MAPKKK), which phosphorylates and activates MAPK kinases (MAPKKs or MKKs or MAP2Ks), which in turn phosphorylate and activate MAPKs during signaling cascades that are important in mediating cellular responses to extracellular signals. It functions in the linear Ras-Raf-MEK-ERK pathway that regulates many cellular processes including cycle regulation, proliferation, differentiation, survival, and apoptosis. The A-Raf subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271052 [Multi-domain]  Cd Length: 265  Bit Score: 91.23  E-value: 5.29e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 7991 ILEEIGTGAFGVVHRCRERstGNIfAAKFIPVSHSVEKDL--IRREIDIMNQLHHQKLInLHDAFEDDDEMILILEFLSG 8068
Cdd:cd14150     4 MLKRIGTGSFGTVFRGKWH--GDV-AVKILKVTEPTPEQLqaFKNEMQVLRKTRHVNIL-LFMGFMTRPNFAIITQWCEG 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 8069 GELFERITAEGYVMTEAEVINYMRQICEGIRHMHEQNIIHLDIKPENIMCQtrSSTNVKLIDFGLAT---RLDPNEVVKI 8145
Cdd:cd14150    80 SSLYRHLHVTETRFDTMQLIDVARQTAQGMDYLHAKNIIHRDLKSNNIFLH--EGLTVKIGDFGLATvktRWSGSQQVEQ 157
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*....
gi 281359561 8146 TTGTAEFAAPEIVNRE---PVGFYTDMWATGVLSYVLLSGLSPFAGDND 8191
Cdd:cd14150   158 PSGSILWMAPEVIRMQdtnPYSFQSDVYAYGVVLYELMSGTLPYSNINN 206
STKc_MAP3K8 cd13995
Catalytic domain of the Serine/Threonine kinase, Mitogen-Activated Protein Kinase (MAPK) ...
7995-8186 5.54e-19

Catalytic domain of the Serine/Threonine kinase, Mitogen-Activated Protein Kinase (MAPK) Kinase Kinase 8; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MAP3K8 is also called Tumor progression locus 2 (Tpl2) or Cancer Osaka thyroid (Cot), and was first identified as a proto-oncogene in T-cell lymphoma induced by MoMuL virus and in breast carcinoma induced by MMTV. Activated MAP3K8 induces various MAPK pathways including Extracellular Regulated Kinase (ERK) 1/2, c-Jun N-terminal kinase (JNK), and p38. It plays a pivotal role in innate immunity, linking Toll-like receptors to the production of TNF and the activation of ERK in macrophages. It is also required in interleukin-1beta production and is critical in host defense against Gram-positive bacteria. MAP3Ks (MKKKs or MAPKKKs) phosphorylate and activate MAPK kinases (MAPKKs or MKKs or MAP2Ks), which in turn phosphorylate and activate MAPKs during signaling cascades that are important in mediating cellular responses to extracellular signals. The MAP3K8 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270897 [Multi-domain]  Cd Length: 256  Bit Score: 90.84  E-value: 5.54e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 7995 IGTGAFGVVHRCRERSTGNIFAAKFIPVSHSVEKDlirreIDIMNQLHHQKLINLHDAFEDDDEMILILEFLSGGELFER 8074
Cdd:cd13995    12 IPRGAFGKVYLAQDTKTKKRMACKLIPVEQFKPSD-----VEIQACFRHENIAELYGALLWEETVHLFMEAGEGGSVLEK 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 8075 ITAEGyVMTEAEVINYMRQICEGIRHMHEQNIIHLDIKPENIMCQtrsSTNVKLIDFGLATRL-DPNEVVKITTGTAEFA 8153
Cdd:cd13995    87 LESCG-PMREFEIIWVTKHVLKGLDFLHSKNIIHHDIKPSNIVFM---STKAVLVDFGLSVQMtEDVYVPKDLRGTEIYM 162
                         170       180       190
                  ....*....|....*....|....*....|...
gi 281359561 8154 APEIVNREPVGFYTDMWATGVLSYVLLSGLSPF 8186
Cdd:cd13995   163 SPEVILCRGHNTKADIYSLGATIIHMQTGSPPW 195
FN3 COG3401
Fibronectin type 3 domain [General function prediction only];
2376-2753 6.78e-19

Fibronectin type 3 domain [General function prediction only];


Pssm-ID: 442628 [Multi-domain]  Cd Length: 603  Bit Score: 95.45  E-value: 6.78e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 2376 YKLVLSNSSGTIESEAQVVVLDRPLPPGgpfEPEEIRAS-----HIKMKWKRPDDDGgceISGYALERMDEETGRWIPAG 2450
Cdd:COG3401   207 YRVAATDTGGESAPSNEVSVTTPTTPPS---APTGLTATadtpgSVTLSWDPVTESD---ATGYRVYRSNSGDGPFTKVA 280
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 2451 EVgpNETSFDFKGLTPNKKYKFRVKAINKEG-ESEPLETFDAIVARNpydPPSPPSQPVIDDYDNKSVLLKWKrPPSDGG 2529
Cdd:COG3401   281 TV--TTTSYTDTGLTNGTTYYYRVTAVDAAGnESAPSNVVSVTTDLT---PPAAPSGLTATAVGSSSITLSWT-ASSDAD 354
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 2530 rpITHYIVEIKDKFAPSWSEVAKTDDpNPECNVEGLKEKMVYQFRVRAVNKAG----PSEPSQPTDNHLCKHKNLKPQID 2605
Cdd:COG3401   355 --VTGYNVYRSTSGGGTYTKIAETVT-TTSYTDTGLTPGTTYYYKVTAVDAAGnesaPSEEVSATTASAASGESLTASVD 431
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 2606 RSTFKRVTIKSGRTHKWSVDVLGEPI----PELHWSWRDDIPLTNGDRIKIENVDYHTDFSITNvlrKDSGFYTLKAENR 2681
Cdd:COG3401   432 AVPLTDVAGATAAASAASNPGVSAAVladgGDTGNAVPFTTTSSTVTATTTDTTTANLSVTTGS---LVGGSGASSVTNS 508
                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 281359561 2682 NGIDRETVELVVLGKPSSPKGPLAVSDVTASGCKLQWKKPEDDGGVPIKEYVVEkmDTATGKWVRVGRSPGE 2753
Cdd:COG3401   509 VSVIGASAAAAVGGAPDGTPNVTGASPVTVGASTGDVLITDLVSLTTSASSSVS--GAGLGSGNLYLITTLG 578
STKc_TSSK6-like cd14164
Catalytic domain of testis-specific serine/threonine kinase 6 and similar proteins; STKs ...
7989-8244 8.10e-19

Catalytic domain of testis-specific serine/threonine kinase 6 and similar proteins; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. TSSK proteins are almost exclusively expressed postmeiotically in the testis and play important roles in spermatogenesis and/or spermiogenesis. There are five mammalian TSSK proteins which show differences in their localization and timing of expression. TSSK6, also called SSTK, is expressed at the head of elongated sperm. It can phosphorylate histones and associate with heat shock protens HSP90 and HSC70. Male mice deficient in TSSK6 are infertile, showing spermatogenic impairment including reduced sperm counts, impaired DNA condensation, abnormal morphology and decreased motility rates. The TSSK6-like subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271066 [Multi-domain]  Cd Length: 256  Bit Score: 90.30  E-value: 8.10e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 7989 YDILEEIGTGAFGVV-------HRC--------RERSTGNiFAAKFIPvshsvekdlirREIDIMNQLHHQKLINLHDAF 8053
Cdd:cd14164     2 YTLGTTIGEGSFSKVklatsqkYCCkvaikivdRRRASPD-FVQKFLP-----------RELSILRRVNHPNIVQMFECI 69
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 8054 EDDDEMILILEFLSGGELFERITAEGYVmTEAEVINYMRQICEGIRHMHEQNIIHLDIKPENIMCqTRSSTNVKLIDFGL 8133
Cdd:cd14164    70 EVANGRLYIVMEAAATDLLQKIQEVHHI-PKDLARDMFAQMVGAVNYLHDMNIVHRDLKCENILL-SADDRKIKIADFGF 147
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 8134 ATRL-DPNEVVKITTGTAEFAAPEIVNREPvgfYT----DMWATGVLSYVLLSGLSPFAGDNDVQTLKNVKACDWDFDVE 8208
Cdd:cd14164   148 ARFVeDYPELSTTFCGSRAYTPPEVILGTP---YDpkkyDVWSLGVVLYVMVTGTMPFDETNVRRLRLQQRGVLYPSGVA 224
                         250       260       270
                  ....*....|....*....|....*....|....*.
gi 281359561 8209 sfkyISEEAKDFIRKLLVRNKEKRMTAHECLLHPWL 8244
Cdd:cd14164   225 ----LEEPCRALIRTLLQFNPSTRPSIQQVAGNSWL 256
FN3 cd00063
Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein ...
3694-3781 9.35e-19

Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein fibronectin. Its tenth fibronectin type III repeat contains an RGD cell recognition sequence in a flexible loop between 2 strands. Approximately 2% of all animal proteins contain the FN3 repeat; including extracellular and intracellular proteins, membrane spanning cytokine receptors, growth hormone receptors, tyrosine phosphatase receptors, and adhesion molecules. FN3-like domains are also found in bacterial glycosyl hydrolases.


Pssm-ID: 238020 [Multi-domain]  Cd Length: 93  Bit Score: 84.86  E-value: 9.35e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 3694 PDRPGKPEPTNWDKDFVDLAWDPPKNDGGaPIQKYVIQMRDKSGRAWVDSATVPGDKCNGTVTGVEEGHEYEFRIVAVNK 3773
Cdd:cd00063     1 PSPPTNLRVTDVTSTSVTLSWTPPEDDGG-PITGYVVEYREKGSGDWKEVEVTPGSETSYTLTGLKPGTEYEFRVRAVNG 79

                  ....*...
gi 281359561 3774 AGPSDPSD 3781
Cdd:cd00063    80 GGESPPSE 87
FN3 cd00063
Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein ...
3102-3191 9.91e-19

Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein fibronectin. Its tenth fibronectin type III repeat contains an RGD cell recognition sequence in a flexible loop between 2 strands. Approximately 2% of all animal proteins contain the FN3 repeat; including extracellular and intracellular proteins, membrane spanning cytokine receptors, growth hormone receptors, tyrosine phosphatase receptors, and adhesion molecules. FN3-like domains are also found in bacterial glycosyl hydrolases.


Pssm-ID: 238020 [Multi-domain]  Cd Length: 93  Bit Score: 84.86  E-value: 9.91e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 3102 SKPGTPNIVDYNEHMVKLKWEAPRSDGGaPISGYIIEKKDKFSPIWDEILSTNTSVPEATVEGLVEGNIYQFRVRAVNKA 3181
Cdd:cd00063     2 SPPTNLRVTDVTSTSVTLSWTPPEDDGG-PITGYVVEYREKGSGDWKEVEVTPGSETSYTLTGLKPGTEYEFRVRAVNGG 80
                          90
                  ....*....|
gi 281359561 3182 GFSDPSDATE 3191
Cdd:cd00063    81 GESPPSESVT 90
STKc_PCTAIRE1 cd07873
Catalytic domain of the Serine/Threonine Kinase, PCTAIRE-1 kinase; STKs catalyze the transfer ...
7987-8244 1.41e-18

Catalytic domain of the Serine/Threonine Kinase, PCTAIRE-1 kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PCTAIRE-1 is expressed ubiquitously and is localized in the cytoplasm. Its kinase activity is cell cycle dependent and peaks at the S and G2 phases. PCTAIRE-1 is highly expressed in the brain and may play a role in regulating neurite outgrowth. It can also associate with Trap (Tudor repeat associator with PCTAIRE-2), a physiological partner of PCTAIRE-2; with p11, a small dimeric protein with similarity to S100; and with 14-3-3 proteins, mediators of phosphorylation-dependent interactions in many different proteins. PCTAIRE-1 shares sequence similarity with Cyclin-Dependent Kinases (CDKs), which belong to a large family of STKs that are regulated by their cognate cyclins. Together, CDKs and cyclins are involved in the control of cell-cycle progression, transcription, and neuronal function. The PCTAIRE-1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270854 [Multi-domain]  Cd Length: 297  Bit Score: 90.45  E-value: 1.41e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 7987 DRYDILEEIGTGAFGVVHRCRERSTGNIFAAKFIPVSHSVEKDLIR-REIDIMNQLHHQKLINLHDAFEDDDEMILILEF 8065
Cdd:cd07873     2 ETYIKLDKLGEGTYATVYKGRSKLTDNLVALKEIRLEHEEGAPCTAiREVSLLKDLKHANIVTLHDIIHTEKSLTLVFEY 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 8066 LSgGELFERITAEGYVMTEAEVINYMRQICEGIRHMHEQNIIHLDIKPENIMCQTRSStnVKLIDFGLA------TRLDP 8139
Cdd:cd07873    82 LD-KDLKQYLDDCGNSINMHNVKLFLFQLLRGLAYCHRRKVLHRDLKPQNLLINERGE--LKLADFGLAraksipTKTYS 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 8140 NEVVkittgTAEFAAPEI-VNREPVGFYTDMWATGVLSYVLLSGLSPFAGDNDVQTLKNV-------KACDW-----DFD 8206
Cdd:cd07873   159 NEVV-----TLWYRPPDIlLGSTDYSTQIDMWGVGCIFYEMSTGRPLFPGSTVEEQLHFIfrilgtpTEETWpgilsNEE 233
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|..
gi 281359561 8207 VESFKY--------------ISEEAKDFIRKLLVRNKEKRMTAHECLLHPWL 8244
Cdd:cd07873   234 FKSYNYpkyradalhnhaprLDSDGADLLSKLLQFEGRKRISAEEAMKHPYF 285
STKc_MASTL cd05610
Catalytic domain of the Serine/Threonine Kinase, Microtubule-associated serine/threonine-like ...
7989-8246 1.71e-18

Catalytic domain of the Serine/Threonine Kinase, Microtubule-associated serine/threonine-like kinase (also called greatwall kinase); STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The MASTL kinases in this group carry only a catalytic domain, which contains a long insertion relative to MAST kinases. MASTL, also called greatwall kinase (Gwl), is involved in the regulation of mitotic entry, which is controlled by the coordinated activities of protein kinases and opposing protein phosphatases (PPs). The cyclin B/CDK1 complex induces entry into M-phase while PP2A-B55 shows anti-mitotic activity. MASTL/Gwl is activated downstream of cyclin B/CDK1 and indirectly inhibits PP2A-B55 by phosphorylating the small protein alpha-endosulfine (Ensa) or the cAMP-regulated phosphoprotein 19 (Arpp19), resulting in M-phase progression. Gwl kinase may also play roles in mRNA stabilization and DNA checkpoint recovery. The human MASTL gene has also been named FLJ14813; a missense mutation in FLJ14813 is associated with autosomal dominant thrombocytopenia. The MASTL kinase subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270761 [Multi-domain]  Cd Length: 349  Bit Score: 91.48  E-value: 1.71e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 7989 YDILEEIGTGAFGVVHRCRERSTGNIFAAKFIPVSHSVEKDL---IRREIDIMNQLHHQKLINLHDAFEDDDEMILILEF 8065
Cdd:cd05610     6 FVIVKPISRGAFGKVYLGRKKNNSKLYAVKVVKKADMINKNMvhqVQAERDALALSKSPFIVHLYYSLQSANNVYLVMEY 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 8066 LSGGELFERITAEGYvMTEAEVINYMRQICEGIRHMHEQNIIHLDIKPENIMCQtrSSTNVKLIDFGLA-TRLD------ 8138
Cdd:cd05610    86 LIGGDVKSLLHIYGY-FDEEMAVKYISEVALALDYLHRHGIIHRDLKPDNMLIS--NEGHIKLTDFGLSkVTLNrelnmm 162
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 8139 ------------------PNEVVKITT-----------------------------GTAEFAAPEIVNREPVGFYTDMWA 8171
Cdd:cd05610   163 dilttpsmakpkndysrtPGQVLSLISslgfntptpyrtpksvrrgaarvegerilGTPDYLAPELLLGKPHGPAVDWWA 242
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 281359561 8172 TGVLSYVLLSGLSPFAGDNDVQTLKNV--KACDWDfdvESFKYISEEAKDFIRKLLVRNKEKRMTAHECLLHPWLTG 8246
Cdd:cd05610   243 LGVCLFEFLTGIPPFNDETPQQVFQNIlnRDIPWP---EGEEELSVNAQNAIEILLTMDPTKRAGLKELKQHPLFHG 316
FN3 cd00063
Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein ...
5470-5561 1.81e-18

Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein fibronectin. Its tenth fibronectin type III repeat contains an RGD cell recognition sequence in a flexible loop between 2 strands. Approximately 2% of all animal proteins contain the FN3 repeat; including extracellular and intracellular proteins, membrane spanning cytokine receptors, growth hormone receptors, tyrosine phosphatase receptors, and adhesion molecules. FN3-like domains are also found in bacterial glycosyl hydrolases.


Pssm-ID: 238020 [Multi-domain]  Cd Length: 93  Bit Score: 84.09  E-value: 1.81e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 5470 PDKPGQPQATDWGKHFVDLEWSTPKRDGGaPISSYIIEKRPKF-GQWERAAVVLGDNCKAHVPELTNGGEYEFRVIAVNR 5548
Cdd:cd00063     1 PSPPTNLRVTDVTSTSVTLSWTPPEDDGG-PITGYVVEYREKGsGDWKEVEVTPGSETSYTLTGLKPGTEYEFRVRAVNG 79
                          90
                  ....*....|...
gi 281359561 5549 GGPSDPSDPSSTI 5561
Cdd:cd00063    80 GGESPPSESVTVT 92
PKc_MKK5 cd06619
Catalytic domain of the dual-specificity Protein Kinase, Mitogen-activated protein Kinase ...
7992-8244 1.91e-18

Catalytic domain of the dual-specificity Protein Kinase, Mitogen-activated protein Kinase Kinase 5; PKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine (ST) or tyrosine residues on protein substrates. MKK5 (also called MEK5) is a dual-specificity PK that phosphorylates its downstream target, extracellular signal-regulated kinase 5 (ERK5), on specific threonine and tyrosine residues. MKK5 is activated by MEKK2 and MEKK3 in response to mitogenic and stress stimuli. The ERK5 cascade promotes cell proliferation, differentiation, neuronal survival, and neuroprotection. This cascade plays an essential role in heart development. Mice deficient in either ERK5 or MKK5 die around embryonic day 10 due to cardiovascular defects including underdevelopment of the myocardium. In addition, MKK5 is associated with metastasis and unfavorable prognosis in prostate cancer. The MKK5 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 132950 [Multi-domain]  Cd Length: 279  Bit Score: 89.94  E-value: 1.91e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 7992 LEEIGTGAFGVVHRCRERSTGNIFAAKFIPVSHSVE-KDLIRREIDIMNQLHHQKLINLHDAFEDDDEMILILEFLSGGE 8070
Cdd:cd06619     6 QEILGHGNGGTVYKAYHLLTRRILAVKVIPLDITVElQKQIMSELEILYKCDSPYIIGFYGAFFVENRISICTEFMDGGS 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 8071 LFERITAEGYVMTEAEVinymrQICEGIRHMHEQNIIHLDIKPENIMCQTRSstNVKLIDFGLATRLdPNEVVKITTGTA 8150
Cdd:cd06619    86 LDVYRKIPEHVLGRIAV-----AVVKGLTYLWSLKILHRDVKPSNMLVNTRG--QVKLCDFGVSTQL-VNSIAKTYVGTN 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 8151 EFAAPEIVNREPVGFYTDMWATGVLSYVLLSGLSPFAgdndvQTLKN--------VKAC--DWDFDVESFKYISEEAKDF 8220
Cdd:cd06619   158 AYMAPERISGEQYGIHSDVWSLGISFMELALGRFPYP-----QIQKNqgslmplqLLQCivDEDPPVLPVGQFSEKFVHF 232
                         250       260
                  ....*....|....*....|....
gi 281359561 8221 IRKLLVRNKEKRMTAHECLLHPWL 8244
Cdd:cd06619   233 ITQCMRKQPKERPAPENLMDHPFI 256
PKc_MKK7 cd06618
Catalytic domain of the dual-specificity Protein Kinase, Mitogen-activated protein Kinase ...
7991-8245 1.91e-18

Catalytic domain of the dual-specificity Protein Kinase, Mitogen-activated protein Kinase Kinase 7; PKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine (ST) or tyrosine residues on protein substrates. MKK7 is a dual-specificity PK that phosphorylates and activates its downstream target, c-Jun N-terminal kinase (JNK), on specific threonine and tyrosine residues. Although MKK7 is capable of dual phosphorylation, it prefers to phosphorylate the threonine residue of JNK. Thus, optimal activation of JNK requires both MKK4 and MKK7. MKK7 is primarily activated by cytokines. MKK7 is essential for liver formation during embryogenesis. It plays roles in G2/M cell cycle arrest and cell growth. In addition, it is involved in the control of programmed cell death, which is crucial in oncogenesis, cancer chemoresistance, and antagonism to TNFalpha-induced killing, through its inhibition by Gadd45beta and the subsequent suppression of the JNK cascade. The MKK7 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270791 [Multi-domain]  Cd Length: 295  Bit Score: 90.13  E-value: 1.91e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 7991 ILEEIGTGAFGVVHRCRERSTGNIFAAKFIPVSH-SVEKDLIRREIDIMNQLHHQKLI-NLHDAFEDDDEMILILEFLS- 8067
Cdd:cd06618    19 NLGEIGSGTCGQVYKMRHKKTGHVMAVKQMRRSGnKEENKRILMDLDVVLKSHDCPYIvKCYGYFITDSDVFICMELMSt 98
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 8068 ---------GGELFERITAEgyvMTEAEV--INYMRQicegirhmhEQNIIHLDIKPENIMCQtrSSTNVKLIDFGLATR 8136
Cdd:cd06618    99 cldkllkriQGPIPEDILGK---MTVSIVkaLHYLKE---------KHGVIHRDVKPSNILLD--ESGNVKLCDFGISGR 164
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 8137 LDPNEVVKITTGTAEFAAPEIVNREPVGFY---TDMWATGVLSYVLLSGLSPFAGdndvqtlknvkaCDWDFDV------ 8207
Cdd:cd06618   165 LVDSKAKTRSAGCAAYMAPERIDPPDNPKYdirADVWSLGISLVELATGQFPYRN------------CKTEFEVltkiln 232
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*..
gi 281359561 8208 ---------ESFkyiSEEAKDFIRKLLVRNKEKRMTAHECLLHPWLT 8245
Cdd:cd06618   233 eeppslppnEGF---SPDFCSFVDLCLTKDHRYRPKYRELLQHPFIR 276
STKc_JNK2 cd07876
Catalytic domain of the Serine/Threonine Kinase, c-Jun N-terminal Kinase 2; STKs catalyze the ...
7971-8245 1.96e-18

Catalytic domain of the Serine/Threonine Kinase, c-Jun N-terminal Kinase 2; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. JNK2 is expressed in every cell and tissue type. It is specifically translocated to the mitochondria during dopaminergic cell death. Specific substrates include the microtubule-associated proteins DCX and Tau, as well as TIF-IA which is involved in ribosomal RNA synthesis regulation. Mice deficient in Jnk2 show protection against arthritis, type 1 diabetes, atherosclerosis, abdominal aortic aneurysm, cardiac cell death, TNF-induced liver damage, and tumor growth, indicating that JNK2 may play roles in the pathogenesis of these diseases. Initially it was thought that JNK1 and JNK2 were functionally redundant as mice deficient in either genes could survive but disruption of both genes resulted in lethality. However, recent studies have shown that JNK1 and JNK2 perform distinct functions through specific binding partners and substrates. JNKs are mitogen-activated protein kinases (MAPKs) that are involved in many stress-activated responses including those during inflammation, neurodegeneration, apoptosis, and persistent pain sensitization, among others. The JNK2 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 143381 [Multi-domain]  Cd Length: 359  Bit Score: 91.24  E-value: 1.96e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 7971 SKFVPQPVEISQQSVYDRYDILEEIGTGAFGVVHRCRERSTGNIFAAKFI--PVSHSVEKDLIRREIDIMNQLHHQKLIN 8048
Cdd:cd07876     5 SQFYSVQVADSTFTVLKRYQQLKPIGSGAQGIVCAAFDTVLGINVAVKKLsrPFQNQTHAKRAYRELVLLKCVNHKNIIS 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 8049 LHDAF------EDDDEMILILEFLSGgELFERITAEgyvmTEAEVINYM-RQICEGIRHMHEQNIIHLDIKPENIMcqTR 8121
Cdd:cd07876    85 LLNVFtpqkslEEFQDVYLVMELMDA-NLCQVIHME----LDHERMSYLlYQMLCGIKHLHSAGIIHRDLKPSNIV--VK 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 8122 SSTNVKLIDFGLATRLDPNEVVKITTGTAEFAAPEIVNREPVGFYTDMWATGVLSYVLLSGLSPFAGDNDV--------- 8192
Cdd:cd07876   158 SDCTLKILDFGLARTACTNFMMTPYVVTRYYRAPEVILGMGYKENVDIWSVGCIMGELVKGSVIFQGTDHIdqwnkvieq 237
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 8193 -------------QTLKNVKAC--------------DWDF--DVESFKYISEEAKDFIRKLLVRNKEKRMTAHECLLHPW 8243
Cdd:cd07876   238 lgtpsaefmnrlqPTVRNYVENrpqypgisfeelfpDWIFpsESERDKLKTSQARDLLSKMLVIDPDKRISVDEALRHPY 317

                  ..
gi 281359561 8244 LT 8245
Cdd:cd07876   318 IT 319
Ig_Titin_like cd05748
Immunoglobulin (Ig)-like domain of titin and similar proteins; The members here are composed ...
3509-3590 2.06e-18

Immunoglobulin (Ig)-like domain of titin and similar proteins; The members here are composed of the immunoglobulin (Ig)-like domain found in titin-like proteins and similar proteins. Titin (also called connectin) is a fibrous sarcomeric protein specifically found in vertebrate striated muscle. Titin is a giant protein; depending on isoform composition, it ranges from 2970 to 3700 kDa, and is of a length that spans half a sarcomere. Titin largely consists of multiple repeats of Ig-like and fibronectin type 3 (FN-III)-like domains. Titin connects the ends of myosin thick filaments to Z disks and extends along the thick filament to the H zone. It appears to function similarly to an elastic band, keeping the myosin filaments centered in the sarcomere during muscle contraction or stretching. Within the sarcomere, titin is also attached to or is associated with myosin binding protein C (MyBP-C). MyBP-C appears to contribute to the generation of passive tension by titin and like titin has repeated Ig-like and FN-III domains. Also included in this group are worm twitchin and insect projectin, thick filament proteins of invertebrate muscle which also have repeated Ig-like and FN-III domains.


Pssm-ID: 409406 [Multi-domain]  Cd Length: 82  Bit Score: 83.41  E-value: 2.06e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 3509 VIVKTGLSISLDINIRGEPAPKVEWFFNNSSVTSDEHsVKIDNVDYNTKFFVMRAQRSQSGKYIIKATNEVGEDEAELEV 3588
Cdd:cd05748     2 IVVRAGESLRLDIPIKGRPTPTVTWSKDGQPLKETGR-VQIETTASSTSLVIKNAKRSDSGKYTLTLKNSAGEKSATINV 80

                  ..
gi 281359561 3589 TV 3590
Cdd:cd05748    81 KV 82
FN3 COG3401
Fibronectin type 3 domain [General function prediction only];
2463-2845 2.30e-18

Fibronectin type 3 domain [General function prediction only];


Pssm-ID: 442628 [Multi-domain]  Cd Length: 603  Bit Score: 93.91  E-value: 2.30e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 2463 GLTPNKKYKFRVKAINKEGESEPLETFDAIVarnPYDPPSPPSQPVIDDYDNKSVLLKWkRPPSDGGrpITHYIVEIKDK 2542
Cdd:COG3401   198 DIEPGTTYYYRVAATDTGGESAPSNEVSVTT---PTTPPSAPTGLTATADTPGSVTLSW-DPVTESD--ATGYRVYRSNS 271
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 2543 FAPSWSEVAKTDdpNPECNVEGLKEKMVYQFRVRAVNKAG-PSEPSQPtdnhlckhknlkpqidrstfkrvtiksgrthk 2621
Cdd:COG3401   272 GDGPFTKVATVT--TTSYTDTGLTNGTTYYYRVTAVDAAGnESAPSNV-------------------------------- 317
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 2622 wsVDVLGEPIPelhwswrddipltngdrikienvdyhtdfsitnvlrkdsgfytlkaenrngidretvelvvlgkPSSPK 2701
Cdd:COG3401   318 --VSVTTDLTP----------------------------------------------------------------PAAPS 331
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 2702 GpLAVSDVTASGCKLQWKKPEDdggVPIKEYVVEKMDTATGKWVRVGRSPGEkepPSFDVTGLSLGSEYMFRVSAVNEEG 2781
Cdd:COG3401   332 G-LTATAVGSSSITLSWTASSD---ADVTGYNVYRSTSGGGTYTKIAETVTT---TSYTDTGLTPGTTYYYKVTAVDAAG 404
                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 281359561 2782 -ESEPLTTLVGVVAKDPFDEPNKPGTPEVT--DYDNQSISLKWAAPNNDGGAPIQKYIIEKKNKNKT 2845
Cdd:COG3401   405 nESAPSEEVSATTASAASGESLTASVDAVPltDVAGATAAASAASNPGVSAAVLADGGDTGNAVPFT 471
PKc_like cd13968
Catalytic domain of the Protein Kinase superfamily; The PK superfamily contains the large ...
7995-8132 2.60e-18

Catalytic domain of the Protein Kinase superfamily; The PK superfamily contains the large family of typical PKs that includes serine/threonine kinases (STKs), protein tyrosine kinases (PTKs), and dual-specificity PKs that phosphorylate both serine/threonine and tyrosine residues of target proteins, as well as pseudokinases that lack crucial residues for catalytic activity and/or ATP binding. It also includes phosphoinositide 3-kinases (PI3Ks), aminoglycoside 3'-phosphotransferases (APHs), choline kinase (ChoK), Actin-Fragmin Kinase (AFK), and the atypical RIO and Abc1p-like protein kinases. These proteins catalyze the transfer of the gamma-phosphoryl group from ATP to their target substrates; these include serine/threonine/tyrosine residues in proteins for typical or atypical PKs, the 3-hydroxyl of the inositol ring of D-myo-phosphatidylinositol (PtdIns) or its derivatives for PI3Ks, the 4-hydroxyl of PtdIns for PI4Ks, and other small molecule substrates for APH/ChoK and similar proteins such as aminoglycosides, macrolides, choline, ethanolamine, and homoserine.


Pssm-ID: 270870 [Multi-domain]  Cd Length: 136  Bit Score: 85.19  E-value: 2.60e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 7995 IGTGAFGVVHRCRERSTGNIFAAKFIPVSHSVEKDLIRREIDIMNQL--HHQKLINLHDAFEDDDEMILILEFLSGGELF 8072
Cdd:cd13968     1 MGEGASAKVFWAEGECTTIGVAVKIGDDVNNEEGEDLESEMDILRRLkgLELNIPKVLVTEDVDGPNILLMELVKGGTLI 80
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 8073 ERITAEgyVMTEAEVINYMRQICEGIRHMHEQNIIHLDIKPENIMCQTRSstNVKLIDFG 8132
Cdd:cd13968    81 AYTQEE--ELDEKDVESIMYQLAECMRLLHSFHLIHRDLNNDNILLSEDG--NVKLIDFG 136
PTKc_Lyn cd05072
Catalytic domain of the Protein Tyrosine Kinase, Lyn; PTKs catalyze the transfer of the ...
7979-8194 3.09e-18

Catalytic domain of the Protein Tyrosine Kinase, Lyn; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Lyn is a member of the Src subfamily of proteins, which are cytoplasmic (or non-receptor) PTKs. Lyn is expressed in B lymphocytes and myeloid cells. It exhibits both positive and negative regulatory roles in B cell receptor (BCR) signaling. Lyn, as well as Fyn and Blk, promotes B cell activation by phosphorylating ITAMs (immunoreceptor tyr activation motifs) in CD19 and in Ig components of BCR. It negatively regulates signaling by its unique ability to phosphorylate ITIMs (immunoreceptor tyr inhibition motifs) in cell surface receptors like CD22 and CD5. Lyn also plays an important role in G-CSF receptor signaling by phosphorylating a variety of adaptor molecules. Src kinases contain an N-terminal SH4 domain with a myristoylation site, followed by SH3 and SH2 domains, a tyr kinase domain, and a regulatory C-terminal region containing a conserved tyr. They are activated by autophosphorylation at the tyr kinase domain, but are negatively regulated by phosphorylation at the C-terminal tyr by Csk (C-terminal Src Kinase). The Lyn subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270657 [Multi-domain]  Cd Length: 272  Bit Score: 88.94  E-value: 3.09e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 7979 EISQQSVydryDILEEIGTGAFGVVHRCRERSTGNIFAAKFIPVSHSVEKDLirREIDIMNQLHHQKLINLHDAFEDDDE 8058
Cdd:cd05072     3 EIPRESI----KLVKKLGAGQFGEVWMGYYNNSTKVAVKTLKPGTMSVQAFL--EEANLMKTLQHDKLVRLYAVVTKEEP 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 8059 MILILEFLSGGELFERITA-EGYVMTEAEVINYMRQICEGIRHMHEQNIIHLDIKPENIMcqTRSSTNVKLIDFGLATRL 8137
Cdd:cd05072    77 IYIITEYMAKGSLLDFLKSdEGGKVLLPKLIDFSAQIAEGMAYIERKNYIHRDLRAANVL--VSESLMCKIADFGLARVI 154
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 281359561 8138 DPNEVVkiTTGTAEF----AAPEIVNREPVGFYTDMWATGVLSYVLLS-GLSPFAG--DNDVQT 8194
Cdd:cd05072   155 EDNEYT--AREGAKFpikwTAPEAINFGSFTIKSDVWSFGILLYEIVTyGKIPYPGmsNSDVMS 216
STKc_nPKC_epsilon cd05591
Catalytic domain of the Serine/Threonine Kinase, Novel Protein Kinase C epsilon; STKs catalyze ...
7995-8233 3.18e-18

Catalytic domain of the Serine/Threonine Kinase, Novel Protein Kinase C epsilon; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PKC-epsilon has been shown to behave as an oncoprotein. Its overexpression contributes to neoplastic transformation depending on the cell type. It contributes to oncogenesis by inducing disordered cell growth and inhibiting cell death. It also plays a role in tumor invasion and metastasis. PKC-epsilon has also been found to confer cardioprotection against ischemia and reperfusion-mediated damage. Other cellular functions include the regulation of gene expression, cell adhesion, and cell motility. PKCs are classified into three groups (classical, atypical, and novel) depending on their mode of activation and the structural characteristics of their regulatory domain. nPKCs are calcium-independent, but require DAG (1,2-diacylglycerol) and phosphatidylserine (PS) for activity. The nPKC-epsilon subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270743 [Multi-domain]  Cd Length: 321  Bit Score: 89.86  E-value: 3.18e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 7995 IGTGAFGVVHRCRERSTGNIFAAKFIpvshsvEKDLIRREIDI---MNQ-------LHHQKLINLHDAFEDDDEMILILE 8064
Cdd:cd05591     3 LGKGSFGKVMLAERKGTDEVYAIKVL------KKDVILQDDDVdctMTEkrilalaAKHPFLTALHSCFQTKDRLFFVME 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 8065 FLSGGELFERITaEGYVMTEAEVINYMRQICEGIRHMHEQNIIHLDIKPENIMCQtrSSTNVKLIDFGLATR-LDPNEVV 8143
Cdd:cd05591    77 YVNGGDLMFQIQ-RARKFDEPRARFYAAEVTLALMFLHRHGVIYRDLKLDNILLD--AEGHCKLADFGMCKEgILNGKTT 153
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 8144 KITTGTAEFAAPEIVNREPVGFYTDMWATGVLSYVLLSGLSPFAGDNDVQTLKNVKACDWDFDVesfkYISEEAKDFIRK 8223
Cdd:cd05591   154 TTFCGTPDYIAPEILQELEYGPSVDWWALGVLMYEMMAGQPPFEADNEDDLFESILHDDVLYPV----WLSKEAVSILKA 229
                         250
                  ....*....|
gi 281359561 8224 LLVRNKEKRM 8233
Cdd:cd05591   230 FMTKNPAKRL 239
STKc_PCTAIRE2 cd07872
Catalytic domain of the Serine/Threonine Kinase, PCTAIRE-2 kinase; STKs catalyze the transfer ...
7987-8188 3.48e-18

Catalytic domain of the Serine/Threonine Kinase, PCTAIRE-2 kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PCTAIRE-2 is specifically expressed in neurons in the central nervous system, mainly in terminally differentiated neurons. It associates with Trap (Tudor repeat associator with PCTAIRE-2) and could play a role in regulating mitochondrial function in neurons. PCTAIRE-2 shares sequence similarity with Cyclin-Dependent Kinases (CDKs), which belong to a large family of STKs that are regulated by their cognate cyclins. Together, CDKs and cyclins are involved in the control of cell-cycle progression, transcription, and neuronal function. The PCTAIRE-2 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 143377 [Multi-domain]  Cd Length: 309  Bit Score: 89.67  E-value: 3.48e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 7987 DRYDILEEIGTGAFGVVHRCRERSTGNIFAAKFIPVSHSVEKDLIR-REIDIMNQLHHQKLINLHDAFEDDDEMILILEF 8065
Cdd:cd07872     6 ETYIKLEKLGEGTYATVFKGRSKLTENLVALKEIRLEHEEGAPCTAiREVSLLKDLKHANIVTLHDIVHTDKSLTLVFEY 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 8066 LSGgELFERITAEGYVMTEAEVINYMRQICEGIRHMHEQNIIHLDIKPENIMCQTRSStnVKLIDFGLA------TRLDP 8139
Cdd:cd07872    86 LDK-DLKQYMDDCGNIMSMHNVKIFLYQILRGLAYCHRRKVLHRDLKPQNLLINERGE--LKLADFGLAraksvpTKTYS 162
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|
gi 281359561 8140 NEVVkittgTAEFAAPEI-VNREPVGFYTDMWATGVLSYVLLSGLSPFAG 8188
Cdd:cd07872   163 NEVV-----TLWYRPPDVlLGSSEYSTQIDMWGVGCIFFEMASGRPLFPG 207
FN3 cd00063
Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein ...
5370-5462 4.35e-18

Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein fibronectin. Its tenth fibronectin type III repeat contains an RGD cell recognition sequence in a flexible loop between 2 strands. Approximately 2% of all animal proteins contain the FN3 repeat; including extracellular and intracellular proteins, membrane spanning cytokine receptors, growth hormone receptors, tyrosine phosphatase receptors, and adhesion molecules. FN3-like domains are also found in bacterial glycosyl hydrolases.


Pssm-ID: 238020 [Multi-domain]  Cd Length: 93  Bit Score: 82.93  E-value: 4.35e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 5370 PSVPEGpLRNGDVSKNSIVLRWRPPKDDGGsEITHYVVEKMDNEAMRW--VPVGDCTDTEIRADNLIENHDYSFRVRAVN 5447
Cdd:cd00063     1 PSPPTN-LRVTDVTSTSVTLSWTPPEDDGG-PITGYVVEYREKGSGDWkeVEVTPGSETSYTLTGLKPGTEYEFRVRAVN 78
                          90
                  ....*....|....*
gi 281359561 5448 KQGQSQPLTTSQPIT 5462
Cdd:cd00063    79 GGGESPPSESVTVTT 93
PTZ00024 PTZ00024
cyclin-dependent protein kinase; Provisional
7995-8247 4.71e-18

cyclin-dependent protein kinase; Provisional


Pssm-ID: 240233 [Multi-domain]  Cd Length: 335  Bit Score: 89.82  E-value: 4.71e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 7995 IGTGAFGVVHRCRERSTGNIFA---AKFIPVSHSVEKD-----------LIRREIDIMNQLHHQKLINLHDAFEDDDEMI 8060
Cdd:PTZ00024   17 LGEGTYGKVEKAYDTLTGKIVAikkVKIIEISNDVTKDrqlvgmcgihfTTLRELKIMNEIKHENIMGLVDVYVEGDFIN 96
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 8061 LILEFLSGGelFERITAEGYVMTEAEVINYMRQICEGIRHMHEQNIIHLDIKPENIMCQTRSStnVKLIDFGLATRLDPN 8140
Cdd:PTZ00024   97 LVMDIMASD--LKKVVDRKIRLTESQVKCILLQILNGLNVLHKWYFMHRDLSPANIFINSKGI--CKIADFGLARRYGYP 172
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 8141 EVVKITTG---------------TAEFAAPEIV-NREPVGFYTDMWATGVLSYVLLSGLSPFAGDNDVQTLKNV------ 8198
Cdd:PTZ00024  173 PYSDTLSKdetmqrreemtskvvTLWYRAPELLmGAEKYHFAVDMWSVGCIFAELLTGKPLFPGENEIDQLGRIfellgt 252
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 281359561 8199 -------------------KACDWDFDvESFKYISEEAKDFIRKLLVRNKEKRMTAHECLLHPWLTGD 8247
Cdd:PTZ00024  253 pnednwpqakklplyteftPRKPKDLK-TIFPNASDDAIDLLQSLLKLNPLERISAKEALKHEYFKSD 319
STKc_aPKC cd05588
Catalytic domain of the Serine/Threonine Kinase, Atypical Protein Kinase C; STKs catalyze the ...
7995-8191 4.80e-18

Catalytic domain of the Serine/Threonine Kinase, Atypical Protein Kinase C; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. aPKCs only require phosphatidylserine (PS) for activation. They contain a C2-like region, instead of a calcium-binding (C2) region found in classical PKCs, in their regulatory domain. There are two aPKC isoforms, zeta and iota. aPKCs are involved in many cellular functions including proliferation, migration, apoptosis, polarity maintenance and cytoskeletal regulation. They also play a critical role in the regulation of glucose metabolism and in the pathogenesis of type 2 diabetes. PKCs are classified into three groups (classical, atypical, and novel) depending on their mode of activation and the structural characteristics of their regulatory domain. The aPKC subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270740 [Multi-domain]  Cd Length: 328  Bit Score: 89.79  E-value: 4.80e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 7995 IGTGAFGVVHRCRERSTGNIFAAKFIpvshsvEKDLIRREIDI---MNQLH-------HQKLINLHDAFEDDDEMILILE 8064
Cdd:cd05588     3 IGRGSYAKVLMVELKKTKRIYAMKVI------KKELVNDDEDIdwvQTEKHvfetasnHPFLVGLHSCFQTESRLFFVIE 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 8065 FLSGGELFERITAEGYvMTEAEVINYMRQICEGIRHMHEQNIIHLDIKPENIMCQtrSSTNVKLIDFGLATR-LDPNEVV 8143
Cdd:cd05588    77 FVNGGDLMFHMQRQRR-LPEEHARFYSAEISLALNFLHEKGIIYRDLKLDNVLLD--SEGHIKLTDYGMCKEgLRPGDTT 153
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|
gi 281359561 8144 KITTGTAEFAAPEIVNREPVGFYTDMWATGVLSYVLLSGLSPF--AGDND 8191
Cdd:cd05588   154 STFCGTPNYIAPEILRGEDYGFSVDWWALGVLMFEMLAGRSPFdiVGSSD 203
Ig_Titin_like cd05748
Immunoglobulin (Ig)-like domain of titin and similar proteins; The members here are composed ...
5286-5366 5.47e-18

Immunoglobulin (Ig)-like domain of titin and similar proteins; The members here are composed of the immunoglobulin (Ig)-like domain found in titin-like proteins and similar proteins. Titin (also called connectin) is a fibrous sarcomeric protein specifically found in vertebrate striated muscle. Titin is a giant protein; depending on isoform composition, it ranges from 2970 to 3700 kDa, and is of a length that spans half a sarcomere. Titin largely consists of multiple repeats of Ig-like and fibronectin type 3 (FN-III)-like domains. Titin connects the ends of myosin thick filaments to Z disks and extends along the thick filament to the H zone. It appears to function similarly to an elastic band, keeping the myosin filaments centered in the sarcomere during muscle contraction or stretching. Within the sarcomere, titin is also attached to or is associated with myosin binding protein C (MyBP-C). MyBP-C appears to contribute to the generation of passive tension by titin and like titin has repeated Ig-like and FN-III domains. Also included in this group are worm twitchin and insect projectin, thick filament proteins of invertebrate muscle which also have repeated Ig-like and FN-III domains.


Pssm-ID: 409406 [Multi-domain]  Cd Length: 82  Bit Score: 82.25  E-value: 5.47e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 5286 IKIKAGNVFEFDVPVTGEPLPSKDWTHEGNMIINTDRVKISNFDDRTKIRILDAKRSDTGVYTLTARNINGTDRHNVKVT 5365
Cdd:cd05748     2 IVVRAGESLRLDIPIKGRPTPTVTWSKDGQPLKETGRVQIETTASSTSLVIKNAKRSDSGKYTLTLKNSAGEKSATINVK 81

                  .
gi 281359561 5366 I 5366
Cdd:cd05748    82 V 82
FN3 cd00063
Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein ...
6654-6745 5.55e-18

Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein fibronectin. Its tenth fibronectin type III repeat contains an RGD cell recognition sequence in a flexible loop between 2 strands. Approximately 2% of all animal proteins contain the FN3 repeat; including extracellular and intracellular proteins, membrane spanning cytokine receptors, growth hormone receptors, tyrosine phosphatase receptors, and adhesion molecules. FN3-like domains are also found in bacterial glycosyl hydrolases.


Pssm-ID: 238020 [Multi-domain]  Cd Length: 93  Bit Score: 82.54  E-value: 5.55e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 6654 PSPPTRLRADEFSGDSLTLYWNPPNDDGGsAIQNYIIEKKEARSSTWSKVSS-FCTVPFVRIRNLVLNKEYDFRVIAENK 6732
Cdd:cd00063     1 PSPPTNLRVTDVTSTSVTLSWTPPEDDGG-PITGYVVEYREKGSGDWKEVEVtPGSETSYTLTGLKPGTEYEFRVRAVNG 79
                          90
                  ....*....|...
gi 281359561 6733 YGQSDPANTSEPI 6745
Cdd:cd00063    80 GGESPPSESVTVT 92
STKc_Bck1_like cd06629
Catalytic domain of the Serine/Threonine Kinases, fungal Bck1-like Mitogen-Activated Protein ...
7993-8244 6.73e-18

Catalytic domain of the Serine/Threonine Kinases, fungal Bck1-like Mitogen-Activated Protein Kinase Kinase Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Members of this group include the MAPKKKs Saccharomyces cerevisiae Bck1 and Schizosaccharomyces pombe Mkh1, and related proteins. Budding yeast Bck1 is part of the cell integrity MAPK pathway, which is activated by stresses and aggressions to the cell wall. The MAPKKK Bck1, MAPKKs Mkk1 and Mkk2, and the MAPK Slt2 make up the cascade that is important in the maintenance of cell wall homeostasis. Fission yeast Mkh1 is involved in MAPK cascades regulating cell morphology, cell wall integrity, salt resistance, and filamentous growth in response to stress. MAPKKKs phosphorylate and activate MAPK kinases, which in turn phosphorylate and activate MAPKs during signaling cascades that are important in mediating cellular responses to extracellular signals. The Bck1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270799 [Multi-domain]  Cd Length: 270  Bit Score: 87.82  E-value: 6.73e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 7993 EEIGTGAFGVVHRCRERSTGNIFAAKFIPV-SHSVEK---------DLIRREIDIMNQLHHQKLINlHDAFEDDDEMILI 8062
Cdd:cd06629     7 ELIGKGTYGRVYLAMNATTGEMLAVKQVELpKTSSDRadsrqktvvDALKSEIDTLKDLDHPNIVQ-YLGFEETEDYFSI 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 8063 -LEFLSGGELFERITAEGYVmtEAEVI-NYMRQICEGIRHMHEQNIIHLDIKPENIMCQTRSstNVKLIDFGLATRLD-- 8138
Cdd:cd06629    86 fLEYVPGGSIGSCLRKYGKF--EEDLVrFFTRQILDGLAYLHSKGILHRDLKADNILVDLEG--ICKISDFGISKKSDdi 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 8139 -PNEVVKITTGTAEFAAPEIVNREPVGF--YTDMWATGVLSYVLLSGLSPFAGDNDVQTLKNV----KACDWDFDVEsfk 8211
Cdd:cd06629   162 yGNNGATSMQGSVFWMAPEVIHSQGQGYsaKVDIWSLGCVVLEMLAGRRPWSDDEAIAAMFKLgnkrSAPPVPEDVN--- 238
                         250       260       270
                  ....*....|....*....|....*....|...
gi 281359561 8212 yISEEAKDFIRKLLVRNKEKRMTAHECLLHPWL 8244
Cdd:cd06629   239 -LSPEALDFLNACFAIDPRDRPTAAELLSHPFL 270
PTZ00283 PTZ00283
serine/threonine protein kinase; Provisional
7988-8242 6.91e-18

serine/threonine protein kinase; Provisional


Pssm-ID: 240344 [Multi-domain]  Cd Length: 496  Bit Score: 91.47  E-value: 6.91e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 7988 RYDILEEIGTGAFGVVHRCRERSTGNIFAAKFIPVSHSVEKDLIRR--EIDIMNQLHHQKLINLHDAFEDDDE------- 8058
Cdd:PTZ00283   33 KYWISRVLGSGATGTVLCAKRVSDGEPFAVKVVDMEGMSEADKNRAqaEVCCLLNCDFFSIVKCHEDFAKKDPrnpenvl 112
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 8059 -MILILEFLSGGELFERI-----TAEGYVMTEAEVInyMRQICEGIRHMHEQNIIHLDIKPENIM-CqtrSSTNVKLIDF 8131
Cdd:PTZ00283  113 mIALVLDYANAGDLRQEIksrakTNRTFREHEAGLL--FIQVLLAVHHVHSKHMIHRDIKSANILlC---SNGLVKLGDF 187
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 8132 GL-----ATRLDpnEVVKITTGTAEFAAPEIVNREPVGFYTDMWATGVLSYVLLSGLSPFAGDNDVQTLKNVKACDWDFD 8206
Cdd:PTZ00283  188 GFskmyaATVSD--DVGRTFCGTPYYVAPEIWRRKPYSKKADMFSLGVLLYELLTLKRPFDGENMEEVMHKTLAGRYDPL 265
                         250       260       270
                  ....*....|....*....|....*....|....*.
gi 281359561 8207 VESfkyISEEAKDFIRKLLVRNKEKRMTAHECLLHP 8242
Cdd:PTZ00283  266 PPS---ISPEMQEIVTALLSSDPKRRPSSSKLLNMP 298
FN3 cd00063
Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein ...
3889-3980 7.01e-18

Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein fibronectin. Its tenth fibronectin type III repeat contains an RGD cell recognition sequence in a flexible loop between 2 strands. Approximately 2% of all animal proteins contain the FN3 repeat; including extracellular and intracellular proteins, membrane spanning cytokine receptors, growth hormone receptors, tyrosine phosphatase receptors, and adhesion molecules. FN3-like domains are also found in bacterial glycosyl hydrolases.


Pssm-ID: 238020 [Multi-domain]  Cd Length: 93  Bit Score: 82.16  E-value: 7.01e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 3889 PSKPKGpLAVSNVTAETLHLKWEKPEDDGGdPIEQYLVERMDTETGRW--VPVLTTKTPEADVTGLTEGKEYLFRVKAVN 3966
Cdd:cd00063     1 PSPPTN-LRVTDVTSTSVTLSWTPPEDDGG-PITGYVVEYREKGSGDWkeVEVTPGSETSYTLTGLKPGTEYEFRVRAVN 78
                          90
                  ....*....|....
gi 281359561 3967 SEGESEPLVTDIPT 3980
Cdd:cd00063    79 GGGESPPSESVTVT 92
PTKc_Frk_like cd05068
Catalytic domain of Fyn-related kinase-like Protein Tyrosine Kinases; PTKs catalyze the ...
7979-8198 7.90e-18

Catalytic domain of Fyn-related kinase-like Protein Tyrosine Kinases; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Frk and Srk are members of the Src subfamily of proteins, which are cytoplasmic (or non-receptor) PTKs. Frk, also known as Rak, is specifically expressed in liver, lung, kidney, intestine, mammary glands, and the islets of Langerhans. Rodent homologs were previously referred to as GTK (gastrointestinal tyr kinase), BSK (beta-cell Src-like kinase), or IYK (intestinal tyr kinase). Studies in mice reveal that Frk is not essential for viability. It plays a role in the signaling that leads to cytokine-induced beta-cell death in Type I diabetes. It also regulates beta-cell number during embryogenesis and early in life. Src kinases contain an N-terminal SH4 domain with a myristoylation site, followed by SH3 and SH2 domains, a tyr kinase domain, and a regulatory C-terminal region containing a conserved tyr. They are activated by autophosphorylation at the tyr kinase domain, but are negatively regulated by phosphorylation at the C-terminal tyr by Csk (C-terminal Src Kinase). The Frk-like subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270653 [Multi-domain]  Cd Length: 267  Bit Score: 87.46  E-value: 7.90e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 7979 EISQQSVydryDILEEIGTGAFGVVHRCRERSTGNIFAAKFIPVSHSVEKDLirREIDIMNQLHHQKLINLHDAFEDDDE 8058
Cdd:cd05068     4 EIDRKSL----KLLRKLGSGQFGEVWEGLWNNTTPVAVKTLKPGTMDPEDFL--REAQIMKKLRHPKLIQLYAVCTLEEP 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 8059 MILILEFLSGGELFERITAEGYVMTEAEVINYMRQICEGIRHMHEQNIIHLDIKPENIMCQTRSStnVKLIDFGLATRLD 8138
Cdd:cd05068    78 IYIITELMKHGSLLEYLQGKGRSLQLPQLIDMAAQVASGMAYLESQNYIHRDLAARNVLVGENNI--CKVADFGLARVIK 155
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 281359561 8139 PNEVVKITTGTA---EFAAPEIVNREPVGFYTDMWATGVLSYVLLS-GLSPFAGDNDVQTLKNV 8198
Cdd:cd05068   156 VEDEYEAREGAKfpiKWTAPEAANYNRFSIKSDVWSFGILLTEIVTyGRIPYPGMTNAEVLQQV 219
PTZ00426 PTZ00426
cAMP-dependent protein kinase catalytic subunit; Provisional
7986-8276 8.24e-18

cAMP-dependent protein kinase catalytic subunit; Provisional


Pssm-ID: 173616 [Multi-domain]  Cd Length: 340  Bit Score: 89.27  E-value: 8.24e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 7986 YDRYDILEEIGTGAFGVVHRCRERStgnifaAKFIPVS-HSVEK---------DLIRREIDIMNQLHHQKLINLHDAFED 8055
Cdd:PTZ00426   29 YEDFNFIRTLGTGSFGRVILATYKN------EDFPPVAiKRFEKskiikqkqvDHVFSERKILNYINHPFCVNLYGSFKD 102
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 8056 DDEMILILEFLSGGELFERITAEGYVMTEAEVInYMRQICEGIRHMHEQNIIHLDIKPENIMCQTRSStnVKLIDFGLAT 8135
Cdd:PTZ00426  103 ESYLYLVLEFVIGGEFFTFLRRNKRFPNDVGCF-YAAQIVLIFEYLQSLNIVYRDLKPENLLLDKDGF--IKMTDFGFAK 179
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 8136 RLDPNEVVkiTTGTAEFAAPEIVNREPVGFYTDMWATGVLSYVLLSGLSPFAGDNDVQTLKNVKACDWDFDvesfKYISE 8215
Cdd:PTZ00426  180 VVDTRTYT--LCGTPEYIAPEILLNVGHGKAADWWTLGIFIYEILVGCPPFYANEPLLIYQKILEGIIYFP----KFLDN 253
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 281359561 8216 EAKDFIRKLLVRNKEKRM-----TAHECLLHPWLTG-DHSAMkqeINRDRYLAYREKLRRKYE--DFER 8276
Cdd:PTZ00426  254 NCKHLMKKLLSHDLTKRYgnlkkGAQNVKEHPWFGNiDWVSL---LHKNVEVPYKPKYKNVFDssNFER 319
STKc_Mos cd13979
Catalytic domain of the Serine/Threonine kinase, Oocyte maturation factor Mos; STKs catalyze ...
7992-8240 8.25e-18

Catalytic domain of the Serine/Threonine kinase, Oocyte maturation factor Mos; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Mos (or c-Mos) is a germ-cell specific kinase that plays roles in both the release of primary arrest and the induction of secondary arrest in oocytes. It is expressed towards the end of meiosis I and is quickly degraded upon fertilization. It is a component of the cytostatic factor (CSF), which is responsible for metaphase II arrest. In addition, Mos activates a phoshorylation cascade that leads to the activation of the p34 subunit of MPF (mitosis-promoting factor or maturation promoting factor), a cyclin-dependent kinase that is responsible for the release of primary arrest in meiosis I. The Mos subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270881 [Multi-domain]  Cd Length: 265  Bit Score: 87.44  E-value: 8.25e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 7992 LEEIGTGAFGVVHRCRERstGNIFAAKFIPVS--HSVEKDLIRREIDIMNqLHHQKLINL---HDAFEDDDEMILILEFL 8066
Cdd:cd13979     8 QEPLGSGGFGSVYKATYK--GETVAVKIVRRRrkNRASRQSFWAELNAAR-LRHENIVRVlaaETGTDFASLGLIIMEYC 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 8067 SGGELFERITAEGYVMTEAEVINYMRQICEGIRHMHEQNIIHLDIKPENI-MCQtrsSTNVKLIDFGLATRL-DPNEV-- 8142
Cdd:cd13979    85 GNGTLQQLIYEGSEPLPLAHRILISLDIARALRFCHSHGIVHLDVKPANIlISE---QGVCKLCDFGCSVKLgEGNEVgt 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 8143 -VKITTGTAEFAAPEIVNREPVGFYTDMWATGVLSYVLLSGLSPFAGDNDVQTL----KNVKACDWDFDVESFKyisEEA 8217
Cdd:cd13979   162 pRSHIGGTYTYRAPELLKGERVTPKADIYSFGITLWQMLTRELPYAGLRQHVLYavvaKDLRPDLSGLEDSEFG---QRL 238
                         250       260
                  ....*....|....*....|...
gi 281359561 8218 KDFIRKLLVRNKEKRMTAHECLL 8240
Cdd:cd13979   239 RSLISRCWSAQPAERPNADESLL 261
I-set pfam07679
Immunoglobulin I-set domain;
8437-8525 9.29e-18

Immunoglobulin I-set domain;


Pssm-ID: 400151 [Multi-domain]  Cd Length: 90  Bit Score: 81.92  E-value: 9.29e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561  8437 PSFTFLLRPRVMQARDTCKLLCCLSGKPVPNVRWYKDGREL-SKYEYAMTHSDGVVTMEIIDCKPSDSGKYSCKATNCHG 8515
Cdd:pfam07679    1 PKFTQKPKDVEVQEGESARFTCTVTGTPDPEVSWFKDGQPLrSSDRFKVTYEGGTYTLTISNVQPDDSGKYTCVATNSAG 80
                           90
                   ....*....|
gi 281359561  8516 TDETDCVVIV 8525
Cdd:pfam07679   81 EAEASAELTV 90
STKc_EIF2AK2_PKR cd14047
Catalytic domain of the Serine/Threonine kinase, eukaryotic translation Initiation Factor ...
7989-8241 1.12e-17

Catalytic domain of the Serine/Threonine kinase, eukaryotic translation Initiation Factor 2-Alpha Kinase 2 or Protein Kinase regulated by RNA; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PKR (or EIF2AK2) contains an N-terminal double-stranded RNA (dsRNA) binding domain and a C-terminal catalytic kinase domain. It is activated by dsRNA, which is produced as a replication intermediate in virally infected cells. It plays a key role in mediating innate immune responses to viral infection. PKR is also directly activated by PACT (protein activator of PKR) and heparin, and is inhibited by viral proteins and RNAs. PKR also regulates transcription and signal transduction in diseased cells, playing roles in tumorigenesis and neurodegenerative diseases. EIF2AKs phosphorylate the alpha subunit of eIF-2, resulting in the downregulation of protein synthesis. The PKR subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270949 [Multi-domain]  Cd Length: 267  Bit Score: 87.16  E-value: 1.12e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 7989 YDILEEIGTGAFGVVHRCRERSTGNIFAAKFIPVSHSVEKdlirREIDIMNQLHHQKLINLHDAFEDDDEMI-------- 8060
Cdd:cd14047     8 FKEIELIGSGGFGQVFKAKHRIDGKTYAIKRVKLNNEKAE----REVKALAKLDHPNIVRYNGCWDGFDYDPetsssnss 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 8061 --------LILEFLSGGELFERITAEGYVMTEA-EVINYMRQICEGIRHMHEQNIIHLDIKPENIMCQtrSSTNVKLIDF 8131
Cdd:cd14047    84 rsktkclfIQMEFCEKGTLESWIEKRNGEKLDKvLALEIFEQITKGVEYIHSKKLIHRDLKPSNIFLV--DTGKVKIGDF 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 8132 GLATRL-DPNEVVKiTTGTAEFAAPEIVNREPVGFYTDMWATGVLSYVLLSGL-SPFAGDNDVQTLKNVKACDwDFDVes 8209
Cdd:cd14047   162 GLVTSLkNDGKRTK-SKGTLSYMSPEQISSQDYGKEVDIYALGLILFELLHVCdSAFEKSKFWTDLRNGILPD-IFDK-- 237
                         250       260       270
                  ....*....|....*....|....*....|..
gi 281359561 8210 fKYISEEAkdFIRKLLVRNKEKRMTAHECLLH 8241
Cdd:cd14047   238 -RYKIEKT--IIKKMLSKKPEDRPNASEILRT 266
FN3 cd00063
Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein ...
6259-6350 1.12e-17

Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein fibronectin. Its tenth fibronectin type III repeat contains an RGD cell recognition sequence in a flexible loop between 2 strands. Approximately 2% of all animal proteins contain the FN3 repeat; including extracellular and intracellular proteins, membrane spanning cytokine receptors, growth hormone receptors, tyrosine phosphatase receptors, and adhesion molecules. FN3-like domains are also found in bacterial glycosyl hydrolases.


Pssm-ID: 238020 [Multi-domain]  Cd Length: 93  Bit Score: 81.77  E-value: 1.12e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 6259 PSPPEGpLSYTETAPDHISLHWYSPKDDGGsDITGYIIEFTEFGVDDWKPVPGTCPN-TNFTVKNLVEGKKYVFRIRAEN 6337
Cdd:cd00063     1 PSPPTN-LRVTDVTSTSVTLSWTPPEDDGG-PITGYVVEYREKGSGDWKEVEVTPGSeTSYTLTGLKPGTEYEFRVRAVN 78
                          90
                  ....*....|...
gi 281359561 6338 IYGASEALEGKPV 6350
Cdd:cd00063    79 GGGESPPSESVTV 91
FN3 cd00063
Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein ...
4285-4383 1.13e-17

Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein fibronectin. Its tenth fibronectin type III repeat contains an RGD cell recognition sequence in a flexible loop between 2 strands. Approximately 2% of all animal proteins contain the FN3 repeat; including extracellular and intracellular proteins, membrane spanning cytokine receptors, growth hormone receptors, tyrosine phosphatase receptors, and adhesion molecules. FN3-like domains are also found in bacterial glycosyl hydrolases.


Pssm-ID: 238020 [Multi-domain]  Cd Length: 93  Bit Score: 81.77  E-value: 1.13e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 4285 PGKPGTPEAVDWDKDHVDLVWRPPiNDGGSPITGYVVEKREKGTDKWikgTEITIPClGEECKATVPTLNENCEYEFRVK 4364
Cdd:cd00063     1 PSPPTNLRVTDVTSTSVTLSWTPP-EDDGGPITGYVVEYREKGSGDW---KEVEVTP-GSETSYTLTGLKPGTEYEFRVR 75
                          90
                  ....*....|....*....
gi 281359561 4365 AINAAGPGEPSDaSKPIIT 4383
Cdd:cd00063    76 AVNGGGESPPSE-SVTVTT 93
PTKc_Tec_like cd05059
Catalytic domain of Tec-like Protein Tyrosine Kinases; PTKs catalyze the transfer of the ...
7992-8200 1.14e-17

Catalytic domain of Tec-like Protein Tyrosine Kinases; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. The Tec-like subfamily is composed of Tec, Btk, Bmx (Etk), Itk (Tsk, Emt), Rlk (Txk), and similar proteins. They are cytoplasmic (or nonreceptor) PTKs with similarity to Src kinases in that they contain Src homology protein interaction domains (SH3, SH2) N-terminal to the catalytic tyr kinase domain. Unlike Src kinases, most Tec subfamily members except Rlk also contain an N-terminal pleckstrin homology (PH) domain, which binds the products of PI3K and allows membrane recruitment and activation. In addition, some members contain the Tec homology (TH) domain, which contains proline-rich and zinc-binding regions. Tec kinases form the second largest subfamily of nonreceptor PTKs and are expressed mainly by haematopoietic cells, although Tec and Bmx are also found in endothelial cells. B-cells express Btk and Tec, while T-cells express Itk, Txk, and Tec. Collectively, Tec kinases are expressed in a variety of myeloid cells such as mast cells, platelets, macrophages, and dendritic cells. Each Tec kinase shows a distinct cell-type pattern of expression. Tec kinases play important roles in the development, differentiation, maturation, regulation, survival, and function of B-cells and T-cells. Mutations in Btk cause the severe B-cell immunodeficiency, X-linked agammaglobulinaemia (XLA). The Tec-like subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 173637 [Multi-domain]  Cd Length: 256  Bit Score: 86.73  E-value: 1.14e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 7992 LEEIGTGAFGVVHRCRERSTGNIfAAKFIPVSHSVEKDLIrREIDIMNQLHHQKLINLHDAFEDDDEMILILEFLSGGEL 8071
Cdd:cd05059     9 LKELGSGQFGVVHLGKWRGKIDV-AIKMIKEGSMSEDDFI-EEAKVMMKLSHPKLVQLYGVCTKQRPIFIVTEYMANGCL 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 8072 FERITAEGYVMTEAEVINYMRQICEGIRHMHEQNIIHLDIKPENimCQTRSSTNVKLIDFGLATRLDPNEVVKiTTGT-- 8149
Cdd:cd05059    87 LNYLRERRGKFQTEQLLEMCKDVCEAMEYLESNGFIHRDLAARN--CLVGEQNVVKVSDFGLARYVLDDEYTS-SVGTkf 163
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 281359561 8150 -AEFAAPEIVNREPVGFYTDMWATGVLSYVLLS-GLSPFAGDNDVQTLKNVKA 8200
Cdd:cd05059   164 pVKWSPPEVFMYSKFSSKSDVWSFGVLMWEVFSeGKMPYERFSNSEVVEHISQ 216
FN3 cd00063
Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein ...
4484-4571 1.16e-17

Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein fibronectin. Its tenth fibronectin type III repeat contains an RGD cell recognition sequence in a flexible loop between 2 strands. Approximately 2% of all animal proteins contain the FN3 repeat; including extracellular and intracellular proteins, membrane spanning cytokine receptors, growth hormone receptors, tyrosine phosphatase receptors, and adhesion molecules. FN3-like domains are also found in bacterial glycosyl hydrolases.


Pssm-ID: 238020 [Multi-domain]  Cd Length: 93  Bit Score: 81.77  E-value: 1.16e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 4484 PGKPEGpLEVSEVHKDGCKLKWKKPKDDGGePVESYLVEKFDPDTGIW--LPVGRSDGPEYNVDGLVPGHDYKFRVKAVN 4561
Cdd:cd00063     1 PSPPTN-LRVTDVTSTSVTLSWTPPEDDGG-PITGYVVEYREKGSGDWkeVEVTPGSETSYTLTGLKPGTEYEFRVRAVN 78
                          90
                  ....*....|
gi 281359561 4562 KEGESEPLET 4571
Cdd:cd00063    79 GGGESPPSES 88
Ig_Titin_like cd05748
Immunoglobulin (Ig)-like domain of titin and similar proteins; The members here are composed ...
7758-7833 1.24e-17

Immunoglobulin (Ig)-like domain of titin and similar proteins; The members here are composed of the immunoglobulin (Ig)-like domain found in titin-like proteins and similar proteins. Titin (also called connectin) is a fibrous sarcomeric protein specifically found in vertebrate striated muscle. Titin is a giant protein; depending on isoform composition, it ranges from 2970 to 3700 kDa, and is of a length that spans half a sarcomere. Titin largely consists of multiple repeats of Ig-like and fibronectin type 3 (FN-III)-like domains. Titin connects the ends of myosin thick filaments to Z disks and extends along the thick filament to the H zone. It appears to function similarly to an elastic band, keeping the myosin filaments centered in the sarcomere during muscle contraction or stretching. Within the sarcomere, titin is also attached to or is associated with myosin binding protein C (MyBP-C). MyBP-C appears to contribute to the generation of passive tension by titin and like titin has repeated Ig-like and FN-III domains. Also included in this group are worm twitchin and insect projectin, thick filament proteins of invertebrate muscle which also have repeated Ig-like and FN-III domains.


Pssm-ID: 409406 [Multi-domain]  Cd Length: 82  Bit Score: 81.10  E-value: 1.24e-17
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 281359561 7758 GENVVIKIPFTGFPKPRIHWVRDGENIESGGHYTVEVKERHAVLIIRDGSHLDSGPYRITAENELGSDTAIIQVQI 7833
Cdd:cd05748     7 GESLRLDIPIKGRPTPTVTWSKDGQPLKETGRVQIETTASSTSLVIKNAKRSDSGKYTLTLKNSAGEKSATINVKV 82
STKc_MAP3K12_13 cd14059
Catalytic domain of the Serine/Threonine Kinases, Mitogen-Activated Protein Kinase Kinase ...
7995-8186 1.24e-17

Catalytic domain of the Serine/Threonine Kinases, Mitogen-Activated Protein Kinase Kinase Kinases 12 and 13; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MAP3K12 is also called MAPK upstream kinase (MUK), dual leucine zipper-bearing kinase (DLK) or leucine-zipper protein kinase (ZPK). It is involved in the c-Jun N-terminal kinase (JNK) pathway that directly regulates axonal regulation through the phosphorylation of microtubule-associated protein 1B (MAP1B). It also regulates the differentiation of many cell types including adipocytes and may play a role in adipogenesis. MAP3K13, also called leucine zipper-bearing kinase (LZK), directly phosphorylates and activates MKK7, which in turn activates the JNK pathway. It also activates NF-kB through IKK activation and this activity is enhanced by antioxidant protein-1 (AOP-1). MAP3Ks (MKKKs or MAPKKKs) phosphorylate and activate MAP2Ks (MAPKKs or MKKs), which in turn phosphorylate and activate MAPKs during signaling cascades that are important in mediating cellular responses to extracellular signals. The MAP3K12/13 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270961 [Multi-domain]  Cd Length: 237  Bit Score: 86.39  E-value: 1.24e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 7995 IGTGAFGVVhrcrerstgniFAAKFIPVSHSVEKDLIRREIDI--MNQLHHQKLINLHDAFEDDDEMILILEFLSGGELF 8072
Cdd:cd14059     1 LGSGAQGAV-----------FLGKFRGEEVAVKKVRDEKETDIkhLRKLNHPNIIKFKGVCTQAPCYCILMEYCPYGQLY 69
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 8073 ErITAEGYVMTEAEVINYMRQICEGIRHMHEQNIIHLDIKPENIMCQTRSStnVKLIDFGLATRLDPNEVVKITTGTAEF 8152
Cdd:cd14059    70 E-VLRAGREITPSLLVDWSKQIASGMNYLHLHKIIHRDLKSPNVLVTYNDV--LKISDFGTSKELSEKSTKMSFAGTVAW 146
                         170       180       190
                  ....*....|....*....|....*....|....
gi 281359561 8153 AAPEIVNREPVGFYTDMWATGVLSYVLLSGLSPF 8186
Cdd:cd14059   147 MAPEVIRNEPCSEKVDIWSFGVVLWELLTGEIPY 180
STKc_MST3 cd06641
Catalytic domain of the Serine/Threonine Kinase, Mammalian Ste20-like protein kinase 3; STKs ...
7992-8244 1.31e-17

Catalytic domain of the Serine/Threonine Kinase, Mammalian Ste20-like protein kinase 3; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MST3 phosphorylates the STK NDR and may play a role in cell cycle progression and cell morphology. It may also regulate paxillin and consequently, cell migration. MST3 is present in human placenta, where it plays an essential role in the oxidative stress-induced apoptosis of trophoblasts in normal spontaneous delivery. Dysregulation of trophoblast apoptosis may result in pregnancy complications such as preeclampsia and intrauterine growth retardation. The MST3 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270809 [Multi-domain]  Cd Length: 277  Bit Score: 87.44  E-value: 1.31e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 7992 LEEIGTGAFGVVHRCRERSTGNIFAAKFIPVSHSVEK-DLIRREIDIMNQLHHQKLINLHDAFEDDDEMILILEFLSGGE 8070
Cdd:cd06641     9 LEKIGKGSFGEVFKGIDNRTQKVVAIKIIDLEEAEDEiEDIQQEITVLSQCDSPYVTKYYGSYLKDTKLWIIMEYLGGGS 88
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 8071 LFERItaEGYVMTEAEVINYMRQICEGIRHMHEQNIIHLDIKPENIMCQTRSStnVKLIDFGLATRLDPNEVVK-ITTGT 8149
Cdd:cd06641    89 ALDLL--EPGPLDETQIATILREILKGLDYLHSEKKIHRDIKAANVLLSEHGE--VKLADFGVAGQLTDTQIKRn*FVGT 164
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 8150 AEFAAPEIVNREPVGFYTDMWATGVLSYVLLSGLSPFAGDNDVQTLKNVKACDWDFDVESFkyiSEEAKDFIRKLLVRNK 8229
Cdd:cd06641   165 PFWMAPEVIKQSAYDSKADIWSLGITAIELARGEPPHSELHPMKVLFLIPKNNPPTLEGNY---SKPLKEFVEACLNKEP 241
                         250
                  ....*....|....*
gi 281359561 8230 EKRMTAHECLLHPWL 8244
Cdd:cd06641   242 SFRPTAKELLKHKFI 256
STKc_MST4 cd06640
Catalytic domain of the Serine/Threonine Kinase, Mammalian Ste20-like protein kinase 4; STKs ...
7992-8244 1.34e-17

Catalytic domain of the Serine/Threonine Kinase, Mammalian Ste20-like protein kinase 4; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MST4 is sometimes referred to as MASK (MST3 and SOK1-related kinase). It plays a role in mitogen-activated protein kinase (MAPK) signaling during cytoskeletal rearrangement, morphogenesis, and apoptosis. It influences cell growth and transformation by modulating the extracellular signal-regulated kinase (ERK) pathway. MST4 may also play a role in tumor formation and progression. It localizes in the Golgi apparatus by interacting with the Golgi matrix protein GM130 and may play a role in cell migration. The MST4 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 132971 [Multi-domain]  Cd Length: 277  Bit Score: 87.42  E-value: 1.34e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 7992 LEEIGTGAFGVVHRCRERSTGNIFAAKFIPVSHSV-EKDLIRREIDIMNQLHHQKLINLHDAFEDDDEMILILEFLSGGE 8070
Cdd:cd06640     9 LERIGKGSFGEVFKGIDNRTQQVVAIKIIDLEEAEdEIEDIQQEITVLSQCDSPYVTKYYGSYLKGTKLWIIMEYLGGGS 88
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 8071 LFERITAEGYvmTEAEVINYMRQICEGIRHMHEQNIIHLDIKPENIMCQTRSstNVKLIDFGLATRLDPNEVVKIT-TGT 8149
Cdd:cd06640    89 ALDLLRAGPF--DEFQIATMLKEILKGLDYLHSEKKIHRDIKAANVLLSEQG--DVKLADFGVAGQLTDTQIKRNTfVGT 164
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 8150 AEFAAPEIVNREPVGFYTDMWATGVLSYVLLSGLSPFAGDNDVQTLKNVKACDWDFDVESFkyiSEEAKDFIRKLLVRNK 8229
Cdd:cd06640   165 PFWMAPEVIQQSAYDSKADIWSLGITAIELAKGEPPNSDMHPMRVLFLIPKNNPPTLVGDF---SKPFKEFIDACLNKDP 241
                         250
                  ....*....|....*
gi 281359561 8230 EKRMTAHECLLHPWL 8244
Cdd:cd06640   242 SFRPTAKELLKHKFI 256
STKc_PIM3 cd14102
Catalytic domain of the Serine/Threonine kinase, Proviral Integration Moloney virus (PIM) ...
7989-8244 1.49e-17

Catalytic domain of the Serine/Threonine kinase, Proviral Integration Moloney virus (PIM) kinase 3; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The PIM gene locus was discovered as a result of the cloning of retroviral intergration sites in murine Moloney leukemia virus, leading to the identification of PIM kinases. They are constitutively active STKs with a broad range of cellular targets and are overexpressed in many haematopoietic malignancies and solid cancers. Vertebrates contain three distinct PIM kinase genes (PIM1-3). PIM3 can inhibit apoptosis and promote cell survival and protein translation, therefore, it can enhance the proliferation of normal and cancer cells. Mice deficient with PIM3 show minimal effects, suggesting that PIM3 msy not be essential. Since its expression is enhanced in several cancers, it may make a good molecular target for cancer drugs. The PIM3 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271004 [Multi-domain]  Cd Length: 253  Bit Score: 86.55  E-value: 1.49e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 7989 YDILEEIGTGAFGVVHRCRERSTGNIFAAKFIPVSHSVE-----KDLIRREIDIMNQL--HHQKLINLHDAFEDDDEMIL 8061
Cdd:cd14102     2 YQVGSVLGSGGFGTVYAGSRIADGLPVAVKHVVKERVTEwgtlnGVMVPLEIVLLKKVgsGFRGVIKLLDWYERPDGFLI 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 8062 ILEFLS-GGELFERITAEGyVMTEAEVINYMRQICEGIRHMHEQNIIHLDIKPENIMCQTRSStNVKLIDFGLATRLDpN 8140
Cdd:cd14102    82 VMERPEpVKDLFDFITEKG-ALDEDTARGFFRQVLEAVRHCYSCGVVHRDIKDENLLVDLRTG-ELKLIDFGSGALLK-D 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 8141 EVVKITTGTAEFAAPEIVNREPV-GFYTDMWATGVLSYVLLSGLSPFAGDNDVQTLKnvkacdwdfdVESFKYISEEAKD 8219
Cdd:cd14102   159 TVYTDFDGTRVYSPPEWIRYHRYhGRSATVWSLGVLLYDMVCGDIPFEQDEEILRGR----------LYFRRRVSPECQQ 228
                         250       260
                  ....*....|....*....|....*
gi 281359561 8220 FIRKLLVRNKEKRMTAHECLLHPWL 8244
Cdd:cd14102   229 LIKWCLSLRPSDRPTLEQIFDHPWM 253
FN3 cd00063
Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein ...
7444-7531 2.10e-17

Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein fibronectin. Its tenth fibronectin type III repeat contains an RGD cell recognition sequence in a flexible loop between 2 strands. Approximately 2% of all animal proteins contain the FN3 repeat; including extracellular and intracellular proteins, membrane spanning cytokine receptors, growth hormone receptors, tyrosine phosphatase receptors, and adhesion molecules. FN3-like domains are also found in bacterial glycosyl hydrolases.


Pssm-ID: 238020 [Multi-domain]  Cd Length: 93  Bit Score: 81.00  E-value: 2.10e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 7444 PSAPTGPMgISYINKNSCMLNWRPPSYDGGlKVSHYVIERKDVSSPHWITVSST-CKDTAFNVQGLIENQEYIFRVMAVN 7522
Cdd:cd00063     1 PSPPTNLR-VTDVTSTSVTLSWTPPEDDGG-PITGYVVEYREKGSGDWKEVEVTpGSETSYTLTGLKPGTEYEFRVRAVN 78

                  ....*....
gi 281359561 7523 ENGMGPPLE 7531
Cdd:cd00063    79 GGGESPPSE 87
PKc_MKK3_6 cd06617
Catalytic domain of the dual-specificity Protein Kinases, Mitogen-activated protein Kinase ...
7987-8245 2.24e-17

Catalytic domain of the dual-specificity Protein Kinases, Mitogen-activated protein Kinase Kinases 3 and 6; PKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine (ST) or tyrosine residues on protein substrates. MKK3 and MKK6 are dual-specificity PKs that phosphorylate and activate their downstream target, p38 MAPK, on specific threonine and tyrosine residues. MKK3/6 play roles in the regulation of cell cycle progression, cytokine- and stress-induced apoptosis, oncogenic transformation, and adult tissue regeneration. In addition, MKK6 plays a critical role in osteoclast survival in inflammatory disease while MKK3 is associated with tumor invasion, progression, and poor patient survival in glioma. The MKK3/6 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 173729 [Multi-domain]  Cd Length: 283  Bit Score: 86.71  E-value: 2.24e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 7987 DRYDILEEIGTGAFGVVHRCRERSTGNIFAAKFIPVS-HSVEKDLIRREIDI-MNQLHHQKLINLHDA-FEDDDEMILiL 8063
Cdd:cd06617     1 DDLEVIEELGRGAYGVVDKMRHVPTGTIMAVKRIRATvNSQEQKRLLMDLDIsMRSVDCPYTVTFYGAlFREGDVWIC-M 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 8064 EFL--SGGELFERITAEGYVMTEaEVINYMR-QICEGIRHMHEQ-NIIHLDIKPENIMCQTRSstNVKLIDFGLATRLdP 8139
Cdd:cd06617    80 EVMdtSLDKFYKKVYDKGLTIPE-DILGKIAvSIVKALEYLHSKlSVIHRDVKPSNVLINRNG--QVKLCDFGISGYL-V 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 8140 NEVVK-ITTGTAEFAAPEIVN--REPVGF--YTDMWATGVLSYVLLSGLSPFAG-DNDVQTLKNV-KACDWDFDVESFky 8212
Cdd:cd06617   156 DSVAKtIDAGCKPYMAPERINpeLNQKGYdvKSDVWSLGITMIELATGRFPYDSwKTPFQQLKQVvEEPSPQLPAEKF-- 233
                         250       260       270
                  ....*....|....*....|....*....|...
gi 281359561 8213 iSEEAKDFIRKLLVRNKEKRMTAHECLLHPWLT 8245
Cdd:cd06617   234 -SPEFQDFVNKCLKKNYKERPNYPELLQHPFFE 265
IgI_4_MYLK-like cd20976
Fourth Ig-like domain from smooth muscle myosin light chain kinase and similar domains ; a ...
7254-7344 2.34e-17

Fourth Ig-like domain from smooth muscle myosin light chain kinase and similar domains ; a member of the I-set of IgSF domains; The members here are composed of the fourth immunoglobulin (Ig)-like domain from smooth muscle myosin light chain kinase (MYLK) and similar domains. The Ig superfamily (IgSF) is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. Unlike the V-set, one of the distinctive features of I-set domains is the lack of a C" strand. The structure of this group shows that the fourth Ig-like domain from myosin light chain kinase lacks this strand and thus belongs to the I-set of the IgSF. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors, the hemolymph protein hemolin, the muscle proteins titin, telokin, and twitchin, the neuronal adhesion molecule axonin-1, and the signaling molecule semaphorin 4D that is involved in axonal guidance, immune function and angiogenesis.


Pssm-ID: 409568 [Multi-domain]  Cd Length: 90  Bit Score: 80.76  E-value: 2.34e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 7254 PDWITRLQDKVAPFGKDYTLQCAASGKPSPTARWLRNGKEIQMNGGRMTCDSkdGVFRLHISNVQTGDDGDYTCEAMNSL 7333
Cdd:cd20976     2 PSFSSVPKDLEAVEGQDFVAQCSARGKPVPRITWIRNAQPLQYAADRSTCEA--GVGELHIQDVLPEDHGTYTCLAKNAA 79
                          90
                  ....*....|.
gi 281359561 7334 GFVNTSGYLKI 7344
Cdd:cd20976    80 GQVSCSAWVTV 90
fn3 pfam00041
Fibronectin type III domain;
6360-6444 2.43e-17

Fibronectin type III domain;


Pssm-ID: 394996 [Multi-domain]  Cd Length: 85  Bit Score: 80.54  E-value: 2.43e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561  6360 GAPSQPTISAYTPNSANLEWHPPDDCGGkPITGYIVERRERGGEWIKcNNYPTPNT--SYTVSNLRDGARYEFRVLAVNE 6437
Cdd:pfam00041    1 SAPSNLTVTDVTSTSLTVSWTPPPDGNG-PITGYEVEYRPKNSGEPW-NEITVPGTttSVTLTGLKPGTEYEVRVQAVNG 78

                   ....*..
gi 281359561  6438 AGPGHPS 6444
Cdd:pfam00041   79 GGEGPPS 85
FN3 cd00063
Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein ...
7545-7637 2.76e-17

Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein fibronectin. Its tenth fibronectin type III repeat contains an RGD cell recognition sequence in a flexible loop between 2 strands. Approximately 2% of all animal proteins contain the FN3 repeat; including extracellular and intracellular proteins, membrane spanning cytokine receptors, growth hormone receptors, tyrosine phosphatase receptors, and adhesion molecules. FN3-like domains are also found in bacterial glycosyl hydrolases.


Pssm-ID: 238020 [Multi-domain]  Cd Length: 93  Bit Score: 80.62  E-value: 2.76e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 7545 PSPPGSPQITEIGGDFVHLEWEKPESDGGAhIQGYWIDKREVGSNTWQRVNATICAANQINCINLIEGRQYEFRIFAQNV 7624
Cdd:cd00063     1 PSPPTNLRVTDVTSTSVTLSWTPPEDDGGP-ITGYVVEYREKGSGDWKEVEVTPGSETSYTLTGLKPGTEYEFRVRAVNG 79
                          90
                  ....*....|...
gi 281359561 7625 AGLSTESSASQAV 7637
Cdd:cd00063    80 GGESPPSESVTVT 92
FN3 cd00063
Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein ...
2399-2493 2.96e-17

Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein fibronectin. Its tenth fibronectin type III repeat contains an RGD cell recognition sequence in a flexible loop between 2 strands. Approximately 2% of all animal proteins contain the FN3 repeat; including extracellular and intracellular proteins, membrane spanning cytokine receptors, growth hormone receptors, tyrosine phosphatase receptors, and adhesion molecules. FN3-like domains are also found in bacterial glycosyl hydrolases.


Pssm-ID: 238020 [Multi-domain]  Cd Length: 93  Bit Score: 80.62  E-value: 2.96e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 2399 PLPPGGPfEPEEIRASHIKMKWKRPDDDGGcEISGYALERMDEETGRWIPAGEVGPNETSFDFKGLTPNKKYKFRVKAIN 2478
Cdd:cd00063     1 PSPPTNL-RVTDVTSTSVTLSWTPPEDDGG-PITGYVVEYREKGSGDWKEVEVTPGSETSYTLTGLKPGTEYEFRVRAVN 78
                          90
                  ....*....|....*
gi 281359561 2479 KEGESEPLETFDAIV 2493
Cdd:cd00063    79 GGGESPPSESVTVTT 93
STKc_MAPK4_6 cd07854
Catalytic domain of the Serine/Threonine Kinases, Mitogen-Activated Protein Kinases 4 (also ...
7988-8244 3.06e-17

Catalytic domain of the Serine/Threonine Kinases, Mitogen-Activated Protein Kinases 4 (also called ERK4) and 6 (also called ERK3); STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MAPK4 (also called ERK4 or p63MAPK) and MAPK6 (also called ERK3 or p97MAPK) are atypical MAPKs that are not regulated by MAPK kinases. MAPK6 is expressed ubiquitously with highest amounts in brain and skeletal muscle. It may be involved in the control of cell differentiation by negatively regulating cell cycle progression in certain conditions. It may also play a role in glucose-induced insulin secretion. MAPK6 and MAPK4 cooperate to regulate the activity of MAPK-activated protein kinase 5 (MK5), leading to its relocation to the cytoplasm and exclusion from the nucleus. The MAPK6/MK5 and MAPK4/MK5 pathways may play critical roles in embryonic and post-natal development. MAPKs are important mediators of cellular responses to extracellular signals. The MAPK4/6 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 143359 [Multi-domain]  Cd Length: 342  Bit Score: 87.53  E-value: 3.06e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 7988 RYDILEEIGTGAFGVVHRCRERSTGNIFAAKFIPVS--HSVEKDLirREIDIMNQLHHQKLINLHDAF----EDDDEMIL 8061
Cdd:cd07854     6 RYMDLRPLGCGSNGLVFSAVDSDCDKRVAVKKIVLTdpQSVKHAL--REIKIIRRLDHDNIVKVYEVLgpsgSDLTEDVG 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 8062 IL-EFLS---GGELFE---RITAEGYVMTEAEVINYMRQICEGIRHMHEQNIIHLDIKPENIMCQTRSSTnVKLIDFGLA 8134
Cdd:cd07854    84 SLtELNSvyiVQEYMEtdlANVLEQGPLSEEHARLFMYQLLRGLKYIHSANVLHRDLKPANVFINTEDLV-LKIGDFGLA 162
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 8135 TRLDPNEVVK----ITTGTAEFAAPEIVnREPVGfYT---DMWATGVLSYVLLSGLSPFAGDNDVQ----TLKNVKACDW 8203
Cdd:cd07854   163 RIVDPHYSHKgylsEGLVTKWYRSPRLL-LSPNN-YTkaiDMWAAGCIFAEMLTGKPLFAGAHELEqmqlILESVPVVRE 240
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 281359561 8204 DFDVESFKYI----------------------SEEAKDFIRKLLVRNKEKRMTAHECLLHPWL 8244
Cdd:cd07854   241 EDRNELLNVIpsfvrndggeprrplrdllpgvNPEALDFLEQILTFNPMDRLTAEEALMHPYM 303
STKc_MLK4 cd14146
Catalytic domain of the Serine/Threonine Kinase, Mixed Lineage Kinase 4; STKs catalyze the ...
7995-8188 3.19e-17

Catalytic domain of the Serine/Threonine Kinase, Mixed Lineage Kinase 4; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MLK4 is a mitogen-activated protein kinase kinase kinase (MAP3K, MKKK, MAPKKK), which phosphorylates and activates MAPK kinases (MAPKKs or MKKs or MAP2Ks), which in turn phosphorylate and activate MAPKs during signaling cascades that are important in mediating cellular responses to extracellular signals. The specific function of MLK4 is yet to be determined. Mutations in the kinase domain of MLK4 have been detected in colorectal cancers. Mammals have four MLKs, mostly conserved in vertebrates, which contain an SH3 domain, a catalytic kinase domain, a leucine zipper, a proline-rich region, and a CRIB domain that mediates binding to GTP-bound Cdc42 and Rac. MLKs play roles in immunity and inflammation, as well as in cell death, proliferation, and cell cycle regulation.The MLK4 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271048 [Multi-domain]  Cd Length: 268  Bit Score: 85.86  E-value: 3.19e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 7995 IGTGAFGVVHRCRERSTG-NIFAAKFIPVSH-SVEKDLIRREIDIMNQLHHQKLINLHDAFEDDDEMILILEFLSGGELF 8072
Cdd:cd14146     2 IGVGGFGKVYRATWKGQEvAVKAARQDPDEDiKATAESVRQEAKLFSMLRHPNIIKLEGVCLEEPNLCLVMEFARGGTLN 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 8073 ERITAEGYVMTEAE--------VINYMRQICEGIRHMHEQN---IIHLDIKPENIMCQTR------SSTNVKLIDFGLAT 8135
Cdd:cd14146    82 RALAAANAAPGPRRarripphiLVNWAVQIARGMLYLHEEAvvpILHRDLKSSNILLLEKiehddiCNKTLKITDFGLAR 161
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....
gi 281359561 8136 RLdpNEVVKITT-GTAEFAAPEIVNREPVGFYTDMWATGVLSYVLLSGLSPFAG 8188
Cdd:cd14146   162 EW--HRTTKMSAaGTYAWMAPEVIKSSLFSKGSDIWSYGVLLWELLTGEVPYRG 213
FN3 cd00063
Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein ...
2697-2793 3.33e-17

Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein fibronectin. Its tenth fibronectin type III repeat contains an RGD cell recognition sequence in a flexible loop between 2 strands. Approximately 2% of all animal proteins contain the FN3 repeat; including extracellular and intracellular proteins, membrane spanning cytokine receptors, growth hormone receptors, tyrosine phosphatase receptors, and adhesion molecules. FN3-like domains are also found in bacterial glycosyl hydrolases.


Pssm-ID: 238020 [Multi-domain]  Cd Length: 93  Bit Score: 80.23  E-value: 3.33e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 2697 PSSPKGpLAVSDVTASGCKLQWKKPEDDGGvPIKEYVVEKMDTATGKWVRVGRSPGEKepPSFDVTGLSLGSEYMFRVSA 2776
Cdd:cd00063     1 PSPPTN-LRVTDVTSTSVTLSWTPPEDDGG-PITGYVVEYREKGSGDWKEVEVTPGSE--TSYTLTGLKPGTEYEFRVRA 76
                          90
                  ....*....|....*..
gi 281359561 2777 VNEEGESEPLTTLVGVV 2793
Cdd:cd00063    77 VNGGGESPPSESVTVTT 93
FN3 cd00063
Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein ...
6950-7042 3.74e-17

Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein fibronectin. Its tenth fibronectin type III repeat contains an RGD cell recognition sequence in a flexible loop between 2 strands. Approximately 2% of all animal proteins contain the FN3 repeat; including extracellular and intracellular proteins, membrane spanning cytokine receptors, growth hormone receptors, tyrosine phosphatase receptors, and adhesion molecules. FN3-like domains are also found in bacterial glycosyl hydrolases.


Pssm-ID: 238020 [Multi-domain]  Cd Length: 93  Bit Score: 80.23  E-value: 3.74e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 6950 PLPPQGpLNAYDITPDTCTLAWKTPLDDGGsPITNYVVE-KLDNSGSWVKISS-FVRNTHYDVMGLEPHYKYNFRVRAEN 7027
Cdd:cd00063     1 PSPPTN-LRVTDVTSTSVTLSWTPPEDDGG-PITGYVVEyREKGSGDWKEVEVtPGSETSYTLTGLKPGTEYEFRVRAVN 78
                          90
                  ....*....|....*
gi 281359561 7028 QYGLSDPLDIIEPIV 7042
Cdd:cd00063    79 GGGESPPSESVTVTT 93
PTZ00267 PTZ00267
NIMA-related protein kinase; Provisional
7997-8257 3.99e-17

NIMA-related protein kinase; Provisional


Pssm-ID: 140293 [Multi-domain]  Cd Length: 478  Bit Score: 88.92  E-value: 3.99e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 7997 TGAFgVVHRCRERSTGNIfaAKFIPVSHSVEKDLIRREIDIMNQLHHQKLINLHDAFEDDDEMILILEFLSGGELFERIT 8076
Cdd:PTZ00267   81 TAAF-VATRGSDPKEKVV--AKFVMLNDERQAAYARSELHCLAACDHFGIVKHFDDFKSDDKLLLIMEYGSGGDLNKQIK 157
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 8077 ---AEGYVMTEAEVINYMRQICEGIRHMHEQNIIHLDIKPENIMCQtrSSTNVKLIDFGLATRLDPN---EVVKITTGTA 8150
Cdd:PTZ00267  158 qrlKEHLPFQEYEVGLLFYQIVLALDEVHSRKMMHRDLKSANIFLM--PTGIIKLGDFGFSKQYSDSvslDVASSFCGTP 235
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 8151 EFAAPEIVNREPVGFYTDMWATGVLSYVLLSGLSPFAGDNDVQTLKNVKACDWD-FDVEsfkyISEEAKDFIRKLLVRNK 8229
Cdd:PTZ00267  236 YYLAPELWERKRYSKKADMWSLGVILYELLTLHRPFKGPSQREIMQQVLYGKYDpFPCP----VSSGMKALLDPLLSKNP 311
                         250       260
                  ....*....|....*....|....*...
gi 281359561 8230 EKRMTAHEcLLHPWLTGDHSAMKQEINR 8257
Cdd:PTZ00267  312 ALRPTTQQ-LLHTEFLKYVANLFQDIVR 338
IgI_4_hemolin-like cd20978
Fourth immunoglobulin (Ig)-like domain of hemolin, and similar domains; a member of the I-set ...
8632-8721 4.21e-17

Fourth immunoglobulin (Ig)-like domain of hemolin, and similar domains; a member of the I-set of IgSF domains; The members here are composed of the fourth immunoglobulin (Ig)-like domain of hemolin and similar proteins. Hemolin, an insect immunoglobulin superfamily (IgSF) member containing four Ig-like domains, is a lipopolysaccharide-binding immune protein induced during bacterial infection. Hemolin shares significant sequence similarity with the first four Ig-like domains of the transmembrane cell adhesion molecules (CAMs) of the L1 family. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. The fourth Ig-like domain of hemolin is a member of the I-set Ig domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set domains, members of the I-set have a discontinuous A strand but lack a C" strand. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors, the muscle proteins titin, telokin, and twitchin, the neuronal adhesion molecule axonin-1, and the signaling molecule semaphorin 4D that is involved in axonal guidance, immune function and angiogenesis.


Pssm-ID: 409570 [Multi-domain]  Cd Length: 88  Bit Score: 79.74  E-value: 4.21e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 8632 PEFT-KPLHDLTIHDGEQLILTCYVKGDPEPQISWSKNGKSLSSSdilDLRYKNGIATLTINEVFPEDEGVITCTATNSV 8710
Cdd:cd20978     1 PKFIqKPEKNVVVKGGQDVTLPCQVTGVPQPKITWLHNGKPLQGP---MERATVEDGTLTIINVQPEDTGYYGCVATNEI 77
                          90
                  ....*....|.
gi 281359561 8711 GAVETKCKLTI 8721
Cdd:cd20978    78 GDIYTETLLHV 88
STKc_PIM1 cd14100
Catalytic domain of the Serine/Threonine kinase, Proviral Integration Moloney virus (PIM) ...
7989-8244 4.32e-17

Catalytic domain of the Serine/Threonine kinase, Proviral Integration Moloney virus (PIM) kinase 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The PIM gene locus was discovered as a result of the cloning of retroviral intergration sites in murine Moloney leukemia virus, leading to the identification of PIM kinases. They are constitutively active STKs with a broad range of cellular targets and are overexpressed in many haematopoietic malignancies and solid cancers. Vertebrates contain three distinct PIM kinase genes (PIM1-3); each gene may result in mutliple protein isoforms. There are two PIM1 isoforms resulting from alternative translation initiation sites. PIM1 is the founding member of the PIM subfamily. It is involved in regulating cell growth, differentiation, and apoptosis. It promotes cancer development when overexpressed by inhibiting apoptosis, promoting cell proliferation, and promoting genomic instability. The PIM1 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271002 [Multi-domain]  Cd Length: 254  Bit Score: 85.02  E-value: 4.32e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 7989 YDILEEIGTGAFGVVHRCRERSTGNIFAAKfipvshSVEKDLIRR------------EIDIMNQLHH--QKLINLHDAFE 8054
Cdd:cd14100     2 YQVGPLLGSGGFGSVYSGIRVADGAPVAIK------HVEKDRVSEwgelpngtrvpmEIVLLKKVGSgfRGVIRLLDWFE 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 8055 DDDEMILILEFLSG-GELFERITAEGyVMTEAEVINYMRQICEGIRHMHEQNIIHLDIKPENIMCQTRSStNVKLIDFGL 8133
Cdd:cd14100    76 RPDSFVLVLERPEPvQDLFDFITERG-ALPEELARSFFRQVLEAVRHCHNCGVLHRDIKDENILIDLNTG-ELKLIDFGS 153
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 8134 ATRLDpNEVVKITTGTAEFAAPEIVNREPV-GFYTDMWATGVLSYVLLSGLSPFAGDNDVqtlknVKAcdwdfDVESFKY 8212
Cdd:cd14100   154 GALLK-DTVYTDFDGTRVYSPPEWIRFHRYhGRSAAVWSLGILLYDMVCGDIPFEHDEEI-----IRG-----QVFFRQR 222
                         250       260       270
                  ....*....|....*....|....*....|..
gi 281359561 8213 ISEEAKDFIRKLLVRNKEKRMTAHECLLHPWL 8244
Cdd:cd14100   223 VSSECQHLIKWCLALRPSDRPSFEDIQNHPWM 254
PKc_LIMK_like cd14065
Catalytic domain of the LIM domain kinase-like protein kinases; PKs catalyze the transfer of ...
7995-8175 4.46e-17

Catalytic domain of the LIM domain kinase-like protein kinases; PKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine or tyrosine residues on protein substrates. Members of this subfamily include LIMK, Testicular or testis-specific protein kinase (TESK), and similar proteins. LIMKs are characterized as serine/threonine kinases (STKs) while TESKs are dual-specificity protein kinases. Both LIMK and TESK phosphorylate and inactivate cofilin, an actin depolymerizing factor, to induce the reorganization of the actin cytoskeleton. They are implicated in many cellular functions including cell spreading, motility, morphogenesis, meiosis, mitosis, and spermatogenesis. The LIMK-like subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270967 [Multi-domain]  Cd Length: 252  Bit Score: 85.24  E-value: 4.46e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 7995 IGTGAFGVVHRCRERSTGNIFAAKFIpvSHSVEKDLIRREIDIMNQLHHQKLINLHDAFEDDDEMILILEFLSGGELFER 8074
Cdd:cd14065     1 LGKGFFGEVYKVTHRETGKVMVMKEL--KRFDEQRSFLKEVKLMRRLSHPNILRFIGVCVKDNKLNFITEYVNGGTLEEL 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 8075 ITAEGYVMTEAEVINYMRQICEGIRHMHEQNIIHLDIKPENimCQTRSST---NVKLIDFGLATRL------DPNEVVKI 8145
Cdd:cd14065    79 LKSMDEQLPWSQRVSLAKDIASGMAYLHSKNIIHRDLNSKN--CLVREANrgrNAVVADFGLAREMpdektkKPDRKKRL 156
                         170       180       190
                  ....*....|....*....|....*....|.
gi 281359561 8146 TT-GTAEFAAPEIVNREPVGFYTDMWATGVL 8175
Cdd:cd14065   157 TVvGSPYWMAPEMLRGESYDEKVDVFSFGIV 187
PTZ00266 PTZ00266
NIMA-related protein kinase; Provisional
7983-8239 4.95e-17

NIMA-related protein kinase; Provisional


Pssm-ID: 173502 [Multi-domain]  Cd Length: 1021  Bit Score: 90.18  E-value: 4.95e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 7983 QSVYDRYDILEEIGTGAFGVVHRCRERSTGNIFAAKFIPVS--HSVEKDLIRREIDIMNQLHHQKLINLHDAF--EDDDE 8058
Cdd:PTZ00266    9 ESRLNEYEVIKKIGNGRFGEVFLVKHKRTQEFFCWKAISYRglKEREKSQLVIEVNVMRELKHKNIVRYIDRFlnKANQK 88
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 8059 MILILEFLSGGELFERITaEGYVM----TEAEVINYMRQICEGIRHMHE-------QNIIHLDIKPENIMCQT------- 8120
Cdd:PTZ00266   89 LYILMEFCDAGDLSRNIQ-KCYKMfgkiEEHAIVDITRQLLHALAYCHNlkdgpngERVLHRDLKPQNIFLSTgirhigk 167
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 8121 --RSSTNV------KLIDFGLATRLDPNEVVKITTGTAEFAAPEIVNREPVGF--YTDMWATGVLSYVLLSGLSPFAGDN 8190
Cdd:PTZ00266  168 itAQANNLngrpiaKIGDFGLSKNIGIESMAHSCVGTPYYWSPELLLHETKSYddKSDMWALGCIIYELCSGKTPFHKAN 247
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*....
gi 281359561 8191 DVQTLKNVKACDWDFDVesfKYISEEAKDFIRKLLVRNKEKRMTAHECL 8239
Cdd:PTZ00266  248 NFSQLISELKRGPDLPI---KGKSKELNILIKNLLNLSAKERPSALQCL 293
FN3 cd00063
Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein ...
4185-4271 5.79e-17

Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein fibronectin. Its tenth fibronectin type III repeat contains an RGD cell recognition sequence in a flexible loop between 2 strands. Approximately 2% of all animal proteins contain the FN3 repeat; including extracellular and intracellular proteins, membrane spanning cytokine receptors, growth hormone receptors, tyrosine phosphatase receptors, and adhesion molecules. FN3-like domains are also found in bacterial glycosyl hydrolases.


Pssm-ID: 238020 [Multi-domain]  Cd Length: 93  Bit Score: 79.85  E-value: 5.79e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 4185 PGPPEGpLRVTDVHKEGCKLKWNAPLDDGGlPIDHYIIEKMDVESGRW--LPSGRFKESFAELNNLEPSHEYKFRVLAVN 4262
Cdd:cd00063     1 PSPPTN-LRVTDVTSTSVTLSWTPPEDDGG-PITGYVVEYREKGSGDWkeVEVTPGSETSYTLTGLKPGTEYEFRVRAVN 78

                  ....*....
gi 281359561 4263 TEGESEPLT 4271
Cdd:cd00063    79 GGGESPPSE 87
STKc_MPK1 cd07857
Catalytic domain of the Serine/Threonine Kinase, Fungal Mitogen-Activated Protein Kinase MPK1; ...
7988-8244 5.93e-17

Catalytic domain of the Serine/Threonine Kinase, Fungal Mitogen-Activated Protein Kinase MPK1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily is composed of the MAPKs MPK1 from Saccharomyces cerevisiae, Pmk1 from Schizosaccharomyces pombe, and similar proteins. MPK1 (also called Slt2) and Pmk1 (also called Spm1) are stress-activated MAPKs that regulate the cell wall integrity pathway, and are therefore important in the maintainance of cell shape, cell wall construction, morphogenesis, and ion homeostasis. MPK1 is activated in response to cell wall stress including heat stimulation, osmotic shock, UV irradiation, and any agents that interfere with cell wall biogenesis such as chitin antagonists, caffeine, or zymolase. MPK1 is regulated by the MAP2Ks Mkk1/2, which are regulated by the MAP3K Bck1. Pmk1 is also activated by multiple stresses including elevated temperatures, hyper- or hypotonic stress, glucose deprivation, exposure to cell-wall damaging compounds, and oxidative stress. It is regulated by the MAP2K Pek1, which is regulated by the MAP3K Mkh1. MAPKs are important mediators of cellular responses to extracellular signals. The MPK1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 173750 [Multi-domain]  Cd Length: 332  Bit Score: 86.30  E-value: 5.93e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 7988 RYDILEEIGTGAFGVVHRCR--ERSTGNIFAAKFIPVSHSVEKDLIR--REIDIMNQLH-HQKLINLHD---AFEDDDEM 8059
Cdd:cd07857     1 RYELIKELGQGAYGIVCSARnaETSEEETVAIKKITNVFSKKILAKRalRELKLLRHFRgHKNITCLYDmdiVFPGNFNE 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 8060 ILILEflsggELFE----RITAEGYVMTEAEVINYMRQICEGIRHMHEQNIIHLDIKPENIMCQtrSSTNVKLIDFGLAT 8135
Cdd:cd07857    81 LYLYE-----ELMEadlhQIIRSGQPLTDAHFQSFIYQILCGLKYIHSANVLHRDLKPGNLLVN--ADCELKICDFGLAR 153
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 8136 RLDPNEVV---KIT--TGTAEFAAPEIV--NREpvgfYT---DMWATGVLSYVLLSGLSPFAGDNDVQTL---------- 8195
Cdd:cd07857   154 GFSENPGEnagFMTeyVATRWYRAPEIMlsFQS----YTkaiDVWSVGCILAELLGRKPVFKGKDYVDQLnqilqvlgtp 229
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 281359561 8196 --------KNVKACDWDFD---------VESFKYISEEAKDFIRKLLVRNKEKRMTAHECLLHPWL 8244
Cdd:cd07857   230 deetlsriGSPKAQNYIRSlpnipkkpfESIFPNANPLALDLLEKLLAFDPTKRISVEEALEHPYL 295
I-set pfam07679
Immunoglobulin I-set domain;
4989-5069 6.38e-17

Immunoglobulin I-set domain;


Pssm-ID: 400151 [Multi-domain]  Cd Length: 90  Bit Score: 79.22  E-value: 6.38e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561  4989 VRIKAGQSFTFDCKVSGEPAPQTKWLLKKKEVYSKDNVKVTNVDYNTKLKVNSATRSDSGIYTVFAENANGEDSADVKVT 5068
Cdd:pfam07679   10 VEVQEGESARFTCTVTGTPDPEVSWFKDGQPLRSSDRFKVTYEGGTYTLTISNVQPDDSGKYTCVATNSAGEAEASAELT 89

                   .
gi 281359561  5069 V 5069
Cdd:pfam07679   90 V 90
STKc_TAK1 cd14058
Catalytic domain of the Serine/Threonine Kinase, Transforming Growth Factor beta Activated ...
7995-8186 6.40e-17

Catalytic domain of the Serine/Threonine Kinase, Transforming Growth Factor beta Activated Kinase-1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. TAK1 is also known as mitogen-activated protein kinase kinase kinase 7 (MAPKKK7 or MAP3K7), TAK, or MEKK7. As a MAPKKK, it is an important mediator of cellular responses to extracellular signals. It regulates both the c-Jun N-terminal kinase and p38 MAPK cascades by activating the MAPK kinases, MKK4 and MKK3/6. In addition, TAK1 plays diverse roles in immunity and development, in different biological contexts, through many signaling pathways including TGFbeta/BMP, Wnt/Fz, and NF-kB. It is also implicated in the activation of the tumor suppressor kinase, LKB1. The TAK1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270960 [Multi-domain]  Cd Length: 253  Bit Score: 84.80  E-value: 6.40e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 7995 IGTGAFGVVHRCRERStgNIFAAKFIPVSHsvEKDLIRREIDIMNQLHHQKLINLHDAFEDDDEMILILEFLSGGELFER 8074
Cdd:cd14058     1 VGRGSFGVVCKARWRN--QIVAVKIIESES--EKKAFEVEVRQLSRVDHPNIIKLYGACSNQKPVCLVMEYAEGGSLYNV 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 8075 ITAEGY--VMTEAEVINYMRQICEGIRHMH---EQNIIHLDIKPENiMCQTRSSTNVKLIDFGLATRLDPNEVVkiTTGT 8149
Cdd:cd14058    77 LHGKEPkpIYTAAHAMSWALQCAKGVAYLHsmkPKALIHRDLKPPN-LLLTNGGTVLKICDFGTACDISTHMTN--NKGS 153
                         170       180       190
                  ....*....|....*....|....*....|....*..
gi 281359561 8150 AEFAAPEIVNREPVGFYTDMWATGVLSYVLLSGLSPF 8186
Cdd:cd14058   154 AAWMAPEVFEGSKYSEKCDVFSWGIILWEVITRRKPF 190
STKc_IRAK4 cd14158
Catalytic domain of the Serine/Threonine kinase, Interleukin-1 Receptor Associated Kinase 4; ...
7995-8210 6.44e-17

Catalytic domain of the Serine/Threonine kinase, Interleukin-1 Receptor Associated Kinase 4; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. IRAKs are involved in Toll-like receptor (TLR) and interleukin-1 (IL-1) signalling pathways, and are thus critical in regulating innate immune responses and inflammation. IRAKs contain an N-terminal Death domain (DD), a proST region (rich in serines, prolines, and threonines), a central kinase domain, and a C-terminal domain; IRAK-4 lacks the C-terminal domain. Vertebrates contain four IRAKs (IRAK-1, -2, -3 (or -M), and -4) that display distinct functions and patterns of expression and subcellular distribution, and can differentially mediate TLR signaling. IRAK4 plays a critical role in NFkB activation by its interaction with MyD88, which acts as a scaffold that enables IRAK4 to phosphorylate and activate IRAK1 and/or IRAK2. It also plays an important role in type I IFN production induced by TLR7/8/9. The IRAK4 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271060 [Multi-domain]  Cd Length: 288  Bit Score: 85.63  E-value: 6.44e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 7995 IGTGAFGVVHRCReRSTGNIFAAKFIPVSHSVEKDLIR---REIDIMNQLHHQKLINLHDAFEDDDEMILILEFLSGGEL 8071
Cdd:cd14158    23 LGEGGFGVVFKGY-INDKNVAVKKLAAMVDISTEDLTKqfeQEIQVMAKCQHENLVELLGYSCDGPQLCLVYTYMPNGSL 101
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 8072 FERITA--EGYVMTEAEVINYMRQICEGIRHMHEQNIIHLDIKPENIMCQtrSSTNVKLIDFGLAtRLDPNEVVKITT-- 8147
Cdd:cd14158   102 LDRLAClnDTPPLSWHMRCKIAQGTANGINYLHENNHIHRDIKSANILLD--ETFVPKISDFGLA-RASEKFSQTIMTer 178
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 281359561 8148 --GTAEFAAPEIVNREpVGFYTDMWATGVLSYVLLSGLSPFAGDNDVQTLKNVKA--CDWDFDVESF 8210
Cdd:cd14158   179 ivGTTAYMAPEALRGE-ITPKSDIFSFGVVLLEIITGLPPVDENRDPQLLLDIKEeiEDEEKTIEDY 244
I-set pfam07679
Immunoglobulin I-set domain;
119-210 6.70e-17

Immunoglobulin I-set domain;


Pssm-ID: 400151 [Multi-domain]  Cd Length: 90  Bit Score: 79.22  E-value: 6.70e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561   119 PTFAKKP--AIRQEedGKRLLFECRVNADPIPAIIWFHNGAAVKESERHKITVDKDVHsyfaTLEILNVTVEDAGKYKVN 196
Cdd:pfam07679    1 PKFTQKPkdVEVQE--GESARFTCTVTGTPDPEVSWFKDGQPLRSSDRFKVTYEGGTY----TLTISNVQPDDSGKYTCV 74
                           90
                   ....*....|....
gi 281359561   197 AKNELGESNATISL 210
Cdd:pfam07679   75 ATNSAGEAEASAEL 88
STKc_GRK3 cd05633
Catalytic domain of the Serine/Threonine Kinase, G protein-coupled Receptor Kinase 3; STKs ...
7987-8236 7.10e-17

Catalytic domain of the Serine/Threonine Kinase, G protein-coupled Receptor Kinase 3; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. GRK3, also called beta-adrenergic receptor kinase 2 (beta-ARK2), is widely expressed in many tissues. It is involved in modulating the cholinergic response of airway smooth muscles, and also plays a role in dopamine receptor regulation. GRK3-deficient mice show a lack of olfactory receptor desensitization and altered regulation of the M2 muscarinic airway. GRK3 promoter polymorphisms may also be associated with bipolar disorder. GRK3 contains an N-terminal RGS homology (RH) domain, a central catalytic domain, and C-terminal pleckstrin homology (PH) domain that mediates PIP2 and G protein betagamma-subunit translocation to the membrane. GRKs phosphorylate and regulate G protein-coupled receptors (GPCRs), the largest superfamily of cell surface receptors which regulate some part of nearly all physiological functions. Phosphorylated GPCRs bind to arrestins, which prevents further G protein signaling despite the presence of activating ligand. The GRK3 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270781 [Multi-domain]  Cd Length: 346  Bit Score: 86.65  E-value: 7.10e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 7987 DRYDILEEIGTGAFGVVHRCRERSTGNIFAAKfipvshSVEKDLIRR---EIDIMNQLHHQKLINLHD---------AFE 8054
Cdd:cd05633     5 NDFSVHRIIGRGGFGEVYGCRKADTGKMYAMK------CLDKKRIKMkqgETLALNERIMLSLVSTGDcpfivcmtyAFH 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 8055 DDDEMILILEFLSGGELFERITAEGyVMTEAEVINYMRQICEGIRHMHEQNIIHLDIKPENIMCQTRSstNVKLIDFGLA 8134
Cdd:cd05633    79 TPDKLCFILDLMNGGDLHYHLSQHG-VFSEKEMRFYATEIILGLEHMHNRFVVYRDLKPANILLDEHG--HVRISDLGLA 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 8135 TRLDPNEvVKITTGTAEFAAPEIVNR-EPVGFYTDMWATGVLSYVLLSGLSPFAgDNDVQTLKNVKACDWDFDVESFKYI 8213
Cdd:cd05633   156 CDFSKKK-PHASVGTHGYMAPEVLQKgTAYDSSADWFSLGCMLFKLLRGHSPFR-QHKTKDKHEIDRMTLTVNVELPDSF 233
                         250       260
                  ....*....|....*....|...
gi 281359561 8214 SEEAKDFIRKLLVRNKEKRMTAH 8236
Cdd:cd05633   234 SPELKSLLEGLLQRDVSKRLGCH 256
FN3 cd00063
Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein ...
6062-6153 7.39e-17

Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein fibronectin. Its tenth fibronectin type III repeat contains an RGD cell recognition sequence in a flexible loop between 2 strands. Approximately 2% of all animal proteins contain the FN3 repeat; including extracellular and intracellular proteins, membrane spanning cytokine receptors, growth hormone receptors, tyrosine phosphatase receptors, and adhesion molecules. FN3-like domains are also found in bacterial glycosyl hydrolases.


Pssm-ID: 238020 [Multi-domain]  Cd Length: 93  Bit Score: 79.46  E-value: 7.39e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 6062 PGAPGKPELTDSDKNHITIKWKQPiSNGGSPIIGYDIERRDVNTGRWIKINGQPVPTAEYQDDRVTSNHQYQYRISAVNA 6141
Cdd:cd00063     1 PSPPTNLRVTDVTSTSVTLSWTPP-EDDGGPITGYVVEYREKGSGDWKEVEVTPGSETSYTLTGLKPGTEYEFRVRAVNG 79
                          90
                  ....*....|..
gi 281359561 6142 AGNGKTSEPSAI 6153
Cdd:cd00063    80 GGESPPSESVTV 91
FN3 COG3401
Fibronectin type 3 domain [General function prediction only];
5347-5561 8.00e-17

Fibronectin type 3 domain [General function prediction only];


Pssm-ID: 442628 [Multi-domain]  Cd Length: 603  Bit Score: 88.91  E-value: 8.00e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 5347 YTLTARNINGTDRHNVKVTILDAPSVPEGP--LRNGDVSKNSIVLRWRPPKDDGgseITHYVVEKMDNEAMRWVPVGDCT 5424
Cdd:COG3401   207 YRVAATDTGGESAPSNEVSVTTPTTPPSAPtgLTATADTPGSVTLSWDPVTESD---ATGYRVYRSNSGDGPFTKVATVT 283
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 5425 DTEIRADNLIENHDYSFRVRAVNKQG-QSQPlttSQPITAKDPYSHPDKPGQPQATDWGKHFVDLEWSTPKrdgGAPISS 5503
Cdd:COG3401   284 TTSYTDTGLTNGTTYYYRVTAVDAAGnESAP---SNVVSVTTDLTPPAAPSGLTATAVGSSSITLSWTASS---DADVTG 357
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 5504 YIIE-KRPKFGQWERAAVVLGDNcKAHVPELTNGGEYEFRVIAVNRGGP-SDPSDPSSTI 5561
Cdd:COG3401   358 YNVYrSTSGGGTYTKIAETVTTT-SYTDTGLTPGTTYYYKVTAVDAAGNeSAPSEEVSAT 416
FN3 cd00063
Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein ...
3594-3682 8.89e-17

Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein fibronectin. Its tenth fibronectin type III repeat contains an RGD cell recognition sequence in a flexible loop between 2 strands. Approximately 2% of all animal proteins contain the FN3 repeat; including extracellular and intracellular proteins, membrane spanning cytokine receptors, growth hormone receptors, tyrosine phosphatase receptors, and adhesion molecules. FN3-like domains are also found in bacterial glycosyl hydrolases.


Pssm-ID: 238020 [Multi-domain]  Cd Length: 93  Bit Score: 79.08  E-value: 8.89e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 3594 PGKPKGpLQVNDITKHSCKLKWEKPDDDGGsPIDYYEIEKLDPHTGQWLPCGK--STEPEAKVIGLHEGKAYKFRVRAVN 3671
Cdd:cd00063     1 PSPPTN-LRVTDVTSTSVTLSWTPPEDDGG-PITGYVVEYREKGSGDWKEVEVtpGSETSYTLTGLKPGTEYEFRVRAVN 78
                          90
                  ....*....|.
gi 281359561 3672 KEGESEDLETE 3682
Cdd:cd00063    79 GGGESPPSESV 89
FN3 smart00060
Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, ...
6950-7032 9.20e-17

Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, fibronectin. The tenth fibronectin type III repeat contains a RGD cell recognition sequence in a flexible loop between 2 strands. Type III modules are present in both extracellular and intracellular proteins.


Pssm-ID: 214495 [Multi-domain]  Cd Length: 83  Bit Score: 78.81  E-value: 9.20e-17
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561   6950 PLPPQGpLNAYDITPDTCTLAWKTPLDDGG-SPITNYVVEKLDNSGSWVKISSFVRNTHYDVMGLEPHYKYNFRVRAENQ 7028
Cdd:smart00060    1 PSPPSN-LRVTDVTSTSVTLSWEPPPDDGItGYIVGYRVEYREEGSEWKEVNVTPSSTSYTLTGLKPGTEYEFRVRAVNG 79

                    ....
gi 281359561   7029 YGLS 7032
Cdd:smart00060   80 AGEG 83
FN3 smart00060
Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, ...
4879-4961 9.29e-17

Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, fibronectin. The tenth fibronectin type III repeat contains a RGD cell recognition sequence in a flexible loop between 2 strands. Type III modules are present in both extracellular and intracellular proteins.


Pssm-ID: 214495 [Multi-domain]  Cd Length: 83  Bit Score: 78.81  E-value: 9.29e-17
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561   4879 PGKPENLKATDWDKDHVDLAWTPPLIDGG-SPISCYIIEKQDKYGKWERaLDVPADQCKATIPDLVEGQTYKFRVSAVNA 4957
Cdd:smart00060    1 PSPPSNLRVTDVTSTSVTLSWEPPPDDGItGYIVGYRVEYREEGSEWKE-VNVTPSSTSYTLTGLKPGTEYEFRVRAVNG 79

                    ....
gi 281359561   4958 AGTG 4961
Cdd:smart00060   80 AGEG 83
Ig_3 pfam13927
Immunoglobulin domain; This family contains immunoglobulin-like domains.
8631-8708 9.99e-17

Immunoglobulin domain; This family contains immunoglobulin-like domains.


Pssm-ID: 464046 [Multi-domain]  Cd Length: 78  Bit Score: 78.38  E-value: 9.99e-17
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 281359561  8631 KPEFTKPLHDLTIHDGEQLILTCYVKGDPEPQISWSKNGKSLSSSDILDLRYKNGIATLTINEVFPEDEGVITCTATN 8708
Cdd:pfam13927    1 KPVITVSPSSVTVREGETVTLTCEATGSPPPTITWYKNGEPISSGSTRSRSLSGSNSTLTISNVTRSDAGTYTCVASN 78
Ig_Titin_like cd05748
Immunoglobulin (Ig)-like domain of titin and similar proteins; The members here are composed ...
3212-3292 1.35e-16

Immunoglobulin (Ig)-like domain of titin and similar proteins; The members here are composed of the immunoglobulin (Ig)-like domain found in titin-like proteins and similar proteins. Titin (also called connectin) is a fibrous sarcomeric protein specifically found in vertebrate striated muscle. Titin is a giant protein; depending on isoform composition, it ranges from 2970 to 3700 kDa, and is of a length that spans half a sarcomere. Titin largely consists of multiple repeats of Ig-like and fibronectin type 3 (FN-III)-like domains. Titin connects the ends of myosin thick filaments to Z disks and extends along the thick filament to the H zone. It appears to function similarly to an elastic band, keeping the myosin filaments centered in the sarcomere during muscle contraction or stretching. Within the sarcomere, titin is also attached to or is associated with myosin binding protein C (MyBP-C). MyBP-C appears to contribute to the generation of passive tension by titin and like titin has repeated Ig-like and FN-III domains. Also included in this group are worm twitchin and insect projectin, thick filament proteins of invertebrate muscle which also have repeated Ig-like and FN-III domains.


Pssm-ID: 409406 [Multi-domain]  Cd Length: 82  Bit Score: 78.02  E-value: 1.35e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 3212 IKVRAGQPVKFDVDVKGEPAPSLTWFLKETELTSTGQVRLENIDYNTKLTLLDTDRKQSGQYKLRAENINGVDEAVVEVI 3291
Cdd:cd05748     2 IVVRAGESLRLDIPIKGRPTPTVTWSKDGQPLKETGRVQIETTASSTSLVIKNAKRSDSGKYTLTLKNSAGEKSATINVK 81

                  .
gi 281359561 3292 I 3292
Cdd:cd05748    82 V 82
FN3 COG3401
Fibronectin type 3 domain [General function prediction only];
4756-5122 1.35e-16

Fibronectin type 3 domain [General function prediction only];


Pssm-ID: 442628 [Multi-domain]  Cd Length: 603  Bit Score: 88.14  E-value: 1.35e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 4756 YLVTATNTSGKDSVLVNVVITDKPSPPNGP--LQISDVHKEGCHLKWkRPSDDGGtpIEYFQIDKLEPETGCWIPSCRST 4833
Cdd:COG3401   207 YRVAATDTGGESAPSNEVSVTTPTTPPSAPtgLTATADTPGSVTLSW-DPVTESD--ATGYRVYRSNSGDGPFTKVATVT 283
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 4834 EPQVDVTGLSPGNEYKFRVSAVNAEG-ESQPLVGDESIVARNPfdePGKPENLKATDWDKDHVDLAWTPPLidgGSPISC 4912
Cdd:COG3401   284 TTSYTDTGLTNGTTYYYRVTAVDAAGnESAPSNVVSVTTDLTP---PAAPSGLTATAVGSSSITLSWTASS---DADVTG 357
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 4913 YIIE-KQDKYGKWERaLDVPADQCKATIPDLVEGQTYKFRVSAVNAAGTGEPSDSTPPIIAKARNKPPIIDRSSlVEVRI 4991
Cdd:COG3401   358 YNVYrSTSGGGTYTK-IAETVTTTSYTDTGLTPGTTYYYKVTAVDAAGNESAPSEEVSATTASAASGESLTASV-DAVPL 435
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 4992 KAGQSFTFDCKVSGEPAPQTKWLLKKKEVYSKDNVKVTNVDYNTKLKVNsaTRSDSGIYTVFAENANGEDSADVKVTVID 5071
Cdd:COG3401   436 TDVAGATAAASAASNPGVSAAVLADGGDTGNAVPFTTTSSTVTATTTDT--TTANLSVTTGSLVGGSGASSVTNSVSVIG 513
                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|.
gi 281359561 5072 KPAPPNGPLKVDEInsESCTLHWNPPDDDGGQPIDNYVVEKLDETTGRWIP 5122
Cdd:COG3401   514 ASAAAAVGGAPDGT--PNVTGASPVTVGASTGDVLITDLVSLTTSASSSVS 562
STKc_MLK cd14061
Catalytic domain of the Serine/Threonine Kinases, Mixed Lineage Kinases; STKs catalyze the ...
7995-8188 1.38e-16

Catalytic domain of the Serine/Threonine Kinases, Mixed Lineage Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MLKs act as mitogen-activated protein kinase kinase kinases (MAP3Ks, MKKKs, MAPKKKs), which phosphorylate and activate MAPK kinases (MAPKKs or MKKs or MAP2Ks), which in turn phosphorylate and activate MAPKs during signaling cascades that are important in mediating cellular responses to extracellular signals. Mammals have four MLKs (MLK1-4), mostly conserved in vertebrates, which contain an SH3 domain, a catalytic kinase domain, a leucine zipper, a proline-rich region, and a CRIB domain that mediates binding to GTP-bound Cdc42 and Rac. MLKs play roles in immunity and inflammation, as well as in cell death, proliferation, and cell cycle regulation. The MLK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270963 [Multi-domain]  Cd Length: 258  Bit Score: 83.60  E-value: 1.38e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 7995 IGTGAFGVVHRCRER-STGNIFAAKFIPVS-HSVEKDLIRREIDIMNQLHHQKLINLHDAFEDDDEMILILEFLSGGELf 8072
Cdd:cd14061     2 IGVGGFGKVYRGIWRgEEVAVKAARQDPDEdISVTLENVRQEARLFWMLRHPNIIALRGVCLQPPNLCLVMEYARGGAL- 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 8073 ERITAeGYVMTEAEVINYMRQICEGIRHMHEQN---IIHLDIKPENIM----CQTRSSTN--VKLIDFGLA------TRL 8137
Cdd:cd14061    81 NRVLA-GRKIPPHVLVDWAIQIARGMNYLHNEApvpIIHRDLKSSNILileaIENEDLENktLKITDFGLArewhktTRM 159
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|.
gi 281359561 8138 DpnevvkiTTGTAEFAAPEIVNREPVGFYTDMWATGVLSYVLLSGLSPFAG 8188
Cdd:cd14061   160 S-------AAGTYAWMAPEVIKSSTFSKASDVWSYGVLLWELLTGEVPYKG 203
IgI_2_Titin_Z1z2-like cd20972
Second Ig-like domain of the giant muscle protein titin Z1z2 in the sarcomeric Z-disk, and ...
8739-8829 1.43e-16

Second Ig-like domain of the giant muscle protein titin Z1z2 in the sarcomeric Z-disk, and similar domains; a member of the I-set of IgSF domains; The members here are composed of the second immunoglobulin (Ig)-like domain of the giant muscle protein titin Z1z2 in the sarcomeric Z-disk and similar proteins. Titin is a key component in the assembly and functioning of vertebrate striated muscles. By providing connections at the level of individual microfilaments, it contributes to the fine balance of forces between the two halves of the sarcomere. The Ig superfamily (IgSF) is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. Unlike the V-set, one of the distinctive features of I-set domains is the lack of a C" strand. The structure of the titin Z1z2 lacks this strand and thus it belongs to the I-set of the IgSF. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors, the hemolymph protein hemolin, the muscle proteins titin, telokin, and twitchin, the neuronal adhesion molecule axonin-1, and the signaling molecule semaphorin 4D that is involved in axonal guidance, immune function and angiogenesis.


Pssm-ID: 409564 [Multi-domain]  Cd Length: 91  Bit Score: 78.39  E-value: 1.43e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 8739 APKIVSHLESRFVRDGDAVNLACRIIGAQHFDVVWLHNNKEIKPSKDFQYTNEANIYRLQIAEIFPEDGGTYTCEAFNDI 8818
Cdd:cd20972     1 PPQFIQKLRSQEVAEGSKVRLECRVTGNPTPVVRWFCEGKELQNSPDIQIHQEGDLHSLIIAEAFEEDTGRYSCLATNSV 80
                          90
                  ....*....|.
gi 281359561 8819 GESFSTCTINV 8829
Cdd:cd20972    81 GSDTTSAEIFV 91
PTKc_Wee1b cd14139
Catalytic domain of the Protein Tyrosine Kinase, Wee1b; PTKs catalyze the transfer of the ...
7992-8191 1.48e-16

Catalytic domain of the Protein Tyrosine Kinase, Wee1b; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. This subfamily is composed of human Wee1b (also called Wee2), Xenopus laevis Wee1a (XeWee1a) and similar vertebrate proteins. XeWee1a accumulates after exiting the metaphase II stage in oocytes and in early mitotic cells. It functions during the first zygotic cell division and not during subsequent divisions. Mammalian Wee2/Wee1b is an oocyte-specific inhibitor of meiosis that functions downstream of cAMP. Wee1 is a cell cycle checkpoint kinase that helps keep the cyclin-dependent kinase CDK1 in an inactive state through phosphorylation of an N-terminal tyr (Y15) residue. During the late G2 phase, CDK1 is activated and mitotic entry is promoted by the removal of this inhibitory phosphorylation by the phosphatase Cdc25. Although Wee1 is functionally a tyr kinase, it is more closely related to serine/threonine kinases (STKs). It contains a catalytic kinase domain sandwiched in between N- and C-terminal regulatory domains. It is regulated by phosphorylation and degradation, and its expression levels are also controlled by circadian clock proteins. The Wee1b subfamily is part of a larger superfamily that includes the catalytic domains of STKs, other PTKs, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271041 [Multi-domain]  Cd Length: 274  Bit Score: 84.21  E-value: 1.48e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 7992 LEEIGTGAFGVVHRCRERSTGNIFAAK--FIPVSHSVEKDLIRREIDIMNQL-HHQKLINLHDAFEDDDEMILILEFLSG 8068
Cdd:cd14139     5 LEKIGVGEFGSVYKCIKRLDGCVYAIKrsMRPFAGSSNEQLALHEVYAHAVLgHHPHVVRYYSAWAEDDHMIIQNEYCNG 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 8069 GELFERIT---AEGYVMTEAEVINYMRQICEGIRHMHEQNIIHLDIKPENI-MCQTR-----------------SSTNV- 8126
Cdd:cd14139    85 GSLQDAISentKSGNHFEEPELKDILLQVSMGLKYIHNSGLVHLDIKPSNIfICHKMqsssgvgeevsneedefLSANVv 164
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 281359561 8127 -KLIDFGLATRLDPNEVVKittGTAEFAAPEIVNREpvgfYT-----DMWATGvLSYVLLSGLSPFAGDND 8191
Cdd:cd14139   165 yKIGDLGHVTSINKPQVEE---GDSRFLANEILQED----YRhlpkaDIFALG-LTVALAAGAEPLPTNGA 227
Ig_Titin_like cd05748
Immunoglobulin (Ig)-like domain of titin and similar proteins; The members here are composed ...
4700-4775 1.62e-16

Immunoglobulin (Ig)-like domain of titin and similar proteins; The members here are composed of the immunoglobulin (Ig)-like domain found in titin-like proteins and similar proteins. Titin (also called connectin) is a fibrous sarcomeric protein specifically found in vertebrate striated muscle. Titin is a giant protein; depending on isoform composition, it ranges from 2970 to 3700 kDa, and is of a length that spans half a sarcomere. Titin largely consists of multiple repeats of Ig-like and fibronectin type 3 (FN-III)-like domains. Titin connects the ends of myosin thick filaments to Z disks and extends along the thick filament to the H zone. It appears to function similarly to an elastic band, keeping the myosin filaments centered in the sarcomere during muscle contraction or stretching. Within the sarcomere, titin is also attached to or is associated with myosin binding protein C (MyBP-C). MyBP-C appears to contribute to the generation of passive tension by titin and like titin has repeated Ig-like and FN-III domains. Also included in this group are worm twitchin and insect projectin, thick filament proteins of invertebrate muscle which also have repeated Ig-like and FN-III domains.


Pssm-ID: 409406 [Multi-domain]  Cd Length: 82  Bit Score: 78.02  E-value: 1.62e-16
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 281359561 4700 GTALKLDANITGEPAPKVEWKLSNYHLQSGKNVTIETPDYYTKLVIRPTQRSDSGEYLVTATNTSGKDSVLVNVVI 4775
Cdd:cd05748     7 GESLRLDIPIKGRPTPTVTWSKDGQPLKETGRVQIETTASSTSLVIKNAKRSDSGKYTLTLKNSAGEKSATINVKV 82
STKc_MLK1 cd14145
Catalytic domain of the Serine/Threonine Kinase, Mixed Lineage Kinase 1; STKs catalyze the ...
7991-8188 2.05e-16

Catalytic domain of the Serine/Threonine Kinase, Mixed Lineage Kinase 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MLK1 is a mitogen-activated protein kinase kinase kinase (MAP3K, MKKK, MAPKKK) and is also called MAP3K9. MAP3Ks phosphorylate and activate MAPK kinases (MAPKKs or MKKs or MAP2Ks), which in turn phosphorylate and activate MAPKs during signaling cascades that are important in mediating cellular responses to extracellular signals. Little is known about the specific function of MLK1. It is capable of activating the c-Jun N-terminal kinase pathway. Mice lacking both MLK1 and MLK2 are viable, fertile, and have normal life spans. There could be redundancy in the function of MLKs. Mammals have four MLKs, mostly conserved in vertebrates, which contain an SH3 domain, a catalytic kinase domain, a leucine zipper, a proline-rich region, and a CRIB domain that mediates binding to GTP-bound Cdc42 and Rac. MLKs play roles in immunity and inflammation, as well as in cell death, proliferation, and cell cycle regulation. The MLK1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271047 [Multi-domain]  Cd Length: 270  Bit Score: 83.55  E-value: 2.05e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 7991 ILEE-IGTGAFGVVHRC-RERSTGNIFAAKFIP---VSHSVEKdlIRREIDIMNQLHHQKLINLHDAFEDDDEMILILEF 8065
Cdd:cd14145     9 VLEEiIGIGGFGKVYRAiWIGDEVAVKAARHDPdedISQTIEN--VRQEAKLFAMLKHPNIIALRGVCLKEPNLCLVMEF 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 8066 LSGGELfERITAeGYVMTEAEVINYMRQICEGIRHMHEQNI---IHLDIKPENIMCQTR------SSTNVKLIDFGLATR 8136
Cdd:cd14145    87 ARGGPL-NRVLS-GKRIPPDILVNWAVQIARGMNYLHCEAIvpvIHRDLKSSNILILEKvengdlSNKILKITDFGLARE 164
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 281359561 8137 LdpNEVVKITT-GTAEFAAPEIVNREPVGFYTDMWATGVLSYVLLSGLSPFAG 8188
Cdd:cd14145   165 W--HRTTKMSAaGTYAWMAPEVIRSSMFSKGSDVWSYGVLLWELLTGEVPFRG 215
FN3 cd00063
Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein ...
5958-6049 2.05e-16

Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein fibronectin. Its tenth fibronectin type III repeat contains an RGD cell recognition sequence in a flexible loop between 2 strands. Approximately 2% of all animal proteins contain the FN3 repeat; including extracellular and intracellular proteins, membrane spanning cytokine receptors, growth hormone receptors, tyrosine phosphatase receptors, and adhesion molecules. FN3-like domains are also found in bacterial glycosyl hydrolases.


Pssm-ID: 238020 [Multi-domain]  Cd Length: 93  Bit Score: 77.92  E-value: 2.05e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 5958 PGPPEGPmEYEEITANSVTISWKPPKDNGGsEISSYVIEKRDlTHGGGWVPaVNYVSAKYNHAVVPRLLEGTMYELRVMA 6037
Cdd:cd00063     1 PSPPTNL-RVTDVTSTSVTLSWTPPEDDGG-PITGYVVEYRE-KGSGDWKE-VEVTPGSETSYTLTGLKPGTEYEFRVRA 76
                          90
                  ....*....|..
gi 281359561 6038 ENLQGRSDPLTS 6049
Cdd:cd00063    77 VNGGGESPPSES 88
STKc_MLK3 cd14147
Catalytic domain of the Serine/Threonine Kinase, Mixed Lineage Kinase 3; STKs catalyze the ...
7992-8188 2.13e-16

Catalytic domain of the Serine/Threonine Kinase, Mixed Lineage Kinase 3; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MLK3 is a mitogen-activated protein kinase kinase kinases (MAP3K, MKKK, MAPKKK), which phosphorylates and activates MAPK kinases (MAPKKs or MKKs or MAP2Ks), which in turn phosphorylate and activate MAPKs during signaling cascades that are important in mediating cellular responses to extracellular signals. MLK3 activates multiple MAPK pathways and plays a role in apoptosis, proliferation, migration, and differentiation, depending on the cellular context. It is highly expressed in breast cancer cells and its signaling through c-Jun N-terminal kinase has been implicated in the migration, invasion, and malignancy of cancer cells. MLK3 also functions as a negative regulator of Inhibitor of Nuclear Factor-KappaB Kinase (IKK) and consequently, it also impacts inflammation and immunity. Mammals have four MLKs, mostly conserved in vertebrates, which contain an SH3 domain, a catalytic kinase domain, a leucine zipper, a proline-rich region, and a CRIB domain that mediates binding to GTP-bound Cdc42 and Rac. MLKs play roles in immunity and inflammation, as well as in cell death, proliferation, and cell cycle regulation.The MLK3 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271049 [Multi-domain]  Cd Length: 267  Bit Score: 83.54  E-value: 2.13e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 7992 LEE-IGTGAFGVVHRCRERstGNIFAAKFI---PVSH-SVEKDLIRREIDIMNQLHHQKLINLHDAFEDDDEMILILEFL 8066
Cdd:cd14147     7 LEEvIGIGGFGKVYRGSWR--GELVAVKAArqdPDEDiSVTAESVRQEARLFAMLAHPNIIALKAVCLEEPNLCLVMEYA 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 8067 SGGELfERITAeGYVMTEAEVINYMRQICEGIRHMHEQNI---IHLDIKPENIMC------QTRSSTNVKLIDFGLATRL 8137
Cdd:cd14147    85 AGGPL-SRALA-GRRVPPHVLVNWAVQIARGMHYLHCEALvpvIHRDLKSNNILLlqpienDDMEHKTLKITDFGLAREW 162
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 281359561 8138 dpNEVVKITT-GTAEFAAPEIVNREPVGFYTDMWATGVLSYVLLSGLSPFAG 8188
Cdd:cd14147   163 --HKTTQMSAaGTYAWMAPEVIKASTFSKGSDVWSFGVLLWELLTGEVPYRG 212
FN3 cd00063
Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein ...
2100-2194 2.28e-16

Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein fibronectin. Its tenth fibronectin type III repeat contains an RGD cell recognition sequence in a flexible loop between 2 strands. Approximately 2% of all animal proteins contain the FN3 repeat; including extracellular and intracellular proteins, membrane spanning cytokine receptors, growth hormone receptors, tyrosine phosphatase receptors, and adhesion molecules. FN3-like domains are also found in bacterial glycosyl hydrolases.


Pssm-ID: 238020 [Multi-domain]  Cd Length: 93  Bit Score: 77.92  E-value: 2.28e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 2100 PQPPQDVDITDVYQTSCVVSFNPPSDDGGtPITKYVIERQDLSKKhGWESVAEVLPSEPCLKkIDDLIPKKQYRFRIRAV 2179
Cdd:cd00063     1 PSPPTNLRVTDVTSTSVTLSWTPPEDDGG-PITGYVVEYREKGSG-DWKEVEVTPGSETSYT-LTGLKPGTEYEFRVRAV 77
                          90
                  ....*....|....*
gi 281359561 2180 NAIGQSDPATFKNTI 2194
Cdd:cd00063    78 NGGGESPPSESVTVT 92
FN3 cd00063
Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein ...
7050-7139 2.45e-16

Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein fibronectin. Its tenth fibronectin type III repeat contains an RGD cell recognition sequence in a flexible loop between 2 strands. Approximately 2% of all animal proteins contain the FN3 repeat; including extracellular and intracellular proteins, membrane spanning cytokine receptors, growth hormone receptors, tyrosine phosphatase receptors, and adhesion molecules. FN3-like domains are also found in bacterial glycosyl hydrolases.


Pssm-ID: 238020 [Multi-domain]  Cd Length: 93  Bit Score: 77.92  E-value: 2.45e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 7050 PDEPGQPKVIDWDSGNVTLIWTRPLSDGGsRIQGYQIEYRDILNDSSWNAYDYIIKDTKYQLYNLINGSEYEFRIKAKNA 7129
Cdd:cd00063     1 PSPPTNLRVTDVTSTSVTLSWTPPEDDGG-PITGYVVEYREKGSGDWKEVEVTPGSETSYTLTGLKPGTEYEFRVRAVNG 79
                          90
                  ....*....|
gi 281359561 7130 AGLSKPSSPS 7139
Cdd:cd00063    80 GGESPPSESV 89
STKc_EIF2AK1_HRI cd14049
Catalytic domain of the Serine/Threonine kinase, eukaryotic translation Initiation Factor ...
7989-8235 2.62e-16

Catalytic domain of the Serine/Threonine kinase, eukaryotic translation Initiation Factor 2-Alpha Kinase 2 or Heme-Regulated Inhibitor kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. HRI (or EIF2AK1) contains an N-terminal regulatory heme-binding domain and a C-terminal catalytic kinase domain. It is suppressed under normal conditions by binding of the heme iron, and is activated during heme deficiency. It functions as a critical regulator that ensures balanced synthesis of globins and heme, in order to form stable hemoglobin during erythroid differentiation and maturation. HRI also protects cells and enhances survival under iron-deficient conditions. EIF2AKs phosphorylate the alpha subunit of eIF-2, resulting in the downregulation of protein synthesis. The HRI subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270951 [Multi-domain]  Cd Length: 284  Bit Score: 83.71  E-value: 2.62e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 7989 YDILEEIGTGAFGVVHRCRERSTGNIFAAKFIPVSHSVEKDLIR--REIDIMNQLHHQKLINLHDAF-EDDDEMILILEF 8065
Cdd:cd14049     8 FEEIARLGKGGYGKVYKVRNKLDGQYYAIKKILIKKVTKRDCMKvlREVKVLAGLQHPNIVGYHTAWmEHVQLMLYIQMQ 87
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 8066 LSGGELFERITAE--------------GYVMTEAeVINYMRQICEGIRHMHEQNIIHLDIKPENIMCQTrSSTNVKLIDF 8131
Cdd:cd14049    88 LCELSLWDWIVERnkrpceeefksapyTPVDVDV-TTKILQQLLEGVTYIHSMGIVHRDLKPRNIFLHG-SDIHVRIGDF 165
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 8132 GLATRLDPNEVVKITT-------------GTAEFAAPEIVNREPVGFYTDMWATGVlsyVLLSGLSPFAGDND-VQTLKN 8197
Cdd:cd14049   166 GLACPDILQDGNDSTTmsrlnglthtsgvGTCLYAAPEQLEGSHYDFKSDMYSIGV---ILLELFQPFGTEMErAEVLTQ 242
                         250       260       270
                  ....*....|....*....|....*....|....*...
gi 281359561 8198 VKACDWDfdvESFKYISEEAKDFIRKLLVRNKEKRMTA 8235
Cdd:cd14049   243 LRNGQIP---KSLCKRWPVQAKYIKLLTSTEPSERPSA 277
Ig cd00096
Immunoglobulin domain; The members here are composed of the immunoglobulin (Ig) domain found ...
8649-8716 2.72e-16

Immunoglobulin domain; The members here are composed of the immunoglobulin (Ig) domain found in the Ig superfamily. The Ig superfamily is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. Members of this group are components of immunoglobulin, neuroglia, cell surface glycoproteins, including T-cell receptors, CD2, CD4, CD8, and membrane glycoproteins, including butyrophilin and chondroitin sulfate proteoglycan core protein. A predominant feature of most Ig domains is a disulfide bridge connecting the two beta-sheets with a tryptophan residue packed against the disulfide bond. Ig superfamily (IgSF) domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. Typically, the V-set domains have A, B, E, and D strands in one sheet and A', G, F, C, C' and C" in the other. The structures in C1-set are smaller than those in the V-set; they have one beta sheet that is formed by strands A, B, E, and D and the other by strands G, F, C, and C'. Moreover, a C1-set Ig domain contains a short C' strand (three residues) and lacks A' and C" strand. Unlike other Ig domain sets, C2-set structures do not have a D strand. Like the V-set Ig domains, members of the I-set have a discontinuous A strand, but lack a C" strand.


Pssm-ID: 409353 [Multi-domain]  Cd Length: 70  Bit Score: 76.98  E-value: 2.72e-16
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 281359561 8649 LILTCYVKGDPEPQISWSKNGKSLSSSDILDLRYKNGIATLTINEVFPEDEGVITCTATNSVGAVETK 8716
Cdd:cd00096     1 VTLTCSASGNPPPTITWYKNGKPLPPSSRDSRRSELGNGTLTISNVTLEDSGTYTCVASNSAGGSASA 68
STKc_C-Raf cd14149
Catalytic domain of the Serine/Threonine Kinase, C-Raf (Rapidly Accelerated Fibrosarcoma) ...
7991-8191 3.10e-16

Catalytic domain of the Serine/Threonine Kinase, C-Raf (Rapidly Accelerated Fibrosarcoma) kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. C-Raf, also known as Raf-1 or c-Raf-1, is ubiquitously expressed and was the first Raf identified. It was characterized as the acquired oncogene from an acutely transforming murine sarcoma virus (3611-MSV) and the transforming agent from the avian retrovirus MH2. C-Raf-deficient mice embryos die around midgestation with increased apoptosis of embryonic tissues, especially in the fetal liver. One of the main functions of C-Raf is restricting caspase activation to promote survival in response to specific stimuli such as Fas stimulation, macrophage apoptosis, and erythroid differentiation. C-Raf is a mitogen-activated protein kinase kinase kinase (MAP3K, MKKK, MAPKKK), which phosphorylates and activates MAPK kinases (MAPKKs or MKKs or MAP2Ks), which in turn phosphorylate and activate MAPKs during signaling cascades that are important in mediating cellular responses to extracellular signals. It functions in the linear Ras-Raf-MEK-ERK pathway that regulates many cellular processes including cycle regulation, proliferation, differentiation, survival, and apoptosis. The C-Raf subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271051 [Multi-domain]  Cd Length: 283  Bit Score: 83.16  E-value: 3.10e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 7991 ILEEIGTGAFGVVHRCRERstGNIfAAKFIPVSHSVEKDL--IRREIDIMNQLHHQKLInLHDAFEDDDEMILILEFLSG 8068
Cdd:cd14149    16 LSTRIGSGSFGTVYKGKWH--GDV-AVKILKVVDPTPEQFqaFRNEVAVLRKTRHVNIL-LFMGYMTKDNLAIVTQWCEG 91
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 8069 GELFERITAEGYVMTEAEVINYMRQICEGIRHMHEQNIIHLDIKPENIMCQtrSSTNVKLIDFGLAT---RLDPNEVVKI 8145
Cdd:cd14149    92 SSLYKHLHVQETKFQMFQLIDIARQTAQGMDYLHAKNIIHRDMKSNNIFLH--EGLTVKIGDFGLATvksRWSGSQQVEQ 169
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*....
gi 281359561 8146 TTGTAEFAAPEIV---NREPVGFYTDMWATGVLSYVLLSGLSPFAGDND 8191
Cdd:cd14149   170 PTGSILWMAPEVIrmqDNNPFSFQSDVYSYGIVLYELMTGELPYSHINN 218
FN3 COG3401
Fibronectin type 3 domain [General function prediction only];
2718-3199 3.40e-16

Fibronectin type 3 domain [General function prediction only];


Pssm-ID: 442628 [Multi-domain]  Cd Length: 603  Bit Score: 86.59  E-value: 3.40e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 2718 WKKPEDDGGVPIKEYVVEKMDTATGKWVRVGRSPGEKEPPSFDVTGLSLGSEYMFRVSAVNEEGESEPLTTLVGVVAKDP 2797
Cdd:COG3401   153 ANASGTTASSVAGAGVVVSPDTSATAAVATTSLTVTSTTLVDGGGDIEPGTTYYYRVAATDTGGESAPSNEVSVTTPTTP 232
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 2798 fdePNKPGTPEVTDYDNQSISLKWAAPNNDGgapIQKYIIEKKNKNKTEWEKALEIPGdqLEATVAGLQEYGEYQFRVIA 2877
Cdd:COG3401   233 ---PSAPTGLTATADTPGSVTLSWDPVTESD---ATGYRVYRSNSGDGPFTKVATVTT--TSYTDTGLTNGTTYYYRVTA 304
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 2878 VNKAGL-SPPSDasvpqivkykklkpridrsnlkplliragkpirydvnvrgepapvitwyqndkelkpeelpssseikn 2956
Cdd:COG3401   305 VDAAGNeSAPSN-------------------------------------------------------------------- 316
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 2957 ipyntkisiietvrkhtgiykiiavnehgqdEATVEVNIlAPPSKPRGpLDVKDVTKDSCKLKWKKPEDDGgkpISAYQV 3036
Cdd:COG3401   317 -------------------------------VVSVTTDL-TPPAAPSG-LTATAVGSSSITLSWTASSDAD---VTGYNV 360
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 3037 EKFDKKQGRWVPLGRTsANDTEFDVKGLQEGHEYQFRVKAINEEGE----SDPLDSDDSIIAKNPYDAASKPGTPNIVDY 3112
Cdd:COG3401   361 YRSTSGGGTYTKIAET-VTTTSYTDTGLTPGTTYYYKVTAVDAAGNesapSEEVSATTASAASGESLTASVDAVPLTDVA 439
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 3113 NEHMVKLKWEAPRSDGGAPISGYIIEKKDKFSPIWDEILSTNTSVPEATVEGLVEGNIYQFRVRAVNKAGFSDPSDATEP 3192
Cdd:COG3401   440 GATAAASAASNPGVSAAVLADGGDTGNAVPFTTTSSTVTATTTDTTTANLSVTTGSLVGGSGASSVTNSVSVIGASAAAA 519

                  ....*..
gi 281359561 3193 HLAKPRN 3199
Cdd:COG3401   520 VGGAPDG 526
IG_like smart00410
Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.
8640-8721 3.99e-16

Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.


Pssm-ID: 214653 [Multi-domain]  Cd Length: 85  Bit Score: 77.16  E-value: 3.99e-16
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561   8640 DLTIHDGEQLILTCYVKGDPEPQISWSKNG-KSLSSSDILDLRYKNGIATLTINEVFPEDEGVITCTATNSVGAVETKCK 8718
Cdd:smart00410    3 SVTVKEGESVTLSCEASGSPPPEVTWYKQGgKLLAESGRFSVSRSGSTSTLTISNVTPEDSGTYTCAATNSSGSASSGTT 82

                    ...
gi 281359561   8719 LTI 8721
Cdd:smart00410   83 LTV 85
Ig_Titin_like cd05748
Immunoglobulin (Ig)-like domain of titin and similar proteins; The members here are composed ...
6866-6946 5.32e-16

Immunoglobulin (Ig)-like domain of titin and similar proteins; The members here are composed of the immunoglobulin (Ig)-like domain found in titin-like proteins and similar proteins. Titin (also called connectin) is a fibrous sarcomeric protein specifically found in vertebrate striated muscle. Titin is a giant protein; depending on isoform composition, it ranges from 2970 to 3700 kDa, and is of a length that spans half a sarcomere. Titin largely consists of multiple repeats of Ig-like and fibronectin type 3 (FN-III)-like domains. Titin connects the ends of myosin thick filaments to Z disks and extends along the thick filament to the H zone. It appears to function similarly to an elastic band, keeping the myosin filaments centered in the sarcomere during muscle contraction or stretching. Within the sarcomere, titin is also attached to or is associated with myosin binding protein C (MyBP-C). MyBP-C appears to contribute to the generation of passive tension by titin and like titin has repeated Ig-like and FN-III domains. Also included in this group are worm twitchin and insect projectin, thick filament proteins of invertebrate muscle which also have repeated Ig-like and FN-III domains.


Pssm-ID: 409406 [Multi-domain]  Cd Length: 82  Bit Score: 76.47  E-value: 5.32e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 6866 MTVIAGDEFRITVPYHASPRPTASWSLNGLEVIPGERIKFDSNDYASMYYNKSAKRDETGSYTITLTNNKGSDTASCHVT 6945
Cdd:cd05748     2 IVVRAGESLRLDIPIKGRPTPTVTWSKDGQPLKETGRVQIETTASSTSLVIKNAKRSDSGKYTLTLKNSAGEKSATINVK 81

                  .
gi 281359561 6946 V 6946
Cdd:cd05748    82 V 82
FN3 cd00063
Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein ...
7837-7927 5.43e-16

Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein fibronectin. Its tenth fibronectin type III repeat contains an RGD cell recognition sequence in a flexible loop between 2 strands. Approximately 2% of all animal proteins contain the FN3 repeat; including extracellular and intracellular proteins, membrane spanning cytokine receptors, growth hormone receptors, tyrosine phosphatase receptors, and adhesion molecules. FN3-like domains are also found in bacterial glycosyl hydrolases.


Pssm-ID: 238020 [Multi-domain]  Cd Length: 93  Bit Score: 76.77  E-value: 5.43e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 7837 PDPPRFPLIESIGTESLSLSWKAPVWDGcSDITNYYVERREHPLSSWIRVGNTRF--TSMAVSGLTPGKEYDFRIFADNV 7914
Cdd:cd00063     1 PSPPTNLRVTDVTSTSVTLSWTPPEDDG-GPITGYVVEYREKGSGDWKEVEVTPGseTSYTLTGLKPGTEYEFRVRAVNG 79
                          90
                  ....*....|...
gi 281359561 7915 YGRSDASDTSTLI 7927
Cdd:cd00063    80 GGESPPSESVTVT 92
STKc_LATS2 cd05626
Catalytic domain of the Protein Serine/Threonine Kinase, Large Tumor Suppressor 2; STKs ...
7992-8245 6.96e-16

Catalytic domain of the Protein Serine/Threonine Kinase, Large Tumor Suppressor 2; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. LATS2 is an essential mitotic regulator responsible for coordinating accurate cytokinesis completion and governing the stabilization of other mitotic regulators. It is also critical in the maintenance of proper chromosome number, genomic stability, mitotic fidelity, and the integrity of centrosome duplication. Downregulation of LATS2 is associated with poor prognosis in acute lymphoblastic leukemia and breast cancer. The LATS2 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 173715 [Multi-domain]  Cd Length: 381  Bit Score: 83.91  E-value: 6.96e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 7992 LEEIGTGAFGVVHRCRERSTGNIFAAKFIPvshsvEKDLIRR--------EIDIMNQLHHQKLINLHDAFEDDDEMILIL 8063
Cdd:cd05626     6 IKTLGIGAFGEVCLACKVDTHALYAMKTLR-----KKDVLNRnqvahvkaERDILAEADNEWVVKLYYSFQDKDNLYFVM 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 8064 EFLSGGELFERITAEGyVMTEAEVINYMRQICEGIRHMHEQNIIHLDIKPENIMCQTrsSTNVKLIDFGLAT-------- 8135
Cdd:cd05626    81 DYIPGGDMMSLLIRME-VFPEVLARFYIAELTLAIESVHKMGFIHRDIKPDNILIDL--DGHIKLTDFGLCTgfrwthns 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 8136 ------------RLDPNE----------------------------VVKITTGTAEFAAPEIVNREPVGFYTDMWATGVL 8175
Cdd:cd05626   158 kyyqkgshirqdSMEPSDlwddvsncrcgdrlktleqratkqhqrcLAHSLVGTPNYIAPEVLLRKGYTQLCDWWSVGVI 237
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 281359561 8176 SYVLLSGLSPFAGDNDVQTlkNVKACDWD--FDVESFKYISEEAKDFIRKLLVRNKEK--RMTAHECLLHPWLT 8245
Cdd:cd05626   238 LFEMLVGQPPFLAPTPTET--QLKVINWEntLHIPPQVKLSPEAVDLITKLCCSAEERlgRNGADDIKAHPFFS 309
PTKc_Jak2_rpt2 cd14205
Catalytic (repeat 2) domain of the Protein Tyrosine Kinase, Janus kinase 2; PTKs catalyze the ...
7992-8181 8.67e-16

Catalytic (repeat 2) domain of the Protein Tyrosine Kinase, Janus kinase 2; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Jak2 is widely expressed in many tissues and is essential for the signaling of hormone-like cytokines such as growth hormone, erythropoietin, thrombopoietin, and prolactin, as well as some IFNs and cytokines that signal through the IL-3 and gp130 receptors. Disruption of Jak2 in mice results in an embryonic lethal phenotype with multiple defects including erythropoietic and cardiac abnormalities. It is the only Jak gene that results in a lethal phenotype when disrupted in mice. A mutation in the pseudokinase domain of Jak2, V617F, is present in many myeloproliferative diseases, including almost all patients with polycythemia vera, and 50% of patients with essential thrombocytosis and myelofibrosis. Jak2 is a member of the Janus kinase (Jak) subfamily of proteins, which are cytoplasmic (or nonreceptor) PTKs containing an N-terminal FERM domain, followed by a Src homology 2 (SH2) domain, a pseudokinase domain, and a C-terminal catalytic tyr kinase domain. Jaks are crucial for cytokine receptor signaling. They are activated by autophosphorylation upon cytokine-induced receptor aggregation, and subsequently trigger downstream signaling events such as the phosphorylation of signal transducers and activators of transcription (STATs). The PTKc family is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271107 [Multi-domain]  Cd Length: 284  Bit Score: 81.99  E-value: 8.67e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 7992 LEEIGTGAFGVVHRCR----ERSTGNIFAAKfiPVSHSVEKDL--IRREIDIMNQLHHQKLINLHDAF--EDDDEMILIL 8063
Cdd:cd14205     9 LQQLGKGNFGSVEMCRydplQDNTGEVVAVK--KLQHSTEEHLrdFEREIEILKSLQHDNIVKYKGVCysAGRRNLRLIM 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 8064 EFLSGGELFERITAEGYVMTEAEVINYMRQICEGIRHMHEQNIIHLDIKPENIMCQtrSSTNVKLIDFGLATRLDPNEVV 8143
Cdd:cd14205    87 EYLPYGSLRDYLQKHKERIDHIKLLQYTSQICKGMEYLGTKRYIHRDLATRNILVE--NENRVKIGDFGLTKVLPQDKEY 164
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|..
gi 281359561 8144 KITTGTAE----FAAPEIVNREPVGFYTDMWATGVLSYVLLS 8181
Cdd:cd14205   165 YKVKEPGEspifWYAPESLTESKFSVASDVWSFGVVLYELFT 206
PTKc_Itk cd05112
Catalytic domain of the Protein Tyrosine Kinase, Interleukin-2-inducible T-cell Kinase; PTKs ...
7987-8200 9.06e-16

Catalytic domain of the Protein Tyrosine Kinase, Interleukin-2-inducible T-cell Kinase; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Itk, also known as Tsk or Emt, is a member of the Tec-like subfamily of proteins, which are cytoplasmic (or nonreceptor) PTKs with similarity to Src kinases in that they contain Src homology protein interaction domains (SH3, SH2) N-terminal to the catalytic tyr kinase domain. Unlike Src kinases, most Tec subfamily members except Rlk also contain an N-terminal pleckstrin homology (PH) domain, which binds the products of PI3K and allows membrane recruitment and activation. In addition, Itk contains the Tec homology (TH) domain containing one proline-rich region and a zinc-binding region. Itk is expressed in T-cells and mast cells, and is important in their development and differentiation. Of the three Tec kinases expressed in T-cells, Itk plays the predominant role in T-cell receptor (TCR) signaling. It is activated by phosphorylation upon TCR crosslinking and is involved in the pathway resulting in phospholipase C-gamma1 activation and actin polymerization. It also plays a role in the downstream signaling of the T-cell costimulatory receptor CD28, the T-cell surface receptor CD2, and the chemokine receptor CXCR4. In addition, Itk is crucial for the development of T-helper(Th)2 effector responses. The Itk subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 133243 [Multi-domain]  Cd Length: 256  Bit Score: 81.15  E-value: 9.06e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 7987 DRYDILEEIGTGAFGVVHRCRERSTGNIfAAKFIPVSHSVEKDLIRrEIDIMNQLHHQKLINLHDAFEDDDEMILILEFL 8066
Cdd:cd05112     4 SELTFVQEIGSGQFGLVHLGYWLNKDKV-AIKTIREGAMSEEDFIE-EAEVMMKLSHPKLVQLYGVCLEQAPICLVFEFM 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 8067 SGGELFERITAEGYVMTEAEVINYMRQICEGIRHMHEQNIIHLDIKPENimCQTRSSTNVKLIDFGLaTRLDPNEVVKIT 8146
Cdd:cd05112    82 EHGCLSDYLRTQRGLFSAETLLGMCLDVCEGMAYLEEASVIHRDLAARN--CLVGENQVVKVSDFGM-TRFVLDDQYTSS 158
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 281359561 8147 TGT---AEFAAPEIVNREPVGFYTDMWATGVLSYVLLS-GLSPFAGDNDVQTLKNVKA 8200
Cdd:cd05112   159 TGTkfpVKWSSPEVFSFSRYSSKSDVWSFGVLMWEVFSeGKIPYENRSNSEVVEDINA 216
fn3 pfam00041
Fibronectin type III domain;
2201-2289 1.01e-15

Fibronectin type III domain;


Pssm-ID: 394996 [Multi-domain]  Cd Length: 85  Bit Score: 75.91  E-value: 1.01e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561  2201 DEPGKPKAVDLTDwdkDHADLKWEAPEtDGGDPITAYIVEYKEKFSNDWVSGKEVDGDARTATVDGLKEGQQYEFRVRAV 2280
Cdd:pfam00041    1 SAPSNLTVTDVTS---TSLTVSWTPPP-DGNGPITGYEVEYRPKNSGEPWNEITVPGTTTSVTLTGLKPGTEYEVRVQAV 76

                   ....*....
gi 281359561  2281 NRAGPGEPS 2289
Cdd:pfam00041   77 NGGGEGPPS 85
STKc_p38delta cd07879
Catalytic domain of the Serine/Threonine Kinase, p38delta Mitogen-Activated Protein Kinase ...
7988-8244 1.02e-15

Catalytic domain of the Serine/Threonine Kinase, p38delta Mitogen-Activated Protein Kinase (also called MAPK13); STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. p38delta/MAPK13 is found in skeletal muscle, heart, lung, testis, pancreas, and small intestine. It regulates microtubule function by phosphorylating Tau. It activates the c-jun promoter and plays a role in G2 cell cycle arrest. It also controls the degration of c-Myb, which is associated with myeloid leukemia and poor prognosis in colorectal cancer. p38delta is the main isoform involved in regulating the differentiation and apoptosis of keratinocytes. p38 kinases are MAPKs, serving as important mediators of cellular responses to extracellular signals. They are activated by the MAPK kinases MKK3 and MKK6, which in turn are activated by upstream MAPK kinase kinases including TAK1, ASK1, and MLK3, in response to cellular stresses or inflammatory cytokines. The p38delta subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 143384 [Multi-domain]  Cd Length: 342  Bit Score: 83.03  E-value: 1.02e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 7988 RYDILEEIGTGAFGVVHRCRERSTGNIFAAKFI--PVSHSVEKDLIRREIDIMNQLHHQKLINLHDAF------EDDDEM 8059
Cdd:cd07879    16 RYTSLKQVGSGAYGSVCSAIDKRTGEKVAIKKLsrPFQSEIFAKRAYRELTLLKHMQHENVIGLLDVFtsavsgDEFQDF 95
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 8060 ILILEFLSGGelFERITaeGYVMTEAEVINYMRQICEGIRHMHEQNIIHLDIKPENImcQTRSSTNVKLIDFGLATRLDP 8139
Cdd:cd07879    96 YLVMPYMQTD--LQKIM--GHPLSEDKVQYLVYQMLCGLKYIHSAGIIHRDLKPGNL--AVNEDCELKILDFGLARHADA 169
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 8140 NevvkiTTG---TAEFAAPE-IVNREPVGFYTDMWATGVLSYVLLSGLSPFAG----DNDVQTLKNVKACDWDF-----D 8206
Cdd:cd07879   170 E-----MTGyvvTRWYRAPEvILNWMHYNQTVDIWSVGCIMAEMLTGKTLFKGkdylDQLTQILKVTGVPGPEFvqkleD 244
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 281359561 8207 VESFKYI------------------SEEAKDFIRKLLVRNKEKRMTAHECLLHPWL 8244
Cdd:cd07879   245 KAAKSYIkslpkyprkdfstlfpkaSPQAVDLLEKMLELDVDKRLTATEALEHPYF 300
STKc_GRK2 cd14223
Catalytic domain of the Serine/Threonine Kinase, G protein-coupled Receptor Kinase 2; STKs ...
7995-8233 1.12e-15

Catalytic domain of the Serine/Threonine Kinase, G protein-coupled Receptor Kinase 2; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. GRK2, also called beta-adrenergic receptor kinase (beta-ARK) or beta-ARK1, is important in regulating several cardiac receptor responses. It plays a role in cardiac development and in hypertension. Deletion of GRK2 in mice results in embryonic lethality, caused by hypoplasia of the ventricular myocardium. GRK2 also plays important roles in the liver (as a regulator of portal blood pressure), in immune cells, and in the nervous system. Altered GRK2 expression has been reported in several disorders including major depression, schizophrenia, bipolar disorder, and Parkinsonism. GRK2 contains an N-terminal RGS homology (RH) domain, a central catalytic domain, and C-terminal pleckstrin homology (PH) domain that mediates PIP2 and G protein betagamma-subunit translocation to the membrane. GRKs phosphorylate and regulate G protein-coupled receptors (GPCRs), the largest superfamily of cell surface receptors which regulate some part of nearly all physiological functions. Phosphorylated GPCRs bind to arrestins, which prevents further G protein signaling despite the presence of activating ligand. TheGRK2 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271125 [Multi-domain]  Cd Length: 321  Bit Score: 82.40  E-value: 1.12e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 7995 IGTGAFGVVHRCRERSTGNIFAAKfipvshSVEKDLIRR---EIDIMNQLHHQKLINLHD---------AFEDDDEMILI 8062
Cdd:cd14223     8 IGRGGFGEVYGCRKADTGKMYAMK------CLDKKRIKMkqgETLALNERIMLSLVSTGDcpfivcmsyAFHTPDKLSFI 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 8063 LEFLSGGELFERITAEGyVMTEAEVINYMRQICEGIRHMHEQNIIHLDIKPENIMCQTRSstNVKLIDFGLATRLDPNEv 8142
Cdd:cd14223    82 LDLMNGGDLHYHLSQHG-VFSEAEMRFYAAEIILGLEHMHSRFVVYRDLKPANILLDEFG--HVRISDLGLACDFSKKK- 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 8143 VKITTGTAEFAAPEIVNREpVGFYT--DMWATGVLSYVLLSGLSPFAgDNDVQTLKNVKACDWDFDVESFKYISEEAKDF 8220
Cdd:cd14223   158 PHASVGTHGYMAPEVLQKG-VAYDSsaDWFSLGCMLFKLLRGHSPFR-QHKTKDKHEIDRMTLTMAVELPDSFSPELRSL 235
                         250
                  ....*....|...
gi 281359561 8221 IRKLLVRNKEKRM 8233
Cdd:cd14223   236 LEGLLQRDVNRRL 248
STKc_CdkB_plant cd07837
Catalytic domain of the Serine/Threonine Kinase, Plant B-type Cyclin-Dependent protein Kinase; ...
7987-8243 1.15e-15

Catalytic domain of the Serine/Threonine Kinase, Plant B-type Cyclin-Dependent protein Kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The plant-specific B-type CDKs are expressed from the late S to the M phase of the cell cycle. They are characterized by the cyclin binding motif PPT[A/T]LRE. They play a role in controlling mitosis and integrating developmental pathways, such as stomata and leaf development. CdkB has been shown to associate with both cyclin B, which controls G2/M transition, and cyclin D, which acts as a mediator in linking extracellular signals to the cell cycle. CDKs belong to a large family of STKs that are regulated by their cognate cyclins. Together, they are involved in the control of cell-cycle progression, transcription, and neuronal function. The CdkB subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270830 [Multi-domain]  Cd Length: 294  Bit Score: 81.81  E-value: 1.15e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 7987 DRYDILEEIGTGAFGVVHRCRERSTGNIFAAKFIPVSHSVE--KDLIRREIDIMNQLHHQ----KLINLHDAFEDDDEMI 8060
Cdd:cd07837     1 DAYEKLEKIGEGTYGKVYKARDKNTGKLVALKKTRLEMEEEgvPSTALREVSLLQMLSQSiyivRLLDVEHVEENGKPLL 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 8061 -LILEFLSGgELFERITAEG----YVMTEAEVINYMRQICEGIRHMHEQNIIHLDIKPENIMCQtRSSTNVKLIDFGLAT 8135
Cdd:cd07837    81 yLVFEYLDT-DLKKFIDSYGrgphNPLPAKTIQSFMYQLCKGVAHCHSHGVMHRDLKPQNLLVD-KQKGLLKIADLGLGR 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 8136 RLdpneVVKITTGTAE-----FAAPEIV-----NREPVgfytDMWATGVLSYVLLSGLSPFAGDNDVQTLKNV------- 8198
Cdd:cd07837   159 AF----TIPIKSYTHEivtlwYRAPEVLlgsthYSTPV----DMWSVGCIFAEMSRKQPLFPGDSELQQLLHIfrllgtp 230
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 281359561 8199 ---------KACDWDF-------DVES-FKYISEEAKDFIRKLLVRNKEKRMTAHECLLHPW 8243
Cdd:cd07837   231 neevwpgvsKLRDWHEypqwkpqDLSRaVPDLEPEGVDLLTKMLAYDPAKRISAKAALQHPY 292
I-set pfam07679
Immunoglobulin I-set domain;
3795-3885 1.17e-15

Immunoglobulin I-set domain;


Pssm-ID: 400151 [Multi-domain]  Cd Length: 90  Bit Score: 75.76  E-value: 1.17e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561  3795 PHIDRKnLQKKIMRSGQMLHIDALIKAEPPAKVTWTYNKTEIKTSDHIKIENEDYKTTFIMPKVKRADRGIYIVTAKNDS 3874
Cdd:pfam07679    1 PKFTQK-PKDVEVQEGESARFTCTVTGTPDPEVSWFKDGQPLRSSDRFKVTYEGGTYTLTISNVQPDDSGKYTCVATNSA 79
                           90
                   ....*....|.
gi 281359561  3875 GSDTVEVELEV 3885
Cdd:pfam07679   80 GEAEASAELTV 90
STKc_MLTK cd14060
Catalytic domain of the Serine/Threonine Kinase, Mixed lineage kinase-Like mitogen-activated ...
8006-8188 1.46e-15

Catalytic domain of the Serine/Threonine Kinase, Mixed lineage kinase-Like mitogen-activated protein Triple Kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MLTK, also called zipper sterile-alpha-motif kinase (ZAK), contains a catalytic kinase domain and a leucine zipper. There are two alternatively-spliced variants, MLTK-alpha and MLTK-beta. MLTK-alpha contains a sterile-alpha-motif (SAM) at the C-terminus. MLTK regulates the c-Jun N-terminal kinase, extracellular signal-regulated kinase, p38 MAPK, and NF-kB pathways. ZAK is the MAP3K involved in the signaling cascade that leads to the ribotoxic stress response initiated by cellular damage due to Shiga toxins and ricin. It may also play a role in cell transformation and cancer development. MAP3Ks (MKKKs or MAPKKKs) phosphorylate and activate MAPK kinases (MAPKKs or MKKs or MAP2Ks), which in turn phosphorylate and activate MAPKs during signaling cascades that are important in mediating cellular responses to extracellular signals.The MLTK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270962 [Multi-domain]  Cd Length: 242  Bit Score: 80.39  E-value: 1.46e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 8006 CRERSTGNIFAAKFIPVSHSVE-KDL--IRREIDIMNQLHHQKLINLHDAFEDDDEMILILEFLSGGELFERI-TAEGYV 8081
Cdd:cd14060     1 CGGGSFGSVYRAIWVSQDKEVAvKKLlkIEKEAEILSVLSHRNIIQFYGAILEAPNYGIVTEYASYGSLFDYLnSNESEE 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 8082 MTEAEVINYMRQICEGIRHMHEQ---NIIHLDIKPENIMCQtrSSTNVKLIDFGlATRLDPNEVVKITTGTAEFAAPEIV 8158
Cdd:cd14060    81 MDMDQIMTWATDIAKGMHYLHMEapvKVIHRDLKSRNVVIA--ADGVLKICDFG-ASRFHSHTTHMSLVGTFPWMAPEVI 157
                         170       180       190
                  ....*....|....*....|....*....|
gi 281359561 8159 NREPVGFYTDMWATGVLSYVLLSGLSPFAG 8188
Cdd:cd14060   158 QSLPVSETCDTYSYGVVLWEMLTREVPFKG 187
PTKc_Btk_Bmx cd05113
Catalytic domain of the Protein Tyrosine Kinases, Bruton's tyrosine kinase and Bone marrow ...
7987-8198 1.49e-15

Catalytic domain of the Protein Tyrosine Kinases, Bruton's tyrosine kinase and Bone marrow kinase on the X chromosome; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Btk and Bmx (also named Etk) are members of the Tec-like subfamily of proteins, which are cytoplasmic (or nonreceptor) PTKs with similarity to Src kinases in that they contain Src homology protein interaction domains (SH3, SH2) N-terminal to the catalytic tyr kinase domain. Unlike Src kinases, most Tec subfamily members except Rlk also contain an N-terminal pleckstrin homology (PH) domain, which binds the products of PI3K and allows membrane recruitment and activation. In addition, Btk contains the Tec homology (TH) domain with proline-rich and zinc-binding regions. Btk is expressed in B-cells, and a variety of myeloid cells including mast cells, platelets, neutrophils, and dendrictic cells. It interacts with a variety of partners, from cytosolic proteins to nuclear transcription factors, suggesting a diversity of functions. Stimulation of a diverse array of cell surface receptors, including antigen engagement of the B-cell receptor, leads to PH-mediated membrane translocation of Btk and subsequent phosphorylation by Src kinase and activation. Btk plays an important role in the life cycle of B-cells including their development, differentiation, proliferation, survival, and apoptosis. Mutations in Btk cause the primary immunodeficiency disease, X-linked agammaglobulinaemia (XLA) in humans. Bmx is primarily expressed in bone marrow and the arterial endothelium, and plays an important role in ischemia-induced angiogenesis. It facilitates arterial growth, capillary formation, vessel maturation, and bone marrow-derived endothelial progenitor cell mobilization. The Btk/Bmx subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 173657 [Multi-domain]  Cd Length: 256  Bit Score: 80.69  E-value: 1.49e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 7987 DRYDI--LEEIGTGAFGVVHRCRERSTGNIfAAKFIPVSHSVEKDLIRrEIDIMNQLHHQKLINLHDAFEDDDEMILILE 8064
Cdd:cd05113     2 DPKDLtfLKELGTGQFGVVKYGKWRGQYDV-AIKMIKEGSMSEDEFIE-EAKVMMNLSHEKLVQLYGVCTKQRPIFIITE 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 8065 FLSGGELFERITAEGYVMTEAEVINYMRQICEGIRHMHEQNIIHLDIKPENimCQTRSSTNVKLIDFGLATRLDPNEVVK 8144
Cdd:cd05113    80 YMANGCLLNYLREMRKRFQTQQLLEMCKDVCEAMEYLESKQFLHRDLAARN--CLVNDQGVVKVSDFGLSRYVLDDEYTS 157
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 281359561 8145 iTTGT---AEFAAPEIVNREPVGFYTDMWATGVLSYVLLS-GLSPFAGDNDVQTLKNV 8198
Cdd:cd05113   158 -SVGSkfpVRWSPPEVLMYSKFSSKSDVWAFGVLMWEVYSlGKMPYERFTNSETVEHV 214
STKc_CDK8_like cd07842
Catalytic domain of Cyclin-Dependent protein Kinase 8-like Serine/Threonine Kinases; STKs ...
7988-8243 1.50e-15

Catalytic domain of Cyclin-Dependent protein Kinase 8-like Serine/Threonine Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily is composed of CDK8, CDC2L6, and similar proteins. CDK8 functions as a negative or positive regulator of transcription, depending on the scenario. Together with its regulator, cyclin C, it reversibly associates with the multi-subunit core Mediator complex, a cofactor that is involved in regulating RNA polymerase II-dependent transcription. CDC2L6 also associates with Mediator in complexes lacking CDK8. In VP16-dependent transcriptional activation, CDK8 and CDC2L6 exerts opposing effects by positive and negative regulation, respectively, in similar conditions. CDKs belong to a large family of STKs that are regulated by their cognate cyclins. Together, they are involved in the control of cell-cycle progression, transcription, and neuronal function. The CDK8-like subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270834 [Multi-domain]  Cd Length: 316  Bit Score: 81.95  E-value: 1.50e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 7988 RYDILEEIGTGAFGVVHRCR--ERSTGNIFAAKFIpVSHSVEKDLIR----REIDIMNQLHHQKLINLHDAFEDDDEMIL 8061
Cdd:cd07842     1 KYEIEGCIGRGTYGRVYKAKrkNGKDGKEYAIKKF-KGDKEQYTGISqsacREIALLRELKHENVVSLVEVFLEHADKSV 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 8062 ILEF-LSGGELFERI----TAEGYVMTEAEVINYMRQICEGIRHMHEQNIIHLDIKPENI--MCQTRSSTNVKLIDFGLA 8134
Cdd:cd07842    80 YLLFdYAEHDLWQIIkfhrQAKRVSIPPSMVKSLLWQILNGIHYLHSNWVLHRDLKPANIlvMGEGPERGVVKIGDLGLA 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 8135 tRL---------DPNEVVKittgTAEFAAPEIVnrepVG--FYT---DMWATGVLSYVLLSGLSPFAGDND--------- 8191
Cdd:cd07842   160 -RLfnaplkplaDLDPVVV----TIWYRAPELL----LGarHYTkaiDIWAIGCIFAELLTLEPIFKGREAkikksnpfq 230
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 8192 -------VQTLKNVKACDW-------------------DFD-------VESFKYISEEAKDFIRKLLVRNKEKRMTAHEC 8238
Cdd:cd07842   231 rdqleriFEVLGTPTEKDWpdikkmpeydtlksdtkasTYPnsllakwMHKHKKPDSQGFDLLRKLLEYDPTKRITAEEA 310

                  ....*
gi 281359561 8239 LLHPW 8243
Cdd:cd07842   311 LEHPY 315
STKc_PCTAIRE_like cd07844
Catalytic domain of PCTAIRE-like Serine/Threonine Kinases; STKs catalyze the transfer of the ...
7989-8244 1.59e-15

Catalytic domain of PCTAIRE-like Serine/Threonine Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PCTAIRE-like proteins show unusual expression patterns with high levels in post-mitotic tissues, suggesting that they may be involved in regulating post-mitotic cellular events. They share sequence similarity with Cyclin-Dependent Kinases (CDKs), which belong to a large family of STKs that are regulated by their cognate cyclins. Together, CDKs and cyclins are involved in the control of cell-cycle progression, transcription, and neuronal function. The association of PCTAIRE-like proteins with cyclins has not been widely studied, although PFTAIRE-1 has been shown to function as a CDK which is regulated by cyclin D3 as well as the membrane-associated cyclin Y. The PCTAIRE-like subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270835 [Multi-domain]  Cd Length: 286  Bit Score: 81.27  E-value: 1.59e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 7989 YDILEEIGTGAFGVVHRCRERSTGNIFAAKFIPVSHsvEKDL----IRrEIDIMNQLHHQKLINLHDAFEDDDEMILILE 8064
Cdd:cd07844     2 YKKLDKLGEGSYATVYKGRSKLTGQLVALKEIRLEH--EEGApftaIR-EASLLKDLKHANIVTLHDIIHTKKTLTLVFE 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 8065 FLSGgELFERITAEGYVMTEAEVINYMRQICEGIRHMHEQNIIHLDIKPENIMCQTRSStnVKLIDFGLA------TRLD 8138
Cdd:cd07844    79 YLDT-DLKQYMDDCGGGLSMHNVRLFLFQLLRGLAYCHQRRVLHRDLKPQNLLISERGE--LKLADFGLAraksvpSKTY 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 8139 PNEVVK-------ITTGTAEFAAPeivnrepvgfyTDMWATGVLSYVLLSGLSPFAGDNDV----------------QTL 8195
Cdd:cd07844   156 SNEVVTlwyrppdVLLGSTEYSTS-----------LDMWGVGCIFYEMATGRPLFPGSTDVedqlhkifrvlgtpteETW 224
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 281359561 8196 KNVKACDwDFDVESFK--------------YISEEAKDFIRKLLVRNKEKRMTAHECLLHPWL 8244
Cdd:cd07844   225 PGVSSNP-EFKPYSFPfypprplinhaprlDRIPHGEELALKFLQYEPKKRISAAEAMKHPYF 286
STKc_CDK6 cd07862
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 6; STKs ...
7988-8243 1.78e-15

Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 6; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. CDK6 is regulated by D-type cyclins and INK4 inhibitors. It is active towards the retinoblastoma (pRb) protein, implicating it to function in regulating the early G1 phase of the cell cycle. It is expressed ubiquitously and is localized in the cytoplasm. It is also present in the ruffling edge of spreading fibroblasts and may play a role in cell spreading. It binds to the p21 inhibitor without any effect on its own activity and it is overexpressed in squamous cell carcinomas and neuroblastomas. CDK6 has also been shown to inhibit cell differentiation in many cell types. CDKs belong to a large family of STKs that are regulated by their cognate cyclins. Together, they are involved in the control of cell-cycle progression, transcription, and neuronal function. The CDK6 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270846 [Multi-domain]  Cd Length: 290  Bit Score: 81.23  E-value: 1.78e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 7988 RYDILEEIGTGAFGVVHRCRERSTGNIFAA-KFIPVSHSVEKDLIR--REIDIMNQLH---HQKLINLHDAF---EDDDE 8058
Cdd:cd07862     2 QYECVAEIGEGAYGKVFKARDLKNGGRFVAlKRVRVQTGEEGMPLStiREVAVLRHLEtfeHPNVVRLFDVCtvsRTDRE 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 8059 MILILEFLSGGE----LFERITAEGyVMTEAeVINYMRQICEGIRHMHEQNIIHLDIKPENIMcqTRSSTNVKLIDFGLA 8134
Cdd:cd07862    82 TKLTLVFEHVDQdlttYLDKVPEPG-VPTET-IKDMMFQLLRGLDFLHSHRVVHRDLKPQNIL--VTSSGQIKLADFGLA 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 8135 TRLDPNEVVKITTGTAEFAAPEIVNREPVGFYTDMWATGVLSYVLLSGLSPFAGDNDVQTLKNV-------KACDWDFDV 8207
Cdd:cd07862   158 RIYSFQMALTSVVVTLWYRAPEVLLQSSYATPVDLWSVGCIFAEMFRRKPLFRGSSDVDQLGKIldviglpGEEDWPRDV 237
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|..
gi 281359561 8208 ---------------ESF-KYISEEAKDFIRKLLVRNKEKRMTAHECLLHPW 8243
Cdd:cd07862   238 alprqafhsksaqpiEKFvTDIDELGKDLLLKCLTFNPAKRISAYSALSHPY 289
IgI_Myotilin_C_like cd05744
Immunoglobulin (Ig)-like domain of myotilin, palladin, and myopalladin; member of the I-set of ...
119-211 1.87e-15

Immunoglobulin (Ig)-like domain of myotilin, palladin, and myopalladin; member of the I-set of Ig superfamily (IgSF) domains; The members here are composed of the immunoglobulin (Ig)-like domain in myotilin, palladin, and myopalladin. Myotilin, palladin, and myopalladin function as scaffolds that regulate actin organization. Myotilin and myopalladin are most abundant in skeletal and cardiac muscle; palladin is ubiquitously expressed in the organs of developing vertebrates and plays a key role in cellular morphogenesis. The three family members each interact with specific molecular partners with all three binding to alpha-actinin; In addition, palladin also binds to vasodilator-stimulated phosphoprotein (VASP) and ezrin, myotilin binds to filamin and actin, and myopalladin also binds to nebulin and cardiac ankyrin repeat protein (CARP). This group belongs to the I-set of IgSF domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand, but lack a C" strand.


Pssm-ID: 409405 [Multi-domain]  Cd Length: 91  Bit Score: 75.22  E-value: 1.87e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561  119 PTFAKKPAIRQEEDGKRLLFECRVNADPIPAIIWFHNGAAVKESERHKITVDKD-VHSyfatLEILNVTVEDAGKYKVNA 197
Cdd:cd05744     1 PHFLQAPGDLEVQEGRLCRFDCKVSGLPTPDLFWQLNGKPVRPDSAHKMLVRENgRHS----LIIEPVTKRDAGIYTCIA 76
                          90
                  ....*....|....
gi 281359561  198 KNELGESNATISLN 211
Cdd:cd05744    77 RNRAGENSFNAELV 90
FN3 COG3401
Fibronectin type 3 domain [General function prediction only];
3571-3782 1.99e-15

Fibronectin type 3 domain [General function prediction only];


Pssm-ID: 442628 [Multi-domain]  Cd Length: 603  Bit Score: 84.28  E-value: 1.99e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 3571 YIIKATNEVGEDEAELEVTVLGK---PGKPKGpLQVNDITKHSCKLKWEKPDDDGgspIDYYEIEKLDPHTGQWLPCGKS 3647
Cdd:COG3401   207 YRVAATDTGGESAPSNEVSVTTPttpPSAPTG-LTATADTPGSVTLSWDPVTESD---ATGYRVYRSNSGDGPFTKVATV 282
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 3648 TEPEAKVIGLHEGKAYKFRVRAVNKEG-ESEDLETEKPIIAKNPydepdrPGKPEP---TNWDKDFVDLAWDPPKndgGA 3723
Cdd:COG3401   283 TTTSYTDTGLTNGTTYYYRVTAVDAAGnESAPSNVVSVTTDLTP------PAAPSGltaTAVGSSSITLSWTASS---DA 353
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 3724 PIQKYVIQMRDKSGRAWVDSATVPgDKCNGTVTGVEEGHEYEFRIVAVNKAGP-SDPSDV 3782
Cdd:COG3401   354 DVTGYNVYRSTSGGGTYTKIAETV-TTTSYTDTGLTPGTTYYYKVTAVDAAGNeSAPSEE 412
I-set pfam07679
Immunoglobulin I-set domain;
5276-5366 2.12e-15

Immunoglobulin I-set domain;


Pssm-ID: 400151 [Multi-domain]  Cd Length: 90  Bit Score: 74.99  E-value: 2.12e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561  5276 PKIDRnFMSDIKIKAGNVFEFDVPVTGEPLPSKDWTHEGNMIINTDRVKISNFDDRTKIRILDAKRSDTGVYTLTARNIN 5355
Cdd:pfam07679    1 PKFTQ-KPKDVEVQEGESARFTCTVTGTPDPEVSWFKDGQPLRSSDRFKVTYEGGTYTLTISNVQPDDSGKYTCVATNSA 79
                           90
                   ....*....|.
gi 281359561  5356 GTDRHNVKVTI 5366
Cdd:pfam07679   80 GEAEASAELTV 90
STKc_LATS1 cd05625
Catalytic domain of the Serine/Threonine Kinase, Large Tumor Suppressor 1; STKs catalyze the ...
7992-8244 2.21e-15

Catalytic domain of the Serine/Threonine Kinase, Large Tumor Suppressor 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. LATS1 functions as a tumor suppressor and is implicated in cell cycle regulation. Inactivation of LATS1 in mice results in the development of various tumors, including sarcomas and ovarian cancer. Promoter methylation, loss of heterozygosity, and missense mutations targeting the LATS1 gene have also been found in human sarcomas and ovarian cancers. In addition, decreased expression of LATS1 is associated with an aggressive phenotype and poor prognosis. LATS1 induces G2 arrest and promotes cytokinesis. It may be a component of the mitotic exit network in higher eukaryotes. The LATS1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270775 [Multi-domain]  Cd Length: 382  Bit Score: 82.40  E-value: 2.21e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 7992 LEEIGTGAFGVVHRCRERSTGNIFAAKFIPvshsvEKDLIRR--------EIDIMNQLHHQKLINLHDAFEDDDEMILIL 8063
Cdd:cd05625     6 IKTLGIGAFGEVCLARKVDTKALYATKTLR-----KKDVLLRnqvahvkaERDILAEADNEWVVRLYYSFQDKDNLYFVM 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 8064 EFLSGGELFERITAEGyVMTEAEVINYMRQICEGIRHMHEQNIIHLDIKPENIMCQtrSSTNVKLIDFGLAT-------- 8135
Cdd:cd05625    81 DYIPGGDMMSLLIRMG-VFPEDLARFYIAELTCAVESVHKMGFIHRDIKPDNILID--RDGHIKLTDFGLCTgfrwthds 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 8136 ------------------------------RLDPNE----------VVKITTGTAEFAAPEIVNREPVGFYTDMWATGVL 8175
Cdd:cd05625   158 kyyqsgdhlrqdsmdfsnewgdpencrcgdRLKPLErraarqhqrcLAHSLVGTPNYIAPEVLLRTGYTQLCDWWSVGVI 237
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 281359561 8176 SYVLLSGLSPFAGDNDVQTLKNVKACDWDFDVESFKYISEEAKDFIRKlLVRNKEKRM---TAHECLLHPWL 8244
Cdd:cd05625   238 LFEMLVGQPPFLAQTPLETQMKVINWQTSLHIPPQAKLSPEASDLIIK-LCRGPEDRLgknGADEIKAHPFF 308
STKc_MLK2 cd14148
Catalytic domain of the Serine/Threonine Kinase, Mixed Lineage Kinase 2; STKs catalyze the ...
7995-8186 2.53e-15

Catalytic domain of the Serine/Threonine Kinase, Mixed Lineage Kinase 2; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MLK2 is a mitogen-activated protein kinase kinase kinase (MAP3K, MKKK, MAPKKK) and is also called MAP3K10. MAP3Ks phosphorylate and activate MAPK kinases (MAPKKs or MKKs or MAP2Ks), which in turn phosphorylate and activate MAPKs during signaling cascades that are important in mediating cellular responses to extracellular signals. MLK2 is abundant in brain, skeletal muscle, and testis. It functions upstream of the MAPK, c-Jun N-terminal kinase. It binds hippocalcin, a calcium-sensor protein that protects neurons against calcium-induced cell death. Both MLK2 and hippocalcin may be associated with the pathogenesis of Parkinson's disease. MLK2 also binds to normal huntingtin (Htt), which is important in neuronal transcription, development, and survival. MLK2 does not bind to the polyglutamine-expanded Htt, which is implicated in the pathogeneis of Huntington's disease, leading to neuronal toxicity. Mammals have four MLKs, mostly conserved in vertebrates, which contain an SH3 domain, a catalytic kinase domain, a leucine zipper, a proline-rich region, and a CRIB domain that mediates binding to GTP-bound Cdc42 and Rac. MLKs play roles in immunity and inflammation, as well as in cell death, proliferation, and cell cycle regulation. The MLK2 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase (PI3K).


Pssm-ID: 271050 [Multi-domain]  Cd Length: 258  Bit Score: 80.03  E-value: 2.53e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 7995 IGTGAFGVVHRCRERstGNIFAAKfiPVSHSVEKDL------IRREIDIMNQLHHQKLINLHDAFEDDDEMILILEFLSG 8068
Cdd:cd14148     2 IGVGGFGKVYKGLWR--GEEVAVK--AARQDPDEDIavtaenVRQEARLFWMLQHPNIIALRGVCLNPPHLCLVMEYARG 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 8069 GELfERITAeGYVMTEAEVINYMRQICEGIRHMHEQN---IIHLDIKPENIMCQTR------SSTNVKLIDFGLATRLdp 8139
Cdd:cd14148    78 GAL-NRALA-GKKVPPHVLVNWAVQIARGMNYLHNEAivpIIHRDLKSSNILILEPienddlSGKTLKITDFGLAREW-- 153
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*...
gi 281359561 8140 NEVVKITT-GTAEFAAPEIVNREPVGFYTDMWATGVLSYVLLSGLSPF 8186
Cdd:cd14148   154 HKTTKMSAaGTYAWMAPEVIRLSLFSKSSDVWSFGVLLWELLTGEVPY 201
FN3 smart00060
Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, ...
6754-6837 2.55e-15

Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, fibronectin. The tenth fibronectin type III repeat contains a RGD cell recognition sequence in a flexible loop between 2 strands. Type III modules are present in both extracellular and intracellular proteins.


Pssm-ID: 214495 [Multi-domain]  Cd Length: 83  Bit Score: 74.57  E-value: 2.55e-15
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561   6754 PNTPGIPHGIDSTEDSITIAWTKPKHDGG-SPITGYIIEKRLlSDDKWTKaVHALCPDLSCKIPNLIENAEYEFRVAAVN 6832
Cdd:smart00060    1 PSPPSNLRVTDVTSTSVTLSWEPPPDDGItGYIVGYRVEYRE-EGSEWKE-VNVTPSSTSYTLTGLKPGTEYEFRVRAVN 78

                    ....*
gi 281359561   6833 AAGQS 6837
Cdd:smart00060   79 GAGEG 83
FN3 smart00060
Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, ...
5073-5157 2.60e-15

Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, fibronectin. The tenth fibronectin type III repeat contains a RGD cell recognition sequence in a flexible loop between 2 strands. Type III modules are present in both extracellular and intracellular proteins.


Pssm-ID: 214495 [Multi-domain]  Cd Length: 83  Bit Score: 74.57  E-value: 2.60e-15
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561   5073 PAPPnGPLKVDEINSESCTLHWNPPDDDGGQ-PIDNYVVEKlDETTGRWIPAgETDGPVTALKVGGLTPGHKYKFRVRAK 5151
Cdd:smart00060    1 PSPP-SNLRVTDVTSTSVTLSWEPPPDDGITgYIVGYRVEY-REEGSEWKEV-NVTPSSTSYTLTGLKPGTEYEFRVRAV 77

                    ....*.
gi 281359561   5152 NRQGTS 5157
Cdd:smart00060   78 NGAGEG 83
FN3 smart00060
Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, ...
2203-2286 2.98e-15

Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, fibronectin. The tenth fibronectin type III repeat contains a RGD cell recognition sequence in a flexible loop between 2 strands. Type III modules are present in both extracellular and intracellular proteins.


Pssm-ID: 214495 [Multi-domain]  Cd Length: 83  Bit Score: 74.57  E-value: 2.98e-15
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561   2203 PGKPKAVDLTDWDKDHADLKWEAPETDGGdpiTAYIVEYKEKFSNDWVSGKEV--DGDARTATVDGLKEGQQYEFRVRAV 2280
Cdd:smart00060    1 PSPPSNLRVTDVTSTSVTLSWEPPPDDGI---TGYIVGYRVEYREEGSEWKEVnvTPSSTSYTLTGLKPGTEYEFRVRAV 77

                    ....*.
gi 281359561   2281 NRAGPG 2286
Cdd:smart00060   78 NGAGEG 83
I-set pfam07679
Immunoglobulin I-set domain;
4685-4775 3.05e-15

Immunoglobulin I-set domain;


Pssm-ID: 400151 [Multi-domain]  Cd Length: 90  Bit Score: 74.60  E-value: 3.05e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561  4685 PKIDRRnLRNITLSSGTALKLDANITGEPAPKVEWKLSNYHLQSGKNVTIETPDYYTKLVIRPTQRSDSGEYLVTATNTS 4764
Cdd:pfam07679    1 PKFTQK-PKDVEVQEGESARFTCTVTGTPDPEVSWFKDGQPLRSSDRFKVTYEGGTYTLTISNVQPDDSGKYTCVATNSA 79
                           90
                   ....*....|.
gi 281359561  4765 GKDSVLVNVVI 4775
Cdd:pfam07679   80 GEAEASAELTV 90
fn3 pfam00041
Fibronectin type III domain;
5765-5850 3.29e-15

Fibronectin type III domain;


Pssm-ID: 394996 [Multi-domain]  Cd Length: 85  Bit Score: 74.37  E-value: 3.29e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561  5765 DAPGKPIITDWDRDHIDLQWAVPKsDGGAPISEYIIQKKEKGSPYWTNVRHVPSNKNTTTIPELTEGQEYEFRVIAVNQA 5844
Cdd:pfam00041    1 SAPSNLTVTDVTSTSLTVSWTPPP-DGNGPITGYEVEYRPKNSGEPWNEITVPGTTTSVTLTGLKPGTEYEVRVQAVNGG 79

                   ....*.
gi 281359561  5845 GQSEPS 5850
Cdd:pfam00041   80 GEGPPS 85
I-set pfam07679
Immunoglobulin I-set domain;
3208-3292 3.33e-15

Immunoglobulin I-set domain;


Pssm-ID: 400151 [Multi-domain]  Cd Length: 90  Bit Score: 74.60  E-value: 3.33e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561  3208 KMKPIKVRAGQPVKFDVDVKGEPAPSLTWFLKETELTSTGQVRLENIDYNTKLTLLDTDRKQSGQYKLRAENINGVDEAV 3287
Cdd:pfam07679    6 KPKDVEVQEGESARFTCTVTGTPDPEVSWFKDGQPLRSSDRFKVTYEGGTYTLTISNVQPDDSGKYTCVATNSAGEAEAS 85

                   ....*
gi 281359561  3288 VEVII 3292
Cdd:pfam07679   86 AELTV 90
PKc_CLK3 cd14214
Catalytic domain of the Dual-specificity protein kinase, CDC-like kinase 3; Dual-specificity ...
7987-8244 3.50e-15

Catalytic domain of the Dual-specificity protein kinase, CDC-like kinase 3; Dual-specificity PKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine as well as tyrosine residues on protein substrates. CLK3 is predominantly expressed in mature spermatozoa, and might play a role in the fertilization process. CLKs are involved in the phosphorylation and regulation of serine/arginine-rich (SR) proteins, which play a crucial role in pre-mRNA splicing by directing splice site selection. SR proteins are phosphorylated first by SR protein kinases (SRPKs) at the N-terminus, which leads to its assembly into nuclear speckles where splicing factors are stored. CLKs phosphorylate the C-terminal part of SR proteins, causing the nuclear speckles to dissolve and splicing factors to be recruited at sites of active transcription. Based on a conserved "EHLAMMERILG" signature motif which may be crucial for substrate specificity, CLKs are also referred to as LAMMER kinases. CLKs autophosphorylate at tyrosine residues and phosphorylate their substrates exclusively on serine/threonine residues. The CLK3 subfamily is part of a larger superfamily that includes the catalytic domains of other protein serine/threonine PKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271116 [Multi-domain]  Cd Length: 331  Bit Score: 81.21  E-value: 3.50e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 7987 DRYDILEEIGTGAFGVVHRCRERSTGNIFAAKFIPVSHSVEKDLIRREIDIMNQLHHQKLIN------LHDAFEDDDEMI 8060
Cdd:cd14214    13 ERYEIVGDLGEGTFGKVVECLDHARGKSQVALKIIRNVGKYREAARLEINVLKKIKEKDKENkflcvlMSDWFNFHGHMC 92
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 8061 LILEFLsGGELFERITAEGYVMTEAEVINYMR-QICEGIRHMHEQNIIHLDIKPENIM---------------CQTRS-- 8122
Cdd:cd14214    93 IAFELL-GKNTFEFLKENNFQPYPLPHIRHMAyQLCHALKFLHENQLTHTDLKPENILfvnsefdtlynesksCEEKSvk 171
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 8123 STNVKLIDFGLATrLDpNEVVKITTGTAEFAAPEIVNREPVGFYTDMWATGVLSYVLLSGLSPFAGDNDVQTLKNVK--- 8199
Cdd:cd14214   172 NTSIRVADFGSAT-FD-HEHHTTIVATRHYRPPEVILELGWAQPCDVWSLGCILFEYYRGFTLFQTHENREHLVMMEkil 249
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 8200 --------------------ACDWDFDVESFKYISEEAK-----------------DFIRKLLVRNKEKRMTAHECLLHP 8242
Cdd:cd14214   250 gpipshmihrtrkqkyfykgSLVWDENSSDGRYVSENCKplmsymlgdslehtqlfDLLRRMLEFDPALRITLKEALLHP 329

                  ..
gi 281359561 8243 WL 8244
Cdd:cd14214   330 FF 331
FN3 smart00060
Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, ...
2501-2584 3.59e-15

Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, fibronectin. The tenth fibronectin type III repeat contains a RGD cell recognition sequence in a flexible loop between 2 strands. Type III modules are present in both extracellular and intracellular proteins.


Pssm-ID: 214495 [Multi-domain]  Cd Length: 83  Bit Score: 74.19  E-value: 3.59e-15
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561   2501 PSPPSQPVIDDYDNKSVLLKWKRPPSDGGR-PITHYIVEIKDKfAPSWSEVaKTDDPNPECNVEGLKEKMVYQFRVRAVN 2579
Cdd:smart00060    1 PSPPSNLRVTDVTSTSVTLSWEPPPDDGITgYIVGYRVEYREE-GSEWKEV-NVTPSSTSYTLTGLKPGTEYEFRVRAVN 78

                    ....*
gi 281359561   2580 KAGPS 2584
Cdd:smart00060   79 GAGEG 83
PTKc_Src_like cd05034
Catalytic domain of Src kinase-like Protein Tyrosine Kinases; PTKs catalyze the transfer of ...
7993-8198 3.96e-15

Catalytic domain of Src kinase-like Protein Tyrosine Kinases; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Src subfamily members include Src, Lck, Hck, Blk, Lyn, Fgr, Fyn, Yrk, and Yes. Src (or c-Src) proteins are cytoplasmic (or non-receptor) PTKs which are anchored to the plasma membrane. They contain an N-terminal SH4 domain with a myristoylation site, followed by SH3 and SH2 domains, a tyr kinase domain, and a regulatory C-terminal region containing a conserved tyr. They are activated by autophosphorylation at the tyr kinase domain, but are negatively regulated by phosphorylation at the C-terminal tyr by Csk (C-terminal Src Kinase). Src proteins are involved in signaling pathways that regulate cytokine and growth factor responses, cytoskeleton dynamics, cell proliferation, survival, and differentiation. They were identified as the first proto-oncogene products, and they regulate cell adhesion, invasion, and motility in cancer cells and tumor vasculature, contributing to cancer progression and metastasis. Src kinases are overexpressed in a variety of human cancers, making them attractive targets for therapy. They are also implicated in acute inflammatory responses and osteoclast function. Src, Fyn, Yes, and Yrk are widely expressed, while Blk, Lck, Hck, Fgr, and Lyn show a limited expression pattern. The Src-like subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270630 [Multi-domain]  Cd Length: 248  Bit Score: 79.25  E-value: 3.96e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 7993 EEIGTGAFGVVHRCRERSTGNIfAAKFI-PVSHSVEKDLirREIDIMNQLHHQKLINLHdAFEDDDEMILIL-EFLSGGE 8070
Cdd:cd05034     1 KKLGAGQFGEVWMGVWNGTTKV-AVKTLkPGTMSPEAFL--QEAQIMKKLRHDKLVQLY-AVCSDEEPIYIVtELMSKGS 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 8071 LFERI-TAEGYVMTEAEVINYMRQICEGIRHMHEQNIIHLDIKPENIMCqtrSSTNV-KLIDFGLATRLDPNEV------ 8142
Cdd:cd05034    77 LLDYLrTGEGRALRLPQLIDMAAQIASGMAYLESRNYIHRDLAARNILV---GENNVcKVADFGLARLIEDDEYtarega 153
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 8143 ---VKITtgtaefaAPEIVNREPVGFYTDMWATGVLSYVLLS-GLSPFAGDNDVQTLKNV 8198
Cdd:cd05034   154 kfpIKWT-------APEAALYGRFTIKSDVWSFGILLYEIVTyGRVPYPGMTNREVLEQV 206
STKc_TAO3 cd06633
Catalytic domain of the Serine/Threonine Kinase, Thousand-and-One Amino acids 3; STKs catalyze ...
7957-8296 4.04e-15

Catalytic domain of the Serine/Threonine Kinase, Thousand-and-One Amino acids 3; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. TAO3 is also known as JIK (c-Jun N-terminal kinase inhibitory kinase) or KFC (kinase from chicken). It specifically activates JNK, presumably by phosphorylating and activating MKK4/MKK7. In Saccharomyces cerevisiae, TAO3 is a component of the RAM (regulation of Ace2p activity and cellular morphogenesis) signaling pathway. TAO3 is upregulated in retinal ganglion cells after axotomy, and may play a role in apoptosis. TAO proteins possess mitogen-activated protein kinase (MAPK) kinase kinase activity. MAPK signaling cascades are important in mediating cellular responses to extracellular signals. The TAO3 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270803 [Multi-domain]  Cd Length: 313  Bit Score: 80.47  E-value: 4.04e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 7957 GPVKDYDsyVFDIYSKFVPQPVEISqqsvydrydiLEEIGTGAFGVVHRCRERSTGNIFAAKFIPVS----HSVEKDLIR 8032
Cdd:cd06633     3 GVLKDPE--IADLFYKDDPEEIFVD----------LHEIGHGSFGAVYFATNSHTNEVVAIKKMSYSgkqtNEKWQDIIK 70
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 8033 rEIDIMNQLHHQKLINLHDAFEDDDEMILILEFL--SGGELFEritAEGYVMTEAEVINYMRQICEGIRHMHEQNIIHLD 8110
Cdd:cd06633    71 -EVKFLQQLKHPNTIEYKGCYLKDHTAWLVMEYClgSASDLLE---VHKKPLQEVEIAAITHGALQGLAYLHSHNMIHRD 146
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 8111 IKPENIMCQtrSSTNVKLIDFGLATRLDP-NEVVkittGTAEFAAPEIVNREPVGFY---TDMWATGVLSYVLLSGLSPF 8186
Cdd:cd06633   147 IKAGNILLT--EPGQVKLADFGSASIASPaNSFV----GTPYWMAPEVILAMDEGQYdgkVDIWSLGITCIELAERKPPL 220
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 8187 AGDNDVQTLKNVKACDwDFDVESFKYiSEEAKDFIRKLLVRNKEKRMTAHECLLHPWltgdhsamkqeINRDRYLAYREK 8266
Cdd:cd06633   221 FNMNAMSALYHIAQND-SPTLQSNEW-TDSFRGFVDYCLQKIPQERPSSAELLRHDF-----------VRRERPPRVLID 287
                         330       340       350
                  ....*....|....*....|....*....|
gi 281359561 8267 LRRKYEDFERFLLPIgrlsEYSSLRKLLME 8296
Cdd:cd06633   288 LIQRTKDAVRELDNL----QYRKMKKILFQ 313
PKc_CLK2 cd14215
Catalytic domain of the Dual-specificity protein kinase, CDC-like kinase 2; Dual-specificity ...
7987-8244 4.21e-15

Catalytic domain of the Dual-specificity protein kinase, CDC-like kinase 2; Dual-specificity PKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine as well as tyrosine residues on protein substrates. CLK2 plays a role in hepatic insulin signaling and glucose metabolism. It is induced by the insulin/Akt pathway as part of the hepatic refeeding reponse, and it directly phosphorylates the SR domain of PGC-1alpha, which results in decreased gluconeogenic gene expression and glucose output. CLKs are involved in the phosphorylation and regulation of serine/arginine-rich (SR) proteins, which play a crucial role in pre-mRNA splicing by directing splice site selection. SR proteins are phosphorylated first by SR protein kinases (SRPKs) at the N-terminus, which leads to its assembly into nuclear speckles where splicing factors are stored. CLKs phosphorylate the C-terminal part of SR proteins, causing the nuclear speckles to dissolve and splicing factors to be recruited at sites of active transcription. Based on a conserved "EHLAMMERILG" signature motif which may be crucial for substrate specificity, CLKs are also referred to as LAMMER kinases. CLKs autophosphorylate at tyrosine residues and phosphorylate their substrates exclusively on serine/threonine residues. The CLK2 subfamily is part of a larger superfamily that includes the catalytic domains of other protein serine/threonine PKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271117 [Multi-domain]  Cd Length: 330  Bit Score: 80.83  E-value: 4.21e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 7987 DRYDILEEIGTGAFGVVHRCRE-RSTGNIFAAKFIpvsHSVEK--DLIRREIDIMNQLHHQKLINLH------DAFEDDD 8057
Cdd:cd14215    12 ERYEIVSTLGEGTFGRVVQCIDhRRGGARVALKII---KNVEKykEAARLEINVLEKINEKDPENKNlcvqmfDWFDYHG 88
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 8058 EMILILEFLsGGELFERITAEGYVMTEAEVINYMR-QICEGIRHMHEQNIIHLDIKPENIMC-----------------Q 8119
Cdd:cd14215    89 HMCISFELL-GLSTFDFLKENNYLPYPIHQVRHMAfQVCQAVKFLHDNKLTHTDLKPENILFvnsdyeltynlekkrdeR 167
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 8120 TRSSTNVKLIDFGLATrLDPNEVVKITTgTAEFAAPEIVNREPVGFYTDMWATGVLSYVLLSGLSPFAGDNDVQTLKNVK 8199
Cdd:cd14215   168 SVKSTAIRVVDFGSAT-FDHEHHSTIVS-TRHYRAPEVILELGWSQPCDVWSIGCIIFEYYVGFTLFQTHDNREHLAMME 245
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 8200 AC-----------------------DWDFDVESFKYISEEAK-----------------DFIRKLLVRNKEKRMTAHECL 8239
Cdd:cd14215   246 RIlgpipsrmirktrkqkyfyhgrlDWDENTSAGRYVRENCKplrryltseaeehhqlfDLIESMLEYEPSKRLTLAAAL 325

                  ....*
gi 281359561 8240 LHPWL 8244
Cdd:cd14215   326 KHPFF 330
Ig_Titin_like cd05748
Immunoglobulin (Ig)-like domain of titin and similar proteins; The members here are composed ...
2611-2693 4.28e-15

Immunoglobulin (Ig)-like domain of titin and similar proteins; The members here are composed of the immunoglobulin (Ig)-like domain found in titin-like proteins and similar proteins. Titin (also called connectin) is a fibrous sarcomeric protein specifically found in vertebrate striated muscle. Titin is a giant protein; depending on isoform composition, it ranges from 2970 to 3700 kDa, and is of a length that spans half a sarcomere. Titin largely consists of multiple repeats of Ig-like and fibronectin type 3 (FN-III)-like domains. Titin connects the ends of myosin thick filaments to Z disks and extends along the thick filament to the H zone. It appears to function similarly to an elastic band, keeping the myosin filaments centered in the sarcomere during muscle contraction or stretching. Within the sarcomere, titin is also attached to or is associated with myosin binding protein C (MyBP-C). MyBP-C appears to contribute to the generation of passive tension by titin and like titin has repeated Ig-like and FN-III domains. Also included in this group are worm twitchin and insect projectin, thick filament proteins of invertebrate muscle which also have repeated Ig-like and FN-III domains.


Pssm-ID: 409406 [Multi-domain]  Cd Length: 82  Bit Score: 73.78  E-value: 4.28e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 2611 RVTIKSGRTHKWSVDVLGEPIPELHWSwRDDIPLTNGDRIKIENVDYHTDFSITNVLRKDSGFYTLKAENRNGIDRETVE 2690
Cdd:cd05748     1 TIVVRAGESLRLDIPIKGRPTPTVTWS-KDGQPLKETGRVQIETTASSTSLVIKNAKRSDSGKYTLTLKNSAGEKSATIN 79

                  ...
gi 281359561 2691 LVV 2693
Cdd:cd05748    80 VKV 82
PTKc_Hck cd05073
Catalytic domain of the Protein Tyrosine Kinase, Hematopoietic cell kinase; PTKs catalyze the ...
7993-8199 4.51e-15

Catalytic domain of the Protein Tyrosine Kinase, Hematopoietic cell kinase; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Hck is a member of the Src subfamily of proteins, which are cytoplasmic (or non-receptor) PTKs. Hck is present in myeloid and lymphoid cells that play a role in the development of cancer. It may be important in the oncogenic signaling of the protein Tel-Abl, which induces a chronic myelogenous leukemia (CML)-like disease. Hck also acts as a negative regulator of G-CSF-induced proliferation of granulocytic precursors, suggesting a possible role in the development of acute myeloid leukemia (AML). In addition, Hck is essential in regulating the degranulation of polymorphonuclear leukocytes. Genetic polymorphisms affect the expression level of Hck, which affects PMN mediator release and influences the development of chronic obstructive pulmonary disease (COPD). Src kinases contain an N-terminal SH4 domain with a myristoylation site, followed by SH3 and SH2 domains, a tyr kinase domain, and a regulatory C-terminal region containing a conserved tyr. They are activated by autophosphorylation at the tyr kinase domain, but are negatively regulated by phosphorylation at the C-terminal tyr by Csk (C-terminal Src Kinase). The Hck subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270658 [Multi-domain]  Cd Length: 265  Bit Score: 79.68  E-value: 4.51e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 7993 EEIGTGAFGVVHRCRERSTGNIFAAKFIPVSHSVEKDLirREIDIMNQLHHQKLINLHdAFEDDDEMILILEFLSGGELF 8072
Cdd:cd05073    17 KKLGAGQFGEVWMATYNKHTKVAVKTMKPGSMSVEAFL--AEANVMKTLQHDKLVKLH-AVVTKEPIYIITEFMAKGSLL 93
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 8073 ERITA-EGYVMTEAEVINYMRQICEGIRHMHEQNIIHLDIKPENIMcqTRSSTNVKLIDFGLATRLDPNEVVKITTGT-- 8149
Cdd:cd05073    94 DFLKSdEGSKQPLPKLIDFSAQIAEGMAFIEQRNYIHRDLRAANIL--VSASLVCKIADFGLARVIEDNEYTAREGAKfp 171
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|.
gi 281359561 8150 AEFAAPEIVNREPVGFYTDMWATGV-LSYVLLSGLSPFAGDNDVQTLKNVK 8199
Cdd:cd05073   172 IKWTAPEAINFGSFTIKSDVWSFGIlLMEIVTYGRIPYPGMSNPEVIRALE 222
I-set pfam07679
Immunoglobulin I-set domain;
7254-7334 5.15e-15

Immunoglobulin I-set domain;


Pssm-ID: 400151 [Multi-domain]  Cd Length: 90  Bit Score: 73.83  E-value: 5.15e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561  7254 PDWITRLQDKVAPFGKDYTLQCAASGKPSPTARWLRNGKEIQmNGGRMTCDSKDGVFRLHISNVQTGDDGDYTCEAMNSL 7333
Cdd:pfam07679    1 PKFTQKPKDVEVQEGESARFTCTVTGTPDPEVSWFKDGQPLR-SSDRFKVTYEGGTYTLTISNVQPDDSGKYTCVATNSA 79

                   .
gi 281359561  7334 G 7334
Cdd:pfam07679   80 G 80
STKc_CDK9 cd07865
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 9; STKs ...
7987-8243 5.25e-15

Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 9; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. CDK9, together with a cyclin partner (cyclin T1, T2a, T2b, or K), is the main component of distinct positive transcription elongation factors (P-TEFb), which function as Ser2 C-terminal domain kinases of RNA polymerase II. P-TEFb participates in multiple steps of gene expression including transcription elongation, mRNA synthesis, processing, export, and translation. It also plays a role in mediating cytokine induced transcription networks such as IL6-induced STAT3 signaling. In addition, the CDK9/cyclin T2a complex promotes muscle differentiation and enhances the function of some myogenic regulatory factors. CDKs belong to a large family of STKs that are regulated by their cognate cyclins. Together, they are involved in the control of cell-cycle progression, transcription, and neuronal function. The CDK9 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270848 [Multi-domain]  Cd Length: 310  Bit Score: 80.11  E-value: 5.25e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 7987 DRYDILEEIGTGAFGVVHRCRERSTGNIFAAKFIPVSHSVEKDLIR--REIDIMNQLHHQKLINLHD-------AFEDDD 8057
Cdd:cd07865    12 SKYEKLAKIGQGTFGEVFKARHRKTGQIVALKKVLMENEKEGFPITalREIKILQLLKHENVVNLIEicrtkatPYNRYK 91
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 8058 EMI-LILEF----LSGgeLFERITAEgyvMTEAEVINYMRQICEGIRHMHEQNIIHLDIKPENIMCqTRSSTnVKLIDFG 8132
Cdd:cd07865    92 GSIyLVFEFcehdLAG--LLSNKNVK---FTLSEIKKVMKMLLNGLYYIHRNKILHRDMKAANILI-TKDGV-LKLADFG 164
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 8133 LA------TRLDP----NEVVkittgTAEFAAPEI-VNREPVGFYTDMWATGVLSYVLLSGLSPFAGDNDVQTLK----- 8196
Cdd:cd07865   165 LArafslaKNSQPnrytNRVV-----TLWYRPPELlLGERDYGPPIDMWGAGCIMAEMWTRSPIMQGNTEQHQLTlisql 239
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 8197 ---------------------NVKACDWDFDVESFK-YISE-EAKDFIRKLLVRNKEKRMTAHECLLHPW 8243
Cdd:cd07865   240 cgsitpevwpgvdklelfkkmELPQGQKRKVKERLKpYVKDpYALDLIDKLLVLDPAKRIDADTALNHDF 309
STKc_PRP4 cd14135
Catalytic domain of the Serine/Threonine Kinase, Pre-mRNA-Processing factor 4; STKs catalyze ...
7988-8244 5.36e-15

Catalytic domain of the Serine/Threonine Kinase, Pre-mRNA-Processing factor 4; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PRP4 phosphorylates a number of factors involved in the formation of active spliceosomes, which catalyze pre-mRNA splicing. It phosphorylates PRP6 and PRP31, components of the U4/U6-U5 tri-small nuclear ribonucleoprotein (snRNP), during spliceosomal complex formation. In fission yeast, PRP4 phosphorylates the splicing factor PRP1 (U5-102 kD in mammals). Thus, PRP4 plays a key role in regulating spliceosome assembly and pre-mRNA splicing. It also plays an important role in mitosis by acting as a spindle assembly checkpoint kinase that is required for chromosome alignment and the recruitment of the checkpoint proteins MPS1, MAD1, and MAD2 at kinetochores. The PRP4 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271037 [Multi-domain]  Cd Length: 318  Bit Score: 80.34  E-value: 5.36e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 7988 RYDILEEIGTGAFGVVHRCRERSTGNI-FAAKFIPvSHSVEKDLIRREIDIMNQLH------HQKLINLHDAFEDDDEMI 8060
Cdd:cd14135     1 RYRVYGYLGKGVFSNVVRARDLARGNQeVAIKIIR-NNELMHKAGLKELEILKKLNdadpddKKHCIRLLRHFEHKNHLC 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 8061 LILEFLSGG--ELFERITAEGYVMTEAeVINYMRQICEGIRHMHEQNIIHLDIKPENIMCQTRSSTnVKLIDFGLATRLD 8138
Cdd:cd14135    80 LVFESLSMNlrEVLKKYGKNVGLNIKA-VRSYAQQLFLALKHLKKCNILHADIKPDNILVNEKKNT-LKLCDFGSASDIG 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 8139 PNEVVKITtgTAEF-AAPEIVNREPVGFYTDMWATGVLSYVLLSGLSPFAGDNDVQTLK---------------NVKACD 8202
Cdd:cd14135   158 ENEITPYL--VSRFyRAPEIILGLPYDYPIDMWSVGCTLYELYTGKILFPGKTNNHMLKlmmdlkgkfpkkmlrKGQFKD 235
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 8203 WDFDvESFKYISEEA------------------------------------------KDFIRKLLVRNKEKRMTAHECLL 8240
Cdd:cd14135   236 QHFD-ENLNFIYREVdkvtkkevrrvmsdikptkdlktlligkqrlpdedrkkllqlKDLLDKCLMLDPEKRITPNEALQ 314

                  ....
gi 281359561 8241 HPWL 8244
Cdd:cd14135   315 HPFI 318
FN3 smart00060
Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, ...
2999-3083 5.89e-15

Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, fibronectin. The tenth fibronectin type III repeat contains a RGD cell recognition sequence in a flexible loop between 2 strands. Type III modules are present in both extracellular and intracellular proteins.


Pssm-ID: 214495 [Multi-domain]  Cd Length: 83  Bit Score: 73.80  E-value: 5.89e-15
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561   2999 PSKPRGpLDVKDVTKDSCKLKWKKPEDDGG-KPISAYQVEKfDKKQGRWVPLgRTSANDTEFDVKGLQEGHEYQFRVKAI 3077
Cdd:smart00060    1 PSPPSN-LRVTDVTSTSVTLSWEPPPDDGItGYIVGYRVEY-REEGSEWKEV-NVTPSSTSYTLTGLKPGTEYEFRVRAV 77

                    ....*.
gi 281359561   3078 NEEGES 3083
Cdd:smart00060   78 NGAGEG 83
FN3 smart00060
Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, ...
6654-6736 6.19e-15

Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, fibronectin. The tenth fibronectin type III repeat contains a RGD cell recognition sequence in a flexible loop between 2 strands. Type III modules are present in both extracellular and intracellular proteins.


Pssm-ID: 214495 [Multi-domain]  Cd Length: 83  Bit Score: 73.42  E-value: 6.19e-15
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561   6654 PSPPTRLRADEFSGDSLTLYWNPPNDDGG-SAIQNYIIEKKEArSSTWSKVSSFCTVPFVRIRNLVLNKEYDFRVIAENK 6732
Cdd:smart00060    1 PSPPSNLRVTDVTSTSVTLSWEPPPDDGItGYIVGYRVEYREE-GSEWKEVNVTPSSTSYTLTGLKPGTEYEFRVRAVNG 79

                    ....
gi 281359561   6733 YGQS 6736
Cdd:smart00060   80 AGEG 83
IG_like smart00410
Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.
4989-5069 6.87e-15

Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.


Pssm-ID: 214653 [Multi-domain]  Cd Length: 85  Bit Score: 73.31  E-value: 6.87e-15
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561   4989 VRIKAGQSFTFDCKVSGEPAPQTKWLLKK-KEVYSKDNVKVTNVDYNTKLKVNSATRSDSGIYTVFAENANGEDSADVKV 5067
Cdd:smart00410    4 VTVKEGESVTLSCEASGSPPPEVTWYKQGgKLLAESGRFSVSRSGSTSTLTISNVTPEDSGTYTCAATNSSGSASSGTTL 83

                    ..
gi 281359561   5068 TV 5069
Cdd:smart00410   84 TV 85
Ig_Titin_like cd05748
Immunoglobulin (Ig)-like domain of titin and similar proteins; The members here are composed ...
4989-5069 6.90e-15

Immunoglobulin (Ig)-like domain of titin and similar proteins; The members here are composed of the immunoglobulin (Ig)-like domain found in titin-like proteins and similar proteins. Titin (also called connectin) is a fibrous sarcomeric protein specifically found in vertebrate striated muscle. Titin is a giant protein; depending on isoform composition, it ranges from 2970 to 3700 kDa, and is of a length that spans half a sarcomere. Titin largely consists of multiple repeats of Ig-like and fibronectin type 3 (FN-III)-like domains. Titin connects the ends of myosin thick filaments to Z disks and extends along the thick filament to the H zone. It appears to function similarly to an elastic band, keeping the myosin filaments centered in the sarcomere during muscle contraction or stretching. Within the sarcomere, titin is also attached to or is associated with myosin binding protein C (MyBP-C). MyBP-C appears to contribute to the generation of passive tension by titin and like titin has repeated Ig-like and FN-III domains. Also included in this group are worm twitchin and insect projectin, thick filament proteins of invertebrate muscle which also have repeated Ig-like and FN-III domains.


Pssm-ID: 409406 [Multi-domain]  Cd Length: 82  Bit Score: 73.39  E-value: 6.90e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 4989 VRIKAGQSFTFDCKVSGEPAPQTKWLLKKKEVYSKDNVKVTNVDYNTKLKVNSATRSDSGIYTVFAENANGEDSADVKVT 5068
Cdd:cd05748     2 IVVRAGESLRLDIPIKGRPTPTVTWSKDGQPLKETGRVQIETTASSTSLVIKNAKRSDSGKYTLTLKNSAGEKSATINVK 81

                  .
gi 281359561 5069 V 5069
Cdd:cd05748    82 V 82
FN3 COG3401
Fibronectin type 3 domain [General function prediction only];
2077-2297 7.59e-15

Fibronectin type 3 domain [General function prediction only];


Pssm-ID: 442628 [Multi-domain]  Cd Length: 603  Bit Score: 82.36  E-value: 7.59e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 2077 YQIKISNGQGE--DTKDVQII-CQDVPQPPQDVDITDVYQTSCVVSFNPPSDDGgtpITKYVIERQDlSKKHGWESVAEV 2153
Cdd:COG3401   207 YRVAATDTGGEsaPSNEVSVTtPTTPPSAPTGLTATADTPGSVTLSWDPVTESD---ATGYRVYRSN-SGDGPFTKVATV 282
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 2154 LPSEpclkKID-DLIPKKQYRFRIRAVNAIG-QSDPATFKNTILAKDPwdePGKPKAVDLTDWDKDHADLKWEAPEtdgG 2231
Cdd:COG3401   283 TTTS----YTDtGLTNGTTYYYRVTAVDAAGnESAPSNVVSVTTDLTP---PAAPSGLTATAVGSSSITLSWTASS---D 352
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 281359561 2232 DPITAYIVEYKEKFSNDWVSGKEVdGDARTATVDGLKEGQQYEFRVRAVNRAGPGEPSDKTKSIIA 2297
Cdd:COG3401   353 ADVTGYNVYRSTSGGGTYTKIAET-VTTTSYTDTGLTPGTTYYYKVTAVDAAGNESAPSEEVSATT 417
PKc_YAK1 cd14212
Catalytic domain of the Dual-specificity protein kinase, YAK1; Dual-specificity PKs catalyze ...
7989-8190 7.84e-15

Catalytic domain of the Dual-specificity protein kinase, YAK1; Dual-specificity PKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine (S/T) as well as tyrosine residues on protein substrates. This subfamily is composed of proteins with similarity to Saccharomyces cerevisiae YAK1 (or Yak1p), a dual-specificity kinase that autophosphorylates at tyrosine residues and phosphorylates substrates on S/T residues. YAK1 phosphorylates and activates the transcription factors Hsf1 and Msn2, which play important roles in cellular homeostasis during stress conditions including heat shock, oxidative stress, and nutrient deficiency. It also phosphorylates the protein POP2, a component of a complex that regulates transcription, under glucose-deprived conditions. It functions as a part of a glucose-sensing system that is involved in controlling growth in yeast. The YAK1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271114 [Multi-domain]  Cd Length: 330  Bit Score: 79.99  E-value: 7.84e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 7989 YDILEEIGTGAFGVVHRCRERSTGNIFAAKFIPvSHSVEKDLIRREIDIMNQL---------HHqkLINLHDAFEDDDEM 8059
Cdd:cd14212     1 YLVLDLLGQGTFGQVVKCQDLKTNKLVAVKVLK-NKPAYFRQAMLEIAILTLLntkydpedkHH--IVRLLDHFMHHGHL 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 8060 ILILEFLsGGELFERITAEGYVMTEAEVI-NYMRQICEGIRHMHEQNIIHLDIKPENIMCQTRSSTNVKLIDFGLATrlD 8138
Cdd:cd14212    78 CIVFELL-GVNLYELLKQNQFRGLSLQLIrKFLQQLLDALSVLKDARIIHCDLKPENILLVNLDSPEIKLIDFGSAC--F 154
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 281359561 8139 PNEVVKITTGTAEFAAPEIVNREPVGFYTDMWATGVLSYVLLSGLSPFAGDN 8190
Cdd:cd14212   155 ENYTLYTYIQSRFYRSPEVLLGLPYSTAIDMWSLGCIAAELFLGLPLFPGNS 206
FN3 smart00060
Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, ...
7151-7234 8.45e-15

Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, fibronectin. The tenth fibronectin type III repeat contains a RGD cell recognition sequence in a flexible loop between 2 strands. Type III modules are present in both extracellular and intracellular proteins.


Pssm-ID: 214495 [Multi-domain]  Cd Length: 83  Bit Score: 73.03  E-value: 8.45e-15
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561   7151 PSPPGAPQVTRVGKNYVDLKWEKPLRDGG-SRITGYIIERRDIGGAvWVKCNDyNVLDTEYTVMNLIEMGDYEFRVFAVN 7229
Cdd:smart00060    1 PSPPSNLRVTDVTSTSVTLSWEPPPDDGItGYIVGYRVEYREEGSE-WKEVNV-TPSSTSYTLTGLKPGTEYEFRVRAVN 78

                    ....*
gi 281359561   7230 SAGRS 7234
Cdd:smart00060   79 GAGEG 83
STKc_RIP cd13978
Catalytic domain of the Serine/Threonine kinase, Receptor Interacting Protein; STKs catalyze ...
7995-8188 9.02e-15

Catalytic domain of the Serine/Threonine kinase, Receptor Interacting Protein; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. RIP kinases serve as essential sensors of cellular stress. They are involved in regulating NF-kappaB and MAPK signaling, and are implicated in mediating cellular processes such as apoptosis, necroptosis, differentiation, and survival. RIP kinases contain a homologous N-terminal kinase domain and varying C-terminal domains. Higher vertebrates contain multiple RIP kinases, with mammals harboring at least five members. RIP1 and RIP2 harbor C-terminal domains from the Death domain (DD) superfamily while RIP4 contains ankyrin (ANK) repeats. RIP3 contain a RIP homotypic interaction motif (RHIM) that facilitates binding to RIP1. RIP1 and RIP3 are important in apoptosis and necroptosis, while RIP2 and RIP4 play roles in keratinocyte differentiation and inflammatory immune responses. The RIP subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270880 [Multi-domain]  Cd Length: 263  Bit Score: 78.65  E-value: 9.02e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 7995 IGTGAFGVVHRCRERSTGNIFAAKFIPVSHS--VEKDLIRREIDIMNQLHHQKLINLHDAFEDDDEMILILEFLSGGELF 8072
Cdd:cd13978     1 LGSGGFGTVSKARHVSWFGMVAIKCLHSSPNciEERKALLKEAEKMERARHSYVLPLLGVCVERRSLGLVMEYMENGSLK 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 8073 ERITAEGYVMTEAEVINYMRQICEGIRHMH--EQNIIHLDIKPENIMCQtrSSTNVKLIDFGLA------TRLDPNEVVK 8144
Cdd:cd13978    81 SLLEREIQDVPWSLRFRIIHEIALGMNFLHnmDPPLLHHDLKPENILLD--NHFHVKISDFGLSklgmksISANRRRGTE 158
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*..
gi 281359561 8145 ITTGTAEFAAPEI---VNREPVGFYtDMWATGVLSYVLLSGLSPFAG 8188
Cdd:cd13978   159 NLGGTPIYMAPEAfddFNKKPTSKS-DVYSFAIVIWAVLTRKEPFEN 204
STKc_B-Raf cd14151
Catalytic domain of the Serine/Threonine Kinase, B-Raf (Rapidly Accelerated Fibrosarcoma) ...
7993-8191 1.11e-14

Catalytic domain of the Serine/Threonine Kinase, B-Raf (Rapidly Accelerated Fibrosarcoma) kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. B-Raf activates ERK with the strongest magnitude, compared with other Raf kinases. Mice embryos deficient in B-Raf die around midgestation due to vascular hemorrhage caused by apoptotic endothelial cells. Mutations in B-Raf have been implicated in initiating tumorigenesis and tumor progression, and are found in malignant cutaneous melanoma, papillary thyroid cancer, as well as in ovarian and colorectal carcinomas. Most oncogenic B-Raf mutations are located at the activation loop of the kinase and surrounding regions; the V600E mutation accounts for around 90% of oncogenic mutations. The V600E mutant constitutively activates MEK, resulting in sustained activation of ERK. B-Raf is a mitogen-activated protein kinase kinase kinase (MAP3K, MKKK, MAPKKK), which phosphorylates and activates MAPK kinases (MAPKKs or MKKs or MAP2Ks), which in turn phosphorylate and activate MAPKs during signaling cascades that are important in mediating cellular responses to extracellular signals. They function in the linear Ras-Raf-MEK-ERK pathway that regulates many cellular processes including cycle regulation, proliferation, differentiation, survival, and apoptosis. The B-Raf subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271053 [Multi-domain]  Cd Length: 274  Bit Score: 78.56  E-value: 1.11e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 7993 EEIGTGAFGVVHRCRERstGNIfAAKFIPVSHSVEKDL--IRREIDIMNQLHHQKLInLHDAFEDDDEMILILEFLSGGE 8070
Cdd:cd14151    14 QRIGSGSFGTVYKGKWH--GDV-AVKMLNVTAPTPQQLqaFKNEVGVLRKTRHVNIL-LFMGYSTKPQLAIVTQWCEGSS 89
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 8071 LFERITAEGYVMTEAEVINYMRQICEGIRHMHEQNIIHLDIKPENIMCQtrSSTNVKLIDFGLAT---RLDPNEVVKITT 8147
Cdd:cd14151    90 LYHHLHIIETKFEMIKLIDIARQTAQGMDYLHAKSIIHRDLKSNNIFLH--EDLTVKIGDFGLATvksRWSGSHQFEQLS 167
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*..
gi 281359561 8148 GTAEFAAPEIV---NREPVGFYTDMWATGVLSYVLLSGLSPFAGDND 8191
Cdd:cd14151   168 GSILWMAPEVIrmqDKNPYSFQSDVYAFGIVLYELMTGQLPYSNINN 214
STKc_PFTAIRE1 cd07869
Catalytic domain of the Serine/Threonine Kinase, PFTAIRE-1 kinase; STKs catalyze the transfer ...
7987-8245 1.12e-14

Catalytic domain of the Serine/Threonine Kinase, PFTAIRE-1 kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PFTAIRE-1 is widely expressed except in the spleen and thymus. It is highly expressed in the brain, heart, pancreas, testis, and ovary, and is localized in the cytoplasm. It is regulated by cyclin D3 and is inhibited by the p21 cell cycle inhibitor. It has also been shown to interact with the membrane-associated cyclin Y, which recruits the protein to the plasma membrane. PFTAIRE-1 shares sequence similarity with Cyclin-Dependent Kinases (CDKs), which belong to a large family of STKs that are regulated by their cognate cyclins. Together, CDKs and cyclins are involved in the control of cell-cycle progression, transcription, and neuronal function. The PFTAIRE-1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 143374 [Multi-domain]  Cd Length: 303  Bit Score: 78.97  E-value: 1.12e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 7987 DRYDILEEIGTGAFGVVHRCRERSTGNIFAAKFIPVSHSVEKDLIR-REIDIMNQLHHQKLINLHDAFEDDDEMILILEF 8065
Cdd:cd07869     5 DSYEKLEKLGEGSYATVYKGKSKVNGKLVALKVIRLQEEEGTPFTAiREASLLKGLKHANIVLLHDIIHTKETLTLVFEY 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 8066 LSGgELFERITAEGYVMTEAEVINYMRQICEGIRHMHEQNIIHLDIKPENIMCQtrSSTNVKLIDFGLA-TRLDPNEVVK 8144
Cdd:cd07869    85 VHT-DLCQYMDKHPGGLHPENVKLFLFQLLRGLSYIHQRYILHRDLKPQNLLIS--DTGELKLADFGLArAKSVPSHTYS 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 8145 ITTGTAEFAAPEI-VNREPVGFYTDMWATGVLSYVLLSGLSPFAGDNDVQ--------TLKNVKACDW-------DFDVE 8208
Cdd:cd07869   162 NEVVTLWYRPPDVlLGSTEYSTCLDMWGVGCIFVEMIQGVAAFPGMKDIQdqleriflVLGTPNEDTWpgvhslpHFKPE 241
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|.
gi 281359561 8209 SFKYISEE--------------AKDFIRKLLVRNKEKRMTAHECLLHPWLT 8245
Cdd:cd07869   242 RFTLYSPKnlrqawnklsyvnhAEDLASKLLQCFPKNRLSAQAALSHEYFS 292
PTKc_FAK cd05056
Catalytic domain of the Protein Tyrosine Kinase, Focal Adhesion Kinase; PTKs catalyze the ...
7987-8192 1.18e-14

Catalytic domain of the Protein Tyrosine Kinase, Focal Adhesion Kinase; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. FAK is a cytoplasmic (or nonreceptor) PTK that contains an autophosphorylation site and a FERM domain at the N-terminus, a central tyr kinase domain, proline-rich regions, and a C-terminal FAT (focal adhesion targeting) domain. FAK activity is dependent on integrin-mediated cell adhesion, which facilitates N-terminal autophosphorylation. Full activation is achieved by the phosphorylation of its two adjacent A-loop tyrosines. FAK is important in mediating signaling initiated at sites of cell adhesions and at growth factor receptors. Through diverse molecular interactions, FAK functions as a biosensor or integrator to control cell motility. It is a key regulator of cell survival, proliferation, migration and invasion, and thus plays an important role in the development and progression of cancer. Src binds to autophosphorylated FAK forming the FAK-Src dual kinase complex, which is activated in a wide variety of tumor cells and generates signals promoting growth and metastasis. FAK is being developed as a target for cancer therapy. The FAK subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 133187 [Multi-domain]  Cd Length: 270  Bit Score: 78.23  E-value: 1.18e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 7987 DRYDIL--EEIGTGAFGVVHR-----------------CRERSTGNIfaakfipvshsveKDLIRREIDIMNQLHHQKLI 8047
Cdd:cd05056     4 QREDITlgRCIGEGQFGDVYQgvymspenekiavavktCKNCTSPSV-------------REKFLQEAYIMRQFDHPHIV 70
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 8048 NLHDAFEDDdEMILILEFLSGGELFERITAEGYVMTEAEVINYMRQICEGIRHMHEQNIIHLDIKPENIMcqTRSSTNVK 8127
Cdd:cd05056    71 KLIGVITEN-PVWIVMELAPLGELRSYLQVNKYSLDLASLILYAYQLSTALAYLESKRFVHRDIAARNVL--VSSPDCVK 147
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 8128 LIDFGLATRLDPNEVVKITTGT--AEFAAPEIVNREPVGFYTDMWATGVLSYVLLS-GLSPFAG--DNDV 8192
Cdd:cd05056   148 LGDFGLSRYMEDESYYKASKGKlpIKWMAPESINFRRFTSASDVWMFGVCMWEILMlGVKPFQGvkNNDV 217
I-set pfam07679
Immunoglobulin I-set domain;
4090-4181 1.19e-14

Immunoglobulin I-set domain;


Pssm-ID: 400151 [Multi-domain]  Cd Length: 90  Bit Score: 73.06  E-value: 1.19e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561  4090 PKIDRTnIKDITIKAGQHIRFDIKVSGEPPATKVWLHNKARLENDDSnYNIDMESYRTKLTVPISKRFHSGKYTLKAENE 4169
Cdd:pfam07679    1 PKFTQK-PKDVEVQEGESARFTCTVTGTPDPEVSWFKDGQPLRSSDR-FKVTYEGGTYTLTISNVQPDDSGKYTCVATNS 78
                           90
                   ....*....|..
gi 281359561  4170 SGRDEASFEVIV 4181
Cdd:pfam07679   79 AGEAEASAELTV 90
FN3 COG3401
Fibronectin type 3 domain [General function prediction only];
4832-5209 1.27e-14

Fibronectin type 3 domain [General function prediction only];


Pssm-ID: 442628 [Multi-domain]  Cd Length: 603  Bit Score: 81.59  E-value: 1.27e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 4832 STEPQVDVTGLSPGNEYKFRVSAVNAEGESQPLVGDESIVARNPfdePGKPENLKATDWDKDHVDLAWTPPlidGGSPIS 4911
Cdd:COG3401   189 STTLVDGGGDIEPGTTYYYRVAATDTGGESAPSNEVSVTTPTTP---PSAPTGLTATADTPGSVTLSWDPV---TESDAT 262
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 4912 CYIIEKQDKY-GKWERALDVPADQckATIPDLVEGQTYKFRVSAVNAAgtGEPSDSTPPIIAKARNKPPIIDRSSLVEVR 4990
Cdd:COG3401   263 GYRVYRSNSGdGPFTKVATVTTTS--YTDTGLTNGTTYYYRVTAVDAA--GNESAPSNVVSVTTDLTPPAAPSGLTATAV 338
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 4991 IKAGQSFTFDcKVSGEPApqTKWLLKKKEVYSKDNVKVTNVDYNTKLKVNSATRSDSGIYTVFAENANG---EDSADVKV 5067
Cdd:COG3401   339 GSSSITLSWT-ASSDADV--TGYNVYRSTSGGGTYTKIAETVTTTSYTDTGLTPGTTYYYKVTAVDAAGnesAPSEEVSA 415
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 5068 TVIDKPAPPNGPLKVDEINSESC------TLHWNPPDDDGGQPIDNYVVEKLDETTGRWIPAGETDGPVTA---LKVGGL 5138
Cdd:COG3401   416 TTASAASGESLTASVDAVPLTDVagataaASAASNPGVSAAVLADGGDTGNAVPFTTTSSTVTATTTDTTTanlSVTTGS 495
                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 281359561 5139 TPGHKYKFRVRAKNRQGTSEPLTTAQAIIAKNPFDVPTKPGTPTIKDFDKEFVDLEWTRPEADGGSPITGY 5209
Cdd:COG3401   496 LVGGSGASSVTNSVSVIGASAAAAVGGAPDGTPNVTGASPVTVGASTGDVLITDLVSLTTSASSSVSGAGL 566
Ig_Titin_like cd05748
Immunoglobulin (Ig)-like domain of titin and similar proteins; The members here are composed ...
4100-4181 1.46e-14

Immunoglobulin (Ig)-like domain of titin and similar proteins; The members here are composed of the immunoglobulin (Ig)-like domain found in titin-like proteins and similar proteins. Titin (also called connectin) is a fibrous sarcomeric protein specifically found in vertebrate striated muscle. Titin is a giant protein; depending on isoform composition, it ranges from 2970 to 3700 kDa, and is of a length that spans half a sarcomere. Titin largely consists of multiple repeats of Ig-like and fibronectin type 3 (FN-III)-like domains. Titin connects the ends of myosin thick filaments to Z disks and extends along the thick filament to the H zone. It appears to function similarly to an elastic band, keeping the myosin filaments centered in the sarcomere during muscle contraction or stretching. Within the sarcomere, titin is also attached to or is associated with myosin binding protein C (MyBP-C). MyBP-C appears to contribute to the generation of passive tension by titin and like titin has repeated Ig-like and FN-III domains. Also included in this group are worm twitchin and insect projectin, thick filament proteins of invertebrate muscle which also have repeated Ig-like and FN-III domains.


Pssm-ID: 409406 [Multi-domain]  Cd Length: 82  Bit Score: 72.24  E-value: 1.46e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 4100 ITIKAGQHIRFDIKVSGEPPATKVWlhNKARLENDDSN-YNIDMESYRTKLTVPISKRFHSGKYTLKAENESGRDEASFE 4178
Cdd:cd05748     2 IVVRAGESLRLDIPIKGRPTPTVTW--SKDGQPLKETGrVQIETTASSTSLVIKNAKRSDSGKYTLTLKNSAGEKSATIN 79

                  ...
gi 281359561 4179 VIV 4181
Cdd:cd05748    80 VKV 82
fn3 pfam00041
Fibronectin type III domain;
2803-2887 1.49e-14

Fibronectin type III domain;


Pssm-ID: 394996 [Multi-domain]  Cd Length: 85  Bit Score: 72.45  E-value: 1.49e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561  2803 KPGTPEVTDYDNQSISLKWAAPNnDGGAPIQKYIIEKKNKNKTEWEKALEIPGDQLEATVAGLQEYGEYQFRVIAVNKAG 2882
Cdd:pfam00041    2 APSNLTVTDVTSTSLTVSWTPPP-DGNGPITGYEVEYRPKNSGEPWNEITVPGTTTSVTLTGLKPGTEYEVRVQAVNGGG 80

                   ....*
gi 281359561  2883 LSPPS 2887
Cdd:pfam00041   81 EGPPS 85
Ig_Titin_like cd05748
Immunoglobulin (Ig)-like domain of titin and similar proteins; The members here are composed ...
2314-2395 1.53e-14

Immunoglobulin (Ig)-like domain of titin and similar proteins; The members here are composed of the immunoglobulin (Ig)-like domain found in titin-like proteins and similar proteins. Titin (also called connectin) is a fibrous sarcomeric protein specifically found in vertebrate striated muscle. Titin is a giant protein; depending on isoform composition, it ranges from 2970 to 3700 kDa, and is of a length that spans half a sarcomere. Titin largely consists of multiple repeats of Ig-like and fibronectin type 3 (FN-III)-like domains. Titin connects the ends of myosin thick filaments to Z disks and extends along the thick filament to the H zone. It appears to function similarly to an elastic band, keeping the myosin filaments centered in the sarcomere during muscle contraction or stretching. Within the sarcomere, titin is also attached to or is associated with myosin binding protein C (MyBP-C). MyBP-C appears to contribute to the generation of passive tension by titin and like titin has repeated Ig-like and FN-III domains. Also included in this group are worm twitchin and insect projectin, thick filament proteins of invertebrate muscle which also have repeated Ig-like and FN-III domains.


Pssm-ID: 409406 [Multi-domain]  Cd Length: 82  Bit Score: 72.24  E-value: 1.53e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 2314 VTVKKGQTIRFDIKYDGEPEPAATWVKGTDNLKfDNQRICLDQLERNSSITIKKSVRKDTGKYKLVLSNSSGTIESEAQV 2393
Cdd:cd05748     2 IVVRAGESLRLDIPIKGRPTPTVTWSKDGQPLK-ETGRVQIETTASSTSLVIKNAKRSDSGKYTLTLKNSAGEKSATINV 80

                  ..
gi 281359561 2394 VV 2395
Cdd:cd05748    81 KV 82
IgI_titin_I1-like cd20951
Immunoglobulin domain I1 of the titin I-band and similar proteins; a member of the I-set of ...
7648-7735 1.70e-14

Immunoglobulin domain I1 of the titin I-band and similar proteins; a member of the I-set of IgSF domains; The members here are composed of the immunoglobulin domain I1 of the titin I-band and similar proteins. Titin is a key component in the assembly and functioning of vertebrate striated muscles. By providing connections at the level of individual microfilaments, it contributes to the fine balance of forces between the two halves of the sarcomere. The Ig superfamily (IgSF) is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. The two sheets are linked together by a conserved disulfide bond between B strand and F strand. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. The Ig I1 domain of the titin I-band is a member of the I-set Ig domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand but lack a C" strand. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors, the hemolymph protein hemolin, the muscle proteins titin, telokin, and twitchin, the neuronal adhesion molecule axonin-1, and the signaling molecule semaphorin 4D that is involved in axonal guidance, immune function and angiogenesis.


Pssm-ID: 409543 [Multi-domain]  Cd Length: 94  Bit Score: 72.84  E-value: 1.70e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 7648 PLIVKPLRDANCIQNHNAQFTCTINGVPKPTISWYKGAREI---SNGARYHMYSEGDNHFLNINDVFGEDADEYVCRAVN 7724
Cdd:cd20951     1 PEFIIRLQSHTVWEKSDAKLRVEVQGKPDPEVKWYKNGVPIdpsSIPGKYKIESEYGVHVLHIRRVTVEDSAVYSAVAKN 80
                          90
                  ....*....|.
gi 281359561 7725 KAGAKSTRATL 7735
Cdd:cd20951    81 IHGEASSSASV 91
IgI_4_hemolin-like cd20978
Fourth immunoglobulin (Ig)-like domain of hemolin, and similar domains; a member of the I-set ...
7254-7344 1.72e-14

Fourth immunoglobulin (Ig)-like domain of hemolin, and similar domains; a member of the I-set of IgSF domains; The members here are composed of the fourth immunoglobulin (Ig)-like domain of hemolin and similar proteins. Hemolin, an insect immunoglobulin superfamily (IgSF) member containing four Ig-like domains, is a lipopolysaccharide-binding immune protein induced during bacterial infection. Hemolin shares significant sequence similarity with the first four Ig-like domains of the transmembrane cell adhesion molecules (CAMs) of the L1 family. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. The fourth Ig-like domain of hemolin is a member of the I-set Ig domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set domains, members of the I-set have a discontinuous A strand but lack a C" strand. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors, the muscle proteins titin, telokin, and twitchin, the neuronal adhesion molecule axonin-1, and the signaling molecule semaphorin 4D that is involved in axonal guidance, immune function and angiogenesis.


Pssm-ID: 409570 [Multi-domain]  Cd Length: 88  Bit Score: 72.42  E-value: 1.72e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 7254 PDWITRLQD-KVAPFGKDYTLQCAASGKPSPTARWLRNGKEIQMNGGRMTCDSkdgvFRLHISNVQTGDDGDYTCEAMNS 7332
Cdd:cd20978     1 PKFIQKPEKnVVVKGGQDVTLPCQVTGVPQPKITWLHNGKPLQGPMERATVED----GTLTIINVQPEDTGYYGCVATNE 76
                          90
                  ....*....|..
gi 281359561 7333 LGFVNTSGYLKI 7344
Cdd:cd20978    77 IGDIYTETLLHV 88
FN3 smart00060
Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, ...
5764-5847 1.74e-14

Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, fibronectin. The tenth fibronectin type III repeat contains a RGD cell recognition sequence in a flexible loop between 2 strands. Type III modules are present in both extracellular and intracellular proteins.


Pssm-ID: 214495 [Multi-domain]  Cd Length: 83  Bit Score: 72.26  E-value: 1.74e-14
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561   5764 PDAPGKPIITDWDRDHIDLQWAVPKSDGG-APISEYIIQKKEKGSPyWTNVrHVPSNKNTTTIPELTEGQEYEFRVIAVN 5842
Cdd:smart00060    1 PSPPSNLRVTDVTSTSVTLSWEPPPDDGItGYIVGYRVEYREEGSE-WKEV-NVTPSSTSYTLTGLKPGTEYEFRVRAVN 78

                    ....*
gi 281359561   5843 QAGQS 5847
Cdd:smart00060   79 GAGEG 83
PK_eIF2AK_GCN2_rpt1 cd14012
Pseudokinase domain, repeat 1, of eukaryotic translation Initiation Factor 2-Alpha Kinase 4 or ...
8030-8242 1.86e-14

Pseudokinase domain, repeat 1, of eukaryotic translation Initiation Factor 2-Alpha Kinase 4 or General Control Non-derepressible-2; The pseudokinase domain shows similarity to protein kinases but lacks crucial residues for catalytic activity. EIF2AKs phosphorylate the alpha subunit of eIF-2, resulting in the overall downregulation of protein synthesis. eIF-2 phosphorylation is induced in response to cellular stresses including virus infection, heat shock, nutrient deficiency, and the accummulation of unfolded proteins, among others. There are four distinct kinases that phosphorylate eIF-2 and control protein synthesis under different stress conditions: GCN2, protein kinase regulated by RNA (PKR), heme-regulated inhibitor kinase (HRI), and PKR-like endoplasmic reticulum kinase (PERK). GCN2 is activated by amino acid or serum starvation and UV irradiation. It induces GCN4, a transcriptional activator of amino acid biosynthetic genes, leading to increased production of amino acids under amino acid-deficient conditions. In serum-starved cells, GCN2 activation induces translation of the stress-responsive transcription factor ATF4, while under UV stress, GCN2 triggers transcriptional rescue via NF-kappaB signaling. GCN2 contains an N-terminal RWD, a degenerate kinase-like (repeat 1), the catalytic kinase (repeat 2), a histidyl-tRNA synthetase (HisRS)-like, and a C-terminal ribosome-binding and dimerization (RB/DD) domains. The degenerate pseudokinase domain of GCN2 may function as a regulatory domain. The GCN2 subfamily is part of a larger superfamily that includes the catalytic domains of serine/threonine kinases, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270914 [Multi-domain]  Cd Length: 254  Bit Score: 77.40  E-value: 1.86e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 8030 LIRREIDIMNQLHHQKLINLHdAF-----EDDDE--MILILEFLSGGELFERITAEGYVMTEAeVINYMRQICEGIRHMH 8102
Cdd:cd14012    44 LLEKELESLKKLRHPNLVSYL-AFsierrGRSDGwkVYLLTEYAPGGSLSELLDSVGSVPLDT-ARRWTLQLLEALEYLH 121
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 8103 EQNIIHLDIKPENIMC-QTRSSTNVKLIDFGLATRL-DPNEVVKITT--GTAEFaAPEIVN-REPVGFYTDMWATGVLSY 8177
Cdd:cd14012   122 RNGVVHKSLHAGNVLLdRDAGTGIVKLTDYSLGKTLlDMCSRGSLDEfkQTYWL-PPELAQgSKSPTRKTDVWDLGLLFL 200
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 281359561 8178 VLLSGLSPFAGDNDVQTLKNVKAcdwdfdvesfkyISEEAKDFIRKLLVRNKEKRMTAHECLLHP 8242
Cdd:cd14012   201 QMLFGLDVLEKYTSPNPVLVSLD------------LSASLQDFLSKCLSLDPKKRPTALELLPHE 253
STKc_HIPK cd14211
Catalytic domain of the Serine/Threonine Kinase, Homeodomain-Interacting Protein Kinase; STKs ...
7989-8173 2.08e-14

Catalytic domain of the Serine/Threonine Kinase, Homeodomain-Interacting Protein Kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. HIPKs, originally identified by their ability to bind homeobox factors, are nuclear proteins containing catalytic kinase and homeobox-interacting domains as well as a PEST region overlapping with the speckle-retention signal (SRS). They show speckled localization in the nucleus, apart from the nucleoles. They play roles in the regulation of many nuclear pathways including gene transcription, cell survival, proliferation, differentiation, development, and DNA damage response. Vertebrates contain three HIPKs (HIPK1-3) and mammals harbor an additional family member HIPK4, which does not contain a homeobox-interacting domain and is localized in the cytoplasm. HIPK2, the most studied HIPK, is a coregulator of many transcription factors and cofactors and it regulates gene transcription during development and in DNA damage response. The HIPK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271113 [Multi-domain]  Cd Length: 329  Bit Score: 78.64  E-value: 2.08e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 7989 YDILEEIGTGAFGVVHRCRERSTGNIFAAKfIPVSHSVEKDLIRREIDIMNQLHHQ-----KLINLHDAFEDDDEMILIL 8063
Cdd:cd14211     1 YEVLEFLGRGTFGQVVKCWKRGTNEIVAIK-ILKNHPSYARQGQIEVSILSRLSQEnadefNFVRAYECFQHKNHTCLVF 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 8064 EFLSgGELFERITAEGYVMTEAEVIN-YMRQICEGIRHMHEQNIIHLDIKPENIMC--QTRSSTNVKLIDFGLATRLdpN 8140
Cdd:cd14211    80 EMLE-QNLYDFLKQNKFSPLPLKYIRpILQQVLTALLKLKSLGLIHADLKPENIMLvdPVRQPYRVKVIDFGSASHV--S 156
                         170       180       190
                  ....*....|....*....|....*....|....
gi 281359561 8141 EVVKITTGTAEF-AAPEIVNREPVGFYTDMWATG 8173
Cdd:cd14211   157 KAVCSTYLQSRYyRAPEIILGLPFCEAIDMWSLG 190
IG_like smart00410
Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.
7268-7344 2.17e-14

Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.


Pssm-ID: 214653 [Multi-domain]  Cd Length: 85  Bit Score: 72.15  E-value: 2.17e-14
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 281359561   7268 GKDYTLQCAASGKPSPTARWLRNGKEIQMNGGRMTCDSKDGVFRLHISNVQTGDDGDYTCEAMNSLGFVNTSGYLKI 7344
Cdd:smart00410    9 GESVTLSCEASGSPPPEVTWYKQGGKLLAESGRFSVSRSGSTSTLTISNVTPEDSGTYTCAATNSSGSASSGTTLTV 85
Ig_Titin_like cd05748
Immunoglobulin (Ig)-like domain of titin and similar proteins; The members here are composed ...
3806-3885 2.55e-14

Immunoglobulin (Ig)-like domain of titin and similar proteins; The members here are composed of the immunoglobulin (Ig)-like domain found in titin-like proteins and similar proteins. Titin (also called connectin) is a fibrous sarcomeric protein specifically found in vertebrate striated muscle. Titin is a giant protein; depending on isoform composition, it ranges from 2970 to 3700 kDa, and is of a length that spans half a sarcomere. Titin largely consists of multiple repeats of Ig-like and fibronectin type 3 (FN-III)-like domains. Titin connects the ends of myosin thick filaments to Z disks and extends along the thick filament to the H zone. It appears to function similarly to an elastic band, keeping the myosin filaments centered in the sarcomere during muscle contraction or stretching. Within the sarcomere, titin is also attached to or is associated with myosin binding protein C (MyBP-C). MyBP-C appears to contribute to the generation of passive tension by titin and like titin has repeated Ig-like and FN-III domains. Also included in this group are worm twitchin and insect projectin, thick filament proteins of invertebrate muscle which also have repeated Ig-like and FN-III domains.


Pssm-ID: 409406 [Multi-domain]  Cd Length: 82  Bit Score: 71.85  E-value: 2.55e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 3806 IMRSGQMLHIDALIKAEPPAKVTWTYNKTEIKTSDHIKIENEDYKTTFIMPKVKRADRGIYIVTAKNDSGSDTVEVELEV 3885
Cdd:cd05748     3 VVRAGESLRLDIPIKGRPTPTVTWSKDGQPLKETGRVQIETTASSTSLVIKNAKRSDSGKYTLTLKNSAGEKSATINVKV 82
IgI_2_Titin_Z1z2-like cd20972
Second Ig-like domain of the giant muscle protein titin Z1z2 in the sarcomeric Z-disk, and ...
8632-8721 2.57e-14

Second Ig-like domain of the giant muscle protein titin Z1z2 in the sarcomeric Z-disk, and similar domains; a member of the I-set of IgSF domains; The members here are composed of the second immunoglobulin (Ig)-like domain of the giant muscle protein titin Z1z2 in the sarcomeric Z-disk and similar proteins. Titin is a key component in the assembly and functioning of vertebrate striated muscles. By providing connections at the level of individual microfilaments, it contributes to the fine balance of forces between the two halves of the sarcomere. The Ig superfamily (IgSF) is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. Unlike the V-set, one of the distinctive features of I-set domains is the lack of a C" strand. The structure of the titin Z1z2 lacks this strand and thus it belongs to the I-set of the IgSF. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors, the hemolymph protein hemolin, the muscle proteins titin, telokin, and twitchin, the neuronal adhesion molecule axonin-1, and the signaling molecule semaphorin 4D that is involved in axonal guidance, immune function and angiogenesis.


Pssm-ID: 409564 [Multi-domain]  Cd Length: 91  Bit Score: 72.23  E-value: 2.57e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 8632 PEFTKPLHDLTIHDGEQLILTCYVKGDPEPQISWSKNGKSLSSSDILDLRYKNGIATLTINEVFPEDEGVITCTATNSVG 8711
Cdd:cd20972     2 PQFIQKLRSQEVAEGSKVRLECRVTGNPTPVVRWFCEGKELQNSPDIQIHQEGDLHSLIIAEAFEEDTGRYSCLATNSVG 81
                          90
                  ....*....|
gi 281359561 8712 AVETKCKLTI 8721
Cdd:cd20972    82 SDTTSAEIFV 91
FN3 COG3401
Fibronectin type 3 domain [General function prediction only];
7398-7831 2.66e-14

Fibronectin type 3 domain [General function prediction only];


Pssm-ID: 442628 [Multi-domain]  Cd Length: 603  Bit Score: 80.82  E-value: 2.66e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 7398 KVNIFDDYVAIYIRNIVKSDGGPYQIEFTNESGSATGEFYVHITGMPSAPTGPMGISYINKNSCMLNWRPPSYDGGLKVS 7477
Cdd:COG3401    87 APPTATGLTTLTGSGSVGGATNTGLTSSDEVPSPAVGTATTATAVAGGAATAGTYALGAGLYGVDGANASGTTASSVAGA 166
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 7478 HYVIERKDVSSPHWITVSSTCKDTAFNVQGLI--ENQEYIFRVMAVNENGMGPPlegLNPIRAKDPIDPPSPPGSPQITE 7555
Cdd:COG3401   167 GVVVSPDTSATAAVATTSLTVTSTTLVDGGGDiePGTTYYYRVAATDTGGESAP---SNEVSVTTPTTPPSAPTGLTATA 243
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 7556 IGGDFVHLEWEKPESDGgahIQGYWIDKREVGSNTWQRVNATicAANQINCINLIEGRQYEFRIFAQNVAGlsTESSASQ 7635
Cdd:COG3401   244 DTPGSVTLSWDPVTESD---ATGYRVYRSNSGDGPFTKVATV--TTTSYTDTGLTNGTTYYYRVTAVDAAG--NESAPSN 316
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 7636 AVKI-IDPQAASPPLIVkplrdanciqnhnaqfTCTINGVPKPTISWykGAREISNGARYHMY--SEGDNHFLNINDVFG 7712
Cdd:COG3401   317 VVSVtTDLTPPAAPSGL----------------TATAVGSSSITLSW--TASSDADVTGYNVYrsTSGGGTYTKIAETVT 378
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 7713 E----DAD-------EYVCRAVNKAGAKSTRAtlAIMTAPKLNVPPRFRDTAYfdkgeNVVIKIPFTGFPKPRIHWVRDG 7781
Cdd:COG3401   379 TtsytDTGltpgttyYYKVTAVDAAGNESAPS--EEVSATTASAASGESLTAS-----VDAVPLTDVAGATAAASAASNP 451
                         410       420       430       440       450
                  ....*....|....*....|....*....|....*....|....*....|...
gi 281359561 7782 E---NIESGGHYTVEVKERHAVLIIRDGSHLDSGPYRITAENELGSDTAIIQV 7831
Cdd:COG3401   452 GvsaAVLADGGDTGNAVPFTTTSSTVTATTTDTTTANLSVTTGSLVGGSGASS 504
PTKc_Jak_rpt2 cd05038
Catalytic (repeat 2) domain of the Protein Tyrosine Kinases, Janus kinases; The Jak subfamily ...
7992-8181 2.76e-14

Catalytic (repeat 2) domain of the Protein Tyrosine Kinases, Janus kinases; The Jak subfamily is composed of Jak1, Jak2, Jak3, TYK2, and similar proteins. They are PTKs, catalyzing the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Jaks are cytoplasmic (or nonreceptor) PTKs containing an N-terminal FERM domain, followed by a Src homology 2 (SH2) domain, a pseudokinase domain, and a C-terminal tyr kinase catalytic domain. Most Jaks are expressed in a wide variety of tissues, except for Jak3, which is expressed only in hematopoietic cells. Jaks are crucial for cytokine receptor signaling. They are activated by autophosphorylation upon cytokine-induced receptor aggregation, and subsequently trigger downstream signaling events such as the phosphorylation of signal transducers and activators of transcription (STATs). Jaks are also involved in regulating the surface expression of some cytokine receptors. The Jak-STAT pathway is involved in many biological processes including hematopoiesis, immunoregulation, host defense, fertility, lactation, growth, and embryogenesis. The Jak subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270634 [Multi-domain]  Cd Length: 284  Bit Score: 77.42  E-value: 2.76e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 7992 LEEIGTGAFGVVHRCR----ERSTGNIFAAKFIPVS--HSVEKDLiRREIDIMNQLHHQKLINLHDAFEDDDE--MILIL 8063
Cdd:cd05038     9 IKQLGEGHFGSVELCRydplGDNTGEQVAVKSLQPSgeEQHMSDF-KREIEILRTLDHEYIVKYKGVCESPGRrsLRLIM 87
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 8064 EFLSGGELferitaEGYVMTEAEVIN------YMRQICEGIRHMHEQNIIHLDIKPENIMCQtrSSTNVKLIDFGLATRL 8137
Cdd:cd05038    88 EYLPSGSL------RDYLQRHRDQIDlkrlllFASQICKGMEYLGSQRYIHRDLAARNILVE--SEDLVKISDFGLAKVL 159
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*...
gi 281359561 8138 DPNEVVKITTGTAEFA----APEIVNREPVGFYTDMWATGVLSYVLLS 8181
Cdd:cd05038   160 PEDKEYYYVKEPGESPifwyAPECLRESRFSSASDVWSFGVTLYELFT 207
PTKc_Jak1_rpt2 cd05079
Catalytic (repeat 2) domain of the Protein Tyrosine Kinase, Janus kinase 1; PTKs catalyze the ...
7992-8181 2.98e-14

Catalytic (repeat 2) domain of the Protein Tyrosine Kinase, Janus kinase 1; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Jak1 is widely expressed in many tissues. Many cytokines are dependent on Jak1 for signaling, including those that use the shared receptor subunits common gamma chain (IL-2, IL-4, IL-7, IL-9, IL-15, IL-21) and gp130 (IL-6, IL-11, oncostatin M, G-CSF, and IFNs, among others). The many varied interactions of Jak1 and its ubiquitous expression suggest many biological roles. Jak1 is important in neurological development, as well as in lymphoid development and function. It also plays a role in the pathophysiology of cardiac hypertrophy and heart failure. A mutation in the ATP-binding site of Jak1 was identified in a human uterine leiomyosarcoma cell line, resulting in defective cytokine induction and antigen presentation, thus allowing the tumor to evade the immune system. Jak1 is a member of the Janus kinase (Jak) subfamily of proteins, which are cytoplasmic (or nonreceptor) PTKs containing an N-terminal FERM domain, followed by a Src homology 2 (SH2) domain, a pseudokinase domain, and a C-terminal tyr kinase domain. Jaks are crucial for cytokine receptor signaling. They are activated by autophosphorylation upon cytokine-induced receptor aggregation, and subsequently trigger downstream signaling events such as the phosphorylation of signal transducers and activators of transcription (STATs). The Jak1 subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 173644 [Multi-domain]  Cd Length: 284  Bit Score: 77.28  E-value: 2.98e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 7992 LEEIGTGAFGVVHRCRER----STGNIFAAKFI-PVSHSVEKDLIRREIDIMNQLHHQKLINLHDAFEDD--DEMILILE 8064
Cdd:cd05079     9 IRDLGEGHFGKVELCRYDpegdNTGEQVAVKSLkPESGGNHIADLKKEIEILRNLYHENIVKYKGICTEDggNGIKLIME 88
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 8065 FLSGGELFERITAEGYVMTEAEVINYMRQICEGIRHMHEQNIIHLDIKPENIMCQtrSSTNVKLIDFGLATRLDPNE--- 8141
Cdd:cd05079    89 FLPSGSLKEYLPRNKNKINLKQQLKYAVQICKGMDYLGSRQYVHRDLAARNVLVE--SEHQVKIGDFGLTKAIETDKeyy 166
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|.
gi 281359561 8142 VVKITTGTAEF-AAPEIVNREPVGFYTDMWATGVLSYVLLS 8181
Cdd:cd05079   167 TVKDDLDSPVFwYAPECLIQSKFYIASDVWSFGVTLYELLT 207
FN3 COG3401
Fibronectin type 3 domain [General function prediction only];
6226-6927 3.02e-14

Fibronectin type 3 domain [General function prediction only];


Pssm-ID: 442628 [Multi-domain]  Cd Length: 603  Bit Score: 80.43  E-value: 3.02e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 6226 DDSNRRDSGKYTVTAANEFGKDTADIEVIVVDKP--SPPEGPLSYTETAPDHISLHWYSPKDDGGSDITGYIIEFTEFGV 6303
Cdd:COG3401    33 GKTILVYLAVVLSVTTKESPGTLLVAAGLSSGGGlgTGGRAGTTSGVAAVAVAAAPPTATGLTTLTGSGSVGGATNTGLT 112
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 6304 DDWKPVPGTcpntnftvknlvegKKYVFRIRAENIYGASEALEGKPVLAKSPFDPPGAPSQPTISAYTPNSAnlewhPPD 6383
Cdd:COG3401   113 SSDEVPSPA--------------VGTATTATAVAGGAATAGTYALGAGLYGVDGANASGTTASSVAGAGVVV-----SPD 173
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 6384 DCGGKPITGYIVERRERGGEWIkcNNYPTPNTSYTvsnlrdgaryeFRVLAVNEAGpghPSKPSDPMTAEHQRYRPDPPE 6463
Cdd:COG3401   174 TSATAAVATTSLTVTSTTLVDG--GGDIEPGTTYY-----------YRVAATDTGG---ESAPSNEVSVTTPTTPPSAPT 237
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 6464 PPKPDRITRNGVTLSWRPPrtdGKSRIKGYYVEMRPKNGKDWKTVNDipINSTVYTVPSLKEGEEYSFRVVAENEVGrsD 6543
Cdd:COG3401   238 GLTATADTPGSVTLSWDPV---TESDATGYRVYRSNSGDGPFTKVAT--VTTTSYTDTGLTNGTTYYYRVTAVDAAG--N 310
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 6544 PSKPSQPITIEeqpnkpcmelgkvrdivcragddfsihvpylafpkpnafwysndnmlddnnrvhkhlTDDAAsvvvkns 6623
Cdd:COG3401   311 ESAPSNVVSVT---------------------------------------------------------TDLTP------- 326
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 6624 kradsgqyrlqlkntsgfdtatinvrvldrPSPPTRLRADEFSGDSLTLYWNPPNDDGgsaIQNYIIEKKEARSSTWSKV 6703
Cdd:COG3401   327 ------------------------------PAAPSGLTATAVGSSSITLSWTASSDAD---VTGYNVYRSTSGGGTYTKI 373
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 6704 SSFCTVPFVRIRNLVLNKEYDFRVIAENKYG-QSDPAN--TSEPILARHPFDIPNTPGIPHGIDSTEDSITIAWTKPKHD 6780
Cdd:COG3401   374 AETVTTTSYTDTGLTPGTTYYYKVTAVDAAGnESAPSEevSATTASAASGESLTASVDAVPLTDVAGATAAASAASNPGV 453
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 6781 GGSPITGYIIEKRLLSDDKWTKAVHALCPDLSCKIPNLIENAEYEFRVAAVNAAGQSAYSGSSdliFCRRPPHAPKITSD 6860
Cdd:COG3401   454 SAAVLADGGDTGNAVPFTTTSSTVTATTTDTTTANLSVTTGSLVGGSGASSVTNSVSVIGASA---AAAVGGAPDGTPNV 530
                         650       660       670       680       690       700       710
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 281359561 6861 LS------IRDMTVIAGDEFRITVPYHASPRPTASWSLNGLEVIPGERIKFDSNDYASMYYNKSAKRDETGSY 6927
Cdd:COG3401   531 TGaspvtvGASTGDVLITDLVSLTTSASSSVSGAGLGSGNLYLITTLGGSLLTTTSTNTNDVAGVHGGTLLVL 603
Ig_C5_MyBP-C cd05894
C5 immunoglobulin (Ig) domain of cardiac myosin binding protein C (MyBP-C); The members here ...
6175-6255 3.33e-14

C5 immunoglobulin (Ig) domain of cardiac myosin binding protein C (MyBP-C); The members here are composed of the C5 immunoglobulin (Ig) domain of cardiac myosin binding protein C (MyBP-C). MyBP-C consists of repeated domains, Ig and fibronectin type 3, and various linkers. Three isoforms of MYBP-C exist: slow-skeletal (ssMyBP-C), fast-skeletal (fsMyBP-C), and cardiac (cMyBP-C). cMYBP-C has insertions between and inside domains and an additional cardiac-specific Ig domain at the N-terminus. For cMYBP_C an interaction has been demonstrated between this C5 domain and the Ig C8 domain.


Pssm-ID: 409475  Cd Length: 86  Bit Score: 71.41  E-value: 3.33e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 6175 IKVRAGEPVNLNIPISGAPTPTIEWKRGDLKLEEGK-RISYETNSERTLFRIDDSNRRDSGKYTVTAANEFGKDTADIEV 6253
Cdd:cd05894     5 IVVVAGNKLRLDVPISGEPAPTVTWSRGDKAFTATEgRVRVESYKDLSSFVIEGAEREDEGVYTITVTNPVGEDHASLFV 84

                  ..
gi 281359561 6254 IV 6255
Cdd:cd05894    85 KV 86
FN3 smart00060
Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, ...
6259-6342 3.37e-14

Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, fibronectin. The tenth fibronectin type III repeat contains a RGD cell recognition sequence in a flexible loop between 2 strands. Type III modules are present in both extracellular and intracellular proteins.


Pssm-ID: 214495 [Multi-domain]  Cd Length: 83  Bit Score: 71.49  E-value: 3.37e-14
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561   6259 PSPPEGpLSYTETAPDHISLHWYSPKDDGG-SDITGYIIEFTEFGvDDWKPVPGTCPNTNFTVKNLVEGKKYVFRIRAEN 6337
Cdd:smart00060    1 PSPPSN-LRVTDVTSTSVTLSWEPPPDDGItGYIVGYRVEYREEG-SEWKEVNVTPSSTSYTLTGLKPGTEYEFRVRAVN 78

                    ....*
gi 281359561   6338 IYGAS 6342
Cdd:smart00060   79 GAGEG 83
STKc_NLK cd07853
Catalytic domain of the Serine/Threonine Kinase, Nemo-Like Kinase; STKs catalyze the transfer ...
7995-8251 3.42e-14

Catalytic domain of the Serine/Threonine Kinase, Nemo-Like Kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. NLK is an atypical mitogen-activated protein kinase (MAPK) that is not regulated by a MAPK kinase. It functions downstream of the MAPK kinase kinase Tak1, which also plays a role in activating the JNK and p38 MAPKs. The Tak1/NLK pathways are regulated by Wnts, a family of secreted proteins that is critical in the control of asymmetric division and cell polarity. NLK can phosphorylate transcription factors from the TCF/LEF family, inhibiting their ability to activate the transcription of target genes. In prostate cancer cells, NLK is involved in regulating androgen receptor-mediated transcription and its expression is altered during cancer progression. MAPKs are important mediators of cellular responses to extracellular signals. The NLK subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 173748 [Multi-domain]  Cd Length: 372  Bit Score: 78.63  E-value: 3.42e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 7995 IGTGAFGVVHRCRERSTGNIFAAKFIPvshSVEKDLIR-----REIDIMNQLHHQKLINLHDAFEDDD-----EMILILE 8064
Cdd:cd07853     8 IGYGAFGVVWSVTDPRDGKRVALKKMP---NVFQNLVSckrvfRELKMLCFFKHDNVLSALDILQPPHidpfeEIYVVTE 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 8065 FLSGGelFERITAEGYVMTEAEVINYMRQICEGIRHMHEQNIIHLDIKPENIMcqTRSSTNVKLIDFGLATRLDPNEVVK 8144
Cdd:cd07853    85 LMQSD--LHKIIVSPQPLSSDHVKVFLYQILRGLKYLHSAGILHRDIKPGNLL--VNSNCVLKICDFGLARVEEPDESKH 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 8145 ITTG--TAEFAAPEIVNREPvgFYT---DMWATGVLSYVLLSGLSPFAGDNDVQTLKNV-------------KACDwdfd 8206
Cdd:cd07853   161 MTQEvvTQYYRAPEILMGSR--HYTsavDIWSVGCIFAELLGRRILFQAQSPIQQLDLItdllgtpsleamrSACE---- 234
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 281359561 8207 vESFKYI--------------------SEEAKDFIRKLLVRNKEKRMTAHECLLHPWLTGD----HSAM 8251
Cdd:cd07853   235 -GARAHIlrgphkppslpvlytlssqaTHEAVHLLCRMLVFDPDKRISAADALAHPYLDEGrlryHTCM 302
STKc_Raf cd14062
Catalytic domain of the Serine/Threonine Kinases, Raf (Rapidly Accelerated Fibrosarcoma) ...
7995-8190 3.50e-14

Catalytic domain of the Serine/Threonine Kinases, Raf (Rapidly Accelerated Fibrosarcoma) kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Raf kinases act as mitogen-activated protein kinase kinase kinases (MAP3Ks, MKKKs, MAPKKKs), which phosphorylate and activate MAPK kinases (MAPKKs or MKKs or MAP2Ks), which in turn phosphorylate and activate MAPKs during signaling cascades that are important in mediating cellular responses to extracellular signals. They function in the linear Ras-Raf-MEK-ERK pathway that regulates many cellular processes including cycle regulation, proliferation, differentiation, survival, and apoptosis. Aberrant expression or activation of components in this pathway are associated with tumor initiation, progression, and metastasis. Raf proteins contain a Ras binding domain, a zinc finger cysteine-rich domain, and a catalytic kinase domain. Vertebrates have three Raf isoforms (A-, B-, and C-Raf) with different expression profiles, modes of regulation, and abilities to function in the ERK cascade, depending on cellular context and stimuli. They have essential and non-overlapping roles during embryo- and organogenesis. Knockout of each isoform results in a lethal phenotype or abnormality in most mouse strains. The Raf subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270964 [Multi-domain]  Cd Length: 253  Bit Score: 76.66  E-value: 3.50e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 7995 IGTGAFGVVHRCRERSTgniFAAKFIPVSHSVEKDL--IRREIDIMNQLHHQKLInLHDAFEDDDEMILILEFLSGGELF 8072
Cdd:cd14062     1 IGSGSFGTVYKGRWHGD---VAVKKLNVTDPTPSQLqaFKNEVAVLRKTRHVNIL-LFMGYMTKPQLAIVTQWCEGSSLY 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 8073 ERItaegYVM-TEAEV---INYMRQICEGIRHMHEQNIIHLDIKPENIMCQtrSSTNVKLIDFGLAT---RLDPNEVVKI 8145
Cdd:cd14062    77 KHL----HVLeTKFEMlqlIDIARQTAQGMDYLHAKNIIHRDLKSNNIFLH--EDLTVKIGDFGLATvktRWSGSQQFEQ 150
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*...
gi 281359561 8146 TTGTAEFAAPEIV---NREPVGFYTDMWATGVLSYVLLSGLSPFAGDN 8190
Cdd:cd14062   151 PTGSILWMAPEVIrmqDENPYSFQSDVYAFGIVLYELLTGQLPYSHIN 198
PTKc_Tec_Rlk cd05114
Catalytic domain of the Protein Tyrosine Kinases, Tyrosine kinase expressed in hepatocellular ...
7992-8200 5.06e-14

Catalytic domain of the Protein Tyrosine Kinases, Tyrosine kinase expressed in hepatocellular carcinoma and Resting lymphocyte kinase; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Tec and Rlk (also named Txk) are members of the Tec-like subfamily of proteins, which are cytoplasmic (or nonreceptor) PTKs with similarity to Src kinases in that they contain Src homology protein interaction domains (SH3, SH2) N-terminal to the catalytic tyr kinase domain. Unlike Src kinases, most Tec subfamily members except Rlk also contain an N-terminal pleckstrin homology (PH) domain, which binds the products of PI3K and allows membrane recruitment and activation. Instead of PH, Rlk contains an N-terminal cysteine-rich region. In addition to PH, Tec also contains the Tec homology (TH) domain with proline-rich and zinc-binding regions. Tec kinases are expressed mainly by haematopoietic cells. Tec is more widely-expressed than other Tec-like subfamily kinases. It is found in endothelial cells, both B- and T-cells, and a variety of myeloid cells including mast cells, erythroid cells, platelets, macrophages and neutrophils. Rlk is expressed in T-cells and mast cell lines. Tec and Rlk are both key components of T-cell receptor (TCR) signaling. They are important in TCR-stimulated proliferation, IL-2 production and phopholipase C-gamma1 activation. The Tec/Rlk subfamily is part of a larger superfamily, that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270685 [Multi-domain]  Cd Length: 260  Bit Score: 76.44  E-value: 5.06e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 7992 LEEIGTGAFGVVHRCRERSTGNIfAAKFIPVSHSVEKDLIRrEIDIMNQLHHQKLINLHDAFEDDDEMILILEFLSGGEL 8071
Cdd:cd05114     9 MKELGSGLFGVVRLGKWRAQYKV-AIKAIREGAMSEEDFIE-EAKVMMKLTHPKLVQLYGVCTQQKPIYIVTEFMENGCL 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 8072 FERITAEGYVMTEAEVINYMRQICEGIRHMHEQNIIHLDIKPENimCQTRSSTNVKLIDFGLATRLDPNEVVkiTTGTAE 8151
Cdd:cd05114    87 LNYLRQRRGKLSRDMLLSMCQDVCEGMEYLERNNFIHRDLAARN--CLVNDTGVVKVSDFGMTRYVLDDQYT--SSSGAK 162
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....
gi 281359561 8152 F----AAPEIVNREPVGFYTDMWATGVLSY-VLLSGLSPFAGDNDVQTLKNVKA 8200
Cdd:cd05114   163 FpvkwSPPEVFNYSKFSSKSDVWSFGVLMWeVFTEGKMPFESKSNYEVVEMVSR 216
PKc_MEK1 cd06650
Catalytic domain of the dual-specificity Protein Kinase, Mitogen-Activated Protein (MAP) ...
7987-8244 5.20e-14

Catalytic domain of the dual-specificity Protein Kinase, Mitogen-Activated Protein (MAP)/Extracellular signal-Regulated Kinase (ERK) Kinase 1; PKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine (ST) or tyrosine residues on protein substrates. MEK1 is a dual-specificity PK and a MAPK kinase (MAPKK or MKK) that phosphorylates and activates the downstream targets, ERK1 and ERK2, on specific threonine and tyrosine residues. The ERK cascade starts with extracellular signals including growth factors, hormones, and neurotransmitters, which act through receptors and ion channels to initiate intracellular signaling that leads to the activation at the MAPKKK (Raf-1 or MOS) level, which leads to the transmission of signals to MEK1, and finally to ERK1/2. The ERK cascade plays an important role in cell proliferation, differentiation, oncogenic transformation, and cell cycle control, as well as in apoptosis and cell survival under certain conditions. Gain-of-function mutations in genes encoding ERK cascade proteins, including MEK1, cause cardiofaciocutaneous (CFC) syndrome, a condition leading to multiple congenital anomalies and mental retardation in patients. MEK1 also plays a role in cell cycle control. The MEK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270816 [Multi-domain]  Cd Length: 319  Bit Score: 77.40  E-value: 5.20e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 7987 DRYDILEEIGTGAFGVVHRCRERSTGNIFAAKFIpvsHSVEKDLIR----REIDIMNQLHHQKLINLHDAFEDDDEMILI 8062
Cdd:cd06650     5 DDFEKISELGAGNGGVVFKVSHKPSGLVMARKLI---HLEIKPAIRnqiiRELQVLHECNSPYIVGFYGAFYSDGEISIC 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 8063 LEFLSGGELFERITAEGYVmTEAEVINYMRQICEGIRHMHEQN-IIHLDIKPENIMCQTRSStnVKLIDFGLATRLdPNE 8141
Cdd:cd06650    82 MEHMDGGSLDQVLKKAGRI-PEQILGKVSIAVIKGLTYLREKHkIMHRDVKPSNILVNSRGE--IKLCDFGVSGQL-IDS 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 8142 VVKITTGTAEFAAPEIVNREPVGFYTDMWATGVLSYVLLSGLSPFAgDNDVQTLKNVKACDWDFD--------------- 8206
Cdd:cd06650   158 MANSFVGTRSYMSPERLQGTHYSVQSDIWSMGLSLVEMAVGRYPIP-PPDAKELELMFGCQVEGDaaetpprprtpgrpl 236
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 281359561 8207 -------------VESFKYI-------------SEEAKDFIRKLLVRNKEKRMTAHECLLHPWL 8244
Cdd:cd06650   237 ssygmdsrppmaiFELLDYIvnepppklpsgvfSLEFQDFVNKCLIKNPAERADLKQLMVHAFI 300
FN3 smart00060
Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, ...
5370-5452 5.44e-14

Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, fibronectin. The tenth fibronectin type III repeat contains a RGD cell recognition sequence in a flexible loop between 2 strands. Type III modules are present in both extracellular and intracellular proteins.


Pssm-ID: 214495 [Multi-domain]  Cd Length: 83  Bit Score: 70.72  E-value: 5.44e-14
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561   5370 PSVPEGpLRNGDVSKNSIVLRWRPPKDDGG-SEITHYVVEKMDNEAmRWVPV-GDCTDTEIRADNLIENHDYSFRVRAVN 5447
Cdd:smart00060    1 PSPPSN-LRVTDVTSTSVTLSWEPPPDDGItGYIVGYRVEYREEGS-EWKEVnVTPSSTSYTLTGLKPGTEYEFRVRAVN 78

                    ....*
gi 281359561   5448 KQGQS 5452
Cdd:smart00060   79 GAGEG 83
PTKc_Lck_Blk cd05067
Catalytic domain of the Protein Tyrosine Kinases, Lymphocyte-specific kinase and Blk; PTKs ...
7991-8199 5.58e-14

Catalytic domain of the Protein Tyrosine Kinases, Lymphocyte-specific kinase and Blk; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Lck and Blk are members of the Src subfamily of proteins, which are cytoplasmic (or non-receptor) PTKs. Lck is expressed in T-cells and natural killer cells. It plays a critical role in T-cell maturation, activation, and T-cell receptor (TCR) signaling. Lck phosphorylates ITAM (immunoreceptor tyr activation motif) sequences on several subunits of TCRs, leading to the activation of different second messenger cascades. Phosphorylated ITAMs serve as binding sites for other signaling factor such as Syk and ZAP-70, leading to their activation and propagation of downstream events. In addition, Lck regulates drug-induced apoptosis by interfering with the mitochondrial death pathway. The apototic role of Lck is independent of its primary function in T-cell signaling. Blk is expressed specifically in B-cells. It is involved in pre-BCR (B-cell receptor) signaling. Src kinases contain an N-terminal SH4 domain with a myristoylation site, followed by SH3 and SH2 domains, a tyr kinase domain, and a regulatory C-terminal region containing a conserved tyr. They are activated by autophosphorylation at the tyr kinase domain, but are negatively regulated by phosphorylation at the C-terminal tyr by Csk (C-terminal Src Kinase). The Lck/Blk subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270652 [Multi-domain]  Cd Length: 264  Bit Score: 76.08  E-value: 5.58e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 7991 ILEEIGTGAFGVVHRCRERSTGNIFAAKFIPVSHSVEKDLirREIDIMNQLHHQKLINLHdAFEDDDEMILILEFLSGGE 8070
Cdd:cd05067    11 LVERLGAGQFGEVWMGYYNGHTKVAIKSLKQGSMSPDAFL--AEANLMKQLQHQRLVRLY-AVVTQEPIYIITEYMENGS 87
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 8071 LFERI-TAEGYVMTEAEVINYMRQICEGIRHMHEQNIIHLDIKPENIMcqTRSSTNVKLIDFGLATRLDPNEVVkiTTGT 8149
Cdd:cd05067    88 LVDFLkTPSGIKLTINKLLDMAAQIAEGMAFIEERNYIHRDLRAANIL--VSDTLSCKIADFGLARLIEDNEYT--AREG 163
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 281359561 8150 AEF----AAPEIVNREPVGFYTDMWATGV-LSYVLLSGLSPFAGDNDVQTLKNVK 8199
Cdd:cd05067   164 AKFpikwTAPEAINYGTFTIKSDVWSFGIlLTEIVTHGRIPYPGMTNPEVIQNLE 218
FN3 smart00060
Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, ...
7444-7527 5.77e-14

Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, fibronectin. The tenth fibronectin type III repeat contains a RGD cell recognition sequence in a flexible loop between 2 strands. Type III modules are present in both extracellular and intracellular proteins.


Pssm-ID: 214495 [Multi-domain]  Cd Length: 83  Bit Score: 70.72  E-value: 5.77e-14
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561   7444 PSAPTGPMgISYINKNSCMLNWRPPSYDGGLK-VSHYVIERKDvSSPHWITVSSTCKDTAFNVQGLIENQEYIFRVMAVN 7522
Cdd:smart00060    1 PSPPSNLR-VTDVTSTSVTLSWEPPPDDGITGyIVGYRVEYRE-EGSEWKEVNVTPSSTSYTLTGLKPGTEYEFRVRAVN 78

                    ....*
gi 281359561   7523 ENGMG 7527
Cdd:smart00060   79 GAGEG 83
I-set pfam07679
Immunoglobulin I-set domain;
228-320 6.42e-14

Immunoglobulin I-set domain;


Pssm-ID: 400151 [Multi-domain]  Cd Length: 90  Bit Score: 70.75  E-value: 6.42e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561   228 PTFTERPVIRQSEDGGNVTFECRCVGDPTPTVTWSHGETELNESNRYKMslTMDQKLYHiacLEISSVVSSDQGEYRAQA 307
Cdd:pfam07679    1 PKFTQKPKDVEVQEGESARFTCTVTGTPDPEVSWFKDGQPLRSSDRFKV--TYEGGTYT---LTISNVQPDDSGKYTCVA 75
                           90
                   ....*....|...
gi 281359561   308 KNKHGSGVATINL 320
Cdd:pfam07679   76 TNSAGEAEASAEL 88
PKc_LIMK_like_unk cd14156
Catalytic domain of an unknown subfamily of LIM domain kinase-like protein kinases; PKs ...
7995-8211 6.53e-14

Catalytic domain of an unknown subfamily of LIM domain kinase-like protein kinases; PKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine or tyrosine residues on protein substrates. This group is composed of uncharacterized proteins with similarity to LIMK and Testicular or testis-specific protein kinase (TESK). LIMKs are characterized as serine/threonine kinases (STKs) while TESKs are dual-specificity protein kinases. Both LIMK and TESK phosphorylate and inactivate cofilin, an actin depolymerizing factor, to induce the reorganization of the actin cytoskeleton. They are implicated in many cellular functions including cell spreading, motility, morphogenesis, meiosis, mitosis, and spermatogenesis. The LIMK-like subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271058 [Multi-domain]  Cd Length: 256  Bit Score: 76.02  E-value: 6.53e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 7995 IGTGAFGVVHRCRERSTGNIFAAKFipVSHSVEKDLIRREIDIMNQLHHQKLINLHDAFEDDDEMILILEFLSGGELFER 8074
Cdd:cd14156     1 IGSGFFSKVYKVTHGATGKVMVVKI--YKNDVDQHKIVREISLLQKLSHPNIVRYLGICVKDEKLHPILEYVSGGCLEEL 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 8075 ITAEGYVMTEAEVINYMRQICEGIRHMHEQNIIHLDIKPENimCQTRSSTNVK---LIDFGLATRL------DPNEVVKI 8145
Cdd:cd14156    79 LAREELPLSWREKVELACDISRGMVYLHSKNIYHRDLNSKN--CLIRVTPRGReavVTDFGLAREVgempanDPERKLSL 156
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 281359561 8146 tTGTAEFAAPEIVNREPVGFYTDMWATGVlsyVLLSGLSPFAGDNDVqtLKNVKacDWDFDVESFK 8211
Cdd:cd14156   157 -VGSAFWMAPEMLRGEPYDRKVDVFSFGI---VLCEILARIPADPEV--LPRTG--DFGLDVQAFK 214
FN3 cd00063
Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein ...
4779-4863 6.74e-14

Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein fibronectin. Its tenth fibronectin type III repeat contains an RGD cell recognition sequence in a flexible loop between 2 strands. Approximately 2% of all animal proteins contain the FN3 repeat; including extracellular and intracellular proteins, membrane spanning cytokine receptors, growth hormone receptors, tyrosine phosphatase receptors, and adhesion molecules. FN3-like domains are also found in bacterial glycosyl hydrolases.


Pssm-ID: 238020 [Multi-domain]  Cd Length: 93  Bit Score: 70.99  E-value: 6.74e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 4779 PSPPNGpLQISDVHKEGCHLKWKRPSDDGGTPIEYF-QIDKLEPETGCWIPSCRSTEPQVDVTGLSPGNEYKFRVSAVNA 4857
Cdd:cd00063     1 PSPPTN-LRVTDVTSTSVTLSWTPPEDDGGPITGYVvEYREKGSGDWKEVEVTPGSETSYTLTGLKPGTEYEFRVRAVNG 79

                  ....*.
gi 281359561 4858 EGESQP 4863
Cdd:cd00063    80 GGESPP 85
PKc_MEK2 cd06649
Catalytic domain of the dual-specificity Protein Kinase, Mitogen-Activated Protein (MAP) ...
7987-8181 8.97e-14

Catalytic domain of the dual-specificity Protein Kinase, Mitogen-Activated Protein (MAP)/Extracellular signal-Regulated Kinase (ERK) Kinase 2; PKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine (ST) or tyrosine residues on protein substrates. MEK2 is a dual-specificity PK and a MAPK kinase (MAPKK or MKK) that phosphorylates and activates the downstream targets, ERK1 and ERK2, on specific threonine and tyrosine residues. The ERK cascade starts with extracellular signals including growth factors, hormones, and neurotransmitters, which act through receptors and ion channels to initiate intracellular signaling that leads to the activation at the MAPKKK (Raf-1 or MOS) level, which leads to the transmission of signals to MEK2, and finally to ERK1/2. The ERK cascade plays an important role in cell proliferation, differentiation, oncogenic transformation, and cell cycle control, as well as in apoptosis and cell survival under certain conditions. Gain-of-function mutations in genes encoding ERK cascade proteins, including MEK2, cause cardiofaciocutaneous (CFC) syndrome, a condition leading to multiple congenital anomalies and mental retardation in patients. The MEK subfamily is part of a larger superfamily that includes the catalytic domains of other protein serine/threonine kinases, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 132980 [Multi-domain]  Cd Length: 331  Bit Score: 77.01  E-value: 8.97e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 7987 DRYDILEEIGTGAFGVVHRCRERSTGNIFAAKFIPVS-HSVEKDLIRREIDIMNQLHHQKLINLHDAFEDDDEMILILEF 8065
Cdd:cd06649     5 DDFERISELGAGNGGVVTKVQHKPSGLIMARKLIHLEiKPAIRNQIIRELQVLHECNSPYIVGFYGAFYSDGEISICMEH 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 8066 LSGGELfERITAEGYVMTEAEVINYMRQICEGIRHMHEQN-IIHLDIKPENIMCQTRSStnVKLIDFGLATRLdPNEVVK 8144
Cdd:cd06649    85 MDGGSL-DQVLKEAKRIPEEILGKVSIAVLRGLAYLREKHqIMHRDVKPSNILVNSRGE--IKLCDFGVSGQL-IDSMAN 160
                         170       180       190
                  ....*....|....*....|....*....|....*..
gi 281359561 8145 ITTGTAEFAAPEIVNREPVGFYTDMWATGvLSYVLLS 8181
Cdd:cd06649   161 SFVGTRSYMSPERLQGTHYSVQSDIWSMG-LSLVELA 196
FN3 cd00063
Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein ...
5664-5755 9.11e-14

Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein fibronectin. Its tenth fibronectin type III repeat contains an RGD cell recognition sequence in a flexible loop between 2 strands. Approximately 2% of all animal proteins contain the FN3 repeat; including extracellular and intracellular proteins, membrane spanning cytokine receptors, growth hormone receptors, tyrosine phosphatase receptors, and adhesion molecules. FN3-like domains are also found in bacterial glycosyl hydrolases.


Pssm-ID: 238020 [Multi-domain]  Cd Length: 93  Bit Score: 70.60  E-value: 9.11e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 5664 PSPPKGpLDITKITRDGCHLTWNVPDDDGGsPILHYIIEKMDLSRSTWS--DAGMSTHIVHDVTRLVHRKEYLFRVKAVN 5741
Cdd:cd00063     1 PSPPTN-LRVTDVTSTSVTLSWTPPEDDGG-PITGYVVEYREKGSGDWKevEVTPGSETSYTLTGLKPGTEYEFRVRAVN 78
                          90
                  ....*....|....
gi 281359561 5742 AIGESDPLEAVNTI 5755
Cdd:cd00063    79 GGGESPPSESVTVT 92
IgI_titin_I1-like cd20951
Immunoglobulin domain I1 of the titin I-band and similar proteins; a member of the I-set of ...
8632-8722 9.14e-14

Immunoglobulin domain I1 of the titin I-band and similar proteins; a member of the I-set of IgSF domains; The members here are composed of the immunoglobulin domain I1 of the titin I-band and similar proteins. Titin is a key component in the assembly and functioning of vertebrate striated muscles. By providing connections at the level of individual microfilaments, it contributes to the fine balance of forces between the two halves of the sarcomere. The Ig superfamily (IgSF) is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. The two sheets are linked together by a conserved disulfide bond between B strand and F strand. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. The Ig I1 domain of the titin I-band is a member of the I-set Ig domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand but lack a C" strand. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors, the hemolymph protein hemolin, the muscle proteins titin, telokin, and twitchin, the neuronal adhesion molecule axonin-1, and the signaling molecule semaphorin 4D that is involved in axonal guidance, immune function and angiogenesis.


Pssm-ID: 409543 [Multi-domain]  Cd Length: 94  Bit Score: 70.53  E-value: 9.14e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 8632 PEFTKPLHDLTIHDGEQLILTCYVKGDPEPQISWSKNGKSLS-SSDILDLRY--KNGIATLTINEVFPEDEGVITCTATN 8708
Cdd:cd20951     1 PEFIIRLQSHTVWEKSDAKLRVEVQGKPDPEVKWYKNGVPIDpSSIPGKYKIesEYGVHVLHIRRVTVEDSAVYSAVAKN 80
                          90
                  ....*....|....
gi 281359561 8709 SVGAVETKCKLTIQ 8722
Cdd:cd20951    81 IHGEASSSASVVVE 94
FN3 smart00060
Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, ...
3889-3971 9.66e-14

Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, fibronectin. The tenth fibronectin type III repeat contains a RGD cell recognition sequence in a flexible loop between 2 strands. Type III modules are present in both extracellular and intracellular proteins.


Pssm-ID: 214495 [Multi-domain]  Cd Length: 83  Bit Score: 70.34  E-value: 9.66e-14
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561   3889 PSKPKGpLAVSNVTAETLHLKWEKPEDDGGDPIEQYLVERMDTETGRWVPVLTT-KTPEADVTGLTEGKEYLFRVKAVNS 3967
Cdd:smart00060    1 PSPPSN-LRVTDVTSTSVTLSWEPPPDDGITGYIVGYRVEYREEGSEWKEVNVTpSSTSYTLTGLKPGTEYEFRVRAVNG 79

                    ....
gi 281359561   3968 EGES 3971
Cdd:smart00060   80 AGEG 83
IgI_Myotilin_C_like cd05744
Immunoglobulin (Ig)-like domain of myotilin, palladin, and myopalladin; member of the I-set of ...
8632-8721 1.14e-13

Immunoglobulin (Ig)-like domain of myotilin, palladin, and myopalladin; member of the I-set of Ig superfamily (IgSF) domains; The members here are composed of the immunoglobulin (Ig)-like domain in myotilin, palladin, and myopalladin. Myotilin, palladin, and myopalladin function as scaffolds that regulate actin organization. Myotilin and myopalladin are most abundant in skeletal and cardiac muscle; palladin is ubiquitously expressed in the organs of developing vertebrates and plays a key role in cellular morphogenesis. The three family members each interact with specific molecular partners with all three binding to alpha-actinin; In addition, palladin also binds to vasodilator-stimulated phosphoprotein (VASP) and ezrin, myotilin binds to filamin and actin, and myopalladin also binds to nebulin and cardiac ankyrin repeat protein (CARP). This group belongs to the I-set of IgSF domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand, but lack a C" strand.


Pssm-ID: 409405 [Multi-domain]  Cd Length: 91  Bit Score: 70.22  E-value: 1.14e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 8632 PEFTKPLHDLTIHDGEQLILTCYVKGDPEPQISWSKNGKSL--SSSDILDLRyKNGIATLTINEVFPEDEGVITCTATNS 8709
Cdd:cd05744     1 PHFLQAPGDLEVQEGRLCRFDCKVSGLPTPDLFWQLNGKPVrpDSAHKMLVR-ENGRHSLIIEPVTKRDAGIYTCIARNR 79
                          90
                  ....*....|..
gi 281359561 8710 VGAVETKCKLTI 8721
Cdd:cd05744    80 AGENSFNAELVV 91
FN3 COG3401
Fibronectin type 3 domain [General function prediction only];
2110-2562 1.20e-13

Fibronectin type 3 domain [General function prediction only];


Pssm-ID: 442628 [Multi-domain]  Cd Length: 603  Bit Score: 78.51  E-value: 1.20e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 2110 DVYQTSCVVSFNPPSDDGGTPITKYVIERQDLSKKHGWESVAEVLPSEPCLKKIDDLIPKKQYRFRIRAVNAIGQSDPAt 2189
Cdd:COG3401   143 LGAGLYGVDGANASGTTASSVAGAGVVVSPDTSATAAVATTSLTVTSTTLVDGGGDIEPGTTYYYRVAATDTGGESAPS- 221
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 2190 fkNTILAKDPWDEPGKPKAVDLTDWDKDHADLKWEAPETDGgdpITAYIVEYKEKFSNDWVsgkEVDGDARTATVD-GLK 2268
Cdd:COG3401   222 --NEVSVTTPTTPPSAPTGLTATADTPGSVTLSWDPVTESD---ATGYRVYRSNSGDGPFT---KVATVTTTSYTDtGLT 293
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 2269 EGQQYEFRVRAVNRAG-PGEPSDKtksiiakcrfvkpfivgeglknVTVKKgqtirfdikyDGEPEPAATWVKGTDNLkf 2347
Cdd:COG3401   294 NGTTYYYRVTAVDAAGnESAPSNV----------------------VSVTT----------DLTPPAAPSGLTATAVG-- 339
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 2348 dnqricldqlerNSSITIkksvrkdtgkyklvlsnssgtieseaqvvvldrplppggpfepeeirashikmKWKRPDDDG 2427
Cdd:COG3401   340 ------------SSSITL-----------------------------------------------------SWTASSDAD 354
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 2428 gceISGYALERMDEETGRWIPAGEVgPNETSFDFKGLTPNKKYKFRVKAINKEG-ESEPLETFDAIVARNPYDPPS--PP 2504
Cdd:COG3401   355 ---VTGYNVYRSTSGGGTYTKIAET-VTTTSYTDTGLTPGTTYYYKVTAVDAAGnESAPSEEVSATTASAASGESLtaSV 430
                         410       420       430       440       450
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 281359561 2505 SQPVIDDYDNKSVLLKWKRPPSDGGRPITH-YIVEIKDKFAPSWSEVAKTDDPNPECNV 2562
Cdd:COG3401   431 DAVPLTDVAGATAAASAASNPGVSAAVLADgGDTGNAVPFTTTSSTVTATTTDTTTANL 489
IgI_titin_I1-like cd20951
Immunoglobulin domain I1 of the titin I-band and similar proteins; a member of the I-set of ...
8437-8526 1.27e-13

Immunoglobulin domain I1 of the titin I-band and similar proteins; a member of the I-set of IgSF domains; The members here are composed of the immunoglobulin domain I1 of the titin I-band and similar proteins. Titin is a key component in the assembly and functioning of vertebrate striated muscles. By providing connections at the level of individual microfilaments, it contributes to the fine balance of forces between the two halves of the sarcomere. The Ig superfamily (IgSF) is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. The two sheets are linked together by a conserved disulfide bond between B strand and F strand. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. The Ig I1 domain of the titin I-band is a member of the I-set Ig domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand but lack a C" strand. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors, the hemolymph protein hemolin, the muscle proteins titin, telokin, and twitchin, the neuronal adhesion molecule axonin-1, and the signaling molecule semaphorin 4D that is involved in axonal guidance, immune function and angiogenesis.


Pssm-ID: 409543 [Multi-domain]  Cd Length: 94  Bit Score: 70.14  E-value: 1.27e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 8437 PSFTFLLRPRVMQARDTCKLLCCLSGKPVPNVRWYKDGRELS------KYEYamtHS-DGVVTMEIIDCKPSDSGKYSCK 8509
Cdd:cd20951     1 PEFIIRLQSHTVWEKSDAKLRVEVQGKPDPEVKWYKNGVPIDpssipgKYKI---ESeYGVHVLHIRRVTVEDSAVYSAV 77
                          90
                  ....*....|....*..
gi 281359561 8510 ATNCHGTDETDCVVIVE 8526
Cdd:cd20951    78 AKNIHGEASSSASVVVE 94
I-set pfam07679
Immunoglobulin I-set domain;
545-636 1.31e-13

Immunoglobulin I-set domain;


Pssm-ID: 400151 [Multi-domain]  Cd Length: 90  Bit Score: 69.98  E-value: 1.31e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561   545 FIEKPRIVSENNGKLVIMECKVKADPKPDVIWFRNGEVIKESNKIKtfIEQRGDQYyiKLELLDPQLEDSGLYKCNIKNT 624
Cdd:pfam07679    3 FTQKPKDVEVQEGESARFTCTVTGTPDPEVSWFKDGQPLRSSDRFK--VTYEGGTY--TLTISNVQPDDSGKYTCVATNS 78
                           90
                   ....*....|..
gi 281359561   625 LGELNANLTLNI 636
Cdd:pfam07679   79 AGEAEASAELTV 90
FN3 smart00060
Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, ...
5175-5258 1.37e-13

Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, fibronectin. The tenth fibronectin type III repeat contains a RGD cell recognition sequence in a flexible loop between 2 strands. Type III modules are present in both extracellular and intracellular proteins.


Pssm-ID: 214495 [Multi-domain]  Cd Length: 83  Bit Score: 69.57  E-value: 1.37e-13
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561   5175 PTKPGTPTIKDFDKEFVDLEWTRPEADGG-SPITGYVVEKRDKfSPDWEKCaEISDDITNAHVPDLIEGLKYEFRVRAVN 5253
Cdd:smart00060    1 PSPPSNLRVTDVTSTSVTLSWEPPPDDGItGYIVGYRVEYREE-GSEWKEV-NVTPSSTSYTLTGLKPGTEYEFRVRAVN 78

                    ....*
gi 281359561   5254 KAGPG 5258
Cdd:smart00060   79 GAGEG 83
PTKc_Ack_like cd05040
Catalytic domain of the Protein Tyrosine Kinase, Activated Cdc42-associated kinase; PTKs ...
7993-8198 1.38e-13

Catalytic domain of the Protein Tyrosine Kinase, Activated Cdc42-associated kinase; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. This subfamily includes Ack1, thirty-eight-negative kinase 1 (Tnk1), and similar proteins. They are cytoplasmic (or nonreceptor) PTKs containing an N-terminal catalytic domain, an SH3 domain, a Cdc42-binding CRIB domain, and a proline-rich region. They are mainly expressed in brain and skeletal tissues and are involved in the regulation of cell adhesion and growth, receptor degradation, and axonal guidance. Ack1 is also associated with androgen-independent prostate cancer progression. Tnk1 regulates TNFalpha signaling and may play an important role in cell death. The Ack-like subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270636 [Multi-domain]  Cd Length: 258  Bit Score: 75.07  E-value: 1.38e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 7993 EEIGTGAFGVVHRCrERSTGNifaAKFIPVSHSVEK----------DLIRREIDIMNQLHHQKLINLHDAFEDDdEMILI 8062
Cdd:cd05040     1 EKLGDGSFGVVRRG-EWTTPS---GKVIQVAVKCLKsdvlsqpnamDDFLKEVNAMHSLDHPNLIRLYGVVLSS-PLMMV 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 8063 LEFLSGGELFERITAEGYVMTEAEVINYMRQICEGIRHMHEQNIIHLDIKPENIMCQTRSStnVKLIDFGLATRLDPNEV 8142
Cdd:cd05040    76 TELAPLGSLLDRLRKDQGHFLISTLCDYAVQIANGMAYLESKRFIHRDLAARNILLASKDK--VKIGDFGLMRALPQNED 153
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 281359561 8143 VKITTGTAE--FA--APEIVNREPVGFYTDMWATGVLSYVLLS-GLSPFAGDNDVQTLKNV 8198
Cdd:cd05040   154 HYVMQEHRKvpFAwcAPESLKTRKFSHASDVWMFGVTLWEMFTyGEEPWLGLNGSQILEKI 214
fn3 pfam00041
Fibronectin type III domain;
5073-5159 1.67e-13

Fibronectin type III domain;


Pssm-ID: 394996 [Multi-domain]  Cd Length: 85  Bit Score: 69.37  E-value: 1.67e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561  5073 PAPPNgpLKVDEINSESCTLHWNPPDDDGGqPIDNYVVEKLDETTGRWIPAGETDGPVTALKVGGLTPGHKYKFRVRAKN 5152
Cdd:pfam00041    1 SAPSN--LTVTDVTSTSLTVSWTPPPDGNG-PITGYEVEYRPKNSGEPWNEITVPGTTTSVTLTGLKPGTEYEVRVQAVN 77

                   ....*..
gi 281359561  5153 RQGTSEP 5159
Cdd:pfam00041   78 GGGEGPP 84
PKc_MEK cd06615
Catalytic domain of the dual-specificity Protein Kinase, Mitogen-Activated Protein (MAP) ...
7987-8244 2.22e-13

Catalytic domain of the dual-specificity Protein Kinase, Mitogen-Activated Protein (MAP)/Extracellular signal-Regulated Kinase (ERK) Kinase; PKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine (ST) or tyrosine residues on protein substrates. MEK1 and MEK2 are MAPK kinases (MAPKKs or MKKs), and are dual-specificity PKs that phosphorylate and activate the downstream targets, ERK1 and ERK2, on specific threonine and tyrosine residues. The ERK cascade starts with extracellular signals including growth factors, hormones, and neurotransmitters, which act through receptors and ion channels to initiate intracellular signaling that leads to the activation at the MAPKKK (Raf-1 or MOS) level, which leads to the transmission of signals to MEK1/2, and finally to ERK1/2. The ERK cascade plays an important role in cell proliferation, differentiation, oncogenic transformation, and cell cycle control, as well as in apoptosis and cell survival under certain conditions. This cascade has also been implicated in synaptic plasticity, migration, morphological determination, and stress response immunological reactions. Gain-of-function mutations in genes encoding ERK cascade proteins, including MEK1/2, cause cardiofaciocutaneous (CFC) syndrome, a condition leading to multiple congenital anomalies and mental retardation in patients. The MEK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 132946 [Multi-domain]  Cd Length: 308  Bit Score: 75.16  E-value: 2.22e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 7987 DRYDILEEIGTGAFGVVHRCRERSTGNIFAAKFI--PVSHSVEKDLIRrEIDIMNQLHHQKLINLHDAFEDDDEMILILE 8064
Cdd:cd06615     1 DDFEKLGELGAGNGGVVTKVLHRPSGLIMARKLIhlEIKPAIRNQIIR-ELKVLHECNSPYIVGFYGAFYSDGEISICME 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 8065 FLSGGELferitaeGYVMTEAEVI--NYMRQIC----EGIRHMHEQ-NIIHLDIKPENIMCQTRSstNVKLIDFGLATRL 8137
Cdd:cd06615    80 HMDGGSL-------DQVLKKAGRIpeNILGKISiavlRGLTYLREKhKIMHRDVKPSNILVNSRG--EIKLCDFGVSGQL 150
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 8138 dPNEVVKITTGTAEFAAPEIVNREPVGFYTDMWATGvLSYVLL------------SGLSPFAGDNDV-------QTLKNV 8198
Cdd:cd06615   151 -IDSMANSFVGTRSYMSPERLQGTHYTVQSDIWSLG-LSLVEMaigrypipppdaKELEAMFGRPVSegeakesHRPVSG 228
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 281359561 8199 KACD----------WDFDVES------FKYISEEAKDFIRKLLVRNKEKRMTAHECLLHPWL 8244
Cdd:cd06615   229 HPPDsprpmaifelLDYIVNEpppklpSGAFSDEFQDFVDKCLKKNPKERADLKELTKHPFI 290
IgI_4_MYLK-like cd20976
Fourth Ig-like domain from smooth muscle myosin light chain kinase and similar domains ; a ...
8632-8721 2.33e-13

Fourth Ig-like domain from smooth muscle myosin light chain kinase and similar domains ; a member of the I-set of IgSF domains; The members here are composed of the fourth immunoglobulin (Ig)-like domain from smooth muscle myosin light chain kinase (MYLK) and similar domains. The Ig superfamily (IgSF) is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. Unlike the V-set, one of the distinctive features of I-set domains is the lack of a C" strand. The structure of this group shows that the fourth Ig-like domain from myosin light chain kinase lacks this strand and thus belongs to the I-set of the IgSF. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors, the hemolymph protein hemolin, the muscle proteins titin, telokin, and twitchin, the neuronal adhesion molecule axonin-1, and the signaling molecule semaphorin 4D that is involved in axonal guidance, immune function and angiogenesis.


Pssm-ID: 409568 [Multi-domain]  Cd Length: 90  Bit Score: 69.20  E-value: 2.33e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 8632 PEFTKPLHDLTIHDGEQLILTCYVKGDPEPQISWSKNGKSLSSsDILDLRYKNGIATLTINEVFPEDEGVITCTATNSVG 8711
Cdd:cd20976     2 PSFSSVPKDLEAVEGQDFVAQCSARGKPVPRITWIRNAQPLQY-AADRSTCEAGVGELHIQDVLPEDHGTYTCLAKNAAG 80
                          90
                  ....*....|
gi 281359561 8712 AVETKCKLTI 8721
Cdd:cd20976    81 QVSCSAWVTV 90
IgI_telokin-like cd20973
immunoglobulin-like domain of telokin and similar proteins; a member of the I-set of IgSF ...
8635-8721 2.36e-13

immunoglobulin-like domain of telokin and similar proteins; a member of the I-set of IgSF domains; The members here are composed of the immunoglobulin (Ig) domain in telokin, the C-terminal domain of myosin light chain kinase which is identical to telokin, and similar proteins. The Ig superfamily (IgSF) is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. Unlike the V-set, one of the distinctive features of I-set domains is the lack of a C" strand. The structure of the telokin Ig domain lacks this strand and thus it belongs to the I-set of the IgSF. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors, the hemolymph protein hemolin, the muscle proteins titin, telokin, and twitchin, the neuronal adhesion molecule axonin-1, and the signaling molecule semaphorin 4D that is involved in axonal guidance, immune function and angiogenesis.


Pssm-ID: 409565 [Multi-domain]  Cd Length: 88  Bit Score: 69.14  E-value: 2.36e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 8635 TKPLHDLTIHDGEQLILTCYVKGDPEPQISWSKNGKSLSSSDILDLRY-KNGIATLTINEVFPEDEGVITCTATNSVGAV 8713
Cdd:cd20973     1 IQTLRDKEVVEGSAARFDCKVEGYPDPEVKWMKDDNPIVESRRFQIDQdEDGLCSLIISDVCGDDSGKYTCKAVNSLGEA 80

                  ....*...
gi 281359561 8714 ETKCKLTI 8721
Cdd:cd20973    81 TCSAELTV 88
STKc_HIPK3 cd14229
Catalytic domain of the Serine/Threonine Kinase, Homeodomain-Interacting Protein Kinase 3; ...
7989-8188 2.41e-13

Catalytic domain of the Serine/Threonine Kinase, Homeodomain-Interacting Protein Kinase 3; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. HIPK3 is a Fas-interacting protein that induces FADD (Fas-associated death domain) phosphorylation and mediates FasL-induced JNK activation. Overexpression of HIPK3 does not affect cell death, however its expression in prostate cancer cells contributes to increased resistance to Fas receptor-mediated apoptosis. HIPK3 also plays a role in regulating steroidogenic gene expression. In response to cAMP, HIPK3 activates the phosphorylation of JNK and c-Jun, leading to increased activity of the transcription factor SF-1 (Steroidogenic factor 1), a key regulator for steroid biosynthesis in the gonad and adrenal gland. HIPKs, originally identified by their ability to bind homeobox factors, are nuclear proteins containing catalytic kinase and homeobox-interacting domains as well as a PEST region overlapping with the speckle-retention signal (SRS). The HIPK3 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase (PI3K).


Pssm-ID: 271131 [Multi-domain]  Cd Length: 330  Bit Score: 75.45  E-value: 2.41e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 7989 YDILEEIGTGAFGVVHRCRERSTGNIFAAKFIPvSHSVEKDLIRREIDIMNQLHHQ-----KLINLHDAFEDDDEMILIL 8063
Cdd:cd14229     2 YEVLDFLGRGTFGQVVKCWKRGTNEIVAVKILK-NHPSYARQGQIEVGILARLSNEnadefNFVRAYECFQHRNHTCLVF 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 8064 EFLSgGELFERITAEGYVMTEAEVIN-YMRQICEGIRHMHEQNIIHLDIKPENIMC--QTRSSTNVKLIDFGLATRLDpN 8140
Cdd:cd14229    81 EMLE-QNLYDFLKQNKFSPLPLKVIRpILQQVATALKKLKSLGLIHADLKPENIMLvdPVRQPYRVKVIDFGSASHVS-K 158
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*...
gi 281359561 8141 EVVKITTGTAEFAAPEIVNREPVGFYTDMWATGVLSYVLLSGLSPFAG 8188
Cdd:cd14229   159 TVCSTYLQSRYYRAPEIILGLPFCEAIDMWSLGCVIAELFLGWPLYPG 206
PTKc_Jak3_rpt2 cd05081
Catalytic (repeat 2) domain of the Protein Tyrosine Kinase, Janus kinase 3; PTKs catalyze the ...
7992-8181 2.50e-13

Catalytic (repeat 2) domain of the Protein Tyrosine Kinase, Janus kinase 3; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Jak3 is expressed only in hematopoietic cells. It binds the shared receptor subunit common gamma chain and thus, is essential in the signaling of cytokines that use it such as IL-2, IL-4, IL-7, IL-9, IL-15, and IL-21. Jak3 is important in lymphoid development and myeloid cell differentiation. Inactivating mutations in Jak3 have been reported in humans with severe combined immunodeficiency (SCID). Jak3 is a member of the Janus kinase (Jak) subfamily of proteins, which are cytoplasmic (or nonreceptor) PTKs containing an N-terminal FERM domain, followed by a Src homology 2 (SH2) domain, a pseudokinase domain, and a C-terminal catalytic tyr kinase domain. Jaks are crucial for cytokine receptor signaling. They are activated by autophosphorylation upon cytokine-induced receptor aggregation, and subsequently trigger downstream signaling events such as the phosphorylation of signal transducers and activators of transcription (STATs). The PTKc family is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270665 [Multi-domain]  Cd Length: 283  Bit Score: 74.54  E-value: 2.50e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 7992 LEEIGTGAFGVVHRCRER----STGNIFAAKFIPVSHSVEKDLIRREIDIMNQLHHQKLINLHDAF--EDDDEMILILEF 8065
Cdd:cd05081     9 ISQLGKGNFGSVELCRYDplgdNTGALVAVKQLQHSGPDQQRDFQREIQILKALHSDFIVKYRGVSygPGRRSLRLVMEY 88
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 8066 LSGGELFERITAEGYVMTEAEVINYMRQICEGIRHMHEQNIIHLDIKPENIMCQTRssTNVKLIDFGLATRL--DPNEVV 8143
Cdd:cd05081    89 LPSGCLRDFLQRHRARLDASRLLLYSSQICKGMEYLGSRRCVHRDLAARNILVESE--AHVKIADFGLAKLLplDKDYYV 166
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|
gi 281359561 8144 KITTGTAE--FAAPEIVNREPVGFYTDMWATGVLSYVLLS 8181
Cdd:cd05081   167 VREPGQSPifWYAPESLSDNIFSRQSDVWSFGVVLYELFT 206
FN3 smart00060
Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, ...
3400-3481 2.56e-13

Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, fibronectin. The tenth fibronectin type III repeat contains a RGD cell recognition sequence in a flexible loop between 2 strands. Type III modules are present in both extracellular and intracellular proteins.


Pssm-ID: 214495 [Multi-domain]  Cd Length: 83  Bit Score: 68.80  E-value: 2.56e-13
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561   3400 PPGLPELEDWDEHHVKLKWEPPIRDGG-SPITNYIIEvmDKDSGEFVKAVETDSPVCKGVVKKLEEGQQYKFRVRAVNKA 3478
Cdd:smart00060    3 PPSNLRVTDVTSTSVTLSWEPPPDDGItGYIVGYRVE--YREEGSEWKEVNVTPSSTSYTLTGLKPGTEYEFRVRAVNGA 80

                    ...
gi 281359561   3479 GPS 3481
Cdd:smart00060   81 GEG 83
fn3 pfam00041
Fibronectin type III domain;
6757-6840 2.56e-13

Fibronectin type III domain;


Pssm-ID: 394996 [Multi-domain]  Cd Length: 85  Bit Score: 68.98  E-value: 2.56e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561  6757 PGIPHGIDSTEDSITIAWTKPKhDGGSPITGYIIEKRLLSDDKWTKAVHALCPDLSCKIPNLIENAEYEFRVAAVNAAGQ 6836
Cdd:pfam00041    3 PSNLTVTDVTSTSLTVSWTPPP-DGNGPITGYEVEYRPKNSGEPWNEITVPGTTTSVTLTGLKPGTEYEVRVQAVNGGGE 81

                   ....
gi 281359561  6837 SAYS 6840
Cdd:pfam00041   82 GPPS 85
FN3 smart00060
Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, ...
3594-3676 2.66e-13

Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, fibronectin. The tenth fibronectin type III repeat contains a RGD cell recognition sequence in a flexible loop between 2 strands. Type III modules are present in both extracellular and intracellular proteins.


Pssm-ID: 214495 [Multi-domain]  Cd Length: 83  Bit Score: 68.80  E-value: 2.66e-13
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561   3594 PGKPKGpLQVNDITKHSCKLKWEKPDDDGG-SPIDYYEIEKLDPHTGQWLPCGKSTEPEAKVIGLHEGKAYKFRVRAVNK 3672
Cdd:smart00060    1 PSPPSN-LRVTDVTSTSVTLSWEPPPDDGItGYIVGYRVEYREEGSEWKEVNVTPSSTSYTLTGLKPGTEYEFRVRAVNG 79

                    ....
gi 281359561   3673 EGES 3676
Cdd:smart00060   80 AGEG 83
PK_TRB1 cd14023
Pseudokinase domain of Tribbles Homolog 1; The pseudokinase domain shows similarity to protein ...
8082-8244 2.73e-13

Pseudokinase domain of Tribbles Homolog 1; The pseudokinase domain shows similarity to protein kinases but lacks crucial residues for catalytic activity. TRB1 interacts directly with the mitogen activated protein kinase (MAPK) kinase MKK4, an activator of JNK. It regulates vascular smooth muscle cell proliferation and chemotaxis through the JNK signaling pathway. It is found to be down-regulated in human acute myeloid leukaemia (AML) and may play a role in the pathogenesis of the disease. It has also been identified as a potential biomarker for antibody-mediated allograft failure. TRB1 is one of three Tribbles Homolog (TRB) proteins present in vertebrates that are encoded by three separate genes. TRB proteins interact with many proteins involved in signalling pathways. They play scaffold-like regulatory functions and affect many cellular processes such as mitosis, apoptosis, and gene expression. The TRB1 subfamily is part of a larger superfamily that includes the catalytic domains of serine/threonine kinases, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270925 [Multi-domain]  Cd Length: 242  Bit Score: 73.54  E-value: 2.73e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 8082 MTEAEVINYMRQICEGIRHMHEQNIIHLDIKPENIMCQTRSSTNVKLIDFGLATRLDPNE-VVKITTGTAEFAAPEIVNr 8160
Cdd:cd14023    81 LREEEAARLFKQIVSAVAHCHQSAIVLGDLKLRKFVFSDEERTQLRLESLEDTHIMKGEDdALSDKHGCPAYVSPEILN- 159
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 8161 ePVGFYT----DMWATGVLSYVLLSGLSPFAgDNDVQTL----KNVKACDWDfdvesfkYISEEAKDFIRKLLVRNKEKR 8232
Cdd:cd14023   160 -TTGTYSgksaDVWSLGVMLYTLLVGRYPFH-DSDPSALfskiRRGQFCIPD-------HVSPKARCLIRSLLRREPSER 230
                         170
                  ....*....|..
gi 281359561 8233 MTAHECLLHPWL 8244
Cdd:cd14023   231 LTAPEILLHPWF 242
STKc_Bub1_BubR1 cd13981
Catalytic domain of the Serine/Threonine kinases, Spindle assembly checkpoint proteins Bub1 ...
7989-8182 3.22e-13

Catalytic domain of the Serine/Threonine kinases, Spindle assembly checkpoint proteins Bub1 and BubR1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily is composed of Bub1 (Budding uninhibited by benzimidazoles 1), BubR1, and similar proteins. They contain an N-terminal Bub1/Mad3 homology domain essential for Cdc20 binding and a C-terminal kinase domain. Bub1 and BubR1 are involved in SAC, a surveillance system that delays metaphase to anaphase transition by blocking the activity of APC/C (the anaphase promoting complex) until all chromosomes achieve proper attachments to the mitotic spindle, to avoid chromosome missegregation. Impaired SAC leads to genomic instabilities and tumor development. Bub1 and BubR1 facilitate the localization of SAC proteins to kinetochores and regulate kinetochore-microtubule (K-MT) attachments. Repression studies of Bub1 and BubR1 show that they exert an additive effect in misalignment phenotypes and may function cooperatively or in parallel pathways in regulating K-MT attachments. The Bub1/BubR1 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270883 [Multi-domain]  Cd Length: 298  Bit Score: 74.70  E-value: 3.22e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 7989 YDILEEIGTGAFGVVHRC---RERSTGNIFAAKfipvshsVEKDLIRREIDIMNQLHhQKLINL---------HDAFEDD 8056
Cdd:cd13981     2 YVISKELGEGGYASVYLAkddDEQSDGSLVALK-------VEKPPSIWEFYICDQLH-SRLKNSrlresisgaHSAHLFQ 73
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 8057 DEMILILEFLSGGELFERI----TAEGYVMTEAEVINYMRQICEGIRHMHEQNIIHLDIKPENIMCQTR----------- 8121
Cdd:cd13981    74 DESILVMDYSSQGTLLDVVnkmkNKTGGGMDEPLAMFFTIELLKVVEALHEVGIIHGDIKPDNFLLRLEicadwpgegen 153
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 281359561 8122 --SSTNVKLIDFGLA---TRLDPNEVVKITTGTAEFAAPEIVNREPVGFYTDMWATGVLSYVLLSG 8182
Cdd:cd13981   154 gwLSKGLKLIDFGRSidmSLFPKNQSFKADWHTDSFDCIEMREGRPWTYQIDYFGIAATIHVMLFG 219
STKc_JNK1 cd07875
Catalytic domain of the Serine/Threonine Kinase, c-Jun N-terminal Kinase 1; STKs catalyze the ...
7981-8244 3.33e-13

Catalytic domain of the Serine/Threonine Kinase, c-Jun N-terminal Kinase 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. JNK1 is expressed in every cell and tissue type. It specifically binds with JAMP (JNK1-associated membrane protein), which regulates the duration of JNK1 activity in response to stimuli. Specific JNK1 substrates include Itch and SG10, which are implicated in Th2 responses and airway inflammation, and microtubule dynamics and axodendritic length, respectively. Mice deficient in JNK1 are protected against arthritis, obesity, type 2 diabetes, cardiac cell death, and non-alcoholic liver disease, suggesting that JNK1 may play roles in the pathogenesis of these diseases. Initially, it was thought that JNK1 and JNK2 were functionally redundant as mice deficient in either genes could survive but disruption of both genes resulted in lethality. However, recent studies have shown that JNK1 and JNK2 perform distinct functions through specific binding partners and substrates. JNKs are mitogen-activated protein kinases that are involved in many stress-activated responses including those during inflammation, neurodegeneration, apoptosis, and persistent pain sensitization, among others. The JNK1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 143380 [Multi-domain]  Cd Length: 364  Bit Score: 75.47  E-value: 3.33e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 7981 SQQSVYDRYDILEEIGTGAFGVVHRCRERSTGNIFAAKFI--PVSHSVEKDLIRREIDIMNQLHHQKLINLHDAF----- 8053
Cdd:cd07875    18 STFTVLKRYQNLKPIGSGAQGIVCAAYDAILERNVAIKKLsrPFQNQTHAKRAYRELVLMKCVNHKNIIGLLNVFtpqks 97
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 8054 -EDDDEMILILEFLSGgELFERITAEgyvmTEAEVINYM-RQICEGIRHMHEQNIIHLDIKPENIMcqTRSSTNVKLIDF 8131
Cdd:cd07875    98 lEEFQDVYIVMELMDA-NLCQVIQME----LDHERMSYLlYQMLCGIKHLHSAGIIHRDLKPSNIV--VKSDCTLKILDF 170
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 8132 GLATRLDPNEVVKITTGTAEFAAPEIVNREPVGFYTDMWATGVLSYVLLSGLSPFAGDNDVQTLKNV------------- 8198
Cdd:cd07875   171 GLARTAGTSFMMTPYVVTRYYRAPEVILGMGYKENVDIWSVGCIMGEMIKGGVLFPGTDHIDQWNKVieqlgtpcpefmk 250
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 281359561 8199 --------------KACDWDF-----------DVESFKYISEEAKDFIRKLLVRNKEKRMTAHECLLHPWL 8244
Cdd:cd07875   251 klqptvrtyvenrpKYAGYSFeklfpdvlfpaDSEHNKLKASQARDLLSKMLVIDASKRISVDEALQHPYI 321
STKc_JNK cd07850
Catalytic domain of the Serine/Threonine Kinase, c-Jun N-terminal Kinase; STKs catalyze the ...
7988-8245 3.91e-13

Catalytic domain of the Serine/Threonine Kinase, c-Jun N-terminal Kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. JNKs are mitogen-activated protein kinases (MAPKs) that are involved in many stress-activated responses including those during inflammation, neurodegeneration, apoptosis, and persistent pain sensitization, among others. They are also essential regulators of physiological and pathological processes and are involved in the pathogenesis of several diseases such as diabetes, atherosclerosis, stroke, Parkinson's and Alzheimer's. Vetebrates harbor three different JNK genes (Jnk1, Jnk2, and Jnk3) that are alternatively spliced to produce at least 10 isoforms. JNKs are specifically activated by the MAPK kinases MKK4 and MKK7, which are in turn activated by upstream MAPK kinase kinases as a result of different stimuli including stresses such as ultraviolet (UV) irradiation, hyperosmolarity, heat shock, or cytokines. JNKs activate a large number of different substrates based on specific stimulus, cell type, and cellular condition, and may be implicated in seemingly contradictory functions. The JNK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270840 [Multi-domain]  Cd Length: 337  Bit Score: 75.14  E-value: 3.91e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 7988 RYDILEEIGTGAFGVVHRCRERSTGNIFAAK-----FIPVSHSVEKdliRREIDIMNQLHHQKLINLHDAF------EDD 8056
Cdd:cd07850     1 RYQNLKPIGSGAQGIVCAAYDTVTGQNVAIKklsrpFQNVTHAKRA---YRELVLMKLVNHKNIIGLLNVFtpqkslEEF 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 8057 DEMILILEFLSGgELFERITAEgyvmTEAEVINYM-RQICEGIRHMHEQNIIHLDIKPENIMcqTRSSTNVKLIDFGLA- 8134
Cdd:cd07850    78 QDVYLVMELMDA-NLCQVIQMD----LDHERMSYLlYQMLCGIKHLHSAGIIHRDLKPSNIV--VKSDCTLKILDFGLAr 150
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 8135 -----TRLDPnEVVkittgTAEFAAPEIVNREPVGFYTDMWATGVLSYVLLSGLSPFAGDNDV----------------- 8192
Cdd:cd07850   151 tagtsFMMTP-YVV-----TRYYRAPEVILGMGYKENVDIWSVGCIMGEMIRGTVLFPGTDHIdqwnkiieqlgtpsdef 224
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 281359561 8193 -----QTLKNVKAC--------------DWDFDVES---FKYISEEAKDFIRKLLVRNKEKRMTAHECLLHPWLT 8245
Cdd:cd07850   225 msrlqPTVRNYVENrpkyagysfeelfpDVLFPPDSeehNKLKASQARDLLSKMLVIDPEKRISVDDALQHPYIN 299
STKc_SHIK cd13974
Catalytic domain of the Serine/Threonine kinase, SINK-homologous inhibitory kinase; STKs ...
8082-8239 4.03e-13

Catalytic domain of the Serine/Threonine kinase, SINK-homologous inhibitory kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. SHIK, also referred to as STK40 or LYK4, is a cytoplasmic and nuclear protein that is involved in the negative regulation of NF-kappaB- and p53-mediated transcription. It was identified as a protein related to SINK, a p65-interacting protein that inhibits p65 phosphorylation by the catalytic subunit of PKA, thereby inhibiting transcriptional competence of NF-kappaB. The SHIK subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270876 [Multi-domain]  Cd Length: 290  Bit Score: 74.36  E-value: 4.03e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 8082 MTEAEVINYMRQICEGIRHMHEQNIIHLDIKPENIMCQTRSStNVKLIDFGLATRL-DPNEVVKITTGTAEFAAPEIVNR 8160
Cdd:cd13974   129 LSEREALVIFYDVVRVVEALHKKNIVHRDLKLGNMVLNKRTR-KITITNFCLGKHLvSEDDLLKDQRGSPAYISPDVLSG 207
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 8161 EP-VGFYTDMWATGVLSYVLLSGLSPFAgDNDVQTL-KNVKACDwdFDVESFKYISEEAKDFIRKLLVRNKEKRMTAHEC 8238
Cdd:cd13974   208 KPyLGKPSDMWALGVVLFTMLYGQFPFY-DSIPQELfRKIKAAE--YTIPEDGRVSENTVCLIRKLLVLNPQKRLTASEV 284

                  .
gi 281359561 8239 L 8239
Cdd:cd13974   285 L 285
FN3 smart00060
Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, ...
2697-2783 4.05e-13

Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, fibronectin. The tenth fibronectin type III repeat contains a RGD cell recognition sequence in a flexible loop between 2 strands. Type III modules are present in both extracellular and intracellular proteins.


Pssm-ID: 214495 [Multi-domain]  Cd Length: 83  Bit Score: 68.41  E-value: 4.05e-13
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561   2697 PSSPKGpLAVSDVTASGCKLQWKKPEDDGGV-PIKEYVVEKMDTaTGKWVRVGRSPGEkepPSFDVTGLSLGSEYMFRVS 2775
Cdd:smart00060    1 PSPPSN-LRVTDVTSTSVTLSWEPPPDDGITgYIVGYRVEYREE-GSEWKEVNVTPSS---TSYTLTGLKPGTEYEFRVR 75

                    ....*...
gi 281359561   2776 AVNEEGES 2783
Cdd:smart00060   76 AVNGAGEG 83
STKc_HIPK1 cd14228
Catalytic domain of the Serine/Threonine Kinase, Homeodomain-Interacting Protein Kinase 1; ...
7984-8198 4.41e-13

Catalytic domain of the Serine/Threonine Kinase, Homeodomain-Interacting Protein Kinase 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. HIPK1 has been implicated in regulating eye size, lens formation, and retinal morphogenesis during late embryogenesis. It also contributes to the regulation of haematopoiesis and leukaemogenesis by phosphorylating and repressing the transcription factor c-Myb, which is crucial in T- and B-cell development. In glucose-deprived conditions, HIPK1 phosphorylates Daxx, leading to its relocalization from the nucleus to the cytoplasm, where it binds and stabilizes ASK1 (apoptosis signal-regulating kinase 1), a mitogen-activated protein kinase (MAPK) kinase kinase that activates the JNK and p38 MAPK pathways. HIPKs, originally identified by their ability to bind homeobox factors, are nuclear proteins containing catalytic kinase and homeobox-interacting domains as well as a PEST region overlapping with the speckle-retention signal (SRS). The HIPK1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271130 [Multi-domain]  Cd Length: 355  Bit Score: 75.13  E-value: 4.41e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 7984 SVYDRYDILEEIGTGAFGVVHRCRERSTGNIFAAKFIPvSHSVEKDLIRREIDIMNQLHHQ-----KLINLHDAFEDDDE 8058
Cdd:cd14228    12 SMTNSYEVLEFLGRGTFGQVAKCWKRSTKEIVAIKILK-NHPSYARQGQIEVSILSRLSSEnadeyNFVRSYECFQHKNH 90
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 8059 MILILEFLSgGELFERITAEGYVMTEAEVIN-YMRQICEGIRHMHEQNIIHLDIKPENIMC--QTRSSTNVKLIDFGLAT 8135
Cdd:cd14228    91 TCLVFEMLE-QNLYDFLKQNKFSPLPLKYIRpILQQVATALMKLKSLGLIHADLKPENIMLvdPVRQPYRVKVIDFGSAS 169
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 281359561 8136 RLDpNEVVKITTGTAEFAAPEIVNREPVGFYTDMWATGVLSYVLLSGLSPFAGDNDVQTLKNV 8198
Cdd:cd14228   170 HVS-KAVCSTYLQSRYYRAPEIILGLPFCEAIDMWSLGCVIAELFLGWPLYPGASEYDQIRYI 231
PKc_DYRK1 cd14226
Catalytic domain of the protein kinase, Dual-specificity tYrosine-phosphorylated and ...
7987-8192 4.42e-13

Catalytic domain of the protein kinase, Dual-specificity tYrosine-phosphorylated and -Regulated Kinase 1; Dual-specificity PKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine (S/T) as well as tyrosine residues on protein substrates. Mammals contain two types of DYRK1 proteins, DYRK1A and DYRK1B. DYRK1A was previously called minibrain kinase homolog (MNBH) or dual-specificity YAK1-related kinase. It phosphorylates various substrates and is involved in many cellular events. It phosphorylates and inhibits the transcription factors, nuclear factor of activated T cells (NFAT) and forkhead in rhabdomyosarcoma (FKHR). It regulates neuronal differentiation by targetting CREB (cAMP response element-binding protein). It also targets many endocytic proteins including dynamin and amphiphysin and may play a role in the endocytic pathway. The gene encoding DYRK1A is located in the DSCR (Down syndrome critical region) of human chromosome 21 and DYRK1A has been implicated in the pathogenesis of DS. DYRK1B, also called minibrain-related kinase (MIRK), is highly expressed in muscle and plays a critical role in muscle differentiation by regulating transcription, cell motility, survival, and cell cycle progression. It is overexpressed in many solid tumors where it acts as a tumor survival factor. DYRKs autophosphorylate themselves on tyrosine residues and phosphorylate their substrates exclusively on S/T residues. The DYRK1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271128 [Multi-domain]  Cd Length: 339  Bit Score: 74.66  E-value: 4.42e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 7987 DRYDILEEIGTGAFGVVHRCRERSTGNIFAAKFIPVSHS-VEKDLIrrEIDIMNQLHHQ------KLINLHDAFEDDDEM 8059
Cdd:cd14226    13 DRYEIDSLIGKGSFGQVVKAYDHVEQEWVAIKIIKNKKAfLNQAQI--EVRLLELMNKHdtenkyYIVRLKRHFMFRNHL 90
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 8060 ILILEFLSGgELFERITAEGYVMTEAEVI-NYMRQICEGIRHMH--EQNIIHLDIKPENIMCQTRSSTNVKLIDFGLATR 8136
Cdd:cd14226    91 CLVFELLSY-NLYDLLRNTNFRGVSLNLTrKFAQQLCTALLFLStpELSIIHCDLKPENILLCNPKRSAIKIIDFGSSCQ 169
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 281359561 8137 LdpNEVVKITTGTAEFAAPEIVNREPVGFYTDMWATGVLSYVLLSGLSPFAGDNDV 8192
Cdd:cd14226   170 L--GQRIYQYIQSRFYRSPEVLLGLPYDLAIDMWSLGCILVEMHTGEPLFSGANEV 223
fn3 pfam00041
Fibronectin type III domain;
6470-6545 5.02e-13

Fibronectin type III domain;


Pssm-ID: 394996 [Multi-domain]  Cd Length: 85  Bit Score: 68.21  E-value: 5.02e-13
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 281359561  6470 ITRNGVTLSWRPPrTDGKSRIKGYYVEMRPKNGKDWKTVNDIPINSTVYTVPSLKEGEEYSFRVVAENEVGRSDPS 6545
Cdd:pfam00041   11 VTSTSLTVSWTPP-PDGNGPITGYEVEYRPKNSGEPWNEITVPGTTTSVTLTGLKPGTEYEVRVQAVNGGGEGPPS 85
FN3 COG3401
Fibronectin type 3 domain [General function prediction only];
5029-5561 5.34e-13

Fibronectin type 3 domain [General function prediction only];


Pssm-ID: 442628 [Multi-domain]  Cd Length: 603  Bit Score: 76.58  E-value: 5.34e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 5029 TNVDYNTKLKVNSATRSDSGIYTVFAENANGEDSADVKVTVIDKPAPPNGPLKVDEINSESCTLHWNPPDDDGGQPIDNY 5108
Cdd:COG3401    90 TATGLTTLTGSGSVGGATNTGLTSSDEVPSPAVGTATTATAVAGGAATAGTYALGAGLYGVDGANASGTTASSVAGAGVV 169
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 5109 VVEKLDETTGRWIPAGETDGPVTALKVGGLTPGHKYKFRVRAKNRQGTSEPLTTAQAIIAKNPfdvPTKPGTPTIKDFDK 5188
Cdd:COG3401   170 VSPDTSATAAVATTSLTVTSTTLVDGGGDIEPGTTYYYRVAATDTGGESAPSNEVSVTTPTTP---PSAPTGLTATADTP 246
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 5189 EFVDLEWTRPEADGgspITGYVVEKRDKFSPDWEKCAEISDdiTNAHVPDLIEGLKYEFRVRAVNKAgpGSPSDATEThv 5268
Cdd:COG3401   247 GSVTLSWDPVTESD---ATGYRVYRSNSGDGPFTKVATVTT--TSYTDTGLTNGTTYYYRVTAVDAA--GNESAPSNV-- 317
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 5269 arpkntppkidrnfmsdikikagnvfefdVPVTgeplpskdwthegnmiintdrvkisnfddrtkirildakrsdtgvyt 5348
Cdd:COG3401   318 -----------------------------VSVT----------------------------------------------- 321
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 5349 ltarningtdrhnvkvTILDAPSVPEGpLRNGDVSKNSIVLRWRPPKDDGgseITHYVVEKMDNEAMRWVPVGD------ 5422
Cdd:COG3401   322 ----------------TDLTPPAAPSG-LTATAVGSSSITLSWTASSDAD---VTGYNVYRSTSGGGTYTKIAEtvttts 381
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 5423 CTDTeiradNLIENHDYSFRVRAVNKQGQSQPLTTSQPITAKDPYSHPDKPGQPQATD----WGKHFVDLEWSTPKRDGG 5498
Cdd:COG3401   382 YTDT-----GLTPGTTYYYKVTAVDAAGNESAPSEEVSATTASAASGESLTASVDAVPltdvAGATAAASAASNPGVSAA 456
                         490       500       510       520       530       540
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 281359561 5499 APISSYIIEKRPKFGQWERAAVVLGDNCKAHVPELTNGGEYEFRVIAVNRGGPSDPSDPSSTI 5561
Cdd:COG3401   457 VLADGGDTGNAVPFTTTSSTVTATTTDTTTANLSVTTGSLVGGSGASSVTNSVSVIGASAAAA 519
STKc_PFTAIRE2 cd07870
Catalytic domain of the Serine/Threonine Kinase, PFTAIRE-2 kinase; STKs catalyze the transfer ...
7992-8244 5.58e-13

Catalytic domain of the Serine/Threonine Kinase, PFTAIRE-2 kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PFTAIRE-2 is also referred to as ALS2CR7 (amyotrophic lateral sclerosis 2 (juvenile) chromosome region candidate 7). It may be associated with amyotrophic lateral sclerosis 2 (ALS2), an autosomal recessive form of juvenile ALS. The function of PFTAIRE-2 is not yet known. It shares sequence similarity with Cyclin-Dependent Kinases (CDKs), which belong to a large family of STKs that are regulated by their cognate cyclins. Together, CDKs and cyclins are involved in the control of cell-cycle progression, transcription, and neuronal function. The PFTAIRE-2 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270852 [Multi-domain]  Cd Length: 286  Bit Score: 73.84  E-value: 5.58e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 7992 LEEIGTGAFGVVHRCRERSTGNIFAAKFIpvSHSVEKDL---IRREIDIMNQLHHQKLINLHDAFEDDDEMILILEFLSG 8068
Cdd:cd07870     5 LEKLGEGSYATVYKGISRINGQLVALKVI--SMKTEEGVpftAIREASLLKGLKHANIVLLHDIIHTKETLTFVFEYMHT 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 8069 gELFERITAEGYVMTEAEVINYMRQICEGIRHMHEQNIIHLDIKPENIMCQTRSStnVKLIDFGLA-TRLDPNEVVKITT 8147
Cdd:cd07870    83 -DLAQYMIQHPGGLHPYNVRLFMFQLLRGLAYIHGQHILHRDLKPQNLLISYLGE--LKLADFGLArAKSIPSQTYSSEV 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 8148 GTAEFAAPEIV-NREPVGFYTDMWATGVLSYVLLSGLSPFAGDNDV--QTLK-----NVKACD-W-------DFDVESFK 8211
Cdd:cd07870   160 VTLWYRPPDVLlGATDYSSALDIWGAGCIFIEMLQGQPAFPGVSDVfeQLEKiwtvlGVPTEDtWpgvsklpNYKPEWFL 239
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*..
gi 281359561 8212 YIS--------------EEAKDFIRKLLVRNKEKRMTAHECLLHPWL 8244
Cdd:cd07870   240 PCKpqqlrvvwkrlsrpPKAEDLASQMLMMFPKDRISAQDALLHPYF 286
STKc_TDY_MAPK cd07859
Catalytic domain of the Serine/Threonine Kinases, Plant TDY Mitogen-Activated Protein Kinases; ...
7988-8267 5.70e-13

Catalytic domain of the Serine/Threonine Kinases, Plant TDY Mitogen-Activated Protein Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Plant MAPKs are typed based on the conserved phosphorylation motif present in the activation loop, TEY and TDY. This subfamily represents the TDY subtype and is composed of Group D plant MAPKs including Arabidopsis thaliana MPK18 (AtMPK18), Oryza sativa Blast- and Wound-induced MAPK1 (OsBWMK1), OsWJUMK1 (Wound- and JA-Uninducible MAPK1), Zea mays MPK6, and the Medicago sativa TDY1 gene product. OsBWMK1 enhances resistance to pathogenic infections. It mediates stress-activated defense responses by activating a transcription factor that affects the expression of stress-related genes. AtMPK18 is involved in microtubule-related functions. In plants, MAPKs are associated with physiological, developmental, hormonal, and stress responses. Some plants show numerous gene duplications of MAPKs; Arabidopsis thaliana harbors at least 20 MAPKs, named AtMPK1-20 while Oryza sativa contains at least 17 MAPKs. Arabidopsis thaliana contains more TEY-type MAPKs than TDY-type, whereas the reverse is true for Oryza sativa. The TDY MAPK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 143364 [Multi-domain]  Cd Length: 338  Bit Score: 74.43  E-value: 5.70e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 7988 RYDILEEIGTGAFGVVHRCRERSTGNIFAAKFIP--VSHSVEKDLIRREIDIMNQLHHQ-----KLINLHDAFEDDDEMI 8060
Cdd:cd07859     1 RYKIQEVIGKGSYGVVCSAIDTHTGEKVAIKKINdvFEHVSDATRILREIKLLRLLRHPdiveiKHIMLPPSRREFKDIY 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 8061 LILEfLSGGELFERITAEGYVMTEAEVInYMRQICEGIRHMHEQNIIHLDIKPENIMCQtrSSTNVKLIDFGLAtRLDPN 8140
Cdd:cd07859    81 VVFE-LMESDLHQVIKANDDLTPEHHQF-FLYQLLRALKYIHTANVFHRDLKPKNILAN--ADCKLKICDFGLA-RVAFN 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 8141 EvvkitTGTAEF----------AAPEIVNrepvGFYT------DMWATGVLSYVLLSGLSPFAGDNDVQTL--------- 8195
Cdd:cd07859   156 D-----TPTAIFwtdyvatrwyRAPELCG----SFFSkytpaiDIWSIGCIFAEVLTGKPLFPGKNVVHQLdlitdllgt 226
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 8196 ---------KNVKACDWDFDV---------ESFKYISEEAKDFIRKLLVRNKEKRMTAHECLLHPWLTGDHSAMKQ---- 8253
Cdd:cd07859   227 pspetisrvRNEKARRYLSSMrkkqpvpfsQKFPNADPLALRLLERLLAFDPKDRPTAEEALADPYFKGLAKVEREpsaq 306
                         330       340
                  ....*....|....*....|....*...
gi 281359561 8254 ------------EINRD--RYLAYREKL 8267
Cdd:cd07859   307 pitklefeferrRLTKEdvRELIYREIL 334
FN3 smart00060
Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, ...
7050-7133 6.28e-13

Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, fibronectin. The tenth fibronectin type III repeat contains a RGD cell recognition sequence in a flexible loop between 2 strands. Type III modules are present in both extracellular and intracellular proteins.


Pssm-ID: 214495 [Multi-domain]  Cd Length: 83  Bit Score: 68.02  E-value: 6.28e-13
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561   7050 PDEPGQPKVIDWDSGNVTLIWTRPLSDGG-SRIQGYQIEYRDilNDSSWNAYDYIIKDTKYQLYNLINGSEYEFRIKAKN 7128
Cdd:smart00060    1 PSPPSNLRVTDVTSTSVTLSWEPPPDDGItGYIVGYRVEYRE--EGSEWKEVNVTPSSTSYTLTGLKPGTEYEFRVRAVN 78

                    ....*
gi 281359561   7129 AAGLS 7133
Cdd:smart00060   79 GAGEG 83
Ig_Titin_like cd05748
Immunoglobulin (Ig)-like domain of titin and similar proteins; The members here are composed ...
5874-5954 6.36e-13

Immunoglobulin (Ig)-like domain of titin and similar proteins; The members here are composed of the immunoglobulin (Ig)-like domain found in titin-like proteins and similar proteins. Titin (also called connectin) is a fibrous sarcomeric protein specifically found in vertebrate striated muscle. Titin is a giant protein; depending on isoform composition, it ranges from 2970 to 3700 kDa, and is of a length that spans half a sarcomere. Titin largely consists of multiple repeats of Ig-like and fibronectin type 3 (FN-III)-like domains. Titin connects the ends of myosin thick filaments to Z disks and extends along the thick filament to the H zone. It appears to function similarly to an elastic band, keeping the myosin filaments centered in the sarcomere during muscle contraction or stretching. Within the sarcomere, titin is also attached to or is associated with myosin binding protein C (MyBP-C). MyBP-C appears to contribute to the generation of passive tension by titin and like titin has repeated Ig-like and FN-III domains. Also included in this group are worm twitchin and insect projectin, thick filament proteins of invertebrate muscle which also have repeated Ig-like and FN-III domains.


Pssm-ID: 409406 [Multi-domain]  Cd Length: 82  Bit Score: 67.61  E-value: 6.36e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 5874 VRIKCGLIFHTDIHFIGEPAPEATWTLNSNPLLSNDRSTITSIGHHSVVHTVNCQRSDSGIYHLLLRNSSGIDEGSFELV 5953
Cdd:cd05748     2 IVVRAGESLRLDIPIKGRPTPTVTWSKDGQPLKETGRVQIETTASSTSLVIKNAKRSDSGKYTLTLKNSAGEKSATINVK 81

                  .
gi 281359561 5954 V 5954
Cdd:cd05748    82 V 82
FN3 COG3401
Fibronectin type 3 domain [General function prediction only];
3322-3786 6.50e-13

Fibronectin type 3 domain [General function prediction only];


Pssm-ID: 442628 [Multi-domain]  Cd Length: 603  Bit Score: 76.19  E-value: 6.50e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 3322 DDGGIPITGYVIEKMDTATGKWVPAGSVDPEKYDIEIKGLDPNHRYQFRVKAVNEEGESEPLETESAITAKNPfdVSAPP 3401
Cdd:COG3401   160 ASSVAGAGVVVSPDTSATAAVATTSLTVTSTTLVDGGGDIEPGTTYYYRVAATDTGGESAPSNEVSVTTPTTP--PSAPT 237
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 3402 GLpELEDWDEHHVKLKWEPPirdGGSPITNYIIEVMDKDSGEFVKAVETDSPVckGVVKKLEEGQQYKFRVRAVNKAGps 3481
Cdd:COG3401   238 GL-TATADTPGSVTLSWDPV---TESDATGYRVYRSNSGDGPFTKVATVTTTS--YTDTGLTNGTTYYYRVTAVDAAG-- 309
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 3482 dpseqtnwhvakprflkphidrvnlkpvivktglsisldinirgepapkvewffnNSSVTSDEHSVKIDnvdyntkffvm 3561
Cdd:COG3401   310 -------------------------------------------------------NESAPSNVVSVTTD----------- 323
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 3562 raqrsqsgkyiikatnevgedeaelevtvLGKPGKPKGpLQVNDITKHSCKLKWEKPDDdggSPIDYYEIEKLDPHTGQW 3641
Cdd:COG3401   324 -----------------------------LTPPAAPSG-LTATAVGSSSITLSWTASSD---ADVTGYNVYRSTSGGGTY 370
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 3642 LPCGKS-TEPEAKVIGLHEGKAYKFRVRAVNKEGESEDLETEKPIIAKNPY--DEPDRPGKPEPTNWDKDFVDLAWDPPK 3718
Cdd:COG3401   371 TKIAETvTTTSYTDTGLTPGTTYYYKVTAVDAAGNESAPSEEVSATTASAAsgESLTASVDAVPLTDVAGATAAASAASN 450
                         410       420       430       440       450       460
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 281359561 3719 NDGGAPIQKYVIQMRDKSGRAWVDSATVPGDKCNGT-VTGVEEGHEYEFRIVAVNKAGPSDPSDVSKSV 3786
Cdd:COG3401   451 PGVSAAVLADGGDTGNAVPFTTTSSTVTATTTDTTTaNLSVTTGSLVGGSGASSVTNSVSVIGASAAAA 519
Ig cd00096
Immunoglobulin domain; The members here are composed of the immunoglobulin (Ig) domain found ...
7665-7734 6.60e-13

Immunoglobulin domain; The members here are composed of the immunoglobulin (Ig) domain found in the Ig superfamily. The Ig superfamily is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. Members of this group are components of immunoglobulin, neuroglia, cell surface glycoproteins, including T-cell receptors, CD2, CD4, CD8, and membrane glycoproteins, including butyrophilin and chondroitin sulfate proteoglycan core protein. A predominant feature of most Ig domains is a disulfide bridge connecting the two beta-sheets with a tryptophan residue packed against the disulfide bond. Ig superfamily (IgSF) domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. Typically, the V-set domains have A, B, E, and D strands in one sheet and A', G, F, C, C' and C" in the other. The structures in C1-set are smaller than those in the V-set; they have one beta sheet that is formed by strands A, B, E, and D and the other by strands G, F, C, and C'. Moreover, a C1-set Ig domain contains a short C' strand (three residues) and lacks A' and C" strand. Unlike other Ig domain sets, C2-set structures do not have a D strand. Like the V-set Ig domains, members of the I-set have a discontinuous A strand, but lack a C" strand.


Pssm-ID: 409353 [Multi-domain]  Cd Length: 70  Bit Score: 67.35  E-value: 6.60e-13
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 7665 AQFTCTINGVPKPTISWYKGAREISNGARYHMYSEGDNHFLNINDVFGEDADEYVCRAVNKAGAKSTRAT 7734
Cdd:cd00096     1 VTLTCSASGNPPPTITWYKNGKPLPPSSRDSRRSELGNGTLTISNVTLEDSGTYTCVASNSAGGSASASV 70
fn3 pfam00041
Fibronectin type III domain;
4880-4964 6.73e-13

Fibronectin type III domain;


Pssm-ID: 394996 [Multi-domain]  Cd Length: 85  Bit Score: 67.83  E-value: 6.73e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561  4880 GKPENLKATDWDKDHVDLAWTPPLiDGGSPISCYIIEKQDKY-GKWERALDVPADQCKATIPDLVEGQTYKFRVSAVNAA 4958
Cdd:pfam00041    1 SAPSNLTVTDVTSTSLTVSWTPPP-DGNGPITGYEVEYRPKNsGEPWNEITVPGTTTSVTLTGLKPGTEYEVRVQAVNGG 79

                   ....*.
gi 281359561  4959 GTGEPS 4964
Cdd:pfam00041   80 GEGPPS 85
FN3 smart00060
Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, ...
4779-4861 7.20e-13

Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, fibronectin. The tenth fibronectin type III repeat contains a RGD cell recognition sequence in a flexible loop between 2 strands. Type III modules are present in both extracellular and intracellular proteins.


Pssm-ID: 214495 [Multi-domain]  Cd Length: 83  Bit Score: 67.64  E-value: 7.20e-13
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561   4779 PSPPnGPLQISDVHKEGCHLKWKRPSDDGGT-PIEYFQIDKLEPETGCWIPSCRSTEPQVDVTGLSPGNEYKFRVSAVNA 4857
Cdd:smart00060    1 PSPP-SNLRVTDVTSTSVTLSWEPPPDDGITgYIVGYRVEYREEGSEWKEVNVTPSSTSYTLTGLKPGTEYEFRVRAVNG 79

                    ....
gi 281359561   4858 EGES 4861
Cdd:smart00060   80 AGEG 83
FN3 smart00060
Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, ...
5470-5552 7.20e-13

Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, fibronectin. The tenth fibronectin type III repeat contains a RGD cell recognition sequence in a flexible loop between 2 strands. Type III modules are present in both extracellular and intracellular proteins.


Pssm-ID: 214495 [Multi-domain]  Cd Length: 83  Bit Score: 67.64  E-value: 7.20e-13
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561   5470 PDKPGQPQATDWGKHFVDLEWSTPKRDGG-APISSYIIEKRPKFGQWERAAVVLGDNcKAHVPELTNGGEYEFRVIAVNR 5548
Cdd:smart00060    1 PSPPSNLRVTDVTSTSVTLSWEPPPDDGItGYIVGYRVEYREEGSEWKEVNVTPSST-SYTLTGLKPGTEYEFRVRAVNG 79

                    ....
gi 281359561   5549 GGPS 5552
Cdd:smart00060   80 AGEG 83
FN3 smart00060
Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, ...
2100-2185 7.86e-13

Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, fibronectin. The tenth fibronectin type III repeat contains a RGD cell recognition sequence in a flexible loop between 2 strands. Type III modules are present in both extracellular and intracellular proteins.


Pssm-ID: 214495 [Multi-domain]  Cd Length: 83  Bit Score: 67.64  E-value: 7.86e-13
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561   2100 PQPPQDVDITDVYQTSCVVSFNPPSDDGGT-PITKYVIERQDlsKKHGWESVAEVLPSEPClkKIDDLIPKKQYRFRIRA 2178
Cdd:smart00060    1 PSPPSNLRVTDVTSTSVTLSWEPPPDDGITgYIVGYRVEYRE--EGSEWKEVNVTPSSTSY--TLTGLKPGTEYEFRVRA 76

                    ....*..
gi 281359561   2179 VNAIGQS 2185
Cdd:smart00060   77 VNGAGEG 83
STKc_GAK cd14036
Catalytic domain of the Serine/Threonine protein kinase, cyclin G-Associated Kinase; STKs ...
7995-8239 8.27e-13

Catalytic domain of the Serine/Threonine protein kinase, cyclin G-Associated Kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. GAK, also called auxilin-2, contains an N-terminal kinase domain that phosphorylates the mu subunits of adaptor protein (AP) 1 and AP2. In addition, it contains an auxilin-1-like domain structure consisting of PTEN-like, clathrin-binding, and J domains. Like auxilin-1, GAK facilitates Hsc70-mediated dissociation of clathrin from clathrin-coated vesicles. GAK is expressed ubiquitously and is enriched in the Golgi, unlike auxilin-1 which is nerve-specific. GAK also plays regulatory roles outside of clathrin-mediated membrane traffic including the maintenance of centrosome integrity and chromosome congression, neural patterning, survival of neurons, and immune responses through interaction with the interleukin 12 receptor. It also interacts with the androgen receptor, acting as a transcriptional coactivator, and its expression is significantly increased with the progression of prostate cancer. The GAK subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270938 [Multi-domain]  Cd Length: 282  Bit Score: 72.93  E-value: 8.27e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 7995 IGTGAFGVVHRCRERSTGNIFAAKFIpVSHSVEKD-LIRREIDIMNQLH-HQKLINLHDAF-----EDD---DEMILILE 8064
Cdd:cd14036     8 IAEGGFAFVYEAQDVGTGKEYALKRL-LSNEEEKNkAIIQEINFMKKLSgHPNIVQFCSAAsigkeESDqgqAEYLLLTE 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 8065 FLSGG--ELFERITAEGyVMTEAEVINYMRQICEGIRHMHEQN--IIHLDIKPENIMCQTRSStnVKLIDFGLATR---- 8136
Cdd:cd14036    87 LCKGQlvDFVKKVEAPG-PFSPDTVLKIFYQTCRAVQHMHKQSppIIHRDLKIENLLIGNQGQ--IKLCDFGSATTeahy 163
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 8137 -----------LDPNEVVKITtgTAEFAAPEIVN---REPVGFYTDMWATGVLSYVLLSGLSPFagdNDVQTLKNVKAcd 8202
Cdd:cd14036   164 pdyswsaqkrsLVEDEITRNT--TPMYRTPEMIDlysNYPIGEKQDIWALGCILYLLCFRKHPF---EDGAKLRIINA-- 236
                         250       260       270
                  ....*....|....*....|....*....|....*..
gi 281359561 8203 wDFDVESFKYISEEAKDFIRKLLVRNKEKRMTAHECL 8239
Cdd:cd14036   237 -KYTIPPNDTQYTVFHDLIRSTLKVNPEERLSITEIV 272
FN3 COG3401
Fibronectin type 3 domain [General function prediction only];
3647-4163 8.63e-13

Fibronectin type 3 domain [General function prediction only];


Pssm-ID: 442628 [Multi-domain]  Cd Length: 603  Bit Score: 75.81  E-value: 8.63e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 3647 STEPEAKVIGLHEGKAYKFRVRAVNKEGESEDLETekpIIAKNPYDEPDRPGKPEPTNWDKDFVDLAWDPPKNDGgapIQ 3726
Cdd:COG3401   189 STTLVDGGGDIEPGTTYYYRVAATDTGGESAPSNE---VSVTTPTTPPSAPTGLTATADTPGSVTLSWDPVTESD---AT 262
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 3727 KYVIQMRDKSGRAWVDSATVPGDkcNGTVTGVEEGHEYEFRIVAVNKAG-PSDPSDVsksviakprflkphidrknlqkk 3805
Cdd:COG3401   263 GYRVYRSNSGDGPFTKVATVTTT--SYTDTGLTNGTTYYYRVTAVDAAGnESAPSNV----------------------- 317
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 3806 imrsgqmlhidalikaeppakvtwtynkteiktsdhikienedykttfimpkvkradrgiyiVTAKNDSGsdtvevelev 3885
Cdd:COG3401   318 --------------------------------------------------------------VSVTTDLT---------- 325
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 3886 lcKPSKPKGpLAVSNVTAETLHLKWEKPEDDGgdpIEQYLVERMDTETGRWVPVLTT-KTPEADVTGLTEGKEYLFRVKA 3964
Cdd:COG3401   326 --PPAAPSG-LTATAVGSSSITLSWTASSDAD---VTGYNVYRSTSGGGTYTKIAETvTTTSYTDTGLTPGTTYYYKVTA 399
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 3965 VNSEG-ESEP--LVTDIPTKAKNPFDAADTPGKPQIVDWSGNHCDLKWRAPEDDGGASITGYIVERKDPNTGKWQkALET 4041
Cdd:COG3401   400 VDAAGnESAPseEVSATTASAASGESLTASVDAVPLTDVAGATAAASAASNPGVSAAVLADGGDTGNAVPFTTTS-STVT 478
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 4042 STPDCKARVNDLIAGNKYQFRIMAVNKAGKSKPSEPSDQM-TAKDRFAPPKIDRTNIKDITIKAGQHIRFDIKVSGEPPA 4120
Cdd:COG3401   479 ATTTDTTTANLSVTTGSLVGGSGASSVTNSVSVIGASAAAaVGGAPDGTPNVTGASPVTVGASTGDVLITDLVSLTTSAS 558
                         490       500       510       520
                  ....*....|....*....|....*....|....*....|....*
gi 281359561 4121 TKVW--LHNKARLENDDSNYNIDmeSYRTKLTVPISKRFHSGKYT 4163
Cdd:COG3401   559 SSVSgaGLGSGNLYLITTLGGSL--LTTTSTNTNDVAGVHGGTLL 601
STKc_LRRK cd14000
Catalytic domain of the Serine/Threonine kinase, Leucine-Rich Repeat Kinase; STKs catalyze the ...
7995-8235 8.83e-13

Catalytic domain of the Serine/Threonine kinase, Leucine-Rich Repeat Kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. LRRKs are also classified as ROCO proteins because they contain a ROC (Ras of complex proteins)/GTPase domain followed by a COR (C-terminal of ROC) domain of unknown function. In addition, LRRKs contain a catalytic kinase domain and protein-protein interaction motifs including a WD40 domain, LRRs and ankyrin (ANK) repeats. LRRKs possess both GTPase and kinase activities, with the ROC domain acting as a molecular switch for the kinase domain, cycling between a GTP-bound state which drives kinase activity and a GDP-bound state which decreases the activity. Vertebrates contain two members, LRRK1 and LRRK2, which show complementary expression in the brain. Mutations in LRRK2 are linked to both familial and sporadic forms of Parkinson's disease. The normal roles of LRRKs are not clearly defined. They may be involved in mitogen-activated protein kinase (MAPK) pathways, protein translation control, programmed cell death pathways, and cytoskeletal dynamics. The LRRK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270902 [Multi-domain]  Cd Length: 275  Bit Score: 73.03  E-value: 8.83e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 7995 IGTGAFGVVHRCRER------------------STGNIFAAKFIPVSHSVEKD-LIRREIDIMNQLHHQKLINLHDAFED 8055
Cdd:cd14000     2 LGDGGFGSVYRASYKgepvavkifnkhtssnfaNVPADTMLRHLRATDAMKNFrLLRQELTVLSHLHHPSIVYLLGIGIH 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 8056 DDEMILILEFLSG-GELFERITAEGYVMTEAEVINYMRQICEGIRHMHEQNIIHLDIKPENIMCQT---RSSTNVKLIDF 8131
Cdd:cd14000    82 PLMLVLELAPLGSlDHLLQQDSRSFASLGRTLQQRIALQVADGLRYLHSAMIIYRDLKSHNVLVWTlypNSAIIIKIADY 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 8132 GLAtRLDPNEVVKITTGTAEFAAPEIVNREPVgfYT---DMWATGVLSYVLLSGLSPFAGDNDVQTLKNVKACDWDFDVE 8208
Cdd:cd14000   162 GIS-RQCCRMGAKGSEGTPGFRAPEIARGNVI--YNekvDVFSFGMLLYEILSGGAPMVGHLKFPNEFDIHGGLRPPLKQ 238
                         250       260
                  ....*....|....*....|....*..
gi 281359561 8209 SFKYISEEAKDFIRKLLVRNKEKRMTA 8235
Cdd:cd14000   239 YECAPWPEVEVLMKKCWKENPQQRPTA 265
fn3 pfam00041
Fibronectin type III domain;
4586-4670 9.28e-13

Fibronectin type III domain;


Pssm-ID: 394996 [Multi-domain]  Cd Length: 85  Bit Score: 67.44  E-value: 9.28e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561  4586 KPGVPEPTDWTANKVELAWpEPASDGGSPIQGYIVEVKDKYSPLWEKALETNSPTPTATVQGLIEGNEYQFRVVALNKGG 4665
Cdd:pfam00041    2 APSNLTVTDVTSTSLTVSW-TPPPDGNGPITGYEVEYRPKNSGEPWNEITVPGTTTSVTLTGLKPGTEYEVRVQAVNGGG 80

                   ....*
gi 281359561  4666 LSEPS 4670
Cdd:pfam00041   81 EGPPS 85
FN3 smart00060
Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, ...
4285-4372 1.00e-12

Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, fibronectin. The tenth fibronectin type III repeat contains a RGD cell recognition sequence in a flexible loop between 2 strands. Type III modules are present in both extracellular and intracellular proteins.


Pssm-ID: 214495 [Multi-domain]  Cd Length: 83  Bit Score: 67.25  E-value: 1.00e-12
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561   4285 PGKPGTPEAVDWDKDHVDLVWRPPINDGG-SPITGYVVEKREKGtdkwikGTEITIPCLGEECKATVPTLNENCEYEFRV 4363
Cdd:smart00060    1 PSPPSNLRVTDVTSTSVTLSWEPPPDDGItGYIVGYRVEYREEG------SEWKEVNVTPSSTSYTLTGLKPGTEYEFRV 74

                    ....*....
gi 281359561   4364 KAINAAGPG 4372
Cdd:smart00060   75 RAVNGAGEG 83
FN3 smart00060
Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, ...
7545-7628 1.01e-12

Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, fibronectin. The tenth fibronectin type III repeat contains a RGD cell recognition sequence in a flexible loop between 2 strands. Type III modules are present in both extracellular and intracellular proteins.


Pssm-ID: 214495 [Multi-domain]  Cd Length: 83  Bit Score: 67.25  E-value: 1.01e-12
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561   7545 PSPPGSPQITEIGGDFVHLEWEKPESDGGAH-IQGYWIDKREVGSNtWQRVNATiCAANQINCINLIEGRQYEFRIFAQN 7623
Cdd:smart00060    1 PSPPSNLRVTDVTSTSVTLSWEPPPDDGITGyIVGYRVEYREEGSE-WKEVNVT-PSSTSYTLTGLKPGTEYEFRVRAVN 78

                    ....*
gi 281359561   7624 VAGLS 7628
Cdd:smart00060   79 GAGEG 83
PK_KSR cd14063
Pseudokinase domain of Kinase Suppressor of Ras; The pseudokinase domain shows similarity to ...
7990-8190 1.04e-12

Pseudokinase domain of Kinase Suppressor of Ras; The pseudokinase domain shows similarity to protein kinases but lacks crucial residues for catalytic activity. KSR is a scaffold protein that functions downstream of Ras and upstream of Raf in the Extracellular signal-Regulated Kinase (ERK) pathway that regulates many cellular processes including cycle regulation, proliferation, differentiation, survival, and apoptosis. KSR proteins regulate the assembly and activation of the Raf/MEK/ERK module upon Ras activation at the membrane by direct association of its components. They are widely regarded as pseudokinases, but there is some debate in this designation as a few groups have reported detecting kinase catalytic activity for KSRs, specifically KSR1. Vertebrates contain two KSR proteins, KSR1 and KSR2. The KSR subfamily is part of a larger superfamily that includes the catalytic domains of other protein kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270965 [Multi-domain]  Cd Length: 271  Bit Score: 72.77  E-value: 1.04e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 7990 DILEEIGTGAFGVVHRCRERstGNIfAAKFIPVSHSVEKDL--IRREIDIMNQLHHQKLINLHDAFEDDDEMILILEFLS 8067
Cdd:cd14063     3 EIKEVIGKGRFGRVHRGRWH--GDV-AIKLLNIDYLNEEQLeaFKEEVAAYKNTRHDNLVLFMGACMDPPHLAIVTSLCK 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 8068 GGELFERITAEGYVMTEAEVINYMRQICEGIRHMHEQNIIHLDIKPENIMCQtrsSTNVKLIDFGL--ATRLDP----NE 8141
Cdd:cd14063    80 GRTLYSLIHERKEKFDFNKTVQIAQQICQGMGYLHAKGIIHKDLKSKNIFLE---NGRVVITDFGLfsLSGLLQpgrrED 156
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 281359561 8142 VVKITTGTAEFAAPEIV----------NREPVGFYTDMWATGVLSYVLLSGLSPFAGDN 8190
Cdd:cd14063   157 TLVIPNGWLCYLAPEIIralspdldfeESLPFTKASDVYAFGTVWYELLAGRWPFKEQP 215
FN3 COG3401
Fibronectin type 3 domain [General function prediction only];
3144-3488 1.04e-12

Fibronectin type 3 domain [General function prediction only];


Pssm-ID: 442628 [Multi-domain]  Cd Length: 603  Bit Score: 75.42  E-value: 1.04e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 3144 SPIWDEILSTNTSVPEATVEGLVEGNIYQFRVRAVNKAGFSDPSD-------ATEPhlAKPRNLkpyinrdkmkpiKVRA 3216
Cdd:COG3401   178 AAVATTSLTVTSTTLVDGGGDIEPGTTYYYRVAATDTGGESAPSNevsvttpTTPP--SAPTGL------------TATA 243
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 3217 GQPVKFDVDVKGEPAPSLTWFlkETELTSTGQVRLENIDYNTKLTLLDTDrKQSGQ---YKLRAENINGV---DEAVVEV 3290
Cdd:COG3401   244 DTPGSVTLSWDPVTESDATGY--RVYRSNSGDGPFTKVATVTTTSYTDTG-LTNGTtyyYRVTAVDAAGNesaPSNVVSV 320
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 3291 II-LDKPSKPEGpIEVSDIHKEGCKLKWRKPKDDGgipITGYVIEKMDTATGKWVP-AGSVDPEKYDieIKGLDPNHRYQ 3368
Cdd:COG3401   321 TTdLTPPAAPSG-LTATAVGSSSITLSWTASSDAD---VTGYNVYRSTSGGGTYTKiAETVTTTSYT--DTGLTPGTTYY 394
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 3369 FRVKAVNEEG-ESEPLETESAITAKNPFDVS--APPGLPELEDWDEHHVKLKW-EPPIRDGGSPITNYIIEVMDKDSGEF 3444
Cdd:COG3401   395 YKVTAVDAAGnESAPSEEVSATTASAASGESltASVDAVPLTDVAGATAAASAaSNPGVSAAVLADGGDTGNAVPFTTTS 474
                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....*...
gi 281359561 3445 VKAV----ETDSPVCKGVVKKLEEGQQYKFRVRAVNKAGPSDPSEQTN 3488
Cdd:COG3401   475 STVTatttDTTTANLSVTTGSLVGGSGASSVTNSVSVIGASAAAAVGG 522
FN3 smart00060
Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, ...
5958-6044 1.10e-12

Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, fibronectin. The tenth fibronectin type III repeat contains a RGD cell recognition sequence in a flexible loop between 2 strands. Type III modules are present in both extracellular and intracellular proteins.


Pssm-ID: 214495 [Multi-domain]  Cd Length: 83  Bit Score: 67.25  E-value: 1.10e-12
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561   5958 PGPPEGPmEYEEITANSVTISWKPPK-DNGGSEISSYVIEKRDLthGGGWVPAVnyVSAKYNHAVVPRLLEGTMYELRVM 6036
Cdd:smart00060    1 PSPPSNL-RVTDVTSTSVTLSWEPPPdDGITGYIVGYRVEYREE--GSEWKEVN--VTPSSTSYTLTGLKPGTEYEFRVR 75

                    ....*...
gi 281359561   6037 AENLQGRS 6044
Cdd:smart00060   76 AVNGAGEG 83
PTKc_Csk_like cd05039
Catalytic domain of C-terminal Src kinase-like Protein Tyrosine Kinases; PTKs catalyze the ...
7990-8186 1.11e-12

Catalytic domain of C-terminal Src kinase-like Protein Tyrosine Kinases; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. This subfamily is composed of Csk, Chk, and similar proteins. They are cytoplasmic (or nonreceptor) PTKs containing the Src homology domains, SH3 and SH2, N-terminal to the catalytic tyr kinase domain. They negatively regulate the activity of Src kinases that are anchored to the plasma membrane. To inhibit Src kinases, Csk and Chk are translocated to the membrane via binding to specific transmembrane proteins, G-proteins, or adaptor proteins near the membrane. Csk catalyzes the tyr phosphorylation of the regulatory C-terminal tail of Src kinases, resulting in their inactivation. Chk inhibit Src kinases using a noncatalytic mechanism by simply binding to them. As negative regulators of Src kinases, Csk and Chk play important roles in cell proliferation, survival, and differentiation, and consequently, in cancer development and progression. The Csk-like subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270635 [Multi-domain]  Cd Length: 256  Bit Score: 72.00  E-value: 1.11e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 7990 DILEEIGTGAFGVVHRCRERstGNIFAAKFIPvSHSVEKDLIRREIDIMNQLHHQKLINLHDAFEDDDEMILILEFLSGG 8069
Cdd:cd05039     9 KLGELIGKGEFGDVMLGDYR--GQKVAVKCLK-DDSTAAQAFLAEASVMTTLRHPNLVQLLGVVLEGNGLYIVTEYMAKG 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 8070 ELFERITAEG-YVMTEAEVINYMRQICEGIRHMHEQNIIHLDIKPENIMCqtrSSTNV-KLIDFGLATRLDPNEV----- 8142
Cdd:cd05039    86 SLVDYLRSRGrAVITRKDQLGFALDVCEGMEYLESKKFVHRDLAARNVLV---SEDNVaKVSDFGLAKEASSNQDggklp 162
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*
gi 281359561 8143 VKITtgtaefaAPEIVNREPVGFYTDMWATGVLSYVLLS-GLSPF 8186
Cdd:cd05039   163 IKWT-------APEALREKKFSTKSDVWSFGILLWEIYSfGRVPY 200
I-set pfam07679
Immunoglobulin I-set domain;
7758-7833 1.12e-12

Immunoglobulin I-set domain;


Pssm-ID: 400151 [Multi-domain]  Cd Length: 90  Bit Score: 67.28  E-value: 1.12e-12
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 281359561  7758 GENVVIKIPFTGFPKPRIHWVRDGENIESGGHYTVEVKERHAVLIIRDGSHLDSGPYRITAENELGSDTAIIQVQI 7833
Cdd:pfam07679   15 GESARFTCTVTGTPDPEVSWFKDGQPLRSSDRFKVTYEGGTYTLTISNVQPDDSGKYTCVATNSAGEAEASAELTV 90
STKc_SRPK cd14136
Catalytic domain of the Serine/Threonine Kinase, Serine-aRginine Protein Kinase; STKs catalyze ...
7977-8244 1.13e-12

Catalytic domain of the Serine/Threonine Kinase, Serine-aRginine Protein Kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. SRPKs phosphorylate and regulate splicing factors from the SR protein family by specifically phosphorylating multiple serine residues residing in SR/RS dipeptide motifs (also known as RS domains). Phosphorylation of the RS domains enhances interaction with transportin SR and facilitates entry of the SR proteins into the nucleus. SRPKs contain a nonconserved insert domain, within the well-conserved catalytic kinase domain, that regulates their subcellular localization. They play important roles in mediating pre-mRNA processing and mRNA maturation, as well as other cellular functions such as chromatin reorganization, cell cycle and p53 regulation, and metabolic signaling. Vertebrates contain three distinct SRPKs, called SRPK1-3. The SRPK homolog in budding yeast, Sky1p, recognizes and phosphorylates its substrate Npl3p, which lacks a classic RS domain but contains a single RS dipeptide at the C-terminus of its RGG domain. Npl3p is a shuttling heterogeneous nuclear ribonucleoprotein (hnRNP) that exports a distinct class of mRNA from the nucleus to the cytoplasm. The SRPK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271038 [Multi-domain]  Cd Length: 320  Bit Score: 73.38  E-value: 1.13e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 7977 PVEISQqsVY-DRYDILEEIGTGAFGVVHRCRERSTGNIFAAKFIPvSHSVEKDLIRREIDIMNQLHH--------QKLI 8047
Cdd:cd14136     1 PVKIGE--VYnGRYHVVRKLGWGHFSTVWLCWDLQNKRFVALKVVK-SAQHYTEAALDEIKLLKCVREadpkdpgrEHVV 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 8048 NLHDAFE----DDDEMILILEFLsgGE----LFERITAEGYVMTEAEVInyMRQICEGIRHMHEQ-NIIHLDIKPENIMC 8118
Cdd:cd14136    78 QLLDDFKhtgpNGTHVCMVFEVL--GPnllkLIKRYNYRGIPLPLVKKI--ARQVLQGLDYLHTKcGIIHTDIKPENVLL 153
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 8119 qTRSSTNVKLIDFGLATRLD---PNEVvkittGTAEFAAPEIVNREPVGFYTDMWATGVLSYVLLSG---LSPFAGDN-- 8190
Cdd:cd14136   154 -CISKIEVKIADLGNACWTDkhfTEDI-----QTRQYRSPEVILGAGYGTPADIWSTACMAFELATGdylFDPHSGEDys 227
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 8191 ---D-----VQTLKNV----------------KACD---------WDFD---VESFKYISEEAK---DFIRKLLVRNKEK 8231
Cdd:cd14136   228 rdeDhlaliIELLGRIprsiilsgkysreffnRKGElrhisklkpWPLEdvlVEKYKWSKEEAKefaSFLLPMLEYDPEK 307
                         330
                  ....*....|...
gi 281359561 8232 RMTAHECLLHPWL 8244
Cdd:cd14136   308 RATAAQCLQHPWL 320
Ig_C5_MyBP-C cd05894
C5 immunoglobulin (Ig) domain of cardiac myosin binding protein C (MyBP-C); The members here ...
3509-3590 1.13e-12

C5 immunoglobulin (Ig) domain of cardiac myosin binding protein C (MyBP-C); The members here are composed of the C5 immunoglobulin (Ig) domain of cardiac myosin binding protein C (MyBP-C). MyBP-C consists of repeated domains, Ig and fibronectin type 3, and various linkers. Three isoforms of MYBP-C exist: slow-skeletal (ssMyBP-C), fast-skeletal (fsMyBP-C), and cardiac (cMyBP-C). cMYBP-C has insertions between and inside domains and an additional cardiac-specific Ig domain at the N-terminus. For cMYBP_C an interaction has been demonstrated between this C5 domain and the Ig C8 domain.


Pssm-ID: 409475  Cd Length: 86  Bit Score: 67.17  E-value: 1.13e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 3509 VIVKTGLSISLDINIRGEPAPKVEWFFNNSSVTSDEHSVKIDNVDYNTKFFVMRAQRSQSGKYIIKATNEVGEDEAELEV 3588
Cdd:cd05894     5 IVVVAGNKLRLDVPISGEPAPTVTWSRGDKAFTATEGRVRVESYKDLSSFVIEGAEREDEGVYTITVTNPVGEDHASLFV 84

                  ..
gi 281359561 3589 TV 3590
Cdd:cd05894    85 KV 86
FN3 smart00060
Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, ...
4484-4566 1.15e-12

Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, fibronectin. The tenth fibronectin type III repeat contains a RGD cell recognition sequence in a flexible loop between 2 strands. Type III modules are present in both extracellular and intracellular proteins.


Pssm-ID: 214495 [Multi-domain]  Cd Length: 83  Bit Score: 67.25  E-value: 1.15e-12
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561   4484 PGKPEGpLEVSEVHKDGCKLKWKKPKDDGGEPVESYLVEKFDPDTGIWLPVGRSDG-PEYNVDGLVPGHDYKFRVKAVNK 4562
Cdd:smart00060    1 PSPPSN-LRVTDVTSTSVTLSWEPPPDDGITGYIVGYRVEYREEGSEWKEVNVTPSsTSYTLTGLKPGTEYEFRVRAVNG 79

                    ....
gi 281359561   4563 EGES 4566
Cdd:smart00060   80 AGEG 83
FN3 smart00060
Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, ...
6470-6542 1.43e-12

Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, fibronectin. The tenth fibronectin type III repeat contains a RGD cell recognition sequence in a flexible loop between 2 strands. Type III modules are present in both extracellular and intracellular proteins.


Pssm-ID: 214495 [Multi-domain]  Cd Length: 83  Bit Score: 66.87  E-value: 1.43e-12
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 281359561   6470 ITRNGVTLSWRPPRTDG-KSRIKGYYVEMRPKNGkDWKTVNDIPiNSTVYTVPSLKEGEEYSFRVVAENEVGRS 6542
Cdd:smart00060   12 VTSTSVTLSWEPPPDDGiTGYIVGYRVEYREEGS-EWKEVNVTP-SSTSYTLTGLKPGTEYEFRVRAVNGAGEG 83
FN3 smart00060
Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, ...
3694-3777 1.45e-12

Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, fibronectin. The tenth fibronectin type III repeat contains a RGD cell recognition sequence in a flexible loop between 2 strands. Type III modules are present in both extracellular and intracellular proteins.


Pssm-ID: 214495 [Multi-domain]  Cd Length: 83  Bit Score: 66.87  E-value: 1.45e-12
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561   3694 PDRPGKPEPTNWDKDFVDLAWDPPKNDGG-APIQKYVIQMRDKSGRaWVdSATVPGDKCNGTVTGVEEGHEYEFRIVAVN 3772
Cdd:smart00060    1 PSPPSNLRVTDVTSTSVTLSWEPPPDDGItGYIVGYRVEYREEGSE-WK-EVNVTPSSTSYTLTGLKPGTEYEFRVRAVN 78

                    ....*
gi 281359561   3773 KAGPS 3777
Cdd:smart00060   79 GAGEG 83
STKc_JNK3 cd07874
Catalytic domain of the Serine/Threonine Kinase, c-Jun N-terminal Kinase 3; STKs catalyze the ...
7971-8244 1.60e-12

Catalytic domain of the Serine/Threonine Kinase, c-Jun N-terminal Kinase 3; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. JNK3 is expressed primarily in the brain, and to a lesser extent in the heart and testis. Mice deficient in JNK3 are protected against kainic acid-induced seizures, stroke, sciatic axotomy neural death, and neuronal death due to NGF deprivation, oxidative stress, or exposure to beta-amyloid peptide. This suggests that JNK3 may play roles in the pathogenesis of these diseases. JNKs are mitogen-activated protein kinases (MAPKs) that are involved in many stress-activated responses including those during inflammation, neurodegeneration, apoptosis, and persistent pain sensitization, among others. The JNK3 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 143379 [Multi-domain]  Cd Length: 355  Bit Score: 73.20  E-value: 1.60e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 7971 SKFVPQPVEISQQSVYDRYDILEEIGTGAFGVVHRCRERSTGNIFAAKFI--PVSHSVEKDLIRREIDIMNQLHHQKLIN 8048
Cdd:cd07874     1 NQFYSVEVGDSTFTVLKRYQNLKPIGSGAQGIVCAAYDAVLDRNVAIKKLsrPFQNQTHAKRAYRELVLMKCVNHKNIIS 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 8049 LHDAF------EDDDEMILILEFLSGgELFERITAEgyvmTEAEVINYM-RQICEGIRHMHEQNIIHLDIKPENIMcqTR 8121
Cdd:cd07874    81 LLNVFtpqkslEEFQDVYLVMELMDA-NLCQVIQME----LDHERMSYLlYQMLCGIKHLHSAGIIHRDLKPSNIV--VK 153
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 8122 SSTNVKLIDFGLATRLDPNEVVKITTGTAEFAAPEIVNREPVGFYTDMWATGVLSYVLLSGLSPFAGDNDVQ-------- 8193
Cdd:cd07874   154 SDCTLKILDFGLARTAGTSFMMTPYVVTRYYRAPEVILGMGYKENVDIWSVGCIMGEMVRHKILFPGRDYIDqwnkvieq 233
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 8194 --------------TLKNV-----KACDWDF-----------DVESFKYISEEAKDFIRKLLVRNKEKRMTAHECLLHPW 8243
Cdd:cd07874   234 lgtpcpefmkklqpTVRNYvenrpKYAGLTFpklfpdslfpaDSEHNKLKASQARDLLSKMLVIDPAKRISVDEALQHPY 313

                  .
gi 281359561 8244 L 8244
Cdd:cd07874   314 I 314
COG4733 COG4733
Phage-related protein, tail protein J [Mobilome: prophages, transposons];
4982-5270 1.61e-12

Phage-related protein, tail protein J [Mobilome: prophages, transposons];


Pssm-ID: 443767 [Multi-domain]  Cd Length: 978  Bit Score: 75.37  E-value: 1.61e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 4982 DRSSLVEVRIKAGQSFTFDCKVSGEPAPQTKWLLKKKEVYSKDnVKVTNVdyntklkvnsaTRSDSGIYTVFAENANGE- 5060
Cdd:COG4733   448 GTSVARTVQSVAGRTLTVSTAYSETPEAGAVWAFGPDELETQL-FRVVSI-----------EENEDGTYTITAVQHAPEk 515
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 5061 -DSADVKVTVIDKPAPPNGPLKVDEI------NSESCTLH--WNPPDDDggqpiDNYVVEKLDETtGRWIPAGETDGpvT 5131
Cdd:COG4733   516 yAAIDAGAFDDVPPQWPPVNVTTSESlsvvaqGTAVTTLTvsWDAPAGA-----VAYEVEWRRDD-GNWVSVPRTSG--T 587
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 5132 ALKVGGLTPGHkYKFRVRAKNRQGTSEPLTTAQAIIAKNPFDVPTKPG--TPTIKDFDkefVDLEWTRPEadgGSPITGY 5209
Cdd:COG4733   588 SFEVPGIYAGD-YEVRVRAINALGVSSAWAASSETTVTGKTAPPPAPTglTATGGLGG---ITLSWSFPV---DADTLRT 660
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 281359561 5210 VVEKRDkfSPDWEKcAEISDDITNAH---VPDLIEGLKYEFRVRAVNKAGPGSPSDATETHVAR 5270
Cdd:COG4733   661 EIRYST--TGDWAS-ATVAQALYPGNtytLAGLKAGQTYYYRARAVDRSGNVSAWWVSGQASAD 721
FN3 smart00060
Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, ...
3296-3380 1.80e-12

Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, fibronectin. The tenth fibronectin type III repeat contains a RGD cell recognition sequence in a flexible loop between 2 strands. Type III modules are present in both extracellular and intracellular proteins.


Pssm-ID: 214495 [Multi-domain]  Cd Length: 83  Bit Score: 66.48  E-value: 1.80e-12
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561   3296 PSKPEGpIEVSDIHKEGCKLKWRKPKDDGGI-PITGYVIEKMDTaTGKWVPAgSVDPEKYDIEIKGLDPNHRYQFRVKAV 3374
Cdd:smart00060    1 PSPPSN-LRVTDVTSTSVTLSWEPPPDDGITgYIVGYRVEYREE-GSEWKEV-NVTPSSTSYTLTGLKPGTEYEFRVRAV 77

                    ....*.
gi 281359561   3375 NEEGES 3380
Cdd:smart00060   78 NGAGEG 83
IG_like smart00410
Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.
7664-7735 1.96e-12

Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.


Pssm-ID: 214653 [Multi-domain]  Cd Length: 85  Bit Score: 66.37  E-value: 1.96e-12
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 281359561   7664 NAQFTCTINGVPKPTISWYK-GAREISNGARYHMYSEGDNHFLNINDVFGEDADEYVCRAVNKAGAKSTRATL 7735
Cdd:smart00410   11 SVTLSCEASGSPPPEVTWYKqGGKLLAESGRFSVSRSGSTSTLTISNVTPEDSGTYTCAATNSSGSASSGTTL 83
STKc_TAO1 cd06635
Catalytic domain of the Serine/Threonine Kinase, Thousand-and-One Amino acids 1; STKs catalyze ...
7992-8241 2.47e-12

Catalytic domain of the Serine/Threonine Kinase, Thousand-and-One Amino acids 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. TAO1 is sometimes referred to as prostate-derived sterile 20-like kinase 2 (PSK2). TAO1 activates the p38 MAPK through direct interaction with and activation of MEK3. TAO1 is highly expressed in the brain and may play a role in neuronal apoptosis. TAO1 interacts with the checkpoint proteins BubR1 and Mad2, and plays an important role in regulating mitotic progression, which is required for both chromosome congression and checkpoint-induced anaphase delay. TAO1 may play a role in protecting genomic stability. TAO proteins possess MAPK kinase kinase activity. MAPK signaling cascades are important in mediating cellular responses to extracellular signals. The TAO1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270805 [Multi-domain]  Cd Length: 317  Bit Score: 72.39  E-value: 2.47e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 7992 LEEIGTGAFGVVHRCRERSTGNIFAAKFIPVS--HSVEK--DLIRrEIDIMNQLHHQKLINLHDAFEDDDEMILILEFL- 8066
Cdd:cd06635    30 LREIGHGSFGAVYFARDVRTSEVVAIKKMSYSgkQSNEKwqDIIK-EVKFLQRIKHPNSIEYKGCYLREHTAWLVMEYCl 108
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 8067 -SGGELFEritAEGYVMTEAEVINYMRQICEGIRHMHEQNIIHLDIKPENIMCQtrSSTNVKLIDFGLATRLDP-NEVVk 8144
Cdd:cd06635   109 gSASDLLE---VHKKPLQEIEIAAITHGALQGLAYLHSHNMIHRDIKAGNILLT--EPGQVKLADFGSASIASPaNSFV- 182
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 8145 ittGTAEFAAPEIVNREPVGFY---TDMWATGVLSYVLLSGLSPFAGDNDVQTLKNVkACDWDFDVESFKYiSEEAKDFI 8221
Cdd:cd06635   183 ---GTPYWMAPEVILAMDEGQYdgkVDVWSLGITCIELAERKPPLFNMNAMSALYHI-AQNESPTLQSNEW-SDYFRNFV 257
                         250       260
                  ....*....|....*....|
gi 281359561 8222 RKLLVRNKEKRMTAHECLLH 8241
Cdd:cd06635   258 DSCLQKIPQDRPTSEELLKH 277
FN3 smart00060
Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, ...
4584-4667 2.49e-12

Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, fibronectin. The tenth fibronectin type III repeat contains a RGD cell recognition sequence in a flexible loop between 2 strands. Type III modules are present in both extracellular and intracellular proteins.


Pssm-ID: 214495 [Multi-domain]  Cd Length: 83  Bit Score: 66.10  E-value: 2.49e-12
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561   4584 PTKPGVPEPTDWTANKVELAWPEPASDGG-SPIQGYIVEVKDKySPLWEKaLETNSPTPTATVQGLIEGNEYQFRVVALN 4662
Cdd:smart00060    1 PSPPSNLRVTDVTSTSVTLSWEPPPDDGItGYIVGYRVEYREE-GSEWKE-VNVTPSSTSYTLTGLKPGTEYEFRVRAVN 78

                    ....*
gi 281359561   4663 KGGLS 4667
Cdd:smart00060   79 GAGEG 83
PTKc_Syk_like cd05060
Catalytic domain of Spleen Tyrosine Kinase-like Protein Tyrosine Kinases; PTKs catalyze the ...
7993-8201 2.62e-12

Catalytic domain of Spleen Tyrosine Kinase-like Protein Tyrosine Kinases; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. The Syk-like subfamily is composed of Syk, ZAP-70, Shark, and similar proteins. They are cytoplasmic (or nonreceptor) PTKs containing two Src homology 2 (SH2) domains N-terminal to the catalytic tyr kinase domain. They are involved in the signaling downstream of activated receptors (including B-cell, T-cell, and Fc receptors) that contain ITAMs (immunoreceptor tyr activation motifs), leading to processes such as cell proliferation, differentiation, survival, adhesion, migration, and phagocytosis. Syk is important in B-cell receptor signaling, while Zap-70 is primarily expressed in T-cells and NK cells, and is a crucial component in T-cell receptor signaling. Syk also plays a central role in Fc receptor-mediated phagocytosis in the adaptive immune system. Shark is exclusively expressed in ectodermally derived epithelia, and is localized preferentially to the apical surface of the epithelial cells, it may play a role in a signaling pathway for epithelial cell polarity. The Syk-like subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270650 [Multi-domain]  Cd Length: 257  Bit Score: 71.23  E-value: 2.62e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 7993 EEIGTGAFGVVHRCRERSTGNI---FAAKFIPVSHSV-EKDLIRREIDIMNQLHHQ---KLINLHDAfeddDEMILILEF 8065
Cdd:cd05060     1 KELGHGNFGSVRKGVYLMKSGKeveVAVKTLKQEHEKaGKKEFLREASVMAQLDHPcivRLIGVCKG----EPLMLVMEL 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 8066 LSGGELFERITAEGyVMTEAEVINYMRQICEGIRHMHEQNIIHLDIKPENIMCQTRSstNVKLIDFGLATRLDP-NEVVK 8144
Cdd:cd05060    77 APLGPLLKYLKKRR-EIPVSDLKELAHQVAMGMAYLESKHFVHRDLAARNVLLVNRH--QAKISDFGMSRALGAgSDYYR 153
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 281359561 8145 ITTG---TAEFAAPEIVNREPVGFYTDMWATGVLSYVLLS-GLSPFAGDNDVQTLKNVKAC 8201
Cdd:cd05060   154 ATTAgrwPLKWYAPECINYGKFSSKSDVWSYGVTLWEAFSyGAKPYGEMKGPEVIAMLESG 214
FN3 COG3401
Fibronectin type 3 domain [General function prediction only];
5640-5860 2.67e-12

Fibronectin type 3 domain [General function prediction only];


Pssm-ID: 442628 [Multi-domain]  Cd Length: 603  Bit Score: 74.27  E-value: 2.67e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 5640 RYTLILKNEHGSFDASAHATVLDRPSPPKGP--LDITKITRDGCHLTWNVPDDDGgspILHYIIEKMDLSRSTWSDAGMS 5717
Cdd:COG3401   206 YYRVAATDTGGESAPSNEVSVTTPTTPPSAPtgLTATADTPGSVTLSWDPVTESD---ATGYRVYRSNSGDGPFTKVATV 282
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 5718 THIVHDVTRLVHRKEYLFRVKAVNAIG-ESDPLEAVNTIIAKNEfdePDAPGKPIITDWDRDHIDLQWAvPKSDGGApiS 5796
Cdd:COG3401   283 TTTSYTDTGLTNGTTYYYRVTAVDAAGnESAPSNVVSVTTDLTP---PAAPSGLTATAVGSSSITLSWT-ASSDADV--T 356
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 281359561 5797 EYIIQKKEKGSPYWTNVrHVPSNKNTTTIPELTEGQEYEFRVIAVNQAGQSepSEPSDMIMAKP 5860
Cdd:COG3401   357 GYNVYRSTSGGGTYTKI-AETVTTTSYTDTGLTPGTTYYYKVTAVDAAGNE--SAPSEEVSATT 417
IgI_telokin-like cd20973
immunoglobulin-like domain of telokin and similar proteins; a member of the I-set of IgSF ...
7652-7737 2.72e-12

immunoglobulin-like domain of telokin and similar proteins; a member of the I-set of IgSF domains; The members here are composed of the immunoglobulin (Ig) domain in telokin, the C-terminal domain of myosin light chain kinase which is identical to telokin, and similar proteins. The Ig superfamily (IgSF) is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. Unlike the V-set, one of the distinctive features of I-set domains is the lack of a C" strand. The structure of the telokin Ig domain lacks this strand and thus it belongs to the I-set of the IgSF. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors, the hemolymph protein hemolin, the muscle proteins titin, telokin, and twitchin, the neuronal adhesion molecule axonin-1, and the signaling molecule semaphorin 4D that is involved in axonal guidance, immune function and angiogenesis.


Pssm-ID: 409565 [Multi-domain]  Cd Length: 88  Bit Score: 66.06  E-value: 2.72e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 7652 KPLRDANCIQNHNAQFTCTINGVPKPTISWYKGAREISNGARYHMYSEGD-NHFLNINDVFGEDADEYVCRAVNKAGAKS 7730
Cdd:cd20973     2 QTLRDKEVVEGSAARFDCKVEGYPDPEVKWMKDDNPIVESRRFQIDQDEDgLCSLIISDVCGDDSGKYTCKAVNSLGEAT 81

                  ....*..
gi 281359561 7731 TRATLAI 7737
Cdd:cd20973    82 CSAELTV 88
I-set pfam07679
Immunoglobulin I-set domain;
2902-2995 2.79e-12

Immunoglobulin I-set domain;


Pssm-ID: 400151 [Multi-domain]  Cd Length: 90  Bit Score: 66.13  E-value: 2.79e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561  2902 PRIDRSnLKPLLIRAGKPIRYDVNVRGEPAPVITWYQNDKELKPEelpSSSEIKNIPYNTKISIIETVRKHTGIYKIIAV 2981
Cdd:pfam07679    1 PKFTQK-PKDVEVQEGESARFTCTVTGTPDPEVSWFKDGQPLRSS---DRFKVTYEGGTYTLTISNVQPDDSGKYTCVAT 76
                           90
                   ....*....|....
gi 281359561  2982 NEHGQDEATVEVNI 2995
Cdd:pfam07679   77 NSAGEAEASAELTV 90
STKc_HIPK2 cd14227
Catalytic domain of the Serine/Threonine Kinase, Homeodomain-Interacting Protein Kinase 2; ...
7984-8198 2.83e-12

Catalytic domain of the Serine/Threonine Kinase, Homeodomain-Interacting Protein Kinase 2; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. HIPK2, the most studied HIPK, is a coregulator of many transcription factors and cofactors including homeodomain proteins (Nkx and HOX families), Smad1-4, Pax6, c-Myb, AML1, the histone acetyltransferase p300, and the tumor repressor p53, among others. It regulates gene transcription during development and in DNA damage response (DDR), and mediates cell processes such as apoptosis, survival, differentiation, and proliferation. HIPK2 mediates apoptosis by phosphorylating and activating p53 during DDR, resulting in the activation of apoptotic genes. In the absence of p53, HIPK2 targets the anti-apoptotic corepressor C-terminal binding protein (CtBP), leading to CtBP's degradation and the promotion of apoptosis. HIPKs, originally identified by their ability to bind homeobox factors, are nuclear proteins containing catalytic kinase and homeobox-interacting domains as well as a PEST region overlapping with the speckle-retention signal (SRS). The HIPK2 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271129 [Multi-domain]  Cd Length: 355  Bit Score: 72.82  E-value: 2.83e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 7984 SVYDRYDILEEIGTGAFGVVHRCRERSTGNIFAAKFIPvSHSVEKDLIRREIDIMNQLHHQ-----KLINLHDAFEDDDE 8058
Cdd:cd14227    12 SMTNTYEVLEFLGRGTFGQVVKCWKRGTNEIVAIKILK-NHPSYARQGQIEVSILARLSTEsaddyNFVRAYECFQHKNH 90
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 8059 MILILEFLSgGELFERITAEGYVMTEAEVIN-YMRQICEGIRHMHEQNIIHLDIKPENIMC--QTRSSTNVKLIDFGLAT 8135
Cdd:cd14227    91 TCLVFEMLE-QNLYDFLKQNKFSPLPLKYIRpILQQVATALMKLKSLGLIHADLKPENIMLvdPSRQPYRVKVIDFGSAS 169
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 281359561 8136 RLDpNEVVKITTGTAEFAAPEIVNREPVGFYTDMWATGVLSYVLLSGLSPFAGDNDVQTLKNV 8198
Cdd:cd14227   170 HVS-KAVCSTYLQSRYYRAPEIILGLPFCEAIDMWSLGCVIAELFLGWPLYPGASEYDQIRYI 231
PTKc_Src_Fyn_like cd14203
Catalytic domain of a subset of Src kinase-like Protein Tyrosine Kinases; PTKs catalyze the ...
7994-8199 3.12e-12

Catalytic domain of a subset of Src kinase-like Protein Tyrosine Kinases; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. This subfamily includes a subset of Src-like PTKs including Src, Fyn, Yrk, and Yes, which are all widely expressed. Yrk has been detected only in chickens. It is primarily found in neuronal and epithelial cells and in macrophages. It may play a role in inflammation and in response to injury. Src (or c-Src) proteins are cytoplasmic (or non-receptor) PTKs which are anchored to the plasma membrane. They contain an N-terminal SH4 domain with a myristoylation site, followed by SH3 and SH2 domains, a tyr kinase domain, and a regulatory C-terminal region containing a conserved tyr. They are activated by autophosphorylation at the tyr kinase domain, but are negatively regulated by phosphorylation at the C-terminal tyr by Csk (C-terminal Src Kinase). Src proteins are involved in signaling pathways that regulate cytokine and growth factor responses, cytoskeleton dynamics, cell proliferation, survival, and differentiation. They were identified as the first proto-oncogene products, and they regulate cell adhesion, invasion, and motility in cancer cells and tumor vasculature, contributing to cancer progression and metastasis. They are also implicated in acute inflammatory responses and osteoclast function. The Src/Fyn-like subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271105 [Multi-domain]  Cd Length: 248  Bit Score: 70.72  E-value: 3.12e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 7994 EIGTGAFGVVHRCRERSTGNIFAAKFIPVSHSVEKDLirREIDIMNQLHHQKLINLHdAFEDDDEMILILEFLSGGELFE 8073
Cdd:cd14203     2 KLGQGCFGEVWMGTWNGTTKVAIKTLKPGTMSPEAFL--EEAQIMKKLRHDKLVQLY-AVVSEEPIYIVTEFMSKGSLLD 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 8074 RIT-AEGYVMTEAEVINYMRQICEGIRHMHEQNIIHLDIKPENIMCQTRSStnVKLIDFGLATRLDPNEVVkiTTGTAEF 8152
Cdd:cd14203    79 FLKdGEGKYLKLPQLVDMAAQIASGMAYIERMNYIHRDLRAANILVGDNLV--CKIADFGLARLIEDNEYT--ARQGAKF 154
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 281359561 8153 ----AAPEIVNREPVGFYTDMWATGVLSYVLLS-GLSPFAGDNDVQTLKNVK 8199
Cdd:cd14203   155 pikwTAPEAALYGRFTIKSDVWSFGILLTELVTkGRVPYPGMNNREVLEQVE 206
IgI_1_Titin_Z1z2-like cd20974
First Ig-like domain of the giant muscle protein titin Z1z2 in the sarcomeric Z-disk and ...
3506-3591 4.22e-12

First Ig-like domain of the giant muscle protein titin Z1z2 in the sarcomeric Z-disk and similar proteins; a member of the I-set of IgSF domains; The members here are composed of the first immunoglobulin (Ig)-like domain of the giant muscle protein titin Z1z2 in the sarcomeric Z-disk and similar proteins. Titin is a key component in the assembly and functioning of vertebrate striated muscles. By providing connections at the level of individual microfilaments, it contributes to the fine balance of forces between the two halves of the sarcomere. The Ig superfamily (IgSF) is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. Unlike the V-set, one of the distinctive features of I-set domains is the lack of a C" strand. The structure of the titin Z1z2 lacks this strand and thus it belongs to the I-set of the IgSF. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors, the hemolymph protein hemolin, the muscle proteins titin, telokin, and twitchin, the neuronal adhesion molecule axonin-1, and the signaling molecule semaphorin 4D that is involved in axonal guidance, immune function and angiogenesis.


Pssm-ID: 409566 [Multi-domain]  Cd Length: 93  Bit Score: 65.84  E-value: 4.22e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 3506 LKPVIVKTGLSISLDINIRGEPAPKVEWFFNNSSV-TSDEHSVKIDNVDYNTKFFVMRAQRSQSGKYIIKATNEVGEDEA 3584
Cdd:cd20974     7 LQSVVVLEGSTATFEAHVSGKPVPEVSWFRDGQVIsTSTLPGVQISFSDGRAKLSIPAVTKANSGRYSLTATNGSGQATS 86

                  ....*..
gi 281359561 3585 ELEVTVL 3591
Cdd:cd20974    87 TAELLVL 93
PKc_CLK1_4 cd14213
Catalytic domain of the Dual-specificity protein kinases, CDC-like kinases 1 and 4; ...
7988-8244 4.42e-12

Catalytic domain of the Dual-specificity protein kinases, CDC-like kinases 1 and 4; Dual-specificity PKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine as well as tyrosine residues on protein substrates. CLK1 plays a role in neuronal differentiation. CLKs are involved in the phosphorylation and regulation of serine/arginine-rich (SR) proteins, which play a crucial role in pre-mRNA splicing by directing splice site selection. SR proteins are phosphorylated first by SR protein kinases (SRPKs) at the N-terminus, which leads to its assembly into nuclear speckles where splicing factors are stored. CLKs phosphorylate the C-terminal part of SR proteins, causing the nuclear speckles to dissolve and splicing factors to be recruited at sites of active transcription. Based on a conserved "EHLAMMERILG" signature motif which may be crucial for substrate specificity, CLKs are also referred to as LAMMER kinases. CLKs autophosphorylate at tyrosine residues and phosphorylate their substrates exclusively on serine/threonine residues. The CLK1/4 subfamily is part of a larger superfamily that includes the catalytic domains of other protein serine/threonine PKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271115 [Multi-domain]  Cd Length: 330  Bit Score: 71.81  E-value: 4.42e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 7988 RYDILEEIGTGAFGVVHRCRERSTGNIFAAKFIPVSHSVEKDLIRREIDIMNQLHHQ------KLINLHDAFEDDDEMIL 8061
Cdd:cd14213    13 RYEIVDTLGEGAFGKVVECIDHKMGGMHVAVKIVKNVDRYREAARSEIQVLEHLNTTdpnstfRCVQMLEWFDHHGHVCI 92
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 8062 ILEFLsGGELFERITAEGYVMTEAEVINYMR-QICEGIRHMHEQNIIHLDIKPENIMC-----------------QTRSS 8123
Cdd:cd14213    93 VFELL-GLSTYDFIKENSFLPFPIDHIRNMAyQICKSVNFLHHNKLTHTDLKPENILFvqsdyvvkynpkmkrdeRTLKN 171
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 8124 TNVKLIDFGLATRLDPNEVVKITtgTAEFAAPEIVNREPVGFYTDMWATG--VLSYVL-------------LSGLSPFAG 8188
Cdd:cd14213   172 PDIKVVDFGSATYDDEHHSTLVS--TRHYRAPEVILALGWSQPCDVWSIGciLIEYYLgftvfqthdskehLAMMERILG 249
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 8189 DNDVQTLKNVKA--------CDWDFDVESFKYISEEAK-----------------DFIRKLLVRNKEKRMTAHECLLHPW 8243
Cdd:cd14213   250 PLPKHMIQKTRKrkyfhhdqLDWDEHSSAGRYVRRRCKplkefmlsqdvdheqlfDLIQKMLEYDPAKRITLDEALKHPF 329

                  .
gi 281359561 8244 L 8244
Cdd:cd14213   330 F 330
IG_like smart00410
Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.
8751-8829 4.44e-12

Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.


Pssm-ID: 214653 [Multi-domain]  Cd Length: 85  Bit Score: 65.60  E-value: 4.44e-12
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561   8751 VRDGDAVNLACRIIGAQHFDVVWLHNN-KEIKPSKDFQYTNEANIYRLQIAEIFPEDGGTYTCEAFNDIGESFSTCTINV 8829
Cdd:smart00410    6 VKEGESVTLSCEASGSPPPEVTWYKQGgKLLAESGRFSVSRSGSTSTLTISNVTPEDSGTYTCAATNSSGSASSGTTLTV 85
FN3 smart00060
Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, ...
2801-2884 4.55e-12

Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, fibronectin. The tenth fibronectin type III repeat contains a RGD cell recognition sequence in a flexible loop between 2 strands. Type III modules are present in both extracellular and intracellular proteins.


Pssm-ID: 214495 [Multi-domain]  Cd Length: 83  Bit Score: 65.33  E-value: 4.55e-12
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561   2801 PNKPGTPEVTDYDNQSISLKWAAPNNDGG-APIQKYIIEKKNKNkTEWEKaLEIPGDQLEATVAGLQEYGEYQFRVIAVN 2879
Cdd:smart00060    1 PSPPSNLRVTDVTSTSVTLSWEPPPDDGItGYIVGYRVEYREEG-SEWKE-VNVTPSSTSYTLTGLKPGTEYEFRVRAVN 78

                    ....*
gi 281359561   2880 KAGLS 2884
Cdd:smart00060   79 GAGEG 83
FN3 smart00060
Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, ...
4185-4267 5.64e-12

Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, fibronectin. The tenth fibronectin type III repeat contains a RGD cell recognition sequence in a flexible loop between 2 strands. Type III modules are present in both extracellular and intracellular proteins.


Pssm-ID: 214495 [Multi-domain]  Cd Length: 83  Bit Score: 65.33  E-value: 5.64e-12
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561   4185 PGPPEGpLRVTDVHKEGCKLKWNAPLDDGGL-PIDHYIIEKMDVESGRWLPSGRFKESFAELNNLEPSHEYKFRVLAVNT 4263
Cdd:smart00060    1 PSPPSN-LRVTDVTSTSVTLSWEPPPDDGITgYIVGYRVEYREEGSEWKEVNVTPSSTSYTLTGLKPGTEYEFRVRAVNG 79

                    ....
gi 281359561   4264 EGES 4267
Cdd:smart00060   80 AGEG 83
FN3 smart00060
Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, ...
3990-4072 6.16e-12

Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, fibronectin. The tenth fibronectin type III repeat contains a RGD cell recognition sequence in a flexible loop between 2 strands. Type III modules are present in both extracellular and intracellular proteins.


Pssm-ID: 214495 [Multi-domain]  Cd Length: 83  Bit Score: 64.94  E-value: 6.16e-12
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561   3990 DTPGKPQIVDWSGNHCDLKWRAPEDDGGAS-ITGYIVERKDPNtGKWQKaLETSTPDCKARVNDLIAGNKYQFRIMAVNK 4068
Cdd:smart00060    2 SPPSNLRVTDVTSTSVTLSWEPPPDDGITGyIVGYRVEYREEG-SEWKE-VNVTPSSTSYTLTGLKPGTEYEFRVRAVNG 79

                    ....
gi 281359561   4069 AGKS 4072
Cdd:smart00060   80 AGEG 83
I-set pfam07679
Immunoglobulin I-set domain;
2602-2693 7.54e-12

Immunoglobulin I-set domain;


Pssm-ID: 400151 [Multi-domain]  Cd Length: 90  Bit Score: 64.97  E-value: 7.54e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561  2602 PQIDRSTfKRVTIKSGRTHKWSVDVLGEPIPELHWSwRDDIPLTNGDRIKIENVDYHTDFSITNVLRKDSGFYTLKAENR 2681
Cdd:pfam07679    1 PKFTQKP-KDVEVQEGESARFTCTVTGTPDPEVSWF-KDGQPLRSSDRFKVTYEGGTYTLTISNVQPDDSGKYTCVATNS 78
                           90
                   ....*....|..
gi 281359561  2682 NGIDRETVELVV 2693
Cdd:pfam07679   79 AGEAEASAELTV 90
FN3 smart00060
Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, ...
7837-7918 7.86e-12

Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, fibronectin. The tenth fibronectin type III repeat contains a RGD cell recognition sequence in a flexible loop between 2 strands. Type III modules are present in both extracellular and intracellular proteins.


Pssm-ID: 214495 [Multi-domain]  Cd Length: 83  Bit Score: 64.56  E-value: 7.86e-12
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561   7837 PDPPRFPLIESIGTESLSLSWKAPVWDGC-SDITNYYVERREHPlSSWIRV-GNTRFTSMAVSGLTPGKEYDFRIFADNV 7914
Cdd:smart00060    1 PSPPSNLRVTDVTSTSVTLSWEPPPDDGItGYIVGYRVEYREEG-SEWKEVnVTPSSTSYTLTGLKPGTEYEFRVRAVNG 79

                    ....
gi 281359561   7915 YGRS 7918
Cdd:smart00060   80 AGEG 83
Ig_Titin_like cd05748
Immunoglobulin (Ig)-like domain of titin and similar proteins; The members here are composed ...
2914-2993 8.19e-12

Immunoglobulin (Ig)-like domain of titin and similar proteins; The members here are composed of the immunoglobulin (Ig)-like domain found in titin-like proteins and similar proteins. Titin (also called connectin) is a fibrous sarcomeric protein specifically found in vertebrate striated muscle. Titin is a giant protein; depending on isoform composition, it ranges from 2970 to 3700 kDa, and is of a length that spans half a sarcomere. Titin largely consists of multiple repeats of Ig-like and fibronectin type 3 (FN-III)-like domains. Titin connects the ends of myosin thick filaments to Z disks and extends along the thick filament to the H zone. It appears to function similarly to an elastic band, keeping the myosin filaments centered in the sarcomere during muscle contraction or stretching. Within the sarcomere, titin is also attached to or is associated with myosin binding protein C (MyBP-C). MyBP-C appears to contribute to the generation of passive tension by titin and like titin has repeated Ig-like and FN-III domains. Also included in this group are worm twitchin and insect projectin, thick filament proteins of invertebrate muscle which also have repeated Ig-like and FN-III domains.


Pssm-ID: 409406 [Multi-domain]  Cd Length: 82  Bit Score: 64.53  E-value: 8.19e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 2914 IRAGKPIRYDVNVRGEPAPVITWYQNDKELKPEELPSsseIKNIPYNTKISIIETVRKHTGIYKIIAVNEHGQDEATVEV 2993
Cdd:cd05748     4 VRAGESLRLDIPIKGRPTPTVTWSKDGQPLKETGRVQ---IETTASSTSLVIKNAKRSDSGKYTLTLKNSAGEKSATINV 80
PTKc_Fes cd05084
Catalytic domain of the Protein Tyrosine Kinase, Fes; PTKs catalyze the transfer of the ...
7993-8199 8.25e-12

Catalytic domain of the Protein Tyrosine Kinase, Fes; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Fes (or Fps) is a cytoplasmic (or nonreceptor) PTK containing an N-terminal region with FCH (Fes/Fer/CIP4 homology) and coiled-coil domains, followed by a SH2 domain, and a C-terminal catalytic domain. The genes for Fes (feline sarcoma) and Fps (Fujinami poultry sarcoma) were first isolated from tumor-causing retroviruses. The viral oncogenes encode chimeric Fes proteins consisting of Gag sequences at the N-termini, resulting in unregulated PTK activity. Fes kinase is expressed in myeloid, vascular endothelial, epithelial, and neuronal cells. It plays important roles in cell growth and differentiation, angiogenesis, inflammation and immunity, and cytoskeletal regulation. A recent study implicates Fes kinase as a tumor suppressor in colorectal cancer. The Fes subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270667 [Multi-domain]  Cd Length: 252  Bit Score: 69.57  E-value: 8.25e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 7993 EEIGTGAFGVVHRCRERSTGNIFAAKF----IPVSHsveKDLIRREIDIMNQLHHQKLINLHDAFEDDDEMILILEFLSG 8068
Cdd:cd05084     2 ERIGRGNFGEVFSGRLRADNTPVAVKScretLPPDL---KAKFLQEARILKQYSHPNIVRLIGVCTQKQPIYIVMELVQG 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 8069 GELFERITAEGYVMTEAEVINYMRQICEGIRHMHEQNIIHLDIKPENimCQTRSSTNVKLIDFGLaTRLDPNEVVKITTG 8148
Cdd:cd05084    79 GDFLTFLRTEGPRLKVKELIRMVENAAAGMEYLESKHCIHRDLAARN--CLVTEKNVLKISDFGM-SREEEDGVYAATGG 155
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 281359561 8149 TAE----FAAPEIVNREPVGFYTDMWATGVLSYVLLS-GLSPFAGDNDVQTLKNVK 8199
Cdd:cd05084   156 MKQipvkWTAPEALNYGRYSSESDVWSFGILLWETFSlGAVPYANLSNQQTREAVE 211
fn3 pfam00041
Fibronectin type III domain;
3890-3973 8.41e-12

Fibronectin type III domain;


Pssm-ID: 394996 [Multi-domain]  Cd Length: 85  Bit Score: 64.74  E-value: 8.41e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561  3890 SKPKGpLAVSNVTAETLHLKWEKPEDDGGdPIEQYLVE-RMDTETGRWVPVLTTKTP-EADVTGLTEGKEYLFRVKAVNS 3967
Cdd:pfam00041    1 SAPSN-LTVTDVTSTSLTVSWTPPPDGNG-PITGYEVEyRPKNSGEPWNEITVPGTTtSVTLTGLKPGTEYEVRVQAVNG 78

                   ....*.
gi 281359561  3968 EGESEP 3973
Cdd:pfam00041   79 GGEGPP 84
FN3 smart00060
Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, ...
3102-3184 9.09e-12

Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, fibronectin. The tenth fibronectin type III repeat contains a RGD cell recognition sequence in a flexible loop between 2 strands. Type III modules are present in both extracellular and intracellular proteins.


Pssm-ID: 214495 [Multi-domain]  Cd Length: 83  Bit Score: 64.56  E-value: 9.09e-12
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561   3102 SKPGTPNIVDYNEHMVKLKWEAPRSDGG-APISGYIIEKKDKfSPIWDEIlSTNTSVPEATVEGLVEGNIYQFRVRAVNK 3180
Cdd:smart00060    2 SPPSNLRVTDVTSTSVTLSWEPPPDDGItGYIVGYRVEYREE-GSEWKEV-NVTPSSTSYTLTGLKPGTEYEFRVRAVNG 79

                    ....
gi 281359561   3181 AGFS 3184
Cdd:smart00060   80 AGEG 83
fn3 pfam00041
Fibronectin type III domain;
2502-2587 9.18e-12

Fibronectin type III domain;


Pssm-ID: 394996 [Multi-domain]  Cd Length: 85  Bit Score: 64.74  E-value: 9.18e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561  2502 SPPSQPVIDDYDNKSVLLKWKrPPSDGGRPITHYIVEIKDKFAPSWsEVAKTDDPNP-ECNVEGLKEKMVYQFRVRAVNK 2580
Cdd:pfam00041    1 SAPSNLTVTDVTSTSLTVSWT-PPPDGNGPITGYEVEYRPKNSGEP-WNEITVPGTTtSVTLTGLKPGTEYEVRVQAVNG 78

                   ....*..
gi 281359561  2581 AGPSEPS 2587
Cdd:pfam00041   79 GGEGPPS 85
COG4733 COG4733
Phage-related protein, tail protein J [Mobilome: prophages, transposons];
5335-5550 9.24e-12

Phage-related protein, tail protein J [Mobilome: prophages, transposons];


Pssm-ID: 443767 [Multi-domain]  Cd Length: 978  Bit Score: 73.06  E-value: 9.24e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 5335 RILDAKRSDTGVYTLTAR----NI-----NGT-DRHNVKVTILDAPSVPEGPLRNGDVSKNSIVLRWRPPKDDGGSEITH 5404
Cdd:COG4733   492 RVVSIEENEDGTYTITAVqhapEKyaaidAGAfDDVPPQWPPVNVTTSESLSVVAQGTAVTTLTVSWDAPAGAVAYEVEW 571
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 5405 YVvekmDNEAmrWVPVGDCTDTEIRADNlIENHDYSFRVRAVNKQGQSQPLTTS--QPITAKDPYshpdkPGQPQ----- 5477
Cdd:COG4733   572 RR----DDGN--WVSVPRTSGTSFEVPG-IYAGDYEVRVRAINALGVSSAWAASseTTVTGKTAP-----PPAPTgltat 639
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 281359561 5478 ATDWGkhfVDLEWSTPKrdgGAPISSYIIEkRPKFGQWERAAVVLGDNCKAH--VPELTNGGEYEFRVIAVNRGG 5550
Cdd:COG4733   640 GGLGG---ITLSWSFPV---DADTLRTEIR-YSTTGDWASATVAQALYPGNTytLAGLKAGQTYYYRARAVDRSG 707
FN3 COG3401
Fibronectin type 3 domain [General function prediction only];
3930-4466 9.39e-12

Fibronectin type 3 domain [General function prediction only];


Pssm-ID: 442628 [Multi-domain]  Cd Length: 603  Bit Score: 72.34  E-value: 9.39e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 3930 DTETGRWVPVLTTKTPEADVTGLTEGKEYLFRVKAVNSEGESEP----LVTDIPTKAKNPFDAADTPGKPQIVdwsgnhc 4005
Cdd:COG3401   177 TAAVATTSLTVTSTTLVDGGGDIEPGTTYYYRVAATDTGGESAPsnevSVTTPTTPPSAPTGLTATADTPGSV------- 249
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 4006 DLKWRAPEDDGgasITGYIVERKDPNTGKWQKAleTSTPDCKARVNDLIAGNKYQFRIMAVNKAGksKPSEPSDQMTAkd 4085
Cdd:COG3401   250 TLSWDPVTESD---ATGYRVYRSNSGDGPFTKV--ATVTTTSYTDTGLTNGTTYYYRVTAVDAAG--NESAPSNVVSV-- 320
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 4086 rfappkidrtnikditikagqhirfdiKVSGEPPAtkvwlhnkarlenddsnynidmesyrtkltvpiskrfhsgkytlk 4165
Cdd:COG3401   321 ---------------------------TTDLTPPA--------------------------------------------- 328
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 4166 aenesgrdeasfevivldkpgPPEGpLRVTDVHKEGCKLKWNAPLDDGglpIDHYIIEKMDVESGRWLPSGR-FKESFAE 4244
Cdd:COG3401   329 ---------------------APSG-LTATAVGSSSITLSWTASSDAD---VTGYNVYRSTSGGGTYTKIAEtVTTTSYT 383
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 4245 LNNLEPSHEYKFRVLAVNTEG-ESEPLTGEQSVIAKNPFDEPGKPGTPEAVDWDKDHVDLVWRPPINDGGSPITGYVVEK 4323
Cdd:COG3401   384 DTGLTPGTTYYYKVTAVDAAGnESAPSEEVSATTASAASGESLTASVDAVPLTDVAGATAAASAASNPGVSAAVLADGGD 463
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 4324 RekGTDKWIKGTEITIPCLGEECKATVPTLNENCEYEFRVKAINAAGPGEPSDASKPIITKPRKLAPKIDRKNIRTYNFK 4403
Cdd:COG3401   464 T--GNAVPFTTTSSTVTATTTDTTTANLSVTTGSLVGGSGASSVTNSVSVIGASAAAAVGGAPDGTPNVTGASPVTVGAS 541
                         490       500       510       520       530       540
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 281359561 4404 SGEPIFLDINISGepAPDVTWNQNNKSVQTTSFSHIENLPYNTKYINNNPERKDTGLYKISAH 4466
Cdd:COG3401   542 TGDVLITDLVSLT--TSASSSVSGAGLGSGNLYLITTLGGSLLTTTSTNTNDVAGVHGGTLLV 602
Ig_3 pfam13927
Immunoglobulin domain; This family contains immunoglobulin-like domains.
7647-7724 9.45e-12

Immunoglobulin domain; This family contains immunoglobulin-like domains.


Pssm-ID: 464046 [Multi-domain]  Cd Length: 78  Bit Score: 64.51  E-value: 9.45e-12
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 281359561  7647 PPLIVKPLRDANCIQNHNAQFTCTINGVPKPTISWYKGAREISNGARYHMYSEGDNHFLNINDVFGEDADEYVCRAVN 7724
Cdd:pfam13927    1 KPVITVSPSSVTVREGETVTLTCEATGSPPPTITWYKNGEPISSGSTRSRSLSGSNSTLTISNVTRSDAGTYTCVASN 78
fn3 pfam00041
Fibronectin type III domain;
7546-7631 9.93e-12

Fibronectin type III domain;


Pssm-ID: 394996 [Multi-domain]  Cd Length: 85  Bit Score: 64.36  E-value: 9.93e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561  7546 SPPGSPQITEIGGDFVHLEWEKPEsDGGAHIQGYWIDKREVGSNT-WQRVNATicaANQINCI--NLIEGRQYEFRIFAQ 7622
Cdd:pfam00041    1 SAPSNLTVTDVTSTSLTVSWTPPP-DGNGPITGYEVEYRPKNSGEpWNEITVP---GTTTSVTltGLKPGTEYEVRVQAV 76

                   ....*....
gi 281359561  7623 NVAGLSTES 7631
Cdd:pfam00041   77 NGGGEGPPS 85
I-set pfam07679
Immunoglobulin I-set domain;
8839-8922 1.07e-11

Immunoglobulin I-set domain;


Pssm-ID: 400151 [Multi-domain]  Cd Length: 90  Bit Score: 64.59  E-value: 1.07e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561  8839 PSFVKFPTSVSVLEGEGTTFECEID-SELLNLVWLKDGKPIDETlPRYSFTKDGHRYSFAVAKCNMDDVGQYQAKAV--S 8915
Cdd:pfam07679    1 PKFTQKPKDVEVQEGESARFTCTVTgTPDPEVSWFKDGQPLRSS-DRFKVTYEGGTYTLTISNVQPDDSGKYTCVATnsA 79

                   ....*..
gi 281359561  8916 GKAESIC 8922
Cdd:pfam07679   80 GEAEASA 86
Ig cd00096
Immunoglobulin domain; The members here are composed of the immunoglobulin (Ig) domain found ...
7272-7339 1.16e-11

Immunoglobulin domain; The members here are composed of the immunoglobulin (Ig) domain found in the Ig superfamily. The Ig superfamily is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. Members of this group are components of immunoglobulin, neuroglia, cell surface glycoproteins, including T-cell receptors, CD2, CD4, CD8, and membrane glycoproteins, including butyrophilin and chondroitin sulfate proteoglycan core protein. A predominant feature of most Ig domains is a disulfide bridge connecting the two beta-sheets with a tryptophan residue packed against the disulfide bond. Ig superfamily (IgSF) domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. Typically, the V-set domains have A, B, E, and D strands in one sheet and A', G, F, C, C' and C" in the other. The structures in C1-set are smaller than those in the V-set; they have one beta sheet that is formed by strands A, B, E, and D and the other by strands G, F, C, and C'. Moreover, a C1-set Ig domain contains a short C' strand (three residues) and lacks A' and C" strand. Unlike other Ig domain sets, C2-set structures do not have a D strand. Like the V-set Ig domains, members of the I-set have a discontinuous A strand, but lack a C" strand.


Pssm-ID: 409353 [Multi-domain]  Cd Length: 70  Bit Score: 63.89  E-value: 1.16e-11
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 281359561 7272 TLQCAASGKPSPTARWLRNGKEIQMNGGRMTcDSKDGVFRLHISNVQTGDDGDYTCEAMNSLGFVNTS 7339
Cdd:cd00096     2 TLTCSASGNPPPTITWYKNGKPLPPSSRDSR-RSELGNGTLTISNVTLEDSGTYTCVASNSAGGSASA 68
fn3 pfam00041
Fibronectin type III domain;
7152-7237 1.41e-11

Fibronectin type III domain;


Pssm-ID: 394996 [Multi-domain]  Cd Length: 85  Bit Score: 63.97  E-value: 1.41e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561  7152 SPPGAPQVTRVGKNYVDLKWEKPlRDGGSRITGYIIERRDIG-GAVWVKCNDYNVLdTEYTVMNLIEMGDYEFRVFAVNS 7230
Cdd:pfam00041    1 SAPSNLTVTDVTSTSLTVSWTPP-PDGNGPITGYEVEYRPKNsGEPWNEITVPGTT-TSVTLTGLKPGTEYEVRVQAVNG 78

                   ....*..
gi 281359561  7231 AGRSEPS 7237
Cdd:pfam00041   79 GGEGPPS 85
FN3 smart00060
Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, ...
5664-5746 1.68e-11

Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, fibronectin. The tenth fibronectin type III repeat contains a RGD cell recognition sequence in a flexible loop between 2 strands. Type III modules are present in both extracellular and intracellular proteins.


Pssm-ID: 214495 [Multi-domain]  Cd Length: 83  Bit Score: 63.79  E-value: 1.68e-11
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561   5664 PSPPKGpLDITKITRDGCHLTWNVPDDDGG-SPILHYIIEKMDLSRSTWSDAGMSTHIVHDVTRLVHRKEYLFRVKAVNA 5742
Cdd:smart00060    1 PSPPSN-LRVTDVTSTSVTLSWEPPPDDGItGYIVGYRVEYREEGSEWKEVNVTPSSTSYTLTGLKPGTEYEFRVRAVNG 79

                    ....
gi 281359561   5743 IGES 5746
Cdd:smart00060   80 AGEG 83
fn3 pfam00041
Fibronectin type III domain;
5177-5261 1.77e-11

Fibronectin type III domain;


Pssm-ID: 394996 [Multi-domain]  Cd Length: 85  Bit Score: 63.59  E-value: 1.77e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561  5177 KPGTPTIKDFDKEFVDLEWTRPEaDGGSPITGYVVEKRDKFSPDWEKCAEISDDITNAHVPDLIEGLKYEFRVRAVNKAG 5256
Cdd:pfam00041    2 APSNLTVTDVTSTSLTVSWTPPP-DGNGPITGYEVEYRPKNSGEPWNEITVPGTTTSVTLTGLKPGTEYEVRVQAVNGGG 80

                   ....*
gi 281359561  5257 PGSPS 5261
Cdd:pfam00041   81 EGPPS 85
IgI_LRIG1-like cd05763
Immunoglobulin (Ig)-like ectodomain of the LRIG1 (Leucine-rich Repeats And Immunoglobulin-like ...
8634-8721 1.89e-11

Immunoglobulin (Ig)-like ectodomain of the LRIG1 (Leucine-rich Repeats And Immunoglobulin-like Domains Protein 1) and similar proteins; member of the I-set of IgSF domains; The members here are composed of subgroup of the immunoglobulin (Ig) domain found in the Ig superfamily. The Ig superfamily is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. A predominant feature of most Ig domains is a disulfide bridge connecting the two beta-sheets with a tryptophan residue packed against the disulfide bond. The ectodomain of LRIG1 has two distinct regions: the proposed 15 LRRs and three Ig-like domains closer to the membrane. LRIG1 has been reported to interact with many receptor tyrosine kinases, GDNF/c-Ret, E-cadherin, JAK/STAT, c-Met, and the EGFR family signaling systems. Immunoglobulin Superfamily (IgSF) domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. The structure of the LRIG1 extracellular Ig domain lacks a C" strand and thus is better described as a member of the I-set of IgSF domains.


Pssm-ID: 409420 [Multi-domain]  Cd Length: 91  Bit Score: 63.79  E-value: 1.89e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 8634 FTKPLHDLTIHDGEQLILTCYVKGDPEPQISWSKNGKS-LSSSDILDLRYKNGIATLTINEVFPEDEGVITCTATNSVGA 8712
Cdd:cd05763     2 FTKTPHDITIRAGSTARLECAATGHPTPQIAWQKDGGTdFPAARERRMHVMPEDDVFFIVDVKIEDTGVYSCTAQNSAGS 81

                  ....*....
gi 281359561 8713 VETKCKLTI 8721
Cdd:cd05763    82 ISANATLTV 90
FN3 smart00060
Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, ...
6062-6145 1.93e-11

Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, fibronectin. The tenth fibronectin type III repeat contains a RGD cell recognition sequence in a flexible loop between 2 strands. Type III modules are present in both extracellular and intracellular proteins.


Pssm-ID: 214495 [Multi-domain]  Cd Length: 83  Bit Score: 63.79  E-value: 1.93e-11
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561   6062 PGAPGKPELTDSDKNHITIKWKQPIS-NGGSPIIGYDIERRDVNtGRWIKINGQPVPTaEYQDDRVTSNHQYQYRISAVN 6140
Cdd:smart00060    1 PSPPSNLRVTDVTSTSVTLSWEPPPDdGITGYIVGYRVEYREEG-SEWKEVNVTPSST-SYTLTGLKPGTEYEFRVRAVN 78

                    ....*
gi 281359561   6141 AAGNG 6145
Cdd:smart00060   79 GAGEG 83
I-set pfam07679
Immunoglobulin I-set domain;
9-101 2.06e-11

Immunoglobulin I-set domain;


Pssm-ID: 400151 [Multi-domain]  Cd Length: 90  Bit Score: 63.82  E-value: 2.06e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561     9 PSFVKKPQLHQEDDGNRLIFECQLLSSPKPDIEWFRSDNKVVEDVRtkFKIQPVGeNKYTvvLELDDVVETDAGLYKVKA 88
Cdd:pfam07679    1 PKFTQKPKDVEVQEGESARFTCTVTGTPDPEVSWFKDGQPLRSSDR--FKVTYEG-GTYT--LTISNVQPDDSGKYTCVA 75
                           90
                   ....*....|...
gi 281359561    89 KNKSGEVSASINL 101
Cdd:pfam07679   76 TNSAGEAEASAEL 88
STKc_EIF2AK3_PERK cd14048
Catalytic domain of the Serine/Threonine kinase, eukaryotic translation Initiation Factor ...
7989-8241 2.15e-11

Catalytic domain of the Serine/Threonine kinase, eukaryotic translation Initiation Factor 2-Alpha Kinase 3 or PKR-like Endoplasmic Reticulum Kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PERK (or EIF2AK3) is a type-I ER transmembrane protein containing a luminal domain bound with the chaperone BiP under unstressed conditions and a cytoplasmic catalytic kinase domain. In response to the accumulation of misfolded or unfolded proteins in the ER, PERK is activated through the release of BiP, allowing it to dimerize and autophosphorylate. It functions as the central regulator of translational control during the Unfolded Protein Response (UPR) pathway. In addition to the eIF-2 alpha subunit, PERK also phosphorylates Nrf2, a leucine zipper transcription factor which regulates cellular redox status and promotes cell survival during the UPR. EIF2AKs phosphorylate the alpha subunit of eIF-2, resulting in the downregulation of protein synthesis. The PERK subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270950 [Multi-domain]  Cd Length: 281  Bit Score: 68.75  E-value: 2.15e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 7989 YDILEEIGTGAFGVVHRCRERSTGNIFAAKFIPVSHSVE-KDLIRREIDIMNQLHHQKLINLHDAF---------EDDDE 8058
Cdd:cd14048     8 FEPIQCLGRGGFGVVFEAKNKVDDCNYAVKRIRLPNNELaREKVLREVRALAKLDHPGIVRYFNAWlerppegwqEKMDE 87
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 8059 MILILEF-LSGGELFERITAEGYVMTEAE---VINYMRQICEGIRHMHEQNIIHLDIKPENI---MCQTrsstnVKLIDF 8131
Cdd:cd14048    88 VYLYIQMqLCRKENLKDWMNRRCTMESRElfvCLNIFKQIASAVEYLHSKGLIHRDLKPSNVffsLDDV-----VKVGDF 162
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 8132 GLATRLDPNEvVKIT--------------TGTAEFAAPEIVNREPVGFYTDMWATGVLSYVLLSGLSpfAGDNDVQTLKN 8197
Cdd:cd14048   163 GLVTAMDQGE-PEQTvltpmpayakhtgqVGTRLYMSPEQIHGNQYSEKVDIFALGLILFELIYSFS--TQMERIRTLTD 239
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....
gi 281359561 8198 VKacDWDFDVESFKYISEEaKDFIRKLLVRNKEKRMTAHECLLH 8241
Cdd:cd14048   240 VR--KLKFPALFTNKYPEE-RDMVQQMLSPSPSERPEAHEVIEH 280
IG_like smart00410
Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.
6177-6255 2.22e-11

Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.


Pssm-ID: 214653 [Multi-domain]  Cd Length: 85  Bit Score: 63.68  E-value: 2.22e-11
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561   6177 VRAGEPVNLNIPISGAPTPTIEWKRGDLK-LEEGKRISYETNSERTLFRIDDSNRRDSGKYTVTAANEFGKDTADIEVIV 6255
Cdd:smart00410    6 VKEGESVTLSCEASGSPPPEVTWYKQGGKlLAESGRFSVSRSGSTSTLTISNVTPEDSGTYTCAATNSSGSASSGTTLTV 85
I-set pfam07679
Immunoglobulin I-set domain;
2311-2395 2.22e-11

Immunoglobulin I-set domain;


Pssm-ID: 400151 [Multi-domain]  Cd Length: 90  Bit Score: 63.82  E-value: 2.22e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561  2311 LKNVTVKKGQTIRFDIKYDGEPEPAATWVKGTDNLKfDNQRICLDQLERNSSITIKKSVRKDTGKYKLVLSNSSGTIESE 2390
Cdd:pfam07679    7 PKDVEVQEGESARFTCTVTGTPDPEVSWFKDGQPLR-SSDRFKVTYEGGTYTLTISNVQPDDSGKYTCVATNSAGEAEAS 85

                   ....*
gi 281359561  2391 AQVVV 2395
Cdd:pfam07679   86 AELTV 90
IgI_Titin_like cd05747
Immunoglobulin (Ig)-like domain of human titin C terminus and similar proteins; member of the ...
4991-5068 2.37e-11

Immunoglobulin (Ig)-like domain of human titin C terminus and similar proteins; member of the I-set of Ig superfamily (IgSF) domains; The members here are composed of the fifth immunoglobulin (Ig)-like domain from the C-terminus of human titin x and similar proteins. Titin (also called connectin) is a fibrous sarcomeric protein specifically found in vertebrate striated muscle. Titin is gigantic; depending on isoform composition it ranges from 2970 to 3700 kDa, and is of a length that spans half a sarcomere. Titin largely consists of multiple repeats of Ig-like and fibronectin type 3 (FN-III)-like domains. Titin connects the ends of myosin thick filaments to Z disks and extends along the thick filament to the H zone and appears to function similar to an elastic band, keeping the myosin filaments centered in the sarcomere during muscle contraction or stretching. This group belongs to the I-set of IgSF domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand, but lack a C" strand.


Pssm-ID: 143224 [Multi-domain]  Cd Length: 92  Bit Score: 63.53  E-value: 2.37e-11
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 281359561 4991 IKAGQSFTFDCKVSGEPAPQTKWLLKKKEVYSKDNVKVTNVDYNTKLKVNSATRSDSGIYTVFAENANGEDSADVKVT 5068
Cdd:cd05747    15 VSEGESARFSCDVDGEPAPTVTWMREGQIIVSSQRHQITSTEYKSTFEISKVQMSDEGNYTVVVENSEGKQEAQFTLT 92
IgI_2_Titin_Z1z2-like cd20972
Second Ig-like domain of the giant muscle protein titin Z1z2 in the sarcomeric Z-disk, and ...
7647-7737 2.59e-11

Second Ig-like domain of the giant muscle protein titin Z1z2 in the sarcomeric Z-disk, and similar domains; a member of the I-set of IgSF domains; The members here are composed of the second immunoglobulin (Ig)-like domain of the giant muscle protein titin Z1z2 in the sarcomeric Z-disk and similar proteins. Titin is a key component in the assembly and functioning of vertebrate striated muscles. By providing connections at the level of individual microfilaments, it contributes to the fine balance of forces between the two halves of the sarcomere. The Ig superfamily (IgSF) is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. Unlike the V-set, one of the distinctive features of I-set domains is the lack of a C" strand. The structure of the titin Z1z2 lacks this strand and thus it belongs to the I-set of the IgSF. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors, the hemolymph protein hemolin, the muscle proteins titin, telokin, and twitchin, the neuronal adhesion molecule axonin-1, and the signaling molecule semaphorin 4D that is involved in axonal guidance, immune function and angiogenesis.


Pssm-ID: 409564 [Multi-domain]  Cd Length: 91  Bit Score: 63.37  E-value: 2.59e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 7647 PPLIVKPLRDANCIQNHNAQFTCTINGVPKPTISWYKGAREISNGARYHMYSEGDNHFLNINDVFGEDADEYVCRAVNKA 7726
Cdd:cd20972     1 PPQFIQKLRSQEVAEGSKVRLECRVTGNPTPVVRWFCEGKELQNSPDIQIHQEGDLHSLIIAEAFEEDTGRYSCLATNSV 80
                          90
                  ....*....|.
gi 281359561 7727 GAKSTRATLAI 7737
Cdd:cd20972    81 GSDTTSAEIFV 91
IG_like smart00410
Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.
2610-2693 2.65e-11

Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.


Pssm-ID: 214653 [Multi-domain]  Cd Length: 85  Bit Score: 63.29  E-value: 2.65e-11
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561   2610 KRVTIKSGRTHKWSVDVLGEPIPELHWSWRDDIPLTNGDRIKIENVDYHTDFSITNVLRKDSGFYTLKAENRNGIDRETV 2689
Cdd:smart00410    2 PSVTVKEGESVTLSCEASGSPPPEVTWYKQGGKLLAESGRFSVSRSGSTSTLTISNVTPEDSGTYTCAATNSSGSASSGT 81

                    ....
gi 281359561   2690 ELVV 2693
Cdd:smart00410   82 TLTV 85
PKc_MKK4 cd06616
Catalytic domain of the dual-specificity Protein Kinase, Mitogen-activated protein Kinase ...
7992-8242 2.94e-11

Catalytic domain of the dual-specificity Protein Kinase, Mitogen-activated protein Kinase Kinase 4; PKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine (ST) or tyrosine residues on protein substrates. MKK4 is a dual-specificity PK that phosphorylates and activates the downstream targets, c-Jun N-terminal kinase (JNK) and p38 MAPK, on specific threonine and tyrosine residues. JNK and p38 are collectively known as stress-activated MAPKs, as they are activated in response to a variety of environmental stresses and pro-inflammatory cytokines. Their activation is associated with the induction of cell death. Mice deficient in MKK4 die during embryogenesis and display anemia, severe liver hemorrhage, and abnormal hepatogenesis. MKK4 may also play roles in the immune system and in cardiac hypertrophy. It plays a major role in cancer as a tumor and metastasis suppressor. Under certain conditions, MKK4 is pro-oncogenic. The MKK4 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270790 [Multi-domain]  Cd Length: 291  Bit Score: 68.55  E-value: 2.94e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 7992 LEEIGTGAFGVVHRCRERSTGNIFAAKFIPvSHSVEKDLIR--REID-IMNQLHHQKLINLHDA-FEDDDE------MIL 8061
Cdd:cd06616    11 LGEIGRGAFGTVNKMLHKPSGTIMAVKRIR-STVDEKEQKRllMDLDvVMRSSDCPYIVKFYGAlFREGDCwicmelMDI 89
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 8062 ILEFLS-------GGELFERITAEGYVMTeAEVINYMRQicegirhmhEQNIIHLDIKPENIMCQTRSstNVKLIDFGLA 8134
Cdd:cd06616    90 SLDKFYkyvyevlDSVIPEEILGKIAVAT-VKALNYLKE---------ELKIIHRDVKPSNILLDRNG--NIKLCDFGIS 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 8135 TRLDpNEVVKIT-TGTAEFAAPEIVN----REPVGFYTDMWATGVLSYVLLSGLSPFAGDNDV--QTLKNVKACDWDFDV 8207
Cdd:cd06616   158 GQLV-DSIAKTRdAGCRPYMAPERIDpsasRDGYDVRSDVWSLGITLYEVATGKFPYPKWNSVfdQLTQVVKGDPPILSN 236
                         250       260       270
                  ....*....|....*....|....*....|....*
gi 281359561 8208 ESFKYISEEAKDFIRKLLVRNKEKRMTAHECLLHP 8242
Cdd:cd06616   237 SEEREFSPSFVNFVNLCLIKDESKRPKYKELLKHP 271
PTKc_Syk cd05116
Catalytic domain of the Protein Tyrosine Kinase, Spleen tyrosine kinase; PTKs catalyze the ...
7994-8188 3.31e-11

Catalytic domain of the Protein Tyrosine Kinase, Spleen tyrosine kinase; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Syk is a cytoplasmic (or nonreceptor) PTK containing two Src homology 2 (SH2) domains N-terminal to the catalytic tyr kinase domain. Syk was first cloned from the spleen, and its function in hematopoietic cells is well-established. It is involved in the signaling downstream of activated receptors (including B-cell and Fc receptors) that contain ITAMs (immunoreceptor tyr activation motifs), leading to processes such as cell proliferation, differentiation, survival, adhesion, migration, and phagocytosis. More recently, Syk expression has been detected in other cell types (including epithelial cells, vascular endothelial cells, neurons, hepatocytes, and melanocytes), suggesting a variety of biological functions in non-immune cells. Syk plays a critical role in maintaining vascular integrity and in wound healing during embryogenesis. It also regulates Vav3, which is important in osteoclast function including bone development. In breast epithelial cells, where Syk acts as a negative regulator for EGFR signaling, loss of Syk expression is associated with abnormal proliferation during cancer development suggesting a potential role as a tumor suppressor. In mice, Syk has been shown to inhibit malignant transformation of mammary epithelial cells induced with murine mammary tumor virus (MMTV). The Syk subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 133247 [Multi-domain]  Cd Length: 257  Bit Score: 67.68  E-value: 3.31e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 7994 EIGTGAFGVVHR--CRERSTGNIFAAKFIPVSHSVE--KDLIRREIDIMNQLHHQKLINLHDAFEDDDEMiLILEFLSGG 8069
Cdd:cd05116     2 ELGSGNFGTVKKgyYQMKKVVKTVAVKILKNEANDPalKDELLREANVMQQLDNPYIVRMIGICEAESWM-LVMEMAELG 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 8070 ELFERITAEGYVmTEAEVINYMRQICEGIRHMHEQNIIHLDIKPENIMCQTRSSTnvKLIDFGL--ATRLDPNEVVKITT 8147
Cdd:cd05116    81 PLNKFLQKNRHV-TEKNITELVHQVSMGMKYLEESNFVHRDLAARNVLLVTQHYA--KISDFGLskALRADENYYKAQTH 157
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....
gi 281359561 8148 GT--AEFAAPEIVNREPVGFYTDMWATGVLSYVLLS-GLSPFAG 8188
Cdd:cd05116   158 GKwpVKWYAPECMNYYKFSSKSDVWSFGVLMWEAFSyGQKPYKG 201
IgI_2_Titin_Z1z2-like cd20972
Second Ig-like domain of the giant muscle protein titin Z1z2 in the sarcomeric Z-disk, and ...
8436-8525 3.31e-11

Second Ig-like domain of the giant muscle protein titin Z1z2 in the sarcomeric Z-disk, and similar domains; a member of the I-set of IgSF domains; The members here are composed of the second immunoglobulin (Ig)-like domain of the giant muscle protein titin Z1z2 in the sarcomeric Z-disk and similar proteins. Titin is a key component in the assembly and functioning of vertebrate striated muscles. By providing connections at the level of individual microfilaments, it contributes to the fine balance of forces between the two halves of the sarcomere. The Ig superfamily (IgSF) is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. Unlike the V-set, one of the distinctive features of I-set domains is the lack of a C" strand. The structure of the titin Z1z2 lacks this strand and thus it belongs to the I-set of the IgSF. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors, the hemolymph protein hemolin, the muscle proteins titin, telokin, and twitchin, the neuronal adhesion molecule axonin-1, and the signaling molecule semaphorin 4D that is involved in axonal guidance, immune function and angiogenesis.


Pssm-ID: 409564 [Multi-domain]  Cd Length: 91  Bit Score: 63.37  E-value: 3.31e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 8436 APSFTFLLRPRVMQARDTCKLLCCLSGKPVPNVRWYKDGRELSKYEYAMTHSDG-VVTMEIIDCKPSDSGKYSCKATNCH 8514
Cdd:cd20972     1 PPQFIQKLRSQEVAEGSKVRLECRVTGNPTPVVRWFCEGKELQNSPDIQIHQEGdLHSLIIAEAFEEDTGRYSCLATNSV 80
                          90
                  ....*....|.
gi 281359561 8515 GTDETDCVVIV 8525
Cdd:cd20972    81 GSDTTSAEIFV 91
fn3 pfam00041
Fibronectin type III domain;
3400-3484 3.70e-11

Fibronectin type III domain;


Pssm-ID: 394996 [Multi-domain]  Cd Length: 85  Bit Score: 62.82  E-value: 3.70e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561  3400 PPGLPELEDWDEHHVKLKWEPPiRDGGSPITNYIIEVMDKDSGEFVKAVETDSPVCKGVVKKLEEGQQYKFRVRAVNKAG 3479
Cdd:pfam00041    2 APSNLTVTDVTSTSLTVSWTPP-PDGNGPITGYEVEYRPKNSGEPWNEITVPGTTTSVTLTGLKPGTEYEVRVQAVNGGG 80

                   ....*
gi 281359561  3480 PSDPS 3484
Cdd:pfam00041   81 EGPPS 85
STKc_WNK2_like cd14032
Catalytic domain of With No Lysine (WNK) 2-like Serine/Threonine kinases; STKs catalyze the ...
7988-8247 3.72e-11

Catalytic domain of With No Lysine (WNK) 2-like Serine/Threonine kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. WNK2 is widely expressed and has been shown to be epigenetically silenced in gliomas. It inhibits cell growth by acting as a negative regulator of MEK1-ERK1/2 signaling. WNK2 modulates growth factor-induced cancer cell proliferation, suggesting that it may be a tumor suppressor gene. WNKs comprise a subfamily of STKs with an unusual placement of the catalytic lysine relative to all other protein kinases. They are critical in regulating ion balance and are thus, important components in the control of blood pressure. The WNK2-like subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270934 [Multi-domain]  Cd Length: 266  Bit Score: 67.79  E-value: 3.72e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 7988 RYDIleEIGTGAFGVVHRCRERSTgnifaakFIPVS---------HSVEKDLIRREIDIMNQLHHQKLINLHDAFEDDDE 8058
Cdd:cd14032     4 KFDI--ELGRGSFKTVYKGLDTET-------WVEVAwcelqdrklTKVERQRFKEEAEMLKGLQHPNIVRFYDFWESCAK 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 8059 ----MILILEFLSGGELfERITAEGYVMTEAEVINYMRQICEGIRHMHEQN--IIHLDIKPENIMCqTRSSTNVKLIDFG 8132
Cdd:cd14032    75 gkrcIVLVTELMTSGTL-KTYLKRFKVMKPKVLRSWCRQILKGLLFLHTRTppIIHRDLKCDNIFI-TGPTGSVKIGDLG 152
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 8133 LATrLDPNEVVKITTGTAEFAAPEIVnREPVGFYTDMWATGVLSYVLLSGLSPFAGDNDVQTLKNVKACDwdFDVESFKY 8212
Cdd:cd14032   153 LAT-LKRASFAKSVIGTPEFMAPEMY-EEHYDESVDVYAFGMCMLEMATSEYPYSECQNAAQIYRKVTCG--IKPASFEK 228
                         250       260       270
                  ....*....|....*....|....*....|....*.
gi 281359561 8213 ISE-EAKDFIRKLLVRNKEKRMTAHECLLHPWLTGD 8247
Cdd:cd14032   229 VTDpEIKEIIGECICKNKEERYEIKDLLSHAFFAED 264
PTKc_Fyn cd05070
Catalytic domain of the Protein Tyrosine Kinase, Fyn; PTKs catalyze the transfer of the ...
7979-8199 3.96e-11

Catalytic domain of the Protein Tyrosine Kinase, Fyn; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Fyn and Yrk are members of the Src subfamily of proteins, which are cytoplasmic (or non-receptor) PTKs. Fyn, together with Lck, plays a critical role in T-cell signal transduction by phosphorylating ITAM (immunoreceptor tyr activation motif) sequences on T-cell receptors, ultimately leading to the proliferation and differentiation of T-cells. In addition, Fyn is involved in the myelination of neurons, and is implicated in Alzheimer's and Parkinson's diseases. Src kinases contain an N-terminal SH4 domain with a myristoylation site, followed by SH3 and SH2 domains, a tyr kinase domain, and a regulatory C-terminal region containing a conserved tyr. They are activated by autophosphorylation at the tyr kinase domain, but are negatively regulated by phosphorylation at the C-terminal tyr by Csk (C-terminal Src Kinase). The Fyn/Yrk subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as serine/threonine kinases, RIO kinases, and phosphoinositide 3-kinase.


Pssm-ID: 270655 [Multi-domain]  Cd Length: 274  Bit Score: 67.79  E-value: 3.96e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 7979 EISQQSVYdrydILEEIGTGAFGVVHRCRERSTGNIFAAKFIPVSHSVEKDLirREIDIMNQLHHQKLINLHdAFEDDDE 8058
Cdd:cd05070     5 EIPRESLQ----LIKRLGNGQFGEVWMGTWNGNTKVAIKTLKPGTMSPESFL--EEAQIMKKLKHDKLVQLY-AVVSEEP 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 8059 MILILEFLSGGELFERIT-AEGYVMTEAEVINYMRQICEGIRHMHEQNIIHLDIKPENIMcqTRSSTNVKLIDFGLATRL 8137
Cdd:cd05070    78 IYIVTEYMSKGSLLDFLKdGEGRALKLPNLVDMAAQVAAGMAYIERMNYIHRDLRSANIL--VGNGLICKIADFGLARLI 155
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 281359561 8138 DPNEVVKITTGT--AEFAAPEIVNREPVGFYTDMWATGVLSYVLLS-GLSPFAGDNDVQTLKNVK 8199
Cdd:cd05070   156 EDNEYTARQGAKfpIKWTAPEAALYGRFTIKSDVWSFGILLTELVTkGRVPYPGMNNREVLEQVE 220
PK_TRB cd13976
Pseudokinase domain of Tribbles Homolog proteins; The pseudokinase domain shows similarity to ...
8083-8244 3.97e-11

Pseudokinase domain of Tribbles Homolog proteins; The pseudokinase domain shows similarity to protein kinases but lacks crucial residues for catalytic activity. Tribbles Homolog (TRB) proteins interact with many proteins involved in signaling pathways. They play scaffold-like regulatory functions and affect many cellular processes such as mitosis, apoptosis, differentiation, and gene expression. TRB proteins bind to the middle kinase in mitogen activated protein kinase (MAPK) signaling cascades, MAPK kinases. They regulate the activity of MAPK kinases, and thus, affect MAPK signaling. In Drosophila, Tribbles regulates String, the ortholog of mammalian Cdc25, during morphogenesis. String is implicated in the progression of mitosis during embryonic development. Vertebrates contain three TRB proteins encoded by three separate genes: Tribbles-1 (TRB1 or TRIB1), Tribbles-2 (TRB2 or TRIB2), and Tribbles-3 (TRB3 or TRIB3). The TRB subfamily is part of a larger superfamily that includes the catalytic domains of serine/threonine kinases, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270878 [Multi-domain]  Cd Length: 242  Bit Score: 67.45  E-value: 3.97e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 8083 TEAEVInyMRQICEGIRHMHEQNIIHLDIKPENIMCQTRSSTNVKLIDFGLATRLD-PNEVVKITTGTAEFAAPEIVNre 8161
Cdd:cd13976    84 PEAARL--FRQIASAVAHCHRNGIVLRDLKLRKFVFADEERTKLRLESLEDAVILEgEDDSLSDKHGCPAYVSPEILN-- 159
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 8162 PVGFYT----DMWATGVLSYVLLSGLSPFAgDNDVQTLKNvKACDWDFDVEsfKYISEEAKDFIRKLLVRNKEKRMTAHE 8237
Cdd:cd13976   160 SGATYSgkaaDVWSLGVILYTMLVGRYPFH-DSEPASLFA-KIRRGQFAIP--ETLSPRARCLIRSLLRREPSERLTAED 235

                  ....*..
gi 281359561 8238 CLLHPWL 8244
Cdd:cd13976   236 ILLHPWL 242
I-set pfam07679
Immunoglobulin I-set domain;
438-532 4.11e-11

Immunoglobulin I-set domain;


Pssm-ID: 400151 [Multi-domain]  Cd Length: 90  Bit Score: 63.05  E-value: 4.11e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561   438 PSFIEKPRIIPNESGTLITMKCKCKAKPEPTVTWYRGQDLVEKSKKIKInttviAEDTYELTLEIKDPGATDGGTYRCNV 517
Cdd:pfam07679    1 PKFTQKPKDVEVQEGESARFTCTVTGTPDPEVSWFKDGQPLRSSDRFKV-----TYEGGTYTLTISNVQPDDSGKYTCVA 75
                           90
                   ....*....|....*
gi 281359561   518 KNEYGESNANLNLNI 532
Cdd:pfam07679   76 TNSAGEAEASAELTV 90
IG_like smart00410
Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.
242-320 4.90e-11

Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.


Pssm-ID: 214653 [Multi-domain]  Cd Length: 85  Bit Score: 62.52  E-value: 4.90e-11
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561    242 GGNVTFECRCVGDPTPTVTWSH-GETELNESNRYKMSltmdqKLYHIACLEISSVVSSDQGEYRAQAKNKHGSGVATINL 320
Cdd:smart00410    9 GESVTLSCEASGSPPPEVTWYKqGGKLLAESGRFSVS-----RSGSTSTLTISNVTPEDSGTYTCAATNSSGSASSGTTL 83
fn3 pfam00041
Fibronectin type III domain;
6952-7034 5.31e-11

Fibronectin type III domain;


Pssm-ID: 394996 [Multi-domain]  Cd Length: 85  Bit Score: 62.43  E-value: 5.31e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561  6952 PPQGpLNAYDITPDTCTLAWKTPlDDGGSPITNYVVEKLDNSGSWVKISSFVRNTH--YDVMGLEPHYKYNFRVRAENQY 7029
Cdd:pfam00041    2 APSN-LTVTDVTSTSLTVSWTPP-PDGNGPITGYEVEYRPKNSGEPWNEITVPGTTtsVTLTGLKPGTEYEVRVQAVNGG 79

                   ....*
gi 281359561  7030 GLSDP 7034
Cdd:pfam00041   80 GEGPP 84
PKc_DYRK2_3 cd14224
Catalytic domain of the protein kinases, Dual-specificity tYrosine-phosphorylated and ...
7988-8191 6.55e-11

Catalytic domain of the protein kinases, Dual-specificity tYrosine-phosphorylated and -Regulated Kinases 2 and 3; Dual-specificity PKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine (S/T) as well as tyrosine residues on protein substrates. This subfamily is composed of DYRK2 and DYRK3, and similar proteins. Drosophila DYRK2 interacts and phosphorylates the chromatin remodelling factor, SNR1 (Snf5-related 1), and also interacts with the essential chromatin component, trithorax. It may play a role in chromatin remodelling. Vertebrate DYRK2 phosphorylates and regulates the tumor suppressor p53 to induce apoptosis in response to DNA damage. It can also phosphorylate the transcription factor, nuclear factor of activated T cells (NFAT). DYRK2 is overexpressed in lung adenocarcinoma and esophageal carcinomas, and is a predictor for favorable prognosis in lung adenocarcinoma. DYRK3, also called regulatory erythroid kinase (REDK), is highly expressed in erythroid cells and the testis, and is also present in adult kidney and liver. It promotes cell survival by phosphorylating and activating SIRT1, an NAD(+)-dependent protein deacetylase, which promotes p53 deacetylation, resulting in the inhibition of apoptosis. DYRKs autophosphorylate themselves on tyrosine residues and phosphorylate their substrates exclusively on S/T residues. The DYRK2/3 subfamily is part of a larger superfamily that includes the catalytic domains of other S/T kinases, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271126 [Multi-domain]  Cd Length: 380  Bit Score: 68.62  E-value: 6.55e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 7988 RYDILEEIGTGAFGVVHRCRERSTGNIFAAKFIpvshSVEKDLIRR---EIDIMNQLHHQ------KLINLHDAFEDDDE 8058
Cdd:cd14224    66 RYEVLKVIGKGSFGQVVKAYDHKTHQHVALKMV----RNEKRFHRQaaeEIRILEHLKKQdkdntmNVIHMLESFTFRNH 141
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 8059 MILILEFLSGG--ELFERITAEGYVMTEaeVINYMRQICEGIRHMHEQNIIHLDIKPENIMCQTRSSTNVKLIDFGLATR 8136
Cdd:cd14224   142 ICMTFELLSMNlyELIKKNKFQGFSLQL--VRKFAHSILQCLDALHRNKIIHCDLKPENILLKQQGRSGIKVIDFGSSCY 219
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 281359561 8137 ldpnEVVKITTGTAE--FAAPEIVNREPVGFYTDMWATGVLSYVLLSGLSPFAGDND 8191
Cdd:cd14224   220 ----EHQRIYTYIQSrfYRAPEVILGARYGMPIDMWSFGCILAELLTGYPLFPGEDE 272
STKc_TAO2 cd06634
Catalytic domain of the Serine/Threonine Kinase, Thousand-and-One Amino acids 2; STKs catalyze ...
7992-8244 6.59e-11

Catalytic domain of the Serine/Threonine Kinase, Thousand-and-One Amino acids 2; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Human TAO2 is also known as prostate-derived Ste20-like kinase (PSK) and was identified in a screen for overexpressed RNAs in prostate cancer. TAO2 possesses mitogen-activated protein kinase (MAPK) kinase kinase activity and activates both p38 and c-Jun N-terminal kinase (JNK), by phosphorylating and activating their respective MAP/ERK kinases, MEK3/MEK6 and MKK4/MKK7. It contains a long C-terminal extension with autoinhibitory segments, and is activated by the release of this inhibition and the phosphorylation of its activation loop serine. TAO2 functions as a regulator of actin cytoskeletal and microtubule organization. In addition, it regulates the transforming growth factor-activated kinase 1 (TAK1), which is a MAPKKK that plays an essential role in the signaling pathways of tumor necrosis factor, interleukin 1, and Toll-like receptor. The TAO2 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270804 [Multi-domain]  Cd Length: 308  Bit Score: 67.74  E-value: 6.59e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 7992 LEEIGTGAFGVVHRCRERSTGNIFAAKFIPVS--HSVEK--DLIRrEIDIMNQLHHQKLINLHDAFEDDDEMILILEFL- 8066
Cdd:cd06634    20 LREIGHGSFGAVYFARDVRNNEVVAIKKMSYSgkQSNEKwqDIIK-EVKFLQKLRHPNTIEYRGCYLREHTAWLVMEYCl 98
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 8067 -SGGELFEritAEGYVMTEAEVINYMRQICEGIRHMHEQNIIHLDIKPENIMCQtrSSTNVKLIDFGLATRLDP-NEVVk 8144
Cdd:cd06634    99 gSASDLLE---VHKKPLQEVEIAAITHGALQGLAYLHSHNMIHRDVKAGNILLT--EPGLVKLGDFGSASIMAPaNSFV- 172
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 8145 ittGTAEFAAPEIVNREPVGFY---TDMWATGVLSYVLLSGLSPFAGDNDVQTLKNVkACDWDFDVESFKYiSEEAKDFI 8221
Cdd:cd06634   173 ---GTPYWMAPEVILAMDEGQYdgkVDVWSLGITCIELAERKPPLFNMNAMSALYHI-AQNESPALQSGHW-SEYFRNFV 247
                         250       260
                  ....*....|....*....|...
gi 281359561 8222 RKLLVRNKEKRMTAHECLLHPWL 8244
Cdd:cd06634   248 DSCLQKIPQDRPTSDVLLKHRFL 270
FN3 smart00060
Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, ...
2399-2483 6.72e-11

Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, fibronectin. The tenth fibronectin type III repeat contains a RGD cell recognition sequence in a flexible loop between 2 strands. Type III modules are present in both extracellular and intracellular proteins.


Pssm-ID: 214495 [Multi-domain]  Cd Length: 83  Bit Score: 62.25  E-value: 6.72e-11
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561   2399 PLPPGGPfEPEEIRASHIKMKWKRPDDDGG-CEISGYALERmDEETGRWIPAgEVGPNETSFDFKGLTPNKKYKFRVKAI 2477
Cdd:smart00060    1 PSPPSNL-RVTDVTSTSVTLSWEPPPDDGItGYIVGYRVEY-REEGSEWKEV-NVTPSSTSYTLTGLKPGTEYEFRVRAV 77

                    ....*.
gi 281359561   2478 NKEGES 2483
Cdd:smart00060   78 NGAGEG 83
Ig_3 pfam13927
Immunoglobulin domain; This family contains immunoglobulin-like domains.
4978-5056 6.99e-11

Immunoglobulin domain; This family contains immunoglobulin-like domains.


Pssm-ID: 464046 [Multi-domain]  Cd Length: 78  Bit Score: 61.81  E-value: 6.99e-11
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 281359561  4978 PPIIdRSSLVEVRIKAGQSFTFDCKVSGEPAPQTKWLLKKKEVYSKDNVKVTNVDYNTKLKVNSATRSDSGIYTVFAEN 5056
Cdd:pfam13927    1 KPVI-TVSPSSVTVREGETVTLTCEATGSPPPTITWYKNGEPISSGSTRSRSLSGSNSTLTISNVTRSDAGTYTCVASN 78
PTKc_Fes_like cd05041
Catalytic domain of Fes-like Protein Tyrosine Kinases; Protein Tyrosine Kinase (PTK) family; ...
7993-8194 7.09e-11

Catalytic domain of Fes-like Protein Tyrosine Kinases; Protein Tyrosine Kinase (PTK) family; Fes subfamily; catalytic (c) domain. Fes subfamily members include Fes (or Fps), Fer, and similar proteins. The PTKc family is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, and phosphoinositide 3-kinase (PI3K). PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Fes subfamily proteins are cytoplasmic (or nonreceptor) tyr kinases containing an N-terminal region with FCH (Fes/Fer/CIP4 homology) and coiled-coil domains, followed by a SH2 domain, and a C-terminal catalytic domain. The genes for Fes (feline sarcoma) and Fps (Fujinami poultry sarcoma) were first isolated from tumor-causing retroviruses. The viral oncogenes encode chimeric Fes proteins consisting of Gag sequences at the N-termini, resulting in unregulated tyr kinase activity. Fes and Fer kinases play roles in haematopoiesis, inflammation and immunity, growth factor signaling, cytoskeletal regulation, cell migration and adhesion, and the regulation of cell-cell interactions. Fes and Fer show redundancy in their biological functions.


Pssm-ID: 270637 [Multi-domain]  Cd Length: 251  Bit Score: 66.70  E-value: 7.09e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 7993 EEIGTGAFGVVHRCRERSTGNIFAAKFIPVSHSVE-KDLIRREIDIMNQLHHQKLINLHDAFEDDDEMILILEFLSGGEL 8071
Cdd:cd05041     1 EKIGRGNFGDVYRGVLKPDNTEVAVKTCRETLPPDlKRKFLQEARILKQYDHPNIVKLIGVCVQKQPIMIVMELVPGGSL 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 8072 FERITAEGYVMTEAEVINYMRQICEGIRHMHEQNIIHLDIKPENimCQTRSSTNVKLIDFGLaTRLDPNEVVKITTGTAE 8151
Cdd:cd05041    81 LTFLRKKGARLTVKQLLQMCLDAAAGMEYLESKNCIHRDLAARN--CLVGENNVLKISDFGM-SREEEDGEYTVSDGLKQ 157
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|.
gi 281359561 8152 ----FAAPEIVNrepVGFYT---DMWATGVLSYVLLS-GLSPFAGDNDVQT 8194
Cdd:cd05041   158 ipikWTAPEALN---YGRYTsesDVWSFGILLWEIFSlGATPYPGMSNQQT 205
IgI_8_hMLCK_like cd05762
Eighth immunoglobulin (Ig)-like domain of human myosin light-chain kinase (MLCK) and similar ...
4988-5076 7.24e-11

Eighth immunoglobulin (Ig)-like domain of human myosin light-chain kinase (MLCK) and similar protein; member of the I-set of IgSF domains; The members here are composed of the eighth immunoglobulin (Ig)-like domain of human myosin light-chain kinase (MLCK) and similar proteins. Myosin light-chain kinase (MLCK) is a key regulator of different forms of cell motility involving actin and myosin II. Agonist stimulation of smooth muscle cells increases cytosolic Ca2+ which binds calmodulin. This Ca2+-calmodulin complex in turn binds to and activates MLCK. Activated MLCK leads to the phosphorylation of the 20 kDa myosin regulatory light chain (RLC) of myosin II and the stimulation of actin-activated myosin MgATPase activity. MLCK is widely present in vertebrate tissues; it phosphorylates the 20 kDa RLC of both smooth and nonmuscle myosin II. Phosphorylation leads to the activation of the myosin motor domain and altered structural properties of myosin II. In smooth muscle MLCK it is involved in initiating contraction. In nonmuscle cells, MLCK may participate in cell division and cell motility; it has been suggested MLCK plays a role in cardiomyocyte differentiation and contraction through regulation of nonmuscle myosin II.


Pssm-ID: 409419  Cd Length: 99  Bit Score: 62.66  E-value: 7.24e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 4988 EVRIKAGQSFTFDCKVSGEPAPQTKWLLKKKEVYSKDNVKVTNVDYNTKLKVNSATRSDSGIYTVFAENANGEDSADVKV 5067
Cdd:cd05762    10 DMKVRAGESVELFCKVTGTQPITCTWMKFRKQIQEGEGIKIENTENSSKLTITEGQQEHCGCYTLEVENKLGSRQAQVNL 89

                  ....*....
gi 281359561 5068 TVIDKPAPP 5076
Cdd:cd05762    90 TVVDKPDPP 98
I-set pfam07679
Immunoglobulin I-set domain;
1826-1909 8.13e-11

Immunoglobulin I-set domain;


Pssm-ID: 400151 [Multi-domain]  Cd Length: 90  Bit Score: 61.89  E-value: 8.13e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561  1826 KFVKVLKSQQCIEKDTVTLACEIddaMG----EVQWLRNGEEIKPDKRIQIVKDGRKRKLVIKDCKVTDAGQFKCT-TNA 1900
Cdd:pfam07679    2 KFTQKPKDVEVQEGESARFTCTV---TGtpdpEVSWFKDGQPLRSSDRFKVTYEGGTYTLTISNVQPDDSGKYTCVaTNS 78
                           90
                   ....*....|..
gi 281359561  1901 ---DTTESEIII 1909
Cdd:pfam07679   79 ageAEASAELTV 90
STKc_LIMK cd14154
Catalytic domain of the Serine/Threonine Kinase, LIM domain kinase; STKs catalyze the transfer ...
7995-8134 8.21e-11

Catalytic domain of the Serine/Threonine Kinase, LIM domain kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. LIMKs phosphorylate and inactivate cofilin, an actin depolymerizing factor, to induce the reorganization of the actin cytoskeleton. They act downstream of Rho GTPases and are expressed ubiquitously. As regulators of actin dynamics, they contribute to diverse cellular functions such as cell motility, morphogenesis, differentiation, apoptosis, meiosis, mitosis, and neurite extension. LIMKs contain the LIM (two repeats), PDZ, and catalytic kinase domains. Vertebrate have two members, LIMK1 and LIMK2. The LIMK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271056 [Multi-domain]  Cd Length: 272  Bit Score: 66.76  E-value: 8.21e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 7995 IGTGAFGVVHRCRERSTGNIFAAK-FIPVSHSVEKDLIRrEIDIMNQLHHQKLINLHDAFEDDDEMILILEFLSGGELFE 8073
Cdd:cd14154     1 LGKGFFGQAIKVTHRETGEVMVMKeLIRFDEEAQRNFLK-EVKVMRSLDHPNVLKFIGVLYKDKKLNLITEYIPGGTLKD 79
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 281359561 8074 RITAEGYVMTEAEVINYMRQICEGIRHMHEQNIIHLDIKPENimCQTRSSTNVKLIDFGLA 8134
Cdd:cd14154    80 VLKDMARPLPWAQRVRFAKDIASGMAYLHSMNIIHRDLNSHN--CLVREDKTVVVADFGLA 138
Ig_3 pfam13927
Immunoglobulin domain; This family contains immunoglobulin-like domains.
7268-7331 8.58e-11

Immunoglobulin domain; This family contains immunoglobulin-like domains.


Pssm-ID: 464046 [Multi-domain]  Cd Length: 78  Bit Score: 61.43  E-value: 8.58e-11
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 281359561  7268 GKDYTLQCAASGKPSPTARWLRNGKEIQmNGGRMTCDSKDGVFRLHISNVQTGDDGDYTCEAMN 7331
Cdd:pfam13927   16 GETVTLTCEATGSPPPTITWYKNGEPIS-SGSTRSRSLSGSNSTLTISNVTRSDAGTYTCVASN 78
IgI_Myotilin_C_like cd05744
Immunoglobulin (Ig)-like domain of myotilin, palladin, and myopalladin; member of the I-set of ...
9-102 8.87e-11

Immunoglobulin (Ig)-like domain of myotilin, palladin, and myopalladin; member of the I-set of Ig superfamily (IgSF) domains; The members here are composed of the immunoglobulin (Ig)-like domain in myotilin, palladin, and myopalladin. Myotilin, palladin, and myopalladin function as scaffolds that regulate actin organization. Myotilin and myopalladin are most abundant in skeletal and cardiac muscle; palladin is ubiquitously expressed in the organs of developing vertebrates and plays a key role in cellular morphogenesis. The three family members each interact with specific molecular partners with all three binding to alpha-actinin; In addition, palladin also binds to vasodilator-stimulated phosphoprotein (VASP) and ezrin, myotilin binds to filamin and actin, and myopalladin also binds to nebulin and cardiac ankyrin repeat protein (CARP). This group belongs to the I-set of IgSF domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand, but lack a C" strand.


Pssm-ID: 409405 [Multi-domain]  Cd Length: 91  Bit Score: 62.13  E-value: 8.87e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561    9 PSFVKKPQLHQEDDGNRLIFECQLLSSPKPDIEWFRSDNKVVEDVRTKFKIQPVGenkyTVVLELDDVVETDAGLYKVKA 88
Cdd:cd05744     1 PHFLQAPGDLEVQEGRLCRFDCKVSGLPTPDLFWQLNGKPVRPDSAHKMLVRENG----RHSLIIEPVTKRDAGIYTCIA 76
                          90
                  ....*....|....
gi 281359561   89 KNKSGEVSASINLN 102
Cdd:cd05744    77 RNRAGENSFNAELV 90
Ig_3 pfam13927
Immunoglobulin domain; This family contains immunoglobulin-like domains.
8740-8816 8.92e-11

Immunoglobulin domain; This family contains immunoglobulin-like domains.


Pssm-ID: 464046 [Multi-domain]  Cd Length: 78  Bit Score: 61.43  E-value: 8.92e-11
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 281359561  8740 PKIVSHLESRFVRDGDAVNLACRIIGAQHFDVVWLHNNKEIKPSKDFQYTNEANIYRLQIAEIFPEDGGTYTCEAFN 8816
Cdd:pfam13927    2 PVITVSPSSVTVREGETVTLTCEATGSPPPTITWYKNGEPISSGSTRSRSLSGSNSTLTISNVTRSDAGTYTCVASN 78
Ig5_Contactin cd04969
Fifth immunoglobulin (Ig) domain of contactin; The members here are composed of the fifth ...
119-210 9.86e-11

Fifth immunoglobulin (Ig) domain of contactin; The members here are composed of the fifth immunoglobulin (Ig) domain of contactins. Contactins are neural cell adhesion molecules and are comprised of six Ig domains followed by four fibronectin type III (FnIII) domains anchored to the membrane by glycosylphosphatidylinositol. The first four Ig domains form the intermolecular binding fragment, which arranges as a compact U-shaped module via contacts between Ig domains 1 and 4, and between Ig domains 2 and 3. Contactin-2 (TAG-1, axonin-1) may play a part in the neuronal processes of neurite outgrowth, axon guidance and fasciculation, and neuronal migration. This group also includes contactin-1 and contactin-5. The different contactins show different expression patterns in the central nervous system. During development and in adulthood, contactin-2 is transiently expressed in subsets of central and peripheral neurons. Contactin-5 is expressed specifically in the rat postnatal nervous system, peaking at about 3 weeks postnatal, and a lack of contactin-5 (NB-2) results in an impairment of neuronal activity in the rat auditory system. Contactin-5 is highly expressed in the adult human brain in the occipital lobe and in the amygdala. Contactin-1 is differentially expressed in tumor tissues and may, through a RhoA mechanism, facilitate invasion and metastasis of human lung adenocarcinoma.


Pssm-ID: 409358 [Multi-domain]  Cd Length: 89  Bit Score: 61.71  E-value: 9.86e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561  119 PTFAKKPAIRQE--EDGKRLLFECRVNADPIPAIIWFHNGAAVKESERHKITVDkdvhsyfATLEILNVTVEDAGKYKVN 196
Cdd:cd04969     1 PDFELNPVKKKIlaAKGGDVIIECKPKASPKPTISWSKGTELLTNSSRICILPD-------GSLKIKNVTKSDEGKYTCF 73
                          90
                  ....*....|....
gi 281359561  197 AKNELGESNATISL 210
Cdd:cd04969    74 AVNFFGKANSTGSL 87
I-set pfam07679
Immunoglobulin I-set domain;
1508-1588 9.98e-11

Immunoglobulin I-set domain;


Pssm-ID: 400151 [Multi-domain]  Cd Length: 90  Bit Score: 61.89  E-value: 9.98e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561  1508 VVEDSTAYLTVGVEGSPAPTFKFYKGVSEILEGGRFKFLTDGQTNTITlcMRKCKPNDESKYKIVVSNIHGEDSAEMQLY 1587
Cdd:pfam07679   12 VQEGESARFTCTVTGTPDPEVSWFKDGQPLRSSDRFKVTYEGGTYTLT--ISNVQPDDSGKYTCVATNSAGEAEASAELT 89

                   .
gi 281359561  1588 V 1588
Cdd:pfam07679   90 V 90
PKc_TNNI3K cd14064
Catalytic domain of the Dual-specificity protein kinase, TNNI3-interacting kinase; ...
7995-8187 1.01e-10

Catalytic domain of the Dual-specificity protein kinase, TNNI3-interacting kinase; Dual-specificity PKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine as well as tyrosine residues on protein substrates. TNNI3K, also called cardiac ankyrin repeat kinase (CARK), is a cardiac-specific troponin I-interacting kinase that promotes cardiac myogenesis, improves cardiac performance, and protects the myocardium from ischemic injury. It contains N-terminal ankyrin repeats, a catalytic kinase domain, and a C-terminal serine-rich domain. TNNI3K exerts a disease-accelerating effect on cardiac dysfunction and reduced survival in mouse models of cardiomyopathy. The TNNI3K subfamily is part of a larger superfamily that includes the catalytic domains of other protein serine/threonine PKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270966 [Multi-domain]  Cd Length: 254  Bit Score: 66.40  E-value: 1.01e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 7995 IGTGAFGVVH--RCR------ERSTGNIFAAKfipvshsVEKDLIRREIDIMNQLHHQKLINLHDA-FEDDDEMILILEF 8065
Cdd:cd14064     1 IGSGSFGKVYkgRCRnkivaiKRYRANTYCSK-------SDVDMFCREVSILCRLNHPCVIQFVGAcLDDPSQFAIVTQY 73
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 8066 LSGGELFERITAEGYVMTEAEVINYMRQICEGIRHMHE--QNIIHLDIKPENIMCQTRSSTNVKliDFG---LATRLDPN 8140
Cdd:cd14064    74 VSGGSLFSLLHEQKRVIDLQSKLIIAVDVAKGMEYLHNltQPIIHRDLNSHNILLYEDGHAVVA--DFGesrFLQSLDED 151
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|
gi 281359561 8141 EVVKiTTGTAEFAAPEIVNRepVGFYT---DMWATGVLSYVLLSGLSPFA 8187
Cdd:cd14064   152 NMTK-QPGNLRWMAPEVFTQ--CTRYSikaDVFSYALCLWELLTGEIPFA 198
STKc_LRRK2 cd14068
Catalytic domain of the Serine/Threonine Kinase, Leucine-Rich Repeat Kinase 2; STKs catalyze ...
7995-8182 1.05e-10

Catalytic domain of the Serine/Threonine Kinase, Leucine-Rich Repeat Kinase 2; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. LRRK2 is one of two vertebrate LRRKs which show complementary expression in the brain. Mutations in LRRK2, found in the kinase, ROC-COR, and WD40 domains, are linked to both familial and sporadic forms of Parkinson's disease. The most prevalent mutation, G2019S located in the activation loop of the kinase domain, increases kinase activity. The R1441C/G mutations in the GTPase domain have also been reported to influence kinase activity. LRRKs are also classified as ROCO proteins because they contain a ROC (Ras of complex proteins)/GTPase domain followed by a COR (C-terminal of ROC) domain of unknown function. In addition, LRRKs contain a catalytic kinase domain and protein-protein interaction motifs including a WD40 domain, LRRs and ankyrin (ANK) repeats. LRRKs possess both GTPase and kinase activities, with the ROC domain acting as a molecular switch for the kinase domain, cycling between a GTP-bound state which drives kinase activity and a GDP-bound state which decreases the activity. The LRRK2 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270970 [Multi-domain]  Cd Length: 252  Bit Score: 66.13  E-value: 1.05e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 7995 IGTGAFGVVHRCRERstGNIFAAKfIPVSHSVEKdLIRREIDIMNQLHHQKLINLHDAfeDDDEMILILEFLSGGELFER 8074
Cdd:cd14068     2 LGDGGFGSVYRAVYR--GEDVAVK-IFNKHTSFR-LLRQELVVLSHLHHPSLVALLAA--GTAPRMLVMELAPKGSLDAL 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 8075 ITAEGYVMTEAEVINYMRQICEGIRHMHEQNIIHLDIKPENIM---CQTRSSTNVKLIDFGLAT---RLDpnevVKITTG 8148
Cdd:cd14068    76 LQQDNASLTRTLQHRIALHVADGLRYLHSAMIIYRDLKPHNVLlftLYPNCAIIAKIADYGIAQyccRMG----IKTSEG 151
                         170       180       190
                  ....*....|....*....|....*....|....*.
gi 281359561 8149 TAEFAAPEiVNREPVGF--YTDMWATGVLSYVLLSG 8182
Cdd:cd14068   152 TPGFRAPE-VARGNVIYnqQADVYSFGLLLYDILTC 186
STK_BAK1_like cd14664
Catalytic domain of the Serine/Threonine Kinase, BRI1 associated kinase 1 and related STKs; ...
7995-8200 1.05e-10

Catalytic domain of the Serine/Threonine Kinase, BRI1 associated kinase 1 and related STKs; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily includes three leucine-rich repeat receptor-like kinases (LRR-RLKs): Arabidopsis thaliana BAK1 and CLAVATA1 (CLV1), and Physcomitrella patens CLL1B clavata1-like receptor S/T protein kinase. BAK1 functions in various signaling pathways. It plays a role in BR (brassinosteroid)-regulated plant development as a co-receptor of BRASSINOSTEROID (BR) INSENSITIVE 1 (BRI1), the receptor for BRs, and is required for full activation of BR signaling. It also modulates pathways involved in plant resistance to pathogen infection (pattern-triggered immunity, PTI) and herbivore attack (wound- or herbivore feeding-induced accumulation of jasmonic acid (JA) and JA-isoleucine. CLV1, directly binds small signaling peptides, CLAVATA3 (CLV3) and CLAVATA3/EMBRYO SURROUNDING REGI0N (CLE), to restrict stem cell proliferation: the CLV3-CLV1-WUS (WUSCHEL) module influences stem cell maintenance in the shoot apical meristem, and the CLE40 (CLAVATA3/EMBRYO SURROUNDING REGION40) -ACR4 (CRINKLY4) -CLV1- WOX5 (WUSCHEL-RELATED HOMEOBOX5) module at the root apical meristem. The STK_BAK1-like subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271134 [Multi-domain]  Cd Length: 270  Bit Score: 66.75  E-value: 1.05e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 7995 IGTGAFGVVHRCReRSTGNIFAAKFIPVSHSVEKDL-IRREIDIMNQLHHQKLINLHDAFEDDDEMILILEFLSGGE--- 8070
Cdd:cd14664     1 IGRGGAGTVYKGV-MPNGTLVAVKRLKGEGTQGGDHgFQAEIQTLGMIRHRNIVRLRGYCSNPTTNLLVYEYMPNGSlge 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 8071 -LFERITAEGYVMTEAEViNYMRQICEGIRHMHEQ---NIIHLDIKPENIMCQTRSSTNVKliDFGLATRLDPN--EVVK 8144
Cdd:cd14664    80 lLHSRPESQPPLDWETRQ-RIALGSARGLAYLHHDcspLIIHRDVKSNNILLDEEFEAHVA--DFGLAKLMDDKdsHVMS 156
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 281359561 8145 ITTGTAEFAAPEIVNREPVGFYTDMWATGVLSYVLLSGLSPFA---GDNDVQTLKNVKA 8200
Cdd:cd14664   157 SVAGSYGYIAPEYAYTGKVSEKSDVYSYGVVLLELITGKRPFDeafLDDGVDIVDWVRG 215
IG_like smart00410
Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.
2312-2395 1.10e-10

Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.


Pssm-ID: 214653 [Multi-domain]  Cd Length: 85  Bit Score: 61.37  E-value: 1.10e-10
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561   2312 KNVTVKKGQTIRFDIKYDGEPEPAATWVKGTDNLKFDNQRICLDQLERNSSITIKKSVRKDTGKYKLVLSNSSGTIESEA 2391
Cdd:smart00410    2 PSVTVKEGESVTLSCEASGSPPPEVTWYKQGGKLLAESGRFSVSRSGSTSTLTISNVTPEDSGTYTCAATNSSGSASSGT 81

                    ....
gi 281359561   2392 QVVV 2395
Cdd:smart00410   82 TLTV 85
PTKc_Src cd05071
Catalytic domain of the Protein Tyrosine Kinase, Src; PTKs catalyze the transfer of the ...
7994-8199 1.11e-10

Catalytic domain of the Protein Tyrosine Kinase, Src; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Src (or c-Src) is a cytoplasmic (or non-receptor) PTK, containing an N-terminal SH4 domain with a myristoylation site, followed by SH3 and SH2 domains, a tyr kinase domain, and a regulatory C-terminal region with a conserved tyr. It is activated by autophosphorylation at the tyr kinase domain, and is negatively regulated by phosphorylation at the C-terminal tyr by Csk (C-terminal Src Kinase). c-Src is the vertebrate homolog of the oncogenic protein (v-Src) from Rous sarcoma virus. Together with other Src subfamily proteins, it is involved in signaling pathways that regulate cytokine and growth factor responses, cytoskeleton dynamics, cell proliferation, survival, and differentiation. Src also play a role in regulating cell adhesion, invasion, and motility in cancer cells and tumor vasculature, contributing to cancer progression and metastasis. Elevated levels of Src kinase activity have been reported in a variety of human cancers. Several inhibitors of Src have been developed as anti-cancer drugs. Src is also implicated in acute inflammatory responses and osteoclast function. The Src subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270656 [Multi-domain]  Cd Length: 277  Bit Score: 66.63  E-value: 1.11e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 7994 EIGTGAFGVVHRCRERSTGNIFAAKFIPVSHSVEKDLirREIDIMNQLHHQKLINLHdAFEDDDEMILILEFLSGGELFE 8073
Cdd:cd05071    16 KLGQGCFGEVWMGTWNGTTRVAIKTLKPGTMSPEAFL--QEAQVMKKLRHEKLVQLY-AVVSEEPIYIVTEYMSKGSLLD 92
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 8074 RITAE-GYVMTEAEVINYMRQICEGIRHMHEQNIIHLDIKPENIMcqTRSSTNVKLIDFGLATRLDPNEVVKITTGT--A 8150
Cdd:cd05071    93 FLKGEmGKYLRLPQLVDMAAQIASGMAYVERMNYVHRDLRAANIL--VGENLVCKVADFGLARLIEDNEYTARQGAKfpI 170
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|
gi 281359561 8151 EFAAPEIVNREPVGFYTDMWATGVLSYVLLS-GLSPFAGDNDVQTLKNVK 8199
Cdd:cd05071   171 KWTAPEAALYGRFTIKSDVWSFGILLTELTTkGRVPYPGMVNREVLDQVE 220
PTKc_Tyk2_rpt2 cd05080
Catalytic (repeat 2) domain of the Protein Tyrosine Kinase, Tyrosine kinase 2; PTKs catalyze ...
7992-8185 1.32e-10

Catalytic (repeat 2) domain of the Protein Tyrosine Kinase, Tyrosine kinase 2; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Tyk2 is widely expressed in many tissues. It is involved in signaling via the cytokine receptors IFN-alphabeta, IL-6, IL-10, IL-12, IL-13, and IL-23. It mediates cell surface urokinase receptor (uPAR) signaling and plays a role in modulating vascular smooth muscle cell (VSMC) functional behavior in response to injury. Tyk2 is also important in dendritic cell function and T helper (Th)1 cell differentiation. A homozygous mutation of Tyk2 was found in a patient with hyper-IgE syndrome (HIES), a primary immunodeficiency characterized by recurrent skin abscesses, pneumonia, and elevated serum IgE. This suggests that Tyk2 may play important roles in multiple cytokine signaling involved in innate and adaptive immunity. Tyk2 is a member of the Janus kinase (Jak) subfamily of proteins, which are cytoplasmic (or nonreceptor) PTKs containing an N-terminal FERM domain, followed by a Src homology 2 (SH2) domain, a pseudokinase domain, and a C-terminal tyr kinase catalytic domain. Jaks are crucial for cytokine receptor signaling. They are activated by autophosphorylation upon cytokine-induced receptor aggregation, and subsequently trigger downstream signaling events such as the phosphorylation of signal transducers and activators of transcription (STATs). The Tyk2 subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270664 [Multi-domain]  Cd Length: 283  Bit Score: 66.46  E-value: 1.32e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 7992 LEEIGTGAFGVVHRCR----ERSTGNIFAAKFIPVSHSVE-KDLIRREIDIMNQLHHQKLINLHDAFED--DDEMILILE 8064
Cdd:cd05080     9 IRDLGEGHFGKVSLYCydptNDGTGEMVAVKALKADCGPQhRSGWKQEIDILKTLYHENIVKYKGCCSEqgGKSLQLIME 88
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 8065 FLSGGELFERITAEGyvMTEAEVINYMRQICEGIRHMHEQNIIHLDIKPENIMCQTRSStnVKLIDFGLATRLDPNEVVK 8144
Cdd:cd05080    89 YVPLGSLRDYLPKHS--IGLAQLLLFAQQICEGMAYLHSQHYIHRDLAARNVLLDNDRL--VKIGDFGLAKAVPEGHEYY 164
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*....
gi 281359561 8145 ITTGTAE----FAAPEIVNREPVGFYTDMWATGVLSYVLL----SGLSP 8185
Cdd:cd05080   165 RVREDGDspvfWYAPECLKEYKFYYASDVWSFGVTLYELLthcdSSQSP 213
IgI_Myotilin_C_like cd05744
Immunoglobulin (Ig)-like domain of myotilin, palladin, and myopalladin; member of the I-set of ...
7648-7737 1.34e-10

Immunoglobulin (Ig)-like domain of myotilin, palladin, and myopalladin; member of the I-set of Ig superfamily (IgSF) domains; The members here are composed of the immunoglobulin (Ig)-like domain in myotilin, palladin, and myopalladin. Myotilin, palladin, and myopalladin function as scaffolds that regulate actin organization. Myotilin and myopalladin are most abundant in skeletal and cardiac muscle; palladin is ubiquitously expressed in the organs of developing vertebrates and plays a key role in cellular morphogenesis. The three family members each interact with specific molecular partners with all three binding to alpha-actinin; In addition, palladin also binds to vasodilator-stimulated phosphoprotein (VASP) and ezrin, myotilin binds to filamin and actin, and myopalladin also binds to nebulin and cardiac ankyrin repeat protein (CARP). This group belongs to the I-set of IgSF domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand, but lack a C" strand.


Pssm-ID: 409405 [Multi-domain]  Cd Length: 91  Bit Score: 61.36  E-value: 1.34e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 7648 PLIVKPLRDANCIQNHNAQFTCTINGVPKPTISWYKGAREISNGARYHMY-SEGDNHFLNINDVFGEDADEYVCRAVNKA 7726
Cdd:cd05744     1 PHFLQAPGDLEVQEGRLCRFDCKVSGLPTPDLFWQLNGKPVRPDSAHKMLvRENGRHSLIIEPVTKRDAGIYTCIARNRA 80
                          90
                  ....*....|.
gi 281359561 7727 GAKSTRATLAI 7737
Cdd:cd05744    81 GENSFNAELVV 91
STKc_TTBK cd14017
Catalytic domain of the Serine/Threonine protein kinase, Tau-Tubulin Kinase; STKs catalyze the ...
7988-8224 1.40e-10

Catalytic domain of the Serine/Threonine protein kinase, Tau-Tubulin Kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. TTBK is a neuron-specific kinase that phosphorylates the microtubule-associated protein tau and promotes its aggregation. Higher vertebrates contain two TTBK proteins, TTBK1 and TTBK2, both of which have been implicated in neurodegeneration. TTBK1 has been linked to Alzheimer's disease (AD) while TTBK2 is associated with spinocerebellar ataxia type 11 (SCA11). Both AD and SCA11 patients show the presence of neurofibrillary tangles in the brain. The Drosophila TTBK homolog, Asator, is an essential protein that localizes to the mitotic spindle during mitosis and may be involved in regulating microtubule dynamics and function. The TTBK subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270919 [Multi-domain]  Cd Length: 263  Bit Score: 66.13  E-value: 1.40e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 7988 RYDILEEIGTGAFGVVHRCRERSTGNIFAAKfipV-SHSVEKDLIRREIDIMNQL----HHQKLInlhdAFEDDDEMILI 8062
Cdd:cd14017     1 RWKVVKKIGGGGFGEIYKVRDVVDGEEVAMK---VeSKSQPKQVLKMEVAVLKKLqgkpHFCRLI----GCGRTERYNYI 73
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 8063 LEFLSGGELFE--RITAEGyVMTEAEVINYMRQICEGIRHMHEQNIIHLDIKPENIMCQTRSST--NVKLIDFGLATR-L 8137
Cdd:cd14017    74 VMTLLGPNLAElrRSQPRG-KFSVSTTLRLGIQILKAIEDIHEVGFLHRDVKPSNFAIGRGPSDerTVYILDFGLARQyT 152
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 8138 DPNEVVKITT-------GTAEFAAPEIVNREPVGFYTDMWAtgvLSYVLL---SGLSPFAG-DNDVQTLKNVKACDwdfD 8206
Cdd:cd14017   153 NKDGEVERPPrnaagfrGTVRYASVNAHRNKEQGRRDDLWS---WFYMLIefvTGQLPWRKlKDKEEVGKMKEKID---H 226
                         250       260
                  ....*....|....*....|.
gi 281359561 8207 VESFKYISEEAKDF---IRKL 8224
Cdd:cd14017   227 EELLKGLPKEFFQIlkhIRSL 247
FN3 COG3401
Fibronectin type 3 domain [General function prediction only];
5245-5570 1.62e-10

Fibronectin type 3 domain [General function prediction only];


Pssm-ID: 442628 [Multi-domain]  Cd Length: 603  Bit Score: 68.49  E-value: 1.62e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 5245 YEFRVRAVNKAGPGSPSDATETHVARPKNTPPKIDRNFMSDIKIKAGNVFEFDVPVTGEPLPSKDWTHEGNMIINTDRVK 5324
Cdd:COG3401    22 AVNALSKAGGSGKTILVYLAVVLSVTTKESPGTLLVAAGLSSGGGLGTGGRAGTTSGVAAVAVAAAPPTATGLTTLTGSG 101
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 5325 ISNFDDRTKIRILDAKRSDTGVYTLTARNINGTDRhnvkvtiLDAPSVPEGPLRNGDVSKNSIVLRWRPPKDDGGSEITH 5404
Cdd:COG3401   102 SVGGATNTGLTSSDEVPSPAVGTATTATAVAGGAA-------TAGTYALGAGLYGVDGANASGTTASSVAGAGVVVSPDT 174
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 5405 YVVEKMDNEAMRWVPVGdctdTEIRADNLIENHDYSFRVRAVNKQGQSQPlttSQPITAKDPYSHPDKPGQPQATDWGKH 5484
Cdd:COG3401   175 SATAAVATTSLTVTSTT----LVDGGGDIEPGTTYYYRVAATDTGGESAP---SNEVSVTTPTTPPSAPTGLTATADTPG 247
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 5485 FVDLEWSTPKRDGgapISSYIIEKRP-KFGQWERAAVVLG----DNckahvpELTNGGEYEFRVIAVN-RGGPSDPSDPS 5558
Cdd:COG3401   248 SVTLSWDPVTESD---ATGYRVYRSNsGDGPFTKVATVTTtsytDT------GLTNGTTYYYRVTAVDaAGNESAPSNVV 318
                         330
                  ....*....|..
gi 281359561 5559 STIICKPRFLAP 5570
Cdd:COG3401   319 SVTTDLTPPAAP 330
Ig cd00096
Immunoglobulin domain; The members here are composed of the immunoglobulin (Ig) domain found ...
8757-8824 1.63e-10

Immunoglobulin domain; The members here are composed of the immunoglobulin (Ig) domain found in the Ig superfamily. The Ig superfamily is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. Members of this group are components of immunoglobulin, neuroglia, cell surface glycoproteins, including T-cell receptors, CD2, CD4, CD8, and membrane glycoproteins, including butyrophilin and chondroitin sulfate proteoglycan core protein. A predominant feature of most Ig domains is a disulfide bridge connecting the two beta-sheets with a tryptophan residue packed against the disulfide bond. Ig superfamily (IgSF) domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. Typically, the V-set domains have A, B, E, and D strands in one sheet and A', G, F, C, C' and C" in the other. The structures in C1-set are smaller than those in the V-set; they have one beta sheet that is formed by strands A, B, E, and D and the other by strands G, F, C, and C'. Moreover, a C1-set Ig domain contains a short C' strand (three residues) and lacks A' and C" strand. Unlike other Ig domain sets, C2-set structures do not have a D strand. Like the V-set Ig domains, members of the I-set have a discontinuous A strand, but lack a C" strand.


Pssm-ID: 409353 [Multi-domain]  Cd Length: 70  Bit Score: 60.42  E-value: 1.63e-10
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 281359561 8757 VNLACRIIGAQHFDVVWLHNNKEIKPSKDFQYTNEANIYRLQIAEIFPEDGGTYTCEAFNDIGESFST 8824
Cdd:cd00096     1 VTLTCSASGNPPPTITWYKNGKPLPPSSRDSRRSELGNGTLTISNVTLEDSGTYTCVASNSAGGSASA 68
fn3 pfam00041
Fibronectin type III domain;
3000-3085 1.66e-10

Fibronectin type III domain;


Pssm-ID: 394996 [Multi-domain]  Cd Length: 85  Bit Score: 60.89  E-value: 1.66e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561  3000 SKPRGpLDVKDVTKDSCKLKWKKPEDDGGkPISAYQVEKFDKKQGRWVPLGRTSANDTEFDVKGLQEGHEYQFRVKAINE 3079
Cdd:pfam00041    1 SAPSN-LTVTDVTSTSLTVSWTPPPDGNG-PITGYEVEYRPKNSGEPWNEITVPGTTTSVTLTGLKPGTEYEVRVQAVNG 78

                   ....*.
gi 281359561  3080 EGESDP 3085
Cdd:pfam00041   79 GGEGPP 84
fn3 pfam00041
Fibronectin type III domain;
2401-2485 1.89e-10

Fibronectin type III domain;


Pssm-ID: 394996 [Multi-domain]  Cd Length: 85  Bit Score: 60.89  E-value: 1.89e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561  2401 PPGGpFEPEEIRASHIKMKWKRPDDDGGcEISGYALERMDEETGRWIPAGEVGPNETSFDFKGLTPNKKYKFRVKAINKE 2480
Cdd:pfam00041    2 APSN-LTVTDVTSTSLTVSWTPPPDGNG-PITGYEVEYRPKNSGEPWNEITVPGTTTSVTLTGLKPGTEYEVRVQAVNGG 79

                   ....*
gi 281359561  2481 GESEP 2485
Cdd:pfam00041   80 GEGPP 84
fn3 pfam00041
Fibronectin type III domain;
2102-2187 1.89e-10

Fibronectin type III domain;


Pssm-ID: 394996 [Multi-domain]  Cd Length: 85  Bit Score: 60.89  E-value: 1.89e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561  2102 PPQDVDITDVYQTSCVVSFNPPSDDGGtPITKYVIERQDLSKKHGWESVAEVLPSEPClkKIDDLIPKKQYRFRIRAVNA 2181
Cdd:pfam00041    2 APSNLTVTDVTSTSLTVSWTPPPDGNG-PITGYEVEYRPKNSGEPWNEITVPGTTTSV--TLTGLKPGTEYEVRVQAVNG 78

                   ....*.
gi 281359561  2182 IGQSDP 2187
Cdd:pfam00041   79 GGEGPP 84
PTKc_EGFR_like cd05057
Catalytic domain of Epidermal Growth Factor Receptor-like Protein Tyrosine Kinases; PTKs ...
7995-8188 1.97e-10

Catalytic domain of Epidermal Growth Factor Receptor-like Protein Tyrosine Kinases; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. EGFR (HER, ErbB) subfamily members include EGFR (HER1, ErbB1), HER2 (ErbB2), HER3 (ErbB3), HER4 (ErbB4), and similar proteins. They are receptor PTKs (RTKs) containing an extracellular EGF-related ligand-binding region, a transmembrane helix, and a cytoplasmic region with a tyr kinase domain and a regulatory C-terminal tail. Unlike other PTKs, phosphorylation of the activation loop of EGFR proteins is not critical to their activation. Instead, they are activated by ligand-induced dimerization, resulting in the phosphorylation of tyr residues in the C-terminal tail, which serve as binding sites for downstream signaling molecules. Collectively, they can recognize a variety of ligands including EGF, TGFalpha, and neuregulins, among others. All four subfamily members can form homo- or heterodimers. HER3 contains an impaired kinase domain and depends on its heterodimerization partner for activation. EGFR subfamily members are involved in signaling pathways leading to a broad range of cellular responses including cell proliferation, differentiation, migration, growth inhibition, and apoptosis. Gain of function alterations, through their overexpression, deletions, or point mutations in their kinase domains, have been implicated in various cancers. These receptors are targets of many small molecule inhibitors and monoclonal antibodies used in cancer therapy. The EGFR subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270648 [Multi-domain]  Cd Length: 279  Bit Score: 65.90  E-value: 1.97e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 7995 IGTGAFGVVHRCRERSTGNifAAKfIPVSHSVEKDL--------IRREIDIMNQLHHQKLINLHdAFEDDDEMILILEFL 8066
Cdd:cd05057    15 LGSGAFGTVYKGVWIPEGE--KVK-IPVAIKVLREEtgpkaneeILDEAYVMASVDHPHLVRLL-GICLSSQVQLITQLM 90
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 8067 SGGELFERITAEGYVMTEAEVINYMRQICEGIRHMHEQNIIHLDIKPENIMCQTRSstNVKLIDFGLATRLDPNEVVKIT 8146
Cdd:cd05057    91 PLGCLLDYVRNHRDNIGSQLLLNWCVQIAKGMSYLEEKRLVHRDLAARNVLVKTPN--HVKITDFGLAKLLDVDEKEYHA 168
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|
gi 281359561 8147 TGTA---EFAAPE-IVNREpvgfYT---DMWATGVLSYVLLS-GLSPFAG 8188
Cdd:cd05057   169 EGGKvpiKWMALEsIQYRI----YThksDVWSYGVTVWELMTfGAKPYEG 214
PTKc_Yes cd05069
Catalytic domain of the Protein Tyrosine Kinase, Yes; PTKs catalyze the transfer of the ...
7979-8199 2.09e-10

Catalytic domain of the Protein Tyrosine Kinase, Yes; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Yes (or c-Yes) is a member of the Src subfamily of proteins, which are cytoplasmic (or non-receptor) PTKs. c-Yes kinase is the cellular homolog of the oncogenic protein (v-Yes) encoded by the Yamaguchi 73 and Esh sarcoma viruses. It displays functional overlap with other Src subfamily members, particularly Src. It also shows some unique functions such as binding to occludins, transmembrane proteins that regulate extracellular interactions in tight junctions. Yes also associates with a number of proteins in different cell types that Src does not interact with, like JAK2 and gp130 in pre-adipocytes, and Pyk2 in treated pulmonary vein endothelial cells. Although the biological function of Yes remains unclear, it appears to have a role in regulating cell-cell interactions and vesicle trafficking in polarized cells. Src kinases contain an N-terminal SH4 domain with a myristoylation site, followed by SH3 and SH2 domains, a tyr kinase domain, and a regulatory C-terminal region containing a conserved tyr. They are activated by autophosphorylation at the tyr kinase domain, but are negatively regulated by phosphorylation at the C-terminal tyr by Csk (C-terminal Src Kinase). The Yes subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase (PI3K).


Pssm-ID: 270654 [Multi-domain]  Cd Length: 279  Bit Score: 65.86  E-value: 2.09e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 7979 EISQQSVydRYDIleEIGTGAFGVVHRCRERSTGNIFAAKFIPVSHSVEKDLirREIDIMNQLHHQKLINLHdAFEDDDE 8058
Cdd:cd05069     8 EIPRESL--RLDV--KLGQGCFGEVWMGTWNGTTKVAIKTLKPGTMMPEAFL--QEAQIMKKLRHDKLVPLY-AVVSEEP 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 8059 MILILEFLSGGELFERIT-AEGYVMTEAEVINYMRQICEGIRHMHEQNIIHLDIKPENIMcqTRSSTNVKLIDFGLATRL 8137
Cdd:cd05069    81 IYIVTEFMGKGSLLDFLKeGDGKYLKLPQLVDMAAQIADGMAYIERMNYIHRDLRAANIL--VGDNLVCKIADFGLARLI 158
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 281359561 8138 DPNEVVKITTGT--AEFAAPEIVNREPVGFYTDMWATGVLSYVLLS-GLSPFAGDNDVQTLKNVK 8199
Cdd:cd05069   159 EDNEYTARQGAKfpIKWTAPEAALYGRFTIKSDVWSFGILLTELVTkGRVPYPGMVNREVLEQVE 223
STKc_LIMK1 cd14221
Catalytic domain of the Serine/Threonine Kinase, LIM domain kinase 1; STKs catalyze the ...
7995-8175 2.19e-10

Catalytic domain of the Serine/Threonine Kinase, LIM domain kinase 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. LIMK1 activation is induced by bone morphogenic protein, vascular endothelial growth factor, and thrombin. It plays roles in microtubule disassembly and cell cycle progression, and is critical in the regulation of neurite outgrowth. LIMK1 knockout mice show abnormalities in dendritic spine morphology and synaptic function. LIMK1 is one of the genes deleted in patients with Williams Syndrome, which is characterized by distinct craniofacial features, cardiovascular problems, as well as behavioral and neurological abnormalities. LIMKs phosphorylate and inactivate cofilin, an actin depolymerizing factor, to induce the reorganization of the actin cytoskeleton. They act downstream of Rho GTPases and are expressed ubiquitously. As regulators of actin dynamics, they contribute to diverse cellular functions such as cell motility, morphogenesis, differentiation, apoptosis, meiosis, mitosis, and neurite extension. LIMKs contain the LIM (two repeats), PDZ, and catalytic kinase domains. The LIMK1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271123 [Multi-domain]  Cd Length: 267  Bit Score: 65.75  E-value: 2.19e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 7995 IGTGAFGVVHRCRERSTGNIFAAK-FIPVSHSVEKDLIRrEIDIMNQLHHQKLINLHDAFEDDDEMILILEFLSGGELFE 8073
Cdd:cd14221     1 LGKGCFGQAIKVTHRETGEVMVMKeLIRFDEETQRTFLK-EVKVMRCLEHPNVLKFIGVLYKDKRLNFITEYIKGGTLRG 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 8074 RITAEGYVMTEAEVINYMRQICEGIRHMHEQNIIHLDIKPENimCQTRSSTNVKLIDFGLAtRLDPNEVVK--------- 8144
Cdd:cd14221    80 IIKSMDSHYPWSQRVSFAKDIASGMAYLHSMNIIHRDLNSHN--CLVRENKSVVVADFGLA-RLMVDEKTQpeglrslkk 156
                         170       180       190
                  ....*....|....*....|....*....|....*...
gi 281359561 8145 -------ITTGTAEFAAPEIVNREPVGFYTDMWATGVL 8175
Cdd:cd14221   157 pdrkkryTVVGNPYWMAPEMINGRSYDEKVDVFSFGIV 194
STKc_PDIK1L cd13977
Catalytic domain of the Serine/Threonine kinase, PDLIM1 interacting kinase 1 like; STKs ...
7988-8180 2.32e-10

Catalytic domain of the Serine/Threonine kinase, PDLIM1 interacting kinase 1 like; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PDIK1L is also called STK35 or CLIK-1. It is predominantly a nuclear protein which is capable of autophosphorylation. Through its interaction with the PDZ-LIM protein CLP-36, it is localized to actin stress fibers. The PDIK1L subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase (PI3K).


Pssm-ID: 270879 [Multi-domain]  Cd Length: 322  Bit Score: 66.43  E-value: 2.32e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 7988 RYDILEEIGTGAFGVVHRCRERSTGNIFAAKFIPVSHSVEKDLIRREIDIMN--QLHHQKLINLHDAFEDDDEMI----- 8060
Cdd:cd13977     1 KYSLIREVGRGSYGVVYEAVVRRTGARVAVKKIRCNAPENVELALREFWALSsiQRQHPNVIQLEECVLQRDGLAqrmsh 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 8061 -------------------------------LILEFLSGGELFEritaegYVMTE----AEVINYMRQICEGIRHMHEQN 8105
Cdd:cd13977    81 gssksdlylllvetslkgercfdprsacylwFVMEFCDGGDMNE------YLLSRrpdrQTNTSFMLQLSSALAFLHRNQ 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 8106 IIHLDIKPENIM-CQTRSSTNVKLIDFGLA-----TRLDPNEVVKITT-------GTAEFAAPEIVNrepvGFYT---DM 8169
Cdd:cd13977   155 IVHRDLKPDNILiSHKRGEPILKVADFGLSkvcsgSGLNPEEPANVNKhflssacGSDFYMAPEVWE----GHYTakaDI 230
                         250
                  ....*....|.
gi 281359561 8170 WATGVLSYVLL 8180
Cdd:cd13977   231 FALGIIIWAMV 241
PTKc_EphR_B cd05065
Catalytic domain of the Protein Tyrosine Kinases, Class EphB Ephrin Receptors; PTKs catalyze ...
7991-8186 2.39e-10

Catalytic domain of the Protein Tyrosine Kinases, Class EphB Ephrin Receptors; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Class EphB receptors bind to transmembrane ephrin-B ligands. There are six vertebrate EphB receptors (EphB1-6), which display promiscuous interactions with three ephrin-B ligands. One exception is EphB2, which also interacts with ephrin A5. EphB receptors play important roles in synapse formation and plasticity, spine morphogenesis, axon guidance, and angiogenesis. In the intestinal epithelium, EphBs are Wnt signaling target genes that control cell compartmentalization. They function as suppressors of colon cancer progression. EphRs comprise the largest subfamily of receptor PTKs (RTKs). They contain an ephrin-binding domain and two fibronectin repeats extracellularly, a transmembrane segment, and a cytoplasmic tyr kinase domain. Binding of the ephrin ligand to EphR requires cell-cell contact since both are anchored to the plasma membrane. The resulting downstream signals occur bidirectionally in both EphR-expressing cells (forward signaling) and ephrin-expressing cells (reverse signaling). Ephrin/EphR interaction mainly results in cell-cell repulsion or adhesion. The EphB subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 173638 [Multi-domain]  Cd Length: 269  Bit Score: 65.66  E-value: 2.39e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 7991 ILEEIGTGAFGVVHRCRERSTG---NIFAAKFIPVSHSVEKdliRR----EIDIMNQLHHQKLINLHDAFEDDDEMILIL 8063
Cdd:cd05065     8 IEEVIGAGEFGEVCRGRLKLPGkreIFVAIKTLKSGYTEKQ---RRdflsEASIMGQFDHPNIIHLEGVVTKSRPVMIIT 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 8064 EFLSGGELFERITAEGYVMTEAEVINYMRQICEGIRHMHEQNIIHLDIKPENIMcqTRSSTNVKLIDFGLATRLDPNEVV 8143
Cdd:cd05065    85 EFMENGALDSFLRQNDGQFTVIQLVGMLRGIAAGMKYLSEMNYVHRDLAARNIL--VNSNLVCKVSDFGLSRFLEDDTSD 162
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|
gi 281359561 8144 KITTGT------AEFAAPEIVNREPVGFYTDMWATGVLSYVLLS-GLSPF 8186
Cdd:cd05065   163 PTYTSSlggkipIRWTAPEAIAYRKFTSASDVWSYGIVMWEVMSyGERPY 212
Ig4_Contactin-2-like cd05728
Fourth Ig domain of the neural cell adhesion molecule contactin-2, and similar domains; The ...
7255-7344 2.53e-10

Fourth Ig domain of the neural cell adhesion molecule contactin-2, and similar domains; The members here are composed of the fourth Ig domain of the neural cell adhesion molecule contactin-2. Contactins are comprised of six Ig domains followed by four fibronectin type III (FnIII) domains anchored to the membrane by glycosylphosphatidylinositol. Contactin-2 (also called TAG-1, axonin-1) facilitates cell adhesion by homophilic binding between molecules in apposed membranes. The first four Ig domains form the intermolecular binding fragment which arranges as a compact U-shaped module by contacts between Ig domains 1 and 4, and domains 2 and 3. It has been proposed that a linear zipper-like array forms, from contactin-2 molecules alternatively provided by the two apposed membranes.


Pssm-ID: 143205 [Multi-domain]  Cd Length: 85  Bit Score: 60.69  E-value: 2.53e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 7255 DWITRLQDKVAPFGKDYTLQCAASGKPSPTARWLRNGK------EIQMNGGrmtcdskdgvfRLHISNVQTGDDGDYTCE 7328
Cdd:cd05728     1 EWLKVISDTEADIGSSLRWECKASGNPRPAYRWLKNGQplasenRIEVEAG-----------DLRITKLSLSDSGMYQCV 69
                          90
                  ....*....|....*.
gi 281359561 7329 AMNSLGFVNTSGYLKI 7344
Cdd:cd05728    70 AENKHGTIYASAELAV 85
PTKc_Csk cd05082
Catalytic domain of the Protein Tyrosine Kinase, C-terminal Src kinase; PTKs catalyze the ...
7991-8186 2.60e-10

Catalytic domain of the Protein Tyrosine Kinase, C-terminal Src kinase; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Csk catalyzes the tyr phosphorylation of the regulatory C-terminal tail of Src kinases, resulting in their inactivation. Csk is expressed in a wide variety of tissues. As a negative regulator of Src, Csk plays a role in cell proliferation, survival, and differentiation, and consequently, in cancer development and progression. Csk is a cytoplasmic (or nonreceptor) PTK containing the Src homology domains, SH3 and SH2, N-terminal to the catalytic tyr kinase domain. To inhibit Src kinases, Csk is translocated to the membrane via binding to specific transmembrane proteins, G-proteins, or adaptor proteins near the membrane. In addition, Csk also shows Src-independent functions. It is a critical component in G-protein signaling, and plays a role in cytoskeletal reorganization and cell migration. The Csk subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 133213 [Multi-domain]  Cd Length: 256  Bit Score: 65.00  E-value: 2.60e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 7991 ILEEIGTGAFGVVHRCRERstGNIFAAKFIpvSHSVEKDLIRREIDIMNQLHHQKLINLHDAF-EDDDEMILILEFLSGG 8069
Cdd:cd05082    10 LLQTIGKGEFGDVMLGDYR--GNKVAVKCI--KNDATAQAFLAEASVMTQLRHSNLVQLLGVIvEEKGGLYIVTEYMAKG 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 8070 ELFERITAEGYVMTEAE-VINYMRQICEGIRHMHEQNIIHLDIKPENIMCqtrSSTNV-KLIDFGLATRldpnevVKITT 8147
Cdd:cd05082    86 SLVDYLRSRGRSVLGGDcLLKFSLDVCEAMEYLEGNNFVHRDLAARNVLV---SEDNVaKVSDFGLTKE------ASSTQ 156
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....
gi 281359561 8148 GTA----EFAAPEIVNREPVGFYTDMWATGVLSYVLLS-GLSPF 8186
Cdd:cd05082   157 DTGklpvKWTAPEALREKKFSTKSDVWSFGILLWEIYSfGRVPY 200
IgI_APEG-1_like cd20975
Immunoglobulin-like domain of human Aortic Preferentially Expressed Protein-1 (APEG-1) and ...
7254-7334 2.76e-10

Immunoglobulin-like domain of human Aortic Preferentially Expressed Protein-1 (APEG-1) and similar proteins; a member of the I-set of IgSF domains; The members here are composed of the immunoglobulin I-set (IgI) domain of the Human Aortic Preferentially Expressed Protein-1 (APEG-1) and similar proteins. APEG-1 is a novel specific smooth muscle differentiation marker predicted to play a role in the growth and differentiation of arterial smooth muscle cells (SMCs). The Ig superfamily (IgSF) is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. Unlike the V-set, one of the distinctive features of I-set domains is the lack of a C" strand. The structure of the human APEG-1 lacks this strand and thus it belongs to the I-set of the IgSF. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors, the hemolymph protein hemolin, the muscle proteins titin, telokin, and twitchin, the neuronal adhesion molecule axonin-1, and the signaling molecule semaphorin 4D that is involved in axonal guidance, immune function and angiogenesis.


Pssm-ID: 409567  Cd Length: 91  Bit Score: 60.56  E-value: 2.76e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 7254 PDWITRLQDKVAPFGKDYTLQCAASGKPSPTARWLRNGKEIQMNGGRMTCDSKDGVFRLHISNVQTGDDGDYTCEAMNSL 7333
Cdd:cd20975     1 PTFKVSLMDQSVREGQDVIMSIRVQGEPKPVVSWLRNRQPVRPDQRRFAEEAEGGLCRLRILAAERGDAGFYTCKAVNEY 80

                  .
gi 281359561 7334 G 7334
Cdd:cd20975    81 G 81
IgI_4_hemolin-like cd20978
Fourth immunoglobulin (Ig)-like domain of hemolin, and similar domains; a member of the I-set ...
119-211 2.80e-10

Fourth immunoglobulin (Ig)-like domain of hemolin, and similar domains; a member of the I-set of IgSF domains; The members here are composed of the fourth immunoglobulin (Ig)-like domain of hemolin and similar proteins. Hemolin, an insect immunoglobulin superfamily (IgSF) member containing four Ig-like domains, is a lipopolysaccharide-binding immune protein induced during bacterial infection. Hemolin shares significant sequence similarity with the first four Ig-like domains of the transmembrane cell adhesion molecules (CAMs) of the L1 family. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. The fourth Ig-like domain of hemolin is a member of the I-set Ig domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set domains, members of the I-set have a discontinuous A strand but lack a C" strand. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors, the muscle proteins titin, telokin, and twitchin, the neuronal adhesion molecule axonin-1, and the signaling molecule semaphorin 4D that is involved in axonal guidance, immune function and angiogenesis.


Pssm-ID: 409570 [Multi-domain]  Cd Length: 88  Bit Score: 60.48  E-value: 2.80e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561  119 PTFAKKPAI-RQEEDGKRLLFECRVNADPIPAIIWFHNGAAVkESERHKITVDKDvhsyfaTLEILNVTVEDAGKYKVNA 197
Cdd:cd20978     1 PKFIQKPEKnVVVKGGQDVTLPCQVTGVPQPKITWLHNGKPL-QGPMERATVEDG------TLTIINVQPEDTGYYGCVA 73
                          90
                  ....*....|....
gi 281359561  198 KNELGESNATISLN 211
Cdd:cd20978    74 TNEIGDIYTETLLH 87
fn3 pfam00041
Fibronectin type III domain;
3102-3187 3.05e-10

Fibronectin type III domain;


Pssm-ID: 394996 [Multi-domain]  Cd Length: 85  Bit Score: 60.12  E-value: 3.05e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561  3102 SKPGTPNIVDYNEHMVKLKWEAPRsDGGAPISGYIIEKKDKFSP-IWDEILSTNTSvPEATVEGLVEGNIYQFRVRAVNK 3180
Cdd:pfam00041    1 SAPSNLTVTDVTSTSLTVSWTPPP-DGNGPITGYEVEYRPKNSGePWNEITVPGTT-TSVTLTGLKPGTEYEVRVQAVNG 78

                   ....*..
gi 281359561  3181 AGFSDPS 3187
Cdd:pfam00041   79 GGEGPPS 85
STKc_WNK4 cd14033
Catalytic domain of the Serine/Threonine protein kinase, With No Lysine (WNK) 4; STKs catalyze ...
7986-8241 3.56e-10

Catalytic domain of the Serine/Threonine protein kinase, With No Lysine (WNK) 4; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. WNK4 shows a restricted expression pattern and is usually found in epithelial cells. It is expressed in nephrons and in extrarenal tissues including intestine, eye, mammary glands, and prostate. WNK4 regulates a variety of ion transport proteins including apical or basolateral ion transporters, ion channels in the transcellular pathway, and claudins in the paracellular pathway. Mutations in WNK4 cause PseudoHypoAldosteronism type II (PHAII), characterized by hypertension and hyperkalemia. WNK4 inhibits the activity of the thiazide-sensitive Na-Cl cotransporter (NCC), which is responsible for about 15% of NaCl reabsorption in the kidney. It also inhibits the renal outer medullary potassium channel (ROMK) and decreases its surface expression. Hypertension and hyperkalemia in PHAII patients with WNK4 mutations may be partly due to increased NaCl reabsorption through NCC and impaired renal potassium secretion by ROMK, respectively. The WNK4 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270935 [Multi-domain]  Cd Length: 261  Bit Score: 65.02  E-value: 3.56e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 7986 YDRYDIleEIGTGAFGVVHRCRERSTGNIFAAKFIPVSH--SVEKDLIRREIDIMNQLHHQKLINLHDAFEDDDE----M 8059
Cdd:cd14033     2 FLKFNI--EIGRGSFKTVYRGLDTETTVEVAWCELQTRKlsKGERQRFSEEVEMLKGLQHPNIVRFYDSWKSTVRghkcI 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 8060 ILILEFLSGGELFERITaEGYVMTEAEVINYMRQICEGIRHMHEQN--IIHLDIKPENIMCqTRSSTNVKLIDFGLATrL 8137
Cdd:cd14033    80 ILVTELMTSGTLKTYLK-RFREMKLKLLQRWSRQILKGLHFLHSRCppILHRDLKCDNIFI-TGPTGSVKIGDLGLAT-L 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 8138 DPNEVVKITTGTAEFAAPEIVnREPVGFYTDMWATGVLSYVLLSGLSPFAG-DNDVQTLKNVKAcdwDFDVESFKYIS-E 8215
Cdd:cd14033   157 KRASFAKSVIGTPEFMAPEMY-EEKYDEAVDVYAFGMCILEMATSEYPYSEcQNAAQIYRKVTS---GIKPDSFYKVKvP 232
                         250       260
                  ....*....|....*....|....*.
gi 281359561 8216 EAKDFIRKLLVRNKEKRMTAHECLLH 8241
Cdd:cd14033   233 ELKEIIEGCIRTDKDERFTIQDLLEH 258
Ig_3 pfam13927
Immunoglobulin domain; This family contains immunoglobulin-like domains.
227-309 3.57e-10

Immunoglobulin domain; This family contains immunoglobulin-like domains.


Pssm-ID: 464046 [Multi-domain]  Cd Length: 78  Bit Score: 59.89  E-value: 3.57e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561   227 KPTFTERPVIRQSEDGGNVTFECRCVGDPTPTVTWSHGETELNESNRYKMSLTMDQKLyhiacLEISSVVSSDQGEYRAQ 306
Cdd:pfam13927    1 KPVITVSPSSVTVREGETVTLTCEATGSPPPTITWYKNGEPISSGSTRSRSLSGSNST-----LTISNVTRSDAGTYTCV 75

                   ...
gi 281359561   307 AKN 309
Cdd:pfam13927   76 ASN 78
FN3 COG3401
Fibronectin type 3 domain [General function prediction only];
5723-6243 3.64e-10

Fibronectin type 3 domain [General function prediction only];


Pssm-ID: 442628 [Multi-domain]  Cd Length: 603  Bit Score: 67.33  E-value: 3.64e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 5723 DVTRLVHRKEYLFRVKAVNAIGESDPleaVNTIIAKNEFDEPDAPGKPIITDWDRDHIDLQW-AVPKSDggapISEYIIQ 5801
Cdd:COG3401   195 GGGDIEPGTTYYYRVAATDTGGESAP---SNEVSVTTPTTPPSAPTGLTATADTPGSVTLSWdPVTESD----ATGYRVY 267
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 5802 KKEKGSPYWTNVrhVPSNKNTTTIPELTEGQEYEFRVIAVNQAGqsEPSEPSDMIMAKPRYLPpkiitplnevrikcgli 5881
Cdd:COG3401   268 RSNSGDGPFTKV--ATVTTTSYTDTGLTNGTTYYYRVTAVDAAG--NESAPSNVVSVTTDLTP----------------- 326
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 5882 fhtdihfigepapeatwtlnsnpllsndrstitsighhsvvhtvncqrsdsgiyhlllrnssgidegsfelvvldrPGPP 5961
Cdd:COG3401   327 ----------------------------------------------------------------------------PAAP 330
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 5962 EGpMEYEEITANSVTISWKPPKDNGgseISSYVIEkRDLTHGGGWVPAVNYVSAkyNHAVVPRLLEGTMYELRVMAENLQ 6041
Cdd:COG3401   331 SG-LTATAVGSSSITLSWTASSDAD---VTGYNVY-RSTSGGGTYTKIAETVTT--TSYTDTGLTPGTTYYYKVTAVDAA 403
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 6042 GRSDPLTsdqPVVAKSQYTVPGAPGKPELTDSDKNHITIKWKQPISNGGSPIIGYDIERRDVNTGRW-----IKINGQPV 6116
Cdd:COG3401   404 GNESAPS---EEVSATTASAASGESLTASVDAVPLTDVAGATAAASAASNPGVSAAVLADGGDTGNAvpfttTSSTVTAT 480
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 6117 PTAEYQDDRVTSNHQYQYRISAVNAAGNGKTSEPSAIFNARPLREKPRfYFDGLIGKRIKVRAGEpvNLNIPISGAPTPT 6196
Cdd:COG3401   481 TTDTTTANLSVTTGSLVGGSGASSVTNSVSVIGASAAAAVGGAPDGTP-NVTGASPVTVGASTGD--VLITDLVSLTTSA 557
                         490       500       510       520
                  ....*....|....*....|....*....|....*....|....*..
gi 281359561 6197 IEWKRGDLKLEEGKrISYETNSERTLFRIDDSNRRDSGKYTVTAANE 6243
Cdd:COG3401   558 SSSVSGAGLGSGNL-YLITTLGGSLLTTTSTNTNDVAGVHGGTLLVL 603
PTKc_EphR_A2 cd05063
Catalytic domain of the Protein Tyrosine Kinase, Ephrin Receptor A2; PTKs catalyze the ...
7976-8186 3.78e-10

Catalytic domain of the Protein Tyrosine Kinase, Ephrin Receptor A2; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. The EphA2 receptor is overexpressed in tumor cells and tumor blood vessels in a variety of cancers including breast, prostate, lung, and colon. As a result, it is an attractive target for drug design since its inhibition could affect several aspects of tumor progression. EphRs comprise the largest subfamily of receptor PTKs (RTKs). Class EphA receptors bind GPI-anchored ephrin-A ligands. There are ten vertebrate EphA receptors (EphA1-10), which display promiscuous interactions with six ephrin-A ligands. EphRs contain an ephrin binding domain and two fibronectin repeats extracellularly, a transmembrane segment, and a cytoplasmic tyr kinase domain. Binding of the ephrin ligand to EphR requires cell-cell contact since both are anchored to the plasma membrane. The resulting downstream signals occur bidirectionally in both EphR-expressing cells (forward signaling) and ephrin-expressing cells (reverse signaling). Ephrin/EphR interaction mainly results in cell-cell repulsion or adhesion, making it important in neural development and plasticity, cell morphogenesis, cell-fate determination, embryonic development, tissue patterning, and angiogenesis. The EphA2 subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, and phosphoinositide 3-kinase (PI3K).


Pssm-ID: 133194 [Multi-domain]  Cd Length: 268  Bit Score: 65.00  E-value: 3.78e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 7976 QPVEISQQSVydrydileeIGTGAFGVVHRCRERSTGNIFAAKFIPV-----SHSVEKDLIRrEIDIMNQLHHQKLINLH 8050
Cdd:cd05063     3 HPSHITKQKV---------IGAGEFGEVFRGILKMPGRKEVAVAIKTlkpgyTEKQRQDFLS-EASIMGQFSHHNIIRLE 72
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 8051 DAFEDDDEMILILEFLSGGELFERITAEGYVMTEAEVINYMRQICEGIRHMHEQNIIHLDIKPENIMcqTRSSTNVKLID 8130
Cdd:cd05063    73 GVVTKFKPAMIITEYMENGALDKYLRDHDGEFSSYQLVGMLRGIAAGMKYLSDMNYVHRDLAARNIL--VNSNLECKVSD 150
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 281359561 8131 FGLATRL-DPNEVVKITTGTA---EFAAPEIVNREPVGFYTDMWATGVLSYVLLS-GLSPF 8186
Cdd:cd05063   151 FGLSRVLeDDPEGTYTTSGGKipiRWTAPEAIAYRKFTSASDVWSFGIVMWEVMSfGERPY 211
Ig_C5_MyBP-C cd05894
C5 immunoglobulin (Ig) domain of cardiac myosin binding protein C (MyBP-C); The members here ...
6866-6946 3.80e-10

C5 immunoglobulin (Ig) domain of cardiac myosin binding protein C (MyBP-C); The members here are composed of the C5 immunoglobulin (Ig) domain of cardiac myosin binding protein C (MyBP-C). MyBP-C consists of repeated domains, Ig and fibronectin type 3, and various linkers. Three isoforms of MYBP-C exist: slow-skeletal (ssMyBP-C), fast-skeletal (fsMyBP-C), and cardiac (cMyBP-C). cMYBP-C has insertions between and inside domains and an additional cardiac-specific Ig domain at the N-terminus. For cMYBP_C an interaction has been demonstrated between this C5 domain and the Ig C8 domain.


Pssm-ID: 409475  Cd Length: 86  Bit Score: 59.85  E-value: 3.80e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 6866 MTVIAGDEFRITVPYHASPRPTASWSLNGLEVIPGE-RIKFDSNDYASMYYNKSAKRDETGSYTITLTNNKGSDTASCHV 6944
Cdd:cd05894     5 IVVVAGNKLRLDVPISGEPAPTVTWSRGDKAFTATEgRVRVESYKDLSSFVIEGAEREDEGVYTITVTNPVGEDHASLFV 84

                  ..
gi 281359561 6945 TV 6946
Cdd:cd05894    85 KV 86
PHA03207 PHA03207
serine/threonine kinase US3; Provisional
7988-8188 4.07e-10

serine/threonine kinase US3; Provisional


Pssm-ID: 165473 [Multi-domain]  Cd Length: 392  Bit Score: 66.41  E-value: 4.07e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 7988 RYDILEEIGTGAFGVVHRCRERstGNIFAAKFIPVSHSVEKDLiRREIDIMNQLHHQKLINLHDAFEDDDEMILILEFLS 8067
Cdd:PHA03207   93 QYNILSSLTPGSEGEVFVCTKH--GDEQRKKVIVKAVTGGKTP-GREIDILKTISHRAIINLIHAYRWKSTVCMVMPKYK 169
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 8068 GgELFERITAEGYVMTEaEVINYMRQICEGIRHMHEQNIIHLDIKPENIMCQtrSSTNVKLIDFGLATRLDPNEVVKIT- 8146
Cdd:PHA03207  170 C-DLFTYVDRSGPLPLE-QAITIQRRLLEALAYLHGRGIIHRDVKTENIFLD--EPENAVLGDFGAACKLDAHPDTPQCy 245
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....
gi 281359561 8147 --TGTAEFAAPEIVNREPVGFYTDMWATGVLSYVLLSGLSPFAG 8188
Cdd:PHA03207  246 gwSGTLETNSPELLALDPYCAKTDIWSAGLVLFEMSVKNVTLFG 289
IgI_M-protein_C cd05891
C-terminal immunoglobulin (Ig)-like domain of M-protein; member of the I-set of Ig superfamily ...
132-202 4.32e-10

C-terminal immunoglobulin (Ig)-like domain of M-protein; member of the I-set of Ig superfamily (IgSF) domains; The members here are composed of the C-terminal immunoglobulin (Ig)-like domain of M-protein (also known as myomesin-2). M-protein is a structural protein localized to the M-band, a transverse structure in the center of the sarcomere, and is a candidate for M-band bridges. M-protein is modular consisting mainly of repetitive IG-like and fibronectin type III (FnIII) domains and has a muscle-type specific expression pattern. M-protein is present in fast fibers.


Pssm-ID: 143299  Cd Length: 92  Bit Score: 59.92  E-value: 4.32e-10
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 281359561  132 DGKRLLFECRVNADPIPAIIWFHNGAAVKESERHKITVDKdvhSYFATLEILNVTVEDAGKYKVNAKNELG 202
Cdd:cd05891    15 EGKTLNLTCTVFGNPDPEVIWFKNDQDIELSEHYSVKLEQ---GKYASLTIKGVTSEDSGKYSINVKNKYG 82
fn3 pfam00041
Fibronectin type III domain;
7445-7529 4.33e-10

Fibronectin type III domain;


Pssm-ID: 394996 [Multi-domain]  Cd Length: 85  Bit Score: 59.74  E-value: 4.33e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561  7445 SAPTGPmGISYINKNSCMLNWRPPSYDGGlKVSHYVIERKDVSSP---HWITVSSTckDTAFNVQGLIENQEYIFRVMAV 7521
Cdd:pfam00041    1 SAPSNL-TVTDVTSTSLTVSWTPPPDGNG-PITGYEVEYRPKNSGepwNEITVPGT--TTSVTLTGLKPGTEYEVRVQAV 76

                   ....*...
gi 281359561  7522 NENGMGPP 7529
Cdd:pfam00041   77 NGGGEGPP 84
IG_like smart00410
Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.
7758-7833 4.35e-10

Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.


Pssm-ID: 214653 [Multi-domain]  Cd Length: 85  Bit Score: 59.83  E-value: 4.35e-10
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 281359561   7758 GENVVIKIPFTGFPKPRIHWVRDG-ENIESGGHYTVEVKERHAVLIIRDGSHLDSGPYRITAENELGSDTAIIQVQI 7833
Cdd:smart00410    9 GESVTLSCEASGSPPPEVTWYKQGgKLLAESGRFSVSRSGSTSTLTISNVTPEDSGTYTCAATNSSGSASSGTTLTV 85
Ig_C5_MyBP-C cd05894
C5 immunoglobulin (Ig) domain of cardiac myosin binding protein C (MyBP-C); The members here ...
5286-5366 4.39e-10

C5 immunoglobulin (Ig) domain of cardiac myosin binding protein C (MyBP-C); The members here are composed of the C5 immunoglobulin (Ig) domain of cardiac myosin binding protein C (MyBP-C). MyBP-C consists of repeated domains, Ig and fibronectin type 3, and various linkers. Three isoforms of MYBP-C exist: slow-skeletal (ssMyBP-C), fast-skeletal (fsMyBP-C), and cardiac (cMyBP-C). cMYBP-C has insertions between and inside domains and an additional cardiac-specific Ig domain at the N-terminus. For cMYBP_C an interaction has been demonstrated between this C5 domain and the Ig C8 domain.


Pssm-ID: 409475  Cd Length: 86  Bit Score: 59.85  E-value: 4.39e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 5286 IKIKAGNVFEFDVPVTGEPLPSKDWTHEGNMIINTD-RVKISNFDDRTKIRILDAKRSDTGVYTLTARNINGTDRHNVKV 5364
Cdd:cd05894     5 IVVVAGNKLRLDVPISGEPAPTVTWSRGDKAFTATEgRVRVESYKDLSSFVIEGAEREDEGVYTITVTNPVGEDHASLFV 84

                  ..
gi 281359561 5365 TI 5366
Cdd:cd05894    85 KV 86
fn3 pfam00041
Fibronectin type III domain;
7051-7136 4.42e-10

Fibronectin type III domain;


Pssm-ID: 394996 [Multi-domain]  Cd Length: 85  Bit Score: 59.74  E-value: 4.42e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561  7051 DEPGQPKVIDWDSGNVTLIWTRPlSDGGSRIQGYQIEYRDILNDSSWNayDYIIKDTK--YQLYNLINGSEYEFRIKAKN 7128
Cdd:pfam00041    1 SAPSNLTVTDVTSTSLTVSWTPP-PDGNGPITGYEVEYRPKNSGEPWN--EITVPGTTtsVTLTGLKPGTEYEVRVQAVN 77

                   ....*...
gi 281359561  7129 AAGLSKPS 7136
Cdd:pfam00041   78 GGGEGPPS 85
PK_TRB2 cd14022
Pseudokinase domain of Tribbles Homolog 2; The pseudokinase domain shows similarity to protein ...
8082-8244 4.45e-10

Pseudokinase domain of Tribbles Homolog 2; The pseudokinase domain shows similarity to protein kinases but lacks crucial residues for catalytic activity. TRB2 binds and negatively regulates the mitogen activated protein kinase (MAPK) kinases, MKK7 and MEK1, which are activators of the MAPKs, ERK and JNK. It controls the activation of inflammatory monocytes, which is essential in innate immune responses and the pathogenesis of inflammatory diseases such as atherosclerosis. TRB2 expression is down-regulated in human acute myeloid leukaemia (AML), which may lead to enhanced cell survival and pathogenesis of the disease. TRB2 is one of three Tribbles Homolog (TRB) proteins present in vertebrates that are encoded by three separate genes. TRB proteins interact with many proteins involved in signalling pathways. They play scaffold-like regulatory functions and affect many cellular processes such as mitosis, apoptosis, and gene expression. The TRB2 subfamily is part of a larger superfamily that includes the catalytic domains of serine/threonine kinases, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270924 [Multi-domain]  Cd Length: 242  Bit Score: 64.29  E-value: 4.45e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 8082 MTEAEVINYMRQICEGIRHMHEQNIIHLDIKPENIMCQTRSSTNVKLIDFGLATRLD-PNEVVKITTGTAEFAAPEIVNR 8160
Cdd:cd14022    81 LREEEAARLFYQIASAVAHCHDGGLVLRDLKLRKFVFKDEERTRVKLESLEDAYILRgHDDSLSDKHGCPAYVSPEILNT 160
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 8161 EpvGFYT----DMWATGVLSYVLLSGLSPFAGDNDVQTLKNVKACDWDFDvesfKYISEEAKDFIRKLLVRNKEKRMTAH 8236
Cdd:cd14022   161 S--GSYSgkaaDVWSLGVMLYTMLVGRYPFHDIEPSSLFSKIRRGQFNIP----ETLSPKAKCLIRSILRREPSERLTSQ 234

                  ....*...
gi 281359561 8237 ECLLHPWL 8244
Cdd:cd14022   235 EILDHPWF 242
IgI_3_Robo cd05725
Third immunoglobulin (Ig)-like domain in Robo (roundabout) receptors; member of the I-set of ...
7257-7344 4.53e-10

Third immunoglobulin (Ig)-like domain in Robo (roundabout) receptors; member of the I-set of Ig superfamily (IgSF) domains; The members here are composed of the third immunoglobulin (Ig)-like domain in Robo (roundabout) receptors. Robo receptors play a role in the development of the central nervous system (CNS), and are receptors of Slit protein. Slit is a repellant secreted by the neural cells in the midline. Slit acts through Robo to prevent most neurons from crossing the midline from either side. Three mammalian Robo homologs (Robo1, Robo2, Robo3), and three mammalian Slit homologs (Slit-1,Slit-2, Slit-3), have been identified. Commissural axons, which cross the midline, express low levels of Robo; longitudinal axons, which avoid the midline, express high levels of Robo. Robo1, Robo2, and Robo3 are expressed by commissural neurons in the vertebrate spinal cord and Slit-1, Slit-2, and Slit-3 are expressed at the ventral midline. Robo-3 is a divergent member of the Robo family which instead of being a positive regulator of Slit responsiveness, antagonizes Slit responsiveness in precrossing axons. The Slit-Robo interaction is mediated by the second leucine-rich repeat (LRR) domain of Slit and the two N-terminal Ig domains of Robo, Ig1 and Ig2. The primary Robo binding site for Slit2 has been shown by surface plasmon resonance experiments and mutational analysis to be the Ig1 domain, while the Ig2 domain has been proposed to harbor a weak secondary binding site. This group belongs to the I-set of IgSF domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand, but lack a C" strand.


Pssm-ID: 409390 [Multi-domain]  Cd Length: 83  Bit Score: 59.72  E-value: 4.53e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 7257 ITRLQDKVAPFGKDYTLQCAASGKPSPTARWLRNGKEIQMNGGRMTCDSKdgvfrLHISNVQTGDDGDYTCEAMNSLGFV 7336
Cdd:cd05725     1 VKRPQNQVVLVDDSAEFQCEVGGDPVPTVRWRKEDGELPKGRYEILDDHS-----LKIRKVTAGDMGSYTCVAENMVGKI 75

                  ....*...
gi 281359561 7337 NTSGYLKI 7344
Cdd:cd05725    76 EASATLTV 83
fn3 pfam00041
Fibronectin type III domain;
4286-4375 4.96e-10

Fibronectin type III domain;


Pssm-ID: 394996 [Multi-domain]  Cd Length: 85  Bit Score: 59.74  E-value: 4.96e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561  4286 GKPGTPEAVDWDKDHVDLVWRPPiNDGGSPITGYVVEKREKGTDKWIKgtEITIPclGEECKATVPTLNENCEYEFRVKA 4365
Cdd:pfam00041    1 SAPSNLTVTDVTSTSLTVSWTPP-PDGNGPITGYEVEYRPKNSGEPWN--EITVP--GTTTSVTLTGLKPGTEYEVRVQA 75
                           90
                   ....*....|
gi 281359561  4366 INAAGPGEPS 4375
Cdd:pfam00041   76 VNGGGEGPPS 85
PTKc_Zap-70 cd05115
Catalytic domain of the Protein Tyrosine Kinase, Zeta-chain-associated protein of 70kDa; PTKs ...
7994-8186 5.01e-10

Catalytic domain of the Protein Tyrosine Kinase, Zeta-chain-associated protein of 70kDa; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Zap-70 is a cytoplasmic (or nonreceptor) PTK containing two Src homology 2 (SH2) domains N-terminal to the catalytic tyr kinase domain. Zap-70 is primarily expressed in T-cells and NK cells, and is a crucial component in T-cell receptor (TCR) signaling. Zap-70 binds the phosphorylated ITAM (immunoreceptor tyr activation motif) sequences of the activated TCR zeta-chain through its SH2 domains, leading to its phosphorylation and activation. It then phosphorylates target proteins, which propagate the signals to downstream pathways. Zap-70 is hardly detected in normal peripheral B-cells, but is present in some B-cell malignancies. It is used as a diagnostic marker for chronic lymphocytic leukemia (CLL) as it is associated with the more aggressive subtype of the disease. The Zap-70 subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270686 [Multi-domain]  Cd Length: 269  Bit Score: 64.58  E-value: 5.01e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 7994 EIGTGAFGVVHR--CRERSTGNIFAAKFIPV-SHSVEKDLIRREIDIMNQLHHQKLINLHDAFEDDDEMiLILEFLSGGE 8070
Cdd:cd05115    11 ELGSGNFGCVKKgvYKMRKKQIDVAIKVLKQgNEKAVRDEMMREAQIMHQLDNPYIVRMIGVCEAEALM-LVMEMASGGP 89
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 8071 LFERITAEGYVMTEAEVINYMRQICEGIRHMHEQNIIHLDIKPENIMCQTRSSTnvKLIDFGLATRL--DPNEVVKITTG 8148
Cdd:cd05115    90 LNKFLSGKKDEITVSNVVELMHQVSMGMKYLEEKNFVHRDLAARNVLLVNQHYA--KISDFGLSKALgaDDSYYKARSAG 167
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|.
gi 281359561 8149 T--AEFAAPEIVNREPVGFYTDMWATGVLSYVLLS-GLSPF 8186
Cdd:cd05115   168 KwpLKWYAPECINFRKFSSRSDVWSYGVTMWEAFSyGQKPY 208
IG_like smart00410
Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.
133-210 5.04e-10

Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.


Pssm-ID: 214653 [Multi-domain]  Cd Length: 85  Bit Score: 59.83  E-value: 5.04e-10
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 281359561    133 GKRLLFECRVNADPIPAIIWFHNGA-AVKESERHKITVDKDVHsyfaTLEILNVTVEDAGKYKVNAKNELGESNATISL 210
Cdd:smart00410    9 GESVTLSCEASGSPPPEVTWYKQGGkLLAESGRFSVSRSGSTS----TLTISNVTPEDSGTYTCAATNSSGSASSGTTL 83
IgI_Titin_like cd05747
Immunoglobulin (Ig)-like domain of human titin C terminus and similar proteins; member of the ...
117-210 5.10e-10

Immunoglobulin (Ig)-like domain of human titin C terminus and similar proteins; member of the I-set of Ig superfamily (IgSF) domains; The members here are composed of the fifth immunoglobulin (Ig)-like domain from the C-terminus of human titin x and similar proteins. Titin (also called connectin) is a fibrous sarcomeric protein specifically found in vertebrate striated muscle. Titin is gigantic; depending on isoform composition it ranges from 2970 to 3700 kDa, and is of a length that spans half a sarcomere. Titin largely consists of multiple repeats of Ig-like and fibronectin type 3 (FN-III)-like domains. Titin connects the ends of myosin thick filaments to Z disks and extends along the thick filament to the H zone and appears to function similar to an elastic band, keeping the myosin filaments centered in the sarcomere during muscle contraction or stretching. This group belongs to the I-set of IgSF domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand, but lack a C" strand.


Pssm-ID: 143224 [Multi-domain]  Cd Length: 92  Bit Score: 60.06  E-value: 5.10e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561  117 FAPTFAKKPAIRQEEDGKRLLFECRVNADPIPAIIWFHNGAAVKESERHKITVDKdvhsYFATLEILNVTVEDAGKYKVN 196
Cdd:cd05747     2 LPATILTKPRSLTVSEGESARFSCDVDGEPAPTVTWMREGQIIVSSQRHQITSTE----YKSTFEISKVQMSDEGNYTVV 77
                          90
                  ....*....|....
gi 281359561  197 AKNELGESNATISL 210
Cdd:cd05747    78 VENSEGKQEAQFTL 91
IgI_Myotilin_C_like cd05744
Immunoglobulin (Ig)-like domain of myotilin, palladin, and myopalladin; member of the I-set of ...
545-636 5.18e-10

Immunoglobulin (Ig)-like domain of myotilin, palladin, and myopalladin; member of the I-set of Ig superfamily (IgSF) domains; The members here are composed of the immunoglobulin (Ig)-like domain in myotilin, palladin, and myopalladin. Myotilin, palladin, and myopalladin function as scaffolds that regulate actin organization. Myotilin and myopalladin are most abundant in skeletal and cardiac muscle; palladin is ubiquitously expressed in the organs of developing vertebrates and plays a key role in cellular morphogenesis. The three family members each interact with specific molecular partners with all three binding to alpha-actinin; In addition, palladin also binds to vasodilator-stimulated phosphoprotein (VASP) and ezrin, myotilin binds to filamin and actin, and myopalladin also binds to nebulin and cardiac ankyrin repeat protein (CARP). This group belongs to the I-set of IgSF domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand, but lack a C" strand.


Pssm-ID: 409405 [Multi-domain]  Cd Length: 91  Bit Score: 59.82  E-value: 5.18e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561  545 FIEKPRIVSENNGKLVIMECKVKADPKPDVIWFRNGEVIKESNKIKTFIEQRGDQyyiKLELLDPQLEDSGLYKCNIKNT 624
Cdd:cd05744     3 FLQAPGDLEVQEGRLCRFDCKVSGLPTPDLFWQLNGKPVRPDSAHKMLVRENGRH---SLIIEPVTKRDAGIYTCIARNR 79
                          90
                  ....*....|..
gi 281359561  625 LGELNANLTLNI 636
Cdd:cd05744    80 AGENSFNAELVV 91
IgI_3_Robo cd05725
Third immunoglobulin (Ig)-like domain in Robo (roundabout) receptors; member of the I-set of ...
8636-8721 5.35e-10

Third immunoglobulin (Ig)-like domain in Robo (roundabout) receptors; member of the I-set of Ig superfamily (IgSF) domains; The members here are composed of the third immunoglobulin (Ig)-like domain in Robo (roundabout) receptors. Robo receptors play a role in the development of the central nervous system (CNS), and are receptors of Slit protein. Slit is a repellant secreted by the neural cells in the midline. Slit acts through Robo to prevent most neurons from crossing the midline from either side. Three mammalian Robo homologs (Robo1, Robo2, Robo3), and three mammalian Slit homologs (Slit-1,Slit-2, Slit-3), have been identified. Commissural axons, which cross the midline, express low levels of Robo; longitudinal axons, which avoid the midline, express high levels of Robo. Robo1, Robo2, and Robo3 are expressed by commissural neurons in the vertebrate spinal cord and Slit-1, Slit-2, and Slit-3 are expressed at the ventral midline. Robo-3 is a divergent member of the Robo family which instead of being a positive regulator of Slit responsiveness, antagonizes Slit responsiveness in precrossing axons. The Slit-Robo interaction is mediated by the second leucine-rich repeat (LRR) domain of Slit and the two N-terminal Ig domains of Robo, Ig1 and Ig2. The primary Robo binding site for Slit2 has been shown by surface plasmon resonance experiments and mutational analysis to be the Ig1 domain, while the Ig2 domain has been proposed to harbor a weak secondary binding site. This group belongs to the I-set of IgSF domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand, but lack a C" strand.


Pssm-ID: 409390 [Multi-domain]  Cd Length: 83  Bit Score: 59.33  E-value: 5.35e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 8636 KPLHDLTIHDGEQLILTCYVKGDPEPQISWSKNGKSL--SSSDILDLRykngiaTLTINEVFPEDEGVITCTATNSVGAV 8713
Cdd:cd05725     2 KRPQNQVVLVDDSAEFQCEVGGDPVPTVRWRKEDGELpkGRYEILDDH------SLKIRKVTAGDMGSYTCVAENMVGKI 75

                  ....*...
gi 281359561 8714 ETKCKLTI 8721
Cdd:cd05725    76 EASATLTV 83
Ig_3 pfam13927
Immunoglobulin domain; This family contains immunoglobulin-like domains.
8312-8388 5.59e-10

Immunoglobulin domain; This family contains immunoglobulin-like domains.


Pssm-ID: 464046 [Multi-domain]  Cd Length: 78  Bit Score: 59.12  E-value: 5.59e-10
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 281359561  8312 PRFVIRPSSQFCYEGQSVKFYCRCIAIATPTLTWSHNNIELRQSVKFMKRYVGDDYYFIINRVKLDDRGEYIIRAEN 8388
Cdd:pfam13927    2 PVITVSPSSVTVREGETVTLTCEATGSPPPTITWYKNGEPISSGSTRSRSLSGSNSTLTISNVTRSDAGTYTCVASN 78
STKc_TGFbR_I cd14056
Catalytic domain of the Serine/Threonine Kinases, Transforming Growth Factor beta family Type ...
7993-8159 5.89e-10

Catalytic domain of the Serine/Threonine Kinases, Transforming Growth Factor beta family Type I Receptors; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily is composed of type I receptors for the TGFbeta family of secreted signaling molecules including TGFbeta, bone morphogenetic proteins, activins, growth and differentiation factors, and anti-Mullerian hormone, among others. These receptors contain an extracellular domain that binds ligands, a single transmembrane (TM) region, and a cytoplasmic catalytic kinase domain. Type I receptors are low-affinity receptors that bind ligands only after they are recruited by the ligand/type II high-affinity receptor complex. Following activation through trans-phosphorylation by type II receptors, they start intracellular signaling to the nucleus by phosphorylating SMAD proteins. Type I receptors contain an additional domain located between the TM and kinase domains called the GS domain, which contains the activating phosphorylation site and confers preference for specific SMAD proteins. They are inhibited by the immunophilin FKBP12, which is thought to control leaky signaling caused by receptor oligomerization in the absence of ligand. The TGFbR-I subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270958 [Multi-domain]  Cd Length: 287  Bit Score: 64.60  E-value: 5.89e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 7993 EEIGTGAFGVVHRCRERstGNIFAAKfipVSHSVEKDLIRREIDI--MNQLHHQKLINL--HDAFEDD--DEMILILEFL 8066
Cdd:cd14056     1 KTIGKGRYGEVWLGKYR--GEKVAVK---IFSSRDEDSWFRETEIyqTVMLRHENILGFiaADIKSTGswTQLWLITEYH 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 8067 SGGELFERITAEgyVMTEAEVINYMRQICEGIRHMHEQ--------NIIHLDIKPENIMcqtrsstnVK------LIDFG 8132
Cdd:cd14056    76 EHGSLYDYLQRN--TLDTEEALRLAYSAASGLAHLHTEivgtqgkpAIAHRDLKSKNIL--------VKrdgtccIADLG 145
                         170       180       190
                  ....*....|....*....|....*....|....*.
gi 281359561 8133 LA---------TRLDPNEVVkittGTAEFAAPEIVN 8159
Cdd:cd14056   146 LAvrydsdtntIDIPPNPRV----GTKRYMAPEVLD 177
IgI_1_MuSK cd20970
agrin-responsive first immunoglobulin-like domains (Ig1) of the MuSK ectodomain; a member of ...
8637-8721 7.08e-10

agrin-responsive first immunoglobulin-like domains (Ig1) of the MuSK ectodomain; a member of the I-set of IgSF domains; The members here are composed of the first immunoglobulin-like domains (Ig1) of the Muscle-specific kinase (MuSK). MuSK is a receptor tyrosine kinase specifically expressed in skeletal muscle, where it plays a central role in the formation and maintenance of the neuromuscular junction (NMJ). MuSK is activated by agrin, a neuron-derived heparan sulfate proteoglycan. The activation of MUSK in myotubes regulates the formation of NMJs through the regulation of different processes including the specific expression of genes in subsynaptic nuclei, the reorganization of the actin cytoskeleton and the clustering of the acetylcholine receptors (AChR) in the postsynaptic membrane. The Ig superfamily (IgSF) is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. Unlike the V-set, one of the distinctive features of I-set domains is the lack of a C" strand. The structure of the MuSK lacks this strand and thus it belongs to the I-set of the IgSF. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors, the hemolymph protein hemolin, the muscle proteins titin, telokin, and twitchin, the neuronal adhesion molecule axonin-1, and the signaling molecule semaphorin 4D that is involved in axonal guidance, immune function and angiogenesis.


Pssm-ID: 409562 [Multi-domain]  Cd Length: 92  Bit Score: 59.44  E-value: 7.08e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 8637 PLHDLTIHDGEQLILTCYVKGDPEPQISWSKNGKSLSSSDIlDLRYKNGIATLTINEVFPEDEGVITCTATNSV-GAVET 8715
Cdd:cd20970     8 PSFTVTAREGENATFMCRAEGSPEPEISWTRNGNLIIEFNT-RYIVRENGTTLTIRNIRRSDMGIYLCIASNGVpGSVEK 86

                  ....*.
gi 281359561 8716 KCKLTI 8721
Cdd:cd20970    87 RITLQV 92
I-set pfam07679
Immunoglobulin I-set domain;
335-425 7.81e-10

Immunoglobulin I-set domain;


Pssm-ID: 400151 [Multi-domain]  Cd Length: 90  Bit Score: 59.19  E-value: 7.81e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561   335 PRFPKKP--TIRQEEDLLIMECVLEAHPVPDIVWYCSEKEICNNQRTKMTrkaitKDSYILTLEIQNPTKEDGGNYRCNA 412
Cdd:pfam07679    1 PKFTQKPkdVEVQEGESARFTCTVTGTPDPEVSWFKDGQPLRSSDRFKVT-----YEGGTYTLTISNVQPDDSGKYTCVA 75
                           90
                   ....*....|...
gi 281359561   413 INMYGESNANIAL 425
Cdd:pfam07679   76 TNSAGEAEASAEL 88
Ig_3 pfam13927
Immunoglobulin domain; This family contains immunoglobulin-like domains.
548-623 7.87e-10

Immunoglobulin domain; This family contains immunoglobulin-like domains.


Pssm-ID: 464046 [Multi-domain]  Cd Length: 78  Bit Score: 58.73  E-value: 7.87e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561   548 KPRIVSENN------GKLVIMECKVKADPKPDVIWFRNGEVIKESNKIKTFIeqrgDQYYIKLELLDPQLEDSGLYKCNI 621
Cdd:pfam13927    1 KPVITVSPSsvtvreGETVTLTCEATGSPPPTITWYKNGEPISSGSTRSRSL----SGSNSTLTISNVTRSDAGTYTCVA 76

                   ..
gi 281359561   622 KN 623
Cdd:pfam13927   77 SN 78
Bud32 COG3642
tRNA A-37 threonylcarbamoyl transferase component Bud32 [Translation, ribosomal structure and ...
8032-8141 8.08e-10

tRNA A-37 threonylcarbamoyl transferase component Bud32 [Translation, ribosomal structure and biogenesis]; tRNA A-37 threonylcarbamoyl transferase component Bud32 is part of the Pathway/BioSystem: tRNA modification


Pssm-ID: 442859 [Multi-domain]  Cd Length: 159  Bit Score: 61.51  E-value: 8.08e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 8032 RREIDIMNQLHhQKLIN---LHDAfeDDDEMILILEFLSGGELFEritaegYVMTEAEVINYMRQICEGIRHMHEQNIIH 8108
Cdd:COG3642     4 RREARLLRELR-EAGVPvpkVLDV--DPDDADLVMEYIEGETLAD------LLEEGELPPELLRELGRLLARLHRAGIVH 74
                          90       100       110
                  ....*....|....*....|....*....|...
gi 281359561 8109 LDIKPENIMcqtRSSTNVKLIDFGLATRLDPNE 8141
Cdd:COG3642    75 GDLTTSNIL---VDDGGVYLIDFGLARYSDPLE 104
IG_like smart00410
Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.
8455-8525 8.13e-10

Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.


Pssm-ID: 214653 [Multi-domain]  Cd Length: 85  Bit Score: 59.06  E-value: 8.13e-10
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 281359561   8455 KLLCCLSGKPVPNVRWYKDGRELSKYE--YAMTHSDGVVTMEIIDCKPSDSGKYSCKATNCHGTDETDCVVIV 8525
Cdd:smart00410   13 TLSCEASGSPPPEVTWYKQGGKLLAESgrFSVSRSGSTSTLTISNVTPEDSGTYTCAATNSSGSASSGTTLTV 85
PTZ00036 PTZ00036
glycogen synthase kinase; Provisional
7989-8244 9.17e-10

glycogen synthase kinase; Provisional


Pssm-ID: 173333 [Multi-domain]  Cd Length: 440  Bit Score: 65.44  E-value: 9.17e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 7989 YDILEEIGTGAFGVVHRCRERSTGNIFAAKfipvshSVEKD--LIRREIDIMNQLHHQKLINLHD-----AFEDDDEMI- 8060
Cdd:PTZ00036   68 YKLGNIIGNGSFGVVYEAICIDTSEKVAIK------KVLQDpqYKNRELLIMKNLNHINIIFLKDyyyteCFKKNEKNIf 141
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 8061 --LILEFL--SGGELFERITAEGYVMTEAEVINYMRQICEGIRHMHEQNIIHLDIKPENIMCQTRSSTnVKLIDFGLATR 8136
Cdd:PTZ00036  142 lnVVMEFIpqTVHKYMKHYARNNHALPLFLVKLYSYQLCRALAYIHSKFICHRDLKPQNLLIDPNTHT-LKLCDFGSAKN 220
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 8137 LDPNEVVKITTGTAEFAAPEI-VNREPVGFYTDMWATGVLSYVLLSGLSPFAGDNDVQTL-----------------KNV 8198
Cdd:PTZ00036  221 LLAGQRSVSYICSRFYRAPELmLGATNYTTHIDLWSLGCIIAEMILGYPIFSGQSSVDQLvriiqvlgtptedqlkeMNP 300
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....
gi 281359561 8199 KACDWDF-DVES------F-KYISEEAKDFIRKLLVRNKEKRMTAHECLLHPWL 8244
Cdd:PTZ00036  301 NYADIKFpDVKPkdlkkvFpKGTPDDAINFISQFLKYEPLKRLNPIEALADPFF 354
IgI_2_Titin_Z1z2-like cd20972
Second Ig-like domain of the giant muscle protein titin Z1z2 in the sarcomeric Z-disk, and ...
118-210 9.65e-10

Second Ig-like domain of the giant muscle protein titin Z1z2 in the sarcomeric Z-disk, and similar domains; a member of the I-set of IgSF domains; The members here are composed of the second immunoglobulin (Ig)-like domain of the giant muscle protein titin Z1z2 in the sarcomeric Z-disk and similar proteins. Titin is a key component in the assembly and functioning of vertebrate striated muscles. By providing connections at the level of individual microfilaments, it contributes to the fine balance of forces between the two halves of the sarcomere. The Ig superfamily (IgSF) is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. Unlike the V-set, one of the distinctive features of I-set domains is the lack of a C" strand. The structure of the titin Z1z2 lacks this strand and thus it belongs to the I-set of the IgSF. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors, the hemolymph protein hemolin, the muscle proteins titin, telokin, and twitchin, the neuronal adhesion molecule axonin-1, and the signaling molecule semaphorin 4D that is involved in axonal guidance, immune function and angiogenesis.


Pssm-ID: 409564 [Multi-domain]  Cd Length: 91  Bit Score: 59.13  E-value: 9.65e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561  118 APTFAKKPAIRQEEDGKRLLFECRVNADPIPAIIWFHNGAAVKESERHKITVDKDVHSyfatLEILNVTVEDAGKYKVNA 197
Cdd:cd20972     1 PPQFIQKLRSQEVAEGSKVRLECRVTGNPTPVVRWFCEGKELQNSPDIQIHQEGDLHS----LIIAEAFEEDTGRYSCLA 76
                          90
                  ....*....|...
gi 281359561  198 KNELGESNATISL 210
Cdd:cd20972    77 TNSVGSDTTSAEI 89
fn3 pfam00041
Fibronectin type III domain;
3695-3780 1.03e-09

Fibronectin type III domain;


Pssm-ID: 394996 [Multi-domain]  Cd Length: 85  Bit Score: 58.58  E-value: 1.03e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561  3695 DRPGKPEPTNWDKDFVDLAWDPPKnDGGAPIQKYVIQMRDKSGRAWVDSATVPGDKCNGTVTGVEEGHEYEFRIVAVNKA 3774
Cdd:pfam00041    1 SAPSNLTVTDVTSTSLTVSWTPPP-DGNGPITGYEVEYRPKNSGEPWNEITVPGTTTSVTLTGLKPGTEYEVRVQAVNGG 79

                   ....*.
gi 281359561  3775 GPSDPS 3780
Cdd:pfam00041   80 GEGPPS 85
COG4733 COG4733
Phage-related protein, tail protein J [Mobilome: prophages, transposons];
6887-7234 1.03e-09

Phage-related protein, tail protein J [Mobilome: prophages, transposons];


Pssm-ID: 443767 [Multi-domain]  Cd Length: 978  Bit Score: 66.12  E-value: 1.03e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 6887 TASWS--LNGLEVIPGERIKFDSNDYASMYYnkSAKRDETGSYTITLTNNKGSDTASCHVTVVDrplpPQGPLNAYDIT- 6963
Cdd:COG4733   384 TVTFSvgLDGLVATPGDVIAVADDVLAGRRI--GGRVSSVDGRVVTLDRPVTMEAGDRYLRVRL----PDGTSVARTVQs 457
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 6964 --PDTCTLAWKTPLDdggsPITNYVvekldnsgsWVKISSFVRNTHYDVMGLEPHYKYNFRVRA----ENQYGLSD---- 7033
Cdd:COG4733   458 vaGRTLTVSTAYSET----PEAGAV---------WAFGPDELETQLFRVVSIEENEDGTYTITAvqhaPEKYAAIDagaf 524
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 7034 ----PLDIIEPIVAKHQFTVpDEPGQPKVIdwdsgnVTLIWTRPLSDGGsriqgYQIEYRDilNDSSWNaYDYIIKDTKY 7109
Cdd:COG4733   525 ddvpPQWPPVNVTTSESLSV-VAQGTAVTT------LTVSWDAPAGAVA-----YEVEWRR--DDGNWV-SVPRTSGTSF 589
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 7110 QLYNLINGsEYEFRIKAKNAAGLSKPSSPSLRFKLKGKFTVPSPPGAPQVTRvGKNYVDLKWEKPLrdgGSRITGYIIER 7189
Cdd:COG4733   590 EVPGIYAG-DYEVRVRAINALGVSSAWAASSETTVTGKTAPPPAPTGLTATG-GLGGITLSWSFPV---DADTLRTEIRY 664
                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....*
gi 281359561 7190 RDIGGAVWVKCNDYNVLDTEYTVMNLIEMGDYEFRVFAVNSAGRS 7234
Cdd:COG4733   665 STTGDWASATVAQALYPGNTYTLAGLKAGQTYYYRARAVDRSGNV 709
ig pfam00047
Immunoglobulin domain; Members of the immunoglobulin superfamily are found in hundreds of ...
8636-8716 1.07e-09

Immunoglobulin domain; Members of the immunoglobulin superfamily are found in hundreds of proteins of different functions. Examples include antibodies, the giant muscle kinase titin and receptor tyrosine kinases. Immunoglobulin-like domains may be involved in protein-protein and protein-ligand interactions.


Pssm-ID: 395002  Cd Length: 86  Bit Score: 58.75  E-value: 1.07e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561  8636 KPLHDLTIHDGEQLILTCYVK-GDPEPQISWSKNGKSL-SSSDILDLRYKNGIATLTINEVFPEDEGVITCTATNSVGAV 8713
Cdd:pfam00047    1 SAPPTVTVLEGDSATLTCSAStGSPGPDVTWSKEGGTLiESLKVKHDNGRTTQSSLLISNVTKEDAGTYTCVVNNPGGSA 80

                   ...
gi 281359561  8714 ETK 8716
Cdd:pfam00047   81 TLS 83
IgI_titin_I1-like cd20951
Immunoglobulin domain I1 of the titin I-band and similar proteins; a member of the I-set of ...
7254-7342 1.17e-09

Immunoglobulin domain I1 of the titin I-band and similar proteins; a member of the I-set of IgSF domains; The members here are composed of the immunoglobulin domain I1 of the titin I-band and similar proteins. Titin is a key component in the assembly and functioning of vertebrate striated muscles. By providing connections at the level of individual microfilaments, it contributes to the fine balance of forces between the two halves of the sarcomere. The Ig superfamily (IgSF) is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. The two sheets are linked together by a conserved disulfide bond between B strand and F strand. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. The Ig I1 domain of the titin I-band is a member of the I-set Ig domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand but lack a C" strand. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors, the hemolymph protein hemolin, the muscle proteins titin, telokin, and twitchin, the neuronal adhesion molecule axonin-1, and the signaling molecule semaphorin 4D that is involved in axonal guidance, immune function and angiogenesis.


Pssm-ID: 409543 [Multi-domain]  Cd Length: 94  Bit Score: 58.97  E-value: 1.17e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 7254 PDWITRLQDKVAPFGKDYTLQCAASGKPSPTARWLRNGKEIQ--MNGGRMTCDSKDGVFRLHISNVQTGDDGDYTCEAMN 7331
Cdd:cd20951     1 PEFIIRLQSHTVWEKSDAKLRVEVQGKPDPEVKWYKNGVPIDpsSIPGKYKIESEYGVHVLHIRRVTVEDSAVYSAVAKN 80
                          90
                  ....*....|.
gi 281359561 7332 SLGFVNTSGYL 7342
Cdd:cd20951    81 IHGEASSSASV 91
fn3 pfam00041
Fibronectin type III domain;
6260-6343 1.22e-09

Fibronectin type III domain;


Pssm-ID: 394996 [Multi-domain]  Cd Length: 85  Bit Score: 58.58  E-value: 1.22e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561  6260 SPPEGpLSYTETAPDHISLHWySPKDDGGSDITGYIIEF---TEFGVDDWKPVPGTcpNTNFTVKNLVEGKKYVFRIRAE 6336
Cdd:pfam00041    1 SAPSN-LTVTDVTSTSLTVSW-TPPPDGNGPITGYEVEYrpkNSGEPWNEITVPGT--TTSVTLTGLKPGTEYEVRVQAV 76

                   ....*..
gi 281359561  6337 NIYGASE 6343
Cdd:pfam00041   77 NGGGEGP 83
STKc_LRRK1 cd14067
Catalytic domain of the Serine/Threonine Kinase, Leucine-Rich Repeat Kinase 1; STKs catalyze ...
8093-8198 1.23e-09

Catalytic domain of the Serine/Threonine Kinase, Leucine-Rich Repeat Kinase 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. LRRK1 is one of two vertebrate LRRKs which show complementary expression in the brain. It can form heterodimers with LRRK2, and may influence the age of onset of LRRK2-associated Parkinson's disease. LRRKs are also classified as ROCO proteins because they contain a ROC (Ras of complex proteins)/GTPase domain followed by a COR (C-terminal of ROC) domain of unknown function. In addition, LRRKs contain a catalytic kinase domain and protein-protein interaction motifs including a WD40 domain, LRRs and ankyrin (ANK) repeats. LRRKs possess both GTPase and kinase activities, with the ROC domain acting as a molecular switch for the kinase domain, cycling between a GTP-bound state which drives kinase activity and a GDP-bound state which decreases the activity. The LRRK1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270969 [Multi-domain]  Cd Length: 276  Bit Score: 63.45  E-value: 1.23e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 8093 QICEGIRHMHEQNIIHLDIKPENIMC---QTRSSTNVKLIDFGLaTRLDPNEVVKITTGTAEFAAPEIVNREPVGFYTDM 8169
Cdd:cd14067   122 QIAAGLAYLHKKNIIFCDLKSDNILVwslDVQEHINIKLSDYGI-SRQSFHEGALGVEGTPGYQAPEIRPRIVYDEKVDM 200
                          90       100
                  ....*....|....*....|....*....
gi 281359561 8170 WATGVLSYVLLSGLSPFAGDNDVQTLKNV 8198
Cdd:cd14067   201 FSYGMVLYELLSGQRPSLGHHQLQIAKKL 229
IgI_1_Titin_Z1z2-like cd20974
First Ig-like domain of the giant muscle protein titin Z1z2 in the sarcomeric Z-disk and ...
5283-5357 1.25e-09

First Ig-like domain of the giant muscle protein titin Z1z2 in the sarcomeric Z-disk and similar proteins; a member of the I-set of IgSF domains; The members here are composed of the first immunoglobulin (Ig)-like domain of the giant muscle protein titin Z1z2 in the sarcomeric Z-disk and similar proteins. Titin is a key component in the assembly and functioning of vertebrate striated muscles. By providing connections at the level of individual microfilaments, it contributes to the fine balance of forces between the two halves of the sarcomere. The Ig superfamily (IgSF) is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. Unlike the V-set, one of the distinctive features of I-set domains is the lack of a C" strand. The structure of the titin Z1z2 lacks this strand and thus it belongs to the I-set of the IgSF. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors, the hemolymph protein hemolin, the muscle proteins titin, telokin, and twitchin, the neuronal adhesion molecule axonin-1, and the signaling molecule semaphorin 4D that is involved in axonal guidance, immune function and angiogenesis.


Pssm-ID: 409566 [Multi-domain]  Cd Length: 93  Bit Score: 58.90  E-value: 1.25e-09
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 281359561 5283 MSDIKIKAGNVFEFDVPVTGEPLPSKDWTHEGNMIINTD--RVKISNFDDRTKIRILDAKRSDTGVYTLTARNINGT 5357
Cdd:cd20974     7 LQSVVVLEGSTATFEAHVSGKPVPEVSWFRDGQVISTSTlpGVQISFSDGRAKLSIPAVTKANSGRYSLTATNGSGQ 83
STKc_IRAK1 cd14159
Catalytic domain of the Serine/Threonine kinase, Interleukin-1 Receptor Associated Kinase 1; ...
7995-8218 1.32e-09

Catalytic domain of the Serine/Threonine kinase, Interleukin-1 Receptor Associated Kinase 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. IRAKs are involved in Toll-like receptor (TLR) and interleukin-1 (IL-1) signalling pathways, and are thus critical in regulating innate immune responses and inflammation. IRAKs contain an N-terminal Death domain (DD), a proST region (rich in serines, prolines, and threonines), a central kinase domain, and a C-terminal domain; IRAK-4 lacks the C-terminal domain. Vertebrates contain four IRAKs (IRAK-1, -2, -3 (or -M), and -4) that display distinct functions and patterns of expression and subcellular distribution, and can differentially mediate TLR signaling. IRAK1 plays a role in the activation of IRF3/7, STAT, and NFkB. It mediates IL-6 and IFN-gamma responses following IL-1 and IL-18 stimulation, respectively. It also plays an essential role in IFN-alpha induction downstream of TLR7 and TLR9. The IRAK1 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271061 [Multi-domain]  Cd Length: 296  Bit Score: 63.69  E-value: 1.32e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 7995 IGTGAFGVVHRCRERSTgnIFAAKFIP----VSHSVEKDLIRREIDIMNQLHHQKLINLHDAFEDDDEMILILEFLSGGE 8070
Cdd:cd14159     1 IGEGGFGCVYQAVMRNT--EYAVKRLKedseLDWSVVKNSFLTEVEKLSRFRHPNIVDLAGYSAQQGNYCLIYVYLPNGS 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 8071 LFERITAEGYV--MTEAEVINYMRQICEGIRHMHEQN--IIHLDIKPENIMCQTRssTNVKLIDFGLA--TRLDPN---- 8140
Cdd:cd14159    79 LEDRLHCQVSCpcLSWSQRLHVLLGTARAIQYLHSDSpsLIHGDVKSSNILLDAA--LNPKLGDFGLArfSRRPKQpgms 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 8141 -EVVKITT--GTAEFAAPEIVNREPVGFYTDMWATGVLSYVLLSGLSPFAGDNDVQT--LKN-VKACDWDFDVESFKYIS 8214
Cdd:cd14159   157 sTLARTQTvrGTLAYLPEEYVKTGTLSVEIDVYSFGVVLLELLTGRRAMEVDSCSPTkyLKDlVKEEEEAQHTPTTMTHS 236

                  ....
gi 281359561 8215 EEAK 8218
Cdd:cd14159   237 AEAQ 240
IgI_Myotilin_C_like cd05744
Immunoglobulin (Ig)-like domain of myotilin, palladin, and myopalladin; member of the I-set of ...
228-320 1.32e-09

Immunoglobulin (Ig)-like domain of myotilin, palladin, and myopalladin; member of the I-set of Ig superfamily (IgSF) domains; The members here are composed of the immunoglobulin (Ig)-like domain in myotilin, palladin, and myopalladin. Myotilin, palladin, and myopalladin function as scaffolds that regulate actin organization. Myotilin and myopalladin are most abundant in skeletal and cardiac muscle; palladin is ubiquitously expressed in the organs of developing vertebrates and plays a key role in cellular morphogenesis. The three family members each interact with specific molecular partners with all three binding to alpha-actinin; In addition, palladin also binds to vasodilator-stimulated phosphoprotein (VASP) and ezrin, myotilin binds to filamin and actin, and myopalladin also binds to nebulin and cardiac ankyrin repeat protein (CARP). This group belongs to the I-set of IgSF domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand, but lack a C" strand.


Pssm-ID: 409405 [Multi-domain]  Cd Length: 91  Bit Score: 58.66  E-value: 1.32e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561  228 PTFTERPVIRQSEDGGNVTFECRCVGDPTPTVTWSHGETELNESNRYKMSLtmDQKLYHiaCLEISSVVSSDQGEYRAQA 307
Cdd:cd05744     1 PHFLQAPGDLEVQEGRLCRFDCKVSGLPTPDLFWQLNGKPVRPDSAHKMLV--RENGRH--SLIIEPVTKRDAGIYTCIA 76
                          90
                  ....*....|...
gi 281359561  308 KNKHgsGVATINL 320
Cdd:cd05744    77 RNRA--GENSFNA 87
IgI_4_hemolin-like cd20978
Fourth immunoglobulin (Ig)-like domain of hemolin, and similar domains; a member of the I-set ...
7647-7735 1.35e-09

Fourth immunoglobulin (Ig)-like domain of hemolin, and similar domains; a member of the I-set of IgSF domains; The members here are composed of the fourth immunoglobulin (Ig)-like domain of hemolin and similar proteins. Hemolin, an insect immunoglobulin superfamily (IgSF) member containing four Ig-like domains, is a lipopolysaccharide-binding immune protein induced during bacterial infection. Hemolin shares significant sequence similarity with the first four Ig-like domains of the transmembrane cell adhesion molecules (CAMs) of the L1 family. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. The fourth Ig-like domain of hemolin is a member of the I-set Ig domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set domains, members of the I-set have a discontinuous A strand but lack a C" strand. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors, the muscle proteins titin, telokin, and twitchin, the neuronal adhesion molecule axonin-1, and the signaling molecule semaphorin 4D that is involved in axonal guidance, immune function and angiogenesis.


Pssm-ID: 409570 [Multi-domain]  Cd Length: 88  Bit Score: 58.56  E-value: 1.35e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 7647 PPLIVKPLRDANCIQNHNAQFTCTINGVPKPTISWYKGAREIS-NGARYHMysegDNHFLNINDVFGEDADEYVCRAVNK 7725
Cdd:cd20978     1 PKFIQKPEKNVVVKGGQDVTLPCQVTGVPQPKITWLHNGKPLQgPMERATV----EDGTLTIINVQPEDTGYYGCVATNE 76
                          90
                  ....*....|
gi 281359561 7726 AGAKSTRATL 7735
Cdd:cd20978    77 IGDIYTETLL 86
IgI_titin_I1-like cd20951
Immunoglobulin domain I1 of the titin I-band and similar proteins; a member of the I-set of ...
8740-8829 1.36e-09

Immunoglobulin domain I1 of the titin I-band and similar proteins; a member of the I-set of IgSF domains; The members here are composed of the immunoglobulin domain I1 of the titin I-band and similar proteins. Titin is a key component in the assembly and functioning of vertebrate striated muscles. By providing connections at the level of individual microfilaments, it contributes to the fine balance of forces between the two halves of the sarcomere. The Ig superfamily (IgSF) is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. The two sheets are linked together by a conserved disulfide bond between B strand and F strand. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. The Ig I1 domain of the titin I-band is a member of the I-set Ig domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand but lack a C" strand. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors, the hemolymph protein hemolin, the muscle proteins titin, telokin, and twitchin, the neuronal adhesion molecule axonin-1, and the signaling molecule semaphorin 4D that is involved in axonal guidance, immune function and angiogenesis.


Pssm-ID: 409543 [Multi-domain]  Cd Length: 94  Bit Score: 58.59  E-value: 1.36e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 8740 PKIVSHLESRFVRDGDAVNLACRIIGAQHFDVVWLHNNKEIKPSKD---FQYTNEANIYRLQIAEIFPEDGGTYTCEAFN 8816
Cdd:cd20951     1 PEFIIRLQSHTVWEKSDAKLRVEVQGKPDPEVKWYKNGVPIDPSSIpgkYKIESEYGVHVLHIRRVTVEDSAVYSAVAKN 80
                          90
                  ....*....|...
gi 281359561 8817 DIGESFSTCTINV 8829
Cdd:cd20951    81 IHGEASSSASVVV 93
Ig_Titin_like cd05748
Immunoglobulin (Ig)-like domain of titin and similar proteins; The members here are composed ...
4399-4481 1.49e-09

Immunoglobulin (Ig)-like domain of titin and similar proteins; The members here are composed of the immunoglobulin (Ig)-like domain found in titin-like proteins and similar proteins. Titin (also called connectin) is a fibrous sarcomeric protein specifically found in vertebrate striated muscle. Titin is a giant protein; depending on isoform composition, it ranges from 2970 to 3700 kDa, and is of a length that spans half a sarcomere. Titin largely consists of multiple repeats of Ig-like and fibronectin type 3 (FN-III)-like domains. Titin connects the ends of myosin thick filaments to Z disks and extends along the thick filament to the H zone. It appears to function similarly to an elastic band, keeping the myosin filaments centered in the sarcomere during muscle contraction or stretching. Within the sarcomere, titin is also attached to or is associated with myosin binding protein C (MyBP-C). MyBP-C appears to contribute to the generation of passive tension by titin and like titin has repeated Ig-like and FN-III domains. Also included in this group are worm twitchin and insect projectin, thick filament proteins of invertebrate muscle which also have repeated Ig-like and FN-III domains.


Pssm-ID: 409406 [Multi-domain]  Cd Length: 82  Bit Score: 57.98  E-value: 1.49e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 4399 TYNFKSGEPIFLDINISGEPAPDVTWNQNNKSVQTTSFSHIENLPYNTKYINNNPERKDTGLYKISAHNFYGQDQVEfqI 4478
Cdd:cd05748     1 TIVVRAGESLRLDIPIKGRPTPTVTWSKDGQPLKETGRVQIETTASSTSLVIKNAKRSDSGKYTLTLKNSAGEKSAT--I 78

                  ...
gi 281359561 4479 NII 4481
Cdd:cd05748    79 NVK 81
IG_like smart00410
Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.
455-532 1.61e-09

Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.


Pssm-ID: 214653 [Multi-domain]  Cd Length: 85  Bit Score: 58.29  E-value: 1.61e-09
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 281359561    455 ITMKCKCKAKPEPTVTWYR-GQDLVEKSKKIKINttviaEDTYELTLEIKDPGATDGGTYRCNVKNEYGESNANLNLNI 532
Cdd:smart00410   12 VTLSCEASGSPPPEVTWYKqGGKLLAESGRFSVS-----RSGSTSTLTISNVTPEDSGTYTCAATNSSGSASSGTTLTV 85
STKc_ACVR2 cd14053
Catalytic domain of the Serine/Threonine Kinase, Activin Type II Receptor; STKs catalyze the ...
7993-8181 1.74e-09

Catalytic domain of the Serine/Threonine Kinase, Activin Type II Receptor; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. ACVR2 belongs to a group of receptors for the TGFbeta family of secreted signaling molecules that includes TGFbeta, bone morphogenetic proteins (BMPs), activins, growth and differentiation factors (GDFs), and anti-Mullerian hormone, among others. These receptors contain an extracellular domain that binds ligands, a single transmembrane region, and a cytoplasmic catalytic kinase domain. Type II receptors, such as ACVR2, are high-affinity receptors which bind ligands, autophosphorylate, as well as trans-phosphorylate and activate low-affinity type I receptors. ACVR2 acts primarily as the receptors for activins, nodal, myostatin, GDF11, and a subset of BMPs. ACVR2 signaling impacts many cellular and physiological processes including reproductive and gonadal functions, myogenesis, bone remodeling and tooth development, kidney organogenesis, apoptosis, fibrosis, inflammation, and neurogenesis. Vertebrates contain two ACVR2 proteins, ACVR2a (or ActRIIA) and ACVR2b (or ActRIIB). The ACVR2 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270955 [Multi-domain]  Cd Length: 290  Bit Score: 63.12  E-value: 1.74e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 7993 EEIGTGAFGVVHRCRerSTGNIFAAKFIPvshSVEKDLIRREIDIMN--QLHHQKLINLHDA----FEDDDEMILILEFL 8066
Cdd:cd14053     1 EIKARGRFGAVWKAQ--YLNRLVAVKIFP---LQEKQSWLTEREIYSlpGMKHENILQFIGAekhgESLEAEYWLITEFH 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 8067 SGGELFERItaEGYVMTEAEVINYMRQICEGIRHMHEQ----------NIIHLDIKPENIMcqTRSSTNVKLIDFGLATR 8136
Cdd:cd14053    76 ERGSLCDYL--KGNVISWNELCKIAESMARGLAYLHEDipatngghkpSIAHRDFKSKNVL--LKSDLTACIADFGLALK 151
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 281359561 8137 LDPNEVVKIT---TGTAEFAAPEI----VNREPVGFY-TDMWATGVLSYVLLS 8181
Cdd:cd14053   152 FEPGKSCGDThgqVGTRRYMAPEVlegaINFTRDAFLrIDMYAMGLVLWELLS 204
IgI_4_hemolin-like cd20978
Fourth immunoglobulin (Ig)-like domain of hemolin, and similar domains; a member of the I-set ...
8447-8525 1.77e-09

Fourth immunoglobulin (Ig)-like domain of hemolin, and similar domains; a member of the I-set of IgSF domains; The members here are composed of the fourth immunoglobulin (Ig)-like domain of hemolin and similar proteins. Hemolin, an insect immunoglobulin superfamily (IgSF) member containing four Ig-like domains, is a lipopolysaccharide-binding immune protein induced during bacterial infection. Hemolin shares significant sequence similarity with the first four Ig-like domains of the transmembrane cell adhesion molecules (CAMs) of the L1 family. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. The fourth Ig-like domain of hemolin is a member of the I-set Ig domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set domains, members of the I-set have a discontinuous A strand but lack a C" strand. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors, the muscle proteins titin, telokin, and twitchin, the neuronal adhesion molecule axonin-1, and the signaling molecule semaphorin 4D that is involved in axonal guidance, immune function and angiogenesis.


Pssm-ID: 409570 [Multi-domain]  Cd Length: 88  Bit Score: 58.17  E-value: 1.77e-09
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 281359561 8447 VMQARDTCKLLCCLSGKPVPNVRWYKDGRELSKYEYAMTHSDGVVTmeIIDCKPSDSGKYSCKATNCHGTDETDCVVIV 8525
Cdd:cd20978    12 VVKGGQDVTLPCQVTGVPQPKITWLHNGKPLQGPMERATVEDGTLT--IINVQPEDTGYYGCVATNEIGDIYTETLLHV 88
IgI_4_hemolin-like cd20978
Fourth immunoglobulin (Ig)-like domain of hemolin, and similar domains; a member of the I-set ...
8740-8829 1.93e-09

Fourth immunoglobulin (Ig)-like domain of hemolin, and similar domains; a member of the I-set of IgSF domains; The members here are composed of the fourth immunoglobulin (Ig)-like domain of hemolin and similar proteins. Hemolin, an insect immunoglobulin superfamily (IgSF) member containing four Ig-like domains, is a lipopolysaccharide-binding immune protein induced during bacterial infection. Hemolin shares significant sequence similarity with the first four Ig-like domains of the transmembrane cell adhesion molecules (CAMs) of the L1 family. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. The fourth Ig-like domain of hemolin is a member of the I-set Ig domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set domains, members of the I-set have a discontinuous A strand but lack a C" strand. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors, the muscle proteins titin, telokin, and twitchin, the neuronal adhesion molecule axonin-1, and the signaling molecule semaphorin 4D that is involved in axonal guidance, immune function and angiogenesis.


Pssm-ID: 409570 [Multi-domain]  Cd Length: 88  Bit Score: 58.17  E-value: 1.93e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 8740 PKIVSHLESRFVRD-GDAVNLACRIIGAQHFDVVWLHNNKEIK-PSKDFQYTNeaniYRLQIAEIFPEDGGTYTCEAFND 8817
Cdd:cd20978     1 PKFIQKPEKNVVVKgGQDVTLPCQVTGVPQPKITWLHNGKPLQgPMERATVED----GTLTIINVQPEDTGYYGCVATNE 76
                          90
                  ....*....|..
gi 281359561 8818 IGESFSTCTINV 8829
Cdd:cd20978    77 IGDIYTETLLHV 88
IgI_1_Titin_Z1z2-like cd20974
First Ig-like domain of the giant muscle protein titin Z1z2 in the sarcomeric Z-disk and ...
3795-3886 2.12e-09

First Ig-like domain of the giant muscle protein titin Z1z2 in the sarcomeric Z-disk and similar proteins; a member of the I-set of IgSF domains; The members here are composed of the first immunoglobulin (Ig)-like domain of the giant muscle protein titin Z1z2 in the sarcomeric Z-disk and similar proteins. Titin is a key component in the assembly and functioning of vertebrate striated muscles. By providing connections at the level of individual microfilaments, it contributes to the fine balance of forces between the two halves of the sarcomere. The Ig superfamily (IgSF) is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. Unlike the V-set, one of the distinctive features of I-set domains is the lack of a C" strand. The structure of the titin Z1z2 lacks this strand and thus it belongs to the I-set of the IgSF. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors, the hemolymph protein hemolin, the muscle proteins titin, telokin, and twitchin, the neuronal adhesion molecule axonin-1, and the signaling molecule semaphorin 4D that is involved in axonal guidance, immune function and angiogenesis.


Pssm-ID: 409566 [Multi-domain]  Cd Length: 93  Bit Score: 58.13  E-value: 2.12e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 3795 PHIDRKnLQKKIMRSGQMLHIDALIKAEPPAKVTWTYNK--TEIKTSDHIKIENEDYKTTFIMPKVKRADRGIYIVTAKN 3872
Cdd:cd20974     1 PVFTQP-LQSVVVLEGSTATFEAHVSGKPVPEVSWFRDGqvISTSTLPGVQISFSDGRAKLSIPAVTKANSGRYSLTATN 79
                          90
                  ....*....|....
gi 281359561 3873 DSGSDTVEVELEVL 3886
Cdd:cd20974    80 GSGQATSTAELLVL 93
IgI_Twitchin_like cd20949
C-terminal immunoglobulin-like domain of the myosin-associated giant protein kinase Twitchin, ...
8634-8721 2.15e-09

C-terminal immunoglobulin-like domain of the myosin-associated giant protein kinase Twitchin, and similar domains; member of the I-set IgSF domains; The members here are composed of the C-terminal immunoglobulin-like domain of the myosin-associated giant protein kinase Twitchin and similar proteins, including Caenorhabditis elegans and Aplysia californica Twitchin, Drosophila melanogaster Projectin, and similar proteins. These are very large muscle proteins containing multiple immunoglobulin (Ig)-like and fibronectin type III (FN3) domains and a single kinase domain near the C-terminus. In humans these proteins are called Titin. The Ig superfamily (IgSF) is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. The Ig-like domain of the Twitchin is a member of the I-set IgSF domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand but lack a C" strand. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors, the hemolymph protein hemolin, the muscle proteins (titin, telokin, and twitchin), the neuronal adhesion molecule axonin-1, and the signaling molecule semaphorin 4D.


Pssm-ID: 409541 [Multi-domain]  Cd Length: 89  Bit Score: 58.11  E-value: 2.15e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 8634 FTKPLHDLTIHDGEQLILTCYVKGDPEPQISWSKNGKSLSSSDILDLRYKNGIATLTINEVFPEDEGVITCTATNSVGAV 8713
Cdd:cd20949     2 FTENAYVTTVKEGQSATILCEVKGEPQPNVTWHFNGQPISASVADMSKYRILADGLLINKVTQDDTGEYTCRAYQVNSIA 81

                  ....*...
gi 281359561 8714 ETKCKLTI 8721
Cdd:cd20949    82 SDMQERTV 89
Ig cd00096
Immunoglobulin domain; The members here are composed of the immunoglobulin (Ig) domain found ...
4997-5065 2.21e-09

Immunoglobulin domain; The members here are composed of the immunoglobulin (Ig) domain found in the Ig superfamily. The Ig superfamily is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. Members of this group are components of immunoglobulin, neuroglia, cell surface glycoproteins, including T-cell receptors, CD2, CD4, CD8, and membrane glycoproteins, including butyrophilin and chondroitin sulfate proteoglycan core protein. A predominant feature of most Ig domains is a disulfide bridge connecting the two beta-sheets with a tryptophan residue packed against the disulfide bond. Ig superfamily (IgSF) domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. Typically, the V-set domains have A, B, E, and D strands in one sheet and A', G, F, C, C' and C" in the other. The structures in C1-set are smaller than those in the V-set; they have one beta sheet that is formed by strands A, B, E, and D and the other by strands G, F, C, and C'. Moreover, a C1-set Ig domain contains a short C' strand (three residues) and lacks A' and C" strand. Unlike other Ig domain sets, C2-set structures do not have a D strand. Like the V-set Ig domains, members of the I-set have a discontinuous A strand, but lack a C" strand.


Pssm-ID: 409353 [Multi-domain]  Cd Length: 70  Bit Score: 57.34  E-value: 2.21e-09
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 4997 FTFDCKVSGEPAPQTKWLLKKKEVYSKDNVKVTNVDYNTKLKVNSATRSDSGIYTVFAEN-ANGEDSADV 5065
Cdd:cd00096     1 VTLTCSASGNPPPTITWYKNGKPLPPSSRDSRRSELGNGTLTISNVTLEDSGTYTCVASNsAGGSASASV 70
STKc_SRPK3 cd14218
Catalytic domain of the Serine/Threonine Kinase, Serine-aRginine Protein Kinase 3; STKs ...
7988-8244 2.23e-09

Catalytic domain of the Serine/Threonine Kinase, Serine-aRginine Protein Kinase 3; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. SRPK3 is highly expressed in the heart and skeletal muscles, and is controlled by a muscle-specific enhancer that is regulated by MEF2. It may play an important role in muscle development. SRPKs phosphorylate and regulate splicing factors from the SR protein family by specifically phosphorylating multiple serine residues residing in SR/RS dipeptide motifs (also known as RS domains). Phosphorylation of the RS domains enhances interaction with transportin SR and facilitates entry of the SR proteins into the nucleus. SRPKs contain a nonconserved insert domain, within the well-conserved catalytic kinase domain, that regulates their subcellular localization. The SRPK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271120 [Multi-domain]  Cd Length: 365  Bit Score: 63.88  E-value: 2.23e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 7988 RYDILEEIGTGAFGVVHRCRERSTGNIFAAKFIPVS-HSVEKDLirREIDIMNQLH--------HQKLINLHDAFE---- 8054
Cdd:cd14218    11 RYHVVRKLGWGHFSTVWLCWDIQRKRFVALKVVKSAvHYTETAV--DEIKLLKCVRdsdpsdpkRETIVQLIDDFKisgv 88
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 8055 DDDEMILILEFLsGGELFERITAEGYV-MTEAEVINYMRQICEGIRHMHEQ-NIIHLDIKPENI-MC------------- 8118
Cdd:cd14218    89 NGVHVCMVLEVL-GHQLLKWIIKSNYQgLPLPCVKSILRQVLQGLDYLHTKcKIIHTDIKPENIlMCvdegyvrrlaaea 167
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 8119 ----------QTRSSTNVKLIDFgLATRLDPNEVVKITTGTA-------------------EFAAPEIVNREPVGFYTDM 8169
Cdd:cd14218   168 tiwqqagappPSGSSVSFGASDF-LVNPLEPQNADKIRVKIAdlgnacwvhkhftediqtrQYRALEVLIGAEYGTPADI 246
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 8170 WATGVLSYVLLSG---LSPFAGDN-------------------------------------DVQTLKNVKacDWD-FDV- 8207
Cdd:cd14218   247 WSTACMAFELATGdylFEPHSGEDytrdedhiahivellgdipphfalsgrysreyfnrrgELRHIKNLK--HWGlYEVl 324
                         330       340       350       360
                  ....*....|....*....|....*....|....*....|.
gi 281359561 8208 -ESFKYISEEA---KDFIRKLLVRNKEKRMTAHECLLHPWL 8244
Cdd:cd14218   325 vEKYEWPLEQAaqfTDFLLPMMEFLPEKRATAAQCLQHPWL 365
FN3 COG3401
Fibronectin type 3 domain [General function prediction only];
7814-7925 2.34e-09

Fibronectin type 3 domain [General function prediction only];


Pssm-ID: 442628 [Multi-domain]  Cd Length: 603  Bit Score: 64.64  E-value: 2.34e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 7814 YRITAENELGSDTAIIQVQISDRPDPPRFP---LIESIGTESLSLSWKAPvwdGCSDITNYYVERREHPLSSWIRVGNTR 7890
Cdd:COG3401   207 YRVAATDTGGESAPSNEVSVTTPTTPPSAPtglTATADTPGSVTLSWDPV---TESDATGYRVYRSNSGDGPFTKVATVT 283
                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 281359561 7891 FTSMAVSGLTPGKEYDFRIFADNVYG-RSDASDTST 7925
Cdd:COG3401   284 TTSYTDTGLTNGTTYYYRVTAVDAAGnESAPSNVVS 319
IgI_Titin_like cd05747
Immunoglobulin (Ig)-like domain of human titin C terminus and similar proteins; member of the ...
8634-8720 2.41e-09

Immunoglobulin (Ig)-like domain of human titin C terminus and similar proteins; member of the I-set of Ig superfamily (IgSF) domains; The members here are composed of the fifth immunoglobulin (Ig)-like domain from the C-terminus of human titin x and similar proteins. Titin (also called connectin) is a fibrous sarcomeric protein specifically found in vertebrate striated muscle. Titin is gigantic; depending on isoform composition it ranges from 2970 to 3700 kDa, and is of a length that spans half a sarcomere. Titin largely consists of multiple repeats of Ig-like and fibronectin type 3 (FN-III)-like domains. Titin connects the ends of myosin thick filaments to Z disks and extends along the thick filament to the H zone and appears to function similar to an elastic band, keeping the myosin filaments centered in the sarcomere during muscle contraction or stretching. This group belongs to the I-set of IgSF domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand, but lack a C" strand.


Pssm-ID: 143224 [Multi-domain]  Cd Length: 92  Bit Score: 58.14  E-value: 2.41e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 8634 FTKPlHDLTIHDGEQLILTCYVKGDPEPQISWSKNGKSLSSS---DILDLRYKngiATLTINEVFPEDEGVITCTATNSV 8710
Cdd:cd05747     7 LTKP-RSLTVSEGESARFSCDVDGEPAPTVTWMREGQIIVSSqrhQITSTEYK---STFEISKVQMSDEGNYTVVVENSE 82
                          90
                  ....*....|
gi 281359561 8711 GAVETKCKLT 8720
Cdd:cd05747    83 GKQEAQFTLT 92
IgI_NCAM-1_like cd05732
Immunoglobulin (Ig)-like I-set domain of Neural Cell Adhesion Molecule 1 (NCAM-1) and similar ...
7257-7344 2.42e-09

Immunoglobulin (Ig)-like I-set domain of Neural Cell Adhesion Molecule 1 (NCAM-1) and similar proteins; The members here are composed of the fourth immunoglobulin (Ig)-like domain of Neural Cell Adhesion Molecule (NCAM-1). NCAM plays important roles in the development and regeneration of the central nervous system, in synaptogenesis and neural migration. NCAM mediates cell-cell and cell-substratum recognition and adhesion via homophilic (NCAM-NCAM), and heterophilic (NCAM-non-NCAM), interactions. NCAM is expressed as three major isoforms having different intracellular extensions. The extracellular portion of NCAM has five N-terminal Ig-like domains and two fibronectin type III domains. The double zipper adhesion complex model for NCAM homophilic binding involves Ig1, Ig2, and Ig3. By this model, Ig1 and Ig2 mediate dimerization of NCAM molecules situated on the same cell surface (cis interactions), and Ig3 domains mediate interactions between NCAM molecules expressed on the surface of opposing cells (trans interactions), through binding to the Ig1 and Ig2 domains. The adhesive ability of NCAM is modulated by the addition of polysialic acid chains to the fifth Ig-like domain. Also included in this group is NCAM-2 (also known as OCAM/mamFas II and RNCAM) NCAM-2 is differentially expressed in the developing and mature olfactory epithelium (OE). One of the unique features of I-set domains is the lack of a C" strand. The structures of this group show that the Ig domain lacks this strand and thus is a member of the I-set of Ig domains.


Pssm-ID: 409395 [Multi-domain]  Cd Length: 96  Bit Score: 57.92  E-value: 2.42e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 7257 ITRLQDKVAPFGKDYTLQCAASGKPSPTARWLRNGKEIQMN----GGRMTCDSKDGVFRLHISNVQTGDDGDYTCEAMNS 7332
Cdd:cd05732     5 ITYLENQTAVELEQITLTCEAEGDPIPEITWRRATRGISFEegdlDGRIVVRGHARVSSLTLKDVQLTDAGRYDCEASNR 84
                          90
                  ....*....|..
gi 281359561 7333 LGFVNTSGYLKI 7344
Cdd:cd05732    85 IGGDQQSMYLEV 96
FN3 COG3401
Fibronectin type 3 domain [General function prediction only];
7814-7929 2.63e-09

Fibronectin type 3 domain [General function prediction only];


Pssm-ID: 442628 [Multi-domain]  Cd Length: 603  Bit Score: 64.64  E-value: 2.63e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 7814 YRITAENELG-----SDTAIIQVQISdRPDPPRFPLIESIGTESLSLSWKAPvwDGcSDITNYYVERREHPLSSWIRVG- 7887
Cdd:COG3401   300 YRVTAVDAAGnesapSNVVSVTTDLT-PPAAPSGLTATAVGSSSITLSWTAS--SD-ADVTGYNVYRSTSGGGTYTKIAe 375
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 281359561 7888 ---NTRFTsmaVSGLTPGKEYDFRIFADNVYGR-SDASDTSTLIKT 7929
Cdd:COG3401   376 tvtTTSYT---DTGLTPGTTYYYKVTAVDAAGNeSAPSEEVSATTA 418
STKc_RIP1 cd14027
Catalytic domain of the Serine/Threonine kinase, Receptor Interacting Protein 1; STKs catalyze ...
7998-8186 2.64e-09

Catalytic domain of the Serine/Threonine kinase, Receptor Interacting Protein 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. RIP1 harbors a C-terminal Death domain (DD), which binds death receptors (DRs) including TNF receptor 1, Fas, TNF-related apoptosis-inducing ligand receptor 1 (TRAILR1), and TRAILR2. It also interacts with other DD-containing adaptor proteins such as TRADD and FADD. RIP1 can also recruit other kinases including MEKK1, MEKK3, and RIP3 through an intermediate domain (ID) that bears a RIP homotypic interaction motif (RHIM). RIP1 plays a crucial role in determining a cell's fate, between survival or death, following exposure to stress signals. It is important in the signaling of NF-kappaB and MAPKs, and it links DR-associated signaling to reactive oxygen species (ROS) production. Abnormal RIP1 function may result in ROS accummulation affecting inflammatory responses, innate immunity, stress responses, and cell survival. RIP kinases serve as essential sensors of cellular stress. The RIP1 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270929 [Multi-domain]  Cd Length: 267  Bit Score: 62.13  E-value: 2.64e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 7998 GAFGVVHRCRERSTGN-IFAAKFIPVSHSVEKDLIRREIDIMNQLHHQKLINLHDAFEDDDEMILILEFLSGGELFERIT 8076
Cdd:cd14027     4 GGFGKVSLCFHRTQGLvVLKTVYTGPNCIEHNEALLEEGKMMNRLRHSRVVKLLGVILEEGKYSLVMEYMEKGNLMHVLK 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 8077 AegyVMTEAEVI-NYMRQICEGIRHMHEQNIIHLDIKPENIMCQtrSSTNVKLIDFGLAT-----RLDPNE--------- 8141
Cdd:cd14027    84 K---VSVPLSVKgRIILEIIEGMAYLHGKGVIHKDLKPENILVD--NDFHIKIADLGLASfkmwsKLTKEEhneqrevdg 158
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*...
gi 281359561 8142 VVKITTGTAEFAAPE---IVNREPVGfYTDMWATGVLSYVLLSGLSPF 8186
Cdd:cd14027   159 TAKKNAGTLYYMAPEhlnDVNAKPTE-KSDVYSFAIVLWAIFANKEPY 205
fn3 pfam00041
Fibronectin type III domain;
5968-6046 2.74e-09

Fibronectin type III domain;


Pssm-ID: 394996 [Multi-domain]  Cd Length: 85  Bit Score: 57.42  E-value: 2.74e-09
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 281359561  5968 EEITANSVTISWKPPKDnGGSEISSYVIEKRDLTHGGGWVPAVnyVSAKYNHAVVPRLLEGTMYELRVMAENLQGRSDP 6046
Cdd:pfam00041    9 TDVTSTSLTVSWTPPPD-GNGPITGYEVEYRPKNSGEPWNEIT--VPGTTTSVTLTGLKPGTEYEVRVQAVNGGGEGPP 84
IgI_M-protein_C cd05891
C-terminal immunoglobulin (Ig)-like domain of M-protein; member of the I-set of Ig superfamily ...
8641-8711 3.45e-09

C-terminal immunoglobulin (Ig)-like domain of M-protein; member of the I-set of Ig superfamily (IgSF) domains; The members here are composed of the C-terminal immunoglobulin (Ig)-like domain of M-protein (also known as myomesin-2). M-protein is a structural protein localized to the M-band, a transverse structure in the center of the sarcomere, and is a candidate for M-band bridges. M-protein is modular consisting mainly of repetitive IG-like and fibronectin type III (FnIII) domains and has a muscle-type specific expression pattern. M-protein is present in fast fibers.


Pssm-ID: 143299  Cd Length: 92  Bit Score: 57.61  E-value: 3.45e-09
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 281359561 8641 LTIHDGEQLILTCYVKGDPEPQISWSKNGKSLSSSDILDLRYKNG-IATLTINEVFPEDEGVITCTATNSVG 8711
Cdd:cd05891    11 VTIMEGKTLNLTCTVFGNPDPEVIWFKNDQDIELSEHYSVKLEQGkYASLTIKGVTSEDSGKYSINVKNKYG 82
IgI_5_Robo cd20952
Fifth Ig-like domain of Roundabout (Robo) homolog 1/2, and similar domains; a member of the ...
7261-7344 3.49e-09

Fifth Ig-like domain of Roundabout (Robo) homolog 1/2, and similar domains; a member of the I-set of IgSF domains; The members here are composed of the fifth Ig-like domain of Roundabout (Robo) homolog 1/2 and similar domains. Robo receptors play a role in the development of the central nervous system (CNS), and are receptors of Slit protein. Slit is a repellant secreted by the neural cells in the midline. Slit acts through Robo to prevent most neurons from crossing the midline from either side. Three mammalian Robo homologs (Robo1, -2, and -3), and three mammalian Slit homologs (Slit-1,-2, -3), have been identified. Commissural axons, which cross the midline, express low levels of Robo; longitudinal axons, which avoid the midline, express high levels of Robo. Robo1, -2, and -3 are expressed by commissural neurons in the vertebrate spinal cord and Slits 1, -2, -3 are expressed at the ventral midline. Robo-3 is a divergent member of the Robo family which instead of being a positive regulator of slit responsiveness, antagonizes slit responsiveness in precrossing axons. The Slit-Robo interaction is mediated by the second leucine-rich repeat (LRR) domain of Slit and the two N-terminal Ig domains of Robo, Ig1 and Ig2. The primary Robo binding site for Slit2 has been shown by surface plasmon resonance experiments and mutational analysis to be is the Ig1 domain, while the Ig2 domain has been proposed to harbor a weak secondary binding site. The fifth Ig-like domain of Robo 1 and 2 is a member of the I-set Ig domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand but lack a C" strand. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors


Pssm-ID: 409544 [Multi-domain]  Cd Length: 87  Bit Score: 57.51  E-value: 3.49e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 7261 QDKVAPFGKDYTLQCAASGKPSPTARWLRNGKEIQMNGGRMTCdSKDGVfrLHISNVQTGDDGDYTCEAMNSLGFVNTSG 7340
Cdd:cd20952     7 QNQTVAVGGTVVLNCQATGEPVPTISWLKDGVPLLGKDERITT-LENGS--LQIKGAEKSDTGEYTCVALNLSGEATWSA 83

                  ....
gi 281359561 7341 YLKI 7344
Cdd:cd20952    84 VLDV 87
Ig_3 pfam13927
Immunoglobulin domain; This family contains immunoglobulin-like domains.
119-199 3.58e-09

Immunoglobulin domain; This family contains immunoglobulin-like domains.


Pssm-ID: 464046 [Multi-domain]  Cd Length: 78  Bit Score: 57.19  E-value: 3.58e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561   119 PTFAKKPAIRQEEDGKRLLFECRVNADPIPAIIWFHNGAAVKESERHKITVDKDVhsyfATLEILNVTVEDAGKYKVNAK 198
Cdd:pfam13927    2 PVITVSPSSVTVREGETVTLTCEATGSPPPTITWYKNGEPISSGSTRSRSLSGSN----STLTISNVTRSDAGTYTCVAS 77

                   .
gi 281359561   199 N 199
Cdd:pfam13927   78 N 78
fn3 pfam00041
Fibronectin type III domain;
7838-7921 3.60e-09

Fibronectin type III domain;


Pssm-ID: 394996 [Multi-domain]  Cd Length: 85  Bit Score: 57.04  E-value: 3.60e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561  7838 DPPRFPLIESIGTESLSLSWKAPVwDGCSDITNYYVERREH---PLSSWIRVGNTRfTSMAVSGLTPGKEYDFRIFADNV 7914
Cdd:pfam00041    1 SAPSNLTVTDVTSTSLTVSWTPPP-DGNGPITGYEVEYRPKnsgEPWNEITVPGTT-TSVTLTGLKPGTEYEVRVQAVNG 78

                   ....*..
gi 281359561  7915 YGRSDAS 7921
Cdd:pfam00041   79 GGEGPPS 85
IgI_Titin_like cd05747
Immunoglobulin (Ig)-like domain of human titin C terminus and similar proteins; member of the ...
5559-5654 3.69e-09

Immunoglobulin (Ig)-like domain of human titin C terminus and similar proteins; member of the I-set of Ig superfamily (IgSF) domains; The members here are composed of the fifth immunoglobulin (Ig)-like domain from the C-terminus of human titin x and similar proteins. Titin (also called connectin) is a fibrous sarcomeric protein specifically found in vertebrate striated muscle. Titin is gigantic; depending on isoform composition it ranges from 2970 to 3700 kDa, and is of a length that spans half a sarcomere. Titin largely consists of multiple repeats of Ig-like and fibronectin type 3 (FN-III)-like domains. Titin connects the ends of myosin thick filaments to Z disks and extends along the thick filament to the H zone and appears to function similar to an elastic band, keeping the myosin filaments centered in the sarcomere during muscle contraction or stretching. This group belongs to the I-set of IgSF domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand, but lack a C" strand.


Pssm-ID: 143224 [Multi-domain]  Cd Length: 92  Bit Score: 57.37  E-value: 3.69e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 5559 STIICKPRflapffdksllnDITVHAGKRLGWTLPIEASPRPLITWLYNGKEIGSNSRGESGLFQNELTFEIVSSLRSDE 5638
Cdd:cd05747     4 ATILTKPR------------SLTVSEGESARFSCDVDGEPAPTVTWMREGQIIVSSQRHQITSTEYKSTFEISKVQMSDE 71
                          90
                  ....*....|....*.
gi 281359561 5639 GRYTLILKNEHGSFDA 5654
Cdd:cd05747    72 GNYTVVVENSEGKQEA 87
Ig_3 pfam13927
Immunoglobulin domain; This family contains immunoglobulin-like domains.
438-519 3.72e-09

Immunoglobulin domain; This family contains immunoglobulin-like domains.


Pssm-ID: 464046 [Multi-domain]  Cd Length: 78  Bit Score: 56.80  E-value: 3.72e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561   438 PSFIEKPRIIPNESGTLITMKCKCKAKPEPTVTWYRGQdlvekSKKIKINTTVIAEDTYELTLEIKDPGATDGGTYRCNV 517
Cdd:pfam13927    2 PVITVSPSSVTVREGETVTLTCEATGSPPPTITWYKNG-----EPISSGSTRSRSLSGSNSTLTISNVTRSDAGTYTCVA 76

                   ..
gi 281359561   518 KN 519
Cdd:pfam13927   77 SN 78
IG_like smart00410
Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.
8318-8401 3.84e-09

Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.


Pssm-ID: 214653 [Multi-domain]  Cd Length: 85  Bit Score: 57.13  E-value: 3.84e-09
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561   8318 PSSQFCYEGQSVKFYCRCIAIATPTLTWSHNNIE-LRQSVKFMKRYVGDDYYFIINRVKLDDRGEYIIRAENHYGSREEV 8396
Cdd:smart00410    1 PPSVTVKEGESVTLSCEASGSPPPEVTWYKQGGKlLAESGRFSVSRSGSTSTLTISNVTPEDSGTYTCAATNSSGSASSG 80

                    ....*
gi 281359561   8397 VFLNV 8401
Cdd:smart00410   81 TTLTV 85
IgI_4_hemolin-like cd20978
Fourth immunoglobulin (Ig)-like domain of hemolin, and similar domains; a member of the I-set ...
2304-2395 3.86e-09

Fourth immunoglobulin (Ig)-like domain of hemolin, and similar domains; a member of the I-set of IgSF domains; The members here are composed of the fourth immunoglobulin (Ig)-like domain of hemolin and similar proteins. Hemolin, an insect immunoglobulin superfamily (IgSF) member containing four Ig-like domains, is a lipopolysaccharide-binding immune protein induced during bacterial infection. Hemolin shares significant sequence similarity with the first four Ig-like domains of the transmembrane cell adhesion molecules (CAMs) of the L1 family. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. The fourth Ig-like domain of hemolin is a member of the I-set Ig domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set domains, members of the I-set have a discontinuous A strand but lack a C" strand. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors, the muscle proteins titin, telokin, and twitchin, the neuronal adhesion molecule axonin-1, and the signaling molecule semaphorin 4D that is involved in axonal guidance, immune function and angiogenesis.


Pssm-ID: 409570 [Multi-domain]  Cd Length: 88  Bit Score: 57.40  E-value: 3.86e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 2304 PFIVGEGLKNVTVKKGQTIRFDIKYDGEPEPAATWVKGTDNLKFDNQRICLDQlernSSITIKKSVRKDTGKYKLVLSNS 2383
Cdd:cd20978     1 PKFIQKPEKNVVVKGGQDVTLPCQVTGVPQPKITWLHNGKPLQGPMERATVED----GTLTIINVQPEDTGYYGCVATNE 76
                          90
                  ....*....|..
gi 281359561 2384 SGTIESEAQVVV 2395
Cdd:cd20978    77 IGDIYTETLLHV 88
Ig_3 pfam13927
Immunoglobulin domain; This family contains immunoglobulin-like domains.
7741-7820 4.02e-09

Immunoglobulin domain; This family contains immunoglobulin-like domains.


Pssm-ID: 464046 [Multi-domain]  Cd Length: 78  Bit Score: 56.80  E-value: 4.02e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561  7741 PKLNVPPRfrdTAYFDKGENVVIKIPFTGFPKPRIHWVRDGENIESGGHYTVEVKERHAVLIIRDGSHLDSGPYRITAEN 7820
Cdd:pfam13927    2 PVITVSPS---SVTVREGETVTLTCEATGSPPPTITWYKNGEPISSGSTRSRSLSGSNSTLTISNVTRSDAGTYTCVASN 78
Ig_3 pfam13927
Immunoglobulin domain; This family contains immunoglobulin-like domains.
6177-6242 4.10e-09

Immunoglobulin domain; This family contains immunoglobulin-like domains.


Pssm-ID: 464046 [Multi-domain]  Cd Length: 78  Bit Score: 56.80  E-value: 4.10e-09
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 281359561  6177 VRAGEPVNLNIPISGAPTPTIEWKRGDLKLEEGKRISYETNSERTLFRIDDSNRRDSGKYTVTAAN 6242
Cdd:pfam13927   13 VREGETVTLTCEATGSPPPTITWYKNGEPISSGSTRSRSLSGSNSTLTISNVTRSDAGTYTCVASN 78
Ig4_L1-NrCAM_like cd04978
Fourth immunoglobulin (Ig)-like domain of L1, Ng-CAM (Neuron-glia CAM cell adhesion molecule), ...
7256-7342 4.25e-09

Fourth immunoglobulin (Ig)-like domain of L1, Ng-CAM (Neuron-glia CAM cell adhesion molecule), and NrCAM (Ng-CAM-related); The members here are composed of the fourth immunoglobulin (Ig)-like domain of L1, Ng-CAM (Neuron-glia CAM cell adhesion molecule), and NrCAM (Ng-CAM-related). These proteins belong to the L1 subfamily of cell adhesion molecules (CAMs) and are comprised of an extracellular region having six Ig-like domains and five fibronectin type III domains, a transmembrane region and an intracellular domain. These molecules are primarily expressed in the nervous system. L1 is associated with an X-linked recessive disorder, X-linked hydrocephalus, MASA syndrome, or spastic paraplegia type 1, that involves abnormalities of axonal growth.


Pssm-ID: 409367 [Multi-domain]  Cd Length: 89  Bit Score: 57.07  E-value: 4.25e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 7256 WITRLQDKVAPFGKDYTLQCAASGKPSPTARWLRNGKEIQMNGGrmtcDSKDGVFR--LHISNVQTGDDGDYTCEAMNSL 7333
Cdd:cd04978     2 WIIEPPSLVLSPGETGELICEAEGNPQPTITWRLNGVPIEPAPE----DMRRTVDGrtLIFSNLQPNDTAVYQCNASNVH 77

                  ....*....
gi 281359561 7334 GFVNTSGYL 7342
Cdd:cd04978    78 GYLLANAFL 86
IG_like smart00410
Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.
5284-5366 4.27e-09

Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.


Pssm-ID: 214653 [Multi-domain]  Cd Length: 85  Bit Score: 57.13  E-value: 4.27e-09
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561   5284 SDIKIKAGNVFEFDVPVTGEPLPSKDWTHEG-NMIINTDRVKISNFDDRTKIRILDAKRSDTGVYTLTARNINGTDRHNV 5362
Cdd:smart00410    2 PSVTVKEGESVTLSCEASGSPPPEVTWYKQGgKLLAESGRFSVSRSGSTSTLTISNVTPEDSGTYTCAATNSSGSASSGT 81

                    ....
gi 281359561   5363 KVTI 5366
Cdd:smart00410   82 TLTV 85
COG4733 COG4733
Phage-related protein, tail protein J [Mobilome: prophages, transposons];
6864-7131 4.41e-09

Phage-related protein, tail protein J [Mobilome: prophages, transposons];


Pssm-ID: 443767 [Multi-domain]  Cd Length: 978  Bit Score: 64.20  E-value: 4.41e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 6864 RDMTVIAGDEFRITVPYHASPRPTASWSlnglevipgerikFDSNDYASMYYN-KSAKRDETGSYTITLTN-NKGSDTAS 6941
Cdd:COG4733   453 RTVQSVAGRTLTVSTAYSETPEAGAVWA-------------FGPDELETQLFRvVSIEENEDGTYTITAVQhAPEKYAAI 519
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 6942 CHVTVVDRPlPPQGPLNA-----YDITPD-----TCTLAWKTPLDDggspiTNYVVEKLDNSGSWVKISSfVRNTHYDVM 7011
Cdd:COG4733   520 DAGAFDDVP-PQWPPVNVttsesLSVVAQgtavtTLTVSWDAPAGA-----VAYEVEWRRDDGNWVSVPR-TSGTSFEVP 592
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 7012 GLEPHyKYNFRVRAENQYGLSDPLDIIEPIVAKHQFTVpdePGQPKVIDWDSGN--VTLIWTRPLsdgGSRIQGYQIEYR 7089
Cdd:COG4733   593 GIYAG-DYEVRVRAINALGVSSAWAASSETTVTGKTAP---PPAPTGLTATGGLggITLSWSFPV---DADTLRTEIRYS 665
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|..
gi 281359561 7090 DILNDSSWNAYDYIIKDTKYQLYNLINGSEYEFRIKAKNAAG 7131
Cdd:COG4733   666 TTGDWASATVAQALYPGNTYTLAGLKAGQTYYYRARAVDRSG 707
IgI_5_Dscam cd20958
Fifth immunoglobulin domain of the Drosophila melanogaster Dscam protein, and similar domains; ...
8632-8711 4.50e-09

Fifth immunoglobulin domain of the Drosophila melanogaster Dscam protein, and similar domains; a member of the I-set of IgSF domains; The members here are composed of the fifth immunoglobulin domain of the Drosophila melanogaster Down syndrome cell adhesion molecule (DSCAM) protein and similar proteins. Down syndrome cell adhesion molecule (DSCAM) is a cell adhesion molecule that plays critical roles in neural development, including axon guidance and branching, axon target recognition, self-avoidance and synaptic formation. DSCAM belongs to the immunoglobulin superfamily and contributes to defects in the central nervous system in Down syndrome patients. Vertebrate DSCAMs differ from Drosophila Dscam1 in that they lack the extensive alternative splicing that occurs in the insect gene. Drosophila melanogaster Dscam has 38,016 isoforms generated by the alternative splicing of four variable exon clusters, which allows every neuron in the fly to display a distinctive set of Dscam proteins on its cell surface. Drosophila Dscam1 is a cell-surface protein that plays important roles in neural development and axon tiling of neurons. It is shown that thousands of isoforms bind themselves through specific homophilic (self-binding) interactions, a process which mediates cellular self-recognition. Drosophila Dscam2 is also alternatively spliced and plays a key role in the development of two visual system neurons, monopolar cells L1 and L2. This group is a member of the I-set Ig domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand but lack a C" strand.


Pssm-ID: 409550 [Multi-domain]  Cd Length: 89  Bit Score: 57.19  E-value: 4.50e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 8632 PEFTKPLHDLTIHDGEQLILTCYVKGDPEPQISWSKNGKSLSssdiLDLR---YKNGiaTLTINEVFP-EDEGVITCTAT 8707
Cdd:cd20958     1 PPFIRPMGNLTAVAGQTLRLHCPVAGYPISSITWEKDGRRLP----LNHRqrvFPNG--TLVIENVQRsSDEGEYTCTAR 74

                  ....
gi 281359561 8708 NSVG 8711
Cdd:cd20958    75 NQQG 78
Ig cd00096
Immunoglobulin domain; The members here are composed of the immunoglobulin (Ig) domain found ...
136-204 4.65e-09

Immunoglobulin domain; The members here are composed of the immunoglobulin (Ig) domain found in the Ig superfamily. The Ig superfamily is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. Members of this group are components of immunoglobulin, neuroglia, cell surface glycoproteins, including T-cell receptors, CD2, CD4, CD8, and membrane glycoproteins, including butyrophilin and chondroitin sulfate proteoglycan core protein. A predominant feature of most Ig domains is a disulfide bridge connecting the two beta-sheets with a tryptophan residue packed against the disulfide bond. Ig superfamily (IgSF) domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. Typically, the V-set domains have A, B, E, and D strands in one sheet and A', G, F, C, C' and C" in the other. The structures in C1-set are smaller than those in the V-set; they have one beta sheet that is formed by strands A, B, E, and D and the other by strands G, F, C, and C'. Moreover, a C1-set Ig domain contains a short C' strand (three residues) and lacks A' and C" strand. Unlike other Ig domain sets, C2-set structures do not have a D strand. Like the V-set Ig domains, members of the I-set have a discontinuous A strand, but lack a C" strand.


Pssm-ID: 409353 [Multi-domain]  Cd Length: 70  Bit Score: 56.57  E-value: 4.65e-09
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 281359561  136 LLFECRVNADPIPAIIWFHNGAAVKESERHKITVDKDVhsyfATLEILNVTVEDAGKYKVNAKNELGES 204
Cdd:cd00096     1 VTLTCSASGNPPPTITWYKNGKPLPPSSRDSRRSELGN----GTLTISNVTLEDSGTYTCVASNSAGGS 65
IgI_2_Robo cd05724
Second immunoglobulin (Ig)-like domain in Robo (roundabout) receptors; member of the I-set of ...
8646-8721 5.00e-09

Second immunoglobulin (Ig)-like domain in Robo (roundabout) receptors; member of the I-set of Ig superfamily (IgSF) domains; The members here are composed of the second immunoglobulin (Ig)-like domain in Robo (roundabout) receptors. Robo receptors play a role in the development of the central nervous system (CNS), and are receptors of the Slit protein. Slit is a repellant secreted by the neural cells in the midline. Slit acts through Robo to prevent most neurons from crossing the midline from either side. Three mammalian Robo homologs (Robo1, Robo2, and Robo3), and three mammalian Slit homologs (Slit-1,Slit-2, Slit-3), have been identified. Commissural axons, which cross the midline, express low levels of Robo; longitudinal axons, which avoid the midline, express high levels of Robo. Robo1, Robo2, and Robo3 are expressed by commissural neurons in the vertebrate spinal cord and Slit-1, Slit-2, Slit-3 are expressed at the ventral midline. Robo-3 is a divergent member of the Robo family which instead of being a positive regulator of Slit responsiveness, antagonizes Slit responsiveness in precrossing axons. The Slit-Robo interaction is mediated by the second leucine-rich repeat (LRR) domain of Slit and the two N-terminal Ig domains of Robo, Ig1 and Ig2. The primary Robo binding site for Slit-2 has been shown by surface plasmon resonance experiments and mutational analysis to be the Ig1 domain, while the Ig2 domain has been proposed to harbor a weak secondary binding site. This group belongs to the I-set of IgSF domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand, but lack a C" strand.


Pssm-ID: 409389 [Multi-domain]  Cd Length: 87  Bit Score: 57.03  E-value: 5.00e-09
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 281359561 8646 GEQLILTCYV-KGDPEPQISWSKNGKSLsssDILDLRYKN-GIATLTINEVFPEDEGVITCTATNSVGAVETK-CKLTI 8721
Cdd:cd05724    12 GEMAVLECSPpRGHPEPTVSWRKDGQPL---NLDNERVRIvDDGNLLIAEARKSDEGTYKCVATNMVGERESRaARLSV 87
IgI_2_Titin_Z1z2-like cd20972
Second Ig-like domain of the giant muscle protein titin Z1z2 in the sarcomeric Z-disk, and ...
7254-7344 5.07e-09

Second Ig-like domain of the giant muscle protein titin Z1z2 in the sarcomeric Z-disk, and similar domains; a member of the I-set of IgSF domains; The members here are composed of the second immunoglobulin (Ig)-like domain of the giant muscle protein titin Z1z2 in the sarcomeric Z-disk and similar proteins. Titin is a key component in the assembly and functioning of vertebrate striated muscles. By providing connections at the level of individual microfilaments, it contributes to the fine balance of forces between the two halves of the sarcomere. The Ig superfamily (IgSF) is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. Unlike the V-set, one of the distinctive features of I-set domains is the lack of a C" strand. The structure of the titin Z1z2 lacks this strand and thus it belongs to the I-set of the IgSF. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors, the hemolymph protein hemolin, the muscle proteins titin, telokin, and twitchin, the neuronal adhesion molecule axonin-1, and the signaling molecule semaphorin 4D that is involved in axonal guidance, immune function and angiogenesis.


Pssm-ID: 409564 [Multi-domain]  Cd Length: 91  Bit Score: 57.21  E-value: 5.07e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 7254 PDWITRLQDKVAPFGKDYTLQCAASGKPSPTARWLRNGKEIQmNGGRMTCDSKDGVFRLHISNVQTGDDGDYTCEAMNSL 7333
Cdd:cd20972     2 PQFIQKLRSQEVAEGSKVRLECRVTGNPTPVVRWFCEGKELQ-NSPDIQIHQEGDLHSLIIAEAFEEDTGRYSCLATNSV 80
                          90
                  ....*....|.
gi 281359561 7334 GFVNTSGYLKI 7344
Cdd:cd20972    81 GSDTTSAEIFV 91
COG4733 COG4733
Phage-related protein, tail protein J [Mobilome: prophages, transposons];
6124-6439 5.35e-09

Phage-related protein, tail protein J [Mobilome: prophages, transposons];


Pssm-ID: 443767 [Multi-domain]  Cd Length: 978  Bit Score: 63.81  E-value: 5.35e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 6124 DRVTSNHQYQYRISAVNaagnGKT----SEPSAIFNARPLREKprfYFDGLIGKR-IKVRAGEPVNLNIPISGAPTPTIE 6198
Cdd:COG4733   406 DDVLAGRRIGGRVSSVD----GRVvtldRPVTMEAGDRYLRVR---LPDGTSVARtVQSVAGRTLTVSTAYSETPEAGAV 478
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 6199 WkrgdlkleegkriSYETNSERT-LFRIDDSNRRDSGKYTVTA-ANEFGKDTA-DIEVIVVDKPSPPEGPLSYTE----- 6270
Cdd:COG4733   479 W-------------AFGPDELETqLFRVVSIEENEDGTYTITAvQHAPEKYAAiDAGAFDDVPPQWPPVNVTTSEslsvv 545
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 6271 ---TAPDHISLHWyspkdDGGSDITGYIIEFTEfGVDDWKPVPGTcPNTNFTVKNLVEGKkYVFRIRAENIYGAS---EA 6344
Cdd:COG4733   546 aqgTAVTTLTVSW-----DAPAGAVAYEVEWRR-DDGNWVSVPRT-SGTSFEVPGIYAGD-YEVRVRAINALGVSsawAA 617
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 6345 LEGKPVLAKSpfDPPGAPSQPTISAyTPNSANLEWHPPDDcggKPITGYIVeRRERGGEWI--KCNNYPTPNTSYTVSNL 6422
Cdd:COG4733   618 SSETTVTGKT--APPPAPTGLTATG-GLGGITLSWSFPVD---ADTLRTEI-RYSTTGDWAsaTVAQALYPGNTYTLAGL 690
                         330
                  ....*....|....*..
gi 281359561 6423 RDGARYEFRVLAVNEAG 6439
Cdd:COG4733   691 KAGQTYYYRARAVDRSG 707
IgI_C2_MyBP-C-like cd20967
Domain C2 of human cardiac Myosin Binding Protein C and similar domains; a member of the I-set ...
1842-1896 5.66e-09

Domain C2 of human cardiac Myosin Binding Protein C and similar domains; a member of the I-set of IgSF domains; The members here are composed of the immunoglobulin (Ig) Domain C2 of human cardiac Myosin Binding Protein C (MyBP-C) and similar domains. MyBP-C is a thick filament protein involved in the regulation of muscle contraction. Mutations in cardiac MyBP-C gene are the second most frequent cause of hypertrophic cardiomyopathy. MyBP-C binds to myosin with two binding sites, one at its C-terminus and another at its N-terminus. The N-terminal binding site, consisting of immunoglobulin (lg) domains C1 and C2 connected by a flexible linker, interacts with the S2 segment of myosin in a phosphorylation-regulated manner. The C1 and C2 Ig domains can bind to and activate or inhibit the thin filament. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. Unlike the V-set, one of the distinctive features of I-set domains is the lack of a C" strand. The structures of the Ig domains of MyBP-C lack this strand and thus belong to the I-set of Ig superfamily domains. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors.


Pssm-ID: 409559  Cd Length: 82  Bit Score: 56.48  E-value: 5.66e-09
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 281359561 1842 VTLACEIDDAMGEVQWLRNGEEIKPDKRIQIVKDGRKRKLVIKDCKVTDAGQFKC 1896
Cdd:cd20967    15 IRLTVELADPDAEVKWYKDGQELQSSSKVIFESIGAKRTLTVQQASLADAGEYQC 69
Ig_3 pfam13927
Immunoglobulin domain; This family contains immunoglobulin-like domains.
8437-8512 5.66e-09

Immunoglobulin domain; This family contains immunoglobulin-like domains.


Pssm-ID: 464046 [Multi-domain]  Cd Length: 78  Bit Score: 56.42  E-value: 5.66e-09
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 281359561  8437 PSFTFLLRPRVMQARDTCKLLCCLSGKPVPNVRWYKDGREL-SKYEYAMTHSDGVVTMEIIDCKPSDSGKYSCKATN 8512
Cdd:pfam13927    2 PVITVSPSSVTVREGETVTLTCEATGSPPPTITWYKNGEPIsSGSTRSRSLSGSNSTLTISNVTRSDAGTYTCVASN 78
Ig_C5_MyBP-C cd05894
C5 immunoglobulin (Ig) domain of cardiac myosin binding protein C (MyBP-C); The members here ...
4695-4775 6.07e-09

C5 immunoglobulin (Ig) domain of cardiac myosin binding protein C (MyBP-C); The members here are composed of the C5 immunoglobulin (Ig) domain of cardiac myosin binding protein C (MyBP-C). MyBP-C consists of repeated domains, Ig and fibronectin type 3, and various linkers. Three isoforms of MYBP-C exist: slow-skeletal (ssMyBP-C), fast-skeletal (fsMyBP-C), and cardiac (cMyBP-C). cMYBP-C has insertions between and inside domains and an additional cardiac-specific Ig domain at the N-terminus. For cMYBP_C an interaction has been demonstrated between this C5 domain and the Ig C8 domain.


Pssm-ID: 409475  Cd Length: 86  Bit Score: 56.77  E-value: 6.07e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 4695 ITLSSGTALKLDANITGEPAPKVEWKLSNYHLQSGKN-VTIETPDYYTKLVIRPTQRSDSGEYLVTATNTSGKDSVLVNV 4773
Cdd:cd05894     5 IVVVAGNKLRLDVPISGEPAPTVTWSRGDKAFTATEGrVRVESYKDLSSFVIEGAEREDEGVYTITVTNPVGEDHASLFV 84

                  ..
gi 281359561 4774 VI 4775
Cdd:cd05894    85 KV 86
Ig cd00096
Immunoglobulin domain; The members here are composed of the immunoglobulin (Ig) domain found ...
8456-8519 7.22e-09

Immunoglobulin domain; The members here are composed of the immunoglobulin (Ig) domain found in the Ig superfamily. The Ig superfamily is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. Members of this group are components of immunoglobulin, neuroglia, cell surface glycoproteins, including T-cell receptors, CD2, CD4, CD8, and membrane glycoproteins, including butyrophilin and chondroitin sulfate proteoglycan core protein. A predominant feature of most Ig domains is a disulfide bridge connecting the two beta-sheets with a tryptophan residue packed against the disulfide bond. Ig superfamily (IgSF) domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. Typically, the V-set domains have A, B, E, and D strands in one sheet and A', G, F, C, C' and C" in the other. The structures in C1-set are smaller than those in the V-set; they have one beta sheet that is formed by strands A, B, E, and D and the other by strands G, F, C, and C'. Moreover, a C1-set Ig domain contains a short C' strand (three residues) and lacks A' and C" strand. Unlike other Ig domain sets, C2-set structures do not have a D strand. Like the V-set Ig domains, members of the I-set have a discontinuous A strand, but lack a C" strand.


Pssm-ID: 409353 [Multi-domain]  Cd Length: 70  Bit Score: 55.80  E-value: 7.22e-09
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 281359561 8456 LLCCLSGKPVPNVRWYKDGREL-SKYEYAMTHSDGVVTMEIIDCKPSDSGKYSCKATNCHGTDET 8519
Cdd:cd00096     3 LTCSASGNPPPTITWYKNGKPLpPSSRDSRRSELGNGTLTISNVTLEDSGTYTCVASNSAGGSAS 67
fn3 pfam00041
Fibronectin type III domain;
4485-4568 7.41e-09

Fibronectin type III domain;


Pssm-ID: 394996 [Multi-domain]  Cd Length: 85  Bit Score: 56.27  E-value: 7.41e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561  4485 GKPEGpLEVSEVHKDGCKLKWKKPKDDGGePVESYLVEKFDPDTGIWLPVGRSDGPE--YNVDGLVPGHDYKFRVKAVNK 4562
Cdd:pfam00041    1 SAPSN-LTVTDVTSTSLTVSWTPPPDGNG-PITGYEVEYRPKNSGEPWNEITVPGTTtsVTLTGLKPGTEYEVRVQAVNG 78

                   ....*.
gi 281359561  4563 EGESEP 4568
Cdd:pfam00041   79 GGEGPP 84
Ig_3 pfam13927
Immunoglobulin domain; This family contains immunoglobulin-like domains.
338-414 7.67e-09

Immunoglobulin domain; This family contains immunoglobulin-like domains.


Pssm-ID: 464046 [Multi-domain]  Cd Length: 78  Bit Score: 56.03  E-value: 7.67e-09
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 281359561   338 PKKPTIRQEEDLLIMECVLEAHPVPDIVWYCSEKEICNNQRTKmtrkaITKDSYILTLEIQNPTKEDGGNYRCNAIN 414
Cdd:pfam13927    7 SPSSVTVREGETVTLTCEATGSPPPTITWYKNGEPISSGSTRS-----RSLSGSNSTLTISNVTRSDAGTYTCVASN 78
COG4733 COG4733
Phage-related protein, tail protein J [Mobilome: prophages, transposons];
5970-6306 7.82e-09

Phage-related protein, tail protein J [Mobilome: prophages, transposons];


Pssm-ID: 443767 [Multi-domain]  Cd Length: 978  Bit Score: 63.43  E-value: 7.82e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 5970 ITANSVTISWKPPKDNggseiSSYVIEKRDltHGGGWVPAVNYVSAKYNhavVPRLLEGTmYELRVMAENLQGRSDPLTS 6049
Cdd:COG4733   549 TAVTTLTVSWDAPAGA-----VAYEVEWRR--DDGNWVSVPRTSGTSFE---VPGIYAGD-YEVRVRAINALGVSSAWAA 617
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 6050 DQPVVAKSQYTVPGAPgkPELT-DSDKNHITIKWKQPIsngGSPIIGYDIERRDVNTGRWIKINGQPVPTAEYQDDRVTS 6128
Cdd:COG4733   618 SSETTVTGKTAPPPAP--TGLTaTGGLGGITLSWSFPV---DADTLRTEIRYSTTGDWASATVAQALYPGNTYTLAGLKA 692
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 6129 NHQYQYRISAVNAAGNgkTSEPSAIFNARPLREKPRFYFDGLIGKRIKVRAGEPVNLNIPISGAPTPTIEWKRGDLKLEE 6208
Cdd:COG4733   693 GQTYYYRARAVDRSGN--VSAWWVSGQASADAAGILDAITGQILETELGQELDAIIQNATVAEVVAATVTDVTAQIDTAV 770
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 6209 GKRISYETNS---ERTLFRIDDSNRRDSGKYTVTAANEFGKDTADIEVIVVDkPSPPEGPLSYTETAPDHISLHWYSPKD 6285
Cdd:COG4733   771 LFAGVATAAAigaEARVAATVAESATAAAATGTAADAAGDASGGVTAGTSGT-TGAGDTAASTTRVAAAVVLAGVVVYGD 849
                         330       340
                  ....*....|....*....|.
gi 281359561 6286 DGGSDITGYIIEFTEFGVDDW 6306
Cdd:COG4733   850 AIIESGNTGDIVATGDIASAA 870
fn3 pfam00041
Fibronectin type III domain;
6655-6738 8.09e-09

Fibronectin type III domain;


Pssm-ID: 394996 [Multi-domain]  Cd Length: 85  Bit Score: 56.27  E-value: 8.09e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561  6655 SPPTRLRADEFSGDSLTLYWNPPnDDGGSAIQNYIIEKKEARSSTWSK---VSSfcTVPFVRIRNLVLNKEYDFRVIAEN 6731
Cdd:pfam00041    1 SAPSNLTVTDVTSTSLTVSWTPP-PDGNGPITGYEVEYRPKNSGEPWNeitVPG--TTTSVTLTGLKPGTEYEVRVQAVN 77

                   ....*..
gi 281359561  6732 KYGQSDP 6738
Cdd:pfam00041   78 GGGEGPP 84
Ig cd00096
Immunoglobulin domain; The members here are composed of the immunoglobulin (Ig) domain found ...
245-318 8.61e-09

Immunoglobulin domain; The members here are composed of the immunoglobulin (Ig) domain found in the Ig superfamily. The Ig superfamily is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. Members of this group are components of immunoglobulin, neuroglia, cell surface glycoproteins, including T-cell receptors, CD2, CD4, CD8, and membrane glycoproteins, including butyrophilin and chondroitin sulfate proteoglycan core protein. A predominant feature of most Ig domains is a disulfide bridge connecting the two beta-sheets with a tryptophan residue packed against the disulfide bond. Ig superfamily (IgSF) domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. Typically, the V-set domains have A, B, E, and D strands in one sheet and A', G, F, C, C' and C" in the other. The structures in C1-set are smaller than those in the V-set; they have one beta sheet that is formed by strands A, B, E, and D and the other by strands G, F, C, and C'. Moreover, a C1-set Ig domain contains a short C' strand (three residues) and lacks A' and C" strand. Unlike other Ig domain sets, C2-set structures do not have a D strand. Like the V-set Ig domains, members of the I-set have a discontinuous A strand, but lack a C" strand.


Pssm-ID: 409353 [Multi-domain]  Cd Length: 70  Bit Score: 55.80  E-value: 8.61e-09
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 281359561  245 VTFECRCVGDPTPTVTWSHGETELNESNRYKMSLTMdqklyHIACLEISSVVSSDQGEYRAQAKNKHGSGVATI 318
Cdd:cd00096     1 VTLTCSASGNPPPTITWYKNGKPLPPSSRDSRRSEL-----GNGTLTISNVTLEDSGTYTCVASNSAGGSASAS 69
Ig_3 pfam13927
Immunoglobulin domain; This family contains immunoglobulin-like domains.
9-90 8.62e-09

Immunoglobulin domain; This family contains immunoglobulin-like domains.


Pssm-ID: 464046 [Multi-domain]  Cd Length: 78  Bit Score: 56.03  E-value: 8.62e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561     9 PSFVKKPQLHQEDDGNRLIFECQLLSSPKPDIEWFRsDNKVVEDVRTkfkiQPVGENKYTVVLELDDVVETDAGLYKVKA 88
Cdd:pfam13927    2 PVITVSPSSVTVREGETVTLTCEATGSPPPTITWYK-NGEPISSGST----RSRSLSGSNSTLTISNVTRSDAGTYTCVA 76

                   ..
gi 281359561    89 KN 90
Cdd:pfam13927   77 SN 78
IgI_telokin-like cd20973
immunoglobulin-like domain of telokin and similar proteins; a member of the I-set of IgSF ...
562-636 8.76e-09

immunoglobulin-like domain of telokin and similar proteins; a member of the I-set of IgSF domains; The members here are composed of the immunoglobulin (Ig) domain in telokin, the C-terminal domain of myosin light chain kinase which is identical to telokin, and similar proteins. The Ig superfamily (IgSF) is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. Unlike the V-set, one of the distinctive features of I-set domains is the lack of a C" strand. The structure of the telokin Ig domain lacks this strand and thus it belongs to the I-set of the IgSF. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors, the hemolymph protein hemolin, the muscle proteins titin, telokin, and twitchin, the neuronal adhesion molecule axonin-1, and the signaling molecule semaphorin 4D that is involved in axonal guidance, immune function and angiogenesis.


Pssm-ID: 409565 [Multi-domain]  Cd Length: 88  Bit Score: 56.43  E-value: 8.76e-09
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 281359561  562 MECKVKADPKPDVIWFRNGEVIKESNKIKtfIEQRGDqYYIKLELLDPQLEDSGLYKCNIKNTLGELNANLTLNI 636
Cdd:cd20973    17 FDCKVEGYPDPEVKWMKDDNPIVESRRFQ--IDQDED-GLCSLIISDVCGDDSGKYTCKAVNSLGEATCSAELTV 88
fn3 pfam00041
Fibronectin type III domain;
5381-5454 9.01e-09

Fibronectin type III domain;


Pssm-ID: 394996 [Multi-domain]  Cd Length: 85  Bit Score: 56.27  E-value: 9.01e-09
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 281359561  5381 DVSKNSIVLRWRPPkDDGGSEITHYVVE---KMDNEAMRWVPVgdcTDTEIRAD--NLIENHDYSFRVRAVNKQGQSQP 5454
Cdd:pfam00041   10 DVTSTSLTVSWTPP-PDGNGPITGYEVEyrpKNSGEPWNEITV---PGTTTSVTltGLKPGTEYEVRVQAVNGGGEGPP 84
PTKc_FGFR2 cd05101
Catalytic domain of the Protein Tyrosine Kinase, Fibroblast Growth Factor Receptor 2; PTKs ...
7987-8188 9.33e-09

Catalytic domain of the Protein Tyrosine Kinase, Fibroblast Growth Factor Receptor 2; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. There are many splice variants of FGFR2 which show differential expression and binding to FGF ligands. Disruption of either FGFR2 or FGFR2b is lethal in mice, due to defects in the placenta or severe impairment of tissue development including lung, limb, and thyroid, respectively. Disruption of FGFR2c in mice results in defective bone and skull development. Genetic alterations of FGFR2 are associated with many human skeletal disorders including Apert syndrome, Crouzon syndrome, Jackson-Weiss syndrome, and Pfeiffer syndrome. FGFR2 is part of the FGFR subfamily, which are receptor PTKs (RTKs) containing an extracellular ligand-binding region with three immunoglobulin-like domains, a transmembrane segment, and an intracellular catalytic domain. The binding of FGFRs to their ligands, the FGFs, results in receptor dimerization and activation, and intracellular signaling. The binding of FGFs to FGFRs is promiscuous, in that a receptor may be activated by several ligands and a ligand may bind to more that one type of receptor. The FGFR2 subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270679 [Multi-domain]  Cd Length: 313  Bit Score: 61.18  E-value: 9.33e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 7987 DRYDILEEIGTGAFGVVHRC------RERSTGNIFAAKFIPVSHSVEKDL--IRREIDIMNQL-HHQKLINLHDAFEDDD 8057
Cdd:cd05101    24 DKLTLGKPLGEGCFGQVVMAeavgidKDKPKEAVTVAVKMLKDDATEKDLsdLVSEMEMMKMIgKHKNIINLLGACTQDG 103
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 8058 EMILILEFLSGGELFERITAE---------------GYVMTEAEVINYMRQICEGIRHMHEQNIIHLDIKPENIMCqtrS 8122
Cdd:cd05101   104 PLYVIVEYASKGNLREYLRARrppgmeysydinrvpEEQMTFKDLVSCTYQLARGMEYLASQKCIHRDLAARNVLV---T 180
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 281359561 8123 STNV-KLIDFGLATRLDPNEVVKITTG---TAEFAAPEIVNREPVGFYTDMWATGVLSYVLLS-GLSPFAG 8188
Cdd:cd05101   181 ENNVmKIADFGLARDINNIDYYKKTTNgrlPVKWMAPEALFDRVYTHQSDVWSFGVLMWEIFTlGGSPYPG 251
PTKc_Chk cd05083
Catalytic domain of the Protein Tyrosine Kinase, Csk homologous kinase; PTKs catalyze the ...
7993-8201 9.36e-09

Catalytic domain of the Protein Tyrosine Kinase, Csk homologous kinase; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Chk is also referred to as megakaryocyte-associated tyrosine kinase (Matk). Chk inhibits Src kinases using a noncatalytic mechanism by simply binding to them. As a negative regulator of Src kinases, Chk may play important roles in cell proliferation, survival, and differentiation, and consequently, in cancer development and progression. Chk is expressed in brain and hematopoietic cells. Like Csk, it is a cytoplasmic (or nonreceptor) tyr kinase containing the Src homology domains, SH3 and SH2, N-terminal to the catalytic tyr kinase domain. To inhibit Src kinases that are anchored to the plasma membrane, Chk is translocated to the membrane via binding to specific transmembrane proteins, G-proteins, or adaptor proteins near the membrane. Studies in mice reveal that Chk is not functionally redundant with Csk and that it plays an important role as a regulator of immune responses. Chk also plays a role in neural differentiation in a manner independent of Src by enhancing Mapk activation via Ras-mediated signaling. The Chk subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270666 [Multi-domain]  Cd Length: 254  Bit Score: 60.27  E-value: 9.36e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 7993 EEIGTGAFGVVhrCRERSTGNIFAAKFIPVSHSVEKDLirREIDIMNQLHHQKLINL-----HDAfedddeMILILEFLS 8067
Cdd:cd05083    12 EIIGEGEFGAV--LQGEYMGQKVAVKNIKCDVTAQAFL--EETAVMTKLQHKNLVRLlgvilHNG------LYIVMELMS 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 8068 GGELFERITAEGYVMTE-AEVINYMRQICEGIRHMHEQNIIHLDIKPENIMCqtrSSTNV-KLIDFGLAtRLDPNEvVKI 8145
Cdd:cd05083    82 KGNLVNFLRSRGRALVPvIQLLQFSLDVAEGMEYLESKKLVHRDLAARNILV---SEDGVaKISDFGLA-KVGSMG-VDN 156
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 281359561 8146 TTGTAEFAAPEIVNREPVGFYTDMWATGVLSYVLLS-GLSPFAGdndvQTLKNVKAC 8201
Cdd:cd05083   157 SRLPVKWTAPEALKNKKFSSKSDVWSYGVLLWEVFSyGRAPYPK----MSVKEVKEA 209
fn3 pfam00041
Fibronectin type III domain;
3315-3382 1.02e-08

Fibronectin type III domain;


Pssm-ID: 394996 [Multi-domain]  Cd Length: 85  Bit Score: 55.88  E-value: 1.02e-08
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 281359561  3315 LKWRKPKDDGGiPITGYVIEKMDTATGKWVPAGSVDPEKYDIEIKGLDPNHRYQFRVKAVNEEGESEP 3382
Cdd:pfam00041   18 VSWTPPPDGNG-PITGYEVEYRPKNSGEPWNEITVPGTTTSVTLTGLKPGTEYEVRVQAVNGGGEGPP 84
I-set pfam07679
Immunoglobulin I-set domain;
746-835 1.10e-08

Immunoglobulin I-set domain;


Pssm-ID: 400151 [Multi-domain]  Cd Length: 90  Bit Score: 56.11  E-value: 1.10e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561   746 PEISRKLADQKVAESKTFELlvslsqtdrKCK--------VEWYKGSTVIRETKDITTTFDGTTARLTFSSARTEHTSNY 817
Cdd:pfam07679    1 PKFTQKPKDVEVQEGESARF---------TCTvtgtpdpeVSWFKDGQPLRSSDRFKVTYEGGTYTLTISNVQPDDSGKY 71
                           90
                   ....*....|....*...
gi 281359561   818 KVIVTNEVGKDESSCKIT 835
Cdd:pfam07679   72 TCVATNSAGEAEASAELT 89
IgI_Myotilin_C cd05892
C-terminal immunoglobulin (Ig)-like domain of myotilin; member of the I-set of Ig superfamily ...
119-211 1.12e-08

C-terminal immunoglobulin (Ig)-like domain of myotilin; member of the I-set of Ig superfamily (IgSF) domains; The members here are composed of the C-terminal immunoglobulin (Ig)-like domain of myotilin. Mytolin belongs to the palladin-myotilin-myopalladin family. Proteins belonging to the latter family contain multiple Ig-like domains and function as scaffolds, modulating the actin cytoskeleton. Myotilin is most abundant in skeletal and cardiac muscle and is involved in maintaining sarcomere integrity. It binds to alpha-actinin, filamin, and actin. Mutations in myotilin lead to muscle disorders. This group belongs to the I-set of IgSF domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand, but lack a C" strand.


Pssm-ID: 409473  Cd Length: 92  Bit Score: 55.93  E-value: 1.12e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561  119 PTFAKKPAIRQEEDGKRLLFECRVNADPIPAIIWFHNgaavKESERH---KITVDKDVHSYFaTLEILNVTVEDAGKYKV 195
Cdd:cd05892     1 PMFIQKPQNKKVLEGDPVRLECQISAIPPPQIFWKKN----NEMLQYntdRISLYQDNCGRI-CLLIQNANKKDAGWYTV 75
                          90
                  ....*....|....*.
gi 281359561  196 NAKNELGESNATISLN 211
Cdd:cd05892    76 SAVNEAGVVSCNARLD 91
Ig cd00096
Immunoglobulin domain; The members here are composed of the immunoglobulin (Ig) domain found ...
560-627 1.24e-08

Immunoglobulin domain; The members here are composed of the immunoglobulin (Ig) domain found in the Ig superfamily. The Ig superfamily is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. Members of this group are components of immunoglobulin, neuroglia, cell surface glycoproteins, including T-cell receptors, CD2, CD4, CD8, and membrane glycoproteins, including butyrophilin and chondroitin sulfate proteoglycan core protein. A predominant feature of most Ig domains is a disulfide bridge connecting the two beta-sheets with a tryptophan residue packed against the disulfide bond. Ig superfamily (IgSF) domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. Typically, the V-set domains have A, B, E, and D strands in one sheet and A', G, F, C, C' and C" in the other. The structures in C1-set are smaller than those in the V-set; they have one beta sheet that is formed by strands A, B, E, and D and the other by strands G, F, C, and C'. Moreover, a C1-set Ig domain contains a short C' strand (three residues) and lacks A' and C" strand. Unlike other Ig domain sets, C2-set structures do not have a D strand. Like the V-set Ig domains, members of the I-set have a discontinuous A strand, but lack a C" strand.


Pssm-ID: 409353 [Multi-domain]  Cd Length: 70  Bit Score: 55.41  E-value: 1.24e-08
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 281359561  560 VIMECKVKADPKPDVIWFRNGEVIKESNKIKTFIEQRGDQyyikLELLDPQLEDSGLYKCNIKNTLGE 627
Cdd:cd00096     1 VTLTCSASGNPPPTITWYKNGKPLPPSSRDSRRSELGNGT----LTISNVTLEDSGTYTCVASNSAGG 64
IgI_2_Palladin_C cd20990
Second C-terminal immunoglobulin (Ig)-like domain of palladin; member of the I-set of Ig ...
8632-8711 1.27e-08

Second C-terminal immunoglobulin (Ig)-like domain of palladin; member of the I-set of Ig superfamily (IgSF) domains; The members here are composed of the C-terminal immunoglobulin (Ig)-like domain of palladin. Palladin belongs to the palladin-myotilin-myopalladin family. Proteins belonging to this family contain multiple Ig-like domains and function as scaffolds, modulating actin cytoskeleton. Palladin binds to alpha-actinin ezrin, vasodilator-stimulated phosphoprotein VASP, SPIN90 (also known as DIP or mDia interacting protein), and Src. Palladin also binds F-actin directly, via its Ig3 domain. Palladin is expressed as several alternatively spliced isoforms, having various combinations of Ig-like domains, in a cell-type-specific manner. It has been suggested that palladin's different Ig-like domains may be specialized for distinct functions. This group belongs to the I-set of IgSF domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand, but lack a C" strand.


Pssm-ID: 409582  Cd Length: 91  Bit Score: 55.88  E-value: 1.27e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 8632 PEFTKPLHDLTIHDGEQLILTCYVKGDPEPQISWSKNGKSL--SSSDILDLRyKNGIATLTINEVFPEDEGVITCTATNS 8709
Cdd:cd20990     1 PHFLQAPGDLTVQEGKLCRMDCKVSGLPTPDLSWQLDGKPIrpDSAHKMLVR-ENGVHSLIIEPVTSRDAGIYTCIATNR 79

                  ..
gi 281359561 8710 VG 8711
Cdd:cd20990    80 AG 81
IgI_Myomesin_like_C cd05737
C-terminal immunoglobulin (Ig)-like domain of myomesin and M-protein; member of the I-set of ...
8642-8712 1.27e-08

C-terminal immunoglobulin (Ig)-like domain of myomesin and M-protein; member of the I-set of Ig superfamily (IgSF) domains; The members here are composed of the C-terminal immunoglobulin (Ig)-like domain of myomesin and M-protein (also known as myomesin-2). Myomesin and M-protein are both structural proteins localized to the M-band, a transverse structure in the center of the sarcomere, and are candidates for M-band bridges. Both proteins are modular, consisting mainly of repetitive Ig-like and fibronectin type III (FnIII) domains. Myomesin is expressed in all types of vertebrate striated muscle; M-protein has a muscle-type specific expression pattern. Myomesin is present in both slow and fast fibers; M-protein is present only in fast fibers. It has been suggested that myomesin acts as a molecular spring with alternative splicing as a means of modifying its elasticity.


Pssm-ID: 319300  Cd Length: 92  Bit Score: 56.06  E-value: 1.27e-08
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 281359561 8642 TIHDGEQLILTCYVKGDPEPQISWSKNGKSLSSSDILDLRYKNG-IATLTINEVFPEDEGVITCTATNSVGA 8712
Cdd:cd05737    12 TIMEGKTLNLTCNVWGDPPPEVSWLKNDQALAFLDHCNLKVEAGrTVYFTINGVSSEDSGKYGLVVKNKYGS 83
IgI_4_hemolin-like cd20978
Fourth immunoglobulin (Ig)-like domain of hemolin, and similar domains; a member of the I-set ...
228-321 1.31e-08

Fourth immunoglobulin (Ig)-like domain of hemolin, and similar domains; a member of the I-set of IgSF domains; The members here are composed of the fourth immunoglobulin (Ig)-like domain of hemolin and similar proteins. Hemolin, an insect immunoglobulin superfamily (IgSF) member containing four Ig-like domains, is a lipopolysaccharide-binding immune protein induced during bacterial infection. Hemolin shares significant sequence similarity with the first four Ig-like domains of the transmembrane cell adhesion molecules (CAMs) of the L1 family. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. The fourth Ig-like domain of hemolin is a member of the I-set Ig domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set domains, members of the I-set have a discontinuous A strand but lack a C" strand. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors, the muscle proteins titin, telokin, and twitchin, the neuronal adhesion molecule axonin-1, and the signaling molecule semaphorin 4D that is involved in axonal guidance, immune function and angiogenesis.


Pssm-ID: 409570 [Multi-domain]  Cd Length: 88  Bit Score: 55.86  E-value: 1.31e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561  228 PTFTERPVI-RQSEDGGNVTFECRCVGDPTPTVTWSHGETELNESnrykmsltMDQKLYHIACLEISSVVSSDQGEYRAQ 306
Cdd:cd20978     1 PKFIQKPEKnVVVKGGQDVTLPCQVTGVPQPKITWLHNGKPLQGP--------MERATVEDGTLTIINVQPEDTGYYGCV 72
                          90
                  ....*....|....*
gi 281359561  307 AKNKHGSGVATINLN 321
Cdd:cd20978    73 ATNEIGDIYTETLLH 87
Ig_Titin_like cd05748
Immunoglobulin (Ig)-like domain of titin and similar proteins; The members here are composed ...
146-210 1.36e-08

Immunoglobulin (Ig)-like domain of titin and similar proteins; The members here are composed of the immunoglobulin (Ig)-like domain found in titin-like proteins and similar proteins. Titin (also called connectin) is a fibrous sarcomeric protein specifically found in vertebrate striated muscle. Titin is a giant protein; depending on isoform composition, it ranges from 2970 to 3700 kDa, and is of a length that spans half a sarcomere. Titin largely consists of multiple repeats of Ig-like and fibronectin type 3 (FN-III)-like domains. Titin connects the ends of myosin thick filaments to Z disks and extends along the thick filament to the H zone. It appears to function similarly to an elastic band, keeping the myosin filaments centered in the sarcomere during muscle contraction or stretching. Within the sarcomere, titin is also attached to or is associated with myosin binding protein C (MyBP-C). MyBP-C appears to contribute to the generation of passive tension by titin and like titin has repeated Ig-like and FN-III domains. Also included in this group are worm twitchin and insect projectin, thick filament proteins of invertebrate muscle which also have repeated Ig-like and FN-III domains.


Pssm-ID: 409406 [Multi-domain]  Cd Length: 82  Bit Score: 55.29  E-value: 1.36e-08
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 281359561  146 PIPAIIWFHNGAAVKESERhkitVDKDVHSYFATLEILNVTVEDAGKYKVNAKNELGESNATISL 210
Cdd:cd05748    20 PTPTVTWSKDGQPLKETGR----VQIETTASSTSLVIKNAKRSDSGKYTLTLKNSAGEKSATINV 80
IgI_Titin_like cd05747
Immunoglobulin (Ig)-like domain of human titin C terminus and similar proteins; member of the ...
436-530 1.36e-08

Immunoglobulin (Ig)-like domain of human titin C terminus and similar proteins; member of the I-set of Ig superfamily (IgSF) domains; The members here are composed of the fifth immunoglobulin (Ig)-like domain from the C-terminus of human titin x and similar proteins. Titin (also called connectin) is a fibrous sarcomeric protein specifically found in vertebrate striated muscle. Titin is gigantic; depending on isoform composition it ranges from 2970 to 3700 kDa, and is of a length that spans half a sarcomere. Titin largely consists of multiple repeats of Ig-like and fibronectin type 3 (FN-III)-like domains. Titin connects the ends of myosin thick filaments to Z disks and extends along the thick filament to the H zone and appears to function similar to an elastic band, keeping the myosin filaments centered in the sarcomere during muscle contraction or stretching. This group belongs to the I-set of IgSF domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand, but lack a C" strand.


Pssm-ID: 143224 [Multi-domain]  Cd Length: 92  Bit Score: 55.82  E-value: 1.36e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561  436 FAPSFIEKPRIIPNESGTLITMKCKCKAKPEPTVTWYRGQDLVEKSKKIKINTTviaedTYELTLEIKDPGATDGGTYRC 515
Cdd:cd05747     2 LPATILTKPRSLTVSEGESARFSCDVDGEPAPTVTWMREGQIIVSSQRHQITST-----EYKSTFEISKVQMSDEGNYTV 76
                          90
                  ....*....|....*
gi 281359561  516 NVKNEYGESNANLNL 530
Cdd:cd05747    77 VVENSEGKQEAQFTL 91
IgI_Myomesin_like_C cd05737
C-terminal immunoglobulin (Ig)-like domain of myomesin and M-protein; member of the I-set of ...
132-210 1.49e-08

C-terminal immunoglobulin (Ig)-like domain of myomesin and M-protein; member of the I-set of Ig superfamily (IgSF) domains; The members here are composed of the C-terminal immunoglobulin (Ig)-like domain of myomesin and M-protein (also known as myomesin-2). Myomesin and M-protein are both structural proteins localized to the M-band, a transverse structure in the center of the sarcomere, and are candidates for M-band bridges. Both proteins are modular, consisting mainly of repetitive Ig-like and fibronectin type III (FnIII) domains. Myomesin is expressed in all types of vertebrate striated muscle; M-protein has a muscle-type specific expression pattern. Myomesin is present in both slow and fast fibers; M-protein is present only in fast fibers. It has been suggested that myomesin acts as a molecular spring with alternative splicing as a means of modifying its elasticity.


Pssm-ID: 319300  Cd Length: 92  Bit Score: 55.67  E-value: 1.49e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561  132 DGKRLLFECRVNADPIPAIIWFHNGAAVKESERHKITVDKdvhSYFATLEILNVTVEDAGKYKVNAKNELG--ESNATIS 209
Cdd:cd05737    15 EGKTLNLTCNVWGDPPPEVSWLKNDQALAFLDHCNLKVEA---GRTVYFTINGVSSEDSGKYGLVVKNKYGseTSDVTVS 91

                  .
gi 281359561  210 L 210
Cdd:cd05737    92 V 92
IgI_Myotilin_C_like cd05744
Immunoglobulin (Ig)-like domain of myotilin, palladin, and myopalladin; member of the I-set of ...
3795-3885 1.51e-08

Immunoglobulin (Ig)-like domain of myotilin, palladin, and myopalladin; member of the I-set of Ig superfamily (IgSF) domains; The members here are composed of the immunoglobulin (Ig)-like domain in myotilin, palladin, and myopalladin. Myotilin, palladin, and myopalladin function as scaffolds that regulate actin organization. Myotilin and myopalladin are most abundant in skeletal and cardiac muscle; palladin is ubiquitously expressed in the organs of developing vertebrates and plays a key role in cellular morphogenesis. The three family members each interact with specific molecular partners with all three binding to alpha-actinin; In addition, palladin also binds to vasodilator-stimulated phosphoprotein (VASP) and ezrin, myotilin binds to filamin and actin, and myopalladin also binds to nebulin and cardiac ankyrin repeat protein (CARP). This group belongs to the I-set of IgSF domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand, but lack a C" strand.


Pssm-ID: 409405 [Multi-domain]  Cd Length: 91  Bit Score: 55.58  E-value: 1.51e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 3795 PHIDRKnLQKKIMRSGQMLHIDALIKAEPPAKVTWTYNKTEIK-TSDHIKIENEDYKTTFIMPKVKRADRGIYIVTAKND 3873
Cdd:cd05744     1 PHFLQA-PGDLEVQEGRLCRFDCKVSGLPTPDLFWQLNGKPVRpDSAHKMLVRENGRHSLIIEPVTKRDAGIYTCIARNR 79
                          90
                  ....*....|..
gi 281359561 3874 SGSDTVEVELEV 3885
Cdd:cd05744    80 AGENSFNAELVV 91
IgI_2_Titin_Z1z2-like cd20972
Second Ig-like domain of the giant muscle protein titin Z1z2 in the sarcomeric Z-disk, and ...
545-626 1.54e-08

Second Ig-like domain of the giant muscle protein titin Z1z2 in the sarcomeric Z-disk, and similar domains; a member of the I-set of IgSF domains; The members here are composed of the second immunoglobulin (Ig)-like domain of the giant muscle protein titin Z1z2 in the sarcomeric Z-disk and similar proteins. Titin is a key component in the assembly and functioning of vertebrate striated muscles. By providing connections at the level of individual microfilaments, it contributes to the fine balance of forces between the two halves of the sarcomere. The Ig superfamily (IgSF) is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. Unlike the V-set, one of the distinctive features of I-set domains is the lack of a C" strand. The structure of the titin Z1z2 lacks this strand and thus it belongs to the I-set of the IgSF. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors, the hemolymph protein hemolin, the muscle proteins titin, telokin, and twitchin, the neuronal adhesion molecule axonin-1, and the signaling molecule semaphorin 4D that is involved in axonal guidance, immune function and angiogenesis.


Pssm-ID: 409564 [Multi-domain]  Cd Length: 91  Bit Score: 55.67  E-value: 1.54e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561  545 FIEKPRIVSENNGKLVIMECKVKADPKPDVIWFRNGEVIKESNKIKtfIEQRGDQYyiKLELLDPQLEDSGLYKCNIKNT 624
Cdd:cd20972     4 FIQKLRSQEVAEGSKVRLECRVTGNPTPVVRWFCEGKELQNSPDIQ--IHQEGDLH--SLIIAEAFEEDTGRYSCLATNS 79

                  ..
gi 281359561  625 LG 626
Cdd:cd20972    80 VG 81
IgI_4_MYLK-like cd20976
Fourth Ig-like domain from smooth muscle myosin light chain kinase and similar domains ; a ...
4994-5069 1.55e-08

Fourth Ig-like domain from smooth muscle myosin light chain kinase and similar domains ; a member of the I-set of IgSF domains; The members here are composed of the fourth immunoglobulin (Ig)-like domain from smooth muscle myosin light chain kinase (MYLK) and similar domains. The Ig superfamily (IgSF) is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. Unlike the V-set, one of the distinctive features of I-set domains is the lack of a C" strand. The structure of this group shows that the fourth Ig-like domain from myosin light chain kinase lacks this strand and thus belongs to the I-set of the IgSF. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors, the hemolymph protein hemolin, the muscle proteins titin, telokin, and twitchin, the neuronal adhesion molecule axonin-1, and the signaling molecule semaphorin 4D that is involved in axonal guidance, immune function and angiogenesis.


Pssm-ID: 409568 [Multi-domain]  Cd Length: 90  Bit Score: 55.72  E-value: 1.55e-08
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 281359561 4994 GQSFTFDCKVSGEPAPQTKWLLKKKEVySKDNVKVTNVDYNTKLKVNSATRSDSGIYTVFAENANGEDSADVKVTV 5069
Cdd:cd20976    16 GQDFVAQCSARGKPVPRITWIRNAQPL-QYAADRSTCEAGVGELHIQDVLPEDHGTYTCLAKNAAGQVSCSAWVTV 90
fn3 pfam00041
Fibronectin type III domain;
3990-4075 1.56e-08

Fibronectin type III domain;


Pssm-ID: 394996 [Multi-domain]  Cd Length: 85  Bit Score: 55.50  E-value: 1.56e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561  3990 DTPGKPQIVDWSGNHCDLKWRAPEDdGGASITGYIVERKDPNTGKWQKALETSTPDCKARVNDLIAGNKYQFRIMAVNKA 4069
Cdd:pfam00041    1 SAPSNLTVTDVTSTSLTVSWTPPPD-GNGPITGYEVEYRPKNSGEPWNEITVPGTTTSVTLTGLKPGTEYEVRVQAVNGG 79

                   ....*.
gi 281359561  4070 GKSKPS 4075
Cdd:pfam00041   80 GEGPPS 85
PKc_TESK cd14155
Catalytic domain of the Dual-specificity protein kinase, Testicular protein kinase; ...
7995-8175 1.57e-08

Catalytic domain of the Dual-specificity protein kinase, Testicular protein kinase; Dual-specificity PKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine as well as tyrosine residues on protein substrates. TESK proteins phosphorylate cofilin and induce actin cytoskeletal reorganization. In the Drosphila eye, TESK is required for epithelial cell organization. Mammals contain two TESK proteins, TESK1 and TESK2, which are highly expressed in testis and play roles in spermatogenesis. TESK1 is found in testicular germ cells while TESK2 is expressed mainly in nongerminal Sertoli cells. TESK1 is stimulated by integrin-mediated signaling pathways. It regulates cell spreading and focal adhesion formation. The TESK subfamily is part of a larger superfamily that includes the catalytic domains of other protein serine/threonine PKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271057 [Multi-domain]  Cd Length: 253  Bit Score: 59.80  E-value: 1.57e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 7995 IGTGAFGVVHRCRERSTGNIFAAKFIPVSHSVEKDLirREIDIMNQLHHQKLINLHDAFEDDDEMILILEFLSGGELfER 8074
Cdd:cd14155     1 IGSGFFSEVYKVRHRTSGQVMALKMNTLSSNRANML--REVQLMNRLSHPNILRFMGVCVHQGQLHALTEYINGGNL-EQ 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 8075 ITAEGYVMTEAEVINYMRQICEGIRHMHEQNIIHLDIKPEN--IMCQTRSSTNVkLIDFGLATRL----DPNEVVKiTTG 8148
Cdd:cd14155    78 LLDSNEPLSWTVRVKLALDIARGLSYLHSKGIFHRDLTSKNclIKRDENGYTAV-VGDFGLAEKIpdysDGKEKLA-VVG 155
                         170       180
                  ....*....|....*....|....*..
gi 281359561 8149 TAEFAAPEIVNREPVGFYTDMWATGVL 8175
Cdd:cd14155   156 SPYWMAPEVLRGEPYNEKADVFSYGII 182
IgI_Twitchin_like cd20949
C-terminal immunoglobulin-like domain of the myosin-associated giant protein kinase Twitchin, ...
7661-7730 1.73e-08

C-terminal immunoglobulin-like domain of the myosin-associated giant protein kinase Twitchin, and similar domains; member of the I-set IgSF domains; The members here are composed of the C-terminal immunoglobulin-like domain of the myosin-associated giant protein kinase Twitchin and similar proteins, including Caenorhabditis elegans and Aplysia californica Twitchin, Drosophila melanogaster Projectin, and similar proteins. These are very large muscle proteins containing multiple immunoglobulin (Ig)-like and fibronectin type III (FN3) domains and a single kinase domain near the C-terminus. In humans these proteins are called Titin. The Ig superfamily (IgSF) is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. The Ig-like domain of the Twitchin is a member of the I-set IgSF domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand but lack a C" strand. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors, the hemolymph protein hemolin, the muscle proteins (titin, telokin, and twitchin), the neuronal adhesion molecule axonin-1, and the signaling molecule semaphorin 4D.


Pssm-ID: 409541 [Multi-domain]  Cd Length: 89  Bit Score: 55.41  E-value: 1.73e-08
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 7661 QNHNAQFTCTINGVPKPTISWYKGAREISNGARYHMYSEGDNHFLNINDVFGEDADEYVCRAVNKAGAKS 7730
Cdd:cd20949    13 EGQSATILCEVKGEPQPNVTWHFNGQPISASVADMSKYRILADGLLINKVTQDDTGEYTCRAYQVNSIAS 82
IgI_Myotilin_C_like cd05744
Immunoglobulin (Ig)-like domain of myotilin, palladin, and myopalladin; member of the I-set of ...
438-532 2.07e-08

Immunoglobulin (Ig)-like domain of myotilin, palladin, and myopalladin; member of the I-set of Ig superfamily (IgSF) domains; The members here are composed of the immunoglobulin (Ig)-like domain in myotilin, palladin, and myopalladin. Myotilin, palladin, and myopalladin function as scaffolds that regulate actin organization. Myotilin and myopalladin are most abundant in skeletal and cardiac muscle; palladin is ubiquitously expressed in the organs of developing vertebrates and plays a key role in cellular morphogenesis. The three family members each interact with specific molecular partners with all three binding to alpha-actinin; In addition, palladin also binds to vasodilator-stimulated phosphoprotein (VASP) and ezrin, myotilin binds to filamin and actin, and myopalladin also binds to nebulin and cardiac ankyrin repeat protein (CARP). This group belongs to the I-set of IgSF domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand, but lack a C" strand.


Pssm-ID: 409405 [Multi-domain]  Cd Length: 91  Bit Score: 55.19  E-value: 2.07e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561  438 PSFIEKPRIIPNESGTLITMKCKCKAKPEPTVTWYRGQDLVEKSKKIKInttvIAEDTYELTLEIKDPGATDGGTYRCNV 517
Cdd:cd05744     1 PHFLQAPGDLEVQEGRLCRFDCKVSGLPTPDLFWQLNGKPVRPDSAHKM----LVRENGRHSLIIEPVTKRDAGIYTCIA 76
                          90
                  ....*....|....*
gi 281359561  518 KNEYGESNANLNLNI 532
Cdd:cd05744    77 RNRAGENSFNAELVV 91
IgI_Titin_like cd05747
Immunoglobulin (Ig)-like domain of human titin C terminus and similar proteins; member of the ...
2312-2390 2.10e-08

Immunoglobulin (Ig)-like domain of human titin C terminus and similar proteins; member of the I-set of Ig superfamily (IgSF) domains; The members here are composed of the fifth immunoglobulin (Ig)-like domain from the C-terminus of human titin x and similar proteins. Titin (also called connectin) is a fibrous sarcomeric protein specifically found in vertebrate striated muscle. Titin is gigantic; depending on isoform composition it ranges from 2970 to 3700 kDa, and is of a length that spans half a sarcomere. Titin largely consists of multiple repeats of Ig-like and fibronectin type 3 (FN-III)-like domains. Titin connects the ends of myosin thick filaments to Z disks and extends along the thick filament to the H zone and appears to function similar to an elastic band, keeping the myosin filaments centered in the sarcomere during muscle contraction or stretching. This group belongs to the I-set of IgSF domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand, but lack a C" strand.


Pssm-ID: 143224 [Multi-domain]  Cd Length: 92  Bit Score: 55.44  E-value: 2.10e-08
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 281359561 2312 KNVTVKKGQTIRFDIKYDGEPEPAATWVKGTDNLkFDNQRICLDQLERNSSITIKKSVRKDTGKYKLVLSNSSGTIESE 2390
Cdd:cd05747    11 RSLTVSEGESARFSCDVDGEPAPTVTWMREGQII-VSSQRHQITSTEYKSTFEISKVQMSDEGNYTVVVENSEGKQEAQ 88
IgI_4_hemolin-like cd20978
Fourth immunoglobulin (Ig)-like domain of hemolin, and similar domains; a member of the I-set ...
544-636 2.19e-08

Fourth immunoglobulin (Ig)-like domain of hemolin, and similar domains; a member of the I-set of IgSF domains; The members here are composed of the fourth immunoglobulin (Ig)-like domain of hemolin and similar proteins. Hemolin, an insect immunoglobulin superfamily (IgSF) member containing four Ig-like domains, is a lipopolysaccharide-binding immune protein induced during bacterial infection. Hemolin shares significant sequence similarity with the first four Ig-like domains of the transmembrane cell adhesion molecules (CAMs) of the L1 family. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. The fourth Ig-like domain of hemolin is a member of the I-set Ig domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set domains, members of the I-set have a discontinuous A strand but lack a C" strand. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors, the muscle proteins titin, telokin, and twitchin, the neuronal adhesion molecule axonin-1, and the signaling molecule semaphorin 4D that is involved in axonal guidance, immune function and angiogenesis.


Pssm-ID: 409570 [Multi-domain]  Cd Length: 88  Bit Score: 55.09  E-value: 2.19e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561  544 TFIEKPRI-VSENNGKLVIMECKVKADPKPDVIWFRNGEVIKESNKIKTFIEQRgdqyyikLELLDPQLEDSGLYKCNIK 622
Cdd:cd20978     2 KFIQKPEKnVVVKGGQDVTLPCQVTGVPQPKITWLHNGKPLQGPMERATVEDGT-------LTIINVQPEDTGYYGCVAT 74
                          90
                  ....*....|....
gi 281359561  623 NTLGELNANLTLNI 636
Cdd:cd20978    75 NEIGDIYTETLLHV 88
PTKc_Ror cd05048
Catalytic Domain of the Protein Tyrosine Kinases, Receptor tyrosine kinase-like Orphan ...
7979-8201 2.19e-08

Catalytic Domain of the Protein Tyrosine Kinases, Receptor tyrosine kinase-like Orphan Receptors; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. The Ror subfamily consists of Ror1, Ror2, and similar proteins. Ror proteins are orphan receptor PTKs (RTKs) containing an extracellular region with immunoglobulin-like, cysteine-rich, and kringle domains, a transmembrane segment, and an intracellular catalytic domain. Ror RTKs are unrelated to the nuclear receptor subfamily called retinoid-related orphan receptors (RORs). RTKs are usually activated through ligand binding, which causes dimerization and autophosphorylation of the intracellular tyr kinase catalytic domain. Ror kinases are expressed in many tissues during development. They play important roles in bone and heart formation. Mutations in human Ror2 result in two different bone development genetic disorders, recessive Robinow syndrome and brachydactyly type B. Drosophila Ror is expressed only in the developing nervous system during neurite outgrowth and neuronal differentiation, suggesting a role for Drosophila Ror in neural development. More recently, mouse Ror1 and Ror2 have also been found to play an important role in regulating neurite growth in central neurons. Ror1 and Ror2 are believed to have some overlapping and redundant functions. The Ror subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270642 [Multi-domain]  Cd Length: 283  Bit Score: 59.70  E-value: 2.19e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 7979 EISQQSVydRYdiLEEIGTGAFGVVHRCR-----ERSTGNIFAAKFIPVSHSVE-KDLIRREIDIMNQLHHQKLINLHDA 8052
Cdd:cd05048     1 EIPLSAV--RF--LEELGEGAFGKVYKGEllgpsSEESAISVAIKTLKENASPKtQQDFRREAELMSDLQHPNIVCLLGV 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 8053 FEDDDEMILILEFLSGGELFERI---------------TAEGYVMTEAEVINYMRQICEGIRHMHEQNIIHLDIKPENIM 8117
Cdd:cd05048    77 CTKEQPQCMLFEYMAHGDLHEFLvrhsphsdvgvssddDGTASSLDQSDFLHIAIQIAAGMEYLSSHHYVHRDLAARNCL 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 8118 cqTRSSTNVKLIDFGLAT--------RLDPNEVVKIttgtaEFAAPEIVNREPVGFYTDMWATGVLSYVLLS-GLSPFAG 8188
Cdd:cd05048   157 --VGDGLTVKISDFGLSRdiyssdyyRVQSKSLLPV-----RWMPPEAILYGKFTTESDVWSFGVVLWEIFSyGLQPYYG 229
                         250
                  ....*....|...
gi 281359561 8189 DNDVQTLKNVKAC 8201
Cdd:cd05048   230 YSNQEVIEMIRSR 242
IgI_1_Titin_Z1z2-like cd20974
First Ig-like domain of the giant muscle protein titin Z1z2 in the sarcomeric Z-disk and ...
8437-8516 2.22e-08

First Ig-like domain of the giant muscle protein titin Z1z2 in the sarcomeric Z-disk and similar proteins; a member of the I-set of IgSF domains; The members here are composed of the first immunoglobulin (Ig)-like domain of the giant muscle protein titin Z1z2 in the sarcomeric Z-disk and similar proteins. Titin is a key component in the assembly and functioning of vertebrate striated muscles. By providing connections at the level of individual microfilaments, it contributes to the fine balance of forces between the two halves of the sarcomere. The Ig superfamily (IgSF) is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. Unlike the V-set, one of the distinctive features of I-set domains is the lack of a C" strand. The structure of the titin Z1z2 lacks this strand and thus it belongs to the I-set of the IgSF. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors, the hemolymph protein hemolin, the muscle proteins titin, telokin, and twitchin, the neuronal adhesion molecule axonin-1, and the signaling molecule semaphorin 4D that is involved in axonal guidance, immune function and angiogenesis.


Pssm-ID: 409566 [Multi-domain]  Cd Length: 93  Bit Score: 55.44  E-value: 2.22e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 8437 PSFTFLLRPRVMQARDTCKLLCCLSGKPVPNVRWYKDGRELSKYE---YAMTHSDGVVTMEIIDCKPSDSGKYSCKATNC 8513
Cdd:cd20974     1 PVFTQPLQSVVVLEGSTATFEAHVSGKPVPEVSWFRDGQVISTSTlpgVQISFSDGRAKLSIPAVTKANSGRYSLTATNG 80

                  ...
gi 281359561 8514 HGT 8516
Cdd:cd20974    81 SGQ 83
IgI_Myotilin_C cd05892
C-terminal immunoglobulin (Ig)-like domain of myotilin; member of the I-set of Ig superfamily ...
6175-6245 2.31e-08

C-terminal immunoglobulin (Ig)-like domain of myotilin; member of the I-set of Ig superfamily (IgSF) domains; The members here are composed of the C-terminal immunoglobulin (Ig)-like domain of myotilin. Mytolin belongs to the palladin-myotilin-myopalladin family. Proteins belonging to the latter family contain multiple Ig-like domains and function as scaffolds, modulating the actin cytoskeleton. Myotilin is most abundant in skeletal and cardiac muscle and is involved in maintaining sarcomere integrity. It binds to alpha-actinin, filamin, and actin. Mutations in myotilin lead to muscle disorders. This group belongs to the I-set of IgSF domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand, but lack a C" strand.


Pssm-ID: 409473  Cd Length: 92  Bit Score: 55.16  E-value: 2.31e-08
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 281359561 6175 IKVRAGEPVNLNIPISGAPTPTIEWKRGDLKLEEG-KRIS-YETNSERTLFRIDDSNRRDSGKYTVTAANEFG 6245
Cdd:cd05892    10 KKVLEGDPVRLECQISAIPPPQIFWKKNNEMLQYNtDRISlYQDNCGRICLLIQNANKKDAGWYTVSAVNEAG 82
IgI_1_MuSK cd20970
agrin-responsive first immunoglobulin-like domains (Ig1) of the MuSK ectodomain; a member of ...
7259-7331 2.69e-08

agrin-responsive first immunoglobulin-like domains (Ig1) of the MuSK ectodomain; a member of the I-set of IgSF domains; The members here are composed of the first immunoglobulin-like domains (Ig1) of the Muscle-specific kinase (MuSK). MuSK is a receptor tyrosine kinase specifically expressed in skeletal muscle, where it plays a central role in the formation and maintenance of the neuromuscular junction (NMJ). MuSK is activated by agrin, a neuron-derived heparan sulfate proteoglycan. The activation of MUSK in myotubes regulates the formation of NMJs through the regulation of different processes including the specific expression of genes in subsynaptic nuclei, the reorganization of the actin cytoskeleton and the clustering of the acetylcholine receptors (AChR) in the postsynaptic membrane. The Ig superfamily (IgSF) is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. Unlike the V-set, one of the distinctive features of I-set domains is the lack of a C" strand. The structure of the MuSK lacks this strand and thus it belongs to the I-set of the IgSF. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors, the hemolymph protein hemolin, the muscle proteins titin, telokin, and twitchin, the neuronal adhesion molecule axonin-1, and the signaling molecule semaphorin 4D that is involved in axonal guidance, immune function and angiogenesis.


Pssm-ID: 409562 [Multi-domain]  Cd Length: 92  Bit Score: 54.82  E-value: 2.69e-08
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 281359561 7259 RLQDKVAPFGKDYTLQCAASGKPSPTARWLRNGKEIQM--NGGRMTCDSKDgvfrLHISNVQTGDDGDYTCEAMN 7331
Cdd:cd20970     8 PSFTVTAREGENATFMCRAEGSPEPEISWTRNGNLIIEfnTRYIVRENGTT----LTIRNIRRSDMGIYLCIASN 78
IgI_Myotilin_C_like cd05744
Immunoglobulin (Ig)-like domain of myotilin, palladin, and myopalladin; member of the I-set of ...
7254-7344 2.77e-08

Immunoglobulin (Ig)-like domain of myotilin, palladin, and myopalladin; member of the I-set of Ig superfamily (IgSF) domains; The members here are composed of the immunoglobulin (Ig)-like domain in myotilin, palladin, and myopalladin. Myotilin, palladin, and myopalladin function as scaffolds that regulate actin organization. Myotilin and myopalladin are most abundant in skeletal and cardiac muscle; palladin is ubiquitously expressed in the organs of developing vertebrates and plays a key role in cellular morphogenesis. The three family members each interact with specific molecular partners with all three binding to alpha-actinin; In addition, palladin also binds to vasodilator-stimulated phosphoprotein (VASP) and ezrin, myotilin binds to filamin and actin, and myopalladin also binds to nebulin and cardiac ankyrin repeat protein (CARP). This group belongs to the I-set of IgSF domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand, but lack a C" strand.


Pssm-ID: 409405 [Multi-domain]  Cd Length: 91  Bit Score: 54.81  E-value: 2.77e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 7254 PDWITRLQDKVAPFGKDYTLQCAASGKPSPTARWLRNGKEIQMNGGRMTCDSKDGVFRLHISNVQTGDDGDYTCEAMNSL 7333
Cdd:cd05744     1 PHFLQAPGDLEVQEGRLCRFDCKVSGLPTPDLFWQLNGKPVRPDSAHKMLVRENGRHSLIIEPVTKRDAGIYTCIARNRA 80
                          90
                  ....*....|.
gi 281359561 7334 GFVNTSGYLKI 7344
Cdd:cd05744    81 GENSFNAELVV 91
IgI_telokin-like cd20973
immunoglobulin-like domain of telokin and similar proteins; a member of the I-set of IgSF ...
4983-5069 2.83e-08

immunoglobulin-like domain of telokin and similar proteins; a member of the I-set of IgSF domains; The members here are composed of the immunoglobulin (Ig) domain in telokin, the C-terminal domain of myosin light chain kinase which is identical to telokin, and similar proteins. The Ig superfamily (IgSF) is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. Unlike the V-set, one of the distinctive features of I-set domains is the lack of a C" strand. The structure of the telokin Ig domain lacks this strand and thus it belongs to the I-set of the IgSF. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors, the hemolymph protein hemolin, the muscle proteins titin, telokin, and twitchin, the neuronal adhesion molecule axonin-1, and the signaling molecule semaphorin 4D that is involved in axonal guidance, immune function and angiogenesis.


Pssm-ID: 409565 [Multi-domain]  Cd Length: 88  Bit Score: 54.89  E-value: 2.83e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 4983 RSSLVEVRIKAGQSFTFDCKVSGEPAPQTKWLLKKKEVYSKDNVK-VTNVDYNTKLKVNSATRSDSGIYTVFAENANGED 5061
Cdd:cd20973     1 IQTLRDKEVVEGSAARFDCKVEGYPDPEVKWMKDDNPIVESRRFQiDQDEDGLCSLIISDVCGDDSGKYTCKAVNSLGEA 80

                  ....*...
gi 281359561 5062 SADVKVTV 5069
Cdd:cd20973    81 TCSAELTV 88
IgI_4_Dscam cd20956
Fourth immunoglobulin domain of the Drosophila melanogaster Dscam protein, and similar domains; ...
8642-8721 2.85e-08

Fourth immunoglobulin domain of the Drosophila melanogaster Dscam protein, and similar domains; a member of the I-set of IgSF domains; The members here are composed of the fourth immunoglobulin domain of the Drosophila melanogaster Down syndrome cell adhesion molecule (DSCAM) protein and similar proteins. Down syndrome cell adhesion molecule (DSCAM) is a cell adhesion molecule that plays critical roles in neural development, including axon guidance and branching, axon target recognition, self-avoidance and synaptic formation. DSCAM belongs to the immunoglobulin superfamily and contributes to defects in the central nervous system in Down syndrome patients. Vertebrate DSCAMs differ from Drosophila Dscam1 in that they lack the extensive alternative splicing that occurs in the insect gene. Drosophila melanogaster Dscam has 38,016 isoforms generated by the alternative splicing of four variable exon clusters, which allows every neuron in the fly to display a distinctive set of Dscam proteins on its cell surface. Drosophila Dscam1 is a cell-surface protein that plays important roles in neural development and axon tiling of neurons. It is shown that thousands of isoforms bind themselves through specific homophilic (self-binding) interactions, a process which mediates cellular self-recognition. Drosophila Dscam2 is also alternatively spliced and plays a key role in the development of two visual system neurons, monopolar cells L1 and L2. This group is a member of the I-set Ig domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand but lack a C" strand.


Pssm-ID: 409548 [Multi-domain]  Cd Length: 96  Bit Score: 54.87  E-value: 2.85e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 8642 TIHDGEQLILTCYVKGDPEPQISWSKNGKSLSSSDildlRYKNG---------IATLTINEVFPEDEGVITCTATNSVGA 8712
Cdd:cd20956    12 TLQPGPSVSLKCVASGNPLPQITWTLDGFPIPESP----RFRVGdyvtsdgdvVSYVNISSVRVEDGGEYTCTATNDVGS 87

                  ....*....
gi 281359561 8713 VETKCKLTI 8721
Cdd:cd20956    88 VSHSARINV 96
IG_like smart00410
Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.
3810-3885 3.01e-08

Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.


Pssm-ID: 214653 [Multi-domain]  Cd Length: 85  Bit Score: 54.43  E-value: 3.01e-08
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 281359561   3810 GQMLHIDALIKAEPPAKVTWTYNKTE-IKTSDHIKIENEDYKTTFIMPKVKRADRGIYIVTAKNDSGSDTVEVELEV 3885
Cdd:smart00410    9 GESVTLSCEASGSPPPEVTWYKQGGKlLAESGRFSVSRSGSTSTLTISNVTPEDSGTYTCAATNSSGSASSGTTLTV 85
APH_ChoK_like cd05120
Aminoglycoside 3'-phosphotransferase and Choline Kinase family; This family is composed of APH, ...
8025-8139 3.04e-08

Aminoglycoside 3'-phosphotransferase and Choline Kinase family; This family is composed of APH, ChoK, ethanolamine kinase (ETNK), macrolide 2'-phosphotransferase (MPH2'), an unusual homoserine kinase, and uncharacterized proteins with similarity to the N-terminal domain of acyl-CoA dehydrogenase 10 (ACAD10). The members of this family catalyze the transfer of the gamma-phosphoryl group from ATP (or CTP) to small molecule substrates such as aminoglycosides, macrolides, choline, ethanolamine, and homoserine. Phosphorylation of the antibiotics, aminoglycosides and macrolides, leads to their inactivation and to bacterial antibiotic resistance. Phosphorylation of choline, ethanolamine, and homoserine serves as precursors to the synthesis of important biological compounds, such as the major phospholipids, phosphatidylcholine and phosphatidylethanolamine and the amino acids, threonine, methionine, and isoleucine. The APH/ChoK family is part of a larger superfamily that includes the catalytic domains of other kinases, such as the typical serine/threonine/tyrosine protein kinases (PKs), RIO kinases, actin-fragmin kinase (AFK), and phosphoinositide 3-kinase (PI3K).


Pssm-ID: 270690 [Multi-domain]  Cd Length: 158  Bit Score: 56.93  E-value: 3.04e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 8025 SVEKDLIRREIDIMNQLHHQKLI---NLHDAFEDDDEMILILEFLSGgelfERITAEGYVMTEAEVINYMRQICEGIRHM 8101
Cdd:cd05120    30 PRLKKDLEKEAAMLQLLAGKLSLpvpKVYGFGESDGWEYLLMERIEG----ETLSEVWPRLSEEEKEKIADQLAEILAAL 105
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 281359561 8102 HEQNI---IHLDIKPENIM--CQTRSStnvKLIDFGLATRLDP 8139
Cdd:cd05120   106 HRIDSsvlTHGDLHPGNILvkPDGKLS---GIIDWEFAGYGPP 145
IgI_1_MuSK cd20970
agrin-responsive first immunoglobulin-like domains (Ig1) of the MuSK ectodomain; a member of ...
4978-5069 3.08e-08

agrin-responsive first immunoglobulin-like domains (Ig1) of the MuSK ectodomain; a member of the I-set of IgSF domains; The members here are composed of the first immunoglobulin-like domains (Ig1) of the Muscle-specific kinase (MuSK). MuSK is a receptor tyrosine kinase specifically expressed in skeletal muscle, where it plays a central role in the formation and maintenance of the neuromuscular junction (NMJ). MuSK is activated by agrin, a neuron-derived heparan sulfate proteoglycan. The activation of MUSK in myotubes regulates the formation of NMJs through the regulation of different processes including the specific expression of genes in subsynaptic nuclei, the reorganization of the actin cytoskeleton and the clustering of the acetylcholine receptors (AChR) in the postsynaptic membrane. The Ig superfamily (IgSF) is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. Unlike the V-set, one of the distinctive features of I-set domains is the lack of a C" strand. The structure of the MuSK lacks this strand and thus it belongs to the I-set of the IgSF. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors, the hemolymph protein hemolin, the muscle proteins titin, telokin, and twitchin, the neuronal adhesion molecule axonin-1, and the signaling molecule semaphorin 4D that is involved in axonal guidance, immune function and angiogenesis.


Pssm-ID: 409562 [Multi-domain]  Cd Length: 92  Bit Score: 54.82  E-value: 3.08e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 4978 PPIIDRSSLVEVRIKAGQSFTFDCKVSGEPAPQTKWLLKKKEVySKDNVKVTNVDYNTKLKVNSATRSDSGIYTVFAEN- 5056
Cdd:cd20970     1 PVISTPQPSFTVTAREGENATFMCRAEGSPEPEISWTRNGNLI-IEFNTRYIVRENGTTLTIRNIRRSDMGIYLCIASNg 79
                          90
                  ....*....|...
gi 281359561 5057 ANGEDSADVKVTV 5069
Cdd:cd20970    80 VPGSVEKRITLQV 92
IgI_4_Dscam cd20956
Fourth immunoglobulin domain of the Drosophila melanogaster Dscam protein, and similar domains; ...
7268-7344 3.11e-08

Fourth immunoglobulin domain of the Drosophila melanogaster Dscam protein, and similar domains; a member of the I-set of IgSF domains; The members here are composed of the fourth immunoglobulin domain of the Drosophila melanogaster Down syndrome cell adhesion molecule (DSCAM) protein and similar proteins. Down syndrome cell adhesion molecule (DSCAM) is a cell adhesion molecule that plays critical roles in neural development, including axon guidance and branching, axon target recognition, self-avoidance and synaptic formation. DSCAM belongs to the immunoglobulin superfamily and contributes to defects in the central nervous system in Down syndrome patients. Vertebrate DSCAMs differ from Drosophila Dscam1 in that they lack the extensive alternative splicing that occurs in the insect gene. Drosophila melanogaster Dscam has 38,016 isoforms generated by the alternative splicing of four variable exon clusters, which allows every neuron in the fly to display a distinctive set of Dscam proteins on its cell surface. Drosophila Dscam1 is a cell-surface protein that plays important roles in neural development and axon tiling of neurons. It is shown that thousands of isoforms bind themselves through specific homophilic (self-binding) interactions, a process which mediates cellular self-recognition. Drosophila Dscam2 is also alternatively spliced and plays a key role in the development of two visual system neurons, monopolar cells L1 and L2. This group is a member of the I-set Ig domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand but lack a C" strand.


Pssm-ID: 409548 [Multi-domain]  Cd Length: 96  Bit Score: 54.87  E-value: 3.11e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 7268 GKDYTLQCAASGKPSPTARWLRNGKEIQMNGGRMTCD--SKDG--VFRLHISNVQTGDDGDYTCEAMNSLGFVNTSGYLK 7343
Cdd:cd20956    16 GPSVSLKCVASGNPLPQITWTLDGFPIPESPRFRVGDyvTSDGdvVSYVNISSVRVEDGGEYTCTATNDVGSVSHSARIN 95

                  .
gi 281359561 7344 I 7344
Cdd:cd20956    96 V 96
fn3 pfam00041
Fibronectin type III domain;
4780-4863 3.18e-08

Fibronectin type III domain;


Pssm-ID: 394996 [Multi-domain]  Cd Length: 85  Bit Score: 54.34  E-value: 3.18e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561  4780 SPPnGPLQISDVHKEGCHLKWKRPSDDGGtPIEYFQIDKLEPETGCWIPSCR--STEPQVDVTGLSPGNEYKFRVSAVNA 4857
Cdd:pfam00041    1 SAP-SNLTVTDVTSTSLTVSWTPPPDGNG-PITGYEVEYRPKNSGEPWNEITvpGTTTSVTLTGLKPGTEYEVRVQAVNG 78

                   ....*.
gi 281359561  4858 EGESQP 4863
Cdd:pfam00041   79 GGEGPP 84
Ig_Pro_neuregulin cd05750
Immunoglobulin (Ig)-like domain in neuregulins; The members here are composed of the ...
7259-7344 3.23e-08

Immunoglobulin (Ig)-like domain in neuregulins; The members here are composed of the immunoglobulin (Ig)-like domain in neuregulins (NRGs). NRGs are signaling molecules which participate in cell-cell interactions in the nervous system, breast, heart, and other organ systems, and are implicated in the pathology of diseases including schizophrenia, multiple sclerosis, and breast cancer. There are four members of the neuregulin gene family (NRG-1, NRG-2, NRG-3, and NRG-4). The NRG-1 protein, binds to and activates the tyrosine kinases receptors ErbB3 and ErbB4, initiating signaling cascades. The other NRGs proteins bind one or the other or both of these ErbBs. NRG-1 has multiple functions: in the brain it regulates various processes such as radial glia formation and neuronal migration, dendritic development, and expression of neurotransmitters receptors, while in the peripheral nervous system NRG-1 regulates processes such as target cell differentiation, and Schwann cell survival. There are many NRG-1 isoforms which arise from the alternative splicing of mRNA. Less is known of the functions of the other NRGs. NRG-2 and NRG-3 are expressed predominantly in the nervous system. NRG-2 is expressed by motor neurons and terminal Schwann cells, and is concentrated near synaptic sites and may be a signal that regulates synaptic differentiation. NRG-4 has been shown to direct pancreatic islet cell development towards the delta-cell lineage.


Pssm-ID: 409408 [Multi-domain]  Cd Length: 92  Bit Score: 54.82  E-value: 3.23e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 7259 RLQDKVAPFGKDYTLQC-AASGKPSPTARWLRNGKEIQMNGG-RMTCDSKDGVFRLHISNVQTGDDGDYTCEAMNSLGFV 7336
Cdd:cd05750     5 EMKSQTVQEGSKLVLKCeATSENPSPRYRWFKDGKELNRKRPkNIKIRNKKKNSELQINKAKLEDSGEYTCVVENILGKD 84

                  ....*...
gi 281359561 7337 NTSGYLKI 7344
Cdd:cd05750    85 TVTGNVTV 92
Ig3_Peroxidasin cd05745
Third immunoglobulin (Ig)-like domain of peroxidasin; The members here are composed of the ...
7661-7737 3.49e-08

Third immunoglobulin (Ig)-like domain of peroxidasin; The members here are composed of the third immunoglobulin (Ig)-like domain in peroxidasin. Peroxidasin has a peroxidase domain and interacting extracellular motifs containing four Ig-like domains. It has been suggested that peroxidasin is secreted and has functions related to the stabilization of the extracellular matrix. It may play a part in various other important processes such as removal and destruction of cells which have undergone programmed cell death and protection of the organism against non-self.


Pssm-ID: 143222 [Multi-domain]  Cd Length: 74  Bit Score: 54.17  E-value: 3.49e-08
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 281359561 7661 QNHNAQFTCTINGVPKPTISWYKGAREISNGARYHMYSEGDnhfLNINDVFGEDADEYVCRAVNKAGAKSTRATLAI 7737
Cdd:cd05745     1 EGQTVDFLCEAQGYPQPVIAWTKGGSQLSVDRRHLVLSSGT---LRISRVALHDQGQYECQAVNIVGSQRTVAQLTV 74
IG_like smart00410
Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.
6864-6946 3.52e-08

Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.


Pssm-ID: 214653 [Multi-domain]  Cd Length: 85  Bit Score: 54.43  E-value: 3.52e-08
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561   6864 RDMTVIAGDEFRITVPYHASPRPTASWSLNGLE-VIPGERIKFDSNDYASMYYNKSAKRDETGSYTITLTNNKGSDTASC 6942
Cdd:smart00410    2 PSVTVKEGESVTLSCEASGSPPPEVTWYKQGGKlLAESGRFSVSRSGSTSTLTISNVTPEDSGTYTCAATNSSGSASSGT 81

                    ....
gi 281359561   6943 HVTV 6946
Cdd:smart00410   82 TLTV 85
STKc_LIMK2 cd14222
Catalytic domain of the Serine/Threonine Kinase, LIM domain kinase 2; STKs catalyze the ...
7995-8134 3.57e-08

Catalytic domain of the Serine/Threonine Kinase, LIM domain kinase 2; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. LIMK2 activation is induced by transforming growth factor-beta l (TGFb-l) and shares the same subcellular location as the cofilin family member twinfilin, which may be its biological substrate. LIMK2 plays a role in spermatogenesis, and may contribute to tumor progression and metastasis formation in some cancer cells. LIMKs phosphorylate and inactivate cofilin, an actin depolymerizing factor, to induce the reorganization of the actin cytoskeleton. They act downstream of Rho GTPases and are expressed ubiquitously. As regulators of actin dynamics, they contribute to diverse cellular functions such as cell motility, morphogenesis, differentiation, apoptosis, meiosis, mitosis, and neurite extension. LIMKs contain the LIM (two repeats), PDZ, and catalytic kinase domains. The LIMK2 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271124 [Multi-domain]  Cd Length: 272  Bit Score: 58.80  E-value: 3.57e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 7995 IGTGAFGVVHRCRERSTGNIFAAK-FIPVSHSVEKDLIRrEIDIMNQLHHQKLINLHDAFEDDDEMILILEFLSGGELFE 8073
Cdd:cd14222     1 LGKGFFGQAIKVTHKATGKVMVMKeLIRCDEETQKTFLT-EVKVMRSLDHPNVLKFIGVLYKDKRLNLLTEFIEGGTLKD 79
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 281359561 8074 RITAEGYVMTEAEViNYMRQICEGIRHMHEQNIIHLDIKPENimCQTRSSTNVKLIDFGLA 8134
Cdd:cd14222    80 FLRADDPFPWQQKV-SFAKGIASGMAYLHSMSIIHRDLNSHN--CLIKLDKTVVVADFGLS 137
I-set pfam07679
Immunoglobulin I-set domain;
6855-6946 3.58e-08

Immunoglobulin I-set domain;


Pssm-ID: 400151 [Multi-domain]  Cd Length: 90  Bit Score: 54.57  E-value: 3.58e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561  6855 PKITSdlSIRDMTVIAGDEFRITVPYHASPRPTASWSLNGLEVIPGERIKFDSNDYASMYYNKSAKRDETGSYTITLTNN 6934
Cdd:pfam07679    1 PKFTQ--KPKDVEVQEGESARFTCTVTGTPDPEVSWFKDGQPLRSSDRFKVTYEGGTYTLTISNVQPDDSGKYTCVATNS 78
                           90
                   ....*....|..
gi 281359561  6935 KGSDTASCHVTV 6946
Cdd:pfam07679   79 AGEAEASAELTV 90
PTKc_Abl cd05052
Catalytic domain of the Protein Tyrosine Kinase, Abelson kinase; PTKs catalyze the transfer of ...
7987-8188 3.65e-08

Catalytic domain of the Protein Tyrosine Kinase, Abelson kinase; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Abl (or c-Abl) is a ubiquitously-expressed cytoplasmic (or nonreceptor) PTK that contains SH3, SH2, and tyr kinase domains in its N-terminal region, as well as nuclear localization motifs, a putative DNA-binding domain, and F- and G-actin binding domains in its C-terminal tail. It also contains a short autoinhibitory cap region in its N-terminus. Abl function depends on its subcellular localization. In the cytoplasm, Abl plays a role in cell proliferation and survival. In response to DNA damage or oxidative stress, Abl is transported to the nucleus where it induces apoptosis. In chronic myelogenous leukemia (CML) patients, an aberrant translocation results in the replacement of the first exon of Abl with the BCR (breakpoint cluster region) gene. The resulting BCR-Abl fusion protein is constitutively active and associates into tetramers, resulting in a hyperactive kinase sending a continuous signal. This leads to uncontrolled proliferation, morphological transformation and anti-apoptotic effects. BCR-Abl is the target of selective inhibitors, such as imatinib (Gleevec), used in the treatment of CML. Abl2, also known as ARG (Abelson-related gene), is thought to play a cooperative role with Abl in the proper development of the nervous system. The Tel-ARG fusion protein, resulting from reciprocal translocation between chromosomes 1 and 12, is associated with acute myeloid leukemia (AML). The TEL gene is a frequent fusion partner of other tyr kinase oncogenes, including Tel/Abl, Tel/PDGFRbeta, and Tel/Jak2, found in patients with leukemia and myeloproliferative disorders. The Abl subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270645 [Multi-domain]  Cd Length: 263  Bit Score: 58.97  E-value: 3.65e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 7987 DRYDIL--EEIGTGAFGVVHRCRERSTGNIFAAKFIPVSHSVEKDLIRrEIDIMNQLHHQKLINLHDAFEDDDEMILILE 8064
Cdd:cd05052     4 ERTDITmkHKLGGGQYGEVYEGVWKKYNLTVAVKTLKEDTMEVEEFLK-EAAVMKEIKHPNLVQLLGVCTREPPFYIITE 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 8065 FLSGGELFERITAEGYVMTEAEVINYM-RQICEGIRHMHEQNIIHLDIKPENimCQTRSSTNVKLIDFGLAtRLDPNEVV 8143
Cdd:cd05052    83 FMPYGNLLDYLRECNREELNAVVLLYMaTQIASAMEYLEKKNFIHRDLAARN--CLVGENHLVKVADFGLS-RLMTGDTY 159
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|
gi 281359561 8144 KITTGtAEF----AAPEIVNREPVGFYTDMWATGVLSYVLLS-GLSPFAG 8188
Cdd:cd05052   160 TAHAG-AKFpikwTAPESLAYNKFSIKSDVWAFGVLLWEIATyGMSPYPG 208
IG_like smart00410
Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.
557-636 3.92e-08

Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.


Pssm-ID: 214653 [Multi-domain]  Cd Length: 85  Bit Score: 54.43  E-value: 3.92e-08
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561    557 GKLVIMECKVKADPKPDVIWFRNG-EVIKESNKIKtfIEQRGDQYYikLELLDPQLEDSGLYKCNIKNTLGELNANLTLN 635
Cdd:smart00410    9 GESVTLSCEASGSPPPEVTWYKQGgKLLAESGRFS--VSRSGSTST--LTISNVTPEDSGTYTCAATNSSGSASSGTTLT 84

                    .
gi 281359561    636 I 636
Cdd:smart00410   85 V 85
PK_SCY1_like cd14011
Pseudokinase domain of Scy1-like proteins; The pseudokinase domain shows similarity to protein ...
8079-8244 3.98e-08

Pseudokinase domain of Scy1-like proteins; The pseudokinase domain shows similarity to protein kinases but lacks crucial residues for catalytic activity. This subfamily is composed of the catalytically inactive kinases with similarity to yeast Scy1. It includes four mammalian proteins called SCY1-like protein 1 (SCYL1), SCYL2, SCYL3, as well as Testis-EXpressed protein 14 (TEX14). SCYL1 binds to and co-localizes with the membrane trafficking coatomer I (COPI) complex, and regulates COPI-mediated vesicle trafficking. Null mutations in the SCYL1 gene are responsible for the pathology in mdf (muscle-deficient) mice which display progressive motor neuropathy. SCYL2, also called coated vesicle-associated kinase of 104 kDa (CVAK104), is involved in the trafficking of clathrin-coated vesicles. It also binds the HIV-1 accessory protein Vpu and acts as a regulatory factor that promotes the dephosphorylation of Vpu, facilitating the restriction of HIV-1 release. SCYL3, also called ezrin-binding protein PACE-1, may be involved in regulating cell adhesion and migration. TEX14 is required for spermatogenesis and male fertility. It localizes to kinetochores (KT) during mitosis and is a target of the mitotic kinase PLK1. It regulates the maturation of the outer KT and the KT-microtubule attachment. The SCY1-like subfamily is part of a larger superfamily that includes the catalytic domains of other protein serine/threonine kinases, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270913 [Multi-domain]  Cd Length: 287  Bit Score: 58.87  E-value: 3.98e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 8079 GYVMTEAEVINYMRQICEGIRHMH-EQNIIHLDIKPENIMCQTRSSTnvKLIDFGLAT-------------RLDPNeVVK 8144
Cdd:cd14011   108 DYKLYDVEIKYGLLQISEALSFLHnDVKLVHGNICPESVVINSNGEW--KLAGFDFCIsseqatdqfpyfrEYDPN-LPP 184
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 8145 ITTGTAEFAAPEIVNREPVGFYTDMWATGVLSYVLLSGLSPFAGDNDVQTLKNVKACDWDF-DVESFKYISEEAKDFIRK 8223
Cdd:cd14011   185 LAQPNLNYLAPEYILSKTCDPASDMFSLGVLIYAIYNKGKPLFDCVNNLLSYKKNSNQLRQlSLSLLEKVPEELRDHVKT 264
                         170       180
                  ....*....|....*....|.
gi 281359561 8224 LLVRNKEKRMTAHECLLHPWL 8244
Cdd:cd14011   265 LLNVTPEVRPDAEQLSKIPFF 285
Ig_Titin_like cd05748
Immunoglobulin (Ig)-like domain of titin and similar proteins; The members here are composed ...
8460-8525 4.03e-08

Immunoglobulin (Ig)-like domain of titin and similar proteins; The members here are composed of the immunoglobulin (Ig)-like domain found in titin-like proteins and similar proteins. Titin (also called connectin) is a fibrous sarcomeric protein specifically found in vertebrate striated muscle. Titin is a giant protein; depending on isoform composition, it ranges from 2970 to 3700 kDa, and is of a length that spans half a sarcomere. Titin largely consists of multiple repeats of Ig-like and fibronectin type 3 (FN-III)-like domains. Titin connects the ends of myosin thick filaments to Z disks and extends along the thick filament to the H zone. It appears to function similarly to an elastic band, keeping the myosin filaments centered in the sarcomere during muscle contraction or stretching. Within the sarcomere, titin is also attached to or is associated with myosin binding protein C (MyBP-C). MyBP-C appears to contribute to the generation of passive tension by titin and like titin has repeated Ig-like and FN-III domains. Also included in this group are worm twitchin and insect projectin, thick filament proteins of invertebrate muscle which also have repeated Ig-like and FN-III domains.


Pssm-ID: 409406 [Multi-domain]  Cd Length: 82  Bit Score: 54.13  E-value: 4.03e-08
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 281359561 8460 LSGKPVPNVRWYKDGRELSKYEYAMTHSDGVVTMEIID-CKPSDSGKYSCKATNCHGTDETDCVVIV 8525
Cdd:cd05748    16 IKGRPTPTVTWSKDGQPLKETGRVQIETTASSTSLVIKnAKRSDSGKYTLTLKNSAGEKSATINVKV 82
fn3 pfam00041
Fibronectin type III domain;
3599-3677 4.22e-08

Fibronectin type III domain;


Pssm-ID: 394996 [Multi-domain]  Cd Length: 85  Bit Score: 54.34  E-value: 4.22e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561  3599 GPLQVNDITKHSCKLKWEKPDDdGGSPIDYYEIEKLDPHTGQ-WLPC-GKSTEPEAKVIGLHEGKAYKFRVRAVNKEGES 3676
Cdd:pfam00041    4 SNLTVTDVTSTSLTVSWTPPPD-GNGPITGYEVEYRPKNSGEpWNEItVPGTTTSVTLTGLKPGTEYEVRVQAVNGGGEG 82

                   .
gi 281359561  3677 E 3677
Cdd:pfam00041   83 P 83
Ig_C5_MyBP-C cd05894
C5 immunoglobulin (Ig) domain of cardiac myosin binding protein C (MyBP-C); The members here ...
4404-4480 4.23e-08

C5 immunoglobulin (Ig) domain of cardiac myosin binding protein C (MyBP-C); The members here are composed of the C5 immunoglobulin (Ig) domain of cardiac myosin binding protein C (MyBP-C). MyBP-C consists of repeated domains, Ig and fibronectin type 3, and various linkers. Three isoforms of MYBP-C exist: slow-skeletal (ssMyBP-C), fast-skeletal (fsMyBP-C), and cardiac (cMyBP-C). cMYBP-C has insertions between and inside domains and an additional cardiac-specific Ig domain at the N-terminus. For cMYBP_C an interaction has been demonstrated between this C5 domain and the Ig C8 domain.


Pssm-ID: 409475  Cd Length: 86  Bit Score: 54.08  E-value: 4.23e-08
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 281359561 4404 SGEPIFLDINISGEPAPDVTWNQNNKSVQTTS-FSHIENLPYNTKYINNNPERKDTGLYKISAHNFYGQDQVEFQINI 4480
Cdd:cd05894     9 AGNKLRLDVPISGEPAPTVTWSRGDKAFTATEgRVRVESYKDLSSFVIEGAEREDEGVYTITVTNPVGEDHASLFVKV 86
Ig_2 pfam13895
Immunoglobulin domain; This domain contains immunoglobulin-like domains.
8739-8829 4.28e-08

Immunoglobulin domain; This domain contains immunoglobulin-like domains.


Pssm-ID: 464026 [Multi-domain]  Cd Length: 79  Bit Score: 53.94  E-value: 4.28e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561  8739 APKIVShlESRFVRDGDAVNLACRIIGAQHFDVVWLHNNKEIKPSKDFqYTNEANiyrlqiaeifPEDGGTYTCEAFND- 8817
Cdd:pfam13895    1 KPVLTP--SPTVVTEGEPVTLTCSAPGNPPPSYTWYKDGSAISSSPNF-FTLSVS----------AEDSGTYTCVARNGr 67
                           90
                   ....*....|..
gi 281359561  8818 IGESFSTCTINV 8829
Cdd:pfam13895   68 GGKVSNPVELTV 79
IG_like smart00410
Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.
4098-4181 4.41e-08

Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.


Pssm-ID: 214653 [Multi-domain]  Cd Length: 85  Bit Score: 54.05  E-value: 4.41e-08
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561   4098 KDITIKAGQHIRFDIKVSGEPPATKVWLHNKARLENDDSNYNIDMESYRTKLTVPISKRFHSGKYTLKAENESGRDEASF 4177
Cdd:smart00410    2 PSVTVKEGESVTLSCEASGSPPPEVTWYKQGGKLLAESGRFSVSRSGSTSTLTISNVTPEDSGTYTCAATNSSGSASSGT 81

                    ....
gi 281359561   4178 EVIV 4181
Cdd:smart00410   82 TLTV 85
IG_like smart00410
Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.
1750-1821 4.54e-08

Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.


Pssm-ID: 214653 [Multi-domain]  Cd Length: 85  Bit Score: 54.05  E-value: 4.54e-08
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 281359561   1750 TLECSVSSS-MANVHWFKNNTKLESDDPRYLISKDiNGNLKLIIKDSVLDDAGLYRCQLDKQPDKTECNLKVT 1821
Cdd:smart00410   13 TLSCEASGSpPPEVTWYKQGGKLLAESGRFSVSRS-GSTSTLTISNVTPEDSGTYTCAATNSSGSASSGTTLT 84
IgI_1_Titin_Z1z2-like cd20974
First Ig-like domain of the giant muscle protein titin Z1z2 in the sarcomeric Z-disk and ...
2612-2694 4.57e-08

First Ig-like domain of the giant muscle protein titin Z1z2 in the sarcomeric Z-disk and similar proteins; a member of the I-set of IgSF domains; The members here are composed of the first immunoglobulin (Ig)-like domain of the giant muscle protein titin Z1z2 in the sarcomeric Z-disk and similar proteins. Titin is a key component in the assembly and functioning of vertebrate striated muscles. By providing connections at the level of individual microfilaments, it contributes to the fine balance of forces between the two halves of the sarcomere. The Ig superfamily (IgSF) is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. Unlike the V-set, one of the distinctive features of I-set domains is the lack of a C" strand. The structure of the titin Z1z2 lacks this strand and thus it belongs to the I-set of the IgSF. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors, the hemolymph protein hemolin, the muscle proteins titin, telokin, and twitchin, the neuronal adhesion molecule axonin-1, and the signaling molecule semaphorin 4D that is involved in axonal guidance, immune function and angiogenesis.


Pssm-ID: 409566 [Multi-domain]  Cd Length: 93  Bit Score: 54.28  E-value: 4.57e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 2612 VTIKSGRTHKWSVDVLGEPIPELHWSW-RDDIPLTNGDRIKIENVDYHTDFSITNVLRKDSGFYTLKAENRNGIDRETVE 2690
Cdd:cd20974    10 VVVLEGSTATFEAHVSGKPVPEVSWFRdGQVISTSTLPGVQISFSDGRAKLSIPAVTKANSGRYSLTATNGSGQATSTAE 89

                  ....
gi 281359561 2691 LVVL 2694
Cdd:cd20974    90 LLVL 93
PK_TRB3 cd14024
Pseudokinase domain of Tribbles Homolog 3; The pseudokinase domain shows similarity to protein ...
8082-8244 5.06e-08

Pseudokinase domain of Tribbles Homolog 3; The pseudokinase domain shows similarity to protein kinases but lacks crucial residues for catalytic activity. TRB3 binds and regulates ATF4, p65/RelA, and PKB (or Akt). It negatively regulates ATF4-mediated gene expression including that of CHOP (C/EBP homologous protein) and HO-1, which are both involved in modulating apoptosis. It also inhibits insulin-mediated phosphorylation of PKB and is a possible determinant of insulin resistance and related disorders. In osteoarthritic chondrocytes where it inhibits insulin-like growth factor 1-mediated cell survival, TRB3 is overexpressed, resulting in increased cell death. TRB3 is one of three Tribbles Homolog (TRB) proteins present in vertebrates that are encoded by three separate genes. TRB proteins interact with many proteins involved in signalling pathways. They play scaffold-like regulatory functions and affect many cellular processes such as mitosis, apoptosis, and gene expression. The TRB3 subfamily is part of a larger superfamily that includes the catalytic domains of serine/threonine kinases, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270926 [Multi-domain]  Cd Length: 242  Bit Score: 57.97  E-value: 5.06e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 8082 MTEAEVINYMRQICEGIRHMHEQNIIHLDIKPENIMCQTRSSTNVKLIDFGLATRLD-PNEVVKITTGTAEFAAPEIVN- 8159
Cdd:cd14024    81 LSEDEARGLFTQMARAVAHCHQHGVILRDLKLRRFVFTDELRTKLVLVNLEDSCPLNgDDDSLTDKHGCPAYVGPEILSs 160
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 8160 -REPVGFYTDMWATGVLSYVLLSGLSPFAGDNDVQTLKNVKACDWDFDvesfKYISEEAKDFIRKLLVRNKEKRMTAHEC 8238
Cdd:cd14024   161 rRSYSGKAADVWSLGVCLYTMLLGRYPFQDTEPAALFAKIRRGAFSLP----AWLSPGARCLVSCMLRRSPAERLKASEI 236

                  ....*.
gi 281359561 8239 LLHPWL 8244
Cdd:cd14024   237 LLHPWL 242
Ig cd00096
Immunoglobulin domain; The members here are composed of the immunoglobulin (Ig) domain found ...
455-524 5.15e-08

Immunoglobulin domain; The members here are composed of the immunoglobulin (Ig) domain found in the Ig superfamily. The Ig superfamily is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. Members of this group are components of immunoglobulin, neuroglia, cell surface glycoproteins, including T-cell receptors, CD2, CD4, CD8, and membrane glycoproteins, including butyrophilin and chondroitin sulfate proteoglycan core protein. A predominant feature of most Ig domains is a disulfide bridge connecting the two beta-sheets with a tryptophan residue packed against the disulfide bond. Ig superfamily (IgSF) domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. Typically, the V-set domains have A, B, E, and D strands in one sheet and A', G, F, C, C' and C" in the other. The structures in C1-set are smaller than those in the V-set; they have one beta sheet that is formed by strands A, B, E, and D and the other by strands G, F, C, and C'. Moreover, a C1-set Ig domain contains a short C' strand (three residues) and lacks A' and C" strand. Unlike other Ig domain sets, C2-set structures do not have a D strand. Like the V-set Ig domains, members of the I-set have a discontinuous A strand, but lack a C" strand.


Pssm-ID: 409353 [Multi-domain]  Cd Length: 70  Bit Score: 53.49  E-value: 5.15e-08
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561  455 ITMKCKCKAKPEPTVTWYRGQDLVEKSKKIKINTtviaeDTYELTLEIKDPGATDGGTYRCNVKNEYGES 524
Cdd:cd00096     1 VTLTCSASGNPPPTITWYKNGKPLPPSSRDSRRS-----ELGNGTLTISNVTLEDSGTYTCVASNSAGGS 65
IgI_Titin_like cd05747
Immunoglobulin (Ig)-like domain of human titin C terminus and similar proteins; member of the ...
5856-5952 5.19e-08

Immunoglobulin (Ig)-like domain of human titin C terminus and similar proteins; member of the I-set of Ig superfamily (IgSF) domains; The members here are composed of the fifth immunoglobulin (Ig)-like domain from the C-terminus of human titin x and similar proteins. Titin (also called connectin) is a fibrous sarcomeric protein specifically found in vertebrate striated muscle. Titin is gigantic; depending on isoform composition it ranges from 2970 to 3700 kDa, and is of a length that spans half a sarcomere. Titin largely consists of multiple repeats of Ig-like and fibronectin type 3 (FN-III)-like domains. Titin connects the ends of myosin thick filaments to Z disks and extends along the thick filament to the H zone and appears to function similar to an elastic band, keeping the myosin filaments centered in the sarcomere during muscle contraction or stretching. This group belongs to the I-set of IgSF domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand, but lack a C" strand.


Pssm-ID: 143224 [Multi-domain]  Cd Length: 92  Bit Score: 54.28  E-value: 5.19e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 5856 IMAKPRYLppkIITPLNEVRIKCglifHTDihfiGEPAPEATWTLNSNPLLSNDRSTITSIGHHSVVHTVNCQRSDSGIY 5935
Cdd:cd05747     6 ILTKPRSL---TVSEGESARFSC----DVD----GEPAPTVTWMREGQIIVSSQRHQITSTEYKSTFEISKVQMSDEGNY 74
                          90
                  ....*....|....*..
gi 281359561 5936 HLLLRNSSGIDEGSFEL 5952
Cdd:cd05747    75 TVVVENSEGKQEAQFTL 91
PHA03209 PHA03209
serine/threonine kinase US3; Provisional
8037-8201 5.25e-08

serine/threonine kinase US3; Provisional


Pssm-ID: 177557 [Multi-domain]  Cd Length: 357  Bit Score: 59.50  E-value: 5.25e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 8037 IMNQLHHQKLINLHDAFEDDDEMILILEFLSGgELFERITAEGYVMTEAEVINYMRQICEGIRHMHEQNIIHLDIKPENI 8116
Cdd:PHA03209  110 LLQNVNHPSVIRMKDTLVSGAITCMVLPHYSS-DLYTYLTKRSRPLPIDQALIIEKQILEGLRYLHAQRIIHRDVKTENI 188
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 8117 MCQTRSStnVKLIDFGLA--TRLDPNEVVkiTTGTAEFAAPEIVNREPVGFYTDMWATGVLSYVLLSGLSPFAGDNDVQT 8194
Cdd:PHA03209  189 FINDVDQ--VCIGDLGAAqfPVVAPAFLG--LAGTVETNAPEVLARDKYNSKADIWSAGIVLFEMLAYPSTIFEDPPSTP 264

                  ....*..
gi 281359561 8195 LKNVKAC 8201
Cdd:PHA03209  265 EEYVKSC 271
Ig_3 pfam13927
Immunoglobulin domain; This family contains immunoglobulin-like domains.
3498-3577 5.26e-08

Immunoglobulin domain; This family contains immunoglobulin-like domains.


Pssm-ID: 464046 [Multi-domain]  Cd Length: 78  Bit Score: 53.72  E-value: 5.26e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561  3498 KPHIdRVNLKPVIVKTGLSISLDINIRGEPAPKVEWFFNNsSVTSDEHSVKIDNVDYNTKFFVMRAQRSQSGKYIIKATN 3577
Cdd:pfam13927    1 KPVI-TVSPSSVTVREGETVTLTCEATGSPPPTITWYKNG-EPISSGSTRSRSLSGSNSTLTISNVTRSDAGTYTCVASN 78
IgI_Myotilin_C_like cd05744
Immunoglobulin (Ig)-like domain of myotilin, palladin, and myopalladin; member of the I-set of ...
8740-8824 5.49e-08

Immunoglobulin (Ig)-like domain of myotilin, palladin, and myopalladin; member of the I-set of Ig superfamily (IgSF) domains; The members here are composed of the immunoglobulin (Ig)-like domain in myotilin, palladin, and myopalladin. Myotilin, palladin, and myopalladin function as scaffolds that regulate actin organization. Myotilin and myopalladin are most abundant in skeletal and cardiac muscle; palladin is ubiquitously expressed in the organs of developing vertebrates and plays a key role in cellular morphogenesis. The three family members each interact with specific molecular partners with all three binding to alpha-actinin; In addition, palladin also binds to vasodilator-stimulated phosphoprotein (VASP) and ezrin, myotilin binds to filamin and actin, and myopalladin also binds to nebulin and cardiac ankyrin repeat protein (CARP). This group belongs to the I-set of IgSF domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand, but lack a C" strand.


Pssm-ID: 409405 [Multi-domain]  Cd Length: 91  Bit Score: 54.04  E-value: 5.49e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 8740 PKIVSHLESRFVRDGDAVNLACRIIGAQHFDVVWLHNNKEIKP-SKDFQYTNEANIYRLQIAEIFPEDGGTYTCEAFNDI 8818
Cdd:cd05744     1 PHFLQAPGDLEVQEGRLCRFDCKVSGLPTPDLFWQLNGKPVRPdSAHKMLVRENGRHSLIIEPVTKRDAGIYTCIARNRA 80

                  ....*..
gi 281359561 8819 GE-SFST 8824
Cdd:cd05744    81 GEnSFNA 87
IgI_4_Robo cd05726
Fourth immunoglobulin (Ig)-like domain in Robo (roundabout) receptors; member of the I-set of ...
7256-7344 5.51e-08

Fourth immunoglobulin (Ig)-like domain in Robo (roundabout) receptors; member of the I-set of Ig superfamily (IgSF) domains; Members here are composed the fourth immunoglobulin (Ig)-like domain in Robo (roundabout) receptors. Robo receptors play a role in the development of the central nervous system (CNS), and are receptors of Slit protein. Slit is a repellant secreted by the neural cells in the midline. Slit acts through Robo to prevent most neurons from crossing the midline from either side. Three mammalian Robo homologs (Robo1, Robo2, Robo3), and three mammalian Slit homologs (Slit-1, Slit-2, Slit-3), have been identified. Commissural axons, which cross the midline, express low levels of Robo; longitudinal axons, which avoid the midline, express high levels of Robo. Robo1, Robo2, and Robo3 are expressed by commissural neurons in the vertebrate spinal cord and Slit-1, Slit-2, and Slit-3 are expressed at the ventral midline. Robo-3 is a divergent member of the Robo family which instead of being a positive regulator of Slit responsiveness, antagonizes Slit responsiveness in precrossing axons. The Slit-Robo interaction is mediated by the second leucine-rich repeat (LRR) domain of Slit and the two N-terminal Ig domains of Robo, Ig1 and Ig2. The primary Robo binding site for Slit2 has been shown by surface plasmon resonance experiments and mutational analysis to be the Ig1 domain, while the Ig2 domain has been proposed to harbor a weak secondary binding site. This group belongs to the I-set of IgSF domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand, but lack a C" strand.


Pssm-ID: 409391 [Multi-domain]  Cd Length: 98  Bit Score: 54.19  E-value: 5.51e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 7256 WITRLQDKVAPFGKDYTLQCAASGKPSPTARWLRNGKEI-------QMNGGRMTCdSKDGvfRLHISNVQTGDDGDYTCE 7328
Cdd:cd05726     2 FVVKPRDQVVALGRTVTFQCETKGNPQPAIFWQKEGSQNllfpyqpPQPSSRFSV-SPTG--DLTITNVQRSDVGYYICQ 78
                          90
                  ....*....|....*.
gi 281359561 7329 AMNSLGFVNTSGYLKI 7344
Cdd:cd05726    79 ALNVAGSILAKAQLEV 94
fn3 pfam00041
Fibronectin type III domain;
2699-2785 5.54e-08

Fibronectin type III domain;


Pssm-ID: 394996 [Multi-domain]  Cd Length: 85  Bit Score: 53.96  E-value: 5.54e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561  2699 SPKGPLAVSDVTASGCKLQWKKPEDDGGvPIKEYVVEKMDTATGKWVRVGRSPGEKEppSFDVTGLSLGSEYMFRVSAVN 2778
Cdd:pfam00041    1 SAPSNLTVTDVTSTSLTVSWTPPPDGNG-PITGYEVEYRPKNSGEPWNEITVPGTTT--SVTLTGLKPGTEYEVRVQAVN 77

                   ....*..
gi 281359561  2779 EEGESEP 2785
Cdd:pfam00041   78 GGGEGPP 84
Ig5_Contactin cd04969
Fifth immunoglobulin (Ig) domain of contactin; The members here are composed of the fifth ...
7268-7342 5.70e-08

Fifth immunoglobulin (Ig) domain of contactin; The members here are composed of the fifth immunoglobulin (Ig) domain of contactins. Contactins are neural cell adhesion molecules and are comprised of six Ig domains followed by four fibronectin type III (FnIII) domains anchored to the membrane by glycosylphosphatidylinositol. The first four Ig domains form the intermolecular binding fragment, which arranges as a compact U-shaped module via contacts between Ig domains 1 and 4, and between Ig domains 2 and 3. Contactin-2 (TAG-1, axonin-1) may play a part in the neuronal processes of neurite outgrowth, axon guidance and fasciculation, and neuronal migration. This group also includes contactin-1 and contactin-5. The different contactins show different expression patterns in the central nervous system. During development and in adulthood, contactin-2 is transiently expressed in subsets of central and peripheral neurons. Contactin-5 is expressed specifically in the rat postnatal nervous system, peaking at about 3 weeks postnatal, and a lack of contactin-5 (NB-2) results in an impairment of neuronal activity in the rat auditory system. Contactin-5 is highly expressed in the adult human brain in the occipital lobe and in the amygdala. Contactin-1 is differentially expressed in tumor tissues and may, through a RhoA mechanism, facilitate invasion and metastasis of human lung adenocarcinoma.


Pssm-ID: 409358 [Multi-domain]  Cd Length: 89  Bit Score: 54.00  E-value: 5.70e-08
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 281359561 7268 GKDYTLQCAASGKPSPTARWlRNGKEIQMNGGRMtCDSKDGvfRLHISNVQTGDDGDYTCEAMNSLGFVNTSGYL 7342
Cdd:cd04969    17 GGDVIIECKPKASPKPTISW-SKGTELLTNSSRI-CILPDG--SLKIKNVTKSDEGKYTCFAVNFFGKANSTGSL 87
IgI_LRIG1-like cd05763
Immunoglobulin (Ig)-like ectodomain of the LRIG1 (Leucine-rich Repeats And Immunoglobulin-like ...
7655-7738 6.06e-08

Immunoglobulin (Ig)-like ectodomain of the LRIG1 (Leucine-rich Repeats And Immunoglobulin-like Domains Protein 1) and similar proteins; member of the I-set of IgSF domains; The members here are composed of subgroup of the immunoglobulin (Ig) domain found in the Ig superfamily. The Ig superfamily is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. A predominant feature of most Ig domains is a disulfide bridge connecting the two beta-sheets with a tryptophan residue packed against the disulfide bond. The ectodomain of LRIG1 has two distinct regions: the proposed 15 LRRs and three Ig-like domains closer to the membrane. LRIG1 has been reported to interact with many receptor tyrosine kinases, GDNF/c-Ret, E-cadherin, JAK/STAT, c-Met, and the EGFR family signaling systems. Immunoglobulin Superfamily (IgSF) domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. The structure of the LRIG1 extracellular Ig domain lacks a C" strand and thus is better described as a member of the I-set of IgSF domains.


Pssm-ID: 409420 [Multi-domain]  Cd Length: 91  Bit Score: 53.78  E-value: 6.06e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 7655 RDANCIQNHNAQFTCTINGVPKPTISWYK-------GAREisngARYHMYSEGDNHFlnINDVFGEDADEYVCRAVNKAG 7727
Cdd:cd05763     7 HDITIRAGSTARLECAATGHPTPQIAWQKdggtdfpAARE----RRMHVMPEDDVFF--IVDVKIEDTGVYSCTAQNSAG 80
                          90
                  ....*....|.
gi 281359561 7728 AKSTRATLAIM 7738
Cdd:cd05763    81 SISANATLTVL 91
PTKc_c-ros cd05044
Catalytic domain of the Protein Tyrosine Kinase, C-ros; PTKs catalyze the transfer of the ...
7995-8200 6.06e-08

Catalytic domain of the Protein Tyrosine Kinase, C-ros; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. This subfamily contains c-ros, Sevenless, and similar proteins. The proto-oncogene c-ros encodes an orphan receptor PTK (RTK) with an unknown ligand. RTKs contain an extracellular ligand-binding domain, a transmembrane region, and an intracellular tyr kinase domain. RTKs are usually activated through ligand binding, which causes dimerization and autophosphorylation of the intracellular tyr kinase catalytic domain. C-ros is expressed in embryonic cells of the kidney, intestine and lung, but disappears soon after birth. It persists only in the adult epididymis. Male mice bearing inactive mutations of c-ros lack the initial segment of the epididymis and are infertile. The Drosophila protein, Sevenless, is required for the specification of the R7 photoreceptor cell during eye development. The c-ros subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270640 [Multi-domain]  Cd Length: 268  Bit Score: 58.20  E-value: 6.06e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 7995 IGTGAFGVVHrcrERSTGNIFAAKFIPVSHSV----------EKDLIRREIDIMNQLHHQKLINLHDAFEDDDEMILILE 8064
Cdd:cd05044     3 LGSGAFGEVF---EGTAKDILGDGSGETKVAVktlrkgatdqEKAEFLKEAHLMSNFKHPNILKLLGVCLDNDPQYIILE 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 8065 FLSGGELFE-----RITA-EGYVMTEAEVINYMRQICEGIRHMHEQNIIHLDIKPENIMCQTRSSTN--VKLIDFGLATR 8136
Cdd:cd05044    80 LMEGGDLLSylraaRPTAfTPPLLTLKDLLSICVDVAKGCVYLEDMHFVHRDLAARNCLVSSKDYRErvVKIGDFGLARD 159
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 281359561 8137 LDPNEVV-KITTG--TAEFAAPE-IVNrepvGFYT---DMWATGVLSY-VLLSGLSPFAGDNDVQTLKNVKA 8200
Cdd:cd05044   160 IYKNDYYrKEGEGllPVRWMAPEsLVD----GVFTtqsDVWAFGVLMWeILTLGQQPYPARNNLEVLHFVRA 227
PTKc_TrkB cd05093
Catalytic domain of the Protein Tyrosine Kinase, Tropomyosin Related Kinase B; PTKs catalyze ...
7988-8181 6.90e-08

Catalytic domain of the Protein Tyrosine Kinase, Tropomyosin Related Kinase B; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. TrkB is a receptor PTK (RTK) containing an extracellular region with arrays of leucine-rich motifs flanked by two cysteine-rich clusters followed by two immunoglobulin-like domains, a transmembrane segment, and an intracellular catalytic domain. Binding of TrkB to its ligands, brain-derived neurotrophic factor (BDNF) or neurotrophin 4 (NT4), results in receptor oligomerization and activation of the catalytic domain. TrkB is broadly expressed in the nervous system and in some non-neural tissues. It plays important roles in cell proliferation, differentiation, and survival. BDNF/Trk signaling plays a key role in regulating activity-dependent synaptic plasticity. TrkB also contributes to protection against gp120-induced neuronal cell death. TrkB overexpression is associated with poor prognosis in neuroblastoma (NB) and other human cancers. It acts as a suppressor of anoikis (detachment-induced apoptosis) and contributes to tumor metastasis. The TrkB subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270675 [Multi-domain]  Cd Length: 288  Bit Score: 58.51  E-value: 6.90e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 7988 RYDIL--EEIGTGAFGVV------HRCRERSTGNIFAAKFIPVSHSVEKDLiRREIDIMNQLHHQKLINLHDAFEDDDEM 8059
Cdd:cd05093     4 RHNIVlkRELGEGAFGKVflaecyNLCPEQDKILVAVKTLKDASDNARKDF-HREAELLTNLQHEHIVKFYGVCVEGDPL 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 8060 ILILEFLSGGELFERITAEG------------YVMTEAEVINYMRQICEGIRHMHEQNIIHLDIKPENimCQTRSSTNVK 8127
Cdd:cd05093    83 IMVFEYMKHGDLNKFLRAHGpdavlmaegnrpAELTQSQMLHIAQQIAAGMVYLASQHFVHRDLATRN--CLVGENLLVK 160
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 281359561 8128 LIDFGLATRLDPNEVVKITTGTA---EFAAPEIVNREPVGFYTDMWATGVLSYVLLS 8181
Cdd:cd05093   161 IGDFGMSRDVYSTDYYRVGGHTMlpiRWMPPESIMYRKFTTESDVWSLGVVLWEIFT 217
fn3 pfam00041
Fibronectin type III domain;
5471-5555 6.94e-08

Fibronectin type III domain;


Pssm-ID: 394996 [Multi-domain]  Cd Length: 85  Bit Score: 53.57  E-value: 6.94e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561  5471 DKPGQPQATDWGKHFVDLEWSTPKrDGGAPISSYIIEKRPKF-GQWERAAVVLGDNCKAHVPELTNGGEYEFRVIAVNRG 5549
Cdd:pfam00041    1 SAPSNLTVTDVTSTSLTVSWTPPP-DGNGPITGYEVEYRPKNsGEPWNEITVPGTTTSVTLTGLKPGTEYEVRVQAVNGG 79

                   ....*.
gi 281359561  5550 GPSDPS 5555
Cdd:pfam00041   80 GEGPPS 85
Ig4_NrCAM cd05868
Fourth immunoglobulin (Ig)-like domain of NrCAM (NgCAM-related cell adhesion molecule); The ...
7256-7344 6.99e-08

Fourth immunoglobulin (Ig)-like domain of NrCAM (NgCAM-related cell adhesion molecule); The members here are composed of the fourth immunoglobulin (Ig)-like domain of NrCAM (NgCAM-related cell adhesion molecule). NrCAM belongs to the L1 subfamily of cell adhesion molecules (CAMs) and is comprised of an extracellular region having six IG-like domains and five fibronectin type III domains, a transmembrane region, and an intracellular domain. NrCAM is primarily expressed in the nervous system.


Pssm-ID: 409454  Cd Length: 89  Bit Score: 53.83  E-value: 6.99e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 7256 WITRLQDKVAPFGKDYTLQCAASGKPSPTARWLRNGKEIQM--NGGRMTCDSKDGVFrlhiSNVQTGDDGDYTCEAMNSL 7333
Cdd:cd05868     2 WITAPTNLVLSPGEDGTLICRANGNPKPSISWLTNGVPIEIapTDPSRKVDGDTIIF----SKVQERSSAVYQCNASNEY 77
                          90
                  ....*....|.
gi 281359561 7334 GFVNTSGYLKI 7344
Cdd:cd05868    78 GYLLANAFVNV 88
IgI_Titin_like cd05747
Immunoglobulin (Ig)-like domain of human titin C terminus and similar proteins; member of the ...
2610-2683 7.31e-08

Immunoglobulin (Ig)-like domain of human titin C terminus and similar proteins; member of the I-set of Ig superfamily (IgSF) domains; The members here are composed of the fifth immunoglobulin (Ig)-like domain from the C-terminus of human titin x and similar proteins. Titin (also called connectin) is a fibrous sarcomeric protein specifically found in vertebrate striated muscle. Titin is gigantic; depending on isoform composition it ranges from 2970 to 3700 kDa, and is of a length that spans half a sarcomere. Titin largely consists of multiple repeats of Ig-like and fibronectin type 3 (FN-III)-like domains. Titin connects the ends of myosin thick filaments to Z disks and extends along the thick filament to the H zone and appears to function similar to an elastic band, keeping the myosin filaments centered in the sarcomere during muscle contraction or stretching. This group belongs to the I-set of IgSF domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand, but lack a C" strand.


Pssm-ID: 143224 [Multi-domain]  Cd Length: 92  Bit Score: 53.90  E-value: 7.31e-08
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 281359561 2610 KRVTIKSGRTHKWSVDVLGEPIPELHWSwRDDIPLTNGDRIKIENVDYHTDFSITNVLRKDSGFYTLKAENRNG 2683
Cdd:cd05747    11 RSLTVSEGESARFSCDVDGEPAPTVTWM-REGQIIVSSQRHQITSTEYKSTFEISKVQMSDEGNYTVVVENSEG 83
IgI_4_hemolin-like cd20978
Fourth immunoglobulin (Ig)-like domain of hemolin, and similar domains; a member of the I-set ...
5570-5650 7.43e-08

Fourth immunoglobulin (Ig)-like domain of hemolin, and similar domains; a member of the I-set of IgSF domains; The members here are composed of the fourth immunoglobulin (Ig)-like domain of hemolin and similar proteins. Hemolin, an insect immunoglobulin superfamily (IgSF) member containing four Ig-like domains, is a lipopolysaccharide-binding immune protein induced during bacterial infection. Hemolin shares significant sequence similarity with the first four Ig-like domains of the transmembrane cell adhesion molecules (CAMs) of the L1 family. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. The fourth Ig-like domain of hemolin is a member of the I-set Ig domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set domains, members of the I-set have a discontinuous A strand but lack a C" strand. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors, the muscle proteins titin, telokin, and twitchin, the neuronal adhesion molecule axonin-1, and the signaling molecule semaphorin 4D that is involved in axonal guidance, immune function and angiogenesis.


Pssm-ID: 409570 [Multi-domain]  Cd Length: 88  Bit Score: 53.55  E-value: 7.43e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 5570 PFFDKSLLNDITVHAGKRLGWTLPIEASPRPLITWLYNGKEIgSNSRGESGLFQNELTfeIVSSLRSDEGRYTLILKNEH 5649
Cdd:cd20978     1 PKFIQKPEKNVVVKGGQDVTLPCQVTGVPQPKITWLHNGKPL-QGPMERATVEDGTLT--IINVQPEDTGYYGCVATNEI 77

                  .
gi 281359561 5650 G 5650
Cdd:cd20978    78 G 78
IgI_NCAM-1_like cd05732
Immunoglobulin (Ig)-like I-set domain of Neural Cell Adhesion Molecule 1 (NCAM-1) and similar ...
8631-8711 8.49e-08

Immunoglobulin (Ig)-like I-set domain of Neural Cell Adhesion Molecule 1 (NCAM-1) and similar proteins; The members here are composed of the fourth immunoglobulin (Ig)-like domain of Neural Cell Adhesion Molecule (NCAM-1). NCAM plays important roles in the development and regeneration of the central nervous system, in synaptogenesis and neural migration. NCAM mediates cell-cell and cell-substratum recognition and adhesion via homophilic (NCAM-NCAM), and heterophilic (NCAM-non-NCAM), interactions. NCAM is expressed as three major isoforms having different intracellular extensions. The extracellular portion of NCAM has five N-terminal Ig-like domains and two fibronectin type III domains. The double zipper adhesion complex model for NCAM homophilic binding involves Ig1, Ig2, and Ig3. By this model, Ig1 and Ig2 mediate dimerization of NCAM molecules situated on the same cell surface (cis interactions), and Ig3 domains mediate interactions between NCAM molecules expressed on the surface of opposing cells (trans interactions), through binding to the Ig1 and Ig2 domains. The adhesive ability of NCAM is modulated by the addition of polysialic acid chains to the fifth Ig-like domain. Also included in this group is NCAM-2 (also known as OCAM/mamFas II and RNCAM) NCAM-2 is differentially expressed in the developing and mature olfactory epithelium (OE). One of the unique features of I-set domains is the lack of a C" strand. The structures of this group show that the Ig domain lacks this strand and thus is a member of the I-set of Ig domains.


Pssm-ID: 409395 [Multi-domain]  Cd Length: 96  Bit Score: 53.68  E-value: 8.49e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 8631 KPEFTKpLHDLTIHDGEQLILTCYVKGDPEPQISWSKNGKSLSSSD-ILD----LRYKNGIATLTINEVFPEDEGVITCT 8705
Cdd:cd05732     2 QPKITY-LENQTAVELEQITLTCEAEGDPIPEITWRRATRGISFEEgDLDgrivVRGHARVSSLTLKDVQLTDAGRYDCE 80

                  ....*.
gi 281359561 8706 ATNSVG 8711
Cdd:cd05732    81 ASNRIG 86
IG_like smart00410
Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.
1503-1588 8.56e-08

Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.


Pssm-ID: 214653 [Multi-domain]  Cd Length: 85  Bit Score: 53.28  E-value: 8.56e-08
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561   1503 QESYSVVEDSTAYLTVGVEGSPAPTFKFYK-GVSEILEGGRFKFLTDGQTNTITlcMRKCKPNDESKYKIVVSNIHGEDS 1581
Cdd:smart00410    1 PPSVTVKEGESVTLSCEASGSPPPEVTWYKqGGKLLAESGRFSVSRSGSTSTLT--ISNVTPEDSGTYTCAATNSSGSAS 78

                    ....*..
gi 281359561   1582 AEMQLYV 1588
Cdd:smart00410   79 SGTTLTV 85
I-set pfam07679
Immunoglobulin I-set domain;
5570-5660 8.61e-08

Immunoglobulin I-set domain;


Pssm-ID: 400151 [Multi-domain]  Cd Length: 90  Bit Score: 53.42  E-value: 8.61e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561  5570 PFFDKsLLNDITVHAGKRLGWTLPIEASPRPLITWLYNGKEIGSNSRGESGLFQNELTFEIVSSLRSDEGRYTLILKNEH 5649
Cdd:pfam07679    1 PKFTQ-KPKDVEVQEGESARFTCTVTGTPDPEVSWFKDGQPLRSSDRFKVTYEGGTYTLTISNVQPDDSGKYTCVATNSA 79
                           90
                   ....*....|.
gi 281359561  5650 GSfdASAHATV 5660
Cdd:pfam07679   80 GE--AEASAEL 88
IgI_8_hMLCK_like cd05762
Eighth immunoglobulin (Ig)-like domain of human myosin light-chain kinase (MLCK) and similar ...
4089-4188 9.05e-08

Eighth immunoglobulin (Ig)-like domain of human myosin light-chain kinase (MLCK) and similar protein; member of the I-set of IgSF domains; The members here are composed of the eighth immunoglobulin (Ig)-like domain of human myosin light-chain kinase (MLCK) and similar proteins. Myosin light-chain kinase (MLCK) is a key regulator of different forms of cell motility involving actin and myosin II. Agonist stimulation of smooth muscle cells increases cytosolic Ca2+ which binds calmodulin. This Ca2+-calmodulin complex in turn binds to and activates MLCK. Activated MLCK leads to the phosphorylation of the 20 kDa myosin regulatory light chain (RLC) of myosin II and the stimulation of actin-activated myosin MgATPase activity. MLCK is widely present in vertebrate tissues; it phosphorylates the 20 kDa RLC of both smooth and nonmuscle myosin II. Phosphorylation leads to the activation of the myosin motor domain and altered structural properties of myosin II. In smooth muscle MLCK it is involved in initiating contraction. In nonmuscle cells, MLCK may participate in cell division and cell motility; it has been suggested MLCK plays a role in cardiomyocyte differentiation and contraction through regulation of nonmuscle myosin II.


Pssm-ID: 409419  Cd Length: 99  Bit Score: 53.80  E-value: 9.05e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 4089 PPKIDRTNiKDITIKAGQHIRFDIKVSGEPPATKVWLhnKARLENDDSNY-NIDMESYRTKLTVPISKRFHSGKYTLKAE 4167
Cdd:cd05762     1 PPQIIQFP-EDMKVRAGESVELFCKVTGTQPITCTWM--KFRKQIQEGEGiKIENTENSSKLTITEGQQEHCGCYTLEVE 77
                          90       100
                  ....*....|....*....|.
gi 281359561 4168 NESGRDEASFEVIVLDKPGPP 4188
Cdd:cd05762    78 NKLGSRQAQVNLTVVDKPDPP 98
IgI_1_Titin_Z1z2-like cd20974
First Ig-like domain of the giant muscle protein titin Z1z2 in the sarcomeric Z-disk and ...
4979-5069 9.41e-08

First Ig-like domain of the giant muscle protein titin Z1z2 in the sarcomeric Z-disk and similar proteins; a member of the I-set of IgSF domains; The members here are composed of the first immunoglobulin (Ig)-like domain of the giant muscle protein titin Z1z2 in the sarcomeric Z-disk and similar proteins. Titin is a key component in the assembly and functioning of vertebrate striated muscles. By providing connections at the level of individual microfilaments, it contributes to the fine balance of forces between the two halves of the sarcomere. The Ig superfamily (IgSF) is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. Unlike the V-set, one of the distinctive features of I-set domains is the lack of a C" strand. The structure of the titin Z1z2 lacks this strand and thus it belongs to the I-set of the IgSF. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors, the hemolymph protein hemolin, the muscle proteins titin, telokin, and twitchin, the neuronal adhesion molecule axonin-1, and the signaling molecule semaphorin 4D that is involved in axonal guidance, immune function and angiogenesis.


Pssm-ID: 409566 [Multi-domain]  Cd Length: 93  Bit Score: 53.51  E-value: 9.41e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 4979 PIIDRSsLVEVRIKAGQSFTFDCKVSGEPAPQTKWLlKKKEVYSKDN---VKVTNVDYNTKLKVNSATRSDSGIYTVFAE 5055
Cdd:cd20974     1 PVFTQP-LQSVVVLEGSTATFEAHVSGKPVPEVSWF-RDGQVISTSTlpgVQISFSDGRAKLSIPAVTKANSGRYSLTAT 78
                          90
                  ....*....|....
gi 281359561 5056 NANGEDSADVKVTV 5069
Cdd:cd20974    79 NGSGQATSTAELLV 92
Ig_C5_MyBP-C cd05894
C5 immunoglobulin (Ig) domain of cardiac myosin binding protein C (MyBP-C); The members here ...
4100-4181 9.43e-08

C5 immunoglobulin (Ig) domain of cardiac myosin binding protein C (MyBP-C); The members here are composed of the C5 immunoglobulin (Ig) domain of cardiac myosin binding protein C (MyBP-C). MyBP-C consists of repeated domains, Ig and fibronectin type 3, and various linkers. Three isoforms of MYBP-C exist: slow-skeletal (ssMyBP-C), fast-skeletal (fsMyBP-C), and cardiac (cMyBP-C). cMYBP-C has insertions between and inside domains and an additional cardiac-specific Ig domain at the N-terminus. For cMYBP_C an interaction has been demonstrated between this C5 domain and the Ig C8 domain.


Pssm-ID: 409475  Cd Length: 86  Bit Score: 53.31  E-value: 9.43e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 4100 ITIKAGQHIRFDIKVSGEPPATKVWLhnKARLENDDSNYNIDMESY--RTKLTVPISKRFHSGKYTLKAENESGRDEASF 4177
Cdd:cd05894     5 IVVVAGNKLRLDVPISGEPAPTVTWS--RGDKAFTATEGRVRVESYkdLSSFVIEGAEREDEGVYTITVTNPVGEDHASL 82

                  ....
gi 281359561 4178 EVIV 4181
Cdd:cd05894    83 FVKV 86
IgI_telokin-like cd20973
immunoglobulin-like domain of telokin and similar proteins; a member of the I-set of IgSF ...
8443-8525 9.67e-08

immunoglobulin-like domain of telokin and similar proteins; a member of the I-set of IgSF domains; The members here are composed of the immunoglobulin (Ig) domain in telokin, the C-terminal domain of myosin light chain kinase which is identical to telokin, and similar proteins. The Ig superfamily (IgSF) is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. Unlike the V-set, one of the distinctive features of I-set domains is the lack of a C" strand. The structure of the telokin Ig domain lacks this strand and thus it belongs to the I-set of the IgSF. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors, the hemolymph protein hemolin, the muscle proteins titin, telokin, and twitchin, the neuronal adhesion molecule axonin-1, and the signaling molecule semaphorin 4D that is involved in axonal guidance, immune function and angiogenesis.


Pssm-ID: 409565 [Multi-domain]  Cd Length: 88  Bit Score: 53.35  E-value: 9.67e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 8443 LRPRVMQARDTCKLLCCLSGKPVPNVRWYKDGRELSKYEYAMTHSD--GVVTMEIIDCKPSDSGKYSCKATNCHGTDETD 8520
Cdd:cd20973     4 LRDKEVVEGSAARFDCKVEGYPDPEVKWMKDDNPIVESRRFQIDQDedGLCSLIISDVCGDDSGKYTCKAVNSLGEATCS 83

                  ....*
gi 281359561 8521 CVVIV 8525
Cdd:cd20973    84 AELTV 88
IgI_4_hemolin-like cd20978
Fourth immunoglobulin (Ig)-like domain of hemolin, and similar domains; a member of the I-set ...
8312-8401 9.76e-08

Fourth immunoglobulin (Ig)-like domain of hemolin, and similar domains; a member of the I-set of IgSF domains; The members here are composed of the fourth immunoglobulin (Ig)-like domain of hemolin and similar proteins. Hemolin, an insect immunoglobulin superfamily (IgSF) member containing four Ig-like domains, is a lipopolysaccharide-binding immune protein induced during bacterial infection. Hemolin shares significant sequence similarity with the first four Ig-like domains of the transmembrane cell adhesion molecules (CAMs) of the L1 family. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. The fourth Ig-like domain of hemolin is a member of the I-set Ig domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set domains, members of the I-set have a discontinuous A strand but lack a C" strand. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors, the muscle proteins titin, telokin, and twitchin, the neuronal adhesion molecule axonin-1, and the signaling molecule semaphorin 4D that is involved in axonal guidance, immune function and angiogenesis.


Pssm-ID: 409570 [Multi-domain]  Cd Length: 88  Bit Score: 53.16  E-value: 9.76e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 8312 PRFVIRPSSQFCY-EGQSVKFYCRCIAIATPTLTWSHNNIELRQSvkfMKRYVGDDYYFIINRVKLDDRGEYIIRAENHY 8390
Cdd:cd20978     1 PKFIQKPEKNVVVkGGQDVTLPCQVTGVPQPKITWLHNGKPLQGP---MERATVEDGTLTIINVQPEDTGYYGCVATNEI 77
                          90
                  ....*....|.
gi 281359561 8391 GSREEVVFLNV 8401
Cdd:cd20978    78 GDIYTETLLHV 88
I-set pfam07679
Immunoglobulin I-set domain;
656-726 1.01e-07

Immunoglobulin I-set domain;


Pssm-ID: 400151 [Multi-domain]  Cd Length: 90  Bit Score: 53.42  E-value: 1.01e-07
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 281359561   656 TVVIECTVASKFEPKCTWYKETSTVKESKRHVYQVEqtkegEFAVKLEINDVEESDKGAYKLVASNEKGEA 726
Cdd:pfam07679   17 SARFTCTVTGTPDPEVSWFKDGQPLRSSDRFKVTYE-----GGTYTLTISNVQPDDSGKYTCVATNSAGEA 82
COG4733 COG4733
Phage-related protein, tail protein J [Mobilome: prophages, transposons];
3900-4072 1.01e-07

Phage-related protein, tail protein J [Mobilome: prophages, transposons];


Pssm-ID: 443767 [Multi-domain]  Cd Length: 978  Bit Score: 59.57  E-value: 1.01e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 3900 NVTAETLHLKWEKPEDDGGdpieqYLVE-RMDTetGRWVPVLTTKTPEADVTGLTEGkEYLFRVKAVNSEGESEPLVTDI 3978
Cdd:COG4733   548 GTAVTTLTVSWDAPAGAVA-----YEVEwRRDD--GNWVSVPRTSGTSFEVPGIYAG-DYEVRVRAINALGVSSAWAASS 619
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 3979 PTKAKnpFDAADtPGKPQIVDWSGN--HCDLKWRAPEDdggASITGYIVERKDPNTGKWQKALETSTPDCKARVNDLIAG 4056
Cdd:COG4733   620 ETTVT--GKTAP-PPAPTGLTATGGlgGITLSWSFPVD---ADTLRTEIRYSTTGDWASATVAQALYPGNTYTLAGLKAG 693
                         170
                  ....*....|....*.
gi 281359561 4057 NKYQFRIMAVNKAGKS 4072
Cdd:COG4733   694 QTYYYRARAVDRSGNV 709
Ig4_Peroxidasin cd05746
Fourth immunoglobulin (Ig)-like domain of peroxidasin; The members here are composed of the ...
7666-7736 1.06e-07

Fourth immunoglobulin (Ig)-like domain of peroxidasin; The members here are composed of the fourth immunoglobulin (Ig)-like domain in peroxidasin. Peroxidasin has a peroxidase domain and interacting extracellular motifs containing four Ig-like domains. It has been suggested that peroxidasin is secreted, and has functions related to the stabilization of the extracellular matrix. It may play a part in various other important processes such as removal and destruction of cells which have undergone programmed cell death and protection of the organism against non-self.


Pssm-ID: 143223  Cd Length: 69  Bit Score: 52.57  E-value: 1.06e-07
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 281359561 7666 QFTCTINGVPKPTISWYKGAREISNGARYHMYSEGdnhFLNINDVFGEDADEYVCRAVNKAGAKSTRATLA 7736
Cdd:cd05746     2 QIPCSAQGDPEPTITWNKDGVQVTESGKFHISPEG---YLAIRDVGVADQGRYECVARNTIGYASVSMVLS 69
IgI_Myotilin_C_like cd05744
Immunoglobulin (Ig)-like domain of myotilin, palladin, and myopalladin; member of the I-set of ...
6176-6255 1.09e-07

Immunoglobulin (Ig)-like domain of myotilin, palladin, and myopalladin; member of the I-set of Ig superfamily (IgSF) domains; The members here are composed of the immunoglobulin (Ig)-like domain in myotilin, palladin, and myopalladin. Myotilin, palladin, and myopalladin function as scaffolds that regulate actin organization. Myotilin and myopalladin are most abundant in skeletal and cardiac muscle; palladin is ubiquitously expressed in the organs of developing vertebrates and plays a key role in cellular morphogenesis. The three family members each interact with specific molecular partners with all three binding to alpha-actinin; In addition, palladin also binds to vasodilator-stimulated phosphoprotein (VASP) and ezrin, myotilin binds to filamin and actin, and myopalladin also binds to nebulin and cardiac ankyrin repeat protein (CARP). This group belongs to the I-set of IgSF domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand, but lack a C" strand.


Pssm-ID: 409405 [Multi-domain]  Cd Length: 91  Bit Score: 53.27  E-value: 1.09e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 6176 KVRAGEPVNLNIPISGAPTPTIEWKRGDLKLEEGKRIS-YETNSERTLFRIDDSNRRDSGKYTVTAANEFGKDTADIEVI 6254
Cdd:cd05744    11 EVQEGRLCRFDCKVSGLPTPDLFWQLNGKPVRPDSAHKmLVRENGRHSLIIEPVTKRDAGIYTCIARNRAGENSFNAELV 90

                  .
gi 281359561 6255 V 6255
Cdd:cd05744    91 V 91
IgI_telokin-like cd20973
immunoglobulin-like domain of telokin and similar proteins; a member of the I-set of IgSF ...
138-210 1.16e-07

immunoglobulin-like domain of telokin and similar proteins; a member of the I-set of IgSF domains; The members here are composed of the immunoglobulin (Ig) domain in telokin, the C-terminal domain of myosin light chain kinase which is identical to telokin, and similar proteins. The Ig superfamily (IgSF) is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. Unlike the V-set, one of the distinctive features of I-set domains is the lack of a C" strand. The structure of the telokin Ig domain lacks this strand and thus it belongs to the I-set of the IgSF. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors, the hemolymph protein hemolin, the muscle proteins titin, telokin, and twitchin, the neuronal adhesion molecule axonin-1, and the signaling molecule semaphorin 4D that is involved in axonal guidance, immune function and angiogenesis.


Pssm-ID: 409565 [Multi-domain]  Cd Length: 88  Bit Score: 52.96  E-value: 1.16e-07
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 281359561  138 FECRVNADPIPAIIWFHNGAAVKESERHKITVDKDvhsYFATLEILNVTVEDAGKYKVNAKNELGESNATISL 210
Cdd:cd20973    17 FDCKVEGYPDPEVKWMKDDNPIVESRRFQIDQDED---GLCSLIISDVCGDDSGKYTCKAVNSLGEATCSAEL 86
IgI_1_Titin_Z1z2-like cd20974
First Ig-like domain of the giant muscle protein titin Z1z2 in the sarcomeric Z-disk and ...
4692-4776 1.21e-07

First Ig-like domain of the giant muscle protein titin Z1z2 in the sarcomeric Z-disk and similar proteins; a member of the I-set of IgSF domains; The members here are composed of the first immunoglobulin (Ig)-like domain of the giant muscle protein titin Z1z2 in the sarcomeric Z-disk and similar proteins. Titin is a key component in the assembly and functioning of vertebrate striated muscles. By providing connections at the level of individual microfilaments, it contributes to the fine balance of forces between the two halves of the sarcomere. The Ig superfamily (IgSF) is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. Unlike the V-set, one of the distinctive features of I-set domains is the lack of a C" strand. The structure of the titin Z1z2 lacks this strand and thus it belongs to the I-set of the IgSF. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors, the hemolymph protein hemolin, the muscle proteins titin, telokin, and twitchin, the neuronal adhesion molecule axonin-1, and the signaling molecule semaphorin 4D that is involved in axonal guidance, immune function and angiogenesis.


Pssm-ID: 409566 [Multi-domain]  Cd Length: 93  Bit Score: 53.13  E-value: 1.21e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 4692 LRNITLSSGTALKLDANITGEPAPKVEWKLSN--YHLQSGKNVTIETPDYYTKLVIRPTQRSDSGEYLVTATNTSGKDSV 4769
Cdd:cd20974     7 LQSVVVLEGSTATFEAHVSGKPVPEVSWFRDGqvISTSTLPGVQISFSDGRAKLSIPAVTKANSGRYSLTATNGSGQATS 86

                  ....*..
gi 281359561 4770 LVNVVIT 4776
Cdd:cd20974    87 TAELLVL 93
IgI_Myotilin_C_like cd05744
Immunoglobulin (Ig)-like domain of myotilin, palladin, and myopalladin; member of the I-set of ...
335-426 1.22e-07

Immunoglobulin (Ig)-like domain of myotilin, palladin, and myopalladin; member of the I-set of Ig superfamily (IgSF) domains; The members here are composed of the immunoglobulin (Ig)-like domain in myotilin, palladin, and myopalladin. Myotilin, palladin, and myopalladin function as scaffolds that regulate actin organization. Myotilin and myopalladin are most abundant in skeletal and cardiac muscle; palladin is ubiquitously expressed in the organs of developing vertebrates and plays a key role in cellular morphogenesis. The three family members each interact with specific molecular partners with all three binding to alpha-actinin; In addition, palladin also binds to vasodilator-stimulated phosphoprotein (VASP) and ezrin, myotilin binds to filamin and actin, and myopalladin also binds to nebulin and cardiac ankyrin repeat protein (CARP). This group belongs to the I-set of IgSF domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand, but lack a C" strand.


Pssm-ID: 409405 [Multi-domain]  Cd Length: 91  Bit Score: 53.27  E-value: 1.22e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561  335 PRFPKKPTIR--QEEDLLIMECVLEAHPVPDIVWYCSEKEICNNQRTKMtrkaITKDSYILTLEIQNPTKEDGGNYRCNA 412
Cdd:cd05744     1 PHFLQAPGDLevQEGRLCRFDCKVSGLPTPDLFWQLNGKPVRPDSAHKM----LVRENGRHSLIIEPVTKRDAGIYTCIA 76
                          90
                  ....*....|....
gi 281359561  413 INMYGESNANIALN 426
Cdd:cd05744    77 RNRAGENSFNAELV 90
IgI_LRIG1-like cd05763
Immunoglobulin (Ig)-like ectodomain of the LRIG1 (Leucine-rich Repeats And Immunoglobulin-like ...
7273-7344 1.36e-07

Immunoglobulin (Ig)-like ectodomain of the LRIG1 (Leucine-rich Repeats And Immunoglobulin-like Domains Protein 1) and similar proteins; member of the I-set of IgSF domains; The members here are composed of subgroup of the immunoglobulin (Ig) domain found in the Ig superfamily. The Ig superfamily is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. A predominant feature of most Ig domains is a disulfide bridge connecting the two beta-sheets with a tryptophan residue packed against the disulfide bond. The ectodomain of LRIG1 has two distinct regions: the proposed 15 LRRs and three Ig-like domains closer to the membrane. LRIG1 has been reported to interact with many receptor tyrosine kinases, GDNF/c-Ret, E-cadherin, JAK/STAT, c-Met, and the EGFR family signaling systems. Immunoglobulin Superfamily (IgSF) domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. The structure of the LRIG1 extracellular Ig domain lacks a C" strand and thus is better described as a member of the I-set of IgSF domains.


Pssm-ID: 409420 [Multi-domain]  Cd Length: 91  Bit Score: 53.01  E-value: 1.36e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 7273 LQCAASGKPSPTARWlrngkeiQMNGG---------RMTCDSKDGVFrlHISNVQTGDDGDYTCEAMNSLGFVNTSGYLK 7343
Cdd:cd05763    19 LECAATGHPTPQIAW-------QKDGGtdfpaarerRMHVMPEDDVF--FIVDVKIEDTGVYSCTAQNSAGSISANATLT 89

                  .
gi 281359561 7344 I 7344
Cdd:cd05763    90 V 90
Ig_Pro_neuregulin cd05750
Immunoglobulin (Ig)-like domain in neuregulins; The members here are composed of the ...
4993-5069 1.44e-07

Immunoglobulin (Ig)-like domain in neuregulins; The members here are composed of the immunoglobulin (Ig)-like domain in neuregulins (NRGs). NRGs are signaling molecules which participate in cell-cell interactions in the nervous system, breast, heart, and other organ systems, and are implicated in the pathology of diseases including schizophrenia, multiple sclerosis, and breast cancer. There are four members of the neuregulin gene family (NRG-1, NRG-2, NRG-3, and NRG-4). The NRG-1 protein, binds to and activates the tyrosine kinases receptors ErbB3 and ErbB4, initiating signaling cascades. The other NRGs proteins bind one or the other or both of these ErbBs. NRG-1 has multiple functions: in the brain it regulates various processes such as radial glia formation and neuronal migration, dendritic development, and expression of neurotransmitters receptors, while in the peripheral nervous system NRG-1 regulates processes such as target cell differentiation, and Schwann cell survival. There are many NRG-1 isoforms which arise from the alternative splicing of mRNA. Less is known of the functions of the other NRGs. NRG-2 and NRG-3 are expressed predominantly in the nervous system. NRG-2 is expressed by motor neurons and terminal Schwann cells, and is concentrated near synaptic sites and may be a signal that regulates synaptic differentiation. NRG-4 has been shown to direct pancreatic islet cell development towards the delta-cell lineage.


Pssm-ID: 409408 [Multi-domain]  Cd Length: 92  Bit Score: 52.90  E-value: 1.44e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 4993 AGQSFTFDCKVSGE-PAPQTKWLLKKKEVYSK--DNVKVTNVDYNTKLKVNSATRSDSGIYTVFAENANGEDSADVKVTV 5069
Cdd:cd05750    13 EGSKLVLKCEATSEnPSPRYRWFKDGKELNRKrpKNIKIRNKKKNSELQINKAKLEDSGEYTCVVENILGKDTVTGNVTV 92
IgI_Titin_like cd05747
Immunoglobulin (Ig)-like domain of human titin C terminus and similar proteins; member of the ...
4672-4766 1.47e-07

Immunoglobulin (Ig)-like domain of human titin C terminus and similar proteins; member of the I-set of Ig superfamily (IgSF) domains; The members here are composed of the fifth immunoglobulin (Ig)-like domain from the C-terminus of human titin x and similar proteins. Titin (also called connectin) is a fibrous sarcomeric protein specifically found in vertebrate striated muscle. Titin is gigantic; depending on isoform composition it ranges from 2970 to 3700 kDa, and is of a length that spans half a sarcomere. Titin largely consists of multiple repeats of Ig-like and fibronectin type 3 (FN-III)-like domains. Titin connects the ends of myosin thick filaments to Z disks and extends along the thick filament to the H zone and appears to function similar to an elastic band, keeping the myosin filaments centered in the sarcomere during muscle contraction or stretching. This group belongs to the I-set of IgSF domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand, but lack a C" strand.


Pssm-ID: 143224 [Multi-domain]  Cd Length: 92  Bit Score: 52.74  E-value: 1.47e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 4672 PSKIFTaKPRylapkidrrnlrNITLSSGTALKLDANITGEPAPKVEWKLSNYHLQSGKNVTIETPDYYTKLVIRPTQRS 4751
Cdd:cd05747     3 PATILT-KPR------------SLTVSEGESARFSCDVDGEPAPTVTWMREGQIIVSSQRHQITSTEYKSTFEISKVQMS 69
                          90
                  ....*....|....*
gi 281359561 4752 DSGEYLVTATNTSGK 4766
Cdd:cd05747    70 DEGNYTVVVENSEGK 84
IG_like smart00410
Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.
3507-3590 1.55e-07

Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.


Pssm-ID: 214653 [Multi-domain]  Cd Length: 85  Bit Score: 52.51  E-value: 1.55e-07
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561   3507 KPVIVKTGLSISLDINIRGEPAPKVEWFFNNSSVTSDEHSVKIDNVDYNTKFFVMRAQRSQSGKYIIKATNEVGEDEAEL 3586
Cdd:smart00410    2 PSVTVKEGESVTLSCEASGSPPPEVTWYKQGGKLLAESGRFSVSRSGSTSTLTISNVTPEDSGTYTCAATNSSGSASSGT 81

                    ....
gi 281359561   3587 EVTV 3590
Cdd:smart00410   82 TLTV 85
IgI_Twitchin_like cd20949
C-terminal immunoglobulin-like domain of the myosin-associated giant protein kinase Twitchin, ...
229-312 1.65e-07

C-terminal immunoglobulin-like domain of the myosin-associated giant protein kinase Twitchin, and similar domains; member of the I-set IgSF domains; The members here are composed of the C-terminal immunoglobulin-like domain of the myosin-associated giant protein kinase Twitchin and similar proteins, including Caenorhabditis elegans and Aplysia californica Twitchin, Drosophila melanogaster Projectin, and similar proteins. These are very large muscle proteins containing multiple immunoglobulin (Ig)-like and fibronectin type III (FN3) domains and a single kinase domain near the C-terminus. In humans these proteins are called Titin. The Ig superfamily (IgSF) is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. The Ig-like domain of the Twitchin is a member of the I-set IgSF domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand but lack a C" strand. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors, the hemolymph protein hemolin, the muscle proteins (titin, telokin, and twitchin), the neuronal adhesion molecule axonin-1, and the signaling molecule semaphorin 4D.


Pssm-ID: 409541 [Multi-domain]  Cd Length: 89  Bit Score: 52.72  E-value: 1.65e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561  229 TFTERPVIRQSEDGGNVTFECRCVGDPTPTVTWSHGETELNESnrykmslTMDQKLYHIAC--LEISSVVSSDQGEYRAQ 306
Cdd:cd20949     1 TFTENAYVTTVKEGQSATILCEVKGEPQPNVTWHFNGQPISAS-------VADMSKYRILAdgLLINKVTQDDTGEYTCR 73

                  ....*.
gi 281359561  307 AKNKHG 312
Cdd:cd20949    74 AYQVNS 79
fn3 pfam00041
Fibronectin type III domain;
4186-4269 1.67e-07

Fibronectin type III domain;


Pssm-ID: 394996 [Multi-domain]  Cd Length: 85  Bit Score: 52.42  E-value: 1.67e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561  4186 GPPEGpLRVTDVHKEGCKLKWNAPLDDGGlPIDHYIIEKMDVESGRWLPSGRFK--ESFAELNNLEPSHEYKFRVLAVNT 4263
Cdd:pfam00041    1 SAPSN-LTVTDVTSTSLTVSWTPPPDGNG-PITGYEVEYRPKNSGEPWNEITVPgtTTSVTLTGLKPGTEYEVRVQAVNG 78

                   ....*.
gi 281359561  4264 EGESEP 4269
Cdd:pfam00041   79 GGEGPP 84
IgI_1_Titin_Z1z2-like cd20974
First Ig-like domain of the giant muscle protein titin Z1z2 in the sarcomeric Z-disk and ...
4097-4182 1.77e-07

First Ig-like domain of the giant muscle protein titin Z1z2 in the sarcomeric Z-disk and similar proteins; a member of the I-set of IgSF domains; The members here are composed of the first immunoglobulin (Ig)-like domain of the giant muscle protein titin Z1z2 in the sarcomeric Z-disk and similar proteins. Titin is a key component in the assembly and functioning of vertebrate striated muscles. By providing connections at the level of individual microfilaments, it contributes to the fine balance of forces between the two halves of the sarcomere. The Ig superfamily (IgSF) is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. Unlike the V-set, one of the distinctive features of I-set domains is the lack of a C" strand. The structure of the titin Z1z2 lacks this strand and thus it belongs to the I-set of the IgSF. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors, the hemolymph protein hemolin, the muscle proteins titin, telokin, and twitchin, the neuronal adhesion molecule axonin-1, and the signaling molecule semaphorin 4D that is involved in axonal guidance, immune function and angiogenesis.


Pssm-ID: 409566 [Multi-domain]  Cd Length: 93  Bit Score: 52.74  E-value: 1.77e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 4097 IKDITIKAGQHIRFDIKVSGEPPATKVWLHNKARLENDDS-NYNIDMESYRTKLTVPISKRFHSGKYTLKAENESGRDEA 4175
Cdd:cd20974     7 LQSVVVLEGSTATFEAHVSGKPVPEVSWFRDGQVISTSTLpGVQISFSDGRAKLSIPAVTKANSGRYSLTATNGSGQATS 86

                  ....*..
gi 281359561 4176 SFEVIVL 4182
Cdd:cd20974    87 TAELLVL 93
IgI_Myotilin_C_like cd05744
Immunoglobulin (Ig)-like domain of myotilin, palladin, and myopalladin; member of the I-set of ...
2613-2693 1.89e-07

Immunoglobulin (Ig)-like domain of myotilin, palladin, and myopalladin; member of the I-set of Ig superfamily (IgSF) domains; The members here are composed of the immunoglobulin (Ig)-like domain in myotilin, palladin, and myopalladin. Myotilin, palladin, and myopalladin function as scaffolds that regulate actin organization. Myotilin and myopalladin are most abundant in skeletal and cardiac muscle; palladin is ubiquitously expressed in the organs of developing vertebrates and plays a key role in cellular morphogenesis. The three family members each interact with specific molecular partners with all three binding to alpha-actinin; In addition, palladin also binds to vasodilator-stimulated phosphoprotein (VASP) and ezrin, myotilin binds to filamin and actin, and myopalladin also binds to nebulin and cardiac ankyrin repeat protein (CARP). This group belongs to the I-set of IgSF domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand, but lack a C" strand.


Pssm-ID: 409405 [Multi-domain]  Cd Length: 91  Bit Score: 52.50  E-value: 1.89e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 2613 TIKSGRTHKWSVDVLGEPIPELHWSwRDDIPLTNGDRIKI--ENVDYHTdFSITNVLRKDSGFYTLKAENRNGIDRETVE 2690
Cdd:cd05744    11 EVQEGRLCRFDCKVSGLPTPDLFWQ-LNGKPVRPDSAHKMlvRENGRHS-LIIEPVTKRDAGIYTCIARNRAGENSFNAE 88

                  ...
gi 281359561 2691 LVV 2693
Cdd:cd05744    89 LVV 91
IgI_telokin-like cd20973
immunoglobulin-like domain of telokin and similar proteins; a member of the I-set of IgSF ...
8751-8829 1.99e-07

immunoglobulin-like domain of telokin and similar proteins; a member of the I-set of IgSF domains; The members here are composed of the immunoglobulin (Ig) domain in telokin, the C-terminal domain of myosin light chain kinase which is identical to telokin, and similar proteins. The Ig superfamily (IgSF) is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. Unlike the V-set, one of the distinctive features of I-set domains is the lack of a C" strand. The structure of the telokin Ig domain lacks this strand and thus it belongs to the I-set of the IgSF. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors, the hemolymph protein hemolin, the muscle proteins titin, telokin, and twitchin, the neuronal adhesion molecule axonin-1, and the signaling molecule semaphorin 4D that is involved in axonal guidance, immune function and angiogenesis.


Pssm-ID: 409565 [Multi-domain]  Cd Length: 88  Bit Score: 52.58  E-value: 1.99e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 8751 VRDGDAVNLACRIIGAQHFDVVWLHNNKEIKPSKDFQYT-NEANIYRLQIAEIFPEDGGTYTCEAFNDIGESFSTCTINV 8829
Cdd:cd20973     9 VVEGSAARFDCKVEGYPDPEVKWMKDDNPIVESRRFQIDqDEDGLCSLIISDVCGDDSGKYTCKAVNSLGEATCSAELTV 88
IgI_1_MuSK cd20970
agrin-responsive first immunoglobulin-like domains (Ig1) of the MuSK ectodomain; a member of ...
7648-7737 2.05e-07

agrin-responsive first immunoglobulin-like domains (Ig1) of the MuSK ectodomain; a member of the I-set of IgSF domains; The members here are composed of the first immunoglobulin-like domains (Ig1) of the Muscle-specific kinase (MuSK). MuSK is a receptor tyrosine kinase specifically expressed in skeletal muscle, where it plays a central role in the formation and maintenance of the neuromuscular junction (NMJ). MuSK is activated by agrin, a neuron-derived heparan sulfate proteoglycan. The activation of MUSK in myotubes regulates the formation of NMJs through the regulation of different processes including the specific expression of genes in subsynaptic nuclei, the reorganization of the actin cytoskeleton and the clustering of the acetylcholine receptors (AChR) in the postsynaptic membrane. The Ig superfamily (IgSF) is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. Unlike the V-set, one of the distinctive features of I-set domains is the lack of a C" strand. The structure of the MuSK lacks this strand and thus it belongs to the I-set of the IgSF. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors, the hemolymph protein hemolin, the muscle proteins titin, telokin, and twitchin, the neuronal adhesion molecule axonin-1, and the signaling molecule semaphorin 4D that is involved in axonal guidance, immune function and angiogenesis.


Pssm-ID: 409562 [Multi-domain]  Cd Length: 92  Bit Score: 52.51  E-value: 2.05e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 7648 PLIVKPLR--DANCIQNHNAQFTCTINGVPKPTISWY-KGAREISNGARYHMYSEGDNhfLNINDVFGEDADEYVCRAVN 7724
Cdd:cd20970     1 PVISTPQPsfTVTAREGENATFMCRAEGSPEPEISWTrNGNLIIEFNTRYIVRENGTT--LTIRNIRRSDMGIYLCIASN 78
                          90
                  ....*....|....
gi 281359561 7725 KA-GAKSTRATLAI 7737
Cdd:cd20970    79 GVpGSVEKRITLQV 92
IgI_1_Titin_Z1z2-like cd20974
First Ig-like domain of the giant muscle protein titin Z1z2 in the sarcomeric Z-disk and ...
2311-2396 2.29e-07

First Ig-like domain of the giant muscle protein titin Z1z2 in the sarcomeric Z-disk and similar proteins; a member of the I-set of IgSF domains; The members here are composed of the first immunoglobulin (Ig)-like domain of the giant muscle protein titin Z1z2 in the sarcomeric Z-disk and similar proteins. Titin is a key component in the assembly and functioning of vertebrate striated muscles. By providing connections at the level of individual microfilaments, it contributes to the fine balance of forces between the two halves of the sarcomere. The Ig superfamily (IgSF) is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. Unlike the V-set, one of the distinctive features of I-set domains is the lack of a C" strand. The structure of the titin Z1z2 lacks this strand and thus it belongs to the I-set of the IgSF. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors, the hemolymph protein hemolin, the muscle proteins titin, telokin, and twitchin, the neuronal adhesion molecule axonin-1, and the signaling molecule semaphorin 4D that is involved in axonal guidance, immune function and angiogenesis.


Pssm-ID: 409566 [Multi-domain]  Cd Length: 93  Bit Score: 52.36  E-value: 2.29e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 2311 LKNVTVKKGQTIRFDIKYDGEPEPAATWVKGTDNLKFDNQ-RICLDQLERNSSITIKKSVRKDTGKYKLVLSNSSGTIES 2389
Cdd:cd20974     7 LQSVVVLEGSTATFEAHVSGKPVPEVSWFRDGQVISTSTLpGVQISFSDGRAKLSIPAVTKANSGRYSLTATNGSGQATS 86

                  ....*..
gi 281359561 2390 EAQVVVL 2396
Cdd:cd20974    87 TAELLVL 93
Ig_Titin_like cd05748
Immunoglobulin (Ig)-like domain of titin and similar proteins; The members here are composed ...
242-320 2.46e-07

Immunoglobulin (Ig)-like domain of titin and similar proteins; The members here are composed of the immunoglobulin (Ig)-like domain found in titin-like proteins and similar proteins. Titin (also called connectin) is a fibrous sarcomeric protein specifically found in vertebrate striated muscle. Titin is a giant protein; depending on isoform composition, it ranges from 2970 to 3700 kDa, and is of a length that spans half a sarcomere. Titin largely consists of multiple repeats of Ig-like and fibronectin type 3 (FN-III)-like domains. Titin connects the ends of myosin thick filaments to Z disks and extends along the thick filament to the H zone. It appears to function similarly to an elastic band, keeping the myosin filaments centered in the sarcomere during muscle contraction or stretching. Within the sarcomere, titin is also attached to or is associated with myosin binding protein C (MyBP-C). MyBP-C appears to contribute to the generation of passive tension by titin and like titin has repeated Ig-like and FN-III domains. Also included in this group are worm twitchin and insect projectin, thick filament proteins of invertebrate muscle which also have repeated Ig-like and FN-III domains.


Pssm-ID: 409406 [Multi-domain]  Cd Length: 82  Bit Score: 51.82  E-value: 2.46e-07
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 281359561  242 GGNVTFECRCVGDPTPTVTWSHGETELNESNRYKMSLTMDQklyhiACLEISSVVSSDQGEYRAQAKNKHGSGVATINL 320
Cdd:cd05748     7 GESLRLDIPIKGRPTPTVTWSKDGQPLKETGRVQIETTASS-----TSLVIKNAKRSDSGKYTLTLKNSAGEKSATINV 80
IgI_APEG-1_like cd20975
Immunoglobulin-like domain of human Aortic Preferentially Expressed Protein-1 (APEG-1) and ...
3503-3588 2.55e-07

Immunoglobulin-like domain of human Aortic Preferentially Expressed Protein-1 (APEG-1) and similar proteins; a member of the I-set of IgSF domains; The members here are composed of the immunoglobulin I-set (IgI) domain of the Human Aortic Preferentially Expressed Protein-1 (APEG-1) and similar proteins. APEG-1 is a novel specific smooth muscle differentiation marker predicted to play a role in the growth and differentiation of arterial smooth muscle cells (SMCs). The Ig superfamily (IgSF) is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. Unlike the V-set, one of the distinctive features of I-set domains is the lack of a C" strand. The structure of the human APEG-1 lacks this strand and thus it belongs to the I-set of the IgSF. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors, the hemolymph protein hemolin, the muscle proteins titin, telokin, and twitchin, the neuronal adhesion molecule axonin-1, and the signaling molecule semaphorin 4D that is involved in axonal guidance, immune function and angiogenesis.


Pssm-ID: 409567  Cd Length: 91  Bit Score: 52.09  E-value: 2.55e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 3503 RVNLKPVIVKTGLSISLDINIRGEPAPKVEWFFNNSSVTSDEHSVKIDNVDYNTKFFVMRAQRSQSGKYIIKATNEVG-- 3580
Cdd:cd20975     4 KVSLMDQSVREGQDVIMSIRVQGEPKPVVSWLRNRQPVRPDQRRFAEEAEGGLCRLRILAAERGDAGFYTCKAVNEYGar 83

                  ....*...
gi 281359561 3581 EDEAELEV 3588
Cdd:cd20975    84 QCEARLEV 91
IgI_8_hMLCK_like cd05762
Eighth immunoglobulin (Ig)-like domain of human myosin light-chain kinase (MLCK) and similar ...
3213-3299 2.59e-07

Eighth immunoglobulin (Ig)-like domain of human myosin light-chain kinase (MLCK) and similar protein; member of the I-set of IgSF domains; The members here are composed of the eighth immunoglobulin (Ig)-like domain of human myosin light-chain kinase (MLCK) and similar proteins. Myosin light-chain kinase (MLCK) is a key regulator of different forms of cell motility involving actin and myosin II. Agonist stimulation of smooth muscle cells increases cytosolic Ca2+ which binds calmodulin. This Ca2+-calmodulin complex in turn binds to and activates MLCK. Activated MLCK leads to the phosphorylation of the 20 kDa myosin regulatory light chain (RLC) of myosin II and the stimulation of actin-activated myosin MgATPase activity. MLCK is widely present in vertebrate tissues; it phosphorylates the 20 kDa RLC of both smooth and nonmuscle myosin II. Phosphorylation leads to the activation of the myosin motor domain and altered structural properties of myosin II. In smooth muscle MLCK it is involved in initiating contraction. In nonmuscle cells, MLCK may participate in cell division and cell motility; it has been suggested MLCK plays a role in cardiomyocyte differentiation and contraction through regulation of nonmuscle myosin II.


Pssm-ID: 409419  Cd Length: 99  Bit Score: 52.26  E-value: 2.59e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 3213 KVRAGQPVKFDVDVKGEPAPSLTWFLKETELTSTGQVRLENIDYNTKLTLLDTDRKQSGQYKLRAENINGVDEAVVEVII 3292
Cdd:cd05762    12 KVRAGESVELFCKVTGTQPITCTWMKFRKQIQEGEGIKIENTENSSKLTITEGQQEHCGCYTLEVENKLGSRQAQVNLTV 91

                  ....*..
gi 281359561 3293 LDKPSKP 3299
Cdd:cd05762    92 VDKPDPP 98
IG_like smart00410
Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.
350-425 2.61e-07

Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.


Pssm-ID: 214653 [Multi-domain]  Cd Length: 85  Bit Score: 52.12  E-value: 2.61e-07
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 281359561    350 LIMECVLEAHPVPDIVWYC-SEKEICNNQRTKmtrkaITKDSYILTLEIQNPTKEDGGNYRCNAINMYGESNANIAL 425
Cdd:smart00410   12 VTLSCEASGSPPPEVTWYKqGGKLLAESGRFS-----VSRSGSTSTLTISNVTPEDSGTYTCAATNSSGSASSGTTL 83
IgI_Titin_like cd05747
Immunoglobulin (Ig)-like domain of human titin C terminus and similar proteins; member of the ...
3208-3286 2.62e-07

Immunoglobulin (Ig)-like domain of human titin C terminus and similar proteins; member of the I-set of Ig superfamily (IgSF) domains; The members here are composed of the fifth immunoglobulin (Ig)-like domain from the C-terminus of human titin x and similar proteins. Titin (also called connectin) is a fibrous sarcomeric protein specifically found in vertebrate striated muscle. Titin is gigantic; depending on isoform composition it ranges from 2970 to 3700 kDa, and is of a length that spans half a sarcomere. Titin largely consists of multiple repeats of Ig-like and fibronectin type 3 (FN-III)-like domains. Titin connects the ends of myosin thick filaments to Z disks and extends along the thick filament to the H zone and appears to function similar to an elastic band, keeping the myosin filaments centered in the sarcomere during muscle contraction or stretching. This group belongs to the I-set of IgSF domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand, but lack a C" strand.


Pssm-ID: 143224 [Multi-domain]  Cd Length: 92  Bit Score: 52.36  E-value: 2.62e-07
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 281359561 3208 KMKPIKVRAGQPVKFDVDVKGEPAPSLTWFLKETELTSTGQVRLENIDYNTKLTLLDTDRKQSGQYKLRAENINGVDEA 3286
Cdd:cd05747     9 KPRSLTVSEGESARFSCDVDGEPAPTVTWMREGQIIVSSQRHQITSTEYKSTFEISKVQMSDEGNYTVVVENSEGKQEA 87
IgI_4_MYLK-like cd20976
Fourth Ig-like domain from smooth muscle myosin light chain kinase and similar domains ; a ...
8436-8516 3.32e-07

Fourth Ig-like domain from smooth muscle myosin light chain kinase and similar domains ; a member of the I-set of IgSF domains; The members here are composed of the fourth immunoglobulin (Ig)-like domain from smooth muscle myosin light chain kinase (MYLK) and similar domains. The Ig superfamily (IgSF) is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. Unlike the V-set, one of the distinctive features of I-set domains is the lack of a C" strand. The structure of this group shows that the fourth Ig-like domain from myosin light chain kinase lacks this strand and thus belongs to the I-set of the IgSF. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors, the hemolymph protein hemolin, the muscle proteins titin, telokin, and twitchin, the neuronal adhesion molecule axonin-1, and the signaling molecule semaphorin 4D that is involved in axonal guidance, immune function and angiogenesis.


Pssm-ID: 409568 [Multi-domain]  Cd Length: 90  Bit Score: 51.87  E-value: 3.32e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 8436 APSFTFLLRP-RVMQARDTCkLLCCLSGKPVPNVRWYKDGRELSKYEYAMTHSDGVVTMEIIDCKPSDSGKYSCKATNCH 8514
Cdd:cd20976     1 APSFSSVPKDlEAVEGQDFV-AQCSARGKPVPRITWIRNAQPLQYAADRSTCEAGVGELHIQDVLPEDHGTYTCLAKNAA 79

                  ..
gi 281359561 8515 GT 8516
Cdd:cd20976    80 GQ 81
COG4733 COG4733
Phage-related protein, tail protein J [Mobilome: prophages, transposons];
4692-4972 3.42e-07

Phage-related protein, tail protein J [Mobilome: prophages, transposons];


Pssm-ID: 443767 [Multi-domain]  Cd Length: 978  Bit Score: 58.03  E-value: 3.42e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 4692 LRNITLSSGTALKLDANITGEPAPKVEWklsnyhlqsgknvTIETPDYYTKLV-IRPTQRSDSGEYLVTATN-TSGKDSV 4769
Cdd:COG4733   452 ARTVQSVAGRTLTVSTAYSETPEAGAVW-------------AFGPDELETQLFrVVSIEENEDGTYTITAVQhAPEKYAA 518
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 4770 LVNVVITD-KPSPPNGPLQISDVH--------KEGCHLKWKRPSDDGGTPIEYfqidklEPETGCWIPSCRSTEPQVDVT 4840
Cdd:COG4733   519 IDAGAFDDvPPQWPPVNVTTSESLsvvaqgtaVTTLTVSWDAPAGAVAYEVEW------RRDDGNWVSVPRTSGTSFEVP 592
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 4841 GLSPGNeYKFRVSAVNAEGESQPLVGDESIVARNPFDEPGKPENLKATDwDKDHVDLAWTPPLidgGSPISCYIIEKQDk 4920
Cdd:COG4733   593 GIYAGD-YEVRVRAINALGVSSAWAASSETTVTGKTAPPPAPTGLTATG-GLGGITLSWSFPV---DADTLRTEIRYST- 666
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 281359561 4921 YGKWERAL--DVPADQCKATIPDLVEGQTYKFRVSAVNAAG-------TGEPSDSTPPIIA 4972
Cdd:COG4733   667 TGDWASATvaQALYPGNTYTLAGLKAGQTYYYRARAVDRSGnvsawwvSGQASADAAGILD 727
Ig4_Peroxidasin cd05746
Fourth immunoglobulin (Ig)-like domain of peroxidasin; The members here are composed of the ...
8651-8720 3.50e-07

Fourth immunoglobulin (Ig)-like domain of peroxidasin; The members here are composed of the fourth immunoglobulin (Ig)-like domain in peroxidasin. Peroxidasin has a peroxidase domain and interacting extracellular motifs containing four Ig-like domains. It has been suggested that peroxidasin is secreted, and has functions related to the stabilization of the extracellular matrix. It may play a part in various other important processes such as removal and destruction of cells which have undergone programmed cell death and protection of the organism against non-self.


Pssm-ID: 143223  Cd Length: 69  Bit Score: 51.03  E-value: 3.50e-07
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 8651 LTCYVKGDPEPQISWSKNGKSLSSSDILDLRYKngiATLTINEVFPEDEGVITCTATNSVGAVETKCKLT 8720
Cdd:cd05746     3 IPCSAQGDPEPTITWNKDGVQVTESGKFHISPE---GYLAIRDVGVADQGRYECVARNTIGYASVSMVLS 69
IG_like smart00410
Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.
23-101 3.60e-07

Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.


Pssm-ID: 214653 [Multi-domain]  Cd Length: 85  Bit Score: 51.74  E-value: 3.60e-07
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 281359561     23 GNRLIFECQLLSSPKPDIEWFRSDNKVVEDvRTKFKIQpvgENKYTVVLELDDVVETDAGLYKVKAKNKSGEVSASINL 101
Cdd:smart00410    9 GESVTLSCEASGSPPPEVTWYKQGGKLLAE-SGRFSVS---RSGSTSTLTISNVTPEDSGTYTCAATNSSGSASSGTTL 83
IgI_M-protein_C cd05891
C-terminal immunoglobulin (Ig)-like domain of M-protein; member of the I-set of Ig superfamily ...
549-636 3.61e-07

C-terminal immunoglobulin (Ig)-like domain of M-protein; member of the I-set of Ig superfamily (IgSF) domains; The members here are composed of the C-terminal immunoglobulin (Ig)-like domain of M-protein (also known as myomesin-2). M-protein is a structural protein localized to the M-band, a transverse structure in the center of the sarcomere, and is a candidate for M-band bridges. M-protein is modular consisting mainly of repetitive IG-like and fibronectin type III (FnIII) domains and has a muscle-type specific expression pattern. M-protein is present in fast fibers.


Pssm-ID: 143299  Cd Length: 92  Bit Score: 51.83  E-value: 3.61e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561  549 PRIVSENNGKLVIMECKVKADPKPDVIWFRNGEVIKESNKIKTFIEQrgdQYYIKLELLDPQLEDSGLYKCNIKNTLGEL 628
Cdd:cd05891     8 PDVVTIMEGKTLNLTCTVFGNPDPEVIWFKNDQDIELSEHYSVKLEQ---GKYASLTIKGVTSEDSGKYSINVKNKYGGE 84

                  ....*...
gi 281359561  629 NANLTLNI 636
Cdd:cd05891    85 TVDVTVSV 92
IgI_1_MuSK cd20970
agrin-responsive first immunoglobulin-like domains (Ig1) of the MuSK ectodomain; a member of ...
7752-7833 3.64e-07

agrin-responsive first immunoglobulin-like domains (Ig1) of the MuSK ectodomain; a member of the I-set of IgSF domains; The members here are composed of the first immunoglobulin-like domains (Ig1) of the Muscle-specific kinase (MuSK). MuSK is a receptor tyrosine kinase specifically expressed in skeletal muscle, where it plays a central role in the formation and maintenance of the neuromuscular junction (NMJ). MuSK is activated by agrin, a neuron-derived heparan sulfate proteoglycan. The activation of MUSK in myotubes regulates the formation of NMJs through the regulation of different processes including the specific expression of genes in subsynaptic nuclei, the reorganization of the actin cytoskeleton and the clustering of the acetylcholine receptors (AChR) in the postsynaptic membrane. The Ig superfamily (IgSF) is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. Unlike the V-set, one of the distinctive features of I-set domains is the lack of a C" strand. The structure of the MuSK lacks this strand and thus it belongs to the I-set of the IgSF. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors, the hemolymph protein hemolin, the muscle proteins titin, telokin, and twitchin, the neuronal adhesion molecule axonin-1, and the signaling molecule semaphorin 4D that is involved in axonal guidance, immune function and angiogenesis.


Pssm-ID: 409562 [Multi-domain]  Cd Length: 92  Bit Score: 51.74  E-value: 3.64e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 7752 TAYFDKGENVVIKIPFTGFPKPRIHWVRDGENIESGGHyTVEVKERHAVLIIRDGSHLDSGPYRITAENEL-GSDTAIIQ 7830
Cdd:cd20970    11 TVTAREGENATFMCRAEGSPEPEISWTRNGNLIIEFNT-RYIVRENGTTLTIRNIRRSDMGIYLCIASNGVpGSVEKRIT 89

                  ...
gi 281359561 7831 VQI 7833
Cdd:cd20970    90 LQV 92
Ig5_Contactin cd04969
Fifth immunoglobulin (Ig) domain of contactin; The members here are composed of the fifth ...
228-317 3.90e-07

Fifth immunoglobulin (Ig) domain of contactin; The members here are composed of the fifth immunoglobulin (Ig) domain of contactins. Contactins are neural cell adhesion molecules and are comprised of six Ig domains followed by four fibronectin type III (FnIII) domains anchored to the membrane by glycosylphosphatidylinositol. The first four Ig domains form the intermolecular binding fragment, which arranges as a compact U-shaped module via contacts between Ig domains 1 and 4, and between Ig domains 2 and 3. Contactin-2 (TAG-1, axonin-1) may play a part in the neuronal processes of neurite outgrowth, axon guidance and fasciculation, and neuronal migration. This group also includes contactin-1 and contactin-5. The different contactins show different expression patterns in the central nervous system. During development and in adulthood, contactin-2 is transiently expressed in subsets of central and peripheral neurons. Contactin-5 is expressed specifically in the rat postnatal nervous system, peaking at about 3 weeks postnatal, and a lack of contactin-5 (NB-2) results in an impairment of neuronal activity in the rat auditory system. Contactin-5 is highly expressed in the adult human brain in the occipital lobe and in the amygdala. Contactin-1 is differentially expressed in tumor tissues and may, through a RhoA mechanism, facilitate invasion and metastasis of human lung adenocarcinoma.


Pssm-ID: 409358 [Multi-domain]  Cd Length: 89  Bit Score: 51.69  E-value: 3.90e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561  228 PTFTERPVIRQS--EDGGNVTFECRCVGDPTPTVTWSHGETELNESNRykMSLTMDqklyhiACLEISSVVSSDQGEYRA 305
Cdd:cd04969     1 PDFELNPVKKKIlaAKGGDVIIECKPKASPKPTISWSKGTELLTNSSR--ICILPD------GSLKIKNVTKSDEGKYTC 72
                          90
                  ....*....|..
gi 281359561  306 QAKNKHGSGVAT 317
Cdd:cd04969    73 FAVNFFGKANST 84
Ig cd00096
Immunoglobulin domain; The members here are composed of the immunoglobulin (Ig) domain found ...
8329-8398 4.03e-07

Immunoglobulin domain; The members here are composed of the immunoglobulin (Ig) domain found in the Ig superfamily. The Ig superfamily is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. Members of this group are components of immunoglobulin, neuroglia, cell surface glycoproteins, including T-cell receptors, CD2, CD4, CD8, and membrane glycoproteins, including butyrophilin and chondroitin sulfate proteoglycan core protein. A predominant feature of most Ig domains is a disulfide bridge connecting the two beta-sheets with a tryptophan residue packed against the disulfide bond. Ig superfamily (IgSF) domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. Typically, the V-set domains have A, B, E, and D strands in one sheet and A', G, F, C, C' and C" in the other. The structures in C1-set are smaller than those in the V-set; they have one beta sheet that is formed by strands A, B, E, and D and the other by strands G, F, C, and C'. Moreover, a C1-set Ig domain contains a short C' strand (three residues) and lacks A' and C" strand. Unlike other Ig domain sets, C2-set structures do not have a D strand. Like the V-set Ig domains, members of the I-set have a discontinuous A strand, but lack a C" strand.


Pssm-ID: 409353 [Multi-domain]  Cd Length: 70  Bit Score: 50.79  E-value: 4.03e-07
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 8329 VKFYCRCIAIATPTLTWSHNNIELRQSVKFMKRYVGDDYYFIINRVKLDDRGEYIIRAENHYGSREEVVF 8398
Cdd:cd00096     1 VTLTCSASGNPPPTITWYKNGKPLPPSSRDSRRSELGNGTLTISNVTLEDSGTYTCVASNSAGGSASASV 70
IgI_8_hMLCK_like cd05762
Eighth immunoglobulin (Ig)-like domain of human myosin light-chain kinase (MLCK) and similar ...
6176-6262 4.06e-07

Eighth immunoglobulin (Ig)-like domain of human myosin light-chain kinase (MLCK) and similar protein; member of the I-set of IgSF domains; The members here are composed of the eighth immunoglobulin (Ig)-like domain of human myosin light-chain kinase (MLCK) and similar proteins. Myosin light-chain kinase (MLCK) is a key regulator of different forms of cell motility involving actin and myosin II. Agonist stimulation of smooth muscle cells increases cytosolic Ca2+ which binds calmodulin. This Ca2+-calmodulin complex in turn binds to and activates MLCK. Activated MLCK leads to the phosphorylation of the 20 kDa myosin regulatory light chain (RLC) of myosin II and the stimulation of actin-activated myosin MgATPase activity. MLCK is widely present in vertebrate tissues; it phosphorylates the 20 kDa RLC of both smooth and nonmuscle myosin II. Phosphorylation leads to the activation of the myosin motor domain and altered structural properties of myosin II. In smooth muscle MLCK it is involved in initiating contraction. In nonmuscle cells, MLCK may participate in cell division and cell motility; it has been suggested MLCK plays a role in cardiomyocyte differentiation and contraction through regulation of nonmuscle myosin II.


Pssm-ID: 409419  Cd Length: 99  Bit Score: 51.88  E-value: 4.06e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 6176 KVRAGEPVNLNIPISGAPTPTIEWKRGDLKLEEGKRISYETNSERTLFRIDDSNRRDSGKYTVTAANEFGKDTADIEVIV 6255
Cdd:cd05762    12 KVRAGESVELFCKVTGTQPITCTWMKFRKQIQEGEGIKIENTENSSKLTITEGQQEHCGCYTLEVENKLGSRQAQVNLTV 91

                  ....*..
gi 281359561 6256 VDKPSPP 6262
Cdd:cd05762    92 VDKPDPP 98
IgI_Myotilin_C cd05892
C-terminal immunoglobulin (Ig)-like domain of myotilin; member of the I-set of Ig superfamily ...
228-319 4.35e-07

C-terminal immunoglobulin (Ig)-like domain of myotilin; member of the I-set of Ig superfamily (IgSF) domains; The members here are composed of the C-terminal immunoglobulin (Ig)-like domain of myotilin. Mytolin belongs to the palladin-myotilin-myopalladin family. Proteins belonging to the latter family contain multiple Ig-like domains and function as scaffolds, modulating the actin cytoskeleton. Myotilin is most abundant in skeletal and cardiac muscle and is involved in maintaining sarcomere integrity. It binds to alpha-actinin, filamin, and actin. Mutations in myotilin lead to muscle disorders. This group belongs to the I-set of IgSF domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand, but lack a C" strand.


Pssm-ID: 409473  Cd Length: 92  Bit Score: 51.69  E-value: 4.35e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561  228 PTFTERPVIRQSEDGGNVTFECRCVGDPTPTVTWSHgETELNESNRYKMSLTMDQKLYHiaCLEISSVVSSDQGEYRAQA 307
Cdd:cd05892     1 PMFIQKPQNKKVLEGDPVRLECQISAIPPPQIFWKK-NNEMLQYNTDRISLYQDNCGRI--CLLIQNANKKDAGWYTVSA 77
                          90
                  ....*....|..
gi 281359561  308 KNkhGSGVATIN 319
Cdd:cd05892    78 VN--EAGVVSCN 87
IgI_Myotilin_C_like cd05744
Immunoglobulin (Ig)-like domain of myotilin, palladin, and myopalladin; member of the I-set of ...
2911-2995 4.39e-07

Immunoglobulin (Ig)-like domain of myotilin, palladin, and myopalladin; member of the I-set of Ig superfamily (IgSF) domains; The members here are composed of the immunoglobulin (Ig)-like domain in myotilin, palladin, and myopalladin. Myotilin, palladin, and myopalladin function as scaffolds that regulate actin organization. Myotilin and myopalladin are most abundant in skeletal and cardiac muscle; palladin is ubiquitously expressed in the organs of developing vertebrates and plays a key role in cellular morphogenesis. The three family members each interact with specific molecular partners with all three binding to alpha-actinin; In addition, palladin also binds to vasodilator-stimulated phosphoprotein (VASP) and ezrin, myotilin binds to filamin and actin, and myopalladin also binds to nebulin and cardiac ankyrin repeat protein (CARP). This group belongs to the I-set of IgSF domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand, but lack a C" strand.


Pssm-ID: 409405 [Multi-domain]  Cd Length: 91  Bit Score: 51.34  E-value: 4.39e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 2911 PLLIRA--------GKPIRYDVNVRGEPAPVITWYQNDKELKPEelpssSEIKNIPYNTKIS--IIETV-RKHTGIYKII 2979
Cdd:cd05744     1 PHFLQApgdlevqeGRLCRFDCKVSGLPTPDLFWQLNGKPVRPD-----SAHKMLVRENGRHslIIEPVtKRDAGIYTCI 75
                          90
                  ....*....|....*.
gi 281359561 2980 AVNEHGQDEATVEVNI 2995
Cdd:cd05744    76 ARNRAGENSFNAELVV 91
IgI_telokin-like cd20973
immunoglobulin-like domain of telokin and similar proteins; a member of the I-set of IgSF ...
7260-7344 4.80e-07

immunoglobulin-like domain of telokin and similar proteins; a member of the I-set of IgSF domains; The members here are composed of the immunoglobulin (Ig) domain in telokin, the C-terminal domain of myosin light chain kinase which is identical to telokin, and similar proteins. The Ig superfamily (IgSF) is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. Unlike the V-set, one of the distinctive features of I-set domains is the lack of a C" strand. The structure of the telokin Ig domain lacks this strand and thus it belongs to the I-set of the IgSF. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors, the hemolymph protein hemolin, the muscle proteins titin, telokin, and twitchin, the neuronal adhesion molecule axonin-1, and the signaling molecule semaphorin 4D that is involved in axonal guidance, immune function and angiogenesis.


Pssm-ID: 409565 [Multi-domain]  Cd Length: 88  Bit Score: 51.42  E-value: 4.80e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 7260 LQDKVAPFGKDYTLQCAASGKPSPTARWLRNGKEIQMNGGRMTCDSKDGVFRLHISNVQTGDDGDYTCEAMNSLGFVNTS 7339
Cdd:cd20973     4 LRDKEVVEGSAARFDCKVEGYPDPEVKWMKDDNPIVESRRFQIDQDEDGLCSLIISDVCGDDSGKYTCKAVNSLGEATCS 83

                  ....*
gi 281359561 7340 GYLKI 7344
Cdd:cd20973    84 AELTV 88
IgI_titin_I1-like cd20951
Immunoglobulin domain I1 of the titin I-band and similar proteins; a member of the I-set of ...
438-532 4.81e-07

Immunoglobulin domain I1 of the titin I-band and similar proteins; a member of the I-set of IgSF domains; The members here are composed of the immunoglobulin domain I1 of the titin I-band and similar proteins. Titin is a key component in the assembly and functioning of vertebrate striated muscles. By providing connections at the level of individual microfilaments, it contributes to the fine balance of forces between the two halves of the sarcomere. The Ig superfamily (IgSF) is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. The two sheets are linked together by a conserved disulfide bond between B strand and F strand. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. The Ig I1 domain of the titin I-band is a member of the I-set Ig domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand but lack a C" strand. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors, the hemolymph protein hemolin, the muscle proteins titin, telokin, and twitchin, the neuronal adhesion molecule axonin-1, and the signaling molecule semaphorin 4D that is involved in axonal guidance, immune function and angiogenesis.


Pssm-ID: 409543 [Multi-domain]  Cd Length: 94  Bit Score: 51.65  E-value: 4.81e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561  438 PSFIEKPRIIPNESGTLITMKCKCKAKPEPTVTWYRGQDLVEKSKKIKIntTVIAEDTYELTLEIKDPGATDGGTYRCNV 517
Cdd:cd20951     1 PEFIIRLQSHTVWEKSDAKLRVEVQGKPDPEVKWYKNGVPIDPSSIPGK--YKIESEYGVHVLHIRRVTVEDSAVYSAVA 78
                          90
                  ....*....|....*
gi 281359561  518 KNEYGESNANLNLNI 532
Cdd:cd20951    79 KNIHGEASSSASVVV 93
fn3 pfam00041
Fibronectin type III domain;
6063-6148 5.40e-07

Fibronectin type III domain;


Pssm-ID: 394996 [Multi-domain]  Cd Length: 85  Bit Score: 50.88  E-value: 5.40e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561  6063 GAPGKPELTDSDKNHITIKWKQPiSNGGSPIIGYDIERRDVNTGRwikingqpvPTAEYQDDRVTSNH---------QYQ 6133
Cdd:pfam00041    1 SAPSNLTVTDVTSTSLTVSWTPP-PDGNGPITGYEVEYRPKNSGE---------PWNEITVPGTTTSVtltglkpgtEYE 70
                           90
                   ....*....|....*
gi 281359561  6134 YRISAVNAAGNGKTS 6148
Cdd:pfam00041   71 VRVQAVNGGGEGPPS 85
IgI_Myotilin_C_like cd05744
Immunoglobulin (Ig)-like domain of myotilin, palladin, and myopalladin; member of the I-set of ...
4991-5069 6.17e-07

Immunoglobulin (Ig)-like domain of myotilin, palladin, and myopalladin; member of the I-set of Ig superfamily (IgSF) domains; The members here are composed of the immunoglobulin (Ig)-like domain in myotilin, palladin, and myopalladin. Myotilin, palladin, and myopalladin function as scaffolds that regulate actin organization. Myotilin and myopalladin are most abundant in skeletal and cardiac muscle; palladin is ubiquitously expressed in the organs of developing vertebrates and plays a key role in cellular morphogenesis. The three family members each interact with specific molecular partners with all three binding to alpha-actinin; In addition, palladin also binds to vasodilator-stimulated phosphoprotein (VASP) and ezrin, myotilin binds to filamin and actin, and myopalladin also binds to nebulin and cardiac ankyrin repeat protein (CARP). This group belongs to the I-set of IgSF domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand, but lack a C" strand.


Pssm-ID: 409405 [Multi-domain]  Cd Length: 91  Bit Score: 50.96  E-value: 6.17e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 4991 IKAGQSFTFDCKVSGEPAPQTKWLLKKKEVYSKDNVKVTnVDYNTK--LKVNSATRSDSGIYTVFAENANGEDSADVKVT 5068
Cdd:cd05744    12 VQEGRLCRFDCKVSGLPTPDLFWQLNGKPVRPDSAHKML-VRENGRhsLIIEPVTKRDAGIYTCIARNRAGENSFNAELV 90

                  .
gi 281359561 5069 V 5069
Cdd:cd05744    91 V 91
IgI_4_Dscam cd20956
Fourth immunoglobulin domain of the Drosophila melanogaster Dscam protein, and similar domains; ...
146-203 6.38e-07

Fourth immunoglobulin domain of the Drosophila melanogaster Dscam protein, and similar domains; a member of the I-set of IgSF domains; The members here are composed of the fourth immunoglobulin domain of the Drosophila melanogaster Down syndrome cell adhesion molecule (DSCAM) protein and similar proteins. Down syndrome cell adhesion molecule (DSCAM) is a cell adhesion molecule that plays critical roles in neural development, including axon guidance and branching, axon target recognition, self-avoidance and synaptic formation. DSCAM belongs to the immunoglobulin superfamily and contributes to defects in the central nervous system in Down syndrome patients. Vertebrate DSCAMs differ from Drosophila Dscam1 in that they lack the extensive alternative splicing that occurs in the insect gene. Drosophila melanogaster Dscam has 38,016 isoforms generated by the alternative splicing of four variable exon clusters, which allows every neuron in the fly to display a distinctive set of Dscam proteins on its cell surface. Drosophila Dscam1 is a cell-surface protein that plays important roles in neural development and axon tiling of neurons. It is shown that thousands of isoforms bind themselves through specific homophilic (self-binding) interactions, a process which mediates cellular self-recognition. Drosophila Dscam2 is also alternatively spliced and plays a key role in the development of two visual system neurons, monopolar cells L1 and L2. This group is a member of the I-set Ig domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand but lack a C" strand.


Pssm-ID: 409548 [Multi-domain]  Cd Length: 96  Bit Score: 51.02  E-value: 6.38e-07
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 281359561  146 PIPAIIWFHNGAAVKESER----HKITVDKDVHSYfatLEILNVTVEDAGKYKVNAKNELGE 203
Cdd:cd20956    29 PLPQITWTLDGFPIPESPRfrvgDYVTSDGDVVSY---VNISSVRVEDGGEYTCTATNDVGS 87
Ig cd00096
Immunoglobulin domain; The members here are composed of the immunoglobulin (Ig) domain found ...
7761-7829 6.70e-07

Immunoglobulin domain; The members here are composed of the immunoglobulin (Ig) domain found in the Ig superfamily. The Ig superfamily is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. Members of this group are components of immunoglobulin, neuroglia, cell surface glycoproteins, including T-cell receptors, CD2, CD4, CD8, and membrane glycoproteins, including butyrophilin and chondroitin sulfate proteoglycan core protein. A predominant feature of most Ig domains is a disulfide bridge connecting the two beta-sheets with a tryptophan residue packed against the disulfide bond. Ig superfamily (IgSF) domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. Typically, the V-set domains have A, B, E, and D strands in one sheet and A', G, F, C, C' and C" in the other. The structures in C1-set are smaller than those in the V-set; they have one beta sheet that is formed by strands A, B, E, and D and the other by strands G, F, C, and C'. Moreover, a C1-set Ig domain contains a short C' strand (three residues) and lacks A' and C" strand. Unlike other Ig domain sets, C2-set structures do not have a D strand. Like the V-set Ig domains, members of the I-set have a discontinuous A strand, but lack a C" strand.


Pssm-ID: 409353 [Multi-domain]  Cd Length: 70  Bit Score: 50.41  E-value: 6.70e-07
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 7761 VVIKIPFTGFPKPRIHWVRDGENIESGGHYTVEVKERHAVLIIRDGSHLDSGPYRITAENEL-GSDTAII 7829
Cdd:cd00096     1 VTLTCSASGNPPPTITWYKNGKPLPPSSRDSRRSELGNGTLTISNVTLEDSGTYTCVASNSAgGSASASV 70
IgI_1_Titin_Z1z2-like cd20974
First Ig-like domain of the giant muscle protein titin Z1z2 in the sarcomeric Z-disk and ...
8632-8721 6.82e-07

First Ig-like domain of the giant muscle protein titin Z1z2 in the sarcomeric Z-disk and similar proteins; a member of the I-set of IgSF domains; The members here are composed of the first immunoglobulin (Ig)-like domain of the giant muscle protein titin Z1z2 in the sarcomeric Z-disk and similar proteins. Titin is a key component in the assembly and functioning of vertebrate striated muscles. By providing connections at the level of individual microfilaments, it contributes to the fine balance of forces between the two halves of the sarcomere. The Ig superfamily (IgSF) is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. Unlike the V-set, one of the distinctive features of I-set domains is the lack of a C" strand. The structure of the titin Z1z2 lacks this strand and thus it belongs to the I-set of the IgSF. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors, the hemolymph protein hemolin, the muscle proteins titin, telokin, and twitchin, the neuronal adhesion molecule axonin-1, and the signaling molecule semaphorin 4D that is involved in axonal guidance, immune function and angiogenesis.


Pssm-ID: 409566 [Multi-domain]  Cd Length: 93  Bit Score: 51.20  E-value: 6.82e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 8632 PEFTKPLHDLTIHDGEQLILTCYVKGDPEPQISWSKNGK--SLSSSDILDLRYKNGIATLTINEVFPEDEGVITCTATNS 8709
Cdd:cd20974     1 PVFTQPLQSVVVLEGSTATFEAHVSGKPVPEVSWFRDGQviSTSTLPGVQISFSDGRAKLSIPAVTKANSGRYSLTATNG 80
                          90
                  ....*....|..
gi 281359561 8710 VGAVETKCKLTI 8721
Cdd:cd20974    81 SGQATSTAELLV 92
I-set pfam07679
Immunoglobulin I-set domain;
4405-4480 7.16e-07

Immunoglobulin I-set domain;


Pssm-ID: 400151 [Multi-domain]  Cd Length: 90  Bit Score: 50.72  E-value: 7.16e-07
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 281359561  4405 GEPIFLDINISGEPAPDVTWNQNNKSVQTTSFSHIENLPYNTKYINNNPERKDTGLYKISAHNFYGQDQVEFQINI 4480
Cdd:pfam07679   15 GESARFTCTVTGTPDPEVSWFKDGQPLRSSDRFKVTYEGGTYTLTISNVQPDDSGKYTCVATNSAGEAEASAELTV 90
IgI_LRIG1-like cd05763
Immunoglobulin (Ig)-like ectodomain of the LRIG1 (Leucine-rich Repeats And Immunoglobulin-like ...
5285-5367 7.82e-07

Immunoglobulin (Ig)-like ectodomain of the LRIG1 (Leucine-rich Repeats And Immunoglobulin-like Domains Protein 1) and similar proteins; member of the I-set of IgSF domains; The members here are composed of subgroup of the immunoglobulin (Ig) domain found in the Ig superfamily. The Ig superfamily is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. A predominant feature of most Ig domains is a disulfide bridge connecting the two beta-sheets with a tryptophan residue packed against the disulfide bond. The ectodomain of LRIG1 has two distinct regions: the proposed 15 LRRs and three Ig-like domains closer to the membrane. LRIG1 has been reported to interact with many receptor tyrosine kinases, GDNF/c-Ret, E-cadherin, JAK/STAT, c-Met, and the EGFR family signaling systems. Immunoglobulin Superfamily (IgSF) domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. The structure of the LRIG1 extracellular Ig domain lacks a C" strand and thus is better described as a member of the I-set of IgSF domains.


Pssm-ID: 409420 [Multi-domain]  Cd Length: 91  Bit Score: 50.70  E-value: 7.82e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 5285 DIKIKAGNVFEFDVPVTGEPLPSKDWTHEGNmiinTD-------RVKISNFDDrtKIRILDAKRSDTGVYTLTARNINGT 5357
Cdd:cd05763     8 DITIRAGSTARLECAATGHPTPQIAWQKDGG----TDfpaarerRMHVMPEDD--VFFIVDVKIEDTGVYSCTAQNSAGS 81
                          90
                  ....*....|
gi 281359561 5358 DRHNVKVTIL 5367
Cdd:cd05763    82 ISANATLTVL 91
Ig cd00096
Immunoglobulin domain; The members here are composed of the immunoglobulin (Ig) domain found ...
350-419 8.15e-07

Immunoglobulin domain; The members here are composed of the immunoglobulin (Ig) domain found in the Ig superfamily. The Ig superfamily is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. Members of this group are components of immunoglobulin, neuroglia, cell surface glycoproteins, including T-cell receptors, CD2, CD4, CD8, and membrane glycoproteins, including butyrophilin and chondroitin sulfate proteoglycan core protein. A predominant feature of most Ig domains is a disulfide bridge connecting the two beta-sheets with a tryptophan residue packed against the disulfide bond. Ig superfamily (IgSF) domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. Typically, the V-set domains have A, B, E, and D strands in one sheet and A', G, F, C, C' and C" in the other. The structures in C1-set are smaller than those in the V-set; they have one beta sheet that is formed by strands A, B, E, and D and the other by strands G, F, C, and C'. Moreover, a C1-set Ig domain contains a short C' strand (three residues) and lacks A' and C" strand. Unlike other Ig domain sets, C2-set structures do not have a D strand. Like the V-set Ig domains, members of the I-set have a discontinuous A strand, but lack a C" strand.


Pssm-ID: 409353 [Multi-domain]  Cd Length: 70  Bit Score: 50.02  E-value: 8.15e-07
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561  350 LIMECVLEAHPVPDIVWYCSEKEICNNQRTKMTRkaitkDSYILTLEIQNPTKEDGGNYRCNAINMYGES 419
Cdd:cd00096     1 VTLTCSASGNPPPTITWYKNGKPLPPSSRDSRRS-----ELGNGTLTISNVTLEDSGTYTCVASNSAGGS 65
IgI_3_Robo cd05725
Third immunoglobulin (Ig)-like domain in Robo (roundabout) receptors; member of the I-set of ...
7665-7735 8.28e-07

Third immunoglobulin (Ig)-like domain in Robo (roundabout) receptors; member of the I-set of Ig superfamily (IgSF) domains; The members here are composed of the third immunoglobulin (Ig)-like domain in Robo (roundabout) receptors. Robo receptors play a role in the development of the central nervous system (CNS), and are receptors of Slit protein. Slit is a repellant secreted by the neural cells in the midline. Slit acts through Robo to prevent most neurons from crossing the midline from either side. Three mammalian Robo homologs (Robo1, Robo2, Robo3), and three mammalian Slit homologs (Slit-1,Slit-2, Slit-3), have been identified. Commissural axons, which cross the midline, express low levels of Robo; longitudinal axons, which avoid the midline, express high levels of Robo. Robo1, Robo2, and Robo3 are expressed by commissural neurons in the vertebrate spinal cord and Slit-1, Slit-2, and Slit-3 are expressed at the ventral midline. Robo-3 is a divergent member of the Robo family which instead of being a positive regulator of Slit responsiveness, antagonizes Slit responsiveness in precrossing axons. The Slit-Robo interaction is mediated by the second leucine-rich repeat (LRR) domain of Slit and the two N-terminal Ig domains of Robo, Ig1 and Ig2. The primary Robo binding site for Slit2 has been shown by surface plasmon resonance experiments and mutational analysis to be the Ig1 domain, while the Ig2 domain has been proposed to harbor a weak secondary binding site. This group belongs to the I-set of IgSF domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand, but lack a C" strand.


Pssm-ID: 409390 [Multi-domain]  Cd Length: 83  Bit Score: 50.47  E-value: 8.28e-07
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 281359561 7665 AQFTCTINGVPKPTISWYKGAREISNGaRYHMYsegDNHFLNINDVFGEDADEYVCRAVNKAGAKSTRATL 7735
Cdd:cd05725    15 AEFQCEVGGDPVPTVRWRKEDGELPKG-RYEIL---DDHSLKIRKVTAGDMGSYTCVAENMVGKIEASATL 81
IgI_Myotilin_C_like cd05744
Immunoglobulin (Ig)-like domain of myotilin, palladin, and myopalladin; member of the I-set of ...
8312-8401 8.43e-07

Immunoglobulin (Ig)-like domain of myotilin, palladin, and myopalladin; member of the I-set of Ig superfamily (IgSF) domains; The members here are composed of the immunoglobulin (Ig)-like domain in myotilin, palladin, and myopalladin. Myotilin, palladin, and myopalladin function as scaffolds that regulate actin organization. Myotilin and myopalladin are most abundant in skeletal and cardiac muscle; palladin is ubiquitously expressed in the organs of developing vertebrates and plays a key role in cellular morphogenesis. The three family members each interact with specific molecular partners with all three binding to alpha-actinin; In addition, palladin also binds to vasodilator-stimulated phosphoprotein (VASP) and ezrin, myotilin binds to filamin and actin, and myopalladin also binds to nebulin and cardiac ankyrin repeat protein (CARP). This group belongs to the I-set of IgSF domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand, but lack a C" strand.


Pssm-ID: 409405 [Multi-domain]  Cd Length: 91  Bit Score: 50.57  E-value: 8.43e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 8312 PRFVIRPSSQFCYEGQSVKFYCRCIAIATPTLTWSHNNIELRQSVKfMKRYV--GDDYYFIINRVKLDDRGEYIIRAENH 8389
Cdd:cd05744     1 PHFLQAPGDLEVQEGRLCRFDCKVSGLPTPDLFWQLNGKPVRPDSA-HKMLVreNGRHSLIIEPVTKRDAGIYTCIARNR 79
                          90
                  ....*....|..
gi 281359561 8390 YGSREEVVFLNV 8401
Cdd:cd05744    80 AGENSFNAELVV 91
I-set pfam07679
Immunoglobulin I-set domain;
5865-5954 8.53e-07

Immunoglobulin I-set domain;


Pssm-ID: 400151 [Multi-domain]  Cd Length: 90  Bit Score: 50.72  E-value: 8.53e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561  5865 PKIITPLNEVRIKCG--LIFhtDIHFIGEPAPEATWTLNSNPLLSNDRSTITSIGHHSVVHTVNCQRSDSGIYHLLLRNS 5942
Cdd:pfam07679    1 PKFTQKPKDVEVQEGesARF--TCTVTGTPDPEVSWFKDGQPLRSSDRFKVTYEGGTYTLTISNVQPDDSGKYTCVATNS 78
                           90
                   ....*....|..
gi 281359561  5943 SGIDEGSFELVV 5954
Cdd:pfam07679   79 AGEAEASAELTV 90
IgI_LRIG1-like cd05763
Immunoglobulin (Ig)-like ectodomain of the LRIG1 (Leucine-rich Repeats And Immunoglobulin-like ...
8438-8525 8.62e-07

Immunoglobulin (Ig)-like ectodomain of the LRIG1 (Leucine-rich Repeats And Immunoglobulin-like Domains Protein 1) and similar proteins; member of the I-set of IgSF domains; The members here are composed of subgroup of the immunoglobulin (Ig) domain found in the Ig superfamily. The Ig superfamily is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. A predominant feature of most Ig domains is a disulfide bridge connecting the two beta-sheets with a tryptophan residue packed against the disulfide bond. The ectodomain of LRIG1 has two distinct regions: the proposed 15 LRRs and three Ig-like domains closer to the membrane. LRIG1 has been reported to interact with many receptor tyrosine kinases, GDNF/c-Ret, E-cadherin, JAK/STAT, c-Met, and the EGFR family signaling systems. Immunoglobulin Superfamily (IgSF) domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. The structure of the LRIG1 extracellular Ig domain lacks a C" strand and thus is better described as a member of the I-set of IgSF domains.


Pssm-ID: 409420 [Multi-domain]  Cd Length: 91  Bit Score: 50.70  E-value: 8.62e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 8438 SFTFLLRPRVMQARDTCKLLCCLSGKPVPNVRWYKDG-------RElsKYEYAMTHSDgvvTMEIIDCKPSDSGKYSCKA 8510
Cdd:cd05763     1 SFTKTPHDITIRAGSTARLECAATGHPTPQIAWQKDGgtdfpaaRE--RRMHVMPEDD---VFFIVDVKIEDTGVYSCTA 75
                          90
                  ....*....|....*
gi 281359561 8511 TNCHGTDETDCVVIV 8525
Cdd:cd05763    76 QNSAGSISANATLTV 90
IgI_5_Robo cd20952
Fifth Ig-like domain of Roundabout (Robo) homolog 1/2, and similar domains; a member of the ...
8456-8516 8.68e-07

Fifth Ig-like domain of Roundabout (Robo) homolog 1/2, and similar domains; a member of the I-set of IgSF domains; The members here are composed of the fifth Ig-like domain of Roundabout (Robo) homolog 1/2 and similar domains. Robo receptors play a role in the development of the central nervous system (CNS), and are receptors of Slit protein. Slit is a repellant secreted by the neural cells in the midline. Slit acts through Robo to prevent most neurons from crossing the midline from either side. Three mammalian Robo homologs (Robo1, -2, and -3), and three mammalian Slit homologs (Slit-1,-2, -3), have been identified. Commissural axons, which cross the midline, express low levels of Robo; longitudinal axons, which avoid the midline, express high levels of Robo. Robo1, -2, and -3 are expressed by commissural neurons in the vertebrate spinal cord and Slits 1, -2, -3 are expressed at the ventral midline. Robo-3 is a divergent member of the Robo family which instead of being a positive regulator of slit responsiveness, antagonizes slit responsiveness in precrossing axons. The Slit-Robo interaction is mediated by the second leucine-rich repeat (LRR) domain of Slit and the two N-terminal Ig domains of Robo, Ig1 and Ig2. The primary Robo binding site for Slit2 has been shown by surface plasmon resonance experiments and mutational analysis to be is the Ig1 domain, while the Ig2 domain has been proposed to harbor a weak secondary binding site. The fifth Ig-like domain of Robo 1 and 2 is a member of the I-set Ig domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand but lack a C" strand. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors


Pssm-ID: 409544 [Multi-domain]  Cd Length: 87  Bit Score: 50.57  E-value: 8.68e-07
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 281359561 8456 LLCCLSGKPVPNVRWYKDGRELS-KYEYAMTHSDGvvTMEIIDCKPSDSGKYSCKATNCHGT 8516
Cdd:cd20952    19 LNCQATGEPVPTISWLKDGVPLLgKDERITTLENG--SLQIKGAEKSDTGEYTCVALNLSGE 78
IgI_titin_I1-like cd20951
Immunoglobulin domain I1 of the titin I-band and similar proteins; a member of the I-set of ...
9-102 8.90e-07

Immunoglobulin domain I1 of the titin I-band and similar proteins; a member of the I-set of IgSF domains; The members here are composed of the immunoglobulin domain I1 of the titin I-band and similar proteins. Titin is a key component in the assembly and functioning of vertebrate striated muscles. By providing connections at the level of individual microfilaments, it contributes to the fine balance of forces between the two halves of the sarcomere. The Ig superfamily (IgSF) is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. The two sheets are linked together by a conserved disulfide bond between B strand and F strand. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. The Ig I1 domain of the titin I-band is a member of the I-set Ig domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand but lack a C" strand. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors, the hemolymph protein hemolin, the muscle proteins titin, telokin, and twitchin, the neuronal adhesion molecule axonin-1, and the signaling molecule semaphorin 4D that is involved in axonal guidance, immune function and angiogenesis.


Pssm-ID: 409543 [Multi-domain]  Cd Length: 94  Bit Score: 50.88  E-value: 8.90e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561    9 PSFVKKPQLHQEDDGNRLIFECQLLSSPKPDIEWFRSDNKV-VEDVRTKFKIqpvgENKYTV-VLELDDVVETDAGLYKV 86
Cdd:cd20951     1 PEFIIRLQSHTVWEKSDAKLRVEVQGKPDPEVKWYKNGVPIdPSSIPGKYKI----ESEYGVhVLHIRRVTVEDSAVYSA 76
                          90
                  ....*....|....*.
gi 281359561   87 KAKNKSGEVSASINLN 102
Cdd:cd20951    77 VAKNIHGEASSSASVV 92
COG4733 COG4733
Phage-related protein, tail protein J [Mobilome: prophages, transposons];
4526-4665 8.94e-07

Phage-related protein, tail protein J [Mobilome: prophages, transposons];


Pssm-ID: 443767 [Multi-domain]  Cd Length: 978  Bit Score: 56.49  E-value: 8.94e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 4526 PDTGIWLPVGRSDGPEYNVDGLVPGhDYKFRVKAVNKEGESEPLETLGSIIAKDPFSVPTKPG--VPEPTDWTAnkvELA 4603
Cdd:COG4733   573 RDDGNWVSVPRTSGTSFEVPGIYAG-DYEVRVRAINALGVSSAWAASSETTVTGKTAPPPAPTglTATGGLGGI---TLS 648
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 281359561 4604 WPEPAsdgGSPIQGYIVEVKDKYSPLWEKALETNSPTPTATVQGLIEGNEYQFRVVALNKGG 4665
Cdd:COG4733   649 WSFPV---DADTLRTEIRYSTTGDWASATVAQALYPGNTYTLAGLKAGQTYYYRARAVDRSG 707
I-set pfam07679
Immunoglobulin I-set domain;
6564-6650 8.96e-07

Immunoglobulin I-set domain;


Pssm-ID: 400151 [Multi-domain]  Cd Length: 90  Bit Score: 50.72  E-value: 8.96e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561  6564 LGKVRDIVCRAGD--DFSIHVpyLAFPKPNAFWYSNDNMLDDNNRVHKHLTDDAASVVVKNSKRADSGQYRLQLKNTSGF 6641
Cdd:pfam07679    4 TQKPKDVEVQEGEsaRFTCTV--TGTPDPEVSWFKDGQPLRSSDRFKVTYEGGTYTLTISNVQPDDSGKYTCVATNSAGE 81

                   ....*....
gi 281359561  6642 DTATINVRV 6650
Cdd:pfam07679   82 AEASAELTV 90
IgI_titin_I1-like cd20951
Immunoglobulin domain I1 of the titin I-band and similar proteins; a member of the I-set of ...
228-323 8.98e-07

Immunoglobulin domain I1 of the titin I-band and similar proteins; a member of the I-set of IgSF domains; The members here are composed of the immunoglobulin domain I1 of the titin I-band and similar proteins. Titin is a key component in the assembly and functioning of vertebrate striated muscles. By providing connections at the level of individual microfilaments, it contributes to the fine balance of forces between the two halves of the sarcomere. The Ig superfamily (IgSF) is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. The two sheets are linked together by a conserved disulfide bond between B strand and F strand. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. The Ig I1 domain of the titin I-band is a member of the I-set Ig domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand but lack a C" strand. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors, the hemolymph protein hemolin, the muscle proteins titin, telokin, and twitchin, the neuronal adhesion molecule axonin-1, and the signaling molecule semaphorin 4D that is involved in axonal guidance, immune function and angiogenesis.


Pssm-ID: 409543 [Multi-domain]  Cd Length: 94  Bit Score: 50.88  E-value: 8.98e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561  228 PTFTERPVIRQSEDGGNVTFECRCVGDPTPTVTWSHGETELNESN---RYKMsltmdQKLYHIACLEISSVVSSDQGEYR 304
Cdd:cd20951     1 PEFIIRLQSHTVWEKSDAKLRVEVQGKPDPEVKWYKNGVPIDPSSipgKYKI-----ESEYGVHVLHIRRVTVEDSAVYS 75
                          90
                  ....*....|....*....
gi 281359561  305 AQAKNKHGSGVATINLNFE 323
Cdd:cd20951    76 AVAKNIHGEASSSASVVVE 94
IgI_LRIG1-like cd05763
Immunoglobulin (Ig)-like ectodomain of the LRIG1 (Leucine-rich Repeats And Immunoglobulin-like ...
544-636 9.14e-07

Immunoglobulin (Ig)-like ectodomain of the LRIG1 (Leucine-rich Repeats And Immunoglobulin-like Domains Protein 1) and similar proteins; member of the I-set of IgSF domains; The members here are composed of subgroup of the immunoglobulin (Ig) domain found in the Ig superfamily. The Ig superfamily is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. A predominant feature of most Ig domains is a disulfide bridge connecting the two beta-sheets with a tryptophan residue packed against the disulfide bond. The ectodomain of LRIG1 has two distinct regions: the proposed 15 LRRs and three Ig-like domains closer to the membrane. LRIG1 has been reported to interact with many receptor tyrosine kinases, GDNF/c-Ret, E-cadherin, JAK/STAT, c-Met, and the EGFR family signaling systems. Immunoglobulin Superfamily (IgSF) domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. The structure of the LRIG1 extracellular Ig domain lacks a C" strand and thus is better described as a member of the I-set of IgSF domains.


Pssm-ID: 409420 [Multi-domain]  Cd Length: 91  Bit Score: 50.70  E-value: 9.14e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561  544 TFIEKPRIVSENNGKLVIMECKVKADPKPDVIWFRNGEV-IKESNKIKTFIEQRGDQYYIklelLDPQLEDSGLYKCNIK 622
Cdd:cd05763     1 SFTKTPHDITIRAGSTARLECAATGHPTPQIAWQKDGGTdFPAARERRMHVMPEDDVFFI----VDVKIEDTGVYSCTAQ 76
                          90
                  ....*....|....
gi 281359561  623 NTLGELNANLTLNI 636
Cdd:cd05763    77 NSAGSISANATLTV 90
IgI_telokin-like cd20973
immunoglobulin-like domain of telokin and similar proteins; a member of the I-set of IgSF ...
2311-2395 9.41e-07

immunoglobulin-like domain of telokin and similar proteins; a member of the I-set of IgSF domains; The members here are composed of the immunoglobulin (Ig) domain in telokin, the C-terminal domain of myosin light chain kinase which is identical to telokin, and similar proteins. The Ig superfamily (IgSF) is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. Unlike the V-set, one of the distinctive features of I-set domains is the lack of a C" strand. The structure of the telokin Ig domain lacks this strand and thus it belongs to the I-set of the IgSF. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors, the hemolymph protein hemolin, the muscle proteins titin, telokin, and twitchin, the neuronal adhesion molecule axonin-1, and the signaling molecule semaphorin 4D that is involved in axonal guidance, immune function and angiogenesis.


Pssm-ID: 409565 [Multi-domain]  Cd Length: 88  Bit Score: 50.65  E-value: 9.41e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 2311 LKNVTVKKGQTIRFDIKYDGEPEPAATWVKgTDNLKFDNQRICLDQLER-NSSITIKKSVRKDTGKYKLVLSNSSGTIES 2389
Cdd:cd20973     4 LRDKEVVEGSAARFDCKVEGYPDPEVKWMK-DDNPIVESRRFQIDQDEDgLCSLIISDVCGDDSGKYTCKAVNSLGEATC 82

                  ....*.
gi 281359561 2390 EAQVVV 2395
Cdd:cd20973    83 SAELTV 88
Ig_3 pfam13927
Immunoglobulin domain; This family contains immunoglobulin-like domains.
3201-3279 9.60e-07

Immunoglobulin domain; This family contains immunoglobulin-like domains.


Pssm-ID: 464046 [Multi-domain]  Cd Length: 78  Bit Score: 50.26  E-value: 9.60e-07
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 281359561  3201 KPYINRDKmKPIKVRAGQPVKFDVDVKGEPAPSLTWFLKETELTSTGQVRLENIDYNTKLTLLDTDRKQSGQYKLRAEN 3279
Cdd:pfam13927    1 KPVITVSP-SSVTVREGETVTLTCEATGSPPPTITWYKNGEPISSGSTRSRSLSGSNSTLTISNVTRSDAGTYTCVASN 78
Ig_3 pfam13927
Immunoglobulin domain; This family contains immunoglobulin-like domains.
4685-4762 9.89e-07

Immunoglobulin domain; This family contains immunoglobulin-like domains.


Pssm-ID: 464046 [Multi-domain]  Cd Length: 78  Bit Score: 50.26  E-value: 9.89e-07
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 281359561  4685 PKIdRRNLRNITLSSGTALKLDANITGEPAPKVEWKLSNYHLQSGKNVTIETPDYYTKLVIRPTQRSDSGEYLVTATN 4762
Cdd:pfam13927    2 PVI-TVSPSSVTVREGETVTLTCEATGSPPPTITWYKNGEPISSGSTRSRSLSGSNSTLTISNVTRSDAGTYTCVASN 78
Ig4_L1-NrCAM_like cd04978
Fourth immunoglobulin (Ig)-like domain of L1, Ng-CAM (Neuron-glia CAM cell adhesion molecule), ...
8640-8711 1.01e-06

Fourth immunoglobulin (Ig)-like domain of L1, Ng-CAM (Neuron-glia CAM cell adhesion molecule), and NrCAM (Ng-CAM-related); The members here are composed of the fourth immunoglobulin (Ig)-like domain of L1, Ng-CAM (Neuron-glia CAM cell adhesion molecule), and NrCAM (Ng-CAM-related). These proteins belong to the L1 subfamily of cell adhesion molecules (CAMs) and are comprised of an extracellular region having six Ig-like domains and five fibronectin type III domains, a transmembrane region and an intracellular domain. These molecules are primarily expressed in the nervous system. L1 is associated with an X-linked recessive disorder, X-linked hydrocephalus, MASA syndrome, or spastic paraplegia type 1, that involves abnormalities of axonal growth.


Pssm-ID: 409367 [Multi-domain]  Cd Length: 89  Bit Score: 50.52  E-value: 1.01e-06
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 281359561 8640 DLTIHDGEQLILTCYVKGDPEPQISWSKNGKSLSSSDILDLRYKNGiATLTINEVFPEDEGVITCTATNSVG 8711
Cdd:cd04978     8 SLVLSPGETGELICEAEGNPQPTITWRLNGVPIEPAPEDMRRTVDG-RTLIFSNLQPNDTAVYQCNASNVHG 78
Ig cd00096
Immunoglobulin domain; The members here are composed of the immunoglobulin (Ig) domain found ...
657-731 1.04e-06

Immunoglobulin domain; The members here are composed of the immunoglobulin (Ig) domain found in the Ig superfamily. The Ig superfamily is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. Members of this group are components of immunoglobulin, neuroglia, cell surface glycoproteins, including T-cell receptors, CD2, CD4, CD8, and membrane glycoproteins, including butyrophilin and chondroitin sulfate proteoglycan core protein. A predominant feature of most Ig domains is a disulfide bridge connecting the two beta-sheets with a tryptophan residue packed against the disulfide bond. Ig superfamily (IgSF) domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. Typically, the V-set domains have A, B, E, and D strands in one sheet and A', G, F, C, C' and C" in the other. The structures in C1-set are smaller than those in the V-set; they have one beta sheet that is formed by strands A, B, E, and D and the other by strands G, F, C, and C'. Moreover, a C1-set Ig domain contains a short C' strand (three residues) and lacks A' and C" strand. Unlike other Ig domain sets, C2-set structures do not have a D strand. Like the V-set Ig domains, members of the I-set have a discontinuous A strand, but lack a C" strand.


Pssm-ID: 409353 [Multi-domain]  Cd Length: 70  Bit Score: 49.64  E-value: 1.04e-06
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 281359561  657 VVIECTVASKFEPKCTWYKETSTVKESKRHVYQVEQTKegefaVKLEINDVEESDKGAYKLVASNEKGEAVSQIV 731
Cdd:cd00096     1 VTLTCSASGNPPPTITWYKNGKPLPPSSRDSRRSELGN-----GTLTISNVTLEDSGTYTCVASNSAGGSASASV 70
IgI_2_Titin_Z1z2-like cd20972
Second Ig-like domain of the giant muscle protein titin Z1z2 in the sarcomeric Z-disk, and ...
4692-4775 1.06e-06

Second Ig-like domain of the giant muscle protein titin Z1z2 in the sarcomeric Z-disk, and similar domains; a member of the I-set of IgSF domains; The members here are composed of the second immunoglobulin (Ig)-like domain of the giant muscle protein titin Z1z2 in the sarcomeric Z-disk and similar proteins. Titin is a key component in the assembly and functioning of vertebrate striated muscles. By providing connections at the level of individual microfilaments, it contributes to the fine balance of forces between the two halves of the sarcomere. The Ig superfamily (IgSF) is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. Unlike the V-set, one of the distinctive features of I-set domains is the lack of a C" strand. The structure of the titin Z1z2 lacks this strand and thus it belongs to the I-set of the IgSF. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors, the hemolymph protein hemolin, the muscle proteins titin, telokin, and twitchin, the neuronal adhesion molecule axonin-1, and the signaling molecule semaphorin 4D that is involved in axonal guidance, immune function and angiogenesis.


Pssm-ID: 409564 [Multi-domain]  Cd Length: 91  Bit Score: 50.27  E-value: 1.06e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 4692 LRNITLSSGTALKLDANITGEPAPKVEWKLSNYHLQSGKNVTIETPDYYTKLVIRPTQRSDSGEYLVTATNTSGKDSVLV 4771
Cdd:cd20972     8 LRSQEVAEGSKVRLECRVTGNPTPVVRWFCEGKELQNSPDIQIHQEGDLHSLIIAEAFEEDTGRYSCLATNSVGSDTTSA 87

                  ....
gi 281359561 4772 NVVI 4775
Cdd:cd20972    88 EIFV 91
IgI_1_Titin_Z1z2-like cd20974
First Ig-like domain of the giant muscle protein titin Z1z2 in the sarcomeric Z-disk and ...
3208-3293 1.10e-06

First Ig-like domain of the giant muscle protein titin Z1z2 in the sarcomeric Z-disk and similar proteins; a member of the I-set of IgSF domains; The members here are composed of the first immunoglobulin (Ig)-like domain of the giant muscle protein titin Z1z2 in the sarcomeric Z-disk and similar proteins. Titin is a key component in the assembly and functioning of vertebrate striated muscles. By providing connections at the level of individual microfilaments, it contributes to the fine balance of forces between the two halves of the sarcomere. The Ig superfamily (IgSF) is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. Unlike the V-set, one of the distinctive features of I-set domains is the lack of a C" strand. The structure of the titin Z1z2 lacks this strand and thus it belongs to the I-set of the IgSF. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors, the hemolymph protein hemolin, the muscle proteins titin, telokin, and twitchin, the neuronal adhesion molecule axonin-1, and the signaling molecule semaphorin 4D that is involved in axonal guidance, immune function and angiogenesis.


Pssm-ID: 409566 [Multi-domain]  Cd Length: 93  Bit Score: 50.43  E-value: 1.10e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 3208 KMKPIKVRAGQPVKFDVDVKGEPAPSLTWFL--KETELTSTGQVRLENIDYNTKLTLLDTDRKQSGQYKLRAENINGVDE 3285
Cdd:cd20974     6 PLQSVVVLEGSTATFEAHVSGKPVPEVSWFRdgQVISTSTLPGVQISFSDGRAKLSIPAVTKANSGRYSLTATNGSGQAT 85

                  ....*...
gi 281359561 3286 AVVEVIIL 3293
Cdd:cd20974    86 STAELLVL 93
Ig5_Contactin cd04969
Fifth immunoglobulin (Ig) domain of contactin; The members here are composed of the fifth ...
6191-6246 1.13e-06

Fifth immunoglobulin (Ig) domain of contactin; The members here are composed of the fifth immunoglobulin (Ig) domain of contactins. Contactins are neural cell adhesion molecules and are comprised of six Ig domains followed by four fibronectin type III (FnIII) domains anchored to the membrane by glycosylphosphatidylinositol. The first four Ig domains form the intermolecular binding fragment, which arranges as a compact U-shaped module via contacts between Ig domains 1 and 4, and between Ig domains 2 and 3. Contactin-2 (TAG-1, axonin-1) may play a part in the neuronal processes of neurite outgrowth, axon guidance and fasciculation, and neuronal migration. This group also includes contactin-1 and contactin-5. The different contactins show different expression patterns in the central nervous system. During development and in adulthood, contactin-2 is transiently expressed in subsets of central and peripheral neurons. Contactin-5 is expressed specifically in the rat postnatal nervous system, peaking at about 3 weeks postnatal, and a lack of contactin-5 (NB-2) results in an impairment of neuronal activity in the rat auditory system. Contactin-5 is highly expressed in the adult human brain in the occipital lobe and in the amygdala. Contactin-1 is differentially expressed in tumor tissues and may, through a RhoA mechanism, facilitate invasion and metastasis of human lung adenocarcinoma.


Pssm-ID: 409358 [Multi-domain]  Cd Length: 89  Bit Score: 50.15  E-value: 1.13e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 281359561 6191 GAPTPTIEWKRGDLKLEEGKRISYETNseRTLFrIDDSNRRDSGKYTVTAANEFGK 6246
Cdd:cd04969    28 ASPKPTISWSKGTELLTNSSRICILPD--GSLK-IKNVTKSDEGKYTCFAVNFFGK 80
IgI_4_hemolin-like cd20978
Fourth immunoglobulin (Ig)-like domain of hemolin, and similar domains; a member of the I-set ...
4090-4181 1.14e-06

Fourth immunoglobulin (Ig)-like domain of hemolin, and similar domains; a member of the I-set of IgSF domains; The members here are composed of the fourth immunoglobulin (Ig)-like domain of hemolin and similar proteins. Hemolin, an insect immunoglobulin superfamily (IgSF) member containing four Ig-like domains, is a lipopolysaccharide-binding immune protein induced during bacterial infection. Hemolin shares significant sequence similarity with the first four Ig-like domains of the transmembrane cell adhesion molecules (CAMs) of the L1 family. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. The fourth Ig-like domain of hemolin is a member of the I-set Ig domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set domains, members of the I-set have a discontinuous A strand but lack a C" strand. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors, the muscle proteins titin, telokin, and twitchin, the neuronal adhesion molecule axonin-1, and the signaling molecule semaphorin 4D that is involved in axonal guidance, immune function and angiogenesis.


Pssm-ID: 409570 [Multi-domain]  Cd Length: 88  Bit Score: 50.08  E-value: 1.14e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 4090 PKIDRTNIKDITIKAGQHIRFDIKVSGEPPATKVWLHNKARLENDDSNYNIDmesyRTKLTVPISKRFHSGKYTLKAENE 4169
Cdd:cd20978     1 PKFIQKPEKNVVVKGGQDVTLPCQVTGVPQPKITWLHNGKPLQGPMERATVE----DGTLTIINVQPEDTGYYGCVATNE 76
                          90
                  ....*....|..
gi 281359561 4170 SGRDEASFEVIV 4181
Cdd:cd20978    77 IGDIYTETLLHV 88
Ig cd00096
Immunoglobulin domain; The members here are composed of the immunoglobulin (Ig) domain found ...
1750-1806 1.19e-06

Immunoglobulin domain; The members here are composed of the immunoglobulin (Ig) domain found in the Ig superfamily. The Ig superfamily is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. Members of this group are components of immunoglobulin, neuroglia, cell surface glycoproteins, including T-cell receptors, CD2, CD4, CD8, and membrane glycoproteins, including butyrophilin and chondroitin sulfate proteoglycan core protein. A predominant feature of most Ig domains is a disulfide bridge connecting the two beta-sheets with a tryptophan residue packed against the disulfide bond. Ig superfamily (IgSF) domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. Typically, the V-set domains have A, B, E, and D strands in one sheet and A', G, F, C, C' and C" in the other. The structures in C1-set are smaller than those in the V-set; they have one beta sheet that is formed by strands A, B, E, and D and the other by strands G, F, C, and C'. Moreover, a C1-set Ig domain contains a short C' strand (three residues) and lacks A' and C" strand. Unlike other Ig domain sets, C2-set structures do not have a D strand. Like the V-set Ig domains, members of the I-set have a discontinuous A strand, but lack a C" strand.


Pssm-ID: 409353 [Multi-domain]  Cd Length: 70  Bit Score: 49.64  E-value: 1.19e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 281359561 1750 TLECSVSSS-MANVHWFKNNTKLESDDprYLISKDINGNLKLIIKDSVLDDAGLYRCQ 1806
Cdd:cd00096     2 TLTCSASGNpPPTITWYKNGKPLPPSS--RDSRRSELGNGTLTISNVTLEDSGTYTCV 57
Ig_C5_MyBP-C cd05894
C5 immunoglobulin (Ig) domain of cardiac myosin binding protein C (MyBP-C); The members here ...
4993-5069 1.20e-06

C5 immunoglobulin (Ig) domain of cardiac myosin binding protein C (MyBP-C); The members here are composed of the C5 immunoglobulin (Ig) domain of cardiac myosin binding protein C (MyBP-C). MyBP-C consists of repeated domains, Ig and fibronectin type 3, and various linkers. Three isoforms of MYBP-C exist: slow-skeletal (ssMyBP-C), fast-skeletal (fsMyBP-C), and cardiac (cMyBP-C). cMYBP-C has insertions between and inside domains and an additional cardiac-specific Ig domain at the N-terminus. For cMYBP_C an interaction has been demonstrated between this C5 domain and the Ig C8 domain.


Pssm-ID: 409475  Cd Length: 86  Bit Score: 50.22  E-value: 1.20e-06
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 281359561 4993 AGQSFTFDCKVSGEPAPQTKWLLKKKEVY-SKDNVKVTNVDYNTKLKVNSATRSDSGIYTVFAENANGEDSADVKVTV 5069
Cdd:cd05894     9 AGNKLRLDVPISGEPAPTVTWSRGDKAFTaTEGRVRVESYKDLSSFVIEGAEREDEGVYTITVTNPVGEDHASLFVKV 86
Ig5_Contactin cd04969
Fifth immunoglobulin (Ig) domain of contactin; The members here are composed of the fifth ...
438-525 1.26e-06

Fifth immunoglobulin (Ig) domain of contactin; The members here are composed of the fifth immunoglobulin (Ig) domain of contactins. Contactins are neural cell adhesion molecules and are comprised of six Ig domains followed by four fibronectin type III (FnIII) domains anchored to the membrane by glycosylphosphatidylinositol. The first four Ig domains form the intermolecular binding fragment, which arranges as a compact U-shaped module via contacts between Ig domains 1 and 4, and between Ig domains 2 and 3. Contactin-2 (TAG-1, axonin-1) may play a part in the neuronal processes of neurite outgrowth, axon guidance and fasciculation, and neuronal migration. This group also includes contactin-1 and contactin-5. The different contactins show different expression patterns in the central nervous system. During development and in adulthood, contactin-2 is transiently expressed in subsets of central and peripheral neurons. Contactin-5 is expressed specifically in the rat postnatal nervous system, peaking at about 3 weeks postnatal, and a lack of contactin-5 (NB-2) results in an impairment of neuronal activity in the rat auditory system. Contactin-5 is highly expressed in the adult human brain in the occipital lobe and in the amygdala. Contactin-1 is differentially expressed in tumor tissues and may, through a RhoA mechanism, facilitate invasion and metastasis of human lung adenocarcinoma.


Pssm-ID: 409358 [Multi-domain]  Cd Length: 89  Bit Score: 50.15  E-value: 1.26e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561  438 PSFIEKP--RIIPNESGTLITMKCKCKAKPEPTVTWYRGQDLVEKSKKIKInttviaedTYELTLEIKDPGATDGGTYRC 515
Cdd:cd04969     1 PDFELNPvkKKILAAKGGDVIIECKPKASPKPTISWSKGTELLTNSSRICI--------LPDGSLKIKNVTKSDEGKYTC 72
                          90
                  ....*....|
gi 281359561  516 NVKNEYGESN 525
Cdd:cd04969    73 FAVNFFGKAN 82
Ig_3 pfam13927
Immunoglobulin domain; This family contains immunoglobulin-like domains.
3794-3872 1.31e-06

Immunoglobulin domain; This family contains immunoglobulin-like domains.


Pssm-ID: 464046 [Multi-domain]  Cd Length: 78  Bit Score: 49.87  E-value: 1.31e-06
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 281359561  3794 KPHIdRKNLQKKIMRSGQMLHIDALIKAEPPAKVTWTYNKTEIKTSDHIKIENEDYKTTFIMPKVKRADRGIYIVTAKN 3872
Cdd:pfam13927    1 KPVI-TVSPSSVTVREGETVTLTCEATGSPPPTITWYKNGEPISSGSTRSRSLSGSNSTLTISNVTRSDAGTYTCVASN 78
IgI_Myotilin_C cd05892
C-terminal immunoglobulin (Ig)-like domain of myotilin; member of the I-set of Ig superfamily ...
9-102 1.32e-06

C-terminal immunoglobulin (Ig)-like domain of myotilin; member of the I-set of Ig superfamily (IgSF) domains; The members here are composed of the C-terminal immunoglobulin (Ig)-like domain of myotilin. Mytolin belongs to the palladin-myotilin-myopalladin family. Proteins belonging to the latter family contain multiple Ig-like domains and function as scaffolds, modulating the actin cytoskeleton. Myotilin is most abundant in skeletal and cardiac muscle and is involved in maintaining sarcomere integrity. It binds to alpha-actinin, filamin, and actin. Mutations in myotilin lead to muscle disorders. This group belongs to the I-set of IgSF domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand, but lack a C" strand.


Pssm-ID: 409473  Cd Length: 92  Bit Score: 50.15  E-value: 1.32e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561    9 PSFVKKPQLHQEDDGNRLIFECQLLSSPKPDIEWFRSDNKVVEDVRtkfKIQPVGENKYTVVLELDDVVETDAGLYKVKA 88
Cdd:cd05892     1 PMFIQKPQNKKVLEGDPVRLECQISAIPPPQIFWKKNNEMLQYNTD---RISLYQDNCGRICLLIQNANKKDAGWYTVSA 77
                          90
                  ....*....|....
gi 281359561   89 KNKSGEVSASINLN 102
Cdd:cd05892    78 VNEAGVVSCNARLD 91
IgI_4_Dscam cd20956
Fourth immunoglobulin domain of the Drosophila melanogaster Dscam protein, and similar domains; ...
229-313 1.38e-06

Fourth immunoglobulin domain of the Drosophila melanogaster Dscam protein, and similar domains; a member of the I-set of IgSF domains; The members here are composed of the fourth immunoglobulin domain of the Drosophila melanogaster Down syndrome cell adhesion molecule (DSCAM) protein and similar proteins. Down syndrome cell adhesion molecule (DSCAM) is a cell adhesion molecule that plays critical roles in neural development, including axon guidance and branching, axon target recognition, self-avoidance and synaptic formation. DSCAM belongs to the immunoglobulin superfamily and contributes to defects in the central nervous system in Down syndrome patients. Vertebrate DSCAMs differ from Drosophila Dscam1 in that they lack the extensive alternative splicing that occurs in the insect gene. Drosophila melanogaster Dscam has 38,016 isoforms generated by the alternative splicing of four variable exon clusters, which allows every neuron in the fly to display a distinctive set of Dscam proteins on its cell surface. Drosophila Dscam1 is a cell-surface protein that plays important roles in neural development and axon tiling of neurons. It is shown that thousands of isoforms bind themselves through specific homophilic (self-binding) interactions, a process which mediates cellular self-recognition. Drosophila Dscam2 is also alternatively spliced and plays a key role in the development of two visual system neurons, monopolar cells L1 and L2. This group is a member of the I-set Ig domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand but lack a C" strand.


Pssm-ID: 409548 [Multi-domain]  Cd Length: 96  Bit Score: 50.25  E-value: 1.38e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561  229 TFTERPVirqsEDGGNVTFECRCVGDPTPTVTWSHGETELNESNRYKMS--LTMDQKLyhIACLEISSVVSSDQGEYRAQ 306
Cdd:cd20956     7 TFSEQTL----QPGPSVSLKCVASGNPLPQITWTLDGFPIPESPRFRVGdyVTSDGDV--VSYVNISSVRVEDGGEYTCT 80

                  ....*..
gi 281359561  307 AKNKHGS 313
Cdd:cd20956    81 ATNDVGS 87
IgI_Myotilin_C_like cd05744
Immunoglobulin (Ig)-like domain of myotilin, palladin, and myopalladin; member of the I-set of ...
8437-8519 1.47e-06

Immunoglobulin (Ig)-like domain of myotilin, palladin, and myopalladin; member of the I-set of Ig superfamily (IgSF) domains; The members here are composed of the immunoglobulin (Ig)-like domain in myotilin, palladin, and myopalladin. Myotilin, palladin, and myopalladin function as scaffolds that regulate actin organization. Myotilin and myopalladin are most abundant in skeletal and cardiac muscle; palladin is ubiquitously expressed in the organs of developing vertebrates and plays a key role in cellular morphogenesis. The three family members each interact with specific molecular partners with all three binding to alpha-actinin; In addition, palladin also binds to vasodilator-stimulated phosphoprotein (VASP) and ezrin, myotilin binds to filamin and actin, and myopalladin also binds to nebulin and cardiac ankyrin repeat protein (CARP). This group belongs to the I-set of IgSF domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand, but lack a C" strand.


Pssm-ID: 409405 [Multi-domain]  Cd Length: 91  Bit Score: 50.19  E-value: 1.47e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 8437 PSFTFLLRPRVMQARDTCKLLCCLSGKPVPNVRWYKDGRELSKYE--YAMTHSDGVVTMEIIDCKPSDSGKYSCKATNCH 8514
Cdd:cd05744     1 PHFLQAPGDLEVQEGRLCRFDCKVSGLPTPDLFWQLNGKPVRPDSahKMLVRENGRHSLIIEPVTKRDAGIYTCIARNRA 80

                  ....*
gi 281359561 8515 GTDET 8519
Cdd:cd05744    81 GENSF 85
Ig_C5_MyBP-C cd05894
C5 immunoglobulin (Ig) domain of cardiac myosin binding protein C (MyBP-C); The members here ...
6570-6650 1.51e-06

C5 immunoglobulin (Ig) domain of cardiac myosin binding protein C (MyBP-C); The members here are composed of the C5 immunoglobulin (Ig) domain of cardiac myosin binding protein C (MyBP-C). MyBP-C consists of repeated domains, Ig and fibronectin type 3, and various linkers. Three isoforms of MYBP-C exist: slow-skeletal (ssMyBP-C), fast-skeletal (fsMyBP-C), and cardiac (cMyBP-C). cMYBP-C has insertions between and inside domains and an additional cardiac-specific Ig domain at the N-terminus. For cMYBP_C an interaction has been demonstrated between this C5 domain and the Ig C8 domain.


Pssm-ID: 409475  Cd Length: 86  Bit Score: 49.84  E-value: 1.51e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 6570 IVCRAGDDFSIHVPYLAFPKPNAFWYSNDNML-DDNNRVHKHLTDDAASVVVKNSKRADSGQYRLQLKNTSGFDTATINV 6648
Cdd:cd05894     5 IVVVAGNKLRLDVPISGEPAPTVTWSRGDKAFtATEGRVRVESYKDLSSFVIEGAEREDEGVYTITVTNPVGEDHASLFV 84

                  ..
gi 281359561 6649 RV 6650
Cdd:cd05894    85 KV 86
IgI_telokin-like cd20973
immunoglobulin-like domain of telokin and similar proteins; a member of the I-set of IgSF ...
2606-2693 1.56e-06

immunoglobulin-like domain of telokin and similar proteins; a member of the I-set of IgSF domains; The members here are composed of the immunoglobulin (Ig) domain in telokin, the C-terminal domain of myosin light chain kinase which is identical to telokin, and similar proteins. The Ig superfamily (IgSF) is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. Unlike the V-set, one of the distinctive features of I-set domains is the lack of a C" strand. The structure of the telokin Ig domain lacks this strand and thus it belongs to the I-set of the IgSF. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors, the hemolymph protein hemolin, the muscle proteins titin, telokin, and twitchin, the neuronal adhesion molecule axonin-1, and the signaling molecule semaphorin 4D that is involved in axonal guidance, immune function and angiogenesis.


Pssm-ID: 409565 [Multi-domain]  Cd Length: 88  Bit Score: 49.88  E-value: 1.56e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 2606 RSTFKRVTIKSGRTHKWSVDVLGEPIPELHWSwRDDIPLTNGDRIKIE-NVDYHTDFSITNVLRKDSGFYTLKAENRNGI 2684
Cdd:cd20973     1 IQTLRDKEVVEGSAARFDCKVEGYPDPEVKWM-KDDNPIVESRRFQIDqDEDGLCSLIISDVCGDDSGKYTCKAVNSLGE 79

                  ....*....
gi 281359561 2685 DRETVELVV 2693
Cdd:cd20973    80 ATCSAELTV 88
Ig_Titin_like cd05748
Immunoglobulin (Ig)-like domain of titin and similar proteins; The members here are composed ...
462-530 1.64e-06

Immunoglobulin (Ig)-like domain of titin and similar proteins; The members here are composed of the immunoglobulin (Ig)-like domain found in titin-like proteins and similar proteins. Titin (also called connectin) is a fibrous sarcomeric protein specifically found in vertebrate striated muscle. Titin is a giant protein; depending on isoform composition, it ranges from 2970 to 3700 kDa, and is of a length that spans half a sarcomere. Titin largely consists of multiple repeats of Ig-like and fibronectin type 3 (FN-III)-like domains. Titin connects the ends of myosin thick filaments to Z disks and extends along the thick filament to the H zone. It appears to function similarly to an elastic band, keeping the myosin filaments centered in the sarcomere during muscle contraction or stretching. Within the sarcomere, titin is also attached to or is associated with myosin binding protein C (MyBP-C). MyBP-C appears to contribute to the generation of passive tension by titin and like titin has repeated Ig-like and FN-III domains. Also included in this group are worm twitchin and insect projectin, thick filament proteins of invertebrate muscle which also have repeated Ig-like and FN-III domains.


Pssm-ID: 409406 [Multi-domain]  Cd Length: 82  Bit Score: 49.51  E-value: 1.64e-06
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 281359561  462 KAKPEPTVTWYRGQDLVEKSKKIKINTTviAEDTyelTLEIKDPGATDGGTYRCNVKNEYGESNANLNL 530
Cdd:cd05748    17 KGRPTPTVTWSKDGQPLKETGRVQIETT--ASST---SLVIKNAKRSDSGKYTLTLKNSAGEKSATINV 80
IgI_2_Titin_Z1z2-like cd20972
Second Ig-like domain of the giant muscle protein titin Z1z2 in the sarcomeric Z-disk, and ...
8311-8392 1.70e-06

Second Ig-like domain of the giant muscle protein titin Z1z2 in the sarcomeric Z-disk, and similar domains; a member of the I-set of IgSF domains; The members here are composed of the second immunoglobulin (Ig)-like domain of the giant muscle protein titin Z1z2 in the sarcomeric Z-disk and similar proteins. Titin is a key component in the assembly and functioning of vertebrate striated muscles. By providing connections at the level of individual microfilaments, it contributes to the fine balance of forces between the two halves of the sarcomere. The Ig superfamily (IgSF) is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. Unlike the V-set, one of the distinctive features of I-set domains is the lack of a C" strand. The structure of the titin Z1z2 lacks this strand and thus it belongs to the I-set of the IgSF. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors, the hemolymph protein hemolin, the muscle proteins titin, telokin, and twitchin, the neuronal adhesion molecule axonin-1, and the signaling molecule semaphorin 4D that is involved in axonal guidance, immune function and angiogenesis.


Pssm-ID: 409564 [Multi-domain]  Cd Length: 91  Bit Score: 49.89  E-value: 1.70e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 8311 APRFVIRPSSQFCYEGQSVKFYCRCIAIATPTLTWSHNNIELRQSVKFMKRYVGDDYYFIINRVKLDDRGEYIIRAENHY 8390
Cdd:cd20972     1 PPQFIQKLRSQEVAEGSKVRLECRVTGNPTPVVRWFCEGKELQNSPDIQIHQEGDLHSLIIAEAFEEDTGRYSCLATNSV 80

                  ..
gi 281359561 8391 GS 8392
Cdd:cd20972    81 GS 82
IgI_titin_I1-like cd20951
Immunoglobulin domain I1 of the titin I-band and similar proteins; a member of the I-set of ...
2909-2993 1.71e-06

Immunoglobulin domain I1 of the titin I-band and similar proteins; a member of the I-set of IgSF domains; The members here are composed of the immunoglobulin domain I1 of the titin I-band and similar proteins. Titin is a key component in the assembly and functioning of vertebrate striated muscles. By providing connections at the level of individual microfilaments, it contributes to the fine balance of forces between the two halves of the sarcomere. The Ig superfamily (IgSF) is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. The two sheets are linked together by a conserved disulfide bond between B strand and F strand. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. The Ig I1 domain of the titin I-band is a member of the I-set Ig domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand but lack a C" strand. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors, the hemolymph protein hemolin, the muscle proteins titin, telokin, and twitchin, the neuronal adhesion molecule axonin-1, and the signaling molecule semaphorin 4D that is involved in axonal guidance, immune function and angiogenesis.


Pssm-ID: 409543 [Multi-domain]  Cd Length: 94  Bit Score: 49.73  E-value: 1.71e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 2909 LKPLLIRAGKPIRYDVNVRGEPAPVITWYQNDKELKPEELPSSSEIKNIPYNTKISIIETVRKHTGIYKIIAVNEHGQ-- 2986
Cdd:cd20951     7 LQSHTVWEKSDAKLRVEVQGKPDPEVKWYKNGVPIDPSSIPGKYKIESEYGVHVLHIRRVTVEDSAVYSAVAKNIHGEas 86

                  ....*..
gi 281359561 2987 DEATVEV 2993
Cdd:cd20951    87 SSASVVV 93
IgI_2_Titin_Z1z2-like cd20972
Second Ig-like domain of the giant muscle protein titin Z1z2 in the sarcomeric Z-disk, and ...
4978-5069 1.86e-06

Second Ig-like domain of the giant muscle protein titin Z1z2 in the sarcomeric Z-disk, and similar domains; a member of the I-set of IgSF domains; The members here are composed of the second immunoglobulin (Ig)-like domain of the giant muscle protein titin Z1z2 in the sarcomeric Z-disk and similar proteins. Titin is a key component in the assembly and functioning of vertebrate striated muscles. By providing connections at the level of individual microfilaments, it contributes to the fine balance of forces between the two halves of the sarcomere. The Ig superfamily (IgSF) is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. Unlike the V-set, one of the distinctive features of I-set domains is the lack of a C" strand. The structure of the titin Z1z2 lacks this strand and thus it belongs to the I-set of the IgSF. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors, the hemolymph protein hemolin, the muscle proteins titin, telokin, and twitchin, the neuronal adhesion molecule axonin-1, and the signaling molecule semaphorin 4D that is involved in axonal guidance, immune function and angiogenesis.


Pssm-ID: 409564 [Multi-domain]  Cd Length: 91  Bit Score: 49.89  E-value: 1.86e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 4978 PPIIDRSSLVEVRikAGQSFTFDCKVSGEPAPQTKWLLKKKEVYSKDNVKVTNVDYNTKLKVNSATRSDSGIYTVFAENA 5057
Cdd:cd20972     2 PQFIQKLRSQEVA--EGSKVRLECRVTGNPTPVVRWFCEGKELQNSPDIQIHQEGDLHSLIIAEAFEEDTGRYSCLATNS 79
                          90
                  ....*....|..
gi 281359561 5058 NGEDSADVKVTV 5069
Cdd:cd20972    80 VGSDTTSAEIFV 91
ig pfam00047
Immunoglobulin domain; Members of the immunoglobulin superfamily are found in hundreds of ...
4984-5067 1.92e-06

Immunoglobulin domain; Members of the immunoglobulin superfamily are found in hundreds of proteins of different functions. Examples include antibodies, the giant muscle kinase titin and receptor tyrosine kinases. Immunoglobulin-like domains may be involved in protein-protein and protein-ligand interactions.


Pssm-ID: 395002  Cd Length: 86  Bit Score: 49.50  E-value: 1.92e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561  4984 SSLVEVRIKAGQSFTFDCKVS-GEPAPQTKWLLKKKEVYSKDNVKVTNVD-YNTKLKVNSATRSDSGIYTVFAENANGED 5061
Cdd:pfam00047    1 SAPPTVTVLEGDSATLTCSAStGSPGPDVTWSKEGGTLIESLKVKHDNGRtTQSSLLISNVTKEDAGTYTCVVNNPGGSA 80

                   ....*.
gi 281359561  5062 SADVKV 5067
Cdd:pfam00047   81 TLSTSL 86
IgI_8_hMLCK_like cd05762
Eighth immunoglobulin (Ig)-like domain of human myosin light-chain kinase (MLCK) and similar ...
5275-5373 2.00e-06

Eighth immunoglobulin (Ig)-like domain of human myosin light-chain kinase (MLCK) and similar protein; member of the I-set of IgSF domains; The members here are composed of the eighth immunoglobulin (Ig)-like domain of human myosin light-chain kinase (MLCK) and similar proteins. Myosin light-chain kinase (MLCK) is a key regulator of different forms of cell motility involving actin and myosin II. Agonist stimulation of smooth muscle cells increases cytosolic Ca2+ which binds calmodulin. This Ca2+-calmodulin complex in turn binds to and activates MLCK. Activated MLCK leads to the phosphorylation of the 20 kDa myosin regulatory light chain (RLC) of myosin II and the stimulation of actin-activated myosin MgATPase activity. MLCK is widely present in vertebrate tissues; it phosphorylates the 20 kDa RLC of both smooth and nonmuscle myosin II. Phosphorylation leads to the activation of the myosin motor domain and altered structural properties of myosin II. In smooth muscle MLCK it is involved in initiating contraction. In nonmuscle cells, MLCK may participate in cell division and cell motility; it has been suggested MLCK plays a role in cardiomyocyte differentiation and contraction through regulation of nonmuscle myosin II.


Pssm-ID: 409419  Cd Length: 99  Bit Score: 49.95  E-value: 2.00e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 5275 PPKIDRnFMSDIKIKAGNVFEFDVPVTGEPLPSKDWTHEGNMIINTDRVKISNFDDRTKIRILDAKRSDTGVYTLTARNI 5354
Cdd:cd05762     1 PPQIIQ-FPEDMKVRAGESVELFCKVTGTQPITCTWMKFRKQIQEGEGIKIENTENSSKLTITEGQQEHCGCYTLEVENK 79
                          90
                  ....*....|....*....
gi 281359561 5355 NGTDRHNVKVTILDAPSVP 5373
Cdd:cd05762    80 LGSRQAQVNLTVVDKPDPP 98
IgI_Myomesin_like_C cd05737
C-terminal immunoglobulin (Ig)-like domain of myomesin and M-protein; member of the I-set of ...
549-636 2.01e-06

C-terminal immunoglobulin (Ig)-like domain of myomesin and M-protein; member of the I-set of Ig superfamily (IgSF) domains; The members here are composed of the C-terminal immunoglobulin (Ig)-like domain of myomesin and M-protein (also known as myomesin-2). Myomesin and M-protein are both structural proteins localized to the M-band, a transverse structure in the center of the sarcomere, and are candidates for M-band bridges. Both proteins are modular, consisting mainly of repetitive Ig-like and fibronectin type III (FnIII) domains. Myomesin is expressed in all types of vertebrate striated muscle; M-protein has a muscle-type specific expression pattern. Myomesin is present in both slow and fast fibers; M-protein is present only in fast fibers. It has been suggested that myomesin acts as a molecular spring with alternative splicing as a means of modifying its elasticity.


Pssm-ID: 319300  Cd Length: 92  Bit Score: 49.51  E-value: 2.01e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561  549 PRIVSENNGKLVIMECKVKADPKPDVIWFRNGEVIKESNKIKTFIEQrGDQYYIKLELLDPqlEDSGLYKCNIKNTLGEL 628
Cdd:cd05737     8 PDVVTIMEGKTLNLTCNVWGDPPPEVSWLKNDQALAFLDHCNLKVEA-GRTVYFTINGVSS--EDSGKYGLVVKNKYGSE 84

                  ....*...
gi 281359561  629 NANLTLNI 636
Cdd:cd05737    85 TSDVTVSV 92
IgI_APEG-1_like cd20975
Immunoglobulin-like domain of human Aortic Preferentially Expressed Protein-1 (APEG-1) and ...
2914-2993 2.04e-06

Immunoglobulin-like domain of human Aortic Preferentially Expressed Protein-1 (APEG-1) and similar proteins; a member of the I-set of IgSF domains; The members here are composed of the immunoglobulin I-set (IgI) domain of the Human Aortic Preferentially Expressed Protein-1 (APEG-1) and similar proteins. APEG-1 is a novel specific smooth muscle differentiation marker predicted to play a role in the growth and differentiation of arterial smooth muscle cells (SMCs). The Ig superfamily (IgSF) is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. Unlike the V-set, one of the distinctive features of I-set domains is the lack of a C" strand. The structure of the human APEG-1 lacks this strand and thus it belongs to the I-set of the IgSF. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors, the hemolymph protein hemolin, the muscle proteins titin, telokin, and twitchin, the neuronal adhesion molecule axonin-1, and the signaling molecule semaphorin 4D that is involved in axonal guidance, immune function and angiogenesis.


Pssm-ID: 409567  Cd Length: 91  Bit Score: 49.78  E-value: 2.04e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 2914 IRAGKPIRYDVNVRGEPAPVITWYQNDKELKPEELPSSSEIKNipYNTKISIIETVRKHTGIYKIIAVNEHG--QDEATV 2991
Cdd:cd20975    12 VREGQDVIMSIRVQGEPKPVVSWLRNRQPVRPDQRRFAEEAEG--GLCRLRILAAERGDAGFYTCKAVNEYGarQCEARL 89

                  ..
gi 281359561 2992 EV 2993
Cdd:cd20975    90 EV 91
Ig_2 pfam13895
Immunoglobulin domain; This domain contains immunoglobulin-like domains.
8631-8722 2.08e-06

Immunoglobulin domain; This domain contains immunoglobulin-like domains.


Pssm-ID: 464026 [Multi-domain]  Cd Length: 79  Bit Score: 49.32  E-value: 2.08e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561  8631 KPEFTKPlhDLTIHDGEQLILTCYVKGDPEPQISWSKNGKSLSSSDildlrykngiaTLTINEVFPEDEGVITCTATNSV 8710
Cdd:pfam13895    1 KPVLTPS--PTVVTEGEPVTLTCSAPGNPPPSYTWYKDGSAISSSP-----------NFFTLSVSAEDSGTYTCVARNGR 67
                           90
                   ....*....|..
gi 281359561  8711 GaVETKCKLTIQ 8722
Cdd:pfam13895   68 G-GKVSNPVELT 78
Ig3_Peroxidasin cd05745
Third immunoglobulin (Ig)-like domain of peroxidasin; The members here are composed of the ...
7268-7344 2.11e-06

Third immunoglobulin (Ig)-like domain of peroxidasin; The members here are composed of the third immunoglobulin (Ig)-like domain in peroxidasin. Peroxidasin has a peroxidase domain and interacting extracellular motifs containing four Ig-like domains. It has been suggested that peroxidasin is secreted and has functions related to the stabilization of the extracellular matrix. It may play a part in various other important processes such as removal and destruction of cells which have undergone programmed cell death and protection of the organism against non-self.


Pssm-ID: 143222 [Multi-domain]  Cd Length: 74  Bit Score: 49.17  E-value: 2.11e-06
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 281359561 7268 GKDYTLQCAASGKPSPTARWLRNGKEIQMNGGRMTCDSkdGVFRlhISNVQTGDDGDYTCEAMNSLGFVNTSGYLKI 7344
Cdd:cd05745     2 GQTVDFLCEAQGYPQPVIAWTKGGSQLSVDRRHLVLSS--GTLR--ISRVALHDQGQYECQAVNIVGSQRTVAQLTV 74
I-set pfam07679
Immunoglobulin I-set domain;
1639-1724 2.18e-06

Immunoglobulin I-set domain;


Pssm-ID: 400151 [Multi-domain]  Cd Length: 90  Bit Score: 49.56  E-value: 2.18e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561  1639 SFLSPLIDQFAKEGKDkkVVFEARFS-KPNCKPKWLFRKDEVFTGSKFKFKQENDTYQLIITTPKVEDTGKYTI----EI 1713
Cdd:pfam07679    2 KFTQKPKDVEVQEGES--ARFTCTVTgTPDPEVSWFKDGQPLRSSDRFKVTYEGGTYTLTISNVQPDDSGKYTCvatnSA 79
                           90
                   ....*....|.
gi 281359561  1714 GGVSSTAFLNV 1724
Cdd:pfam07679   80 GEAEASAELTV 90
COG4733 COG4733
Phage-related protein, tail protein J [Mobilome: prophages, transposons];
3615-3846 2.24e-06

Phage-related protein, tail protein J [Mobilome: prophages, transposons];


Pssm-ID: 443767 [Multi-domain]  Cd Length: 978  Bit Score: 55.34  E-value: 2.24e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 3615 WEKPDDDggspiDYYEIEKLDPHtGQWLPCGKSTEPEAKVIGLHEGKaYKFRVRAVNKEGESEDLET--EKPIIAKNPYd 3692
Cdd:COG4733   558 WDAPAGA-----VAYEVEWRRDD-GNWVSVPRTSGTSFEVPGIYAGD-YEVRVRAINALGVSSAWAAssETTVTGKTAP- 629
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 3693 epdrPGKP-----EPTNWDkdfVDLAWDPPKndgGAPIQKYVIQMRDKSGRAwvdSATVPGDKCNG---TVTGVEEGHEY 3764
Cdd:COG4733   630 ----PPAPtgltaTGGLGG---ITLSWSFPV---DADTLRTEIRYSTTGDWA---SATVAQALYPGntyTLAGLKAGQTY 696
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 3765 EFRIVAVNKAGPSDPSDVSKSVIAKPRFLKPHIDRKNLQKKIMRSGQMLHIDALIKAEPPAKVTWTYNKTEIKTSDHIKI 3844
Cdd:COG4733   697 YYRARAVDRSGNVSAWWVSGQASADAAGILDAITGQILETELGQELDAIIQNATVAEVVAATVTDVTAQIDTAVLFAGVA 776

                  ..
gi 281359561 3845 EN 3846
Cdd:COG4733   777 TA 778
IgI_3_Robo cd05725
Third immunoglobulin (Ig)-like domain in Robo (roundabout) receptors; member of the I-set of ...
133-210 2.31e-06

Third immunoglobulin (Ig)-like domain in Robo (roundabout) receptors; member of the I-set of Ig superfamily (IgSF) domains; The members here are composed of the third immunoglobulin (Ig)-like domain in Robo (roundabout) receptors. Robo receptors play a role in the development of the central nervous system (CNS), and are receptors of Slit protein. Slit is a repellant secreted by the neural cells in the midline. Slit acts through Robo to prevent most neurons from crossing the midline from either side. Three mammalian Robo homologs (Robo1, Robo2, Robo3), and three mammalian Slit homologs (Slit-1,Slit-2, Slit-3), have been identified. Commissural axons, which cross the midline, express low levels of Robo; longitudinal axons, which avoid the midline, express high levels of Robo. Robo1, Robo2, and Robo3 are expressed by commissural neurons in the vertebrate spinal cord and Slit-1, Slit-2, and Slit-3 are expressed at the ventral midline. Robo-3 is a divergent member of the Robo family which instead of being a positive regulator of Slit responsiveness, antagonizes Slit responsiveness in precrossing axons. The Slit-Robo interaction is mediated by the second leucine-rich repeat (LRR) domain of Slit and the two N-terminal Ig domains of Robo, Ig1 and Ig2. The primary Robo binding site for Slit2 has been shown by surface plasmon resonance experiments and mutational analysis to be the Ig1 domain, while the Ig2 domain has been proposed to harbor a weak secondary binding site. This group belongs to the I-set of IgSF domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand, but lack a C" strand.


Pssm-ID: 409390 [Multi-domain]  Cd Length: 83  Bit Score: 49.32  E-value: 2.31e-06
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 281359561  133 GKRLLFECRVNADPIPAIIWFHNGAAVKESeRHKITVDKdvhsyfaTLEILNVTVEDAGKYKVNAKNELGESNATISL 210
Cdd:cd05725    12 DDSAEFQCEVGGDPVPTVRWRKEDGELPKG-RYEILDDH-------SLKIRKVTAGDMGSYTCVAENMVGKIEASATL 81
COG4733 COG4733
Phage-related protein, tail protein J [Mobilome: prophages, transposons];
2742-2882 2.34e-06

Phage-related protein, tail protein J [Mobilome: prophages, transposons];


Pssm-ID: 443767 [Multi-domain]  Cd Length: 978  Bit Score: 55.34  E-value: 2.34e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 2742 GKWVRVGRSPGekepPSFDVTGLSLGsEYMFRVSAVNEEGESEPLTTLVGVVAKDPFDEPNKPGTPEVTdYDNQSISLKW 2821
Cdd:COG4733   576 GNWVSVPRTSG----TSFEVPGIYAG-DYEVRVRAINALGVSSAWAASSETTVTGKTAPPPAPTGLTAT-GGLGGITLSW 649
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 281359561 2822 AAPNndgGAPIQKYIIEKKNKNKTEWEKALEIPGDQLEATVAGLQEYGEYQFRVIAVNKAG 2882
Cdd:COG4733   650 SFPV---DADTLRTEIRYSTTGDWASATVAQALYPGNTYTLAGLKAGQTYYYRARAVDRSG 707
IgI_Titin_like cd05747
Immunoglobulin (Ig)-like domain of human titin C terminus and similar proteins; member of the ...
544-634 2.38e-06

Immunoglobulin (Ig)-like domain of human titin C terminus and similar proteins; member of the I-set of Ig superfamily (IgSF) domains; The members here are composed of the fifth immunoglobulin (Ig)-like domain from the C-terminus of human titin x and similar proteins. Titin (also called connectin) is a fibrous sarcomeric protein specifically found in vertebrate striated muscle. Titin is gigantic; depending on isoform composition it ranges from 2970 to 3700 kDa, and is of a length that spans half a sarcomere. Titin largely consists of multiple repeats of Ig-like and fibronectin type 3 (FN-III)-like domains. Titin connects the ends of myosin thick filaments to Z disks and extends along the thick filament to the H zone and appears to function similar to an elastic band, keeping the myosin filaments centered in the sarcomere during muscle contraction or stretching. This group belongs to the I-set of IgSF domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand, but lack a C" strand.


Pssm-ID: 143224 [Multi-domain]  Cd Length: 92  Bit Score: 49.66  E-value: 2.38e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561  544 TFIEKPRIVSENNGKLVIMECKVKADPKPDVIWFRNGEVIKESNKIKTfieqRGDQYYIKLELLDPQLEDSGLYKCNIKN 623
Cdd:cd05747     5 TILTKPRSLTVSEGESARFSCDVDGEPAPTVTWMREGQIIVSSQRHQI----TSTEYKSTFEISKVQMSDEGNYTVVVEN 80
                          90
                  ....*....|.
gi 281359561  624 TLGELNANLTL 634
Cdd:cd05747    81 SEGKQEAQFTL 91
Ig cd00096
Immunoglobulin domain; The members here are composed of the immunoglobulin (Ig) domain found ...
5294-5360 2.39e-06

Immunoglobulin domain; The members here are composed of the immunoglobulin (Ig) domain found in the Ig superfamily. The Ig superfamily is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. Members of this group are components of immunoglobulin, neuroglia, cell surface glycoproteins, including T-cell receptors, CD2, CD4, CD8, and membrane glycoproteins, including butyrophilin and chondroitin sulfate proteoglycan core protein. A predominant feature of most Ig domains is a disulfide bridge connecting the two beta-sheets with a tryptophan residue packed against the disulfide bond. Ig superfamily (IgSF) domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. Typically, the V-set domains have A, B, E, and D strands in one sheet and A', G, F, C, C' and C" in the other. The structures in C1-set are smaller than those in the V-set; they have one beta sheet that is formed by strands A, B, E, and D and the other by strands G, F, C, and C'. Moreover, a C1-set Ig domain contains a short C' strand (three residues) and lacks A' and C" strand. Unlike other Ig domain sets, C2-set structures do not have a D strand. Like the V-set Ig domains, members of the I-set have a discontinuous A strand, but lack a C" strand.


Pssm-ID: 409353 [Multi-domain]  Cd Length: 70  Bit Score: 48.86  E-value: 2.39e-06
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 281359561 5294 FEFDVPVTGEPLPSKDWTHEGNMIINTDRVKISNFDDRTKIRILDAKRSDTGVYTLTARNINGTDRH 5360
Cdd:cd00096     1 VTLTCSASGNPPPTITWYKNGKPLPPSSRDSRRSELGNGTLTISNVTLEDSGTYTCVASNSAGGSAS 67
FN3 COG3401
Fibronectin type 3 domain [General function prediction only];
2077-2281 2.58e-06

Fibronectin type 3 domain [General function prediction only];


Pssm-ID: 442628 [Multi-domain]  Cd Length: 603  Bit Score: 54.62  E-value: 2.58e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 2077 YQIKISNGQGEDTKDVQII----CQDVPQPPQDVDITDVYQTSCVVSFNPPSDDGgtpITKYVIERqDLSKKHGWESVAE 2152
Cdd:COG3401   300 YRVTAVDAAGNESAPSNVVsvttDLTPPAAPSGLTATAVGSSSITLSWTASSDAD---VTGYNVYR-STSGGGTYTKIAE 375
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 2153 VLPSEPClkKIDDLIPKKQYRFRIRAVNAIGQSDPATFKNTILAKDPW--DEPGKPKAVDLTDWDKDHADLKWEAPETDG 2230
Cdd:COG3401   376 TVTTTSY--TDTGLTPGTTYYYKVTAVDAAGNESAPSEEVSATTASAAsgESLTASVDAVPLTDVAGATAAASAASNPGV 453
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|.
gi 281359561 2231 GDPITAYIVEYKEKFSNDWVSGKEVDGDARTATVDGLKEGQQYEFRVRAVN 2281
Cdd:COG3401   454 SAAVLADGGDTGNAVPFTTTSSTVTATTTDTTTANLSVTTGSLVGGSGASS 504
Ig_C5_MyBP-C cd05894
C5 immunoglobulin (Ig) domain of cardiac myosin binding protein C (MyBP-C); The members here ...
2314-2385 2.69e-06

C5 immunoglobulin (Ig) domain of cardiac myosin binding protein C (MyBP-C); The members here are composed of the C5 immunoglobulin (Ig) domain of cardiac myosin binding protein C (MyBP-C). MyBP-C consists of repeated domains, Ig and fibronectin type 3, and various linkers. Three isoforms of MYBP-C exist: slow-skeletal (ssMyBP-C), fast-skeletal (fsMyBP-C), and cardiac (cMyBP-C). cMYBP-C has insertions between and inside domains and an additional cardiac-specific Ig domain at the N-terminus. For cMYBP_C an interaction has been demonstrated between this C5 domain and the Ig C8 domain.


Pssm-ID: 409475  Cd Length: 86  Bit Score: 49.07  E-value: 2.69e-06
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 281359561 2314 VTVKKGQTIRFDIKYDGEPEPAATWVKGTDNLKFDNQRICLDQLERNSSITIKKSVRKDTGKYKLVLSNSSG 2385
Cdd:cd05894     5 IVVVAGNKLRLDVPISGEPAPTVTWSRGDKAFTATEGRVRVESYKDLSSFVIEGAEREDEGVYTITVTNPVG 76
IgI_Titin_like cd05747
Immunoglobulin (Ig)-like domain of human titin C terminus and similar proteins; member of the ...
8311-8394 2.81e-06

Immunoglobulin (Ig)-like domain of human titin C terminus and similar proteins; member of the I-set of Ig superfamily (IgSF) domains; The members here are composed of the fifth immunoglobulin (Ig)-like domain from the C-terminus of human titin x and similar proteins. Titin (also called connectin) is a fibrous sarcomeric protein specifically found in vertebrate striated muscle. Titin is gigantic; depending on isoform composition it ranges from 2970 to 3700 kDa, and is of a length that spans half a sarcomere. Titin largely consists of multiple repeats of Ig-like and fibronectin type 3 (FN-III)-like domains. Titin connects the ends of myosin thick filaments to Z disks and extends along the thick filament to the H zone and appears to function similar to an elastic band, keeping the myosin filaments centered in the sarcomere during muscle contraction or stretching. This group belongs to the I-set of IgSF domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand, but lack a C" strand.


Pssm-ID: 143224 [Multi-domain]  Cd Length: 92  Bit Score: 49.28  E-value: 2.81e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 8311 APRFVIRPSSQFCYEGQSVKFYCRCIAIATPTLTWSHNNIELRQSVKFMKRYVGDDYYFIINRVKLDDRGEYIIRAENHY 8390
Cdd:cd05747     3 PATILTKPRSLTVSEGESARFSCDVDGEPAPTVTWMREGQIIVSSQRHQITSTEYKSTFEISKVQMSDEGNYTVVVENSE 82

                  ....
gi 281359561 8391 GSRE 8394
Cdd:cd05747    83 GKQE 86
Ig3_Peroxidasin cd05745
Third immunoglobulin (Ig)-like domain of peroxidasin; The members here are composed of the ...
8645-8721 2.97e-06

Third immunoglobulin (Ig)-like domain of peroxidasin; The members here are composed of the third immunoglobulin (Ig)-like domain in peroxidasin. Peroxidasin has a peroxidase domain and interacting extracellular motifs containing four Ig-like domains. It has been suggested that peroxidasin is secreted and has functions related to the stabilization of the extracellular matrix. It may play a part in various other important processes such as removal and destruction of cells which have undergone programmed cell death and protection of the organism against non-self.


Pssm-ID: 143222 [Multi-domain]  Cd Length: 74  Bit Score: 48.78  E-value: 2.97e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 8645 DGEQLILTCYVKGDPEPQISWSKNGKSLSssdiLDLRY---KNGiaTLTINEVFPEDEGVITCTATNSVGAVETKCKLTI 8721
Cdd:cd05745     1 EGQTVDFLCEAQGYPQPVIAWTKGGSQLS----VDRRHlvlSSG--TLRISRVALHDQGQYECQAVNIVGSQRTVAQLTV 74
IG_like smart00410
Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.
5874-5954 3.12e-06

Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.


Pssm-ID: 214653 [Multi-domain]  Cd Length: 85  Bit Score: 49.04  E-value: 3.12e-06
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561   5874 VRIKCglifhtdiHFIGEPAPEATWTLNS-NPLLSNDRSTITSIGHHSVVHTVNCQRSDSGIYHLLLRNSSGIDEGSFEL 5952
Cdd:smart00410   12 VTLSC--------EASGSPPPEVTWYKQGgKLLAESGRFSVSRSGSTSTLTISNVTPEDSGTYTCAATNSSGSASSGTTL 83

                    ..
gi 281359561   5953 VV 5954
Cdd:smart00410   84 TV 85
Ig_Titin_like cd05748
Immunoglobulin (Ig)-like domain of titin and similar proteins; The members here are composed ...
8641-8711 3.12e-06

Immunoglobulin (Ig)-like domain of titin and similar proteins; The members here are composed of the immunoglobulin (Ig)-like domain found in titin-like proteins and similar proteins. Titin (also called connectin) is a fibrous sarcomeric protein specifically found in vertebrate striated muscle. Titin is a giant protein; depending on isoform composition, it ranges from 2970 to 3700 kDa, and is of a length that spans half a sarcomere. Titin largely consists of multiple repeats of Ig-like and fibronectin type 3 (FN-III)-like domains. Titin connects the ends of myosin thick filaments to Z disks and extends along the thick filament to the H zone. It appears to function similarly to an elastic band, keeping the myosin filaments centered in the sarcomere during muscle contraction or stretching. Within the sarcomere, titin is also attached to or is associated with myosin binding protein C (MyBP-C). MyBP-C appears to contribute to the generation of passive tension by titin and like titin has repeated Ig-like and FN-III domains. Also included in this group are worm twitchin and insect projectin, thick filament proteins of invertebrate muscle which also have repeated Ig-like and FN-III domains.


Pssm-ID: 409406 [Multi-domain]  Cd Length: 82  Bit Score: 48.74  E-value: 3.12e-06
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 281359561 8641 LTIHDGEQLILTCYVKGDPEPQISWSKNGKSLSSSDILDLRYKNGIATLTINEVFPEDEGVITCTATNSVG 8711
Cdd:cd05748     2 IVVRAGESLRLDIPIKGRPTPTVTWSKDGQPLKETGRVQIETTASSTSLVIKNAKRSDSGKYTLTLKNSAG 72
Ig_C5_MyBP-C cd05894
C5 immunoglobulin (Ig) domain of cardiac myosin binding protein C (MyBP-C); The members here ...
3809-3885 3.15e-06

C5 immunoglobulin (Ig) domain of cardiac myosin binding protein C (MyBP-C); The members here are composed of the C5 immunoglobulin (Ig) domain of cardiac myosin binding protein C (MyBP-C). MyBP-C consists of repeated domains, Ig and fibronectin type 3, and various linkers. Three isoforms of MYBP-C exist: slow-skeletal (ssMyBP-C), fast-skeletal (fsMyBP-C), and cardiac (cMyBP-C). cMYBP-C has insertions between and inside domains and an additional cardiac-specific Ig domain at the N-terminus. For cMYBP_C an interaction has been demonstrated between this C5 domain and the Ig C8 domain.


Pssm-ID: 409475  Cd Length: 86  Bit Score: 49.07  E-value: 3.15e-06
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 281359561 3809 SGQMLHIDALIKAEPPAKVTWTYNKTEIKTSD-HIKIENEDYKTTFIMPKVKRADRGIYIVTAKNDSGSDTVEVELEV 3885
Cdd:cd05894     9 AGNKLRLDVPISGEPAPTVTWSRGDKAFTATEgRVRVESYKDLSSFVIEGAEREDEGVYTITVTNPVGEDHASLFVKV 86
Ig cd00096
Immunoglobulin domain; The members here are composed of the immunoglobulin (Ig) domain found ...
6183-6245 3.18e-06

Immunoglobulin domain; The members here are composed of the immunoglobulin (Ig) domain found in the Ig superfamily. The Ig superfamily is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. Members of this group are components of immunoglobulin, neuroglia, cell surface glycoproteins, including T-cell receptors, CD2, CD4, CD8, and membrane glycoproteins, including butyrophilin and chondroitin sulfate proteoglycan core protein. A predominant feature of most Ig domains is a disulfide bridge connecting the two beta-sheets with a tryptophan residue packed against the disulfide bond. Ig superfamily (IgSF) domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. Typically, the V-set domains have A, B, E, and D strands in one sheet and A', G, F, C, C' and C" in the other. The structures in C1-set are smaller than those in the V-set; they have one beta sheet that is formed by strands A, B, E, and D and the other by strands G, F, C, and C'. Moreover, a C1-set Ig domain contains a short C' strand (three residues) and lacks A' and C" strand. Unlike other Ig domain sets, C2-set structures do not have a D strand. Like the V-set Ig domains, members of the I-set have a discontinuous A strand, but lack a C" strand.


Pssm-ID: 409353 [Multi-domain]  Cd Length: 70  Bit Score: 48.48  E-value: 3.18e-06
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 281359561 6183 VNLNIPISGAPTPTIEWKRGDLKLEEGKRISYETNSERTLFRIDDSNRRDSGKYTVTAANEFG 6245
Cdd:cd00096     1 VTLTCSASGNPPPTITWYKNGKPLPPSSRDSRRSELGNGTLTISNVTLEDSGTYTCVASNSAG 63
IgI_1_Titin_Z1z2-like cd20974
First Ig-like domain of the giant muscle protein titin Z1z2 in the sarcomeric Z-disk and ...
2909-2996 3.22e-06

First Ig-like domain of the giant muscle protein titin Z1z2 in the sarcomeric Z-disk and similar proteins; a member of the I-set of IgSF domains; The members here are composed of the first immunoglobulin (Ig)-like domain of the giant muscle protein titin Z1z2 in the sarcomeric Z-disk and similar proteins. Titin is a key component in the assembly and functioning of vertebrate striated muscles. By providing connections at the level of individual microfilaments, it contributes to the fine balance of forces between the two halves of the sarcomere. The Ig superfamily (IgSF) is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. Unlike the V-set, one of the distinctive features of I-set domains is the lack of a C" strand. The structure of the titin Z1z2 lacks this strand and thus it belongs to the I-set of the IgSF. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors, the hemolymph protein hemolin, the muscle proteins titin, telokin, and twitchin, the neuronal adhesion molecule axonin-1, and the signaling molecule semaphorin 4D that is involved in axonal guidance, immune function and angiogenesis.


Pssm-ID: 409566 [Multi-domain]  Cd Length: 93  Bit Score: 49.27  E-value: 3.22e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 2909 LKPLLIRAGKPIRYDVNVRGEPAPVITWYQNDKELKPEELPsSSEIKNIPYNTKISIIETVRKHTGIYKIIAVNEHGQDE 2988
Cdd:cd20974     7 LQSVVVLEGSTATFEAHVSGKPVPEVSWFRDGQVISTSTLP-GVQISFSDGRAKLSIPAVTKANSGRYSLTATNGSGQAT 85

                  ....*...
gi 281359561 2989 ATVEVNIL 2996
Cdd:cd20974    86 STAELLVL 93
Ig4_Contactin-2-like cd05728
Fourth Ig domain of the neural cell adhesion molecule contactin-2, and similar domains; The ...
563-636 3.25e-06

Fourth Ig domain of the neural cell adhesion molecule contactin-2, and similar domains; The members here are composed of the fourth Ig domain of the neural cell adhesion molecule contactin-2. Contactins are comprised of six Ig domains followed by four fibronectin type III (FnIII) domains anchored to the membrane by glycosylphosphatidylinositol. Contactin-2 (also called TAG-1, axonin-1) facilitates cell adhesion by homophilic binding between molecules in apposed membranes. The first four Ig domains form the intermolecular binding fragment which arranges as a compact U-shaped module by contacts between Ig domains 1 and 4, and domains 2 and 3. It has been proposed that a linear zipper-like array forms, from contactin-2 molecules alternatively provided by the two apposed membranes.


Pssm-ID: 143205 [Multi-domain]  Cd Length: 85  Bit Score: 48.75  E-value: 3.25e-06
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 281359561  563 ECKVKADPKPDVIWFRNGEVIKESNKIKTfieQRGDQYYIKLelldpQLEDSGLYKCNIKNTLGELNANLTLNI 636
Cdd:cd05728    20 ECKASGNPRPAYRWLKNGQPLASENRIEV---EAGDLRITKL-----SLSDSGMYQCVAENKHGTIYASAELAV 85
ig pfam00047
Immunoglobulin domain; Members of the immunoglobulin superfamily are found in hundreds of ...
557-634 3.32e-06

Immunoglobulin domain; Members of the immunoglobulin superfamily are found in hundreds of proteins of different functions. Examples include antibodies, the giant muscle kinase titin and receptor tyrosine kinases. Immunoglobulin-like domains may be involved in protein-protein and protein-ligand interactions.


Pssm-ID: 395002  Cd Length: 86  Bit Score: 48.73  E-value: 3.32e-06
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 281359561   557 GKLVIMECKVK-ADPKPDVIWFRNGEVIKESNKIKtfiEQRGDQYYIKLELLDPQLEDSGLYKCNIKNTLGELNANLTL 634
Cdd:pfam00047   11 GDSATLTCSAStGSPGPDVTWSKEGGTLIESLKVK---HDNGRTTQSSLLISNVTKEDAGTYTCVVNNPGGSATLSTSL 86
IG_like smart00410
Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.
4693-4775 3.37e-06

Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.


Pssm-ID: 214653 [Multi-domain]  Cd Length: 85  Bit Score: 48.66  E-value: 3.37e-06
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561   4693 RNITLSSGTALKLDANITGEPAPKVEW-KLSNYHLQSGKNVTIETPDYYTKLVIRPTQRSDSGEYLVTATNTSGKDSVLV 4771
Cdd:smart00410    2 PSVTVKEGESVTLSCEASGSPPPEVTWyKQGGKLLAESGRFSVSRSGSTSTLTISNVTPEDSGTYTCAATNSSGSASSGT 81

                    ....
gi 281359561   4772 NVVI 4775
Cdd:smart00410   82 TLTV 85
IgI_4_hemolin-like cd20978
Fourth immunoglobulin (Ig)-like domain of hemolin, and similar domains; a member of the I-set ...
4979-5069 3.45e-06

Fourth immunoglobulin (Ig)-like domain of hemolin, and similar domains; a member of the I-set of IgSF domains; The members here are composed of the fourth immunoglobulin (Ig)-like domain of hemolin and similar proteins. Hemolin, an insect immunoglobulin superfamily (IgSF) member containing four Ig-like domains, is a lipopolysaccharide-binding immune protein induced during bacterial infection. Hemolin shares significant sequence similarity with the first four Ig-like domains of the transmembrane cell adhesion molecules (CAMs) of the L1 family. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. The fourth Ig-like domain of hemolin is a member of the I-set Ig domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set domains, members of the I-set have a discontinuous A strand but lack a C" strand. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors, the muscle proteins titin, telokin, and twitchin, the neuronal adhesion molecule axonin-1, and the signaling molecule semaphorin 4D that is involved in axonal guidance, immune function and angiogenesis.


Pssm-ID: 409570 [Multi-domain]  Cd Length: 88  Bit Score: 48.93  E-value: 3.45e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 4979 PIIDRSSLVEVRIKAGQSFTFDCKVSGEPAPQTKWLLKKKEVysKDNVKVTNVDYNTkLKVNSATRSDSGIYTVFAENAN 5058
Cdd:cd20978     1 PKFIQKPEKNVVVKGGQDVTLPCQVTGVPQPKITWLHNGKPL--QGPMERATVEDGT-LTIINVQPEDTGYYGCVATNEI 77
                          90
                  ....*....|.
gi 281359561 5059 GEDSADVKVTV 5069
Cdd:cd20978    78 GDIYTETLLHV 88
Ig_3 pfam13927
Immunoglobulin domain; This family contains immunoglobulin-like domains.
5275-5353 3.56e-06

Immunoglobulin domain; This family contains immunoglobulin-like domains.


Pssm-ID: 464046 [Multi-domain]  Cd Length: 78  Bit Score: 48.33  E-value: 3.56e-06
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 281359561  5275 PPKIdRNFMSDIKIKAGNVFEFDVPVTGEPLPSKDWTHEGNMIINTDRVKISNFDDRTKIRILDAKRSDTGVYTLTARN 5353
Cdd:pfam13927    1 KPVI-TVSPSSVTVREGETVTLTCEATGSPPPTITWYKNGEPISSGSTRSRSLSGSNSTLTISNVTRSDAGTYTCVASN 78
IgI_Twitchin_like cd20949
C-terminal immunoglobulin-like domain of the myosin-associated giant protein kinase Twitchin, ...
8440-8518 3.57e-06

C-terminal immunoglobulin-like domain of the myosin-associated giant protein kinase Twitchin, and similar domains; member of the I-set IgSF domains; The members here are composed of the C-terminal immunoglobulin-like domain of the myosin-associated giant protein kinase Twitchin and similar proteins, including Caenorhabditis elegans and Aplysia californica Twitchin, Drosophila melanogaster Projectin, and similar proteins. These are very large muscle proteins containing multiple immunoglobulin (Ig)-like and fibronectin type III (FN3) domains and a single kinase domain near the C-terminus. In humans these proteins are called Titin. The Ig superfamily (IgSF) is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. The Ig-like domain of the Twitchin is a member of the I-set IgSF domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand but lack a C" strand. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors, the hemolymph protein hemolin, the muscle proteins (titin, telokin, and twitchin), the neuronal adhesion molecule axonin-1, and the signaling molecule semaphorin 4D.


Pssm-ID: 409541 [Multi-domain]  Cd Length: 89  Bit Score: 48.87  E-value: 3.57e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 8440 TFLLRPRVMQARD--TCKLLCCLSGKPVPNVRWYKDGRELSKYEYAMTHSDGVVTMEIID-CKPSDSGKYSCKATNCHGT 8516
Cdd:cd20949     1 TFTENAYVTTVKEgqSATILCEVKGEPQPNVTWHFNGQPISASVADMSKYRILADGLLINkVTQDDTGEYTCRAYQVNSI 80

                  ..
gi 281359561 8517 DE 8518
Cdd:cd20949    81 AS 82
IgI_Myotilin_C_like cd05744
Immunoglobulin (Ig)-like domain of myotilin, palladin, and myopalladin; member of the I-set of ...
4099-4181 3.61e-06

Immunoglobulin (Ig)-like domain of myotilin, palladin, and myopalladin; member of the I-set of Ig superfamily (IgSF) domains; The members here are composed of the immunoglobulin (Ig)-like domain in myotilin, palladin, and myopalladin. Myotilin, palladin, and myopalladin function as scaffolds that regulate actin organization. Myotilin and myopalladin are most abundant in skeletal and cardiac muscle; palladin is ubiquitously expressed in the organs of developing vertebrates and plays a key role in cellular morphogenesis. The three family members each interact with specific molecular partners with all three binding to alpha-actinin; In addition, palladin also binds to vasodilator-stimulated phosphoprotein (VASP) and ezrin, myotilin binds to filamin and actin, and myopalladin also binds to nebulin and cardiac ankyrin repeat protein (CARP). This group belongs to the I-set of IgSF domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand, but lack a C" strand.


Pssm-ID: 409405 [Multi-domain]  Cd Length: 91  Bit Score: 49.03  E-value: 3.61e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 4099 DITIKAGQHIRFDIKVSGEPPATKVWLHNKARLENDDSNYNIDMESYRTKLTVPISKRFHSGKYTLKAENESGRDEASFE 4178
Cdd:cd05744     9 DLEVQEGRLCRFDCKVSGLPTPDLFWQLNGKPVRPDSAHKMLVRENGRHSLIIEPVTKRDAGIYTCIARNRAGENSFNAE 88

                  ...
gi 281359561 4179 VIV 4181
Cdd:cd05744    89 LVV 91
IgI_1_Titin_Z1z2-like cd20974
First Ig-like domain of the giant muscle protein titin Z1z2 in the sarcomeric Z-disk and ...
6177-6255 3.65e-06

First Ig-like domain of the giant muscle protein titin Z1z2 in the sarcomeric Z-disk and similar proteins; a member of the I-set of IgSF domains; The members here are composed of the first immunoglobulin (Ig)-like domain of the giant muscle protein titin Z1z2 in the sarcomeric Z-disk and similar proteins. Titin is a key component in the assembly and functioning of vertebrate striated muscles. By providing connections at the level of individual microfilaments, it contributes to the fine balance of forces between the two halves of the sarcomere. The Ig superfamily (IgSF) is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. Unlike the V-set, one of the distinctive features of I-set domains is the lack of a C" strand. The structure of the titin Z1z2 lacks this strand and thus it belongs to the I-set of the IgSF. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors, the hemolymph protein hemolin, the muscle proteins titin, telokin, and twitchin, the neuronal adhesion molecule axonin-1, and the signaling molecule semaphorin 4D that is involved in axonal guidance, immune function and angiogenesis.


Pssm-ID: 409566 [Multi-domain]  Cd Length: 93  Bit Score: 48.89  E-value: 3.65e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 6177 VRAGEPVNLNIPISGAPTPTIEWKR-GD-LKLEEGKRISYETNSERTLFRIDDSNRRDSGKYTVTAANEFGKDTADIEVI 6254
Cdd:cd20974    12 VLEGSTATFEAHVSGKPVPEVSWFRdGQvISTSTLPGVQISFSDGRAKLSIPAVTKANSGRYSLTATNGSGQATSTAELL 91

                  .
gi 281359561 6255 V 6255
Cdd:cd20974    92 V 92
Ig_3 pfam13927
Immunoglobulin domain; This family contains immunoglobulin-like domains.
5564-5647 3.67e-06

Immunoglobulin domain; This family contains immunoglobulin-like domains.


Pssm-ID: 464046 [Multi-domain]  Cd Length: 78  Bit Score: 48.33  E-value: 3.67e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561  5564 KPRFLAPFfdksllNDITVHAGKRLgwTLPIEAS--PRPLITWLYNGKEIGSNSRGESGLFQNELTFEIVSSLRSDEGRY 5641
Cdd:pfam13927    1 KPVITVSP------SSVTVREGETV--TLTCEATgsPPPTITWYKNGEPISSGSTRSRSLSGSNSTLTISNVTRSDAGTY 72

                   ....*.
gi 281359561  5642 TLILKN 5647
Cdd:pfam13927   73 TCVASN 78
IgI_4_MYLK-like cd20976
Fourth Ig-like domain from smooth muscle myosin light chain kinase and similar domains ; a ...
8739-8831 3.70e-06

Fourth Ig-like domain from smooth muscle myosin light chain kinase and similar domains ; a member of the I-set of IgSF domains; The members here are composed of the fourth immunoglobulin (Ig)-like domain from smooth muscle myosin light chain kinase (MYLK) and similar domains. The Ig superfamily (IgSF) is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. Unlike the V-set, one of the distinctive features of I-set domains is the lack of a C" strand. The structure of this group shows that the fourth Ig-like domain from myosin light chain kinase lacks this strand and thus belongs to the I-set of the IgSF. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors, the hemolymph protein hemolin, the muscle proteins titin, telokin, and twitchin, the neuronal adhesion molecule axonin-1, and the signaling molecule semaphorin 4D that is involved in axonal guidance, immune function and angiogenesis.


Pssm-ID: 409568 [Multi-domain]  Cd Length: 90  Bit Score: 48.79  E-value: 3.70e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 8739 APKIVSHLESRFVRDGDAVNLACRIIGAQHFDVVWLHNNKEIKPSKDfQYTNEANIYRLQIAEIFPEDGGTYTCEAFNDI 8818
Cdd:cd20976     1 APSFSSVPKDLEAVEGQDFVAQCSARGKPVPRITWIRNAQPLQYAAD-RSTCEAGVGELHIQDVLPEDHGTYTCLAKNAA 79
                          90
                  ....*....|...
gi 281359561 8819 GEsfSTCTINVTV 8831
Cdd:cd20976    80 GQ--VSCSAWVTV 90
IgI_Myomesin_like_C cd05737
C-terminal immunoglobulin (Ig)-like domain of myomesin and M-protein; member of the I-set of ...
4989-5069 3.72e-06

C-terminal immunoglobulin (Ig)-like domain of myomesin and M-protein; member of the I-set of Ig superfamily (IgSF) domains; The members here are composed of the C-terminal immunoglobulin (Ig)-like domain of myomesin and M-protein (also known as myomesin-2). Myomesin and M-protein are both structural proteins localized to the M-band, a transverse structure in the center of the sarcomere, and are candidates for M-band bridges. Both proteins are modular, consisting mainly of repetitive Ig-like and fibronectin type III (FnIII) domains. Myomesin is expressed in all types of vertebrate striated muscle; M-protein has a muscle-type specific expression pattern. Myomesin is present in both slow and fast fibers; M-protein is present only in fast fibers. It has been suggested that myomesin acts as a molecular spring with alternative splicing as a means of modifying its elasticity.


Pssm-ID: 319300  Cd Length: 92  Bit Score: 48.74  E-value: 3.72e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 4989 VRIKAGQSFTFDCKVSGEPAPQTKWLLKKKEVYSKD--NVKVTNVDYNTkLKVNSATRSDSGIYTVFAENANGEDSADVK 5066
Cdd:cd05737    11 VTIMEGKTLNLTCNVWGDPPPEVSWLKNDQALAFLDhcNLKVEAGRTVY-FTINGVSSEDSGKYGLVVKNKYGSETSDVT 89

                  ...
gi 281359561 5067 VTV 5069
Cdd:cd05737    90 VSV 92
IgI_Myomesin_like_C cd05737
C-terminal immunoglobulin (Ig)-like domain of myomesin and M-protein; member of the I-set of ...
6175-6255 3.83e-06

C-terminal immunoglobulin (Ig)-like domain of myomesin and M-protein; member of the I-set of Ig superfamily (IgSF) domains; The members here are composed of the C-terminal immunoglobulin (Ig)-like domain of myomesin and M-protein (also known as myomesin-2). Myomesin and M-protein are both structural proteins localized to the M-band, a transverse structure in the center of the sarcomere, and are candidates for M-band bridges. Both proteins are modular, consisting mainly of repetitive Ig-like and fibronectin type III (FnIII) domains. Myomesin is expressed in all types of vertebrate striated muscle; M-protein has a muscle-type specific expression pattern. Myomesin is present in both slow and fast fibers; M-protein is present only in fast fibers. It has been suggested that myomesin acts as a molecular spring with alternative splicing as a means of modifying its elasticity.


Pssm-ID: 319300  Cd Length: 92  Bit Score: 48.74  E-value: 3.83e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 6175 IKVRAGEPVNLNIPISGAPTPTIEWKRGDLKLEEGKRISYETNSERTL-FRIDDSNRRDSGKYTVTAANEFGKDTADIEV 6253
Cdd:cd05737    11 VTIMEGKTLNLTCNVWGDPPPEVSWLKNDQALAFLDHCNLKVEAGRTVyFTINGVSSEDSGKYGLVVKNKYGSETSDVTV 90

                  ..
gi 281359561 6254 IV 6255
Cdd:cd05737    91 SV 92
IgI_titin_I1-like cd20951
Immunoglobulin domain I1 of the titin I-band and similar proteins; a member of the I-set of ...
545-637 4.24e-06

Immunoglobulin domain I1 of the titin I-band and similar proteins; a member of the I-set of IgSF domains; The members here are composed of the immunoglobulin domain I1 of the titin I-band and similar proteins. Titin is a key component in the assembly and functioning of vertebrate striated muscles. By providing connections at the level of individual microfilaments, it contributes to the fine balance of forces between the two halves of the sarcomere. The Ig superfamily (IgSF) is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. The two sheets are linked together by a conserved disulfide bond between B strand and F strand. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. The Ig I1 domain of the titin I-band is a member of the I-set Ig domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand but lack a C" strand. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors, the hemolymph protein hemolin, the muscle proteins titin, telokin, and twitchin, the neuronal adhesion molecule axonin-1, and the signaling molecule semaphorin 4D that is involved in axonal guidance, immune function and angiogenesis.


Pssm-ID: 409543 [Multi-domain]  Cd Length: 94  Bit Score: 48.96  E-value: 4.24e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561  545 FIEKPRIVSENNGKLVIMECKVKADPKPDVIWFRNGEVIKESNKIKTFIEQRgdQYYI-KLELLDPQLEDSGLYKCNIKN 623
Cdd:cd20951     3 FIIRLQSHTVWEKSDAKLRVEVQGKPDPEVKWYKNGVPIDPSSIPGKYKIES--EYGVhVLHIRRVTVEDSAVYSAVAKN 80
                          90
                  ....*....|....
gi 281359561  624 TLGELNANLTLNIE 637
Cdd:cd20951    81 IHGEASSSASVVVE 94
IgI_NCAM-1_like cd05732
Immunoglobulin (Ig)-like I-set domain of Neural Cell Adhesion Molecule 1 (NCAM-1) and similar ...
1831-1897 4.40e-06

Immunoglobulin (Ig)-like I-set domain of Neural Cell Adhesion Molecule 1 (NCAM-1) and similar proteins; The members here are composed of the fourth immunoglobulin (Ig)-like domain of Neural Cell Adhesion Molecule (NCAM-1). NCAM plays important roles in the development and regeneration of the central nervous system, in synaptogenesis and neural migration. NCAM mediates cell-cell and cell-substratum recognition and adhesion via homophilic (NCAM-NCAM), and heterophilic (NCAM-non-NCAM), interactions. NCAM is expressed as three major isoforms having different intracellular extensions. The extracellular portion of NCAM has five N-terminal Ig-like domains and two fibronectin type III domains. The double zipper adhesion complex model for NCAM homophilic binding involves Ig1, Ig2, and Ig3. By this model, Ig1 and Ig2 mediate dimerization of NCAM molecules situated on the same cell surface (cis interactions), and Ig3 domains mediate interactions between NCAM molecules expressed on the surface of opposing cells (trans interactions), through binding to the Ig1 and Ig2 domains. The adhesive ability of NCAM is modulated by the addition of polysialic acid chains to the fifth Ig-like domain. Also included in this group is NCAM-2 (also known as OCAM/mamFas II and RNCAM) NCAM-2 is differentially expressed in the developing and mature olfactory epithelium (OE). One of the unique features of I-set domains is the lack of a C" strand. The structures of this group show that the Ig domain lacks this strand and thus is a member of the I-set of Ig domains.


Pssm-ID: 409395 [Multi-domain]  Cd Length: 96  Bit Score: 48.67  E-value: 4.40e-06
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 281359561 1831 LKSQQCIEKDTVTLACEID-DAMGEVQWLR-----NGEEIKPDKRIQIVKDGRKRKLVIKDCKVTDAGQFKCT 1897
Cdd:cd05732     8 LENQTAVELEQITLTCEAEgDPIPEITWRRatrgiSFEEGDLDGRIVVRGHARVSSLTLKDVQLTDAGRYDCE 80
IgI_APEG-1_like cd20975
Immunoglobulin-like domain of human Aortic Preferentially Expressed Protein-1 (APEG-1) and ...
4094-4179 4.77e-06

Immunoglobulin-like domain of human Aortic Preferentially Expressed Protein-1 (APEG-1) and similar proteins; a member of the I-set of IgSF domains; The members here are composed of the immunoglobulin I-set (IgI) domain of the Human Aortic Preferentially Expressed Protein-1 (APEG-1) and similar proteins. APEG-1 is a novel specific smooth muscle differentiation marker predicted to play a role in the growth and differentiation of arterial smooth muscle cells (SMCs). The Ig superfamily (IgSF) is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. Unlike the V-set, one of the distinctive features of I-set domains is the lack of a C" strand. The structure of the human APEG-1 lacks this strand and thus it belongs to the I-set of the IgSF. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors, the hemolymph protein hemolin, the muscle proteins titin, telokin, and twitchin, the neuronal adhesion molecule axonin-1, and the signaling molecule semaphorin 4D that is involved in axonal guidance, immune function and angiogenesis.


Pssm-ID: 409567  Cd Length: 91  Bit Score: 48.62  E-value: 4.77e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 4094 RTNIKDITIKAGQHIRFDIKVSGEPPATKVWLHNKARLENDDSNYNIDMESYRTKLTVPISKRFHSGKYTLKAENESG-- 4171
Cdd:cd20975     4 KVSLMDQSVREGQDVIMSIRVQGEPKPVVSWLRNRQPVRPDQRRFAEEAEGGLCRLRILAAERGDAGFYTCKAVNEYGar 83

                  ....*...
gi 281359561 4172 RDEASFEV 4179
Cdd:cd20975    84 QCEARLEV 91
IgI_Titin_like cd05747
Immunoglobulin (Ig)-like domain of human titin C terminus and similar proteins; member of the ...
241-320 4.95e-06

Immunoglobulin (Ig)-like domain of human titin C terminus and similar proteins; member of the I-set of Ig superfamily (IgSF) domains; The members here are composed of the fifth immunoglobulin (Ig)-like domain from the C-terminus of human titin x and similar proteins. Titin (also called connectin) is a fibrous sarcomeric protein specifically found in vertebrate striated muscle. Titin is gigantic; depending on isoform composition it ranges from 2970 to 3700 kDa, and is of a length that spans half a sarcomere. Titin largely consists of multiple repeats of Ig-like and fibronectin type 3 (FN-III)-like domains. Titin connects the ends of myosin thick filaments to Z disks and extends along the thick filament to the H zone and appears to function similar to an elastic band, keeping the myosin filaments centered in the sarcomere during muscle contraction or stretching. This group belongs to the I-set of IgSF domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand, but lack a C" strand.


Pssm-ID: 143224 [Multi-domain]  Cd Length: 92  Bit Score: 48.51  E-value: 4.95e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561  241 DGGNVTFECRCVGDPTPTVTWSHGETELNESNRYKMSLTMDQKLYhiaclEISSVVSSDQGEYRAQAKNKHGSGVATINL 320
Cdd:cd05747    17 EGESARFSCDVDGEPAPTVTWMREGQIIVSSQRHQITSTEYKSTF-----EISKVQMSDEGNYTVVVENSEGKQEAQFTL 91
Ig_Titin_like cd05748
Immunoglobulin (Ig)-like domain of titin and similar proteins; The members here are composed ...
5580-5660 5.30e-06

Immunoglobulin (Ig)-like domain of titin and similar proteins; The members here are composed of the immunoglobulin (Ig)-like domain found in titin-like proteins and similar proteins. Titin (also called connectin) is a fibrous sarcomeric protein specifically found in vertebrate striated muscle. Titin is a giant protein; depending on isoform composition, it ranges from 2970 to 3700 kDa, and is of a length that spans half a sarcomere. Titin largely consists of multiple repeats of Ig-like and fibronectin type 3 (FN-III)-like domains. Titin connects the ends of myosin thick filaments to Z disks and extends along the thick filament to the H zone. It appears to function similarly to an elastic band, keeping the myosin filaments centered in the sarcomere during muscle contraction or stretching. Within the sarcomere, titin is also attached to or is associated with myosin binding protein C (MyBP-C). MyBP-C appears to contribute to the generation of passive tension by titin and like titin has repeated Ig-like and FN-III domains. Also included in this group are worm twitchin and insect projectin, thick filament proteins of invertebrate muscle which also have repeated Ig-like and FN-III domains.


Pssm-ID: 409406 [Multi-domain]  Cd Length: 82  Bit Score: 47.97  E-value: 5.30e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 5580 ITVHAGKRLGWTLPIEASPRPLITWLYNGKEIGSNSRgesglFQNELTfEIVSSL------RSDEGRYTLILKNEHGSfd 5653
Cdd:cd05748     2 IVVRAGESLRLDIPIKGRPTPTVTWSKDGQPLKETGR-----VQIETT-ASSTSLviknakRSDSGKYTLTLKNSAGE-- 73

                  ....*..
gi 281359561 5654 ASAHATV 5660
Cdd:cd05748    74 KSATINV 80
Ig4_Peroxidasin cd05746
Fourth immunoglobulin (Ig)-like domain of peroxidasin; The members here are composed of the ...
7273-7339 5.32e-06

Fourth immunoglobulin (Ig)-like domain of peroxidasin; The members here are composed of the fourth immunoglobulin (Ig)-like domain in peroxidasin. Peroxidasin has a peroxidase domain and interacting extracellular motifs containing four Ig-like domains. It has been suggested that peroxidasin is secreted, and has functions related to the stabilization of the extracellular matrix. It may play a part in various other important processes such as removal and destruction of cells which have undergone programmed cell death and protection of the organism against non-self.


Pssm-ID: 143223  Cd Length: 69  Bit Score: 47.56  E-value: 5.32e-06
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 281359561 7273 LQCAASGKPSPTARWLRNGKEIQMNGGRMTcdSKDGVfrLHISNVQTGDDGDYTCEAMNSLGFVNTS 7339
Cdd:cd05746     3 IPCSAQGDPEPTITWNKDGVQVTESGKFHI--SPEGY--LAIRDVGVADQGRYECVARNTIGYASVS 65
Ig_3 pfam13927
Immunoglobulin domain; This family contains immunoglobulin-like domains.
2601-2680 5.75e-06

Immunoglobulin domain; This family contains immunoglobulin-like domains.


Pssm-ID: 464046 [Multi-domain]  Cd Length: 78  Bit Score: 47.95  E-value: 5.75e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561  2601 KPQIdRSTFKRVTIKSGRTHKWSVDVLGEPIPELHWSwRDDIPLTNGDRIKIENVDYHTDFSITNVLRKDSGFYTLKAEN 2680
Cdd:pfam13927    1 KPVI-TVSPSSVTVREGETVTLTCEATGSPPPTITWY-KNGEPISSGSTRSRSLSGSNSTLTISNVTRSDAGTYTCVASN 78
IgI_2_Titin_Z1z2-like cd20972
Second Ig-like domain of the giant muscle protein titin Z1z2 in the sarcomeric Z-disk, and ...
6177-6255 5.87e-06

Second Ig-like domain of the giant muscle protein titin Z1z2 in the sarcomeric Z-disk, and similar domains; a member of the I-set of IgSF domains; The members here are composed of the second immunoglobulin (Ig)-like domain of the giant muscle protein titin Z1z2 in the sarcomeric Z-disk and similar proteins. Titin is a key component in the assembly and functioning of vertebrate striated muscles. By providing connections at the level of individual microfilaments, it contributes to the fine balance of forces between the two halves of the sarcomere. The Ig superfamily (IgSF) is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. Unlike the V-set, one of the distinctive features of I-set domains is the lack of a C" strand. The structure of the titin Z1z2 lacks this strand and thus it belongs to the I-set of the IgSF. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors, the hemolymph protein hemolin, the muscle proteins titin, telokin, and twitchin, the neuronal adhesion molecule axonin-1, and the signaling molecule semaphorin 4D that is involved in axonal guidance, immune function and angiogenesis.


Pssm-ID: 409564 [Multi-domain]  Cd Length: 91  Bit Score: 48.35  E-value: 5.87e-06
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 281359561 6177 VRAGEPVNLNIPISGAPTPTIEWKRGDLKLEEGKRISYETNSERTLFRIDDSNRRDSGKYTVTAANEFGKDTADIEVIV 6255
Cdd:cd20972    13 VAEGSKVRLECRVTGNPTPVVRWFCEGKELQNSPDIQIHQEGDLHSLIIAEAFEEDTGRYSCLATNSVGSDTTSAEIFV 91
IgI_Titin_like cd05747
Immunoglobulin (Ig)-like domain of human titin C terminus and similar proteins; member of the ...
8845-8909 7.17e-06

Immunoglobulin (Ig)-like domain of human titin C terminus and similar proteins; member of the I-set of Ig superfamily (IgSF) domains; The members here are composed of the fifth immunoglobulin (Ig)-like domain from the C-terminus of human titin x and similar proteins. Titin (also called connectin) is a fibrous sarcomeric protein specifically found in vertebrate striated muscle. Titin is gigantic; depending on isoform composition it ranges from 2970 to 3700 kDa, and is of a length that spans half a sarcomere. Titin largely consists of multiple repeats of Ig-like and fibronectin type 3 (FN-III)-like domains. Titin connects the ends of myosin thick filaments to Z disks and extends along the thick filament to the H zone and appears to function similar to an elastic band, keeping the myosin filaments centered in the sarcomere during muscle contraction or stretching. This group belongs to the I-set of IgSF domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand, but lack a C" strand.


Pssm-ID: 143224 [Multi-domain]  Cd Length: 92  Bit Score: 48.12  E-value: 7.17e-06
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 281359561 8845 PTSVSVLEGEGTTFECEIDSE-LLNLVWLKDGKPIdETLPRYSFTKDGHRYSFAVAKCNMDDVGQY 8909
Cdd:cd05747    10 PRSLTVSEGESARFSCDVDGEpAPTVTWMREGQII-VSSQRHQITSTEYKSTFEISKVQMSDEGNY 74
IgI_Twitchin_like cd20949
C-terminal immunoglobulin-like domain of the myosin-associated giant protein kinase Twitchin, ...
4991-5069 7.29e-06

C-terminal immunoglobulin-like domain of the myosin-associated giant protein kinase Twitchin, and similar domains; member of the I-set IgSF domains; The members here are composed of the C-terminal immunoglobulin-like domain of the myosin-associated giant protein kinase Twitchin and similar proteins, including Caenorhabditis elegans and Aplysia californica Twitchin, Drosophila melanogaster Projectin, and similar proteins. These are very large muscle proteins containing multiple immunoglobulin (Ig)-like and fibronectin type III (FN3) domains and a single kinase domain near the C-terminus. In humans these proteins are called Titin. The Ig superfamily (IgSF) is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. The Ig-like domain of the Twitchin is a member of the I-set IgSF domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand but lack a C" strand. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors, the hemolymph protein hemolin, the muscle proteins (titin, telokin, and twitchin), the neuronal adhesion molecule axonin-1, and the signaling molecule semaphorin 4D.


Pssm-ID: 409541 [Multi-domain]  Cd Length: 89  Bit Score: 48.10  E-value: 7.29e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 4991 IKAGQSFTFDCKVSGEPAPQTKWLLKKKEVYS--KDNVKVTNVDYNtkLKVNSATRSDSGIYTVFAENANGEDSADVKVT 5068
Cdd:cd20949    11 VKEGQSATILCEVKGEPQPNVTWHFNGQPISAsvADMSKYRILADG--LLINKVTQDDTGEYTCRAYQVNSIASDMQERT 88

                  .
gi 281359561 5069 V 5069
Cdd:cd20949    89 V 89
IgI_telokin-like cd20973
immunoglobulin-like domain of telokin and similar proteins; a member of the I-set of IgSF ...
3799-3885 7.39e-06

immunoglobulin-like domain of telokin and similar proteins; a member of the I-set of IgSF domains; The members here are composed of the immunoglobulin (Ig) domain in telokin, the C-terminal domain of myosin light chain kinase which is identical to telokin, and similar proteins. The Ig superfamily (IgSF) is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. Unlike the V-set, one of the distinctive features of I-set domains is the lack of a C" strand. The structure of the telokin Ig domain lacks this strand and thus it belongs to the I-set of the IgSF. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors, the hemolymph protein hemolin, the muscle proteins titin, telokin, and twitchin, the neuronal adhesion molecule axonin-1, and the signaling molecule semaphorin 4D that is involved in axonal guidance, immune function and angiogenesis.


Pssm-ID: 409565 [Multi-domain]  Cd Length: 88  Bit Score: 47.95  E-value: 7.39e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 3799 RKNLQKKIMRSGQMLHIDALIKAEPPAKVTWTYNKTEIKTSDHIKIE-NEDYKTTFIMPKVKRADRGIYIVTAKNDSGSD 3877
Cdd:cd20973     1 IQTLRDKEVVEGSAARFDCKVEGYPDPEVKWMKDDNPIVESRRFQIDqDEDGLCSLIISDVCGDDSGKYTCKAVNSLGEA 80

                  ....*...
gi 281359561 3878 TVEVELEV 3885
Cdd:cd20973    81 TCSAELTV 88
Ig_C5_MyBP-C cd05894
C5 immunoglobulin (Ig) domain of cardiac myosin binding protein C (MyBP-C); The members here ...
5578-5660 7.51e-06

C5 immunoglobulin (Ig) domain of cardiac myosin binding protein C (MyBP-C); The members here are composed of the C5 immunoglobulin (Ig) domain of cardiac myosin binding protein C (MyBP-C). MyBP-C consists of repeated domains, Ig and fibronectin type 3, and various linkers. Three isoforms of MYBP-C exist: slow-skeletal (ssMyBP-C), fast-skeletal (fsMyBP-C), and cardiac (cMyBP-C). cMYBP-C has insertions between and inside domains and an additional cardiac-specific Ig domain at the N-terminus. For cMYBP_C an interaction has been demonstrated between this C5 domain and the Ig C8 domain.


Pssm-ID: 409475  Cd Length: 86  Bit Score: 47.91  E-value: 7.51e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 5578 NDITVHAGKRLGWTLPIEASPRPLITWLYNGKEIGSNS---RGESglFQNELTFEIVSSLRSDEGRYTLILKNEHGSFDA 5654
Cdd:cd05894     3 NTIVVVAGNKLRLDVPISGEPAPTVTWSRGDKAFTATEgrvRVES--YKDLSSFVIEGAEREDEGVYTITVTNPVGEDHA 80

                  ....*.
gi 281359561 5655 SAHATV 5660
Cdd:cd05894    81 SLFVKV 86
Ig_3 pfam13927
Immunoglobulin domain; This family contains immunoglobulin-like domains.
2901-2982 7.57e-06

Immunoglobulin domain; This family contains immunoglobulin-like domains.


Pssm-ID: 464046 [Multi-domain]  Cd Length: 78  Bit Score: 47.56  E-value: 7.57e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561  2901 KPRIdRSNLKPLLIRAGKPIRYDVNVRGEPAPVITWYQNDKELKPEelpSSSEIKNIPYNTKISIIETVRKHTGIYKIIA 2980
Cdd:pfam13927    1 KPVI-TVSPSSVTVREGETVTLTCEATGSPPPTITWYKNGEPISSG---STRSRSLSGSNSTLTISNVTRSDAGTYTCVA 76

                   ..
gi 281359561  2981 VN 2982
Cdd:pfam13927   77 SN 78
IgI_titin_I1-like cd20951
Immunoglobulin domain I1 of the titin I-band and similar proteins; a member of the I-set of ...
8312-8402 7.61e-06

Immunoglobulin domain I1 of the titin I-band and similar proteins; a member of the I-set of IgSF domains; The members here are composed of the immunoglobulin domain I1 of the titin I-band and similar proteins. Titin is a key component in the assembly and functioning of vertebrate striated muscles. By providing connections at the level of individual microfilaments, it contributes to the fine balance of forces between the two halves of the sarcomere. The Ig superfamily (IgSF) is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. The two sheets are linked together by a conserved disulfide bond between B strand and F strand. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. The Ig I1 domain of the titin I-band is a member of the I-set Ig domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand but lack a C" strand. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors, the hemolymph protein hemolin, the muscle proteins titin, telokin, and twitchin, the neuronal adhesion molecule axonin-1, and the signaling molecule semaphorin 4D that is involved in axonal guidance, immune function and angiogenesis.


Pssm-ID: 409543 [Multi-domain]  Cd Length: 94  Bit Score: 48.19  E-value: 7.61e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 8312 PRFVIRPSSQFCYEGQSVKFYCRCIAIATPTLTWSHNNIELRQSVKFMKRYVGDDYY---FIINRVKLDDRGEYIIRAEN 8388
Cdd:cd20951     1 PEFIIRLQSHTVWEKSDAKLRVEVQGKPDPEVKWYKNGVPIDPSSIPGKYKIESEYGvhvLHIRRVTVEDSAVYSAVAKN 80
                          90
                  ....*....|....
gi 281359561 8389 HYGSREEVVFLNVQ 8402
Cdd:cd20951    81 IHGEASSSASVVVE 94
Ig cd00096
Immunoglobulin domain; The members here are composed of the immunoglobulin (Ig) domain found ...
5593-5655 7.91e-06

Immunoglobulin domain; The members here are composed of the immunoglobulin (Ig) domain found in the Ig superfamily. The Ig superfamily is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. Members of this group are components of immunoglobulin, neuroglia, cell surface glycoproteins, including T-cell receptors, CD2, CD4, CD8, and membrane glycoproteins, including butyrophilin and chondroitin sulfate proteoglycan core protein. A predominant feature of most Ig domains is a disulfide bridge connecting the two beta-sheets with a tryptophan residue packed against the disulfide bond. Ig superfamily (IgSF) domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. Typically, the V-set domains have A, B, E, and D strands in one sheet and A', G, F, C, C' and C" in the other. The structures in C1-set are smaller than those in the V-set; they have one beta sheet that is formed by strands A, B, E, and D and the other by strands G, F, C, and C'. Moreover, a C1-set Ig domain contains a short C' strand (three residues) and lacks A' and C" strand. Unlike other Ig domain sets, C2-set structures do not have a D strand. Like the V-set Ig domains, members of the I-set have a discontinuous A strand, but lack a C" strand.


Pssm-ID: 409353 [Multi-domain]  Cd Length: 70  Bit Score: 47.32  E-value: 7.91e-06
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 281359561 5593 PIEASPRPLITWLYNGKEIGSNSRGESGLFQNELTFEIVSSLRSDEGRYTLILKNEHGSFDAS 5655
Cdd:cd00096     6 SASGNPPPTITWYKNGKPLPPSSRDSRRSELGNGTLTISNVTLEDSGTYTCVASNSAGGSASA 68
IG_like smart00410
Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.
6568-6650 7.98e-06

Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.


Pssm-ID: 214653 [Multi-domain]  Cd Length: 85  Bit Score: 47.89  E-value: 7.98e-06
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561   6568 RDIVCRAGDDFSIHVPYLAFPKPNAFWYSND-NMLDDNNRVHKHLTDDAASVVVKNSKRADSGQYRLQLKNTSGFDTATI 6646
Cdd:smart00410    2 PSVTVKEGESVTLSCEASGSPPPEVTWYKQGgKLLAESGRFSVSRSGSTSTLTISNVTPEDSGTYTCAATNSSGSASSGT 81

                    ....
gi 281359561   6647 NVRV 6650
Cdd:smart00410   82 TLTV 85
ig pfam00047
Immunoglobulin domain; Members of the immunoglobulin superfamily are found in hundreds of ...
132-210 8.09e-06

Immunoglobulin domain; Members of the immunoglobulin superfamily are found in hundreds of proteins of different functions. Examples include antibodies, the giant muscle kinase titin and receptor tyrosine kinases. Immunoglobulin-like domains may be involved in protein-protein and protein-ligand interactions.


Pssm-ID: 395002  Cd Length: 86  Bit Score: 47.57  E-value: 8.09e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561   132 DGKRLLFECRVN-ADPIPAIIWFHNGAAVKESERHKITVDKDVHSyfaTLEILNVTVEDAGKYKVNAKNELGESNATISL 210
Cdd:pfam00047   10 EGDSATLTCSAStGSPGPDVTWSKEGGTLIESLKVKHDNGRTTQS---SLLISNVTKEDAGTYTCVVNNPGGSATLSTSL 86
IgI_Titin_like cd05747
Immunoglobulin (Ig)-like domain of human titin C terminus and similar proteins; member of the ...
4095-4177 8.22e-06

Immunoglobulin (Ig)-like domain of human titin C terminus and similar proteins; member of the I-set of Ig superfamily (IgSF) domains; The members here are composed of the fifth immunoglobulin (Ig)-like domain from the C-terminus of human titin x and similar proteins. Titin (also called connectin) is a fibrous sarcomeric protein specifically found in vertebrate striated muscle. Titin is gigantic; depending on isoform composition it ranges from 2970 to 3700 kDa, and is of a length that spans half a sarcomere. Titin largely consists of multiple repeats of Ig-like and fibronectin type 3 (FN-III)-like domains. Titin connects the ends of myosin thick filaments to Z disks and extends along the thick filament to the H zone and appears to function similar to an elastic band, keeping the myosin filaments centered in the sarcomere during muscle contraction or stretching. This group belongs to the I-set of IgSF domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand, but lack a C" strand.


Pssm-ID: 143224 [Multi-domain]  Cd Length: 92  Bit Score: 48.12  E-value: 8.22e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 4095 TNIKDITIKAGQHIRFDIKVSGEPPATKVWLHnKARLENDDSNYNIDMESYRTKLTVPISKRFHSGKYTLKAENESGRDE 4174
Cdd:cd05747     8 TKPRSLTVSEGESARFSCDVDGEPAPTVTWMR-EGQIIVSSQRHQITSTEYKSTFEISKVQMSDEGNYTVVVENSEGKQE 86

                  ...
gi 281359561 4175 ASF 4177
Cdd:cd05747    87 AQF 89
Ig5_Contactin cd04969
Fifth immunoglobulin (Ig) domain of contactin; The members here are composed of the fifth ...
7669-7737 8.71e-06

Fifth immunoglobulin (Ig) domain of contactin; The members here are composed of the fifth immunoglobulin (Ig) domain of contactins. Contactins are neural cell adhesion molecules and are comprised of six Ig domains followed by four fibronectin type III (FnIII) domains anchored to the membrane by glycosylphosphatidylinositol. The first four Ig domains form the intermolecular binding fragment, which arranges as a compact U-shaped module via contacts between Ig domains 1 and 4, and between Ig domains 2 and 3. Contactin-2 (TAG-1, axonin-1) may play a part in the neuronal processes of neurite outgrowth, axon guidance and fasciculation, and neuronal migration. This group also includes contactin-1 and contactin-5. The different contactins show different expression patterns in the central nervous system. During development and in adulthood, contactin-2 is transiently expressed in subsets of central and peripheral neurons. Contactin-5 is expressed specifically in the rat postnatal nervous system, peaking at about 3 weeks postnatal, and a lack of contactin-5 (NB-2) results in an impairment of neuronal activity in the rat auditory system. Contactin-5 is highly expressed in the adult human brain in the occipital lobe and in the amygdala. Contactin-1 is differentially expressed in tumor tissues and may, through a RhoA mechanism, facilitate invasion and metastasis of human lung adenocarcinoma.


Pssm-ID: 409358 [Multi-domain]  Cd Length: 89  Bit Score: 47.84  E-value: 8.71e-06
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 281359561 7669 CTINGVPKPTISWYKGAREISNGARYHMYSEGDnhfLNINDVFGEDADEYVCRAVNKAGAKSTRATLAI 7737
Cdd:cd04969    24 CKPKASPKPTISWSKGTELLTNSSRICILPDGS---LKIKNVTKSDEGKYTCFAVNFFGKANSTGSLSV 89
IgI_4_Robo cd05726
Fourth immunoglobulin (Ig)-like domain in Robo (roundabout) receptors; member of the I-set of ...
7650-7737 9.55e-06

Fourth immunoglobulin (Ig)-like domain in Robo (roundabout) receptors; member of the I-set of Ig superfamily (IgSF) domains; Members here are composed the fourth immunoglobulin (Ig)-like domain in Robo (roundabout) receptors. Robo receptors play a role in the development of the central nervous system (CNS), and are receptors of Slit protein. Slit is a repellant secreted by the neural cells in the midline. Slit acts through Robo to prevent most neurons from crossing the midline from either side. Three mammalian Robo homologs (Robo1, Robo2, Robo3), and three mammalian Slit homologs (Slit-1, Slit-2, Slit-3), have been identified. Commissural axons, which cross the midline, express low levels of Robo; longitudinal axons, which avoid the midline, express high levels of Robo. Robo1, Robo2, and Robo3 are expressed by commissural neurons in the vertebrate spinal cord and Slit-1, Slit-2, and Slit-3 are expressed at the ventral midline. Robo-3 is a divergent member of the Robo family which instead of being a positive regulator of Slit responsiveness, antagonizes Slit responsiveness in precrossing axons. The Slit-Robo interaction is mediated by the second leucine-rich repeat (LRR) domain of Slit and the two N-terminal Ig domains of Robo, Ig1 and Ig2. The primary Robo binding site for Slit2 has been shown by surface plasmon resonance experiments and mutational analysis to be the Ig1 domain, while the Ig2 domain has been proposed to harbor a weak secondary binding site. This group belongs to the I-set of IgSF domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand, but lack a C" strand.


Pssm-ID: 409391 [Multi-domain]  Cd Length: 98  Bit Score: 48.03  E-value: 9.55e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 7650 IVKPlRDANCIQNHNAQFTCTINGVPKPTISWYK-GAREI-------SNGARYHMYSEGDnhfLNINDVFGEDADEYVCR 7721
Cdd:cd05726     3 VVKP-RDQVVALGRTVTFQCETKGNPQPAIFWQKeGSQNLlfpyqppQPSSRFSVSPTGD---LTITNVQRSDVGYYICQ 78
                          90
                  ....*....|....*.
gi 281359561 7722 AVNKAGAKSTRATLAI 7737
Cdd:cd05726    79 ALNVAGSILAKAQLEV 94
IgI_2_Titin_Z1z2-like cd20972
Second Ig-like domain of the giant muscle protein titin Z1z2 in the sarcomeric Z-disk, and ...
335-417 9.95e-06

Second Ig-like domain of the giant muscle protein titin Z1z2 in the sarcomeric Z-disk, and similar domains; a member of the I-set of IgSF domains; The members here are composed of the second immunoglobulin (Ig)-like domain of the giant muscle protein titin Z1z2 in the sarcomeric Z-disk and similar proteins. Titin is a key component in the assembly and functioning of vertebrate striated muscles. By providing connections at the level of individual microfilaments, it contributes to the fine balance of forces between the two halves of the sarcomere. The Ig superfamily (IgSF) is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. Unlike the V-set, one of the distinctive features of I-set domains is the lack of a C" strand. The structure of the titin Z1z2 lacks this strand and thus it belongs to the I-set of the IgSF. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors, the hemolymph protein hemolin, the muscle proteins titin, telokin, and twitchin, the neuronal adhesion molecule axonin-1, and the signaling molecule semaphorin 4D that is involved in axonal guidance, immune function and angiogenesis.


Pssm-ID: 409564 [Multi-domain]  Cd Length: 91  Bit Score: 47.58  E-value: 9.95e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561  335 PRFPKKP---TIRQEEDLLiMECVLEAHPVPDIVWYCSEKEICNNQRTKmtrkaITKDSYILTLEIQNPTKEDGGNYRCN 411
Cdd:cd20972     2 PQFIQKLrsqEVAEGSKVR-LECRVTGNPTPVVRWFCEGKELQNSPDIQ-----IHQEGDLHSLIIAEAFEEDTGRYSCL 75

                  ....*.
gi 281359561  412 AINMYG 417
Cdd:cd20972    76 ATNSVG 81
IgI_4_hemolin-like cd20978
Fourth immunoglobulin (Ig)-like domain of hemolin, and similar domains; a member of the I-set ...
5276-5366 1.00e-05

Fourth immunoglobulin (Ig)-like domain of hemolin, and similar domains; a member of the I-set of IgSF domains; The members here are composed of the fourth immunoglobulin (Ig)-like domain of hemolin and similar proteins. Hemolin, an insect immunoglobulin superfamily (IgSF) member containing four Ig-like domains, is a lipopolysaccharide-binding immune protein induced during bacterial infection. Hemolin shares significant sequence similarity with the first four Ig-like domains of the transmembrane cell adhesion molecules (CAMs) of the L1 family. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. The fourth Ig-like domain of hemolin is a member of the I-set Ig domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set domains, members of the I-set have a discontinuous A strand but lack a C" strand. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors, the muscle proteins titin, telokin, and twitchin, the neuronal adhesion molecule axonin-1, and the signaling molecule semaphorin 4D that is involved in axonal guidance, immune function and angiogenesis.


Pssm-ID: 409570 [Multi-domain]  Cd Length: 88  Bit Score: 47.39  E-value: 1.00e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 5276 PKIDRNFMSDIKIKAGNVFEFDVPVTGEPLPSKDWTHEGNMIinTDRVKISNFDDRTkIRILDAKRSDTGVYTLTARNIN 5355
Cdd:cd20978     1 PKFIQKPEKNVVVKGGQDVTLPCQVTGVPQPKITWLHNGKPL--QGPMERATVEDGT-LTIINVQPEDTGYYGCVATNEI 77
                          90
                  ....*....|.
gi 281359561 5356 GTDRHNVKVTI 5366
Cdd:cd20978    78 GDIYTETLLHV 88
COG4733 COG4733
Phage-related protein, tail protein J [Mobilome: prophages, transposons];
2165-2342 1.00e-05

Phage-related protein, tail protein J [Mobilome: prophages, transposons];


Pssm-ID: 443767 [Multi-domain]  Cd Length: 978  Bit Score: 53.03  E-value: 1.00e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 2165 DLIPKKQYRFRIRAVNAIGQSDPATFKNTILAKDPWDEPGKPKAVDLTDwDKDHADLKWEAPEtdgGDPITAYIVEYKEk 2244
Cdd:COG4733   592 PGIYAGDYEVRVRAINALGVSSAWAASSETTVTGKTAPPPAPTGLTATG-GLGGITLSWSFPV---DADTLRTEIRYST- 666
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 2245 fSNDWVSGK--EVDGDARTATVDGLKEGQQYEFRVRAVNRAG-------PGEPSDKTKSIIAkcrfvkpFIVGEGLKNVT 2315
Cdd:COG4733   667 -TGDWASATvaQALYPGNTYTLAGLKAGQTYYYRARAVDRSGnvsawwvSGQASADAAGILD-------AITGQILETEL 738
                         170       180
                  ....*....|....*....|....*..
gi 281359561 2316 VKKGQTIRFDIKYDGEPEPAATWVKGT 2342
Cdd:COG4733   739 GQELDAIIQNATVAEVVAATVTDVTAQ 765
IgI_titin_I1-like cd20951
Immunoglobulin domain I1 of the titin I-band and similar proteins; a member of the I-set of ...
119-211 1.09e-05

Immunoglobulin domain I1 of the titin I-band and similar proteins; a member of the I-set of IgSF domains; The members here are composed of the immunoglobulin domain I1 of the titin I-band and similar proteins. Titin is a key component in the assembly and functioning of vertebrate striated muscles. By providing connections at the level of individual microfilaments, it contributes to the fine balance of forces between the two halves of the sarcomere. The Ig superfamily (IgSF) is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. The two sheets are linked together by a conserved disulfide bond between B strand and F strand. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. The Ig I1 domain of the titin I-band is a member of the I-set Ig domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand but lack a C" strand. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors, the hemolymph protein hemolin, the muscle proteins titin, telokin, and twitchin, the neuronal adhesion molecule axonin-1, and the signaling molecule semaphorin 4D that is involved in axonal guidance, immune function and angiogenesis.


Pssm-ID: 409543 [Multi-domain]  Cd Length: 94  Bit Score: 47.80  E-value: 1.09e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561  119 PTFAKKPAIRQEEDGKRLLFECRVNADPIPAIIWFHNGAAVkesERHKITVDKDVHS--YFATLEILNVTVEDAGKYKVN 196
Cdd:cd20951     1 PEFIIRLQSHTVWEKSDAKLRVEVQGKPDPEVKWYKNGVPI---DPSSIPGKYKIESeyGVHVLHIRRVTVEDSAVYSAV 77
                          90
                  ....*....|....*
gi 281359561  197 AKNELGESNATISLN 211
Cdd:cd20951    78 AKNIHGEASSSASVV 92
IgI_titin_I1-like cd20951
Immunoglobulin domain I1 of the titin I-band and similar proteins; a member of the I-set of ...
1497-1588 1.16e-05

Immunoglobulin domain I1 of the titin I-band and similar proteins; a member of the I-set of IgSF domains; The members here are composed of the immunoglobulin domain I1 of the titin I-band and similar proteins. Titin is a key component in the assembly and functioning of vertebrate striated muscles. By providing connections at the level of individual microfilaments, it contributes to the fine balance of forces between the two halves of the sarcomere. The Ig superfamily (IgSF) is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. The two sheets are linked together by a conserved disulfide bond between B strand and F strand. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. The Ig I1 domain of the titin I-band is a member of the I-set Ig domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand but lack a C" strand. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors, the hemolymph protein hemolin, the muscle proteins titin, telokin, and twitchin, the neuronal adhesion molecule axonin-1, and the signaling molecule semaphorin 4D that is involved in axonal guidance, immune function and angiogenesis.


Pssm-ID: 409543 [Multi-domain]  Cd Length: 94  Bit Score: 47.42  E-value: 1.16e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 1497 PSIVDVQESYSVVEDSTAYLTVGVEGSPAPTFKFYKG---VSEILEGGRFKFLTDGqtNTITLCMRKCKPNDESKYKIVV 1573
Cdd:cd20951     1 PEFIIRLQSHTVWEKSDAKLRVEVQGKPDPEVKWYKNgvpIDPSSIPGKYKIESEY--GVHVLHIRRVTVEDSAVYSAVA 78
                          90
                  ....*....|....*
gi 281359561 1574 SNIHGEDSAEMQLYV 1588
Cdd:cd20951    79 KNIHGEASSSASVVV 93
COG4733 COG4733
Phage-related protein, tail protein J [Mobilome: prophages, transposons];
3341-3479 1.17e-05

Phage-related protein, tail protein J [Mobilome: prophages, transposons];


Pssm-ID: 443767 [Multi-domain]  Cd Length: 978  Bit Score: 53.03  E-value: 1.17e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 3341 GKWVPAGSVDPEkyDIEIKGLdPNHRYQFRVKAVNEEGESEPLETESAITAKnpFDVSAPPGLPELE----DWdehHVKL 3416
Cdd:COG4733   576 GNWVSVPRTSGT--SFEVPGI-YAGDYEVRVRAINALGVSSAWAASSETTVT--GKTAPPPAPTGLTatggLG---GITL 647
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 281359561 3417 KWEPPIrdgGSPITNYIIEVMDKDSGEFVKAVETDSPVCKGVVKKLEEGQQYKFRVRAVNKAG 3479
Cdd:COG4733   648 SWSFPV---DADTLRTEIRYSTTGDWASATVAQALYPGNTYTLAGLKAGQTYYYRARAVDRSG 707
IG_like smart00410
Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.
1838-1897 1.18e-05

Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.


Pssm-ID: 214653 [Multi-domain]  Cd Length: 85  Bit Score: 47.11  E-value: 1.18e-05
                            10        20        30        40        50        60
                    ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 281359561   1838 EKDTVTLACEI-DDAMGEVQWLRNG-EEIKPDKRIQIVKDGRKRKLVIKDCKVTDAGQFKCT 1897
Cdd:smart00410    8 EGESVTLSCEAsGSPPPEVTWYKQGgKLLAESGRFSVSRSGSTSTLTISNVTPEDSGTYTCA 69
IgI_telokin-like cd20973
immunoglobulin-like domain of telokin and similar proteins; a member of the I-set of IgSF ...
4689-4766 1.18e-05

immunoglobulin-like domain of telokin and similar proteins; a member of the I-set of IgSF domains; The members here are composed of the immunoglobulin (Ig) domain in telokin, the C-terminal domain of myosin light chain kinase which is identical to telokin, and similar proteins. The Ig superfamily (IgSF) is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. Unlike the V-set, one of the distinctive features of I-set domains is the lack of a C" strand. The structure of the telokin Ig domain lacks this strand and thus it belongs to the I-set of the IgSF. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors, the hemolymph protein hemolin, the muscle proteins titin, telokin, and twitchin, the neuronal adhesion molecule axonin-1, and the signaling molecule semaphorin 4D that is involved in axonal guidance, immune function and angiogenesis.


Pssm-ID: 409565 [Multi-domain]  Cd Length: 88  Bit Score: 47.18  E-value: 1.18e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 281359561 4689 RRNLRNITLSSGTALKLDANITGEPAPKVEWKLSNYHLQSGKNVTIE-TPDYYTKLVIRPTQRSDSGEYLVTATNTSGK 4766
Cdd:cd20973     1 IQTLRDKEVVEGSAARFDCKVEGYPDPEVKWMKDDNPIVESRRFQIDqDEDGLCSLIISDVCGDDSGKYTCKAVNSLGE 79
IgI_8_hMLCK_like cd05762
Eighth immunoglobulin (Ig)-like domain of human myosin light-chain kinase (MLCK) and similar ...
7746-7840 1.23e-05

Eighth immunoglobulin (Ig)-like domain of human myosin light-chain kinase (MLCK) and similar protein; member of the I-set of IgSF domains; The members here are composed of the eighth immunoglobulin (Ig)-like domain of human myosin light-chain kinase (MLCK) and similar proteins. Myosin light-chain kinase (MLCK) is a key regulator of different forms of cell motility involving actin and myosin II. Agonist stimulation of smooth muscle cells increases cytosolic Ca2+ which binds calmodulin. This Ca2+-calmodulin complex in turn binds to and activates MLCK. Activated MLCK leads to the phosphorylation of the 20 kDa myosin regulatory light chain (RLC) of myosin II and the stimulation of actin-activated myosin MgATPase activity. MLCK is widely present in vertebrate tissues; it phosphorylates the 20 kDa RLC of both smooth and nonmuscle myosin II. Phosphorylation leads to the activation of the myosin motor domain and altered structural properties of myosin II. In smooth muscle MLCK it is involved in initiating contraction. In nonmuscle cells, MLCK may participate in cell division and cell motility; it has been suggested MLCK plays a role in cardiomyocyte differentiation and contraction through regulation of nonmuscle myosin II.


Pssm-ID: 409419  Cd Length: 99  Bit Score: 47.64  E-value: 1.23e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 7746 PPR---FRDTAYFDKGENVVIKIPFTGFPKPRIHWVRDGENIESGGHYTVEVKERHAVLIIRDGSHLDSGPYRITAENEL 7822
Cdd:cd05762     1 PPQiiqFPEDMKVRAGESVELFCKVTGTQPITCTWMKFRKQIQEGEGIKIENTENSSKLTITEGQQEHCGCYTLEVENKL 80
                          90
                  ....*....|....*...
gi 281359561 7823 GSDTAIIQVQISDRPDPP 7840
Cdd:cd05762    81 GSRQAQVNLTVVDKPDPP 98
Ig_3 pfam13927
Immunoglobulin domain; This family contains immunoglobulin-like domains.
1496-1575 1.26e-05

Immunoglobulin domain; This family contains immunoglobulin-like domains.


Pssm-ID: 464046 [Multi-domain]  Cd Length: 78  Bit Score: 46.79  E-value: 1.26e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561  1496 PPSIVDVQESYSVVEDSTAYLTVGVEGSPAPTFKFYKGVSEILEGGRFKFLTDGQTNTITLcmRKCKPNDESKYKIVVSN 1575
Cdd:pfam13927    1 KPVITVSPSSVTVREGETVTLTCEATGSPPPTITWYKNGEPISSGSTRSRSLSGSNSTLTI--SNVTRSDAGTYTCVASN 78
IgI_2_Titin_Z1z2-like cd20972
Second Ig-like domain of the giant muscle protein titin Z1z2 in the sarcomeric Z-disk, and ...
1824-1909 1.32e-05

Second Ig-like domain of the giant muscle protein titin Z1z2 in the sarcomeric Z-disk, and similar domains; a member of the I-set of IgSF domains; The members here are composed of the second immunoglobulin (Ig)-like domain of the giant muscle protein titin Z1z2 in the sarcomeric Z-disk and similar proteins. Titin is a key component in the assembly and functioning of vertebrate striated muscles. By providing connections at the level of individual microfilaments, it contributes to the fine balance of forces between the two halves of the sarcomere. The Ig superfamily (IgSF) is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. Unlike the V-set, one of the distinctive features of I-set domains is the lack of a C" strand. The structure of the titin Z1z2 lacks this strand and thus it belongs to the I-set of the IgSF. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors, the hemolymph protein hemolin, the muscle proteins titin, telokin, and twitchin, the neuronal adhesion molecule axonin-1, and the signaling molecule semaphorin 4D that is involved in axonal guidance, immune function and angiogenesis.


Pssm-ID: 409564 [Multi-domain]  Cd Length: 91  Bit Score: 47.19  E-value: 1.32e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 1824 PYKFVKVLKSQQCIEKDTVTLACEID-DAMGEVQWLRNGEEIKPDKRIQIVKDGRKRKLVIKDCKVTDAGQFKC-TTNA- 1900
Cdd:cd20972     1 PPQFIQKLRSQEVAEGSKVRLECRVTgNPTPVVRWFCEGKELQNSPDIQIHQEGDLHSLIIAEAFEEDTGRYSClATNSv 80
                          90
                  ....*....|.
gi 281359561 1901 --DTTESEIII 1909
Cdd:cd20972    81 gsDTTSAEIFV 91
IgI_M-protein_C cd05891
C-terminal immunoglobulin (Ig)-like domain of M-protein; member of the I-set of Ig superfamily ...
241-312 1.34e-05

C-terminal immunoglobulin (Ig)-like domain of M-protein; member of the I-set of Ig superfamily (IgSF) domains; The members here are composed of the C-terminal immunoglobulin (Ig)-like domain of M-protein (also known as myomesin-2). M-protein is a structural protein localized to the M-band, a transverse structure in the center of the sarcomere, and is a candidate for M-band bridges. M-protein is modular consisting mainly of repetitive IG-like and fibronectin type III (FnIII) domains and has a muscle-type specific expression pattern. M-protein is present in fast fibers.


Pssm-ID: 143299  Cd Length: 92  Bit Score: 47.21  E-value: 1.34e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 281359561  241 DGGNVTFECRCVGDPTPTVTWSHGETELNESNRYKMSLtmDQKLYhiACLEISSVVSSDQGEYRAQAKNKHG 312
Cdd:cd05891    15 EGKTLNLTCTVFGNPDPEVIWFKNDQDIELSEHYSVKL--EQGKY--ASLTIKGVTSEDSGKYSINVKNKYG 82
Ig_Titin_like cd05748
Immunoglobulin (Ig)-like domain of titin and similar proteins; The members here are composed ...
2020-2095 1.34e-05

Immunoglobulin (Ig)-like domain of titin and similar proteins; The members here are composed of the immunoglobulin (Ig)-like domain found in titin-like proteins and similar proteins. Titin (also called connectin) is a fibrous sarcomeric protein specifically found in vertebrate striated muscle. Titin is a giant protein; depending on isoform composition, it ranges from 2970 to 3700 kDa, and is of a length that spans half a sarcomere. Titin largely consists of multiple repeats of Ig-like and fibronectin type 3 (FN-III)-like domains. Titin connects the ends of myosin thick filaments to Z disks and extends along the thick filament to the H zone. It appears to function similarly to an elastic band, keeping the myosin filaments centered in the sarcomere during muscle contraction or stretching. Within the sarcomere, titin is also attached to or is associated with myosin binding protein C (MyBP-C). MyBP-C appears to contribute to the generation of passive tension by titin and like titin has repeated Ig-like and FN-III domains. Also included in this group are worm twitchin and insect projectin, thick filament proteins of invertebrate muscle which also have repeated Ig-like and FN-III domains.


Pssm-ID: 409406 [Multi-domain]  Cd Length: 82  Bit Score: 46.81  E-value: 1.34e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 281359561 2020 PVLLEVPFKvsGtKQTPvEAKLFKDGKPLPVKD-VEVAVTDDKVTFKIKKPSRDLSGPYQIKISNGQGEDTKDVQII 2095
Cdd:cd05748     9 SLRLDIPIK--G-RPTP-TVTWSKDGQPLKETGrVQIETTASSTSLVIKNAKRSDSGKYTLTLKNSAGEKSATINVK 81
IgI_4_MYLK-like cd20976
Fourth Ig-like domain from smooth muscle myosin light chain kinase and similar domains ; a ...
437-532 1.38e-05

Fourth Ig-like domain from smooth muscle myosin light chain kinase and similar domains ; a member of the I-set of IgSF domains; The members here are composed of the fourth immunoglobulin (Ig)-like domain from smooth muscle myosin light chain kinase (MYLK) and similar domains. The Ig superfamily (IgSF) is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. Unlike the V-set, one of the distinctive features of I-set domains is the lack of a C" strand. The structure of this group shows that the fourth Ig-like domain from myosin light chain kinase lacks this strand and thus belongs to the I-set of the IgSF. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors, the hemolymph protein hemolin, the muscle proteins titin, telokin, and twitchin, the neuronal adhesion molecule axonin-1, and the signaling molecule semaphorin 4D that is involved in axonal guidance, immune function and angiogenesis.


Pssm-ID: 409568 [Multi-domain]  Cd Length: 90  Bit Score: 47.24  E-value: 1.38e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561  437 APSFIEKPRIIPNESGTLITMKCKCKAKPEPTVTWYR-GQDLVEKSKKIKINTTViAEdtyeltLEIKDPGATDGGTYRC 515
Cdd:cd20976     1 APSFSSVPKDLEAVEGQDFVAQCSARGKPVPRITWIRnAQPLQYAADRSTCEAGV-GE------LHIQDVLPEDHGTYTC 73
                          90
                  ....*....|....*..
gi 281359561  516 NVKNEYGESNANLNLNI 532
Cdd:cd20976    74 LAKNAAGQVSCSAWVTV 90
Ig cd00096
Immunoglobulin domain; The members here are composed of the immunoglobulin (Ig) domain found ...
3220-3282 1.38e-05

Immunoglobulin domain; The members here are composed of the immunoglobulin (Ig) domain found in the Ig superfamily. The Ig superfamily is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. Members of this group are components of immunoglobulin, neuroglia, cell surface glycoproteins, including T-cell receptors, CD2, CD4, CD8, and membrane glycoproteins, including butyrophilin and chondroitin sulfate proteoglycan core protein. A predominant feature of most Ig domains is a disulfide bridge connecting the two beta-sheets with a tryptophan residue packed against the disulfide bond. Ig superfamily (IgSF) domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. Typically, the V-set domains have A, B, E, and D strands in one sheet and A', G, F, C, C' and C" in the other. The structures in C1-set are smaller than those in the V-set; they have one beta sheet that is formed by strands A, B, E, and D and the other by strands G, F, C, and C'. Moreover, a C1-set Ig domain contains a short C' strand (three residues) and lacks A' and C" strand. Unlike other Ig domain sets, C2-set structures do not have a D strand. Like the V-set Ig domains, members of the I-set have a discontinuous A strand, but lack a C" strand.


Pssm-ID: 409353 [Multi-domain]  Cd Length: 70  Bit Score: 46.55  E-value: 1.38e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 281359561 3220 VKFDVDVKGEPAPSLTWFLKETELTSTGQVRLENIDYNTKLTLLDTDRKQSGQYKLRAENING 3282
Cdd:cd00096     1 VTLTCSASGNPPPTITWYKNGKPLPPSSRDSRRSELGNGTLTISNVTLEDSGTYTCVASNSAG 63
ig pfam00047
Immunoglobulin domain; Members of the immunoglobulin superfamily are found in hundreds of ...
7264-7339 1.41e-05

Immunoglobulin domain; Members of the immunoglobulin superfamily are found in hundreds of proteins of different functions. Examples include antibodies, the giant muscle kinase titin and receptor tyrosine kinases. Immunoglobulin-like domains may be involved in protein-protein and protein-ligand interactions.


Pssm-ID: 395002  Cd Length: 86  Bit Score: 47.19  E-value: 1.41e-05
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 281359561  7264 VAPFGKDYTLQCAAS-GKPSPTARWLRNGKEIQMNGGRMTCDSKDGVFRLHISNVQTGDDGDYTCEAMNSLGFVNTS 7339
Cdd:pfam00047    7 TVLEGDSATLTCSAStGSPGPDVTWSKEGGTLIESLKVKHDNGRTTQSSLLISNVTKEDAGTYTCVVNNPGGSATLS 83
IgI_telokin-like cd20973
immunoglobulin-like domain of telokin and similar proteins; a member of the I-set of IgSF ...
3506-3590 1.42e-05

immunoglobulin-like domain of telokin and similar proteins; a member of the I-set of IgSF domains; The members here are composed of the immunoglobulin (Ig) domain in telokin, the C-terminal domain of myosin light chain kinase which is identical to telokin, and similar proteins. The Ig superfamily (IgSF) is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. Unlike the V-set, one of the distinctive features of I-set domains is the lack of a C" strand. The structure of the telokin Ig domain lacks this strand and thus it belongs to the I-set of the IgSF. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors, the hemolymph protein hemolin, the muscle proteins titin, telokin, and twitchin, the neuronal adhesion molecule axonin-1, and the signaling molecule semaphorin 4D that is involved in axonal guidance, immune function and angiogenesis.


Pssm-ID: 409565 [Multi-domain]  Cd Length: 88  Bit Score: 47.18  E-value: 1.42e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 3506 LKPVIVKTGLSISLDINIRGEPAPKVEWFFNNSSVTSDEHsVKID-NVDYNTKFFVMRAQRSQSGKYIIKATNEVGEDEA 3584
Cdd:cd20973     4 LRDKEVVEGSAARFDCKVEGYPDPEVKWMKDDNPIVESRR-FQIDqDEDGLCSLIISDVCGDDSGKYTCKAVNSLGEATC 82

                  ....*.
gi 281359561 3585 ELEVTV 3590
Cdd:cd20973    83 SAELTV 88
IG_like smart00410
Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.
3210-3292 1.55e-05

Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.


Pssm-ID: 214653 [Multi-domain]  Cd Length: 85  Bit Score: 46.73  E-value: 1.55e-05
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561   3210 KPIKVRAGQPVKFDVDVKGEPAPSLTWFL-KETELTSTGQVRLENIDYNTKLTLLDTDRKQSGQYKLRAENINGVDEAVV 3288
Cdd:smart00410    2 PSVTVKEGESVTLSCEASGSPPPEVTWYKqGGKLLAESGRFSVSRSGSTSTLTISNVTPEDSGTYTCAATNSSGSASSGT 81

                    ....
gi 281359561   3289 EVII 3292
Cdd:smart00410   82 TLTV 85
IgI_4_hemolin-like cd20978
Fourth immunoglobulin (Ig)-like domain of hemolin, and similar domains; a member of the I-set ...
438-529 1.55e-05

Fourth immunoglobulin (Ig)-like domain of hemolin, and similar domains; a member of the I-set of IgSF domains; The members here are composed of the fourth immunoglobulin (Ig)-like domain of hemolin and similar proteins. Hemolin, an insect immunoglobulin superfamily (IgSF) member containing four Ig-like domains, is a lipopolysaccharide-binding immune protein induced during bacterial infection. Hemolin shares significant sequence similarity with the first four Ig-like domains of the transmembrane cell adhesion molecules (CAMs) of the L1 family. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. The fourth Ig-like domain of hemolin is a member of the I-set Ig domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set domains, members of the I-set have a discontinuous A strand but lack a C" strand. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors, the muscle proteins titin, telokin, and twitchin, the neuronal adhesion molecule axonin-1, and the signaling molecule semaphorin 4D that is involved in axonal guidance, immune function and angiogenesis.


Pssm-ID: 409570 [Multi-domain]  Cd Length: 88  Bit Score: 47.00  E-value: 1.55e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561  438 PSFIEKPRI-IPNESGTLITMKCKCKAKPEPTVTW-YRGQDLVEKSKKIKINttviaedtyELTLEIKDPGATDGGTYRC 515
Cdd:cd20978     1 PKFIQKPEKnVVVKGGQDVTLPCQVTGVPQPKITWlHNGKPLQGPMERATVE---------DGTLTIINVQPEDTGYYGC 71
                          90
                  ....*....|....*.
gi 281359561  516 NVKNEYGE--SNANLN 529
Cdd:cd20978    72 VATNEIGDiyTETLLH 87
IgI_4_MYLK-like cd20976
Fourth Ig-like domain from smooth muscle myosin light chain kinase and similar domains ; a ...
7757-7833 1.55e-05

Fourth Ig-like domain from smooth muscle myosin light chain kinase and similar domains ; a member of the I-set of IgSF domains; The members here are composed of the fourth immunoglobulin (Ig)-like domain from smooth muscle myosin light chain kinase (MYLK) and similar domains. The Ig superfamily (IgSF) is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. Unlike the V-set, one of the distinctive features of I-set domains is the lack of a C" strand. The structure of this group shows that the fourth Ig-like domain from myosin light chain kinase lacks this strand and thus belongs to the I-set of the IgSF. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors, the hemolymph protein hemolin, the muscle proteins titin, telokin, and twitchin, the neuronal adhesion molecule axonin-1, and the signaling molecule semaphorin 4D that is involved in axonal guidance, immune function and angiogenesis.


Pssm-ID: 409568 [Multi-domain]  Cd Length: 90  Bit Score: 47.24  E-value: 1.55e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 281359561 7757 KGENVVIKIPFTGFPKPRIHWVRDGENIE-SGGHYTVEVKErhAVLIIRDGSHLDSGPYRITAENELGSDTAIIQVQI 7833
Cdd:cd20976    15 EGQDFVAQCSARGKPVPRITWIRNAQPLQyAADRSTCEAGV--GELHIQDVLPEDHGTYTCLAKNAAGQVSCSAWVTV 90
Ig5_Contactin cd04969
Fifth immunoglobulin (Ig) domain of contactin; The members here are composed of the fifth ...
8632-8711 1.56e-05

Fifth immunoglobulin (Ig) domain of contactin; The members here are composed of the fifth immunoglobulin (Ig) domain of contactins. Contactins are neural cell adhesion molecules and are comprised of six Ig domains followed by four fibronectin type III (FnIII) domains anchored to the membrane by glycosylphosphatidylinositol. The first four Ig domains form the intermolecular binding fragment, which arranges as a compact U-shaped module via contacts between Ig domains 1 and 4, and between Ig domains 2 and 3. Contactin-2 (TAG-1, axonin-1) may play a part in the neuronal processes of neurite outgrowth, axon guidance and fasciculation, and neuronal migration. This group also includes contactin-1 and contactin-5. The different contactins show different expression patterns in the central nervous system. During development and in adulthood, contactin-2 is transiently expressed in subsets of central and peripheral neurons. Contactin-5 is expressed specifically in the rat postnatal nervous system, peaking at about 3 weeks postnatal, and a lack of contactin-5 (NB-2) results in an impairment of neuronal activity in the rat auditory system. Contactin-5 is highly expressed in the adult human brain in the occipital lobe and in the amygdala. Contactin-1 is differentially expressed in tumor tissues and may, through a RhoA mechanism, facilitate invasion and metastasis of human lung adenocarcinoma.


Pssm-ID: 409358 [Multi-domain]  Cd Length: 89  Bit Score: 47.07  E-value: 1.56e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 8632 PEFTK-PLHDLTI-HDGEQLILTCYVKGDPEPQISWSKNGKSL-SSSDILDLryKNGiaTLTINEVFPEDEGVITCTATN 8708
Cdd:cd04969     1 PDFELnPVKKKILaAKGGDVIIECKPKASPKPTISWSKGTELLtNSSRICIL--PDG--SLKIKNVTKSDEGKYTCFAVN 76

                  ...
gi 281359561 8709 SVG 8711
Cdd:cd04969    77 FFG 79
IgI_2_Palladin_C cd20990
Second C-terminal immunoglobulin (Ig)-like domain of palladin; member of the I-set of Ig ...
119-210 1.61e-05

Second C-terminal immunoglobulin (Ig)-like domain of palladin; member of the I-set of Ig superfamily (IgSF) domains; The members here are composed of the C-terminal immunoglobulin (Ig)-like domain of palladin. Palladin belongs to the palladin-myotilin-myopalladin family. Proteins belonging to this family contain multiple Ig-like domains and function as scaffolds, modulating actin cytoskeleton. Palladin binds to alpha-actinin ezrin, vasodilator-stimulated phosphoprotein VASP, SPIN90 (also known as DIP or mDia interacting protein), and Src. Palladin also binds F-actin directly, via its Ig3 domain. Palladin is expressed as several alternatively spliced isoforms, having various combinations of Ig-like domains, in a cell-type-specific manner. It has been suggested that palladin's different Ig-like domains may be specialized for distinct functions. This group belongs to the I-set of IgSF domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand, but lack a C" strand.


Pssm-ID: 409582  Cd Length: 91  Bit Score: 47.02  E-value: 1.61e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561  119 PTFAKKPAIRQEEDGKRLLFECRVNADPIPAIIWFHNGAAVKESERHKITVDKD-VHSyfatLEILNVTVEDAGKYKVNA 197
Cdd:cd20990     1 PHFLQAPGDLTVQEGKLCRMDCKVSGLPTPDLSWQLDGKPIRPDSAHKMLVRENgVHS----LIIEPVTSRDAGIYTCIA 76
                          90
                  ....*....|...
gi 281359561  198 KNELGESNATISL 210
Cdd:cd20990    77 TNRAGQNSFNLEL 89
IgI_5_Robo cd20952
Fifth Ig-like domain of Roundabout (Robo) homolog 1/2, and similar domains; a member of the ...
4981-5069 1.61e-05

Fifth Ig-like domain of Roundabout (Robo) homolog 1/2, and similar domains; a member of the I-set of IgSF domains; The members here are composed of the fifth Ig-like domain of Roundabout (Robo) homolog 1/2 and similar domains. Robo receptors play a role in the development of the central nervous system (CNS), and are receptors of Slit protein. Slit is a repellant secreted by the neural cells in the midline. Slit acts through Robo to prevent most neurons from crossing the midline from either side. Three mammalian Robo homologs (Robo1, -2, and -3), and three mammalian Slit homologs (Slit-1,-2, -3), have been identified. Commissural axons, which cross the midline, express low levels of Robo; longitudinal axons, which avoid the midline, express high levels of Robo. Robo1, -2, and -3 are expressed by commissural neurons in the vertebrate spinal cord and Slits 1, -2, -3 are expressed at the ventral midline. Robo-3 is a divergent member of the Robo family which instead of being a positive regulator of slit responsiveness, antagonizes slit responsiveness in precrossing axons. The Slit-Robo interaction is mediated by the second leucine-rich repeat (LRR) domain of Slit and the two N-terminal Ig domains of Robo, Ig1 and Ig2. The primary Robo binding site for Slit2 has been shown by surface plasmon resonance experiments and mutational analysis to be is the Ig1 domain, while the Ig2 domain has been proposed to harbor a weak secondary binding site. The fifth Ig-like domain of Robo 1 and 2 is a member of the I-set Ig domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand but lack a C" strand. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors


Pssm-ID: 409544 [Multi-domain]  Cd Length: 87  Bit Score: 47.11  E-value: 1.61e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 4981 IDRSSLVEVRIKAGQSFTFDCKVSGEPAPQTKWLLKKKEVYSKDNvKVTNVDyNTKLKVNSATRSDSGIYTVFAENANGE 5060
Cdd:cd20952     1 IILQGPQNQTVAVGGTVVLNCQATGEPVPTISWLKDGVPLLGKDE-RITTLE-NGSLQIKGAEKSDTGEYTCVALNLSGE 78

                  ....*....
gi 281359561 5061 DSADVKVTV 5069
Cdd:cd20952    79 ATWSAVLDV 87
IgI_5_Robo cd20952
Fifth Ig-like domain of Roundabout (Robo) homolog 1/2, and similar domains; a member of the ...
2306-2395 1.64e-05

Fifth Ig-like domain of Roundabout (Robo) homolog 1/2, and similar domains; a member of the I-set of IgSF domains; The members here are composed of the fifth Ig-like domain of Roundabout (Robo) homolog 1/2 and similar domains. Robo receptors play a role in the development of the central nervous system (CNS), and are receptors of Slit protein. Slit is a repellant secreted by the neural cells in the midline. Slit acts through Robo to prevent most neurons from crossing the midline from either side. Three mammalian Robo homologs (Robo1, -2, and -3), and three mammalian Slit homologs (Slit-1,-2, -3), have been identified. Commissural axons, which cross the midline, express low levels of Robo; longitudinal axons, which avoid the midline, express high levels of Robo. Robo1, -2, and -3 are expressed by commissural neurons in the vertebrate spinal cord and Slits 1, -2, -3 are expressed at the ventral midline. Robo-3 is a divergent member of the Robo family which instead of being a positive regulator of slit responsiveness, antagonizes slit responsiveness in precrossing axons. The Slit-Robo interaction is mediated by the second leucine-rich repeat (LRR) domain of Slit and the two N-terminal Ig domains of Robo, Ig1 and Ig2. The primary Robo binding site for Slit2 has been shown by surface plasmon resonance experiments and mutational analysis to be is the Ig1 domain, while the Ig2 domain has been proposed to harbor a weak secondary binding site. The fifth Ig-like domain of Robo 1 and 2 is a member of the I-set Ig domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand but lack a C" strand. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors


Pssm-ID: 409544 [Multi-domain]  Cd Length: 87  Bit Score: 46.72  E-value: 1.64e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 2306 IVGEGLKNVTVKKGQTIRFDIKYDGEPEPAATWVKGTDNLKFDNQRICLDQlerNSSITIKKSVRKDTGKYKLVLSNSSG 2385
Cdd:cd20952     1 IILQGPQNQTVAVGGTVVLNCQATGEPVPTISWLKDGVPLLGKDERITTLE---NGSLQIKGAEKSDTGEYTCVALNLSG 77
                          90
                  ....*....|
gi 281359561 2386 TIESEAQVVV 2395
Cdd:cd20952    78 EATWSAVLDV 87
IgI_2_Titin_Z1z2-like cd20972
Second Ig-like domain of the giant muscle protein titin Z1z2 in the sarcomeric Z-disk, and ...
5275-5366 1.69e-05

Second Ig-like domain of the giant muscle protein titin Z1z2 in the sarcomeric Z-disk, and similar domains; a member of the I-set of IgSF domains; The members here are composed of the second immunoglobulin (Ig)-like domain of the giant muscle protein titin Z1z2 in the sarcomeric Z-disk and similar proteins. Titin is a key component in the assembly and functioning of vertebrate striated muscles. By providing connections at the level of individual microfilaments, it contributes to the fine balance of forces between the two halves of the sarcomere. The Ig superfamily (IgSF) is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. Unlike the V-set, one of the distinctive features of I-set domains is the lack of a C" strand. The structure of the titin Z1z2 lacks this strand and thus it belongs to the I-set of the IgSF. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors, the hemolymph protein hemolin, the muscle proteins titin, telokin, and twitchin, the neuronal adhesion molecule axonin-1, and the signaling molecule semaphorin 4D that is involved in axonal guidance, immune function and angiogenesis.


Pssm-ID: 409564 [Multi-domain]  Cd Length: 91  Bit Score: 47.19  E-value: 1.69e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 5275 PPKIDRNFMSdIKIKAGNVFEFDVPVTGEPLPSKDWTHEGNMIINTDRVKISNFDDRTKIRILDAKRSDTGVYTLTARNI 5354
Cdd:cd20972     1 PPQFIQKLRS-QEVAEGSKVRLECRVTGNPTPVVRWFCEGKELQNSPDIQIHQEGDLHSLIIAEAFEEDTGRYSCLATNS 79
                          90
                  ....*....|..
gi 281359561 5355 NGTDRHNVKVTI 5366
Cdd:cd20972    80 VGSDTTSAEIFV 91
IgI_4_MYLK-like cd20976
Fourth Ig-like domain from smooth muscle myosin light chain kinase and similar domains ; a ...
7647-7737 1.78e-05

Fourth Ig-like domain from smooth muscle myosin light chain kinase and similar domains ; a member of the I-set of IgSF domains; The members here are composed of the fourth immunoglobulin (Ig)-like domain from smooth muscle myosin light chain kinase (MYLK) and similar domains. The Ig superfamily (IgSF) is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. Unlike the V-set, one of the distinctive features of I-set domains is the lack of a C" strand. The structure of this group shows that the fourth Ig-like domain from myosin light chain kinase lacks this strand and thus belongs to the I-set of the IgSF. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors, the hemolymph protein hemolin, the muscle proteins titin, telokin, and twitchin, the neuronal adhesion molecule axonin-1, and the signaling molecule semaphorin 4D that is involved in axonal guidance, immune function and angiogenesis.


Pssm-ID: 409568 [Multi-domain]  Cd Length: 90  Bit Score: 46.86  E-value: 1.78e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 7647 PPLIVKPLRDANCIQNHNAQFTCTINGVPKPTISWYKGAREIsNGARYHMYSEGDNHFLNINDVFGEDADEYVCRAVNKA 7726
Cdd:cd20976     1 APSFSSVPKDLEAVEGQDFVAQCSARGKPVPRITWIRNAQPL-QYAADRSTCEAGVGELHIQDVLPEDHGTYTCLAKNAA 79
                          90
                  ....*....|.
gi 281359561 7727 GAKSTRATLAI 7737
Cdd:cd20976    80 GQVSCSAWVTV 90
IgI_telokin-like cd20973
immunoglobulin-like domain of telokin and similar proteins; a member of the I-set of IgSF ...
28-101 1.80e-05

immunoglobulin-like domain of telokin and similar proteins; a member of the I-set of IgSF domains; The members here are composed of the immunoglobulin (Ig) domain in telokin, the C-terminal domain of myosin light chain kinase which is identical to telokin, and similar proteins. The Ig superfamily (IgSF) is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. Unlike the V-set, one of the distinctive features of I-set domains is the lack of a C" strand. The structure of the telokin Ig domain lacks this strand and thus it belongs to the I-set of the IgSF. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors, the hemolymph protein hemolin, the muscle proteins titin, telokin, and twitchin, the neuronal adhesion molecule axonin-1, and the signaling molecule semaphorin 4D that is involved in axonal guidance, immune function and angiogenesis.


Pssm-ID: 409565 [Multi-domain]  Cd Length: 88  Bit Score: 46.80  E-value: 1.80e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 281359561   28 FECQLLSSPKPDIEWFRSDNKVVEDVRTKFkiqpVGENKYTVVLELDDVVETDAGLYKVKAKNKSGEVSASINL 101
Cdd:cd20973    17 FDCKVEGYPDPEVKWMKDDNPIVESRRFQI----DQDEDGLCSLIISDVCGDDSGKYTCKAVNSLGEATCSAEL 86
IgI_3_Robo cd05725
Third immunoglobulin (Ig)-like domain in Robo (roundabout) receptors; member of the I-set of ...
242-320 1.95e-05

Third immunoglobulin (Ig)-like domain in Robo (roundabout) receptors; member of the I-set of Ig superfamily (IgSF) domains; The members here are composed of the third immunoglobulin (Ig)-like domain in Robo (roundabout) receptors. Robo receptors play a role in the development of the central nervous system (CNS), and are receptors of Slit protein. Slit is a repellant secreted by the neural cells in the midline. Slit acts through Robo to prevent most neurons from crossing the midline from either side. Three mammalian Robo homologs (Robo1, Robo2, Robo3), and three mammalian Slit homologs (Slit-1,Slit-2, Slit-3), have been identified. Commissural axons, which cross the midline, express low levels of Robo; longitudinal axons, which avoid the midline, express high levels of Robo. Robo1, Robo2, and Robo3 are expressed by commissural neurons in the vertebrate spinal cord and Slit-1, Slit-2, and Slit-3 are expressed at the ventral midline. Robo-3 is a divergent member of the Robo family which instead of being a positive regulator of Slit responsiveness, antagonizes Slit responsiveness in precrossing axons. The Slit-Robo interaction is mediated by the second leucine-rich repeat (LRR) domain of Slit and the two N-terminal Ig domains of Robo, Ig1 and Ig2. The primary Robo binding site for Slit2 has been shown by surface plasmon resonance experiments and mutational analysis to be the Ig1 domain, while the Ig2 domain has been proposed to harbor a weak secondary binding site. This group belongs to the I-set of IgSF domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand, but lack a C" strand.


Pssm-ID: 409390 [Multi-domain]  Cd Length: 83  Bit Score: 46.62  E-value: 1.95e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 281359561  242 GGNVTFECRCVGDPTPTVTWSHGETELNESnRYKMsltMDQKlyhiaCLEISSVVSSDQGEYRAQAKNKHGSGVATINL 320
Cdd:cd05725    12 DDSAEFQCEVGGDPVPTVRWRKEDGELPKG-RYEI---LDDH-----SLKIRKVTAGDMGSYTCVAENMVGKIEASATL 81
Ig4_Contactin-2-like cd05728
Fourth Ig domain of the neural cell adhesion molecule contactin-2, and similar domains; The ...
4994-5069 1.97e-05

Fourth Ig domain of the neural cell adhesion molecule contactin-2, and similar domains; The members here are composed of the fourth Ig domain of the neural cell adhesion molecule contactin-2. Contactins are comprised of six Ig domains followed by four fibronectin type III (FnIII) domains anchored to the membrane by glycosylphosphatidylinositol. Contactin-2 (also called TAG-1, axonin-1) facilitates cell adhesion by homophilic binding between molecules in apposed membranes. The first four Ig domains form the intermolecular binding fragment which arranges as a compact U-shaped module by contacts between Ig domains 1 and 4, and domains 2 and 3. It has been proposed that a linear zipper-like array forms, from contactin-2 molecules alternatively provided by the two apposed membranes.


Pssm-ID: 143205 [Multi-domain]  Cd Length: 85  Bit Score: 46.82  E-value: 1.97e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 281359561 4994 GQSFTFDCKVSGEPAPQTKWLLKKKEVYSKDNVKVTnvdyNTKLKVNSATRSDSGIYTVFAENANGEDSADVKVTV 5069
Cdd:cd05728    14 GSSLRWECKASGNPRPAYRWLKNGQPLASENRIEVE----AGDLRITKLSLSDSGMYQCVAENKHGTIYASAELAV 85
IgI_titin_I1-like cd20951
Immunoglobulin domain I1 of the titin I-band and similar proteins; a member of the I-set of ...
7758-7827 2.04e-05

Immunoglobulin domain I1 of the titin I-band and similar proteins; a member of the I-set of IgSF domains; The members here are composed of the immunoglobulin domain I1 of the titin I-band and similar proteins. Titin is a key component in the assembly and functioning of vertebrate striated muscles. By providing connections at the level of individual microfilaments, it contributes to the fine balance of forces between the two halves of the sarcomere. The Ig superfamily (IgSF) is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. The two sheets are linked together by a conserved disulfide bond between B strand and F strand. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. The Ig I1 domain of the titin I-band is a member of the I-set Ig domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand but lack a C" strand. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors, the hemolymph protein hemolin, the muscle proteins titin, telokin, and twitchin, the neuronal adhesion molecule axonin-1, and the signaling molecule semaphorin 4D that is involved in axonal guidance, immune function and angiogenesis.


Pssm-ID: 409543 [Multi-domain]  Cd Length: 94  Bit Score: 47.03  E-value: 2.04e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 281359561 7758 GENVVIKIPFTGFPKPRIHWVRDGENIES---GGHYTVEVKERHAVLIIRDGSHLDSGPYRITAENELGSDTA 7827
Cdd:cd20951    15 KSDAKLRVEVQGKPDPEVKWYKNGVPIDPssiPGKYKIESEYGVHVLHIRRVTVEDSAVYSAVAKNIHGEASS 87
IgI_3_Robo cd05725
Third immunoglobulin (Ig)-like domain in Robo (roundabout) receptors; member of the I-set of ...
8447-8525 2.17e-05

Third immunoglobulin (Ig)-like domain in Robo (roundabout) receptors; member of the I-set of Ig superfamily (IgSF) domains; The members here are composed of the third immunoglobulin (Ig)-like domain in Robo (roundabout) receptors. Robo receptors play a role in the development of the central nervous system (CNS), and are receptors of Slit protein. Slit is a repellant secreted by the neural cells in the midline. Slit acts through Robo to prevent most neurons from crossing the midline from either side. Three mammalian Robo homologs (Robo1, Robo2, Robo3), and three mammalian Slit homologs (Slit-1,Slit-2, Slit-3), have been identified. Commissural axons, which cross the midline, express low levels of Robo; longitudinal axons, which avoid the midline, express high levels of Robo. Robo1, Robo2, and Robo3 are expressed by commissural neurons in the vertebrate spinal cord and Slit-1, Slit-2, and Slit-3 are expressed at the ventral midline. Robo-3 is a divergent member of the Robo family which instead of being a positive regulator of Slit responsiveness, antagonizes Slit responsiveness in precrossing axons. The Slit-Robo interaction is mediated by the second leucine-rich repeat (LRR) domain of Slit and the two N-terminal Ig domains of Robo, Ig1 and Ig2. The primary Robo binding site for Slit2 has been shown by surface plasmon resonance experiments and mutational analysis to be the Ig1 domain, while the Ig2 domain has been proposed to harbor a weak secondary binding site. This group belongs to the I-set of IgSF domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand, but lack a C" strand.


Pssm-ID: 409390 [Multi-domain]  Cd Length: 83  Bit Score: 46.23  E-value: 2.17e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 281359561 8447 VMQARDTCKLLCCLSGKPVPNVRWYKDGRELSKYEYAMTHSDgvvTMEIIDCKPSDSGKYSCKATNCHGTDETDCVVIV 8525
Cdd:cd05725     8 VVLVDDSAEFQCEVGGDPVPTVRWRKEDGELPKGRYEILDDH---SLKIRKVTAGDMGSYTCVAENMVGKIEASATLTV 83
Ig_C5_MyBP-C cd05894
C5 immunoglobulin (Ig) domain of cardiac myosin binding protein C (MyBP-C); The members here ...
2916-2995 2.18e-05

C5 immunoglobulin (Ig) domain of cardiac myosin binding protein C (MyBP-C); The members here are composed of the C5 immunoglobulin (Ig) domain of cardiac myosin binding protein C (MyBP-C). MyBP-C consists of repeated domains, Ig and fibronectin type 3, and various linkers. Three isoforms of MYBP-C exist: slow-skeletal (ssMyBP-C), fast-skeletal (fsMyBP-C), and cardiac (cMyBP-C). cMYBP-C has insertions between and inside domains and an additional cardiac-specific Ig domain at the N-terminus. For cMYBP_C an interaction has been demonstrated between this C5 domain and the Ig C8 domain.


Pssm-ID: 409475  Cd Length: 86  Bit Score: 46.37  E-value: 2.18e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 2916 AGKPIRYDVNVRGEPAPVITWYQNDKELKPEElpSSSEIKNIPYNTKISIIETVRKHTGIYKIIAVNEHGQDEATVEVNI 2995
Cdd:cd05894     9 AGNKLRLDVPISGEPAPTVTWSRGDKAFTATE--GRVRVESYKDLSSFVIEGAEREDEGVYTITVTNPVGEDHASLFVKV 86
COG4733 COG4733
Phage-related protein, tail protein J [Mobilome: prophages, transposons];
6318-6542 2.24e-05

Phage-related protein, tail protein J [Mobilome: prophages, transposons];


Pssm-ID: 443767 [Multi-domain]  Cd Length: 978  Bit Score: 51.87  E-value: 2.24e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 6318 FTVKNLVEGKKYVFRIRA----ENIYGA--SEALEGKPVlaksPFDPPGAPSQPTISAYTPNSAN----LEWHPPDDcgg 6387
Cdd:COG4733   491 FRVVSIEENEDGTYTITAvqhaPEKYAAidAGAFDDVPP----QWPPVNVTTSESLSVVAQGTAVttltVSWDAPAG--- 563
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 6388 kpITGYIVERRERGGEWIkcNNYPTPNTSYTVSNLRDGaRYEFRVLAVNEAGpghpsKPSDPMTAEHQRYRPDPPEPPKP 6467
Cdd:COG4733   564 --AVAYEVEWRRDDGNWV--SVPRTSGTSFEVPGIYAG-DYEVRVRAINALG-----VSSAWAASSETTVTGKTAPPPAP 633
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 6468 DRIT----RNGVTLSWRPPRTDGKSRIkgyyvEMRPKNGKDWK--TVNDIPINSTVYTVPSLKEGEEYSFRVVAENEVGR 6541
Cdd:COG4733   634 TGLTatggLGGITLSWSFPVDADTLRT-----EIRYSTTGDWAsaTVAQALYPGNTYTLAGLKAGQTYYYRARAVDRSGN 708

                  .
gi 281359561 6542 S 6542
Cdd:COG4733   709 V 709
Ig cd00096
Immunoglobulin domain; The members here are composed of the immunoglobulin (Ig) domain found ...
2626-2683 2.35e-05

Immunoglobulin domain; The members here are composed of the immunoglobulin (Ig) domain found in the Ig superfamily. The Ig superfamily is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. Members of this group are components of immunoglobulin, neuroglia, cell surface glycoproteins, including T-cell receptors, CD2, CD4, CD8, and membrane glycoproteins, including butyrophilin and chondroitin sulfate proteoglycan core protein. A predominant feature of most Ig domains is a disulfide bridge connecting the two beta-sheets with a tryptophan residue packed against the disulfide bond. Ig superfamily (IgSF) domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. Typically, the V-set domains have A, B, E, and D strands in one sheet and A', G, F, C, C' and C" in the other. The structures in C1-set are smaller than those in the V-set; they have one beta sheet that is formed by strands A, B, E, and D and the other by strands G, F, C, and C'. Moreover, a C1-set Ig domain contains a short C' strand (three residues) and lacks A' and C" strand. Unlike other Ig domain sets, C2-set structures do not have a D strand. Like the V-set Ig domains, members of the I-set have a discontinuous A strand, but lack a C" strand.


Pssm-ID: 409353 [Multi-domain]  Cd Length: 70  Bit Score: 45.78  E-value: 2.35e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 281359561 2626 VLGEPIPELHWsWRDDIPLTNGDRIKIENVDYHTDFSITNVLRKDSGFYTLKAENRNG 2683
Cdd:cd00096     7 ASGNPPPTITW-YKNGKPLPPSSRDSRRSELGNGTLTISNVTLEDSGTYTCVASNSAG 63
IgI_2_Robo cd05724
Second immunoglobulin (Ig)-like domain in Robo (roundabout) receptors; member of the I-set of ...
7262-7334 2.43e-05

Second immunoglobulin (Ig)-like domain in Robo (roundabout) receptors; member of the I-set of Ig superfamily (IgSF) domains; The members here are composed of the second immunoglobulin (Ig)-like domain in Robo (roundabout) receptors. Robo receptors play a role in the development of the central nervous system (CNS), and are receptors of the Slit protein. Slit is a repellant secreted by the neural cells in the midline. Slit acts through Robo to prevent most neurons from crossing the midline from either side. Three mammalian Robo homologs (Robo1, Robo2, and Robo3), and three mammalian Slit homologs (Slit-1,Slit-2, Slit-3), have been identified. Commissural axons, which cross the midline, express low levels of Robo; longitudinal axons, which avoid the midline, express high levels of Robo. Robo1, Robo2, and Robo3 are expressed by commissural neurons in the vertebrate spinal cord and Slit-1, Slit-2, Slit-3 are expressed at the ventral midline. Robo-3 is a divergent member of the Robo family which instead of being a positive regulator of Slit responsiveness, antagonizes Slit responsiveness in precrossing axons. The Slit-Robo interaction is mediated by the second leucine-rich repeat (LRR) domain of Slit and the two N-terminal Ig domains of Robo, Ig1 and Ig2. The primary Robo binding site for Slit-2 has been shown by surface plasmon resonance experiments and mutational analysis to be the Ig1 domain, while the Ig2 domain has been proposed to harbor a weak secondary binding site. This group belongs to the I-set of IgSF domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand, but lack a C" strand.


Pssm-ID: 409389 [Multi-domain]  Cd Length: 87  Bit Score: 46.24  E-value: 2.43e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 281359561 7262 DKVAPFGKDYTLQCAAS-GKPSPTARWLRNGKEIQMNGGRMTCdSKDGvfRLHISNVQTGDDGDYTCEAMNSLG 7334
Cdd:cd05724     6 DTQVAVGEMAVLECSPPrGHPEPTVSWRKDGQPLNLDNERVRI-VDDG--NLLIAEARKSDEGTYKCVATNMVG 76
Ig cd00096
Immunoglobulin domain; The members here are composed of the immunoglobulin (Ig) domain found ...
3819-3875 2.44e-05

Immunoglobulin domain; The members here are composed of the immunoglobulin (Ig) domain found in the Ig superfamily. The Ig superfamily is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. Members of this group are components of immunoglobulin, neuroglia, cell surface glycoproteins, including T-cell receptors, CD2, CD4, CD8, and membrane glycoproteins, including butyrophilin and chondroitin sulfate proteoglycan core protein. A predominant feature of most Ig domains is a disulfide bridge connecting the two beta-sheets with a tryptophan residue packed against the disulfide bond. Ig superfamily (IgSF) domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. Typically, the V-set domains have A, B, E, and D strands in one sheet and A', G, F, C, C' and C" in the other. The structures in C1-set are smaller than those in the V-set; they have one beta sheet that is formed by strands A, B, E, and D and the other by strands G, F, C, and C'. Moreover, a C1-set Ig domain contains a short C' strand (three residues) and lacks A' and C" strand. Unlike other Ig domain sets, C2-set structures do not have a D strand. Like the V-set Ig domains, members of the I-set have a discontinuous A strand, but lack a C" strand.


Pssm-ID: 409353 [Multi-domain]  Cd Length: 70  Bit Score: 45.78  E-value: 2.44e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 281359561 3819 IKAEPPAKVTWTYNKTEIKTSDHIKIENEDYKTTFIMPKVKRADRGIYIVTAKNDSG 3875
Cdd:cd00096     7 ASGNPPPTITWYKNGKPLPPSSRDSRRSELGNGTLTISNVTLEDSGTYTCVASNSAG 63
COG4733 COG4733
Phage-related protein, tail protein J [Mobilome: prophages, transposons];
3026-3182 2.45e-05

Phage-related protein, tail protein J [Mobilome: prophages, transposons];


Pssm-ID: 443767 [Multi-domain]  Cd Length: 978  Bit Score: 51.87  E-value: 2.45e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 3026 DGGKPISAYQVEkFDKKQGRWVPLGRTSAndTEFDVKGLQEGhEYQFRVKAINEEG-ESDPLDSDDSIIAknpYDAASKP 3104
Cdd:COG4733   559 DAPAGAVAYEVE-WRRDDGNWVSVPRTSG--TSFEVPGIYAG-DYEVRVRAINALGvSSAWAASSETTVT---GKTAPPP 631
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 3105 GTPNI-VDYNEHMVKLKWEAPRsdgGAPISGYII---EKKDKFSPiwdEILSTNTSVPEATVEGLVEGNIYQFRVRAVNK 3180
Cdd:COG4733   632 APTGLtATGGLGGITLSWSFPV---DADTLRTEIrysTTGDWASA---TVAQALYPGNTYTLAGLKAGQTYYYRARAVDR 705

                  ..
gi 281359561 3181 AG 3182
Cdd:COG4733   706 SG 707
IgI_5_Robo cd20952
Fifth Ig-like domain of Roundabout (Robo) homolog 1/2, and similar domains; a member of the ...
4694-4769 2.53e-05

Fifth Ig-like domain of Roundabout (Robo) homolog 1/2, and similar domains; a member of the I-set of IgSF domains; The members here are composed of the fifth Ig-like domain of Roundabout (Robo) homolog 1/2 and similar domains. Robo receptors play a role in the development of the central nervous system (CNS), and are receptors of Slit protein. Slit is a repellant secreted by the neural cells in the midline. Slit acts through Robo to prevent most neurons from crossing the midline from either side. Three mammalian Robo homologs (Robo1, -2, and -3), and three mammalian Slit homologs (Slit-1,-2, -3), have been identified. Commissural axons, which cross the midline, express low levels of Robo; longitudinal axons, which avoid the midline, express high levels of Robo. Robo1, -2, and -3 are expressed by commissural neurons in the vertebrate spinal cord and Slits 1, -2, -3 are expressed at the ventral midline. Robo-3 is a divergent member of the Robo family which instead of being a positive regulator of slit responsiveness, antagonizes slit responsiveness in precrossing axons. The Slit-Robo interaction is mediated by the second leucine-rich repeat (LRR) domain of Slit and the two N-terminal Ig domains of Robo, Ig1 and Ig2. The primary Robo binding site for Slit2 has been shown by surface plasmon resonance experiments and mutational analysis to be is the Ig1 domain, while the Ig2 domain has been proposed to harbor a weak secondary binding site. The fifth Ig-like domain of Robo 1 and 2 is a member of the I-set Ig domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand but lack a C" strand. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors


Pssm-ID: 409544 [Multi-domain]  Cd Length: 87  Bit Score: 46.34  E-value: 2.53e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 281359561 4694 NITLSSGTALKLDANITGEPAPKVEWkLSNYHLQSGKNVTIETPDYYTkLVIRPTQRSDSGEYLVTATNTSGKDSV 4769
Cdd:cd20952     8 NQTVAVGGTVVLNCQATGEPVPTISW-LKDGVPLLGKDERITTLENGS-LQIKGAEKSDTGEYTCVALNLSGEATW 81
Ig5_Contactin cd04969
Fifth immunoglobulin (Ig) domain of contactin; The members here are composed of the fifth ...
2311-2395 2.63e-05

Fifth immunoglobulin (Ig) domain of contactin; The members here are composed of the fifth immunoglobulin (Ig) domain of contactins. Contactins are neural cell adhesion molecules and are comprised of six Ig domains followed by four fibronectin type III (FnIII) domains anchored to the membrane by glycosylphosphatidylinositol. The first four Ig domains form the intermolecular binding fragment, which arranges as a compact U-shaped module via contacts between Ig domains 1 and 4, and between Ig domains 2 and 3. Contactin-2 (TAG-1, axonin-1) may play a part in the neuronal processes of neurite outgrowth, axon guidance and fasciculation, and neuronal migration. This group also includes contactin-1 and contactin-5. The different contactins show different expression patterns in the central nervous system. During development and in adulthood, contactin-2 is transiently expressed in subsets of central and peripheral neurons. Contactin-5 is expressed specifically in the rat postnatal nervous system, peaking at about 3 weeks postnatal, and a lack of contactin-5 (NB-2) results in an impairment of neuronal activity in the rat auditory system. Contactin-5 is highly expressed in the adult human brain in the occipital lobe and in the amygdala. Contactin-1 is differentially expressed in tumor tissues and may, through a RhoA mechanism, facilitate invasion and metastasis of human lung adenocarcinoma.


Pssm-ID: 409358 [Multi-domain]  Cd Length: 89  Bit Score: 46.30  E-value: 2.63e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 2311 LKNVT-VKKGQTIRFDIKYDGEPEPAATWVKGTDNLKfDNQRICLDQlerNSSITIKKSVRKDTGKYKLVLSNSSGTIES 2389
Cdd:cd04969     8 VKKKIlAAKGGDVIIECKPKASPKPTISWSKGTELLT-NSSRICILP---DGSLKIKNVTKSDEGKYTCFAVNFFGKANS 83

                  ....*.
gi 281359561 2390 EAQVVV 2395
Cdd:cd04969    84 TGSLSV 89
Ig4_Contactin-2-like cd05728
Fourth Ig domain of the neural cell adhesion molecule contactin-2, and similar domains; The ...
5585-5660 2.69e-05

Fourth Ig domain of the neural cell adhesion molecule contactin-2, and similar domains; The members here are composed of the fourth Ig domain of the neural cell adhesion molecule contactin-2. Contactins are comprised of six Ig domains followed by four fibronectin type III (FnIII) domains anchored to the membrane by glycosylphosphatidylinositol. Contactin-2 (also called TAG-1, axonin-1) facilitates cell adhesion by homophilic binding between molecules in apposed membranes. The first four Ig domains form the intermolecular binding fragment which arranges as a compact U-shaped module by contacts between Ig domains 1 and 4, and domains 2 and 3. It has been proposed that a linear zipper-like array forms, from contactin-2 molecules alternatively provided by the two apposed membranes.


Pssm-ID: 143205 [Multi-domain]  Cd Length: 85  Bit Score: 46.44  E-value: 2.69e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 281359561 5585 GKRLGWTLPIEASPRPLITWLYNGKEIGSNSRGEsgLFQNELTFEIVSslRSDEGRYTLILKNEHGSFDASAHATV 5660
Cdd:cd05728    14 GSSLRWECKASGNPRPAYRWLKNGQPLASENRIE--VEAGDLRITKLS--LSDSGMYQCVAENKHGTIYASAELAV 85
Ig_3 pfam13927
Immunoglobulin domain; This family contains immunoglobulin-like domains.
2303-2382 2.84e-05

Immunoglobulin domain; This family contains immunoglobulin-like domains.


Pssm-ID: 464046 [Multi-domain]  Cd Length: 78  Bit Score: 46.02  E-value: 2.84e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561  2303 KPFIVGEGlKNVTVKKGQTIRFDIKYDGEPEPAATWVKGtDNLKFDNQRICLDQLERNSSITIKKSVRKDTGKYKLVLSN 2382
Cdd:pfam13927    1 KPVITVSP-SSVTVREGETVTLTCEATGSPPPTITWYKN-GEPISSGSTRSRSLSGSNSTLTISNVTRSDAGTYTCVASN 78
Ig_C5_MyBP-C cd05894
C5 immunoglobulin (Ig) domain of cardiac myosin binding protein C (MyBP-C); The members here ...
7758-7833 2.86e-05

C5 immunoglobulin (Ig) domain of cardiac myosin binding protein C (MyBP-C); The members here are composed of the C5 immunoglobulin (Ig) domain of cardiac myosin binding protein C (MyBP-C). MyBP-C consists of repeated domains, Ig and fibronectin type 3, and various linkers. Three isoforms of MYBP-C exist: slow-skeletal (ssMyBP-C), fast-skeletal (fsMyBP-C), and cardiac (cMyBP-C). cMYBP-C has insertions between and inside domains and an additional cardiac-specific Ig domain at the N-terminus. For cMYBP_C an interaction has been demonstrated between this C5 domain and the Ig C8 domain.


Pssm-ID: 409475  Cd Length: 86  Bit Score: 46.37  E-value: 2.86e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 281359561 7758 GENVVIKIPFTGFPKPRIHWVRDGE-NIESGGHYTVEVKERHAVLIIRDGSHLDSGPYRITAENELGSDTAIIQVQI 7833
Cdd:cd05894    10 GNKLRLDVPISGEPAPTVTWSRGDKaFTATEGRVRVESYKDLSSFVIEGAEREDEGVYTITVTNPVGEDHASLFVKV 86
IgI_8_hMLCK_like cd05762
Eighth immunoglobulin (Ig)-like domain of human myosin light-chain kinase (MLCK) and similar ...
6865-6953 2.89e-05

Eighth immunoglobulin (Ig)-like domain of human myosin light-chain kinase (MLCK) and similar protein; member of the I-set of IgSF domains; The members here are composed of the eighth immunoglobulin (Ig)-like domain of human myosin light-chain kinase (MLCK) and similar proteins. Myosin light-chain kinase (MLCK) is a key regulator of different forms of cell motility involving actin and myosin II. Agonist stimulation of smooth muscle cells increases cytosolic Ca2+ which binds calmodulin. This Ca2+-calmodulin complex in turn binds to and activates MLCK. Activated MLCK leads to the phosphorylation of the 20 kDa myosin regulatory light chain (RLC) of myosin II and the stimulation of actin-activated myosin MgATPase activity. MLCK is widely present in vertebrate tissues; it phosphorylates the 20 kDa RLC of both smooth and nonmuscle myosin II. Phosphorylation leads to the activation of the myosin motor domain and altered structural properties of myosin II. In smooth muscle MLCK it is involved in initiating contraction. In nonmuscle cells, MLCK may participate in cell division and cell motility; it has been suggested MLCK plays a role in cardiomyocyte differentiation and contraction through regulation of nonmuscle myosin II.


Pssm-ID: 409419  Cd Length: 99  Bit Score: 46.49  E-value: 2.89e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 6865 DMTVIAGDEFRITVPYHASPRPTASWSLNGLEVIPGERIKFDSNDYASMYYNKSAKRDETGSYTITLTNNKGSDTASCHV 6944
Cdd:cd05762    10 DMKVRAGESVELFCKVTGTQPITCTWMKFRKQIQEGEGIKIENTENSSKLTITEGQQEHCGCYTLEVENKLGSRQAQVNL 89

                  ....*....
gi 281359561 6945 TVVDRPLPP 6953
Cdd:cd05762    90 TVVDKPDPP 98
COG4733 COG4733
Phage-related protein, tail protein J [Mobilome: prophages, transposons];
2254-2582 2.93e-05

Phage-related protein, tail protein J [Mobilome: prophages, transposons];


Pssm-ID: 443767 [Multi-domain]  Cd Length: 978  Bit Score: 51.48  E-value: 2.93e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 2254 EVDGDARTATV-------DGLKEGQQYEFRVRAVN-------RAGPGEPSDKTKSIIakcrfvkpfiVGEG---LKNVTV 2316
Cdd:COG4733   388 SVGLDGLVATPgdviavaDDVLAGRRIGGRVSSVDgrvvtldRPVTMEAGDRYLRVR----------LPDGtsvARTVQS 457
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 2317 KKGQTIRFDIKYDGEPEPAATWVKGTDNLKfdnqriclDQLERNSSITikksvRKDTGKYKLVLSNSSGTIESEAQVVVL 2396
Cdd:COG4733   458 VAGRTLTVSTAYSETPEAGAVWAFGPDELE--------TQLFRVVSIE-----ENEDGTYTITAVQHAPEKYAAIDAGAF 524
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 2397 DrplPPGGPFEPEEIRASH-------------IKMKWKRPDDDGGCEISGYAlermdeETGRWIPAGEVGpnETSFDFKG 2463
Cdd:COG4733   525 D---DVPPQWPPVNVTTSEslsvvaqgtavttLTVSWDAPAGAVAYEVEWRR------DDGNWVSVPRTS--GTSFEVPG 593
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 2464 LTPNKkYKFRVKAINKEGESEPLETFDAIVARNPYDPPSPPSQpVIDDYDNKSVLLKWKRPPSDggrPITHYIVEIKDKF 2543
Cdd:COG4733   594 IYAGD-YEVRVRAINALGVSSAWAASSETTVTGKTAPPPAPTG-LTATGGLGGITLSWSFPVDA---DTLRTEIRYSTTG 668
                         330       340       350
                  ....*....|....*....|....*....|....*....
gi 281359561 2544 APSWSEVAKTDDPNPECNVEGLKEKMVYQFRVRAVNKAG 2582
Cdd:COG4733   669 DWASATVAQALYPGNTYTLAGLKAGQTYYYRARAVDRSG 707
Ig4_Contactin-2-like cd05728
Fourth Ig domain of the neural cell adhesion molecule contactin-2, and similar domains; The ...
242-320 3.02e-05

Fourth Ig domain of the neural cell adhesion molecule contactin-2, and similar domains; The members here are composed of the fourth Ig domain of the neural cell adhesion molecule contactin-2. Contactins are comprised of six Ig domains followed by four fibronectin type III (FnIII) domains anchored to the membrane by glycosylphosphatidylinositol. Contactin-2 (also called TAG-1, axonin-1) facilitates cell adhesion by homophilic binding between molecules in apposed membranes. The first four Ig domains form the intermolecular binding fragment which arranges as a compact U-shaped module by contacts between Ig domains 1 and 4, and domains 2 and 3. It has been proposed that a linear zipper-like array forms, from contactin-2 molecules alternatively provided by the two apposed membranes.


Pssm-ID: 143205 [Multi-domain]  Cd Length: 85  Bit Score: 46.05  E-value: 3.02e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 281359561  242 GGNVTFECRCVGDPTPTVTWSHGETELNESNRYKMSltmdqklyhIACLEISSVVSSDQGEYRAQAKNKHGSGVATINL 320
Cdd:cd05728    14 GSSLRWECKASGNPRPAYRWLKNGQPLASENRIEVE---------AGDLRITKLSLSDSGMYQCVAENKHGTIYASAEL 83
Ig4_Contactin-2-like cd05728
Fourth Ig domain of the neural cell adhesion molecule contactin-2, and similar domains; The ...
8458-8516 3.11e-05

Fourth Ig domain of the neural cell adhesion molecule contactin-2, and similar domains; The members here are composed of the fourth Ig domain of the neural cell adhesion molecule contactin-2. Contactins are comprised of six Ig domains followed by four fibronectin type III (FnIII) domains anchored to the membrane by glycosylphosphatidylinositol. Contactin-2 (also called TAG-1, axonin-1) facilitates cell adhesion by homophilic binding between molecules in apposed membranes. The first four Ig domains form the intermolecular binding fragment which arranges as a compact U-shaped module by contacts between Ig domains 1 and 4, and domains 2 and 3. It has been proposed that a linear zipper-like array forms, from contactin-2 molecules alternatively provided by the two apposed membranes.


Pssm-ID: 143205 [Multi-domain]  Cd Length: 85  Bit Score: 46.05  E-value: 3.11e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 8458 CCLSGKPVPNVRWYKDGREL-SKYEYAMTHSDGVVTMEIIdckpSDSGKYSCKATNCHGT 8516
Cdd:cd05728    21 CKASGNPRPAYRWLKNGQPLaSENRIEVEAGDLRITKLSL----SDSGMYQCVAENKHGT 76
IgI_2_Titin_Z1z2-like cd20972
Second Ig-like domain of the giant muscle protein titin Z1z2 in the sarcomeric Z-disk, and ...
8-101 3.21e-05

Second Ig-like domain of the giant muscle protein titin Z1z2 in the sarcomeric Z-disk, and similar domains; a member of the I-set of IgSF domains; The members here are composed of the second immunoglobulin (Ig)-like domain of the giant muscle protein titin Z1z2 in the sarcomeric Z-disk and similar proteins. Titin is a key component in the assembly and functioning of vertebrate striated muscles. By providing connections at the level of individual microfilaments, it contributes to the fine balance of forces between the two halves of the sarcomere. The Ig superfamily (IgSF) is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. Unlike the V-set, one of the distinctive features of I-set domains is the lack of a C" strand. The structure of the titin Z1z2 lacks this strand and thus it belongs to the I-set of the IgSF. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors, the hemolymph protein hemolin, the muscle proteins titin, telokin, and twitchin, the neuronal adhesion molecule axonin-1, and the signaling molecule semaphorin 4D that is involved in axonal guidance, immune function and angiogenesis.


Pssm-ID: 409564 [Multi-domain]  Cd Length: 91  Bit Score: 46.04  E-value: 3.21e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561    8 APSFVKKPQLHQEDDGNRLIFECQLLSSPKPDIEWFRsDNKVVEDvRTKFKIQPVGENKYTVVLElddVVETDAGLYKVK 87
Cdd:cd20972     1 PPQFIQKLRSQEVAEGSKVRLECRVTGNPTPVVRWFC-EGKELQN-SPDIQIHQEGDLHSLIIAE---AFEEDTGRYSCL 75
                          90
                  ....*....|....
gi 281359561   88 AKNKSGEVSASINL 101
Cdd:cd20972    76 ATNSVGSDTTSAEI 89
IgI_1_MuSK cd20970
agrin-responsive first immunoglobulin-like domains (Ig1) of the MuSK ectodomain; a member of ...
238-315 3.27e-05

agrin-responsive first immunoglobulin-like domains (Ig1) of the MuSK ectodomain; a member of the I-set of IgSF domains; The members here are composed of the first immunoglobulin-like domains (Ig1) of the Muscle-specific kinase (MuSK). MuSK is a receptor tyrosine kinase specifically expressed in skeletal muscle, where it plays a central role in the formation and maintenance of the neuromuscular junction (NMJ). MuSK is activated by agrin, a neuron-derived heparan sulfate proteoglycan. The activation of MUSK in myotubes regulates the formation of NMJs through the regulation of different processes including the specific expression of genes in subsynaptic nuclei, the reorganization of the actin cytoskeleton and the clustering of the acetylcholine receptors (AChR) in the postsynaptic membrane. The Ig superfamily (IgSF) is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. Unlike the V-set, one of the distinctive features of I-set domains is the lack of a C" strand. The structure of the MuSK lacks this strand and thus it belongs to the I-set of the IgSF. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors, the hemolymph protein hemolin, the muscle proteins titin, telokin, and twitchin, the neuronal adhesion molecule axonin-1, and the signaling molecule semaphorin 4D that is involved in axonal guidance, immune function and angiogenesis.


Pssm-ID: 409562 [Multi-domain]  Cd Length: 92  Bit Score: 46.35  E-value: 3.27e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561  238 QSEDGGNVTFECRCVGDPTPTVTWSHGET---ELNESNRYKMSLTMdqklyhiacLEISSVVSSDQGEYRAQAKNKHGSG 314
Cdd:cd20970    13 TAREGENATFMCRAEGSPEPEISWTRNGNliiEFNTRYIVRENGTT---------LTIRNIRRSDMGIYLCIASNGVPGS 83

                  .
gi 281359561  315 V 315
Cdd:cd20970    84 V 84
IgI_Myotilin_C cd05892
C-terminal immunoglobulin (Ig)-like domain of myotilin; member of the I-set of Ig superfamily ...
7254-7344 3.41e-05

C-terminal immunoglobulin (Ig)-like domain of myotilin; member of the I-set of Ig superfamily (IgSF) domains; The members here are composed of the C-terminal immunoglobulin (Ig)-like domain of myotilin. Mytolin belongs to the palladin-myotilin-myopalladin family. Proteins belonging to the latter family contain multiple Ig-like domains and function as scaffolds, modulating the actin cytoskeleton. Myotilin is most abundant in skeletal and cardiac muscle and is involved in maintaining sarcomere integrity. It binds to alpha-actinin, filamin, and actin. Mutations in myotilin lead to muscle disorders. This group belongs to the I-set of IgSF domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand, but lack a C" strand.


Pssm-ID: 409473  Cd Length: 92  Bit Score: 46.30  E-value: 3.41e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 7254 PDWITRLQDKVAPFGKDYTLQCAASGKPSPTARWLRNGKEIQMNGGRMTCDSKD-GVFRLHISNVQTGDDGDYTCEAMNS 7332
Cdd:cd05892     1 PMFIQKPQNKKVLEGDPVRLECQISAIPPPQIFWKKNNEMLQYNTDRISLYQDNcGRICLLIQNANKKDAGWYTVSAVNE 80
                          90
                  ....*....|..
gi 281359561 7333 LGFVNTSGYLKI 7344
Cdd:cd05892    81 AGVVSCNARLDV 92
Ig_C5_MyBP-C cd05894
C5 immunoglobulin (Ig) domain of cardiac myosin binding protein C (MyBP-C); The members here ...
3212-3290 3.66e-05

C5 immunoglobulin (Ig) domain of cardiac myosin binding protein C (MyBP-C); The members here are composed of the C5 immunoglobulin (Ig) domain of cardiac myosin binding protein C (MyBP-C). MyBP-C consists of repeated domains, Ig and fibronectin type 3, and various linkers. Three isoforms of MYBP-C exist: slow-skeletal (ssMyBP-C), fast-skeletal (fsMyBP-C), and cardiac (cMyBP-C). cMYBP-C has insertions between and inside domains and an additional cardiac-specific Ig domain at the N-terminus. For cMYBP_C an interaction has been demonstrated between this C5 domain and the Ig C8 domain.


Pssm-ID: 409475  Cd Length: 86  Bit Score: 45.99  E-value: 3.66e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 3212 IKVRAGQPVKFDVDVKGEPAPSLTWfLKETEL--TSTGQVRLENIDYNTKLTLLDTDRKQSGQYKLRAENINGVDEAVVE 3289
Cdd:cd05894     5 IVVVAGNKLRLDVPISGEPAPTVTW-SRGDKAftATEGRVRVESYKDLSSFVIEGAEREDEGVYTITVTNPVGEDHASLF 83

                  .
gi 281359561 3290 V 3290
Cdd:cd05894    84 V 84
Ig_3 pfam13927
Immunoglobulin domain; This family contains immunoglobulin-like domains.
4089-4168 3.73e-05

Immunoglobulin domain; This family contains immunoglobulin-like domains.


Pssm-ID: 464046 [Multi-domain]  Cd Length: 78  Bit Score: 45.63  E-value: 3.73e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561  4089 PPKIdRTNIKDITIKAGQHIRFDIKVSGEPPATKVWLHNKARLENDDSNYNIDMESYRTkLTVPISKRFHSGKYTLKAEN 4168
Cdd:pfam13927    1 KPVI-TVSPSSVTVREGETVTLTCEATGSPPPTITWYKNGEPISSGSTRSRSLSGSNST-LTISNVTRSDAGTYTCVASN 78
I-set pfam07679
Immunoglobulin I-set domain;
1914-1998 3.73e-05

Immunoglobulin I-set domain;


Pssm-ID: 400151 [Multi-domain]  Cd Length: 90  Bit Score: 46.10  E-value: 3.73e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561  1914 RFNKKLKDTEAVEREKLILDIELQDQTAP-CDWKFNGEPIVPSESIEIKNMGGgKHQLIFSSLDMSNEGEITC----ESG 1988
Cdd:pfam07679    2 KFTQKPKDVEVQEGESARFTCTVTGTPDPeVSWFKDGQPLRSSDRFKVTYEGG-TYTLTISNVQPDDSGKYTCvatnSAG 80
                           90
                   ....*....|
gi 281359561  1989 QLSSKCKLSI 1998
Cdd:pfam07679   81 EAEASAELTV 90
IgI_1_MuSK cd20970
agrin-responsive first immunoglobulin-like domains (Ig1) of the MuSK ectodomain; a member of ...
6177-6243 3.94e-05

agrin-responsive first immunoglobulin-like domains (Ig1) of the MuSK ectodomain; a member of the I-set of IgSF domains; The members here are composed of the first immunoglobulin-like domains (Ig1) of the Muscle-specific kinase (MuSK). MuSK is a receptor tyrosine kinase specifically expressed in skeletal muscle, where it plays a central role in the formation and maintenance of the neuromuscular junction (NMJ). MuSK is activated by agrin, a neuron-derived heparan sulfate proteoglycan. The activation of MUSK in myotubes regulates the formation of NMJs through the regulation of different processes including the specific expression of genes in subsynaptic nuclei, the reorganization of the actin cytoskeleton and the clustering of the acetylcholine receptors (AChR) in the postsynaptic membrane. The Ig superfamily (IgSF) is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. Unlike the V-set, one of the distinctive features of I-set domains is the lack of a C" strand. The structure of the MuSK lacks this strand and thus it belongs to the I-set of the IgSF. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors, the hemolymph protein hemolin, the muscle proteins titin, telokin, and twitchin, the neuronal adhesion molecule axonin-1, and the signaling molecule semaphorin 4D that is involved in axonal guidance, immune function and angiogenesis.


Pssm-ID: 409562 [Multi-domain]  Cd Length: 92  Bit Score: 45.96  E-value: 3.94e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 281359561 6177 VRAGEPVNLNIPISGAPTPTIEWKRGDLKLEEGKRiSYETNSERTLFRIDDSNRRDSGKYTVTAANE 6243
Cdd:cd20970    14 AREGENATFMCRAEGSPEPEISWTRNGNLIIEFNT-RYIVRENGTTLTIRNIRRSDMGIYLCIASNG 79
Ig5_Contactin cd04969
Fifth immunoglobulin (Ig) domain of contactin; The members here are composed of the fifth ...
557-636 4.04e-05

Fifth immunoglobulin (Ig) domain of contactin; The members here are composed of the fifth immunoglobulin (Ig) domain of contactins. Contactins are neural cell adhesion molecules and are comprised of six Ig domains followed by four fibronectin type III (FnIII) domains anchored to the membrane by glycosylphosphatidylinositol. The first four Ig domains form the intermolecular binding fragment, which arranges as a compact U-shaped module via contacts between Ig domains 1 and 4, and between Ig domains 2 and 3. Contactin-2 (TAG-1, axonin-1) may play a part in the neuronal processes of neurite outgrowth, axon guidance and fasciculation, and neuronal migration. This group also includes contactin-1 and contactin-5. The different contactins show different expression patterns in the central nervous system. During development and in adulthood, contactin-2 is transiently expressed in subsets of central and peripheral neurons. Contactin-5 is expressed specifically in the rat postnatal nervous system, peaking at about 3 weeks postnatal, and a lack of contactin-5 (NB-2) results in an impairment of neuronal activity in the rat auditory system. Contactin-5 is highly expressed in the adult human brain in the occipital lobe and in the amygdala. Contactin-1 is differentially expressed in tumor tissues and may, through a RhoA mechanism, facilitate invasion and metastasis of human lung adenocarcinoma.


Pssm-ID: 409358 [Multi-domain]  Cd Length: 89  Bit Score: 45.91  E-value: 4.04e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561  557 GKLVIMECKVKADPKPDVIWFRNGEVIKESNKIkTFIEQRgdqyyiKLELLDPQLEDSGLYKCNIKNTLGELNANLTLNI 636
Cdd:cd04969    17 GGDVIIECKPKASPKPTISWSKGTELLTNSSRI-CILPDG------SLKIKNVTKSDEGKYTCFAVNFFGKANSTGSLSV 89
IgI_APEG-1_like cd20975
Immunoglobulin-like domain of human Aortic Preferentially Expressed Protein-1 (APEG-1) and ...
8632-8721 4.33e-05

Immunoglobulin-like domain of human Aortic Preferentially Expressed Protein-1 (APEG-1) and similar proteins; a member of the I-set of IgSF domains; The members here are composed of the immunoglobulin I-set (IgI) domain of the Human Aortic Preferentially Expressed Protein-1 (APEG-1) and similar proteins. APEG-1 is a novel specific smooth muscle differentiation marker predicted to play a role in the growth and differentiation of arterial smooth muscle cells (SMCs). The Ig superfamily (IgSF) is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. Unlike the V-set, one of the distinctive features of I-set domains is the lack of a C" strand. The structure of the human APEG-1 lacks this strand and thus it belongs to the I-set of the IgSF. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors, the hemolymph protein hemolin, the muscle proteins titin, telokin, and twitchin, the neuronal adhesion molecule axonin-1, and the signaling molecule semaphorin 4D that is involved in axonal guidance, immune function and angiogenesis.


Pssm-ID: 409567  Cd Length: 91  Bit Score: 45.92  E-value: 4.33e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 8632 PEFTKPLHDLTIHDGEQLILTCYVKGDPEPQISWSKNGKSLSSSD-ILDLRYKNGIATLTINEVFPEDEGVITCTATNSV 8710
Cdd:cd20975     1 PTFKVSLMDQSVREGQDVIMSIRVQGEPKPVVSWLRNRQPVRPDQrRFAEEAEGGLCRLRILAAERGDAGFYTCKAVNEY 80
                          90
                  ....*....|.
gi 281359561 8711 GAVETKCKLTI 8721
Cdd:cd20975    81 GARQCEARLEV 91
IgI_Myotilin_C cd05892
C-terminal immunoglobulin (Ig)-like domain of myotilin; member of the I-set of Ig superfamily ...
8312-8391 4.44e-05

C-terminal immunoglobulin (Ig)-like domain of myotilin; member of the I-set of Ig superfamily (IgSF) domains; The members here are composed of the C-terminal immunoglobulin (Ig)-like domain of myotilin. Mytolin belongs to the palladin-myotilin-myopalladin family. Proteins belonging to the latter family contain multiple Ig-like domains and function as scaffolds, modulating the actin cytoskeleton. Myotilin is most abundant in skeletal and cardiac muscle and is involved in maintaining sarcomere integrity. It binds to alpha-actinin, filamin, and actin. Mutations in myotilin lead to muscle disorders. This group belongs to the I-set of IgSF domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand, but lack a C" strand.


Pssm-ID: 409473  Cd Length: 92  Bit Score: 45.92  E-value: 4.44e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 8312 PRFVIRPSSQFCYEGQSVKFYCRCIAIATPTLTWSHNNIELRQSVKFMKRYVGDDYY--FIINRVKLDDRGEYIIRAENH 8389
Cdd:cd05892     1 PMFIQKPQNKKVLEGDPVRLECQISAIPPPQIFWKKNNEMLQYNTDRISLYQDNCGRicLLIQNANKKDAGWYTVSAVNE 80

                  ..
gi 281359561 8390 YG 8391
Cdd:cd05892    81 AG 82
Ig_3 pfam13927
Immunoglobulin domain; This family contains immunoglobulin-like domains.
745-823 4.54e-05

Immunoglobulin domain; This family contains immunoglobulin-like domains.


Pssm-ID: 464046 [Multi-domain]  Cd Length: 78  Bit Score: 45.25  E-value: 4.54e-05
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 281359561   745 KPEISRKLADQKVAESKTFELLVSLSQTDRKcKVEWYKGSTVIRETKDITTTFDGTTARLTFSSARTEHTSNYKVIVTN 823
Cdd:pfam13927    1 KPVITVSPSSVTVREGETVTLTCEATGSPPP-TITWYKNGEPISSGSTRSRSLSGSNSTLTISNVTRSDAGTYTCVASN 78
IgI_2_Palladin_C cd20990
Second C-terminal immunoglobulin (Ig)-like domain of palladin; member of the I-set of Ig ...
545-634 4.66e-05

Second C-terminal immunoglobulin (Ig)-like domain of palladin; member of the I-set of Ig superfamily (IgSF) domains; The members here are composed of the C-terminal immunoglobulin (Ig)-like domain of palladin. Palladin belongs to the palladin-myotilin-myopalladin family. Proteins belonging to this family contain multiple Ig-like domains and function as scaffolds, modulating actin cytoskeleton. Palladin binds to alpha-actinin ezrin, vasodilator-stimulated phosphoprotein VASP, SPIN90 (also known as DIP or mDia interacting protein), and Src. Palladin also binds F-actin directly, via its Ig3 domain. Palladin is expressed as several alternatively spliced isoforms, having various combinations of Ig-like domains, in a cell-type-specific manner. It has been suggested that palladin's different Ig-like domains may be specialized for distinct functions. This group belongs to the I-set of IgSF domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand, but lack a C" strand.


Pssm-ID: 409582  Cd Length: 91  Bit Score: 45.86  E-value: 4.66e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561  545 FIEKPRIVSENNGKLVIMECKVKADPKPDVIWFRNGEVIKESNKIKTFIEQRGDQYYIklelLDP-QLEDSGLYKCNIKN 623
Cdd:cd20990     3 FLQAPGDLTVQEGKLCRMDCKVSGLPTPDLSWQLDGKPIRPDSAHKMLVRENGVHSLI----IEPvTSRDAGIYTCIATN 78
                          90
                  ....*....|.
gi 281359561  624 TLGELNANLTL 634
Cdd:cd20990    79 RAGQNSFNLEL 89
Ig3_Peroxidasin cd05745
Third immunoglobulin (Ig)-like domain of peroxidasin; The members here are composed of the ...
241-321 4.89e-05

Third immunoglobulin (Ig)-like domain of peroxidasin; The members here are composed of the third immunoglobulin (Ig)-like domain in peroxidasin. Peroxidasin has a peroxidase domain and interacting extracellular motifs containing four Ig-like domains. It has been suggested that peroxidasin is secreted and has functions related to the stabilization of the extracellular matrix. It may play a part in various other important processes such as removal and destruction of cells which have undergone programmed cell death and protection of the organism against non-self.


Pssm-ID: 143222 [Multi-domain]  Cd Length: 74  Bit Score: 45.31  E-value: 4.89e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561  241 DGGNVTFECRCVGDPTPTVTWSHGETELNESNRYKMSLTmdqklyhiACLEISSVVSSDQGEYRAQAKNKHGSGVATINL 320
Cdd:cd05745     1 EGQTVDFLCEAQGYPQPVIAWTKGGSQLSVDRRHLVLSS--------GTLRISRVALHDQGQYECQAVNIVGSQRTVAQL 72

                  .
gi 281359561  321 N 321
Cdd:cd05745    73 T 73
Ig cd00096
Immunoglobulin domain; The members here are composed of the immunoglobulin (Ig) domain found ...
26-99 4.95e-05

Immunoglobulin domain; The members here are composed of the immunoglobulin (Ig) domain found in the Ig superfamily. The Ig superfamily is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. Members of this group are components of immunoglobulin, neuroglia, cell surface glycoproteins, including T-cell receptors, CD2, CD4, CD8, and membrane glycoproteins, including butyrophilin and chondroitin sulfate proteoglycan core protein. A predominant feature of most Ig domains is a disulfide bridge connecting the two beta-sheets with a tryptophan residue packed against the disulfide bond. Ig superfamily (IgSF) domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. Typically, the V-set domains have A, B, E, and D strands in one sheet and A', G, F, C, C' and C" in the other. The structures in C1-set are smaller than those in the V-set; they have one beta sheet that is formed by strands A, B, E, and D and the other by strands G, F, C, and C'. Moreover, a C1-set Ig domain contains a short C' strand (three residues) and lacks A' and C" strand. Unlike other Ig domain sets, C2-set structures do not have a D strand. Like the V-set Ig domains, members of the I-set have a discontinuous A strand, but lack a C" strand.


Pssm-ID: 409353 [Multi-domain]  Cd Length: 70  Bit Score: 45.01  E-value: 4.95e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 281359561   26 LIFECQLLSSPKPDIEWFRSDNKVVEDVRTKFKIQPVgenkyTVVLELDDVVETDAGLYKVKAKNK-SGEVSASI 99
Cdd:cd00096     1 VTLTCSASGNPPPTITWYKNGKPLPPSSRDSRRSELG-----NGTLTISNVTLEDSGTYTCVASNSaGGSASASV 70
Ig_3 pfam13927
Immunoglobulin domain; This family contains immunoglobulin-like domains.
4379-4467 5.06e-05

Immunoglobulin domain; This family contains immunoglobulin-like domains.


Pssm-ID: 464046 [Multi-domain]  Cd Length: 78  Bit Score: 45.25  E-value: 5.06e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561  4379 KPIITKPRklapkidrkniRTYNFKSGEPIFLDINISGEPAPDVTWNQNNKSVQTTSFSHIENLPYNTKYINNNPERKDT 4458
Cdd:pfam13927    1 KPVITVSP-----------SSVTVREGETVTLTCEATGSPPPTITWYKNGEPISSGSTRSRSLSGSNSTLTISNVTRSDA 69

                   ....*....
gi 281359561  4459 GLYKISAHN 4467
Cdd:pfam13927   70 GTYTCVASN 78
IgI_Titin_like cd05747
Immunoglobulin (Ig)-like domain of human titin C terminus and similar proteins; member of the ...
4381-4478 5.25e-05

Immunoglobulin (Ig)-like domain of human titin C terminus and similar proteins; member of the I-set of Ig superfamily (IgSF) domains; The members here are composed of the fifth immunoglobulin (Ig)-like domain from the C-terminus of human titin x and similar proteins. Titin (also called connectin) is a fibrous sarcomeric protein specifically found in vertebrate striated muscle. Titin is gigantic; depending on isoform composition it ranges from 2970 to 3700 kDa, and is of a length that spans half a sarcomere. Titin largely consists of multiple repeats of Ig-like and fibronectin type 3 (FN-III)-like domains. Titin connects the ends of myosin thick filaments to Z disks and extends along the thick filament to the H zone and appears to function similar to an elastic band, keeping the myosin filaments centered in the sarcomere during muscle contraction or stretching. This group belongs to the I-set of IgSF domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand, but lack a C" strand.


Pssm-ID: 143224 [Multi-domain]  Cd Length: 92  Bit Score: 45.81  E-value: 5.25e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 4381 IITKPRKLApkidrknirtynFKSGEPIFLDINISGEPAPDVTWNQNNKSVQTTSFSHIENLPYNTKYINNNPERKDTGL 4460
Cdd:cd05747     6 ILTKPRSLT------------VSEGESARFSCDVDGEPAPTVTWMREGQIIVSSQRHQITSTEYKSTFEISKVQMSDEGN 73
                          90
                  ....*....|....*...
gi 281359561 4461 YKISAHNFYGQDQVEFQI 4478
Cdd:cd05747    74 YTVVVENSEGKQEAQFTL 91
IgI_2_Titin_Z1z2-like cd20972
Second Ig-like domain of the giant muscle protein titin Z1z2 in the sarcomeric Z-disk, and ...
7746-7833 5.34e-05

Second Ig-like domain of the giant muscle protein titin Z1z2 in the sarcomeric Z-disk, and similar domains; a member of the I-set of IgSF domains; The members here are composed of the second immunoglobulin (Ig)-like domain of the giant muscle protein titin Z1z2 in the sarcomeric Z-disk and similar proteins. Titin is a key component in the assembly and functioning of vertebrate striated muscles. By providing connections at the level of individual microfilaments, it contributes to the fine balance of forces between the two halves of the sarcomere. The Ig superfamily (IgSF) is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. Unlike the V-set, one of the distinctive features of I-set domains is the lack of a C" strand. The structure of the titin Z1z2 lacks this strand and thus it belongs to the I-set of the IgSF. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors, the hemolymph protein hemolin, the muscle proteins titin, telokin, and twitchin, the neuronal adhesion molecule axonin-1, and the signaling molecule semaphorin 4D that is involved in axonal guidance, immune function and angiogenesis.


Pssm-ID: 409564 [Multi-domain]  Cd Length: 91  Bit Score: 45.65  E-value: 5.34e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 7746 PPRF------RDTAyfdKGENVVIKIPFTGFPKPRIHWVRDGENIESGGHYTVEVKERHAVLIIRDGSHLDSGPYRITAE 7819
Cdd:cd20972     1 PPQFiqklrsQEVA---EGSKVRLECRVTGNPTPVVRWFCEGKELQNSPDIQIHQEGDLHSLIIAEAFEEDTGRYSCLAT 77
                          90
                  ....*....|....
gi 281359561 7820 NELGSDTAIIQVQI 7833
Cdd:cd20972    78 NSVGSDTTSAEIFV 91
IgI_Titin_like cd05747
Immunoglobulin (Ig)-like domain of human titin C terminus and similar proteins; member of the ...
656-729 5.57e-05

Immunoglobulin (Ig)-like domain of human titin C terminus and similar proteins; member of the I-set of Ig superfamily (IgSF) domains; The members here are composed of the fifth immunoglobulin (Ig)-like domain from the C-terminus of human titin x and similar proteins. Titin (also called connectin) is a fibrous sarcomeric protein specifically found in vertebrate striated muscle. Titin is gigantic; depending on isoform composition it ranges from 2970 to 3700 kDa, and is of a length that spans half a sarcomere. Titin largely consists of multiple repeats of Ig-like and fibronectin type 3 (FN-III)-like domains. Titin connects the ends of myosin thick filaments to Z disks and extends along the thick filament to the H zone and appears to function similar to an elastic band, keeping the myosin filaments centered in the sarcomere during muscle contraction or stretching. This group belongs to the I-set of IgSF domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand, but lack a C" strand.


Pssm-ID: 143224 [Multi-domain]  Cd Length: 92  Bit Score: 45.42  E-value: 5.57e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 281359561  656 TVVIECTVASKFEPKCTWYKETSTVKESKRHvyQVEQTkegEFAVKLEINDVEESDKGAYKLVASNEKGEAVSQ 729
Cdd:cd05747    20 SARFSCDVDGEPAPTVTWMREGQIIVSSQRH--QITST---EYKSTFEISKVQMSDEGNYTVVVENSEGKQEAQ 88
IgI_Titin_like cd05747
Immunoglobulin (Ig)-like domain of human titin C terminus and similar proteins; member of the ...
7649-7735 5.57e-05

Immunoglobulin (Ig)-like domain of human titin C terminus and similar proteins; member of the I-set of Ig superfamily (IgSF) domains; The members here are composed of the fifth immunoglobulin (Ig)-like domain from the C-terminus of human titin x and similar proteins. Titin (also called connectin) is a fibrous sarcomeric protein specifically found in vertebrate striated muscle. Titin is gigantic; depending on isoform composition it ranges from 2970 to 3700 kDa, and is of a length that spans half a sarcomere. Titin largely consists of multiple repeats of Ig-like and fibronectin type 3 (FN-III)-like domains. Titin connects the ends of myosin thick filaments to Z disks and extends along the thick filament to the H zone and appears to function similar to an elastic band, keeping the myosin filaments centered in the sarcomere during muscle contraction or stretching. This group belongs to the I-set of IgSF domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand, but lack a C" strand.


Pssm-ID: 143224 [Multi-domain]  Cd Length: 92  Bit Score: 45.42  E-value: 5.57e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 7649 LIVKPlRDANCIQNHNAQFTCTINGVPKPTISWYKGAREISNGARYHMYSEGDNHFLNINDVFGEDADEYVCRAVNKAGA 7728
Cdd:cd05747     6 ILTKP-RSLTVSEGESARFSCDVDGEPAPTVTWMREGQIIVSSQRHQITSTEYKSTFEISKVQMSDEGNYTVVVENSEGK 84

                  ....*..
gi 281359561 7729 KSTRATL 7735
Cdd:cd05747    85 QEAQFTL 91
IgI_Titin_like cd05747
Immunoglobulin (Ig)-like domain of human titin C terminus and similar proteins; member of the ...
6173-6249 5.62e-05

Immunoglobulin (Ig)-like domain of human titin C terminus and similar proteins; member of the I-set of Ig superfamily (IgSF) domains; The members here are composed of the fifth immunoglobulin (Ig)-like domain from the C-terminus of human titin x and similar proteins. Titin (also called connectin) is a fibrous sarcomeric protein specifically found in vertebrate striated muscle. Titin is gigantic; depending on isoform composition it ranges from 2970 to 3700 kDa, and is of a length that spans half a sarcomere. Titin largely consists of multiple repeats of Ig-like and fibronectin type 3 (FN-III)-like domains. Titin connects the ends of myosin thick filaments to Z disks and extends along the thick filament to the H zone and appears to function similar to an elastic band, keeping the myosin filaments centered in the sarcomere during muscle contraction or stretching. This group belongs to the I-set of IgSF domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand, but lack a C" strand.


Pssm-ID: 143224 [Multi-domain]  Cd Length: 92  Bit Score: 45.42  E-value: 5.62e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 281359561 6173 KRIKVRAGEPVNLNIPISGAPTPTIEWKRGDLKLEEGKRISYETNSERTLFRIDDSNRRDSGKYTVTAANEFGKDTA 6249
Cdd:cd05747    11 RSLTVSEGESARFSCDVDGEPAPTVTWMREGQIIVSSQRHQITSTEYKSTFEISKVQMSDEGNYTVVVENSEGKQEA 87
IgI_5_Robo cd20952
Fifth Ig-like domain of Roundabout (Robo) homolog 1/2, and similar domains; a member of the ...
8640-8713 5.63e-05

Fifth Ig-like domain of Roundabout (Robo) homolog 1/2, and similar domains; a member of the I-set of IgSF domains; The members here are composed of the fifth Ig-like domain of Roundabout (Robo) homolog 1/2 and similar domains. Robo receptors play a role in the development of the central nervous system (CNS), and are receptors of Slit protein. Slit is a repellant secreted by the neural cells in the midline. Slit acts through Robo to prevent most neurons from crossing the midline from either side. Three mammalian Robo homologs (Robo1, -2, and -3), and three mammalian Slit homologs (Slit-1,-2, -3), have been identified. Commissural axons, which cross the midline, express low levels of Robo; longitudinal axons, which avoid the midline, express high levels of Robo. Robo1, -2, and -3 are expressed by commissural neurons in the vertebrate spinal cord and Slits 1, -2, -3 are expressed at the ventral midline. Robo-3 is a divergent member of the Robo family which instead of being a positive regulator of slit responsiveness, antagonizes slit responsiveness in precrossing axons. The Slit-Robo interaction is mediated by the second leucine-rich repeat (LRR) domain of Slit and the two N-terminal Ig domains of Robo, Ig1 and Ig2. The primary Robo binding site for Slit2 has been shown by surface plasmon resonance experiments and mutational analysis to be is the Ig1 domain, while the Ig2 domain has been proposed to harbor a weak secondary binding site. The fifth Ig-like domain of Robo 1 and 2 is a member of the I-set Ig domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand but lack a C" strand. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors


Pssm-ID: 409544 [Multi-domain]  Cd Length: 87  Bit Score: 45.57  E-value: 5.63e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 281359561 8640 DLTIHDGEQLILTCYVKGDPEPQISWSKNGKSLSSSDILDLRYKNGiaTLTINEVFPEDEGVITCTATNSVGAV 8713
Cdd:cd20952     8 NQTVAVGGTVVLNCQATGEPVPTISWLKDGVPLLGKDERITTLENG--SLQIKGAEKSDTGEYTCVALNLSGEA 79
Ig4_Peroxidasin cd05746
Fourth immunoglobulin (Ig)-like domain of peroxidasin; The members here are composed of the ...
140-210 5.66e-05

Fourth immunoglobulin (Ig)-like domain of peroxidasin; The members here are composed of the fourth immunoglobulin (Ig)-like domain in peroxidasin. Peroxidasin has a peroxidase domain and interacting extracellular motifs containing four Ig-like domains. It has been suggested that peroxidasin is secreted, and has functions related to the stabilization of the extracellular matrix. It may play a part in various other important processes such as removal and destruction of cells which have undergone programmed cell death and protection of the organism against non-self.


Pssm-ID: 143223  Cd Length: 69  Bit Score: 44.87  E-value: 5.66e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 281359561  140 CRVNADPIPAIIWFHNGAAVKESERHKITVDkdvhsyfATLEILNVTVEDAGKYKVNAKNELGESNATISL 210
Cdd:cd05746     5 CSAQGDPEPTITWNKDGVQVTESGKFHISPE-------GYLAIRDVGVADQGRYECVARNTIGYASVSMVL 68
Ig cd00096
Immunoglobulin domain; The members here are composed of the immunoglobulin (Ig) domain found ...
2925-2991 5.67e-05

Immunoglobulin domain; The members here are composed of the immunoglobulin (Ig) domain found in the Ig superfamily. The Ig superfamily is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. Members of this group are components of immunoglobulin, neuroglia, cell surface glycoproteins, including T-cell receptors, CD2, CD4, CD8, and membrane glycoproteins, including butyrophilin and chondroitin sulfate proteoglycan core protein. A predominant feature of most Ig domains is a disulfide bridge connecting the two beta-sheets with a tryptophan residue packed against the disulfide bond. Ig superfamily (IgSF) domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. Typically, the V-set domains have A, B, E, and D strands in one sheet and A', G, F, C, C' and C" in the other. The structures in C1-set are smaller than those in the V-set; they have one beta sheet that is formed by strands A, B, E, and D and the other by strands G, F, C, and C'. Moreover, a C1-set Ig domain contains a short C' strand (three residues) and lacks A' and C" strand. Unlike other Ig domain sets, C2-set structures do not have a D strand. Like the V-set Ig domains, members of the I-set have a discontinuous A strand, but lack a C" strand.


Pssm-ID: 409353 [Multi-domain]  Cd Length: 70  Bit Score: 45.01  E-value: 5.67e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 281359561 2925 NVRGEPAPVITWYQNDKELKPEelpSSSEIKNIPYNTKISIIETVRKHTGIYKIIAVNEH-GQDEATV 2991
Cdd:cd00096     6 SASGNPPPTITWYKNGKPLPPS---SRDSRRSELGNGTLTISNVTLEDSGTYTCVASNSAgGSASASV 70
IgI_M-protein_C cd05891
C-terminal immunoglobulin (Ig)-like domain of M-protein; member of the I-set of Ig superfamily ...
4989-5069 5.84e-05

C-terminal immunoglobulin (Ig)-like domain of M-protein; member of the I-set of Ig superfamily (IgSF) domains; The members here are composed of the C-terminal immunoglobulin (Ig)-like domain of M-protein (also known as myomesin-2). M-protein is a structural protein localized to the M-band, a transverse structure in the center of the sarcomere, and is a candidate for M-band bridges. M-protein is modular consisting mainly of repetitive IG-like and fibronectin type III (FnIII) domains and has a muscle-type specific expression pattern. M-protein is present in fast fibers.


Pssm-ID: 143299  Cd Length: 92  Bit Score: 45.67  E-value: 5.84e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 4989 VRIKAGQSFTFDCKVSGEPAPQTKWLLKKKEVYSKDN--VKVTNVDYnTKLKVNSATRSDSGIYTVFAENANGEDSADVK 5066
Cdd:cd05891    11 VTIMEGKTLNLTCTVFGNPDPEVIWFKNDQDIELSEHysVKLEQGKY-ASLTIKGVTSEDSGKYSINVKNKYGGETVDVT 89

                  ...
gi 281359561 5067 VTV 5069
Cdd:cd05891    90 VSV 92
IgI_1_MuSK cd20970
agrin-responsive first immunoglobulin-like domains (Ig1) of the MuSK ectodomain; a member of ...
131-204 5.94e-05

agrin-responsive first immunoglobulin-like domains (Ig1) of the MuSK ectodomain; a member of the I-set of IgSF domains; The members here are composed of the first immunoglobulin-like domains (Ig1) of the Muscle-specific kinase (MuSK). MuSK is a receptor tyrosine kinase specifically expressed in skeletal muscle, where it plays a central role in the formation and maintenance of the neuromuscular junction (NMJ). MuSK is activated by agrin, a neuron-derived heparan sulfate proteoglycan. The activation of MUSK in myotubes regulates the formation of NMJs through the regulation of different processes including the specific expression of genes in subsynaptic nuclei, the reorganization of the actin cytoskeleton and the clustering of the acetylcholine receptors (AChR) in the postsynaptic membrane. The Ig superfamily (IgSF) is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. Unlike the V-set, one of the distinctive features of I-set domains is the lack of a C" strand. The structure of the MuSK lacks this strand and thus it belongs to the I-set of the IgSF. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors, the hemolymph protein hemolin, the muscle proteins titin, telokin, and twitchin, the neuronal adhesion molecule axonin-1, and the signaling molecule semaphorin 4D that is involved in axonal guidance, immune function and angiogenesis.


Pssm-ID: 409562 [Multi-domain]  Cd Length: 92  Bit Score: 45.58  E-value: 5.94e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 281359561  131 EDGKRLLFECRVNADPIPAIIWFHNGAAVKE-SERHKITVDKDvhsyfaTLEILNVTVEDAGKYKVNAKNELGES 204
Cdd:cd20970    15 REGENATFMCRAEGSPEPEISWTRNGNLIIEfNTRYIVRENGT------TLTIRNIRRSDMGIYLCIASNGVPGS 83
IgI_4_Dscam cd20956
Fourth immunoglobulin domain of the Drosophila melanogaster Dscam protein, and similar domains; ...
7668-7737 5.94e-05

Fourth immunoglobulin domain of the Drosophila melanogaster Dscam protein, and similar domains; a member of the I-set of IgSF domains; The members here are composed of the fourth immunoglobulin domain of the Drosophila melanogaster Down syndrome cell adhesion molecule (DSCAM) protein and similar proteins. Down syndrome cell adhesion molecule (DSCAM) is a cell adhesion molecule that plays critical roles in neural development, including axon guidance and branching, axon target recognition, self-avoidance and synaptic formation. DSCAM belongs to the immunoglobulin superfamily and contributes to defects in the central nervous system in Down syndrome patients. Vertebrate DSCAMs differ from Drosophila Dscam1 in that they lack the extensive alternative splicing that occurs in the insect gene. Drosophila melanogaster Dscam has 38,016 isoforms generated by the alternative splicing of four variable exon clusters, which allows every neuron in the fly to display a distinctive set of Dscam proteins on its cell surface. Drosophila Dscam1 is a cell-surface protein that plays important roles in neural development and axon tiling of neurons. It is shown that thousands of isoforms bind themselves through specific homophilic (self-binding) interactions, a process which mediates cellular self-recognition. Drosophila Dscam2 is also alternatively spliced and plays a key role in the development of two visual system neurons, monopolar cells L1 and L2. This group is a member of the I-set Ig domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand but lack a C" strand.


Pssm-ID: 409548 [Multi-domain]  Cd Length: 96  Bit Score: 45.63  E-value: 5.94e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 281359561 7668 TCTINGVPKPTISWYKGAREISNGARYHM--YSEGDNH---FLNINDVFGEDADEYVCRAVNKAGAKSTRATLAI 7737
Cdd:cd20956    22 KCVASGNPLPQITWTLDGFPIPESPRFRVgdYVTSDGDvvsYVNISSVRVEDGGEYTCTATNDVGSVSHSARINV 96
IgI_Titin_like cd05747
Immunoglobulin (Ig)-like domain of human titin C terminus and similar proteins; member of the ...
8435-8518 6.08e-05

Immunoglobulin (Ig)-like domain of human titin C terminus and similar proteins; member of the I-set of Ig superfamily (IgSF) domains; The members here are composed of the fifth immunoglobulin (Ig)-like domain from the C-terminus of human titin x and similar proteins. Titin (also called connectin) is a fibrous sarcomeric protein specifically found in vertebrate striated muscle. Titin is gigantic; depending on isoform composition it ranges from 2970 to 3700 kDa, and is of a length that spans half a sarcomere. Titin largely consists of multiple repeats of Ig-like and fibronectin type 3 (FN-III)-like domains. Titin connects the ends of myosin thick filaments to Z disks and extends along the thick filament to the H zone and appears to function similar to an elastic band, keeping the myosin filaments centered in the sarcomere during muscle contraction or stretching. This group belongs to the I-set of IgSF domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand, but lack a C" strand.


Pssm-ID: 143224 [Multi-domain]  Cd Length: 92  Bit Score: 45.42  E-value: 6.08e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 8435 TAPSfTFLLRPRVMQARD--TCKLLCCLSGKPVPNVRWYKDGREL-SKYEYAMTHSDGVVTMEIIDCKPSDSGKYSCKAT 8511
Cdd:cd05747     1 TLPA-TILTKPRSLTVSEgeSARFSCDVDGEPAPTVTWMREGQIIvSSQRHQITSTEYKSTFEISKVQMSDEGNYTVVVE 79

                  ....*..
gi 281359561 8512 NCHGTDE 8518
Cdd:cd05747    80 NSEGKQE 86
IgI_2_Robo cd05724
Second immunoglobulin (Ig)-like domain in Robo (roundabout) receptors; member of the I-set of ...
8462-8519 6.26e-05

Second immunoglobulin (Ig)-like domain in Robo (roundabout) receptors; member of the I-set of Ig superfamily (IgSF) domains; The members here are composed of the second immunoglobulin (Ig)-like domain in Robo (roundabout) receptors. Robo receptors play a role in the development of the central nervous system (CNS), and are receptors of the Slit protein. Slit is a repellant secreted by the neural cells in the midline. Slit acts through Robo to prevent most neurons from crossing the midline from either side. Three mammalian Robo homologs (Robo1, Robo2, and Robo3), and three mammalian Slit homologs (Slit-1,Slit-2, Slit-3), have been identified. Commissural axons, which cross the midline, express low levels of Robo; longitudinal axons, which avoid the midline, express high levels of Robo. Robo1, Robo2, and Robo3 are expressed by commissural neurons in the vertebrate spinal cord and Slit-1, Slit-2, Slit-3 are expressed at the ventral midline. Robo-3 is a divergent member of the Robo family which instead of being a positive regulator of Slit responsiveness, antagonizes Slit responsiveness in precrossing axons. The Slit-Robo interaction is mediated by the second leucine-rich repeat (LRR) domain of Slit and the two N-terminal Ig domains of Robo, Ig1 and Ig2. The primary Robo binding site for Slit-2 has been shown by surface plasmon resonance experiments and mutational analysis to be the Ig1 domain, while the Ig2 domain has been proposed to harbor a weak secondary binding site. This group belongs to the I-set of IgSF domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand, but lack a C" strand.


Pssm-ID: 409389 [Multi-domain]  Cd Length: 87  Bit Score: 45.08  E-value: 6.26e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 281359561 8462 GKPVPNVRWYKDGREL-SKYEYAMTHSDGvvTMEIIDCKPSDSGKYSCKATNCHGTDET 8519
Cdd:cd05724    24 GHPEPTVSWRKDGQPLnLDNERVRIVDDG--NLLIAEARKSDEGTYKCVATNMVGERES 80
IgI_1_Titin_Z1z2-like cd20974
First Ig-like domain of the giant muscle protein titin Z1z2 in the sarcomeric Z-disk and ...
6566-6651 6.50e-05

First Ig-like domain of the giant muscle protein titin Z1z2 in the sarcomeric Z-disk and similar proteins; a member of the I-set of IgSF domains; The members here are composed of the first immunoglobulin (Ig)-like domain of the giant muscle protein titin Z1z2 in the sarcomeric Z-disk and similar proteins. Titin is a key component in the assembly and functioning of vertebrate striated muscles. By providing connections at the level of individual microfilaments, it contributes to the fine balance of forces between the two halves of the sarcomere. The Ig superfamily (IgSF) is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. Unlike the V-set, one of the distinctive features of I-set domains is the lack of a C" strand. The structure of the titin Z1z2 lacks this strand and thus it belongs to the I-set of the IgSF. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors, the hemolymph protein hemolin, the muscle proteins titin, telokin, and twitchin, the neuronal adhesion molecule axonin-1, and the signaling molecule semaphorin 4D that is involved in axonal guidance, immune function and angiogenesis.


Pssm-ID: 409566 [Multi-domain]  Cd Length: 93  Bit Score: 45.42  E-value: 6.50e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 6566 KVRDIVCRAGDDFSIHVPYLAFPKPNAFWYSNDNMLDDNN--RVHKHLTDDAASVVVKNSKRADSGQYRLQLKNTSGFDT 6643
Cdd:cd20974     6 PLQSVVVLEGSTATFEAHVSGKPVPEVSWFRDGQVISTSTlpGVQISFSDGRAKLSIPAVTKANSGRYSLTATNGSGQAT 85

                  ....*...
gi 281359561 6644 ATINVRVL 6651
Cdd:cd20974    86 STAELLVL 93
ig pfam00047
Immunoglobulin domain; Members of the immunoglobulin superfamily are found in hundreds of ...
8751-8816 6.55e-05

Immunoglobulin domain; Members of the immunoglobulin superfamily are found in hundreds of proteins of different functions. Examples include antibodies, the giant muscle kinase titin and receptor tyrosine kinases. Immunoglobulin-like domains may be involved in protein-protein and protein-ligand interactions.


Pssm-ID: 395002  Cd Length: 86  Bit Score: 45.26  E-value: 6.55e-05
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 281359561  8751 VRDGDAVNLACRIIGAQHF-DVVWLHNNKEIK-PSKDFQYTNEANIYRLQIAEIFPEDGGTYTCEAFN 8816
Cdd:pfam00047    8 VLEGDSATLTCSASTGSPGpDVTWSKEGGTLIeSLKVKHDNGRTTQSSLLISNVTKEDAGTYTCVVNN 75
COG4733 COG4733
Phage-related protein, tail protein J [Mobilome: prophages, transposons];
5628-5847 6.58e-05

Phage-related protein, tail protein J [Mobilome: prophages, transposons];


Pssm-ID: 443767 [Multi-domain]  Cd Length: 978  Bit Score: 50.33  E-value: 6.58e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 5628 FEIVSSLRSDEGRYTLILKNEHGSFDASAHATVLDRPSPPKGPLDITK-----ITRDGC-----HLTWNVPDDDGGSPIL 5697
Cdd:COG4733   491 FRVVSIEENEDGTYTITAVQHAPEKYAAIDAGAFDDVPPQWPPVNVTTseslsVVAQGTavttlTVSWDAPAGAVAYEVE 570
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 5698 HYIiekmdlSRSTWSDAGMSTHIVHDVTRLVHRkEYLFRVKAVNAIG-ESDPLEAVNTIIAkneFDEpDAPGKP--IITD 5774
Cdd:COG4733   571 WRR------DDGNWVSVPRTSGTSFEVPGIYAG-DYEVRVRAINALGvSSAWAASSETTVT---GKT-APPPAPtgLTAT 639
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 281359561 5775 WDRDHIDLQWAVPKsdgGAPISEYIIQKKEKGSPYWTNVRHVPSNKNTTTIPELTEGQEYEFRVIAVNQAGQS 5847
Cdd:COG4733   640 GGLGGITLSWSFPV---DADTLRTEIRYSTTGDWASATVAQALYPGNTYTLAGLKAGQTYYYRARAVDRSGNV 709
IgI_Myomesin_like_C cd05737
C-terminal immunoglobulin (Ig)-like domain of myomesin and M-protein; member of the I-set of ...
3810-3885 6.88e-05

C-terminal immunoglobulin (Ig)-like domain of myomesin and M-protein; member of the I-set of Ig superfamily (IgSF) domains; The members here are composed of the C-terminal immunoglobulin (Ig)-like domain of myomesin and M-protein (also known as myomesin-2). Myomesin and M-protein are both structural proteins localized to the M-band, a transverse structure in the center of the sarcomere, and are candidates for M-band bridges. Both proteins are modular, consisting mainly of repetitive Ig-like and fibronectin type III (FnIII) domains. Myomesin is expressed in all types of vertebrate striated muscle; M-protein has a muscle-type specific expression pattern. Myomesin is present in both slow and fast fibers; M-protein is present only in fast fibers. It has been suggested that myomesin acts as a molecular spring with alternative splicing as a means of modifying its elasticity.


Pssm-ID: 319300  Cd Length: 92  Bit Score: 45.27  E-value: 6.88e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 281359561 3810 GQMLHIDALIKAEPPAKVTWTYNKTEIKTSDHIKIENEDYKT-TFIMPKVKRADRGIYIVTAKNDSGSDTVEVELEV 3885
Cdd:cd05737    16 GKTLNLTCNVWGDPPPEVSWLKNDQALAFLDHCNLKVEAGRTvYFTINGVSSEDSGKYGLVVKNKYGSETSDVTVSV 92
IgI_Myotilin_C_like cd05744
Immunoglobulin (Ig)-like domain of myotilin, palladin, and myopalladin; member of the I-set of ...
2315-2395 7.38e-05

Immunoglobulin (Ig)-like domain of myotilin, palladin, and myopalladin; member of the I-set of Ig superfamily (IgSF) domains; The members here are composed of the immunoglobulin (Ig)-like domain in myotilin, palladin, and myopalladin. Myotilin, palladin, and myopalladin function as scaffolds that regulate actin organization. Myotilin and myopalladin are most abundant in skeletal and cardiac muscle; palladin is ubiquitously expressed in the organs of developing vertebrates and plays a key role in cellular morphogenesis. The three family members each interact with specific molecular partners with all three binding to alpha-actinin; In addition, palladin also binds to vasodilator-stimulated phosphoprotein (VASP) and ezrin, myotilin binds to filamin and actin, and myopalladin also binds to nebulin and cardiac ankyrin repeat protein (CARP). This group belongs to the I-set of IgSF domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand, but lack a C" strand.


Pssm-ID: 409405 [Multi-domain]  Cd Length: 91  Bit Score: 45.18  E-value: 7.38e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 2315 TVKKGQTIRFDIKYDGEPEPAATWVKGTDNLKFDNQRICLDQLERNSSITIKKSVRKDTGKYKLVLSNSSGTIESEAQVV 2394
Cdd:cd05744    11 EVQEGRLCRFDCKVSGLPTPDLFWQLNGKPVRPDSAHKMLVRENGRHSLIIEPVTKRDAGIYTCIARNRAGENSFNAELV 90

                  .
gi 281359561 2395 V 2395
Cdd:cd05744    91 V 91
IgI_5_Dscam cd20958
Fifth immunoglobulin domain of the Drosophila melanogaster Dscam protein, and similar domains; ...
234-312 7.45e-05

Fifth immunoglobulin domain of the Drosophila melanogaster Dscam protein, and similar domains; a member of the I-set of IgSF domains; The members here are composed of the fifth immunoglobulin domain of the Drosophila melanogaster Down syndrome cell adhesion molecule (DSCAM) protein and similar proteins. Down syndrome cell adhesion molecule (DSCAM) is a cell adhesion molecule that plays critical roles in neural development, including axon guidance and branching, axon target recognition, self-avoidance and synaptic formation. DSCAM belongs to the immunoglobulin superfamily and contributes to defects in the central nervous system in Down syndrome patients. Vertebrate DSCAMs differ from Drosophila Dscam1 in that they lack the extensive alternative splicing that occurs in the insect gene. Drosophila melanogaster Dscam has 38,016 isoforms generated by the alternative splicing of four variable exon clusters, which allows every neuron in the fly to display a distinctive set of Dscam proteins on its cell surface. Drosophila Dscam1 is a cell-surface protein that plays important roles in neural development and axon tiling of neurons. It is shown that thousands of isoforms bind themselves through specific homophilic (self-binding) interactions, a process which mediates cellular self-recognition. Drosophila Dscam2 is also alternatively spliced and plays a key role in the development of two visual system neurons, monopolar cells L1 and L2. This group is a member of the I-set Ig domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand but lack a C" strand.


Pssm-ID: 409550 [Multi-domain]  Cd Length: 89  Bit Score: 45.25  E-value: 7.45e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561  234 PVIRQSED-----GGNVTFECRCVGDPTPTVTWSHGETELNESNRykmsltmdQKLYHIACLEISSVV-SSDQGEYRAQA 307
Cdd:cd20958     2 PFIRPMGNltavaGQTLRLHCPVAGYPISSITWEKDGRRLPLNHR--------QRVFPNGTLVIENVQrSSDEGEYTCTA 73

                  ....*
gi 281359561  308 KNKHG 312
Cdd:cd20958    74 RNQQG 78
IgI_1_MuSK cd20970
agrin-responsive first immunoglobulin-like domains (Ig1) of the MuSK ectodomain; a member of ...
557-623 7.58e-05

agrin-responsive first immunoglobulin-like domains (Ig1) of the MuSK ectodomain; a member of the I-set of IgSF domains; The members here are composed of the first immunoglobulin-like domains (Ig1) of the Muscle-specific kinase (MuSK). MuSK is a receptor tyrosine kinase specifically expressed in skeletal muscle, where it plays a central role in the formation and maintenance of the neuromuscular junction (NMJ). MuSK is activated by agrin, a neuron-derived heparan sulfate proteoglycan. The activation of MUSK in myotubes regulates the formation of NMJs through the regulation of different processes including the specific expression of genes in subsynaptic nuclei, the reorganization of the actin cytoskeleton and the clustering of the acetylcholine receptors (AChR) in the postsynaptic membrane. The Ig superfamily (IgSF) is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. Unlike the V-set, one of the distinctive features of I-set domains is the lack of a C" strand. The structure of the MuSK lacks this strand and thus it belongs to the I-set of the IgSF. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors, the hemolymph protein hemolin, the muscle proteins titin, telokin, and twitchin, the neuronal adhesion molecule axonin-1, and the signaling molecule semaphorin 4D that is involved in axonal guidance, immune function and angiogenesis.


Pssm-ID: 409562 [Multi-domain]  Cd Length: 92  Bit Score: 45.19  E-value: 7.58e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 281359561  557 GKLVIMECKVKADPKPDVIWFRNGEVIKESNKiKTFIEQRGDQyyikLELLDPQLEDSGLYKCNIKN 623
Cdd:cd20970    17 GENATFMCRAEGSPEPEISWTRNGNLIIEFNT-RYIVRENGTT----LTIRNIRRSDMGIYLCIASN 78
IgI_APEG-1_like cd20975
Immunoglobulin-like domain of human Aortic Preferentially Expressed Protein-1 (APEG-1) and ...
6177-6245 7.63e-05

Immunoglobulin-like domain of human Aortic Preferentially Expressed Protein-1 (APEG-1) and similar proteins; a member of the I-set of IgSF domains; The members here are composed of the immunoglobulin I-set (IgI) domain of the Human Aortic Preferentially Expressed Protein-1 (APEG-1) and similar proteins. APEG-1 is a novel specific smooth muscle differentiation marker predicted to play a role in the growth and differentiation of arterial smooth muscle cells (SMCs). The Ig superfamily (IgSF) is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. Unlike the V-set, one of the distinctive features of I-set domains is the lack of a C" strand. The structure of the human APEG-1 lacks this strand and thus it belongs to the I-set of the IgSF. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors, the hemolymph protein hemolin, the muscle proteins titin, telokin, and twitchin, the neuronal adhesion molecule axonin-1, and the signaling molecule semaphorin 4D that is involved in axonal guidance, immune function and angiogenesis.


Pssm-ID: 409567  Cd Length: 91  Bit Score: 45.15  E-value: 7.63e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 6177 VRAGEPVNLNIPISGAPTPTIEWKRGDLKLE-EGKRISYETNSERTLFRIDDSNRRDSGKYTVTAANEFG 6245
Cdd:cd20975    12 VREGQDVIMSIRVQGEPKPVVSWLRNRQPVRpDQRRFAEEAEGGLCRLRILAAERGDAGFYTCKAVNEYG 81
IgI_M-protein_C cd05891
C-terminal immunoglobulin (Ig)-like domain of M-protein; member of the I-set of Ig superfamily ...
2612-2693 7.68e-05

C-terminal immunoglobulin (Ig)-like domain of M-protein; member of the I-set of Ig superfamily (IgSF) domains; The members here are composed of the C-terminal immunoglobulin (Ig)-like domain of M-protein (also known as myomesin-2). M-protein is a structural protein localized to the M-band, a transverse structure in the center of the sarcomere, and is a candidate for M-band bridges. M-protein is modular consisting mainly of repetitive IG-like and fibronectin type III (FnIII) domains and has a muscle-type specific expression pattern. M-protein is present in fast fibers.


Pssm-ID: 143299  Cd Length: 92  Bit Score: 45.29  E-value: 7.68e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 2612 VTIKSGRTHKWSVDVLGEPIPELHWSWRD-DIPLTNGDRIKIENVDYhTDFSITNVLRKDSGFYTLKAENRNGidRETVE 2690
Cdd:cd05891    11 VTIMEGKTLNLTCTVFGNPDPEVIWFKNDqDIELSEHYSVKLEQGKY-ASLTIKGVTSEDSGKYSINVKNKYG--GETVD 87

                  ...
gi 281359561 2691 LVV 2693
Cdd:cd05891    88 VTV 90
Ig_Pro_neuregulin cd05750
Immunoglobulin (Ig)-like domain in neuregulins; The members here are composed of the ...
557-638 7.71e-05

Immunoglobulin (Ig)-like domain in neuregulins; The members here are composed of the immunoglobulin (Ig)-like domain in neuregulins (NRGs). NRGs are signaling molecules which participate in cell-cell interactions in the nervous system, breast, heart, and other organ systems, and are implicated in the pathology of diseases including schizophrenia, multiple sclerosis, and breast cancer. There are four members of the neuregulin gene family (NRG-1, NRG-2, NRG-3, and NRG-4). The NRG-1 protein, binds to and activates the tyrosine kinases receptors ErbB3 and ErbB4, initiating signaling cascades. The other NRGs proteins bind one or the other or both of these ErbBs. NRG-1 has multiple functions: in the brain it regulates various processes such as radial glia formation and neuronal migration, dendritic development, and expression of neurotransmitters receptors, while in the peripheral nervous system NRG-1 regulates processes such as target cell differentiation, and Schwann cell survival. There are many NRG-1 isoforms which arise from the alternative splicing of mRNA. Less is known of the functions of the other NRGs. NRG-2 and NRG-3 are expressed predominantly in the nervous system. NRG-2 is expressed by motor neurons and terminal Schwann cells, and is concentrated near synaptic sites and may be a signal that regulates synaptic differentiation. NRG-4 has been shown to direct pancreatic islet cell development towards the delta-cell lineage.


Pssm-ID: 409408 [Multi-domain]  Cd Length: 92  Bit Score: 45.19  E-value: 7.71e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561  557 GKLVIMECKVKAD-PKPDVIWFRNGEVIKESNKIKtfIEQRGDQYYIKLELLDPQLEDSGLYKCNIKNTLGelNANLTLN 635
Cdd:cd05750    14 GSKLVLKCEATSEnPSPRYRWFKDGKELNRKRPKN--IKIRNKKKNSELQINKAKLEDSGEYTCVVENILG--KDTVTGN 89

                  ...
gi 281359561  636 IEI 638
Cdd:cd05750    90 VTV 92
IgI_Titin_like cd05747
Immunoglobulin (Ig)-like domain of human titin C terminus and similar proteins; member of the ...
3503-3589 7.76e-05

Immunoglobulin (Ig)-like domain of human titin C terminus and similar proteins; member of the I-set of Ig superfamily (IgSF) domains; The members here are composed of the fifth immunoglobulin (Ig)-like domain from the C-terminus of human titin x and similar proteins. Titin (also called connectin) is a fibrous sarcomeric protein specifically found in vertebrate striated muscle. Titin is gigantic; depending on isoform composition it ranges from 2970 to 3700 kDa, and is of a length that spans half a sarcomere. Titin largely consists of multiple repeats of Ig-like and fibronectin type 3 (FN-III)-like domains. Titin connects the ends of myosin thick filaments to Z disks and extends along the thick filament to the H zone and appears to function similar to an elastic band, keeping the myosin filaments centered in the sarcomere during muscle contraction or stretching. This group belongs to the I-set of IgSF domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand, but lack a C" strand.


Pssm-ID: 143224 [Multi-domain]  Cd Length: 92  Bit Score: 45.04  E-value: 7.76e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 3503 RVNLKP--VIVKTGLSISLDINIRGEPAPKVEWFFNNSS-VTSDEHsvKIDNVDYNTKFFVMRAQRSQSGKYIIKATNEV 3579
Cdd:cd05747     5 TILTKPrsLTVSEGESARFSCDVDGEPAPTVTWMREGQIiVSSQRH--QITSTEYKSTFEISKVQMSDEGNYTVVVENSE 82
                          90
                  ....*....|
gi 281359561 3580 GEDEAELEVT 3589
Cdd:cd05747    83 GKQEAQFTLT 92
IgI_Titin_like cd05747
Immunoglobulin (Ig)-like domain of human titin C terminus and similar proteins; member of the ...
1496-1586 7.76e-05

Immunoglobulin (Ig)-like domain of human titin C terminus and similar proteins; member of the I-set of Ig superfamily (IgSF) domains; The members here are composed of the fifth immunoglobulin (Ig)-like domain from the C-terminus of human titin x and similar proteins. Titin (also called connectin) is a fibrous sarcomeric protein specifically found in vertebrate striated muscle. Titin is gigantic; depending on isoform composition it ranges from 2970 to 3700 kDa, and is of a length that spans half a sarcomere. Titin largely consists of multiple repeats of Ig-like and fibronectin type 3 (FN-III)-like domains. Titin connects the ends of myosin thick filaments to Z disks and extends along the thick filament to the H zone and appears to function similar to an elastic band, keeping the myosin filaments centered in the sarcomere during muscle contraction or stretching. This group belongs to the I-set of IgSF domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand, but lack a C" strand.


Pssm-ID: 143224 [Multi-domain]  Cd Length: 92  Bit Score: 45.04  E-value: 7.76e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 1496 PPSIVDVQESYSVVEDSTAYLTVGVEGSPAPTFKFYKGVSEILEGGRFKFLTDGQTNTITLcmRKCKPNDESKYKIVVSN 1575
Cdd:cd05747     3 PATILTKPRSLTVSEGESARFSCDVDGEPAPTVTWMREGQIIVSSQRHQITSTEYKSTFEI--SKVQMSDEGNYTVVVEN 80
                          90
                  ....*....|.
gi 281359561 1576 IHGEDSAEMQL 1586
Cdd:cd05747    81 SEGKQEAQFTL 91
IgI_titin_I1-like cd20951
Immunoglobulin domain I1 of the titin I-band and similar proteins; a member of the I-set of ...
3208-3283 7.91e-05

Immunoglobulin domain I1 of the titin I-band and similar proteins; a member of the I-set of IgSF domains; The members here are composed of the immunoglobulin domain I1 of the titin I-band and similar proteins. Titin is a key component in the assembly and functioning of vertebrate striated muscles. By providing connections at the level of individual microfilaments, it contributes to the fine balance of forces between the two halves of the sarcomere. The Ig superfamily (IgSF) is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. The two sheets are linked together by a conserved disulfide bond between B strand and F strand. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. The Ig I1 domain of the titin I-band is a member of the I-set Ig domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand but lack a C" strand. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors, the hemolymph protein hemolin, the muscle proteins titin, telokin, and twitchin, the neuronal adhesion molecule axonin-1, and the signaling molecule semaphorin 4D that is involved in axonal guidance, immune function and angiogenesis.


Pssm-ID: 409543 [Multi-domain]  Cd Length: 94  Bit Score: 45.10  E-value: 7.91e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 281359561 3208 KMKPIKVRAGQPVKFDVDVKGEPAPSLTWFLKETELTSTGQVR---LENIDYNTKLTLLDTDRKQSGQYKLRAENINGV 3283
Cdd:cd20951     6 RLQSHTVWEKSDAKLRVEVQGKPDPEVKWYKNGVPIDPSSIPGkykIESEYGVHVLHIRRVTVEDSAVYSAVAKNIHGE 84
IG_like smart00410
Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.
656-730 8.09e-05

Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.


Pssm-ID: 214653 [Multi-domain]  Cd Length: 85  Bit Score: 44.80  E-value: 8.09e-05
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 281359561    656 TVVIECTVASKFEPKCTWYKET-STVKESKRhvYQVEQTKegeFAVKLEINDVEESDKGAYKLVASNEKGEAVSQI 730
Cdd:smart00410   11 SVTLSCEASGSPPPEVTWYKQGgKLLAESGR--FSVSRSG---STSTLTISNVTPEDSGTYTCAATNSSGSASSGT 81
Ig cd00096
Immunoglobulin domain; The members here are composed of the immunoglobulin (Ig) domain found ...
1842-1909 8.24e-05

Immunoglobulin domain; The members here are composed of the immunoglobulin (Ig) domain found in the Ig superfamily. The Ig superfamily is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. Members of this group are components of immunoglobulin, neuroglia, cell surface glycoproteins, including T-cell receptors, CD2, CD4, CD8, and membrane glycoproteins, including butyrophilin and chondroitin sulfate proteoglycan core protein. A predominant feature of most Ig domains is a disulfide bridge connecting the two beta-sheets with a tryptophan residue packed against the disulfide bond. Ig superfamily (IgSF) domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. Typically, the V-set domains have A, B, E, and D strands in one sheet and A', G, F, C, C' and C" in the other. The structures in C1-set are smaller than those in the V-set; they have one beta sheet that is formed by strands A, B, E, and D and the other by strands G, F, C, and C'. Moreover, a C1-set Ig domain contains a short C' strand (three residues) and lacks A' and C" strand. Unlike other Ig domain sets, C2-set structures do not have a D strand. Like the V-set Ig domains, members of the I-set have a discontinuous A strand, but lack a C" strand.


Pssm-ID: 409353 [Multi-domain]  Cd Length: 70  Bit Score: 44.24  E-value: 8.24e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 1842 VTLACEID-DAMGEVQWLRNGEEIKPDKRIQIVKDGRKRKLVIKDCKVTDAGQFKCT-TNADTTESEIII 1909
Cdd:cd00096     1 VTLTCSASgNPPPTITWYKNGKPLPPSSRDSRRSELGNGTLTISNVTLEDSGTYTCVaSNSAGGSASASV 70
IgI_5_Dscam cd20958
Fifth immunoglobulin domain of the Drosophila melanogaster Dscam protein, and similar domains; ...
8458-8515 8.30e-05

Fifth immunoglobulin domain of the Drosophila melanogaster Dscam protein, and similar domains; a member of the I-set of IgSF domains; The members here are composed of the fifth immunoglobulin domain of the Drosophila melanogaster Down syndrome cell adhesion molecule (DSCAM) protein and similar proteins. Down syndrome cell adhesion molecule (DSCAM) is a cell adhesion molecule that plays critical roles in neural development, including axon guidance and branching, axon target recognition, self-avoidance and synaptic formation. DSCAM belongs to the immunoglobulin superfamily and contributes to defects in the central nervous system in Down syndrome patients. Vertebrate DSCAMs differ from Drosophila Dscam1 in that they lack the extensive alternative splicing that occurs in the insect gene. Drosophila melanogaster Dscam has 38,016 isoforms generated by the alternative splicing of four variable exon clusters, which allows every neuron in the fly to display a distinctive set of Dscam proteins on its cell surface. Drosophila Dscam1 is a cell-surface protein that plays important roles in neural development and axon tiling of neurons. It is shown that thousands of isoforms bind themselves through specific homophilic (self-binding) interactions, a process which mediates cellular self-recognition. Drosophila Dscam2 is also alternatively spliced and plays a key role in the development of two visual system neurons, monopolar cells L1 and L2. This group is a member of the I-set Ig domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand but lack a C" strand.


Pssm-ID: 409550 [Multi-domain]  Cd Length: 89  Bit Score: 44.87  E-value: 8.30e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 281359561 8458 CCLSGKPVPNVRWYKDGRELSKYEYAMTHSDGVVTMEIIDcKPSDSGKYSCKATNCHG 8515
Cdd:cd20958    22 CPVAGYPISSITWEKDGRRLPLNHRQRVFPNGTLVIENVQ-RSSDEGEYTCTARNQQG 78
Ig4_L1-NrCAM_like cd04978
Fourth immunoglobulin (Ig)-like domain of L1, Ng-CAM (Neuron-glia CAM cell adhesion molecule), ...
441-532 8.30e-05

Fourth immunoglobulin (Ig)-like domain of L1, Ng-CAM (Neuron-glia CAM cell adhesion molecule), and NrCAM (Ng-CAM-related); The members here are composed of the fourth immunoglobulin (Ig)-like domain of L1, Ng-CAM (Neuron-glia CAM cell adhesion molecule), and NrCAM (Ng-CAM-related). These proteins belong to the L1 subfamily of cell adhesion molecules (CAMs) and are comprised of an extracellular region having six Ig-like domains and five fibronectin type III domains, a transmembrane region and an intracellular domain. These molecules are primarily expressed in the nervous system. L1 is associated with an X-linked recessive disorder, X-linked hydrocephalus, MASA syndrome, or spastic paraplegia type 1, that involves abnormalities of axonal growth.


Pssm-ID: 409367 [Multi-domain]  Cd Length: 89  Bit Score: 45.13  E-value: 8.30e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561  441 IEKPRII--PNESGTLItmkCKCKAKPEPTVTWyrgqdlvekskkiKINTTVIAE---------DTYELTLEIKDPGATd 509
Cdd:cd04978     4 IEPPSLVlsPGETGELI---CEAEGNPQPTITW-------------RLNGVPIEPapedmrrtvDGRTLIFSNLQPNDT- 66
                          90       100
                  ....*....|....*....|...
gi 281359561  510 gGTYRCNVKNEYGESNANLNLNI 532
Cdd:cd04978    67 -AVYQCNASNVHGYLLANAFLHV 88
Ig cd00096
Immunoglobulin domain; The members here are composed of the immunoglobulin (Ig) domain found ...
4708-4765 8.32e-05

Immunoglobulin domain; The members here are composed of the immunoglobulin (Ig) domain found in the Ig superfamily. The Ig superfamily is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. Members of this group are components of immunoglobulin, neuroglia, cell surface glycoproteins, including T-cell receptors, CD2, CD4, CD8, and membrane glycoproteins, including butyrophilin and chondroitin sulfate proteoglycan core protein. A predominant feature of most Ig domains is a disulfide bridge connecting the two beta-sheets with a tryptophan residue packed against the disulfide bond. Ig superfamily (IgSF) domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. Typically, the V-set domains have A, B, E, and D strands in one sheet and A', G, F, C, C' and C" in the other. The structures in C1-set are smaller than those in the V-set; they have one beta sheet that is formed by strands A, B, E, and D and the other by strands G, F, C, and C'. Moreover, a C1-set Ig domain contains a short C' strand (three residues) and lacks A' and C" strand. Unlike other Ig domain sets, C2-set structures do not have a D strand. Like the V-set Ig domains, members of the I-set have a discontinuous A strand, but lack a C" strand.


Pssm-ID: 409353 [Multi-domain]  Cd Length: 70  Bit Score: 44.24  E-value: 8.32e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 281359561 4708 NITGEPAPKVEWKLSNYHLQSGKNVTIETPDYYTKLVIRPTQRSDSGEYLVTATNTSG 4765
Cdd:cd00096     6 SASGNPPPTITWYKNGKPLPPSSRDSRRSELGNGTLTISNVTLEDSGTYTCVASNSAG 63
Ig_Pro_neuregulin cd05750
Immunoglobulin (Ig)-like domain in neuregulins; The members here are composed of the ...
123-210 8.34e-05

Immunoglobulin (Ig)-like domain in neuregulins; The members here are composed of the immunoglobulin (Ig)-like domain in neuregulins (NRGs). NRGs are signaling molecules which participate in cell-cell interactions in the nervous system, breast, heart, and other organ systems, and are implicated in the pathology of diseases including schizophrenia, multiple sclerosis, and breast cancer. There are four members of the neuregulin gene family (NRG-1, NRG-2, NRG-3, and NRG-4). The NRG-1 protein, binds to and activates the tyrosine kinases receptors ErbB3 and ErbB4, initiating signaling cascades. The other NRGs proteins bind one or the other or both of these ErbBs. NRG-1 has multiple functions: in the brain it regulates various processes such as radial glia formation and neuronal migration, dendritic development, and expression of neurotransmitters receptors, while in the peripheral nervous system NRG-1 regulates processes such as target cell differentiation, and Schwann cell survival. There are many NRG-1 isoforms which arise from the alternative splicing of mRNA. Less is known of the functions of the other NRGs. NRG-2 and NRG-3 are expressed predominantly in the nervous system. NRG-2 is expressed by motor neurons and terminal Schwann cells, and is concentrated near synaptic sites and may be a signal that regulates synaptic differentiation. NRG-4 has been shown to direct pancreatic islet cell development towards the delta-cell lineage.


Pssm-ID: 409408 [Multi-domain]  Cd Length: 92  Bit Score: 45.19  E-value: 8.34e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561  123 KKPAIRQEEDGKRLLFECRVNAD-PIPAIIWFHNGAAVKESERHKITVDKDVHSyfATLEILNVTVEDAGKYKVNAKNEL 201
Cdd:cd05750     4 KEMKSQTVQEGSKLVLKCEATSEnPSPRYRWFKDGKELNRKRPKNIKIRNKKKN--SELQINKAKLEDSGEYTCVVENIL 81

                  ....*....
gi 281359561  202 GESNATISL 210
Cdd:cd05750    82 GKDTVTGNV 90
IgI_4_MYLK-like cd20976
Fourth Ig-like domain from smooth muscle myosin light chain kinase and similar domains ; a ...
118-211 8.42e-05

Fourth Ig-like domain from smooth muscle myosin light chain kinase and similar domains ; a member of the I-set of IgSF domains; The members here are composed of the fourth immunoglobulin (Ig)-like domain from smooth muscle myosin light chain kinase (MYLK) and similar domains. The Ig superfamily (IgSF) is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. Unlike the V-set, one of the distinctive features of I-set domains is the lack of a C" strand. The structure of this group shows that the fourth Ig-like domain from myosin light chain kinase lacks this strand and thus belongs to the I-set of the IgSF. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors, the hemolymph protein hemolin, the muscle proteins titin, telokin, and twitchin, the neuronal adhesion molecule axonin-1, and the signaling molecule semaphorin 4D that is involved in axonal guidance, immune function and angiogenesis.


Pssm-ID: 409568 [Multi-domain]  Cd Length: 90  Bit Score: 44.93  E-value: 8.42e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561  118 APTFAKKPAIRQEEDGKRLLFECRVNADPIPAIIWFHNGAAVKESERHkITVDKDVhsyfATLEILNVTVEDAGKYKVNA 197
Cdd:cd20976     1 APSFSSVPKDLEAVEGQDFVAQCSARGKPVPRITWIRNAQPLQYAADR-STCEAGV----GELHIQDVLPEDHGTYTCLA 75
                          90
                  ....*....|....
gi 281359561  198 KNELGESNATISLN 211
Cdd:cd20976    76 KNAAGQVSCSAWVT 89
IgI_Myotilin_C_like cd05744
Immunoglobulin (Ig)-like domain of myotilin, palladin, and myopalladin; member of the I-set of ...
4410-4480 8.54e-05

Immunoglobulin (Ig)-like domain of myotilin, palladin, and myopalladin; member of the I-set of Ig superfamily (IgSF) domains; The members here are composed of the immunoglobulin (Ig)-like domain in myotilin, palladin, and myopalladin. Myotilin, palladin, and myopalladin function as scaffolds that regulate actin organization. Myotilin and myopalladin are most abundant in skeletal and cardiac muscle; palladin is ubiquitously expressed in the organs of developing vertebrates and plays a key role in cellular morphogenesis. The three family members each interact with specific molecular partners with all three binding to alpha-actinin; In addition, palladin also binds to vasodilator-stimulated phosphoprotein (VASP) and ezrin, myotilin binds to filamin and actin, and myopalladin also binds to nebulin and cardiac ankyrin repeat protein (CARP). This group belongs to the I-set of IgSF domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand, but lack a C" strand.


Pssm-ID: 409405 [Multi-domain]  Cd Length: 91  Bit Score: 45.18  E-value: 8.54e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 281359561 4410 LDINISGEPAPDVTWNQNNKSVQTTSfSHIENLPYNTKY--INNNPERKDTGLYKISAHNFYGQDQVEFQINI 4480
Cdd:cd05744    20 FDCKVSGLPTPDLFWQLNGKPVRPDS-AHKMLVRENGRHslIIEPVTKRDAGIYTCIARNRAGENSFNAELVV 91
IgI_3_Robo cd05725
Third immunoglobulin (Ig)-like domain in Robo (roundabout) receptors; member of the I-set of ...
6177-6255 8.88e-05

Third immunoglobulin (Ig)-like domain in Robo (roundabout) receptors; member of the I-set of Ig superfamily (IgSF) domains; The members here are composed of the third immunoglobulin (Ig)-like domain in Robo (roundabout) receptors. Robo receptors play a role in the development of the central nervous system (CNS), and are receptors of Slit protein. Slit is a repellant secreted by the neural cells in the midline. Slit acts through Robo to prevent most neurons from crossing the midline from either side. Three mammalian Robo homologs (Robo1, Robo2, Robo3), and three mammalian Slit homologs (Slit-1,Slit-2, Slit-3), have been identified. Commissural axons, which cross the midline, express low levels of Robo; longitudinal axons, which avoid the midline, express high levels of Robo. Robo1, Robo2, and Robo3 are expressed by commissural neurons in the vertebrate spinal cord and Slit-1, Slit-2, and Slit-3 are expressed at the ventral midline. Robo-3 is a divergent member of the Robo family which instead of being a positive regulator of Slit responsiveness, antagonizes Slit responsiveness in precrossing axons. The Slit-Robo interaction is mediated by the second leucine-rich repeat (LRR) domain of Slit and the two N-terminal Ig domains of Robo, Ig1 and Ig2. The primary Robo binding site for Slit2 has been shown by surface plasmon resonance experiments and mutational analysis to be the Ig1 domain, while the Ig2 domain has been proposed to harbor a weak secondary binding site. This group belongs to the I-set of IgSF domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand, but lack a C" strand.


Pssm-ID: 409390 [Multi-domain]  Cd Length: 83  Bit Score: 44.69  E-value: 8.88e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 281359561 6177 VRAGEPVNLNIPISGAPTPTIEWKRGDLKLEEGKrisYETNSERTLfRIDDSNRRDSGKYTVTAANEFGKDTADIEVIV 6255
Cdd:cd05725     9 VLVDDSAEFQCEVGGDPVPTVRWRKEDGELPKGR---YEILDDHSL-KIRKVTAGDMGSYTCVAENMVGKIEASATLTV 83
Ig_Titin_like cd05748
Immunoglobulin (Ig)-like domain of titin and similar proteins; The members here are composed ...
7361-7438 9.04e-05

Immunoglobulin (Ig)-like domain of titin and similar proteins; The members here are composed of the immunoglobulin (Ig)-like domain found in titin-like proteins and similar proteins. Titin (also called connectin) is a fibrous sarcomeric protein specifically found in vertebrate striated muscle. Titin is a giant protein; depending on isoform composition, it ranges from 2970 to 3700 kDa, and is of a length that spans half a sarcomere. Titin largely consists of multiple repeats of Ig-like and fibronectin type 3 (FN-III)-like domains. Titin connects the ends of myosin thick filaments to Z disks and extends along the thick filament to the H zone. It appears to function similarly to an elastic band, keeping the myosin filaments centered in the sarcomere during muscle contraction or stretching. Within the sarcomere, titin is also attached to or is associated with myosin binding protein C (MyBP-C). MyBP-C appears to contribute to the generation of passive tension by titin and like titin has repeated Ig-like and FN-III domains. Also included in this group are worm twitchin and insect projectin, thick filament proteins of invertebrate muscle which also have repeated Ig-like and FN-III domains.


Pssm-ID: 409406 [Multi-domain]  Cd Length: 82  Bit Score: 44.50  E-value: 9.04e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 281359561 7361 EGDNSKIKIFYSGDQPLTVILKKNNEVIcdsNDDTHVKVNIFDDYVAIYIRNIVKSDGGPYQIEFTNESGSATGEFYV 7438
Cdd:cd05748     6 AGESLRLDIPIKGRPTPTVTWSKDGQPL---KETGRVQIETTASSTSLVIKNAKRSDSGKYTLTLKNSAGEKSATINV 80
IgI_8_hMLCK_like cd05762
Eighth immunoglobulin (Ig)-like domain of human myosin light-chain kinase (MLCK) and similar ...
4699-4782 9.41e-05

Eighth immunoglobulin (Ig)-like domain of human myosin light-chain kinase (MLCK) and similar protein; member of the I-set of IgSF domains; The members here are composed of the eighth immunoglobulin (Ig)-like domain of human myosin light-chain kinase (MLCK) and similar proteins. Myosin light-chain kinase (MLCK) is a key regulator of different forms of cell motility involving actin and myosin II. Agonist stimulation of smooth muscle cells increases cytosolic Ca2+ which binds calmodulin. This Ca2+-calmodulin complex in turn binds to and activates MLCK. Activated MLCK leads to the phosphorylation of the 20 kDa myosin regulatory light chain (RLC) of myosin II and the stimulation of actin-activated myosin MgATPase activity. MLCK is widely present in vertebrate tissues; it phosphorylates the 20 kDa RLC of both smooth and nonmuscle myosin II. Phosphorylation leads to the activation of the myosin motor domain and altered structural properties of myosin II. In smooth muscle MLCK it is involved in initiating contraction. In nonmuscle cells, MLCK may participate in cell division and cell motility; it has been suggested MLCK plays a role in cardiomyocyte differentiation and contraction through regulation of nonmuscle myosin II.


Pssm-ID: 409419  Cd Length: 99  Bit Score: 45.33  E-value: 9.41e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 4699 SGTALKLDANITGEPAPKVEWKLSNYHLQSGKNVTIETPDYYTKLVIRPTQRSDSGEYLVTATNTSGKDSVLVNVVITDK 4778
Cdd:cd05762    15 AGESVELFCKVTGTQPITCTWMKFRKQIQEGEGIKIENTENSSKLTITEGQQEHCGCYTLEVENKLGSRQAQVNLTVVDK 94

                  ....
gi 281359561 4779 PSPP 4782
Cdd:cd05762    95 PDPP 98
Ig_3 pfam13927
Immunoglobulin domain; This family contains immunoglobulin-like domains.
1750-1806 9.56e-05

Immunoglobulin domain; This family contains immunoglobulin-like domains.


Pssm-ID: 464046 [Multi-domain]  Cd Length: 78  Bit Score: 44.48  E-value: 9.56e-05
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 281359561  1750 TLECSVSSS-MANVHWFKNNTKLESDDPRYLISKDINGNLklIIKDSVLDDAGLYRCQ 1806
Cdd:pfam13927   20 TLTCEATGSpPPTITWYKNGEPISSGSTRSRSLSGSNSTL--TISNVTRSDAGTYTCV 75
IgI_telokin-like cd20973
immunoglobulin-like domain of telokin and similar proteins; a member of the I-set of IgSF ...
4394-4471 9.75e-05

immunoglobulin-like domain of telokin and similar proteins; a member of the I-set of IgSF domains; The members here are composed of the immunoglobulin (Ig) domain in telokin, the C-terminal domain of myosin light chain kinase which is identical to telokin, and similar proteins. The Ig superfamily (IgSF) is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. Unlike the V-set, one of the distinctive features of I-set domains is the lack of a C" strand. The structure of the telokin Ig domain lacks this strand and thus it belongs to the I-set of the IgSF. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors, the hemolymph protein hemolin, the muscle proteins titin, telokin, and twitchin, the neuronal adhesion molecule axonin-1, and the signaling molecule semaphorin 4D that is involved in axonal guidance, immune function and angiogenesis.


Pssm-ID: 409565 [Multi-domain]  Cd Length: 88  Bit Score: 44.87  E-value: 9.75e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 281359561 4394 RKNIRTYNFKSGEPIFLDINISGEPAPDVTWNQNNKSVQTTS-FSHIENLPYNTKYINNNPERKDTGLYKISAHNFYGQ 4471
Cdd:cd20973     1 IQTLRDKEVVEGSAARFDCKVEGYPDPEVKWMKDDNPIVESRrFQIDQDEDGLCSLIISDVCGDDSGKYTCKAVNSLGE 79
IgI_1_Titin_Z1z2-like cd20974
First Ig-like domain of the giant muscle protein titin Z1z2 in the sarcomeric Z-disk and ...
119-211 1.01e-04

First Ig-like domain of the giant muscle protein titin Z1z2 in the sarcomeric Z-disk and similar proteins; a member of the I-set of IgSF domains; The members here are composed of the first immunoglobulin (Ig)-like domain of the giant muscle protein titin Z1z2 in the sarcomeric Z-disk and similar proteins. Titin is a key component in the assembly and functioning of vertebrate striated muscles. By providing connections at the level of individual microfilaments, it contributes to the fine balance of forces between the two halves of the sarcomere. The Ig superfamily (IgSF) is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. Unlike the V-set, one of the distinctive features of I-set domains is the lack of a C" strand. The structure of the titin Z1z2 lacks this strand and thus it belongs to the I-set of the IgSF. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors, the hemolymph protein hemolin, the muscle proteins titin, telokin, and twitchin, the neuronal adhesion molecule axonin-1, and the signaling molecule semaphorin 4D that is involved in axonal guidance, immune function and angiogenesis.


Pssm-ID: 409566 [Multi-domain]  Cd Length: 93  Bit Score: 45.04  E-value: 1.01e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561  119 PTFAKKPAIRQEEDGKRLLFECRVNADPIPAIIWFHNGAAVKESERHKITVDKDVHSyfATLEILNVTVEDAGKYKVNAK 198
Cdd:cd20974     1 PVFTQPLQSVVVLEGSTATFEAHVSGKPVPEVSWFRDGQVISTSTLPGVQISFSDGR--AKLSIPAVTKANSGRYSLTAT 78
                          90
                  ....*....|...
gi 281359561  199 NELGESNATISLN 211
Cdd:cd20974    79 NGSGQATSTAELL 91
IgI_2_Titin_Z1z2-like cd20972
Second Ig-like domain of the giant muscle protein titin Z1z2 in the sarcomeric Z-disk, and ...
1496-1588 1.06e-04

Second Ig-like domain of the giant muscle protein titin Z1z2 in the sarcomeric Z-disk, and similar domains; a member of the I-set of IgSF domains; The members here are composed of the second immunoglobulin (Ig)-like domain of the giant muscle protein titin Z1z2 in the sarcomeric Z-disk and similar proteins. Titin is a key component in the assembly and functioning of vertebrate striated muscles. By providing connections at the level of individual microfilaments, it contributes to the fine balance of forces between the two halves of the sarcomere. The Ig superfamily (IgSF) is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. Unlike the V-set, one of the distinctive features of I-set domains is the lack of a C" strand. The structure of the titin Z1z2 lacks this strand and thus it belongs to the I-set of the IgSF. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors, the hemolymph protein hemolin, the muscle proteins titin, telokin, and twitchin, the neuronal adhesion molecule axonin-1, and the signaling molecule semaphorin 4D that is involved in axonal guidance, immune function and angiogenesis.


Pssm-ID: 409564 [Multi-domain]  Cd Length: 91  Bit Score: 44.88  E-value: 1.06e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 1496 PPSIVDVQESYSVVEDSTAYLTVGVEGSPAPTFKFYKGVSEILEGGRFKFLTDGQTNtiTLCMRKCKPNDESKYKIVVSN 1575
Cdd:cd20972     1 PPQFIQKLRSQEVAEGSKVRLECRVTGNPTPVVRWFCEGKELQNSPDIQIHQEGDLH--SLIIAEAFEEDTGRYSCLATN 78
                          90
                  ....*....|...
gi 281359561 1576 IHGEDSAEMQLYV 1588
Cdd:cd20972    79 SVGSDTTSAEIFV 91
IgI_Titin_like cd05747
Immunoglobulin (Ig)-like domain of human titin C terminus and similar proteins; member of the ...
6864-6945 1.08e-04

Immunoglobulin (Ig)-like domain of human titin C terminus and similar proteins; member of the I-set of Ig superfamily (IgSF) domains; The members here are composed of the fifth immunoglobulin (Ig)-like domain from the C-terminus of human titin x and similar proteins. Titin (also called connectin) is a fibrous sarcomeric protein specifically found in vertebrate striated muscle. Titin is gigantic; depending on isoform composition it ranges from 2970 to 3700 kDa, and is of a length that spans half a sarcomere. Titin largely consists of multiple repeats of Ig-like and fibronectin type 3 (FN-III)-like domains. Titin connects the ends of myosin thick filaments to Z disks and extends along the thick filament to the H zone and appears to function similar to an elastic band, keeping the myosin filaments centered in the sarcomere during muscle contraction or stretching. This group belongs to the I-set of IgSF domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand, but lack a C" strand.


Pssm-ID: 143224 [Multi-domain]  Cd Length: 92  Bit Score: 44.65  E-value: 1.08e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 6864 RDMTVIAGDEFRITVPYHASPRPTASWSLNGLEVIPGERIKFDSNDYASMYYNKSAKRDETGSYTITLTNNKGSDTASCH 6943
Cdd:cd05747    11 RSLTVSEGESARFSCDVDGEPAPTVTWMREGQIIVSSQRHQITSTEYKSTFEISKVQMSDEGNYTVVVENSEGKQEAQFT 90

                  ..
gi 281359561 6944 VT 6945
Cdd:cd05747    91 LT 92
IgI_3_Robo cd05725
Third immunoglobulin (Ig)-like domain in Robo (roundabout) receptors; member of the I-set of ...
4993-5069 1.11e-04

Third immunoglobulin (Ig)-like domain in Robo (roundabout) receptors; member of the I-set of Ig superfamily (IgSF) domains; The members here are composed of the third immunoglobulin (Ig)-like domain in Robo (roundabout) receptors. Robo receptors play a role in the development of the central nervous system (CNS), and are receptors of Slit protein. Slit is a repellant secreted by the neural cells in the midline. Slit acts through Robo to prevent most neurons from crossing the midline from either side. Three mammalian Robo homologs (Robo1, Robo2, Robo3), and three mammalian Slit homologs (Slit-1,Slit-2, Slit-3), have been identified. Commissural axons, which cross the midline, express low levels of Robo; longitudinal axons, which avoid the midline, express high levels of Robo. Robo1, Robo2, and Robo3 are expressed by commissural neurons in the vertebrate spinal cord and Slit-1, Slit-2, and Slit-3 are expressed at the ventral midline. Robo-3 is a divergent member of the Robo family which instead of being a positive regulator of Slit responsiveness, antagonizes Slit responsiveness in precrossing axons. The Slit-Robo interaction is mediated by the second leucine-rich repeat (LRR) domain of Slit and the two N-terminal Ig domains of Robo, Ig1 and Ig2. The primary Robo binding site for Slit2 has been shown by surface plasmon resonance experiments and mutational analysis to be the Ig1 domain, while the Ig2 domain has been proposed to harbor a weak secondary binding site. This group belongs to the I-set of IgSF domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand, but lack a C" strand.


Pssm-ID: 409390 [Multi-domain]  Cd Length: 83  Bit Score: 44.31  E-value: 1.11e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 281359561 4993 AGQSFTFDCKVSGEPAPQTKWllkKKEVYSKDNVKVTNVDYNTkLKVNSATRSDSGIYTVFAENANGEDSADVKVTV 5069
Cdd:cd05725    11 VDDSAEFQCEVGGDPVPTVRW---RKEDGELPKGRYEILDDHS-LKIRKVTAGDMGSYTCVAENMVGKIEASATLTV 83
IgI_M-protein_C cd05891
C-terminal immunoglobulin (Ig)-like domain of M-protein; member of the I-set of Ig superfamily ...
7769-7833 1.12e-04

C-terminal immunoglobulin (Ig)-like domain of M-protein; member of the I-set of Ig superfamily (IgSF) domains; The members here are composed of the C-terminal immunoglobulin (Ig)-like domain of M-protein (also known as myomesin-2). M-protein is a structural protein localized to the M-band, a transverse structure in the center of the sarcomere, and is a candidate for M-band bridges. M-protein is modular consisting mainly of repetitive IG-like and fibronectin type III (FnIII) domains and has a muscle-type specific expression pattern. M-protein is present in fast fibers.


Pssm-ID: 143299  Cd Length: 92  Bit Score: 44.90  E-value: 1.12e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 281359561 7769 GFPKPRIHWVRDGENIESGGHYTVEVKE-RHAVLIIRDGSHLDSGPYRITAENELGSDTAIIQVQI 7833
Cdd:cd05891    27 GNPDPEVIWFKNDQDIELSEHYSVKLEQgKYASLTIKGVTSEDSGKYSINVKNKYGGETVDVTVSV 92
IgI_NCAM-1_like cd05732
Immunoglobulin (Ig)-like I-set domain of Neural Cell Adhesion Molecule 1 (NCAM-1) and similar ...
2302-2385 1.14e-04

Immunoglobulin (Ig)-like I-set domain of Neural Cell Adhesion Molecule 1 (NCAM-1) and similar proteins; The members here are composed of the fourth immunoglobulin (Ig)-like domain of Neural Cell Adhesion Molecule (NCAM-1). NCAM plays important roles in the development and regeneration of the central nervous system, in synaptogenesis and neural migration. NCAM mediates cell-cell and cell-substratum recognition and adhesion via homophilic (NCAM-NCAM), and heterophilic (NCAM-non-NCAM), interactions. NCAM is expressed as three major isoforms having different intracellular extensions. The extracellular portion of NCAM has five N-terminal Ig-like domains and two fibronectin type III domains. The double zipper adhesion complex model for NCAM homophilic binding involves Ig1, Ig2, and Ig3. By this model, Ig1 and Ig2 mediate dimerization of NCAM molecules situated on the same cell surface (cis interactions), and Ig3 domains mediate interactions between NCAM molecules expressed on the surface of opposing cells (trans interactions), through binding to the Ig1 and Ig2 domains. The adhesive ability of NCAM is modulated by the addition of polysialic acid chains to the fifth Ig-like domain. Also included in this group is NCAM-2 (also known as OCAM/mamFas II and RNCAM) NCAM-2 is differentially expressed in the developing and mature olfactory epithelium (OE). One of the unique features of I-set domains is the lack of a C" strand. The structures of this group show that the Ig domain lacks this strand and thus is a member of the I-set of Ig domains.


Pssm-ID: 409395 [Multi-domain]  Cd Length: 96  Bit Score: 44.82  E-value: 1.14e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 2302 VKPFIVGegLKNVTVKKGQTIRFDIKYDGEPEPAATWVKGTDNLKFDNQ----RICLDQLERNSSITIKKSVRKDTGKYK 2377
Cdd:cd05732     1 VQPKITY--LENQTAVELEQITLTCEAEGDPIPEITWRRATRGISFEEGdldgRIVVRGHARVSSLTLKDVQLTDAGRYD 78

                  ....*...
gi 281359561 2378 LVLSNSSG 2385
Cdd:cd05732    79 CEASNRIG 86
IgI_2_Titin_Z1z2-like cd20972
Second Ig-like domain of the giant muscle protein titin Z1z2 in the sarcomeric Z-disk, and ...
228-320 1.15e-04

Second Ig-like domain of the giant muscle protein titin Z1z2 in the sarcomeric Z-disk, and similar domains; a member of the I-set of IgSF domains; The members here are composed of the second immunoglobulin (Ig)-like domain of the giant muscle protein titin Z1z2 in the sarcomeric Z-disk and similar proteins. Titin is a key component in the assembly and functioning of vertebrate striated muscles. By providing connections at the level of individual microfilaments, it contributes to the fine balance of forces between the two halves of the sarcomere. The Ig superfamily (IgSF) is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. Unlike the V-set, one of the distinctive features of I-set domains is the lack of a C" strand. The structure of the titin Z1z2 lacks this strand and thus it belongs to the I-set of the IgSF. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors, the hemolymph protein hemolin, the muscle proteins titin, telokin, and twitchin, the neuronal adhesion molecule axonin-1, and the signaling molecule semaphorin 4D that is involved in axonal guidance, immune function and angiogenesis.


Pssm-ID: 409564 [Multi-domain]  Cd Length: 91  Bit Score: 44.50  E-value: 1.15e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561  228 PTFTERPVIRQSEDGGNVTFECRCVGDPTPTVTWSHGETELNESNRYKMSLTMDqkLYhiaCLEISSVVSSDQGEYRAQA 307
Cdd:cd20972     2 PQFIQKLRSQEVAEGSKVRLECRVTGNPTPVVRWFCEGKELQNSPDIQIHQEGD--LH---SLIIAEAFEEDTGRYSCLA 76
                          90
                  ....*....|...
gi 281359561  308 KNKHGSGVATINL 320
Cdd:cd20972    77 TNSVGSDTTSAEI 89
IgI_APEG-1_like cd20975
Immunoglobulin-like domain of human Aortic Preferentially Expressed Protein-1 (APEG-1) and ...
4983-5069 1.23e-04

Immunoglobulin-like domain of human Aortic Preferentially Expressed Protein-1 (APEG-1) and similar proteins; a member of the I-set of IgSF domains; The members here are composed of the immunoglobulin I-set (IgI) domain of the Human Aortic Preferentially Expressed Protein-1 (APEG-1) and similar proteins. APEG-1 is a novel specific smooth muscle differentiation marker predicted to play a role in the growth and differentiation of arterial smooth muscle cells (SMCs). The Ig superfamily (IgSF) is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. Unlike the V-set, one of the distinctive features of I-set domains is the lack of a C" strand. The structure of the human APEG-1 lacks this strand and thus it belongs to the I-set of the IgSF. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors, the hemolymph protein hemolin, the muscle proteins titin, telokin, and twitchin, the neuronal adhesion molecule axonin-1, and the signaling molecule semaphorin 4D that is involved in axonal guidance, immune function and angiogenesis.


Pssm-ID: 409567  Cd Length: 91  Bit Score: 44.77  E-value: 1.23e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 4983 RSSLVEVRIKAGQSFTFDCKVSGEPAPQTKWLLKKKEVYSKDNVKVTNV-DYNTKLKVNSATRSDSGIYTVFAENANGED 5061
Cdd:cd20975     4 KVSLMDQSVREGQDVIMSIRVQGEPKPVVSWLRNRQPVRPDQRRFAEEAeGGLCRLRILAAERGDAGFYTCKAVNEYGAR 83

                  ....*...
gi 281359561 5062 SADVKVTV 5069
Cdd:cd20975    84 QCEARLEV 91
IgI_2_Palladin_C cd20990
Second C-terminal immunoglobulin (Ig)-like domain of palladin; member of the I-set of Ig ...
4988-5069 1.24e-04

Second C-terminal immunoglobulin (Ig)-like domain of palladin; member of the I-set of Ig superfamily (IgSF) domains; The members here are composed of the C-terminal immunoglobulin (Ig)-like domain of palladin. Palladin belongs to the palladin-myotilin-myopalladin family. Proteins belonging to this family contain multiple Ig-like domains and function as scaffolds, modulating actin cytoskeleton. Palladin binds to alpha-actinin ezrin, vasodilator-stimulated phosphoprotein VASP, SPIN90 (also known as DIP or mDia interacting protein), and Src. Palladin also binds F-actin directly, via its Ig3 domain. Palladin is expressed as several alternatively spliced isoforms, having various combinations of Ig-like domains, in a cell-type-specific manner. It has been suggested that palladin's different Ig-like domains may be specialized for distinct functions. This group belongs to the I-set of IgSF domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand, but lack a C" strand.


Pssm-ID: 409582  Cd Length: 91  Bit Score: 44.71  E-value: 1.24e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 4988 EVRIKAGQSFTFDCKVSGEPAPQTKWLLKKKEVySKDNVKVTNVDYNT--KLKVNSATRSDSGIYTVFAENANGEDSADV 5065
Cdd:cd20990     9 DLTVQEGKLCRMDCKVSGLPTPDLSWQLDGKPI-RPDSAHKMLVRENGvhSLIIEPVTSRDAGIYTCIATNRAGQNSFNL 87

                  ....
gi 281359561 5066 KVTV 5069
Cdd:cd20990    88 ELVV 91
IgI_APEG-1_like cd20975
Immunoglobulin-like domain of human Aortic Preferentially Expressed Protein-1 (APEG-1) and ...
8740-8819 1.24e-04

Immunoglobulin-like domain of human Aortic Preferentially Expressed Protein-1 (APEG-1) and similar proteins; a member of the I-set of IgSF domains; The members here are composed of the immunoglobulin I-set (IgI) domain of the Human Aortic Preferentially Expressed Protein-1 (APEG-1) and similar proteins. APEG-1 is a novel specific smooth muscle differentiation marker predicted to play a role in the growth and differentiation of arterial smooth muscle cells (SMCs). The Ig superfamily (IgSF) is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. Unlike the V-set, one of the distinctive features of I-set domains is the lack of a C" strand. The structure of the human APEG-1 lacks this strand and thus it belongs to the I-set of the IgSF. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors, the hemolymph protein hemolin, the muscle proteins titin, telokin, and twitchin, the neuronal adhesion molecule axonin-1, and the signaling molecule semaphorin 4D that is involved in axonal guidance, immune function and angiogenesis.


Pssm-ID: 409567  Cd Length: 91  Bit Score: 44.77  E-value: 1.24e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 8740 PKIVSHLESRFVRDGDAVNLACRIIGAQHFDVVWLHNNKEIKP-SKDFQYTNEANIYRLQIAEIFPEDGGTYTCEAFNDI 8818
Cdd:cd20975     1 PTFKVSLMDQSVREGQDVIMSIRVQGEPKPVVSWLRNRQPVRPdQRRFAEEAEGGLCRLRILAAERGDAGFYTCKAVNEY 80

                  .
gi 281359561 8819 G 8819
Cdd:cd20975    81 G 81
IgI_Myomesin_like_C cd05737
C-terminal immunoglobulin (Ig)-like domain of myomesin and M-protein; member of the I-set of ...
241-313 1.25e-04

C-terminal immunoglobulin (Ig)-like domain of myomesin and M-protein; member of the I-set of Ig superfamily (IgSF) domains; The members here are composed of the C-terminal immunoglobulin (Ig)-like domain of myomesin and M-protein (also known as myomesin-2). Myomesin and M-protein are both structural proteins localized to the M-band, a transverse structure in the center of the sarcomere, and are candidates for M-band bridges. Both proteins are modular, consisting mainly of repetitive Ig-like and fibronectin type III (FnIII) domains. Myomesin is expressed in all types of vertebrate striated muscle; M-protein has a muscle-type specific expression pattern. Myomesin is present in both slow and fast fibers; M-protein is present only in fast fibers. It has been suggested that myomesin acts as a molecular spring with alternative splicing as a means of modifying its elasticity.


Pssm-ID: 319300  Cd Length: 92  Bit Score: 44.50  E-value: 1.25e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 281359561  241 DGGNVTFECRCVGDPTPTVTWSHGETELNESNRYKMSLTMDQKLYhiacLEISSVVSSDQGEYRAQAKNKHGS 313
Cdd:cd05737    15 EGKTLNLTCNVWGDPPPEVSWLKNDQALAFLDHCNLKVEAGRTVY----FTINGVSSEDSGKYGLVVKNKYGS 83
IgI_Twitchin_like cd20949
C-terminal immunoglobulin-like domain of the myosin-associated giant protein kinase Twitchin, ...
120-211 1.28e-04

C-terminal immunoglobulin-like domain of the myosin-associated giant protein kinase Twitchin, and similar domains; member of the I-set IgSF domains; The members here are composed of the C-terminal immunoglobulin-like domain of the myosin-associated giant protein kinase Twitchin and similar proteins, including Caenorhabditis elegans and Aplysia californica Twitchin, Drosophila melanogaster Projectin, and similar proteins. These are very large muscle proteins containing multiple immunoglobulin (Ig)-like and fibronectin type III (FN3) domains and a single kinase domain near the C-terminus. In humans these proteins are called Titin. The Ig superfamily (IgSF) is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. The Ig-like domain of the Twitchin is a member of the I-set IgSF domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand but lack a C" strand. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors, the hemolymph protein hemolin, the muscle proteins (titin, telokin, and twitchin), the neuronal adhesion molecule axonin-1, and the signaling molecule semaphorin 4D.


Pssm-ID: 409541 [Multi-domain]  Cd Length: 89  Bit Score: 44.63  E-value: 1.28e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561  120 TFAKKPAIRQEEDGKRLLFECRVNADPIPAIIWFHNG----AAVKESERHKITVDKdvhsyfatLEILNVTVEDAGKYKV 195
Cdd:cd20949     1 TFTENAYVTTVKEGQSATILCEVKGEPQPNVTWHFNGqpisASVADMSKYRILADG--------LLINKVTQDDTGEYTC 72
                          90
                  ....*....|....*.
gi 281359561  196 NAKNELGESNATISLN 211
Cdd:cd20949    73 RAYQVNSIASDMQERT 88
IgI_Myotilin_C_like cd05744
Immunoglobulin (Ig)-like domain of myotilin, palladin, and myopalladin; member of the I-set of ...
5285-5356 1.29e-04

Immunoglobulin (Ig)-like domain of myotilin, palladin, and myopalladin; member of the I-set of Ig superfamily (IgSF) domains; The members here are composed of the immunoglobulin (Ig)-like domain in myotilin, palladin, and myopalladin. Myotilin, palladin, and myopalladin function as scaffolds that regulate actin organization. Myotilin and myopalladin are most abundant in skeletal and cardiac muscle; palladin is ubiquitously expressed in the organs of developing vertebrates and plays a key role in cellular morphogenesis. The three family members each interact with specific molecular partners with all three binding to alpha-actinin; In addition, palladin also binds to vasodilator-stimulated phosphoprotein (VASP) and ezrin, myotilin binds to filamin and actin, and myopalladin also binds to nebulin and cardiac ankyrin repeat protein (CARP). This group belongs to the I-set of IgSF domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand, but lack a C" strand.


Pssm-ID: 409405 [Multi-domain]  Cd Length: 91  Bit Score: 44.41  E-value: 1.29e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 281359561 5285 DIKIKAGNVFEFDVPVTGEPLPSKDWTHEGNMIINTDRVK-ISNFDDRTKIRILDAKRSDTGVYTLTARNING 5356
Cdd:cd05744     9 DLEVQEGRLCRFDCKVSGLPTPDLFWQLNGKPVRPDSAHKmLVRENGRHSLIIEPVTKRDAGIYTCIARNRAG 81
IgI_5_Robo cd20952
Fifth Ig-like domain of Roundabout (Robo) homolog 1/2, and similar domains; a member of the ...
5288-5357 1.32e-04

Fifth Ig-like domain of Roundabout (Robo) homolog 1/2, and similar domains; a member of the I-set of IgSF domains; The members here are composed of the fifth Ig-like domain of Roundabout (Robo) homolog 1/2 and similar domains. Robo receptors play a role in the development of the central nervous system (CNS), and are receptors of Slit protein. Slit is a repellant secreted by the neural cells in the midline. Slit acts through Robo to prevent most neurons from crossing the midline from either side. Three mammalian Robo homologs (Robo1, -2, and -3), and three mammalian Slit homologs (Slit-1,-2, -3), have been identified. Commissural axons, which cross the midline, express low levels of Robo; longitudinal axons, which avoid the midline, express high levels of Robo. Robo1, -2, and -3 are expressed by commissural neurons in the vertebrate spinal cord and Slits 1, -2, -3 are expressed at the ventral midline. Robo-3 is a divergent member of the Robo family which instead of being a positive regulator of slit responsiveness, antagonizes slit responsiveness in precrossing axons. The Slit-Robo interaction is mediated by the second leucine-rich repeat (LRR) domain of Slit and the two N-terminal Ig domains of Robo, Ig1 and Ig2. The primary Robo binding site for Slit2 has been shown by surface plasmon resonance experiments and mutational analysis to be is the Ig1 domain, while the Ig2 domain has been proposed to harbor a weak secondary binding site. The fifth Ig-like domain of Robo 1 and 2 is a member of the I-set Ig domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand but lack a C" strand. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors


Pssm-ID: 409544 [Multi-domain]  Cd Length: 87  Bit Score: 44.41  E-value: 1.32e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 281359561 5288 IKAGNVFEFDVPVTGEPLPSKDWTHEGNMIINTD-RVKISNfddRTKIRILDAKRSDTGVYTLTARNINGT 5357
Cdd:cd20952    11 VAVGGTVVLNCQATGEPVPTISWLKDGVPLLGKDeRITTLE---NGSLQIKGAEKSDTGEYTCVALNLSGE 78
IgI_4_hemolin-like cd20978
Fourth immunoglobulin (Ig)-like domain of hemolin, and similar domains; a member of the I-set ...
9-102 1.36e-04

Fourth immunoglobulin (Ig)-like domain of hemolin, and similar domains; a member of the I-set of IgSF domains; The members here are composed of the fourth immunoglobulin (Ig)-like domain of hemolin and similar proteins. Hemolin, an insect immunoglobulin superfamily (IgSF) member containing four Ig-like domains, is a lipopolysaccharide-binding immune protein induced during bacterial infection. Hemolin shares significant sequence similarity with the first four Ig-like domains of the transmembrane cell adhesion molecules (CAMs) of the L1 family. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. The fourth Ig-like domain of hemolin is a member of the I-set Ig domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set domains, members of the I-set have a discontinuous A strand but lack a C" strand. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors, the muscle proteins titin, telokin, and twitchin, the neuronal adhesion molecule axonin-1, and the signaling molecule semaphorin 4D that is involved in axonal guidance, immune function and angiogenesis.


Pssm-ID: 409570 [Multi-domain]  Cd Length: 88  Bit Score: 44.31  E-value: 1.36e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561    9 PSFVKKPQ-LHQEDDGNRLIFECQLLSSPKPDIEWFRsDNKVVEDVRTKFKiqpVGENKYTVVleldDVVETDAGLYKVK 87
Cdd:cd20978     1 PKFIQKPEkNVVVKGGQDVTLPCQVTGVPQPKITWLH-NGKPLQGPMERAT---VEDGTLTII----NVQPEDTGYYGCV 72
                          90
                  ....*....|....*
gi 281359561   88 AKNKSGEVSASINLN 102
Cdd:cd20978    73 ATNEIGDIYTETLLH 87
IgI_telokin-like cd20973
immunoglobulin-like domain of telokin and similar proteins; a member of the I-set of IgSF ...
659-726 1.47e-04

immunoglobulin-like domain of telokin and similar proteins; a member of the I-set of IgSF domains; The members here are composed of the immunoglobulin (Ig) domain in telokin, the C-terminal domain of myosin light chain kinase which is identical to telokin, and similar proteins. The Ig superfamily (IgSF) is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. Unlike the V-set, one of the distinctive features of I-set domains is the lack of a C" strand. The structure of the telokin Ig domain lacks this strand and thus it belongs to the I-set of the IgSF. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors, the hemolymph protein hemolin, the muscle proteins titin, telokin, and twitchin, the neuronal adhesion molecule axonin-1, and the signaling molecule semaphorin 4D that is involved in axonal guidance, immune function and angiogenesis.


Pssm-ID: 409565 [Multi-domain]  Cd Length: 88  Bit Score: 44.10  E-value: 1.47e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 281359561  659 IECTVASKFEPKCTWYKETSTVKESKRhvYQVEQtkEGEFAVKLEINDVEESDKGAYKLVASNEKGEA 726
Cdd:cd20973    17 FDCKVEGYPDPEVKWMKDDNPIVESRR--FQIDQ--DEDGLCSLIISDVCGDDSGKYTCKAVNSLGEA 80
Ig4_L1-NrCAM_like cd04978
Fourth immunoglobulin (Ig)-like domain of L1, Ng-CAM (Neuron-glia CAM cell adhesion molecule), ...
546-636 1.51e-04

Fourth immunoglobulin (Ig)-like domain of L1, Ng-CAM (Neuron-glia CAM cell adhesion molecule), and NrCAM (Ng-CAM-related); The members here are composed of the fourth immunoglobulin (Ig)-like domain of L1, Ng-CAM (Neuron-glia CAM cell adhesion molecule), and NrCAM (Ng-CAM-related). These proteins belong to the L1 subfamily of cell adhesion molecules (CAMs) and are comprised of an extracellular region having six Ig-like domains and five fibronectin type III domains, a transmembrane region and an intracellular domain. These molecules are primarily expressed in the nervous system. L1 is associated with an X-linked recessive disorder, X-linked hydrocephalus, MASA syndrome, or spastic paraplegia type 1, that involves abnormalities of axonal growth.


Pssm-ID: 409367 [Multi-domain]  Cd Length: 89  Bit Score: 44.36  E-value: 1.51e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561  546 IEKPRIVsENNGKLVIMECKVKADPKPDVIWFRNGEVIKESnkiKTFIEQRGDQYYIKLELLDPQleDSGLYKCNIKNTL 625
Cdd:cd04978     4 IEPPSLV-LSPGETGELICEAEGNPQPTITWRLNGVPIEPA---PEDMRRTVDGRTLIFSNLQPN--DTAVYQCNASNVH 77
                          90
                  ....*....|.
gi 281359561  626 GELNANLTLNI 636
Cdd:cd04978    78 GYLLANAFLHV 88
IgI_4_Dscam cd20956
Fourth immunoglobulin domain of the Drosophila melanogaster Dscam protein, and similar domains; ...
8739-8829 1.55e-04

Fourth immunoglobulin domain of the Drosophila melanogaster Dscam protein, and similar domains; a member of the I-set of IgSF domains; The members here are composed of the fourth immunoglobulin domain of the Drosophila melanogaster Down syndrome cell adhesion molecule (DSCAM) protein and similar proteins. Down syndrome cell adhesion molecule (DSCAM) is a cell adhesion molecule that plays critical roles in neural development, including axon guidance and branching, axon target recognition, self-avoidance and synaptic formation. DSCAM belongs to the immunoglobulin superfamily and contributes to defects in the central nervous system in Down syndrome patients. Vertebrate DSCAMs differ from Drosophila Dscam1 in that they lack the extensive alternative splicing that occurs in the insect gene. Drosophila melanogaster Dscam has 38,016 isoforms generated by the alternative splicing of four variable exon clusters, which allows every neuron in the fly to display a distinctive set of Dscam proteins on its cell surface. Drosophila Dscam1 is a cell-surface protein that plays important roles in neural development and axon tiling of neurons. It is shown that thousands of isoforms bind themselves through specific homophilic (self-binding) interactions, a process which mediates cellular self-recognition. Drosophila Dscam2 is also alternatively spliced and plays a key role in the development of two visual system neurons, monopolar cells L1 and L2. This group is a member of the I-set Ig domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand but lack a C" strand.


Pssm-ID: 409548 [Multi-domain]  Cd Length: 96  Bit Score: 44.47  E-value: 1.55e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 8739 APKIVSHLESRFVRDGDAVNLACRIIGAQHFDVVWLHNNKEIKPSKDF---QYTNEAN--IYRLQIAEIFPEDGGTYTCE 8813
Cdd:cd20956     1 APVLLETFSEQTLQPGPSVSLKCVASGNPLPQITWTLDGFPIPESPRFrvgDYVTSDGdvVSYVNISSVRVEDGGEYTCT 80
                          90
                  ....*....|....*.
gi 281359561 8814 AFNDIGESFSTCTINV 8829
Cdd:cd20956    81 ATNDVGSVSHSARINV 96
Ig_2 pfam13895
Immunoglobulin domain; This domain contains immunoglobulin-like domains.
7268-7334 1.56e-04

Immunoglobulin domain; This domain contains immunoglobulin-like domains.


Pssm-ID: 464026 [Multi-domain]  Cd Length: 79  Bit Score: 43.92  E-value: 1.56e-04
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 281359561  7268 GKDYTLQCAASGKPSPTARWLRNGKEIQMNGgrmtcdskdgvfRLHISNVQTGDDGDYTCEAMNSLG 7334
Cdd:pfam13895   14 GEPVTLTCSAPGNPPPSYTWYKDGSAISSSP------------NFFTLSVSAEDSGTYTCVARNGRG 68
IgI_Titin_like cd05747
Immunoglobulin (Ig)-like domain of human titin C terminus and similar proteins; member of the ...
3819-3883 1.63e-04

Immunoglobulin (Ig)-like domain of human titin C terminus and similar proteins; member of the I-set of Ig superfamily (IgSF) domains; The members here are composed of the fifth immunoglobulin (Ig)-like domain from the C-terminus of human titin x and similar proteins. Titin (also called connectin) is a fibrous sarcomeric protein specifically found in vertebrate striated muscle. Titin is gigantic; depending on isoform composition it ranges from 2970 to 3700 kDa, and is of a length that spans half a sarcomere. Titin largely consists of multiple repeats of Ig-like and fibronectin type 3 (FN-III)-like domains. Titin connects the ends of myosin thick filaments to Z disks and extends along the thick filament to the H zone and appears to function similar to an elastic band, keeping the myosin filaments centered in the sarcomere during muscle contraction or stretching. This group belongs to the I-set of IgSF domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand, but lack a C" strand.


Pssm-ID: 143224 [Multi-domain]  Cd Length: 92  Bit Score: 44.27  E-value: 1.63e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 281359561 3819 IKAEPPAKVTWTYNKTEIKTSDHIKIENEDYKTTFIMPKVKRADRGIYIVTAKNDSGSDTVEVEL 3883
Cdd:cd05747    27 VDGEPAPTVTWMREGQIIVSSQRHQITSTEYKSTFEISKVQMSDEGNYTVVVENSEGKQEAQFTL 91
IgI_4_hemolin-like cd20978
Fourth immunoglobulin (Ig)-like domain of hemolin, and similar domains; a member of the I-set ...
335-426 1.64e-04

Fourth immunoglobulin (Ig)-like domain of hemolin, and similar domains; a member of the I-set of IgSF domains; The members here are composed of the fourth immunoglobulin (Ig)-like domain of hemolin and similar proteins. Hemolin, an insect immunoglobulin superfamily (IgSF) member containing four Ig-like domains, is a lipopolysaccharide-binding immune protein induced during bacterial infection. Hemolin shares significant sequence similarity with the first four Ig-like domains of the transmembrane cell adhesion molecules (CAMs) of the L1 family. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. The fourth Ig-like domain of hemolin is a member of the I-set Ig domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set domains, members of the I-set have a discontinuous A strand but lack a C" strand. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors, the muscle proteins titin, telokin, and twitchin, the neuronal adhesion molecule axonin-1, and the signaling molecule semaphorin 4D that is involved in axonal guidance, immune function and angiogenesis.


Pssm-ID: 409570 [Multi-domain]  Cd Length: 88  Bit Score: 43.92  E-value: 1.64e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561  335 PRFPKKP---TIRQEEDLLIMECVLEAHPVPDIVWYCSEKEI-CNNQRTKMTRKaitkdsyilTLEIQNPTKEDGGNYRC 410
Cdd:cd20978     1 PKFIQKPeknVVVKGGQDVTLPCQVTGVPQPKITWLHNGKPLqGPMERATVEDG---------TLTIINVQPEDTGYYGC 71
                          90
                  ....*....|....*.
gi 281359561  411 NAINMYGESNANIALN 426
Cdd:cd20978    72 VATNEIGDIYTETLLH 87
IgI_5_Robo cd20952
Fifth Ig-like domain of Roundabout (Robo) homolog 1/2, and similar domains; a member of the ...
6177-6249 1.70e-04

Fifth Ig-like domain of Roundabout (Robo) homolog 1/2, and similar domains; a member of the I-set of IgSF domains; The members here are composed of the fifth Ig-like domain of Roundabout (Robo) homolog 1/2 and similar domains. Robo receptors play a role in the development of the central nervous system (CNS), and are receptors of Slit protein. Slit is a repellant secreted by the neural cells in the midline. Slit acts through Robo to prevent most neurons from crossing the midline from either side. Three mammalian Robo homologs (Robo1, -2, and -3), and three mammalian Slit homologs (Slit-1,-2, -3), have been identified. Commissural axons, which cross the midline, express low levels of Robo; longitudinal axons, which avoid the midline, express high levels of Robo. Robo1, -2, and -3 are expressed by commissural neurons in the vertebrate spinal cord and Slits 1, -2, -3 are expressed at the ventral midline. Robo-3 is a divergent member of the Robo family which instead of being a positive regulator of slit responsiveness, antagonizes slit responsiveness in precrossing axons. The Slit-Robo interaction is mediated by the second leucine-rich repeat (LRR) domain of Slit and the two N-terminal Ig domains of Robo, Ig1 and Ig2. The primary Robo binding site for Slit2 has been shown by surface plasmon resonance experiments and mutational analysis to be is the Ig1 domain, while the Ig2 domain has been proposed to harbor a weak secondary binding site. The fifth Ig-like domain of Robo 1 and 2 is a member of the I-set Ig domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand but lack a C" strand. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors


Pssm-ID: 409544 [Multi-domain]  Cd Length: 87  Bit Score: 44.02  E-value: 1.70e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 281359561 6177 VRAGEPVNLNIPISGAPTPTIEWKR-GDLKLEEGKRISYETNSErtlFRIDDSNRRDSGKYTVTAANEFGKDTA 6249
Cdd:cd20952    11 VAVGGTVVLNCQATGEPVPTISWLKdGVPLLGKDERITTLENGS---LQIKGAEKSDTGEYTCVALNLSGEATW 81
Ig4_Peroxidasin cd05746
Fourth immunoglobulin (Ig)-like domain of peroxidasin; The members here are composed of the ...
455-530 1.80e-04

Fourth immunoglobulin (Ig)-like domain of peroxidasin; The members here are composed of the fourth immunoglobulin (Ig)-like domain in peroxidasin. Peroxidasin has a peroxidase domain and interacting extracellular motifs containing four Ig-like domains. It has been suggested that peroxidasin is secreted, and has functions related to the stabilization of the extracellular matrix. It may play a part in various other important processes such as removal and destruction of cells which have undergone programmed cell death and protection of the organism against non-self.


Pssm-ID: 143223  Cd Length: 69  Bit Score: 43.32  E-value: 1.80e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 281359561  455 ITMKCKCKAKPEPTVTWYRGQDLVEKSKKIKINTtviaedtyELTLEIKDPGATDGGTYRCNVKNEYGESNANLNL 530
Cdd:cd05746     1 VQIPCSAQGDPEPTITWNKDGVQVTESGKFHISP--------EGYLAIRDVGVADQGRYECVARNTIGYASVSMVL 68
IG_like smart00410
Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.
5579-5660 1.84e-04

Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.


Pssm-ID: 214653 [Multi-domain]  Cd Length: 85  Bit Score: 44.03  E-value: 1.84e-04
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561   5579 DITVHAGKRLgwTLPIEAS--PRPLITWLYNGKEIGSNSRGESGLFQ-NELTFEIVSSLRSDEGRYTLILKNEHGSFDAS 5655
Cdd:smart00410    3 SVTVKEGESV--TLSCEASgsPPPEVTWYKQGGKLLAESGRFSVSRSgSTSTLTISNVTPEDSGTYTCAATNSSGSASSG 80

                    ....*
gi 281359561   5656 AHATV 5660
Cdd:smart00410   81 TTLTV 85
IgI_M-protein_C cd05891
C-terminal immunoglobulin (Ig)-like domain of M-protein; member of the I-set of Ig superfamily ...
6175-6255 1.87e-04

C-terminal immunoglobulin (Ig)-like domain of M-protein; member of the I-set of Ig superfamily (IgSF) domains; The members here are composed of the C-terminal immunoglobulin (Ig)-like domain of M-protein (also known as myomesin-2). M-protein is a structural protein localized to the M-band, a transverse structure in the center of the sarcomere, and is a candidate for M-band bridges. M-protein is modular consisting mainly of repetitive IG-like and fibronectin type III (FnIII) domains and has a muscle-type specific expression pattern. M-protein is present in fast fibers.


Pssm-ID: 143299  Cd Length: 92  Bit Score: 44.13  E-value: 1.87e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 6175 IKVRAGEPVNLNIPISGAPTPTIEWKRGD--LKLEEGKRISYETNSERTLfRIDDSNRRDSGKYTVTAANEFGKDTADIE 6252
Cdd:cd05891    11 VTIMEGKTLNLTCTVFGNPDPEVIWFKNDqdIELSEHYSVKLEQGKYASL-TIKGVTSEDSGKYSINVKNKYGGETVDVT 89

                  ...
gi 281359561 6253 VIV 6255
Cdd:cd05891    90 VSV 92
IgI_4_hemolin-like cd20978
Fourth immunoglobulin (Ig)-like domain of hemolin, and similar domains; a member of the I-set ...
6166-6246 1.91e-04

Fourth immunoglobulin (Ig)-like domain of hemolin, and similar domains; a member of the I-set of IgSF domains; The members here are composed of the fourth immunoglobulin (Ig)-like domain of hemolin and similar proteins. Hemolin, an insect immunoglobulin superfamily (IgSF) member containing four Ig-like domains, is a lipopolysaccharide-binding immune protein induced during bacterial infection. Hemolin shares significant sequence similarity with the first four Ig-like domains of the transmembrane cell adhesion molecules (CAMs) of the L1 family. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. The fourth Ig-like domain of hemolin is a member of the I-set Ig domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set domains, members of the I-set have a discontinuous A strand but lack a C" strand. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors, the muscle proteins titin, telokin, and twitchin, the neuronal adhesion molecule axonin-1, and the signaling molecule semaphorin 4D that is involved in axonal guidance, immune function and angiogenesis.


Pssm-ID: 409570 [Multi-domain]  Cd Length: 88  Bit Score: 43.92  E-value: 1.91e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 6166 YFDGLIGKRIKVRAGEPVNLNIPISGAPTPTIEWkrgdlkLEEGKRISyeTNSERTLF-----RIDDSNRRDSGKYTVTA 6240
Cdd:cd20978     2 KFIQKPEKNVVVKGGQDVTLPCQVTGVPQPKITW------LHNGKPLQ--GPMERATVedgtlTIINVQPEDTGYYGCVA 73

                  ....*.
gi 281359561 6241 ANEFGK 6246
Cdd:cd20978    74 TNEIGD 79
IgI_5_Robo cd20952
Fifth Ig-like domain of Roundabout (Robo) homolog 1/2, and similar domains; a member of the ...
7669-7737 1.93e-04

Fifth Ig-like domain of Roundabout (Robo) homolog 1/2, and similar domains; a member of the I-set of IgSF domains; The members here are composed of the fifth Ig-like domain of Roundabout (Robo) homolog 1/2 and similar domains. Robo receptors play a role in the development of the central nervous system (CNS), and are receptors of Slit protein. Slit is a repellant secreted by the neural cells in the midline. Slit acts through Robo to prevent most neurons from crossing the midline from either side. Three mammalian Robo homologs (Robo1, -2, and -3), and three mammalian Slit homologs (Slit-1,-2, -3), have been identified. Commissural axons, which cross the midline, express low levels of Robo; longitudinal axons, which avoid the midline, express high levels of Robo. Robo1, -2, and -3 are expressed by commissural neurons in the vertebrate spinal cord and Slits 1, -2, -3 are expressed at the ventral midline. Robo-3 is a divergent member of the Robo family which instead of being a positive regulator of slit responsiveness, antagonizes slit responsiveness in precrossing axons. The Slit-Robo interaction is mediated by the second leucine-rich repeat (LRR) domain of Slit and the two N-terminal Ig domains of Robo, Ig1 and Ig2. The primary Robo binding site for Slit2 has been shown by surface plasmon resonance experiments and mutational analysis to be is the Ig1 domain, while the Ig2 domain has been proposed to harbor a weak secondary binding site. The fifth Ig-like domain of Robo 1 and 2 is a member of the I-set Ig domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand but lack a C" strand. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors


Pssm-ID: 409544 [Multi-domain]  Cd Length: 87  Bit Score: 44.02  E-value: 1.93e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 281359561 7669 CTINGVPKPTISWYKGAREISnGARYHMYSEgDNHFLNINDVFGEDADEYVCRAVNKAGAKSTRATLAI 7737
Cdd:cd20952    21 CQATGEPVPTISWLKDGVPLL-GKDERITTL-ENGSLQIKGAEKSDTGEYTCVALNLSGEATWSAVLDV 87
IgI_titin_I1-like cd20951
Immunoglobulin domain I1 of the titin I-band and similar proteins; a member of the I-set of ...
657-728 1.96e-04

Immunoglobulin domain I1 of the titin I-band and similar proteins; a member of the I-set of IgSF domains; The members here are composed of the immunoglobulin domain I1 of the titin I-band and similar proteins. Titin is a key component in the assembly and functioning of vertebrate striated muscles. By providing connections at the level of individual microfilaments, it contributes to the fine balance of forces between the two halves of the sarcomere. The Ig superfamily (IgSF) is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. The two sheets are linked together by a conserved disulfide bond between B strand and F strand. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. The Ig I1 domain of the titin I-band is a member of the I-set Ig domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand but lack a C" strand. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors, the hemolymph protein hemolin, the muscle proteins titin, telokin, and twitchin, the neuronal adhesion molecule axonin-1, and the signaling molecule semaphorin 4D that is involved in axonal guidance, immune function and angiogenesis.


Pssm-ID: 409543 [Multi-domain]  Cd Length: 94  Bit Score: 43.95  E-value: 1.96e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 281359561  657 VVIECTVASKFEPKCTWYKETSTVKESKR-HVYQVEqTKEGEFAvkLEINDVEESDKGAYKLVASNEKGEAVS 728
Cdd:cd20951    18 AKLRVEVQGKPDPEVKWYKNGVPIDPSSIpGKYKIE-SEYGVHV--LHIRRVTVEDSAVYSAVAKNIHGEASS 87
IgI_Titin_like cd05747
Immunoglobulin (Ig)-like domain of human titin C terminus and similar proteins; member of the ...
5286-5356 2.00e-04

Immunoglobulin (Ig)-like domain of human titin C terminus and similar proteins; member of the I-set of Ig superfamily (IgSF) domains; The members here are composed of the fifth immunoglobulin (Ig)-like domain from the C-terminus of human titin x and similar proteins. Titin (also called connectin) is a fibrous sarcomeric protein specifically found in vertebrate striated muscle. Titin is gigantic; depending on isoform composition it ranges from 2970 to 3700 kDa, and is of a length that spans half a sarcomere. Titin largely consists of multiple repeats of Ig-like and fibronectin type 3 (FN-III)-like domains. Titin connects the ends of myosin thick filaments to Z disks and extends along the thick filament to the H zone and appears to function similar to an elastic band, keeping the myosin filaments centered in the sarcomere during muscle contraction or stretching. This group belongs to the I-set of IgSF domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand, but lack a C" strand.


Pssm-ID: 143224 [Multi-domain]  Cd Length: 92  Bit Score: 43.88  E-value: 2.00e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 281359561 5286 IKIKAGNVFEFDVPVTGEPLPSKDWTHEGNMIINTDRVKISNFDDRTKIRILDAKRSDTGVYTLTARNING 5356
Cdd:cd05747    13 LTVSEGESARFSCDVDGEPAPTVTWMREGQIIVSSQRHQITSTEYKSTFEISKVQMSDEGNYTVVVENSEG 83
IgI_C2_MyBP-C-like cd20967
Domain C2 of human cardiac Myosin Binding Protein C and similar domains; a member of the I-set ...
7268-7329 2.04e-04

Domain C2 of human cardiac Myosin Binding Protein C and similar domains; a member of the I-set of IgSF domains; The members here are composed of the immunoglobulin (Ig) Domain C2 of human cardiac Myosin Binding Protein C (MyBP-C) and similar domains. MyBP-C is a thick filament protein involved in the regulation of muscle contraction. Mutations in cardiac MyBP-C gene are the second most frequent cause of hypertrophic cardiomyopathy. MyBP-C binds to myosin with two binding sites, one at its C-terminus and another at its N-terminus. The N-terminal binding site, consisting of immunoglobulin (lg) domains C1 and C2 connected by a flexible linker, interacts with the S2 segment of myosin in a phosphorylation-regulated manner. The C1 and C2 Ig domains can bind to and activate or inhibit the thin filament. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. Unlike the V-set, one of the distinctive features of I-set domains is the lack of a C" strand. The structures of the Ig domains of MyBP-C lack this strand and thus belong to the I-set of Ig superfamily domains. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors.


Pssm-ID: 409559  Cd Length: 82  Bit Score: 43.77  E-value: 2.04e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 281359561 7268 GKDYTLQCAASGKPSPTaRWLRNGKEIQMNgGRMTCDSKDGVFRLHISNVQTGDDGDYTCEA 7329
Cdd:cd20967    12 GHKIRLTVELADPDAEV-KWYKDGQELQSS-SKVIFESIGAKRTLTVQQASLADAGEYQCVA 71
Ig_Pro_neuregulin cd05750
Immunoglobulin (Ig)-like domain in neuregulins; The members here are composed of the ...
8636-8721 2.05e-04

Immunoglobulin (Ig)-like domain in neuregulins; The members here are composed of the immunoglobulin (Ig)-like domain in neuregulins (NRGs). NRGs are signaling molecules which participate in cell-cell interactions in the nervous system, breast, heart, and other organ systems, and are implicated in the pathology of diseases including schizophrenia, multiple sclerosis, and breast cancer. There are four members of the neuregulin gene family (NRG-1, NRG-2, NRG-3, and NRG-4). The NRG-1 protein, binds to and activates the tyrosine kinases receptors ErbB3 and ErbB4, initiating signaling cascades. The other NRGs proteins bind one or the other or both of these ErbBs. NRG-1 has multiple functions: in the brain it regulates various processes such as radial glia formation and neuronal migration, dendritic development, and expression of neurotransmitters receptors, while in the peripheral nervous system NRG-1 regulates processes such as target cell differentiation, and Schwann cell survival. There are many NRG-1 isoforms which arise from the alternative splicing of mRNA. Less is known of the functions of the other NRGs. NRG-2 and NRG-3 are expressed predominantly in the nervous system. NRG-2 is expressed by motor neurons and terminal Schwann cells, and is concentrated near synaptic sites and may be a signal that regulates synaptic differentiation. NRG-4 has been shown to direct pancreatic islet cell development towards the delta-cell lineage.


Pssm-ID: 409408 [Multi-domain]  Cd Length: 92  Bit Score: 44.04  E-value: 2.05e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 8636 KPLHDLTIHDGEQLILTC-YVKGDPEPQISWSKNGKSLSSSDILDLRYKNG--IATLTINEVFPEDEGVITCTATNSVGA 8712
Cdd:cd05750     4 KEMKSQTVQEGSKLVLKCeATSENPSPRYRWFKDGKELNRKRPKNIKIRNKkkNSELQINKAKLEDSGEYTCVVENILGK 83

                  ....*....
gi 281359561 8713 VETKCKLTI 8721
Cdd:cd05750    84 DTVTGNVTV 92
IgI_M-protein_C cd05891
C-terminal immunoglobulin (Ig)-like domain of M-protein; member of the I-set of Ig superfamily ...
6866-6946 2.10e-04

C-terminal immunoglobulin (Ig)-like domain of M-protein; member of the I-set of Ig superfamily (IgSF) domains; The members here are composed of the C-terminal immunoglobulin (Ig)-like domain of M-protein (also known as myomesin-2). M-protein is a structural protein localized to the M-band, a transverse structure in the center of the sarcomere, and is a candidate for M-band bridges. M-protein is modular consisting mainly of repetitive IG-like and fibronectin type III (FnIII) domains and has a muscle-type specific expression pattern. M-protein is present in fast fibers.


Pssm-ID: 143299  Cd Length: 92  Bit Score: 44.13  E-value: 2.10e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 6866 MTVIAGDEFRITVPYHASPRPTASWSLNGLEVIPGER--IKFDSNDYASMYYnKSAKRDETGSYTITLTNNKGSDTASCH 6943
Cdd:cd05891    11 VTIMEGKTLNLTCTVFGNPDPEVIWFKNDQDIELSEHysVKLEQGKYASLTI-KGVTSEDSGKYSINVKNKYGGETVDVT 89

                  ...
gi 281359561 6944 VTV 6946
Cdd:cd05891    90 VSV 92
IgI_8_hMLCK_like cd05762
Eighth immunoglobulin (Ig)-like domain of human myosin light-chain kinase (MLCK) and similar ...
8740-8831 2.11e-04

Eighth immunoglobulin (Ig)-like domain of human myosin light-chain kinase (MLCK) and similar protein; member of the I-set of IgSF domains; The members here are composed of the eighth immunoglobulin (Ig)-like domain of human myosin light-chain kinase (MLCK) and similar proteins. Myosin light-chain kinase (MLCK) is a key regulator of different forms of cell motility involving actin and myosin II. Agonist stimulation of smooth muscle cells increases cytosolic Ca2+ which binds calmodulin. This Ca2+-calmodulin complex in turn binds to and activates MLCK. Activated MLCK leads to the phosphorylation of the 20 kDa myosin regulatory light chain (RLC) of myosin II and the stimulation of actin-activated myosin MgATPase activity. MLCK is widely present in vertebrate tissues; it phosphorylates the 20 kDa RLC of both smooth and nonmuscle myosin II. Phosphorylation leads to the activation of the myosin motor domain and altered structural properties of myosin II. In smooth muscle MLCK it is involved in initiating contraction. In nonmuscle cells, MLCK may participate in cell division and cell motility; it has been suggested MLCK plays a role in cardiomyocyte differentiation and contraction through regulation of nonmuscle myosin II.


Pssm-ID: 409419  Cd Length: 99  Bit Score: 44.17  E-value: 2.11e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 8740 PKIVSHLESRFVRDGDAVNLACRIIGAQHFDVVWLHNNKEIKPSKDFQYTNEANIYRLQIAEIFPEDGGTYTCEAFNDIG 8819
Cdd:cd05762     2 PQIIQFPEDMKVRAGESVELFCKVTGTQPITCTWMKFRKQIQEGEGIKIENTENSSKLTITEGQQEHCGCYTLEVENKLG 81
                          90
                  ....*....|..
gi 281359561 8820 EsfSTCTINVTV 8831
Cdd:cd05762    82 S--RQAQVNLTV 91
Ig_3 pfam13927
Immunoglobulin domain; This family contains immunoglobulin-like domains.
1832-1897 2.35e-04

Immunoglobulin domain; This family contains immunoglobulin-like domains.


Pssm-ID: 464046 [Multi-domain]  Cd Length: 78  Bit Score: 43.32  E-value: 2.35e-04
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 281359561  1832 KSQQCIEKDTVTLACEID-DAMGEVQWLRNGEEIKPDKRIQIVKDGRKRKLVIKDCKVTDAGQFKCT 1897
Cdd:pfam13927    9 SSVTVREGETVTLTCEATgSPPPTITWYKNGEPISSGSTRSRSLSGSNSTLTISNVTRSDAGTYTCV 75
IgI_5_Robo cd20952
Fifth Ig-like domain of Roundabout (Robo) homolog 1/2, and similar domains; a member of the ...
557-636 2.39e-04

Fifth Ig-like domain of Roundabout (Robo) homolog 1/2, and similar domains; a member of the I-set of IgSF domains; The members here are composed of the fifth Ig-like domain of Roundabout (Robo) homolog 1/2 and similar domains. Robo receptors play a role in the development of the central nervous system (CNS), and are receptors of Slit protein. Slit is a repellant secreted by the neural cells in the midline. Slit acts through Robo to prevent most neurons from crossing the midline from either side. Three mammalian Robo homologs (Robo1, -2, and -3), and three mammalian Slit homologs (Slit-1,-2, -3), have been identified. Commissural axons, which cross the midline, express low levels of Robo; longitudinal axons, which avoid the midline, express high levels of Robo. Robo1, -2, and -3 are expressed by commissural neurons in the vertebrate spinal cord and Slits 1, -2, -3 are expressed at the ventral midline. Robo-3 is a divergent member of the Robo family which instead of being a positive regulator of slit responsiveness, antagonizes slit responsiveness in precrossing axons. The Slit-Robo interaction is mediated by the second leucine-rich repeat (LRR) domain of Slit and the two N-terminal Ig domains of Robo, Ig1 and Ig2. The primary Robo binding site for Slit2 has been shown by surface plasmon resonance experiments and mutational analysis to be is the Ig1 domain, while the Ig2 domain has been proposed to harbor a weak secondary binding site. The fifth Ig-like domain of Robo 1 and 2 is a member of the I-set Ig domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand but lack a C" strand. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors


Pssm-ID: 409544 [Multi-domain]  Cd Length: 87  Bit Score: 43.64  E-value: 2.39e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561  557 GKLVIMECKVKADPKPDVIWFRNGEVIKESNKiKTFIEQRGdqyyiKLELLDPQLEDSGLYKCNIKNTLGELNANLTLNI 636
Cdd:cd20952    14 GGTVVLNCQATGEPVPTISWLKDGVPLLGKDE-RITTLENG-----SLQIKGAEKSDTGEYTCVALNLSGEATWSAVLDV 87
IgI_1_Titin_Z1z2-like cd20974
First Ig-like domain of the giant muscle protein titin Z1z2 in the sarcomeric Z-disk and ...
6860-6946 2.50e-04

First Ig-like domain of the giant muscle protein titin Z1z2 in the sarcomeric Z-disk and similar proteins; a member of the I-set of IgSF domains; The members here are composed of the first immunoglobulin (Ig)-like domain of the giant muscle protein titin Z1z2 in the sarcomeric Z-disk and similar proteins. Titin is a key component in the assembly and functioning of vertebrate striated muscles. By providing connections at the level of individual microfilaments, it contributes to the fine balance of forces between the two halves of the sarcomere. The Ig superfamily (IgSF) is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. Unlike the V-set, one of the distinctive features of I-set domains is the lack of a C" strand. The structure of the titin Z1z2 lacks this strand and thus it belongs to the I-set of the IgSF. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors, the hemolymph protein hemolin, the muscle proteins titin, telokin, and twitchin, the neuronal adhesion molecule axonin-1, and the signaling molecule semaphorin 4D that is involved in axonal guidance, immune function and angiogenesis.


Pssm-ID: 409566 [Multi-domain]  Cd Length: 93  Bit Score: 43.88  E-value: 2.50e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 6860 DLSIRDMTVIAGDEFRITVPYHASPRPTASWSLNG----LEVIPGerIKFDSNDYASMYYNKSAKRDETGSYTITLTNNK 6935
Cdd:cd20974     4 TQPLQSVVVLEGSTATFEAHVSGKPVPEVSWFRDGqvisTSTLPG--VQISFSDGRAKLSIPAVTKANSGRYSLTATNGS 81
                          90
                  ....*....|.
gi 281359561 6936 GSDTASCHVTV 6946
Cdd:cd20974    82 GQATSTAELLV 92
IgI_2_Titin_Z1z2-like cd20972
Second Ig-like domain of the giant muscle protein titin Z1z2 in the sarcomeric Z-disk, and ...
437-522 2.55e-04

Second Ig-like domain of the giant muscle protein titin Z1z2 in the sarcomeric Z-disk, and similar domains; a member of the I-set of IgSF domains; The members here are composed of the second immunoglobulin (Ig)-like domain of the giant muscle protein titin Z1z2 in the sarcomeric Z-disk and similar proteins. Titin is a key component in the assembly and functioning of vertebrate striated muscles. By providing connections at the level of individual microfilaments, it contributes to the fine balance of forces between the two halves of the sarcomere. The Ig superfamily (IgSF) is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. Unlike the V-set, one of the distinctive features of I-set domains is the lack of a C" strand. The structure of the titin Z1z2 lacks this strand and thus it belongs to the I-set of the IgSF. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors, the hemolymph protein hemolin, the muscle proteins titin, telokin, and twitchin, the neuronal adhesion molecule axonin-1, and the signaling molecule semaphorin 4D that is involved in axonal guidance, immune function and angiogenesis.


Pssm-ID: 409564 [Multi-domain]  Cd Length: 91  Bit Score: 43.73  E-value: 2.55e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561  437 APSFIEKPRIIPNESGTLITMKCKCKAKPEPTVTWYRGQDLVEKSKKIKINTtviAEDTYelTLEIKDPGATDGGTYRCN 516
Cdd:cd20972     1 PPQFIQKLRSQEVAEGSKVRLECRVTGNPTPVVRWFCEGKELQNSPDIQIHQ---EGDLH--SLIIAEAFEEDTGRYSCL 75

                  ....*.
gi 281359561  517 VKNEYG 522
Cdd:cd20972    76 ATNSVG 81
Ig5_Contactin cd04969
Fifth immunoglobulin (Ig) domain of contactin; The members here are composed of the fifth ...
335-420 2.69e-04

Fifth immunoglobulin (Ig) domain of contactin; The members here are composed of the fifth immunoglobulin (Ig) domain of contactins. Contactins are neural cell adhesion molecules and are comprised of six Ig domains followed by four fibronectin type III (FnIII) domains anchored to the membrane by glycosylphosphatidylinositol. The first four Ig domains form the intermolecular binding fragment, which arranges as a compact U-shaped module via contacts between Ig domains 1 and 4, and between Ig domains 2 and 3. Contactin-2 (TAG-1, axonin-1) may play a part in the neuronal processes of neurite outgrowth, axon guidance and fasciculation, and neuronal migration. This group also includes contactin-1 and contactin-5. The different contactins show different expression patterns in the central nervous system. During development and in adulthood, contactin-2 is transiently expressed in subsets of central and peripheral neurons. Contactin-5 is expressed specifically in the rat postnatal nervous system, peaking at about 3 weeks postnatal, and a lack of contactin-5 (NB-2) results in an impairment of neuronal activity in the rat auditory system. Contactin-5 is highly expressed in the adult human brain in the occipital lobe and in the amygdala. Contactin-1 is differentially expressed in tumor tissues and may, through a RhoA mechanism, facilitate invasion and metastasis of human lung adenocarcinoma.


Pssm-ID: 409358 [Multi-domain]  Cd Length: 89  Bit Score: 43.60  E-value: 2.69e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561  335 PRFPKKPTIRQE-----EDLLImECVLEAHPVPDIVWYCSEKEICNNQRTkmtrkAITKDSyilTLEIQNPTKEDGGNYR 409
Cdd:cd04969     1 PDFELNPVKKKIlaakgGDVII-ECKPKASPKPTISWSKGTELLTNSSRI-----CILPDG---SLKIKNVTKSDEGKYT 71
                          90
                  ....*....|.
gi 281359561  410 CNAINMYGESN 420
Cdd:cd04969    72 CFAVNFFGKAN 82
IgI_telokin-like cd20973
immunoglobulin-like domain of telokin and similar proteins; a member of the I-set of IgSF ...
6177-6255 2.69e-04

immunoglobulin-like domain of telokin and similar proteins; a member of the I-set of IgSF domains; The members here are composed of the immunoglobulin (Ig) domain in telokin, the C-terminal domain of myosin light chain kinase which is identical to telokin, and similar proteins. The Ig superfamily (IgSF) is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. Unlike the V-set, one of the distinctive features of I-set domains is the lack of a C" strand. The structure of the telokin Ig domain lacks this strand and thus it belongs to the I-set of the IgSF. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors, the hemolymph protein hemolin, the muscle proteins titin, telokin, and twitchin, the neuronal adhesion molecule axonin-1, and the signaling molecule semaphorin 4D that is involved in axonal guidance, immune function and angiogenesis.


Pssm-ID: 409565 [Multi-domain]  Cd Length: 88  Bit Score: 43.33  E-value: 2.69e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 6177 VRAGEPVNLNIPISGAPTPTIEWKRGDLKLEEGKRISYETNSERTL-FRIDDSNRRDSGKYTVTAANEFGKDTADIEVIV 6255
Cdd:cd20973     9 VVEGSAARFDCKVEGYPDPEVKWMKDDNPIVESRRFQIDQDEDGLCsLIISDVCGDDSGKYTCKAVNSLGEATCSAELTV 88
IgI_titin_I1-like cd20951
Immunoglobulin domain I1 of the titin I-band and similar proteins; a member of the I-set of ...
8839-8928 2.71e-04

Immunoglobulin domain I1 of the titin I-band and similar proteins; a member of the I-set of IgSF domains; The members here are composed of the immunoglobulin domain I1 of the titin I-band and similar proteins. Titin is a key component in the assembly and functioning of vertebrate striated muscles. By providing connections at the level of individual microfilaments, it contributes to the fine balance of forces between the two halves of the sarcomere. The Ig superfamily (IgSF) is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. The two sheets are linked together by a conserved disulfide bond between B strand and F strand. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. The Ig I1 domain of the titin I-band is a member of the I-set Ig domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand but lack a C" strand. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors, the hemolymph protein hemolin, the muscle proteins titin, telokin, and twitchin, the neuronal adhesion molecule axonin-1, and the signaling molecule semaphorin 4D that is involved in axonal guidance, immune function and angiogenesis.


Pssm-ID: 409543 [Multi-domain]  Cd Length: 94  Bit Score: 43.56  E-value: 2.71e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 8839 PSFVKFPTSVSVLEGEGTTFECEIDSELLNLV-WLKDGKPID--ETLPRYSFTKDGHRYSFAVAKCNMDDVGQYQAKAVS 8915
Cdd:cd20951     1 PEFIIRLQSHTVWEKSDAKLRVEVQGKPDPEVkWYKNGVPIDpsSIPGKYKIESEYGVHVLHIRRVTVEDSAVYSAVAKN 80
                          90
                  ....*....|...
gi 281359561 8916 GKAESICAFSMNV 8928
Cdd:cd20951    81 IHGEASSSASVVV 93
IgI_Myotilin_C cd05892
C-terminal immunoglobulin (Ig)-like domain of myotilin; member of the I-set of Ig superfamily ...
7348-7433 3.07e-04

C-terminal immunoglobulin (Ig)-like domain of myotilin; member of the I-set of Ig superfamily (IgSF) domains; The members here are composed of the C-terminal immunoglobulin (Ig)-like domain of myotilin. Mytolin belongs to the palladin-myotilin-myopalladin family. Proteins belonging to the latter family contain multiple Ig-like domains and function as scaffolds, modulating the actin cytoskeleton. Myotilin is most abundant in skeletal and cardiac muscle and is involved in maintaining sarcomere integrity. It binds to alpha-actinin, filamin, and actin. Mutations in myotilin lead to muscle disorders. This group belongs to the I-set of IgSF domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand, but lack a C" strand.


Pssm-ID: 409473  Cd Length: 92  Bit Score: 43.60  E-value: 3.07e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 7348 PIINRCPSELKLPEGDNSKIKIFYSGDQPLTVILKKNNEVICDSNDdthvKVNIFDD---YVAIYIRNIVKSDGGPYQIE 7424
Cdd:cd05892     1 PMFIQKPQNKKVLEGDPVRLECQISAIPPPQIFWKKNNEMLQYNTD----RISLYQDncgRICLLIQNANKKDAGWYTVS 76

                  ....*....
gi 281359561 7425 FTNESGSAT 7433
Cdd:cd05892    77 AVNEAGVVS 85
I-set pfam07679
Immunoglobulin I-set domain;
1733-1806 3.14e-04

Immunoglobulin I-set domain;


Pssm-ID: 400151 [Multi-domain]  Cd Length: 90  Bit Score: 43.40  E-value: 3.14e-04
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 281359561  1733 FTKPLKKK--LEGFTqheTTLECSVS-SSMANVHWFKNNTKLESDDpRYLISKDiNGNLKLIIKDSVLDDAGLYRCQ 1806
Cdd:pfam07679    3 FTQKPKDVevQEGES---ARFTCTVTgTPDPEVSWFKDGQPLRSSD-RFKVTYE-GGTYTLTISNVQPDDSGKYTCV 74
IgI_5_Dscam cd20958
Fifth immunoglobulin domain of the Drosophila melanogaster Dscam protein, and similar domains; ...
125-204 3.20e-04

Fifth immunoglobulin domain of the Drosophila melanogaster Dscam protein, and similar domains; a member of the I-set of IgSF domains; The members here are composed of the fifth immunoglobulin domain of the Drosophila melanogaster Down syndrome cell adhesion molecule (DSCAM) protein and similar proteins. Down syndrome cell adhesion molecule (DSCAM) is a cell adhesion molecule that plays critical roles in neural development, including axon guidance and branching, axon target recognition, self-avoidance and synaptic formation. DSCAM belongs to the immunoglobulin superfamily and contributes to defects in the central nervous system in Down syndrome patients. Vertebrate DSCAMs differ from Drosophila Dscam1 in that they lack the extensive alternative splicing that occurs in the insect gene. Drosophila melanogaster Dscam has 38,016 isoforms generated by the alternative splicing of four variable exon clusters, which allows every neuron in the fly to display a distinctive set of Dscam proteins on its cell surface. Drosophila Dscam1 is a cell-surface protein that plays important roles in neural development and axon tiling of neurons. It is shown that thousands of isoforms bind themselves through specific homophilic (self-binding) interactions, a process which mediates cellular self-recognition. Drosophila Dscam2 is also alternatively spliced and plays a key role in the development of two visual system neurons, monopolar cells L1 and L2. This group is a member of the I-set Ig domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand but lack a C" strand.


Pssm-ID: 409550 [Multi-domain]  Cd Length: 89  Bit Score: 43.32  E-value: 3.20e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561  125 PAIRQEED-----GKRLLFECRVNADPIPAIIWFHNGAAVKESERHKitvdkdVHSYfATLEILNVT-VEDAGKYKVNAK 198
Cdd:cd20958     2 PFIRPMGNltavaGQTLRLHCPVAGYPISSITWEKDGRRLPLNHRQR------VFPN-GTLVIENVQrSSDEGEYTCTAR 74

                  ....*.
gi 281359561  199 NELGES 204
Cdd:cd20958    75 NQQGQS 80
fn3 pfam00041
Fibronectin type III domain;
5665-5748 3.23e-04

Fibronectin type III domain;


Pssm-ID: 394996 [Multi-domain]  Cd Length: 85  Bit Score: 43.17  E-value: 3.23e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561  5665 SPPKGpLDITKITRDGCHLTWNVPDDdGGSPILHYIIE---KMDLSRSTWSDAGmSTHIVHDVTRLVHRKEYLFRVKAVN 5741
Cdd:pfam00041    1 SAPSN-LTVTDVTSTSLTVSWTPPPD-GNGPITGYEVEyrpKNSGEPWNEITVP-GTTTSVTLTGLKPGTEYEVRVQAVN 77

                   ....*..
gi 281359561  5742 AIGESDP 5748
Cdd:pfam00041   78 GGGEGPP 84
IgI_1_MuSK cd20970
agrin-responsive first immunoglobulin-like domains (Ig1) of the MuSK ectodomain; a member of ...
657-734 3.28e-04

agrin-responsive first immunoglobulin-like domains (Ig1) of the MuSK ectodomain; a member of the I-set of IgSF domains; The members here are composed of the first immunoglobulin-like domains (Ig1) of the Muscle-specific kinase (MuSK). MuSK is a receptor tyrosine kinase specifically expressed in skeletal muscle, where it plays a central role in the formation and maintenance of the neuromuscular junction (NMJ). MuSK is activated by agrin, a neuron-derived heparan sulfate proteoglycan. The activation of MUSK in myotubes regulates the formation of NMJs through the regulation of different processes including the specific expression of genes in subsynaptic nuclei, the reorganization of the actin cytoskeleton and the clustering of the acetylcholine receptors (AChR) in the postsynaptic membrane. The Ig superfamily (IgSF) is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. Unlike the V-set, one of the distinctive features of I-set domains is the lack of a C" strand. The structure of the MuSK lacks this strand and thus it belongs to the I-set of the IgSF. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors, the hemolymph protein hemolin, the muscle proteins titin, telokin, and twitchin, the neuronal adhesion molecule axonin-1, and the signaling molecule semaphorin 4D that is involved in axonal guidance, immune function and angiogenesis.


Pssm-ID: 409562 [Multi-domain]  Cd Length: 92  Bit Score: 43.27  E-value: 3.28e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 281359561  657 VVIECTVASKFEPKCTWYKETSTVKE-SKRHVYQveqtkegEFAVKLEINDVEESDKGAYKLVASNEKGEAVSQIVNLV 734
Cdd:cd20970    20 ATFMCRAEGSPEPEISWTRNGNLIIEfNTRYIVR-------ENGTTLTIRNIRRSDMGIYLCIASNGVPGSVEKRITLQ 91
IgI_1_MuSK cd20970
agrin-responsive first immunoglobulin-like domains (Ig1) of the MuSK ectodomain; a member of ...
21-101 3.34e-04

agrin-responsive first immunoglobulin-like domains (Ig1) of the MuSK ectodomain; a member of the I-set of IgSF domains; The members here are composed of the first immunoglobulin-like domains (Ig1) of the Muscle-specific kinase (MuSK). MuSK is a receptor tyrosine kinase specifically expressed in skeletal muscle, where it plays a central role in the formation and maintenance of the neuromuscular junction (NMJ). MuSK is activated by agrin, a neuron-derived heparan sulfate proteoglycan. The activation of MUSK in myotubes regulates the formation of NMJs through the regulation of different processes including the specific expression of genes in subsynaptic nuclei, the reorganization of the actin cytoskeleton and the clustering of the acetylcholine receptors (AChR) in the postsynaptic membrane. The Ig superfamily (IgSF) is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. Unlike the V-set, one of the distinctive features of I-set domains is the lack of a C" strand. The structure of the MuSK lacks this strand and thus it belongs to the I-set of the IgSF. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors, the hemolymph protein hemolin, the muscle proteins titin, telokin, and twitchin, the neuronal adhesion molecule axonin-1, and the signaling molecule semaphorin 4D that is involved in axonal guidance, immune function and angiogenesis.


Pssm-ID: 409562 [Multi-domain]  Cd Length: 92  Bit Score: 43.27  E-value: 3.34e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561   21 DDGNRLIFECQLLSSPKPDIEWFRSDNKVVEDVrTKFKIQPVGEnkytvVLELDDVVETDAGLYKVKAKNK-SGEVSASI 99
Cdd:cd20970    15 REGENATFMCRAEGSPEPEISWTRNGNLIIEFN-TRYIVRENGT-----TLTIRNIRRSDMGIYLCIASNGvPGSVEKRI 88

                  ..
gi 281359561  100 NL 101
Cdd:cd20970    89 TL 90
IgI_Myotilin_C cd05892
C-terminal immunoglobulin (Ig)-like domain of myotilin; member of the I-set of Ig superfamily ...
8632-8721 3.49e-04

C-terminal immunoglobulin (Ig)-like domain of myotilin; member of the I-set of Ig superfamily (IgSF) domains; The members here are composed of the C-terminal immunoglobulin (Ig)-like domain of myotilin. Mytolin belongs to the palladin-myotilin-myopalladin family. Proteins belonging to the latter family contain multiple Ig-like domains and function as scaffolds, modulating the actin cytoskeleton. Myotilin is most abundant in skeletal and cardiac muscle and is involved in maintaining sarcomere integrity. It binds to alpha-actinin, filamin, and actin. Mutations in myotilin lead to muscle disorders. This group belongs to the I-set of IgSF domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand, but lack a C" strand.


Pssm-ID: 409473  Cd Length: 92  Bit Score: 43.22  E-value: 3.49e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 8632 PEFTKPLHDLTIHDGEQLILTCYVKGDPEPQISWSKNGKSLS-SSDILDLRYKN-GIATLTINEVFPEDEGVITCTATNS 8709
Cdd:cd05892     1 PMFIQKPQNKKVLEGDPVRLECQISAIPPPQIFWKKNNEMLQyNTDRISLYQDNcGRICLLIQNANKKDAGWYTVSAVNE 80
                          90
                  ....*....|..
gi 281359561 8710 VGAVETKCKLTI 8721
Cdd:cd05892    81 AGVVSCNARLDV 92
IG_like smart00410
Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.
778-835 3.51e-04

Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.


Pssm-ID: 214653 [Multi-domain]  Cd Length: 85  Bit Score: 43.26  E-value: 3.51e-04
                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|....*....
gi 281359561    778 VEWYK-GSTVIRETKDITTTFDGTTARLTFSSARTEHTSNYKVIVTNEVGKDESSCKIT 835
Cdd:smart00410   26 VTWYKqGGKLLAESGRFSVSRSGSTSTLTISNVTPEDSGTYTCAATNSSGSASSGTTLT 84
IgI_2_Robo cd05724
Second immunoglobulin (Ig)-like domain in Robo (roundabout) receptors; member of the I-set of ...
656-728 3.67e-04

Second immunoglobulin (Ig)-like domain in Robo (roundabout) receptors; member of the I-set of Ig superfamily (IgSF) domains; The members here are composed of the second immunoglobulin (Ig)-like domain in Robo (roundabout) receptors. Robo receptors play a role in the development of the central nervous system (CNS), and are receptors of the Slit protein. Slit is a repellant secreted by the neural cells in the midline. Slit acts through Robo to prevent most neurons from crossing the midline from either side. Three mammalian Robo homologs (Robo1, Robo2, and Robo3), and three mammalian Slit homologs (Slit-1,Slit-2, Slit-3), have been identified. Commissural axons, which cross the midline, express low levels of Robo; longitudinal axons, which avoid the midline, express high levels of Robo. Robo1, Robo2, and Robo3 are expressed by commissural neurons in the vertebrate spinal cord and Slit-1, Slit-2, Slit-3 are expressed at the ventral midline. Robo-3 is a divergent member of the Robo family which instead of being a positive regulator of Slit responsiveness, antagonizes Slit responsiveness in precrossing axons. The Slit-Robo interaction is mediated by the second leucine-rich repeat (LRR) domain of Slit and the two N-terminal Ig domains of Robo, Ig1 and Ig2. The primary Robo binding site for Slit-2 has been shown by surface plasmon resonance experiments and mutational analysis to be the Ig1 domain, while the Ig2 domain has been proposed to harbor a weak secondary binding site. This group belongs to the I-set of IgSF domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand, but lack a C" strand.


Pssm-ID: 409389 [Multi-domain]  Cd Length: 87  Bit Score: 43.16  E-value: 3.67e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 281359561  656 TVVIECTVASKF-EPKCTWYKETSTVKESKRHVYQVEQTKegefavkLEINDVEESDKGAYKLVASNEKGEAVS 728
Cdd:cd05724    14 MAVLECSPPRGHpEPTVSWRKDGQPLNLDNERVRIVDDGN-------LLIAEARKSDEGTYKCVATNMVGERES 80
IgI_5_Dscam cd20958
Fifth immunoglobulin domain of the Drosophila melanogaster Dscam protein, and similar domains; ...
7648-7732 3.92e-04

Fifth immunoglobulin domain of the Drosophila melanogaster Dscam protein, and similar domains; a member of the I-set of IgSF domains; The members here are composed of the fifth immunoglobulin domain of the Drosophila melanogaster Down syndrome cell adhesion molecule (DSCAM) protein and similar proteins. Down syndrome cell adhesion molecule (DSCAM) is a cell adhesion molecule that plays critical roles in neural development, including axon guidance and branching, axon target recognition, self-avoidance and synaptic formation. DSCAM belongs to the immunoglobulin superfamily and contributes to defects in the central nervous system in Down syndrome patients. Vertebrate DSCAMs differ from Drosophila Dscam1 in that they lack the extensive alternative splicing that occurs in the insect gene. Drosophila melanogaster Dscam has 38,016 isoforms generated by the alternative splicing of four variable exon clusters, which allows every neuron in the fly to display a distinctive set of Dscam proteins on its cell surface. Drosophila Dscam1 is a cell-surface protein that plays important roles in neural development and axon tiling of neurons. It is shown that thousands of isoforms bind themselves through specific homophilic (self-binding) interactions, a process which mediates cellular self-recognition. Drosophila Dscam2 is also alternatively spliced and plays a key role in the development of two visual system neurons, monopolar cells L1 and L2. This group is a member of the I-set Ig domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand but lack a C" strand.


Pssm-ID: 409550 [Multi-domain]  Cd Length: 89  Bit Score: 42.94  E-value: 3.92e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 7648 PLIVKPLRDANCIQNHNAQFTCTINGVPKPTISWYKGAREISNGARYHMYSEGDnhfLNINDVFG-EDADEYVCRAVNKA 7726
Cdd:cd20958     1 PPFIRPMGNLTAVAGQTLRLHCPVAGYPISSITWEKDGRRLPLNHRQRVFPNGT---LVIENVQRsSDEGEYTCTARNQQ 77

                  ....*.
gi 281359561 7727 GAKSTR 7732
Cdd:cd20958    78 GQSASR 83
IgI_3_Robo cd05725
Third immunoglobulin (Ig)-like domain in Robo (roundabout) receptors; member of the I-set of ...
8317-8394 3.93e-04

Third immunoglobulin (Ig)-like domain in Robo (roundabout) receptors; member of the I-set of Ig superfamily (IgSF) domains; The members here are composed of the third immunoglobulin (Ig)-like domain in Robo (roundabout) receptors. Robo receptors play a role in the development of the central nervous system (CNS), and are receptors of Slit protein. Slit is a repellant secreted by the neural cells in the midline. Slit acts through Robo to prevent most neurons from crossing the midline from either side. Three mammalian Robo homologs (Robo1, Robo2, Robo3), and three mammalian Slit homologs (Slit-1,Slit-2, Slit-3), have been identified. Commissural axons, which cross the midline, express low levels of Robo; longitudinal axons, which avoid the midline, express high levels of Robo. Robo1, Robo2, and Robo3 are expressed by commissural neurons in the vertebrate spinal cord and Slit-1, Slit-2, and Slit-3 are expressed at the ventral midline. Robo-3 is a divergent member of the Robo family which instead of being a positive regulator of Slit responsiveness, antagonizes Slit responsiveness in precrossing axons. The Slit-Robo interaction is mediated by the second leucine-rich repeat (LRR) domain of Slit and the two N-terminal Ig domains of Robo, Ig1 and Ig2. The primary Robo binding site for Slit2 has been shown by surface plasmon resonance experiments and mutational analysis to be the Ig1 domain, while the Ig2 domain has been proposed to harbor a weak secondary binding site. This group belongs to the I-set of IgSF domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand, but lack a C" strand.


Pssm-ID: 409390 [Multi-domain]  Cd Length: 83  Bit Score: 42.77  E-value: 3.93e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 281359561 8317 RPSSQFCYEGQSVKFYCRCIAIATPTLTWSHNNIELRQSvkfmkRY-VGDDYYFIINRVKLDDRGEYIIRAENHYGSRE 8394
Cdd:cd05725     3 RPQNQVVLVDDSAEFQCEVGGDPVPTVRWRKEDGELPKG-----RYeILDDHSLKIRKVTAGDMGSYTCVAENMVGKIE 76
IgI_2_Palladin_C cd20990
Second C-terminal immunoglobulin (Ig)-like domain of palladin; member of the I-set of Ig ...
7254-7334 4.11e-04

Second C-terminal immunoglobulin (Ig)-like domain of palladin; member of the I-set of Ig superfamily (IgSF) domains; The members here are composed of the C-terminal immunoglobulin (Ig)-like domain of palladin. Palladin belongs to the palladin-myotilin-myopalladin family. Proteins belonging to this family contain multiple Ig-like domains and function as scaffolds, modulating actin cytoskeleton. Palladin binds to alpha-actinin ezrin, vasodilator-stimulated phosphoprotein VASP, SPIN90 (also known as DIP or mDia interacting protein), and Src. Palladin also binds F-actin directly, via its Ig3 domain. Palladin is expressed as several alternatively spliced isoforms, having various combinations of Ig-like domains, in a cell-type-specific manner. It has been suggested that palladin's different Ig-like domains may be specialized for distinct functions. This group belongs to the I-set of IgSF domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand, but lack a C" strand.


Pssm-ID: 409582  Cd Length: 91  Bit Score: 43.17  E-value: 4.11e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 7254 PDWITRLQDKVAPFGKDYTLQCAASGKPSPTARWLRNGKEIQMNGGRMTCDSKDGVFRLHISNVQTGDDGDYTCEAMNSL 7333
Cdd:cd20990     1 PHFLQAPGDLTVQEGKLCRMDCKVSGLPTPDLSWQLDGKPIRPDSAHKMLVRENGVHSLIIEPVTSRDAGIYTCIATNRA 80

                  .
gi 281359561 7334 G 7334
Cdd:cd20990    81 G 81
IgI_8_hMLCK_like cd05762
Eighth immunoglobulin (Ig)-like domain of human myosin light-chain kinase (MLCK) and similar ...
2316-2402 4.18e-04

Eighth immunoglobulin (Ig)-like domain of human myosin light-chain kinase (MLCK) and similar protein; member of the I-set of IgSF domains; The members here are composed of the eighth immunoglobulin (Ig)-like domain of human myosin light-chain kinase (MLCK) and similar proteins. Myosin light-chain kinase (MLCK) is a key regulator of different forms of cell motility involving actin and myosin II. Agonist stimulation of smooth muscle cells increases cytosolic Ca2+ which binds calmodulin. This Ca2+-calmodulin complex in turn binds to and activates MLCK. Activated MLCK leads to the phosphorylation of the 20 kDa myosin regulatory light chain (RLC) of myosin II and the stimulation of actin-activated myosin MgATPase activity. MLCK is widely present in vertebrate tissues; it phosphorylates the 20 kDa RLC of both smooth and nonmuscle myosin II. Phosphorylation leads to the activation of the myosin motor domain and altered structural properties of myosin II. In smooth muscle MLCK it is involved in initiating contraction. In nonmuscle cells, MLCK may participate in cell division and cell motility; it has been suggested MLCK plays a role in cardiomyocyte differentiation and contraction through regulation of nonmuscle myosin II.


Pssm-ID: 409419  Cd Length: 99  Bit Score: 43.40  E-value: 4.18e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 2316 VKKGQTIRFDIKYDGEPEPAATWVKGTDNLKfDNQRICLDQLERNSSITIKKSVRKDTGKYKLVLSNSSGTIESEAQVVV 2395
Cdd:cd05762    13 VRAGESVELFCKVTGTQPITCTWMKFRKQIQ-EGEGIKIENTENSSKLTITEGQQEHCGCYTLEVENKLGSRQAQVNLTV 91

                  ....*..
gi 281359561 2396 LDRPLPP 2402
Cdd:cd05762    92 VDKPDPP 98
IgI_Myotilin_C_like cd05744
Immunoglobulin (Ig)-like domain of myotilin, palladin, and myopalladin; member of the I-set of ...
4690-4768 4.24e-04

Immunoglobulin (Ig)-like domain of myotilin, palladin, and myopalladin; member of the I-set of Ig superfamily (IgSF) domains; The members here are composed of the immunoglobulin (Ig)-like domain in myotilin, palladin, and myopalladin. Myotilin, palladin, and myopalladin function as scaffolds that regulate actin organization. Myotilin and myopalladin are most abundant in skeletal and cardiac muscle; palladin is ubiquitously expressed in the organs of developing vertebrates and plays a key role in cellular morphogenesis. The three family members each interact with specific molecular partners with all three binding to alpha-actinin; In addition, palladin also binds to vasodilator-stimulated phosphoprotein (VASP) and ezrin, myotilin binds to filamin and actin, and myopalladin also binds to nebulin and cardiac ankyrin repeat protein (CARP). This group belongs to the I-set of IgSF domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand, but lack a C" strand.


Pssm-ID: 409405 [Multi-domain]  Cd Length: 91  Bit Score: 42.87  E-value: 4.24e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 4690 RNLRNITLSSGTALKLDANITGEPAPKVEWKLSNYHLQSGKNVTI---ETPDYytKLVIRPTQRSDSGEYLVTATNTSGK 4766
Cdd:cd05744     5 QAPGDLEVQEGRLCRFDCKVSGLPTPDLFWQLNGKPVRPDSAHKMlvrENGRH--SLIIEPVTKRDAGIYTCIARNRAGE 82

                  ..
gi 281359561 4767 DS 4768
Cdd:cd05744    83 NS 84
Ig4_Contactin-2-like cd05728
Fourth Ig domain of the neural cell adhesion molecule contactin-2, and similar domains; The ...
8633-8721 4.32e-04

Fourth Ig domain of the neural cell adhesion molecule contactin-2, and similar domains; The members here are composed of the fourth Ig domain of the neural cell adhesion molecule contactin-2. Contactins are comprised of six Ig domains followed by four fibronectin type III (FnIII) domains anchored to the membrane by glycosylphosphatidylinositol. Contactin-2 (also called TAG-1, axonin-1) facilitates cell adhesion by homophilic binding between molecules in apposed membranes. The first four Ig domains form the intermolecular binding fragment which arranges as a compact U-shaped module by contacts between Ig domains 1 and 4, and domains 2 and 3. It has been proposed that a linear zipper-like array forms, from contactin-2 molecules alternatively provided by the two apposed membranes.


Pssm-ID: 143205 [Multi-domain]  Cd Length: 85  Bit Score: 42.97  E-value: 4.32e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 8633 EFTKPLHDLTIHDGEQLILTCYVKGDPEPQISWSKNGKSLSSSDilDLRYKNGiaTLTINEVFPEDEGVITCTATNSVGA 8712
Cdd:cd05728     1 EWLKVISDTEADIGSSLRWECKASGNPRPAYRWLKNGQPLASEN--RIEVEAG--DLRITKLSLSDSGMYQCVAENKHGT 76

                  ....*....
gi 281359561 8713 VETKCKLTI 8721
Cdd:cd05728    77 IYASAELAV 85
IgI_Twitchin_like cd20949
C-terminal immunoglobulin-like domain of the myosin-associated giant protein kinase Twitchin, ...
8751-8816 4.37e-04

C-terminal immunoglobulin-like domain of the myosin-associated giant protein kinase Twitchin, and similar domains; member of the I-set IgSF domains; The members here are composed of the C-terminal immunoglobulin-like domain of the myosin-associated giant protein kinase Twitchin and similar proteins, including Caenorhabditis elegans and Aplysia californica Twitchin, Drosophila melanogaster Projectin, and similar proteins. These are very large muscle proteins containing multiple immunoglobulin (Ig)-like and fibronectin type III (FN3) domains and a single kinase domain near the C-terminus. In humans these proteins are called Titin. The Ig superfamily (IgSF) is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. The Ig-like domain of the Twitchin is a member of the I-set IgSF domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand but lack a C" strand. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors, the hemolymph protein hemolin, the muscle proteins (titin, telokin, and twitchin), the neuronal adhesion molecule axonin-1, and the signaling molecule semaphorin 4D.


Pssm-ID: 409541 [Multi-domain]  Cd Length: 89  Bit Score: 43.09  E-value: 4.37e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 281359561 8751 VRDGDAVNLACRIIGAQHFDVVWLHNNKEIKPSKDFQYTNEANIYRLQIAEIFPEDGGTYTCEAFN 8816
Cdd:cd20949    11 VKEGQSATILCEVKGEPQPNVTWHFNGQPISASVADMSKYRILADGLLINKVTQDDTGEYTCRAYQ 76
IgI_8_hMLCK_like cd05762
Eighth immunoglobulin (Ig)-like domain of human myosin light-chain kinase (MLCK) and similar ...
3795-3892 4.52e-04

Eighth immunoglobulin (Ig)-like domain of human myosin light-chain kinase (MLCK) and similar protein; member of the I-set of IgSF domains; The members here are composed of the eighth immunoglobulin (Ig)-like domain of human myosin light-chain kinase (MLCK) and similar proteins. Myosin light-chain kinase (MLCK) is a key regulator of different forms of cell motility involving actin and myosin II. Agonist stimulation of smooth muscle cells increases cytosolic Ca2+ which binds calmodulin. This Ca2+-calmodulin complex in turn binds to and activates MLCK. Activated MLCK leads to the phosphorylation of the 20 kDa myosin regulatory light chain (RLC) of myosin II and the stimulation of actin-activated myosin MgATPase activity. MLCK is widely present in vertebrate tissues; it phosphorylates the 20 kDa RLC of both smooth and nonmuscle myosin II. Phosphorylation leads to the activation of the myosin motor domain and altered structural properties of myosin II. In smooth muscle MLCK it is involved in initiating contraction. In nonmuscle cells, MLCK may participate in cell division and cell motility; it has been suggested MLCK plays a role in cardiomyocyte differentiation and contraction through regulation of nonmuscle myosin II.


Pssm-ID: 409419  Cd Length: 99  Bit Score: 43.40  E-value: 4.52e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 3795 PHIDRKNLQKKIMRsGQMLHIDALIKAEPPAKVTWTYNKTEIKTSDHIKIENEDYKTTFIMPKVKRADRGIYIVTAKNDS 3874
Cdd:cd05762     2 PQIIQFPEDMKVRA-GESVELFCKVTGTQPITCTWMKFRKQIQEGEGIKIENTENSSKLTITEGQQEHCGCYTLEVENKL 80
                          90
                  ....*....|....*...
gi 281359561 3875 GSDTVEVELEVLCKPSKP 3892
Cdd:cd05762    81 GSRQAQVNLTVVDKPDPP 98
IgI_Myotilin_C_like cd05744
Immunoglobulin (Ig)-like domain of myotilin, palladin, and myopalladin; member of the I-set of ...
8839-8928 4.63e-04

Immunoglobulin (Ig)-like domain of myotilin, palladin, and myopalladin; member of the I-set of Ig superfamily (IgSF) domains; The members here are composed of the immunoglobulin (Ig)-like domain in myotilin, palladin, and myopalladin. Myotilin, palladin, and myopalladin function as scaffolds that regulate actin organization. Myotilin and myopalladin are most abundant in skeletal and cardiac muscle; palladin is ubiquitously expressed in the organs of developing vertebrates and plays a key role in cellular morphogenesis. The three family members each interact with specific molecular partners with all three binding to alpha-actinin; In addition, palladin also binds to vasodilator-stimulated phosphoprotein (VASP) and ezrin, myotilin binds to filamin and actin, and myopalladin also binds to nebulin and cardiac ankyrin repeat protein (CARP). This group belongs to the I-set of IgSF domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand, but lack a C" strand.


Pssm-ID: 409405 [Multi-domain]  Cd Length: 91  Bit Score: 42.87  E-value: 4.63e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 8839 PSFVKFPTSVSVLEGEGTTFECEIDS-ELLNLVWLKDGKPIDETLPRYSFTKDGHRYSFAVAKCNMDDVGQYQAKAVSGK 8917
Cdd:cd05744     1 PHFLQAPGDLEVQEGRLCRFDCKVSGlPTPDLFWQLNGKPVRPDSAHKMLVRENGRHSLIIEPVTKRDAGIYTCIARNRA 80
                          90
                  ....*....|.
gi 281359561 8918 AESICAFSMNV 8928
Cdd:cd05744    81 GENSFNAELVV 91
IgI_Myotilin_C_like cd05744
Immunoglobulin (Ig)-like domain of myotilin, palladin, and myopalladin; member of the I-set of ...
3511-3590 4.67e-04

Immunoglobulin (Ig)-like domain of myotilin, palladin, and myopalladin; member of the I-set of Ig superfamily (IgSF) domains; The members here are composed of the immunoglobulin (Ig)-like domain in myotilin, palladin, and myopalladin. Myotilin, palladin, and myopalladin function as scaffolds that regulate actin organization. Myotilin and myopalladin are most abundant in skeletal and cardiac muscle; palladin is ubiquitously expressed in the organs of developing vertebrates and plays a key role in cellular morphogenesis. The three family members each interact with specific molecular partners with all three binding to alpha-actinin; In addition, palladin also binds to vasodilator-stimulated phosphoprotein (VASP) and ezrin, myotilin binds to filamin and actin, and myopalladin also binds to nebulin and cardiac ankyrin repeat protein (CARP). This group belongs to the I-set of IgSF domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand, but lack a C" strand.


Pssm-ID: 409405 [Multi-domain]  Cd Length: 91  Bit Score: 42.87  E-value: 4.67e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 3511 VKTGLSISLDINIRGEPAPKVEWFFNNSSVTSD-EHSVKIDNVDYNTkFFVMRAQRSQSGKYIIKATNEVGEDEAELEVT 3589
Cdd:cd05744    12 VQEGRLCRFDCKVSGLPTPDLFWQLNGKPVRPDsAHKMLVRENGRHS-LIIEPVTKRDAGIYTCIARNRAGENSFNAELV 90

                  .
gi 281359561 3590 V 3590
Cdd:cd05744    91 V 91
IgI_2_Titin_Z1z2-like cd20972
Second Ig-like domain of the giant muscle protein titin Z1z2 in the sarcomeric Z-disk, and ...
2909-2995 4.76e-04

Second Ig-like domain of the giant muscle protein titin Z1z2 in the sarcomeric Z-disk, and similar domains; a member of the I-set of IgSF domains; The members here are composed of the second immunoglobulin (Ig)-like domain of the giant muscle protein titin Z1z2 in the sarcomeric Z-disk and similar proteins. Titin is a key component in the assembly and functioning of vertebrate striated muscles. By providing connections at the level of individual microfilaments, it contributes to the fine balance of forces between the two halves of the sarcomere. The Ig superfamily (IgSF) is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. Unlike the V-set, one of the distinctive features of I-set domains is the lack of a C" strand. The structure of the titin Z1z2 lacks this strand and thus it belongs to the I-set of the IgSF. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors, the hemolymph protein hemolin, the muscle proteins titin, telokin, and twitchin, the neuronal adhesion molecule axonin-1, and the signaling molecule semaphorin 4D that is involved in axonal guidance, immune function and angiogenesis.


Pssm-ID: 409564 [Multi-domain]  Cd Length: 91  Bit Score: 42.96  E-value: 4.76e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 2909 LKPLLIRAGKPIRYDVNVRGEPAPVITWYQNDKELKpeelpSSSEIKnIPYNTKIS---IIETVRKHTGIYKIIAVNEHG 2985
Cdd:cd20972     8 LRSQEVAEGSKVRLECRVTGNPTPVVRWFCEGKELQ-----NSPDIQ-IHQEGDLHsliIAEAFEEDTGRYSCLATNSVG 81
                          90
                  ....*....|
gi 281359561 2986 QDEATVEVNI 2995
Cdd:cd20972    82 SDTTSAEIFV 91
IgI_APEG-1_like cd20975
Immunoglobulin-like domain of human Aortic Preferentially Expressed Protein-1 (APEG-1) and ...
2311-2395 4.79e-04

Immunoglobulin-like domain of human Aortic Preferentially Expressed Protein-1 (APEG-1) and similar proteins; a member of the I-set of IgSF domains; The members here are composed of the immunoglobulin I-set (IgI) domain of the Human Aortic Preferentially Expressed Protein-1 (APEG-1) and similar proteins. APEG-1 is a novel specific smooth muscle differentiation marker predicted to play a role in the growth and differentiation of arterial smooth muscle cells (SMCs). The Ig superfamily (IgSF) is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. Unlike the V-set, one of the distinctive features of I-set domains is the lack of a C" strand. The structure of the human APEG-1 lacks this strand and thus it belongs to the I-set of the IgSF. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors, the hemolymph protein hemolin, the muscle proteins titin, telokin, and twitchin, the neuronal adhesion molecule axonin-1, and the signaling molecule semaphorin 4D that is involved in axonal guidance, immune function and angiogenesis.


Pssm-ID: 409567  Cd Length: 91  Bit Score: 42.84  E-value: 4.79e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 2311 LKNVTVKKGQTIRFDIKYDGEPEPAATWVKGTDNLKFDNQRICLDQLERNSSITIKKSVRKDTGKYKLVLSNSSGTIESE 2390
Cdd:cd20975     7 LMDQSVREGQDVIMSIRVQGEPKPVVSWLRNRQPVRPDQRRFAEEAEGGLCRLRILAAERGDAGFYTCKAVNEYGARQCE 86

                  ....*
gi 281359561 2391 AQVVV 2395
Cdd:cd20975    87 ARLEV 91
IgI_1_Titin_Z1z2-like cd20974
First Ig-like domain of the giant muscle protein titin Z1z2 in the sarcomeric Z-disk and ...
228-321 4.90e-04

First Ig-like domain of the giant muscle protein titin Z1z2 in the sarcomeric Z-disk and similar proteins; a member of the I-set of IgSF domains; The members here are composed of the first immunoglobulin (Ig)-like domain of the giant muscle protein titin Z1z2 in the sarcomeric Z-disk and similar proteins. Titin is a key component in the assembly and functioning of vertebrate striated muscles. By providing connections at the level of individual microfilaments, it contributes to the fine balance of forces between the two halves of the sarcomere. The Ig superfamily (IgSF) is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. Unlike the V-set, one of the distinctive features of I-set domains is the lack of a C" strand. The structure of the titin Z1z2 lacks this strand and thus it belongs to the I-set of the IgSF. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors, the hemolymph protein hemolin, the muscle proteins titin, telokin, and twitchin, the neuronal adhesion molecule axonin-1, and the signaling molecule semaphorin 4D that is involved in axonal guidance, immune function and angiogenesis.


Pssm-ID: 409566 [Multi-domain]  Cd Length: 93  Bit Score: 43.11  E-value: 4.90e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561  228 PTFTERPVIRQSEDGGNVTFECRCVGDPTPTVTWSHGE--TELNESNRYKMSLTMDQklyhiACLEISSVVSSDQGEYRA 305
Cdd:cd20974     1 PVFTQPLQSVVVLEGSTATFEAHVSGKPVPEVSWFRDGqvISTSTLPGVQISFSDGR-----AKLSIPAVTKANSGRYSL 75
                          90
                  ....*....|....*.
gi 281359561  306 QAKNKHGSGVATINLN 321
Cdd:cd20974    76 TATNGSGQATSTAELL 91
IgI_4_hemolin-like cd20978
Fourth immunoglobulin (Ig)-like domain of hemolin, and similar domains; a member of the I-set ...
4402-4480 5.03e-04

Fourth immunoglobulin (Ig)-like domain of hemolin, and similar domains; a member of the I-set of IgSF domains; The members here are composed of the fourth immunoglobulin (Ig)-like domain of hemolin and similar proteins. Hemolin, an insect immunoglobulin superfamily (IgSF) member containing four Ig-like domains, is a lipopolysaccharide-binding immune protein induced during bacterial infection. Hemolin shares significant sequence similarity with the first four Ig-like domains of the transmembrane cell adhesion molecules (CAMs) of the L1 family. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. The fourth Ig-like domain of hemolin is a member of the I-set Ig domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set domains, members of the I-set have a discontinuous A strand but lack a C" strand. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors, the muscle proteins titin, telokin, and twitchin, the neuronal adhesion molecule axonin-1, and the signaling molecule semaphorin 4D that is involved in axonal guidance, immune function and angiogenesis.


Pssm-ID: 409570 [Multi-domain]  Cd Length: 88  Bit Score: 42.76  E-value: 5.03e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 4402 FKSGEPIFLDINISGEPAPDVTWNQNNKSVQTTSF-SHIENlpyNTKYINN-NPErkDTGLYKISAHNFYGQDQVEFQIN 4479
Cdd:cd20978    13 VKGGQDVTLPCQVTGVPQPKITWLHNGKPLQGPMErATVED---GTLTIINvQPE--DTGYYGCVATNEIGDIYTETLLH 87

                  .
gi 281359561 4480 I 4480
Cdd:cd20978    88 V 88
IgI_Twitchin_like cd20949
C-terminal immunoglobulin-like domain of the myosin-associated giant protein kinase Twitchin, ...
8840-8921 5.06e-04

C-terminal immunoglobulin-like domain of the myosin-associated giant protein kinase Twitchin, and similar domains; member of the I-set IgSF domains; The members here are composed of the C-terminal immunoglobulin-like domain of the myosin-associated giant protein kinase Twitchin and similar proteins, including Caenorhabditis elegans and Aplysia californica Twitchin, Drosophila melanogaster Projectin, and similar proteins. These are very large muscle proteins containing multiple immunoglobulin (Ig)-like and fibronectin type III (FN3) domains and a single kinase domain near the C-terminus. In humans these proteins are called Titin. The Ig superfamily (IgSF) is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. The Ig-like domain of the Twitchin is a member of the I-set IgSF domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand but lack a C" strand. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors, the hemolymph protein hemolin, the muscle proteins (titin, telokin, and twitchin), the neuronal adhesion molecule axonin-1, and the signaling molecule semaphorin 4D.


Pssm-ID: 409541 [Multi-domain]  Cd Length: 89  Bit Score: 42.70  E-value: 5.06e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 8840 SFVKFPTSVSVLEGEGTTFECEIDSELL-NLVWLKDGKPIDETlprysfTKDGHRYS-----FAVAKCNMDDVGQY--QA 8911
Cdd:cd20949     1 TFTENAYVTTVKEGQSATILCEVKGEPQpNVTWHFNGQPISAS------VADMSKYRiladgLLINKVTQDDTGEYtcRA 74
                          90
                  ....*....|
gi 281359561 8912 KAVSGKAESI 8921
Cdd:cd20949    75 YQVNSIASDM 84
IgI_Myotilin_C cd05892
C-terminal immunoglobulin (Ig)-like domain of myotilin; member of the I-set of Ig superfamily ...
7648-7735 5.10e-04

C-terminal immunoglobulin (Ig)-like domain of myotilin; member of the I-set of Ig superfamily (IgSF) domains; The members here are composed of the C-terminal immunoglobulin (Ig)-like domain of myotilin. Mytolin belongs to the palladin-myotilin-myopalladin family. Proteins belonging to the latter family contain multiple Ig-like domains and function as scaffolds, modulating the actin cytoskeleton. Myotilin is most abundant in skeletal and cardiac muscle and is involved in maintaining sarcomere integrity. It binds to alpha-actinin, filamin, and actin. Mutations in myotilin lead to muscle disorders. This group belongs to the I-set of IgSF domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand, but lack a C" strand.


Pssm-ID: 409473  Cd Length: 92  Bit Score: 42.83  E-value: 5.10e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 7648 PLIVKPLRDANCIQNHNAQFTCTINGVPKPTISWYKGAREIS-NGARYHMYSEGDN-HFLNINDVFGEDADEYVCRAVNK 7725
Cdd:cd05892     1 PMFIQKPQNKKVLEGDPVRLECQISAIPPPQIFWKKNNEMLQyNTDRISLYQDNCGrICLLIQNANKKDAGWYTVSAVNE 80
                          90
                  ....*....|
gi 281359561 7726 AGAKSTRATL 7735
Cdd:cd05892    81 AGVVSCNARL 90
Ig4_Peroxidasin cd05746
Fourth immunoglobulin (Ig)-like domain of peroxidasin; The members here are composed of the ...
8455-8523 5.35e-04

Fourth immunoglobulin (Ig)-like domain of peroxidasin; The members here are composed of the fourth immunoglobulin (Ig)-like domain in peroxidasin. Peroxidasin has a peroxidase domain and interacting extracellular motifs containing four Ig-like domains. It has been suggested that peroxidasin is secreted, and has functions related to the stabilization of the extracellular matrix. It may play a part in various other important processes such as removal and destruction of cells which have undergone programmed cell death and protection of the organism against non-self.


Pssm-ID: 143223  Cd Length: 69  Bit Score: 42.17  E-value: 5.35e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 281359561 8455 KLLCCLSGKPVPNVRWYKDGRELSkyEYAMTHSDGVVTMEIIDCKPSDSGKYSCKATNCHGTDETDCVV 8523
Cdd:cd05746     2 QIPCSAQGDPEPTITWNKDGVQVT--ESGKFHISPEGYLAIRDVGVADQGRYECVARNTIGYASVSMVL 68
IgI_Twitchin_like cd20949
C-terminal immunoglobulin-like domain of the myosin-associated giant protein kinase Twitchin, ...
544-626 5.37e-04

C-terminal immunoglobulin-like domain of the myosin-associated giant protein kinase Twitchin, and similar domains; member of the I-set IgSF domains; The members here are composed of the C-terminal immunoglobulin-like domain of the myosin-associated giant protein kinase Twitchin and similar proteins, including Caenorhabditis elegans and Aplysia californica Twitchin, Drosophila melanogaster Projectin, and similar proteins. These are very large muscle proteins containing multiple immunoglobulin (Ig)-like and fibronectin type III (FN3) domains and a single kinase domain near the C-terminus. In humans these proteins are called Titin. The Ig superfamily (IgSF) is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. The Ig-like domain of the Twitchin is a member of the I-set IgSF domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand but lack a C" strand. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors, the hemolymph protein hemolin, the muscle proteins (titin, telokin, and twitchin), the neuronal adhesion molecule axonin-1, and the signaling molecule semaphorin 4D.


Pssm-ID: 409541 [Multi-domain]  Cd Length: 89  Bit Score: 42.70  E-value: 5.37e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561  544 TFIEKPRIVSENNGKLVIMECKVKADPKPDVIWFRNGEVIKESnkIKTFIEQRGDQYYIKLELLdpQLEDSGLYKCNIKN 623
Cdd:cd20949     1 TFTENAYVTTVKEGQSATILCEVKGEPQPNVTWHFNGQPISAS--VADMSKYRILADGLLINKV--TQDDTGEYTCRAYQ 76

                  ...
gi 281359561  624 TLG 626
Cdd:cd20949    77 VNS 79
IgI_1_Titin_Z1z2-like cd20974
First Ig-like domain of the giant muscle protein titin Z1z2 in the sarcomeric Z-disk and ...
8839-8928 5.51e-04

First Ig-like domain of the giant muscle protein titin Z1z2 in the sarcomeric Z-disk and similar proteins; a member of the I-set of IgSF domains; The members here are composed of the first immunoglobulin (Ig)-like domain of the giant muscle protein titin Z1z2 in the sarcomeric Z-disk and similar proteins. Titin is a key component in the assembly and functioning of vertebrate striated muscles. By providing connections at the level of individual microfilaments, it contributes to the fine balance of forces between the two halves of the sarcomere. The Ig superfamily (IgSF) is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. Unlike the V-set, one of the distinctive features of I-set domains is the lack of a C" strand. The structure of the titin Z1z2 lacks this strand and thus it belongs to the I-set of the IgSF. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors, the hemolymph protein hemolin, the muscle proteins titin, telokin, and twitchin, the neuronal adhesion molecule axonin-1, and the signaling molecule semaphorin 4D that is involved in axonal guidance, immune function and angiogenesis.


Pssm-ID: 409566 [Multi-domain]  Cd Length: 93  Bit Score: 42.73  E-value: 5.51e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 8839 PSFVKFPTSVSVLEGEGTTFECEID-SELLNLVWLKDGKPID-ETLPRYSFTKDGHRYSFAVAKCNMDDVGQYQAKAVSG 8916
Cdd:cd20974     1 PVFTQPLQSVVVLEGSTATFEAHVSgKPVPEVSWFRDGQVIStSTLPGVQISFSDGRAKLSIPAVTKANSGRYSLTATNG 80
                          90
                  ....*....|..
gi 281359561 8917 KAESICAFSMNV 8928
Cdd:cd20974    81 SGQATSTAELLV 92
Ig_3 pfam13927
Immunoglobulin domain; This family contains immunoglobulin-like domains.
6855-6933 5.52e-04

Immunoglobulin domain; This family contains immunoglobulin-like domains.


Pssm-ID: 464046 [Multi-domain]  Cd Length: 78  Bit Score: 42.17  E-value: 5.52e-04
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 281359561  6855 PKITSdlSIRDMTVIAGDEFRITVPYHASPRPTASWSLNGLEVIPGERIKFDSNDYASMYYNKSAKRDETGSYTITLTN 6933
Cdd:pfam13927    2 PVITV--SPSSVTVREGETVTLTCEATGSPPPTITWYKNGEPISSGSTRSRSLSGSNSTLTISNVTRSDAGTYTCVASN 78
IgI_NCAM-1_like cd05732
Immunoglobulin (Ig)-like I-set domain of Neural Cell Adhesion Molecule 1 (NCAM-1) and similar ...
4685-4768 5.66e-04

Immunoglobulin (Ig)-like I-set domain of Neural Cell Adhesion Molecule 1 (NCAM-1) and similar proteins; The members here are composed of the fourth immunoglobulin (Ig)-like domain of Neural Cell Adhesion Molecule (NCAM-1). NCAM plays important roles in the development and regeneration of the central nervous system, in synaptogenesis and neural migration. NCAM mediates cell-cell and cell-substratum recognition and adhesion via homophilic (NCAM-NCAM), and heterophilic (NCAM-non-NCAM), interactions. NCAM is expressed as three major isoforms having different intracellular extensions. The extracellular portion of NCAM has five N-terminal Ig-like domains and two fibronectin type III domains. The double zipper adhesion complex model for NCAM homophilic binding involves Ig1, Ig2, and Ig3. By this model, Ig1 and Ig2 mediate dimerization of NCAM molecules situated on the same cell surface (cis interactions), and Ig3 domains mediate interactions between NCAM molecules expressed on the surface of opposing cells (trans interactions), through binding to the Ig1 and Ig2 domains. The adhesive ability of NCAM is modulated by the addition of polysialic acid chains to the fifth Ig-like domain. Also included in this group is NCAM-2 (also known as OCAM/mamFas II and RNCAM) NCAM-2 is differentially expressed in the developing and mature olfactory epithelium (OE). One of the unique features of I-set domains is the lack of a C" strand. The structures of this group show that the Ig domain lacks this strand and thus is a member of the I-set of Ig domains.


Pssm-ID: 409395 [Multi-domain]  Cd Length: 96  Bit Score: 42.90  E-value: 5.66e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 4685 PKIDRrnLRNITLSSGTALKLDANITGEPAPKVEWKLSNYHLQSGK-----NVTIETPDYYTKLVIRPTQRSDSGEYLVT 4759
Cdd:cd05732     3 PKITY--LENQTAVELEQITLTCEAEGDPIPEITWRRATRGISFEEgdldgRIVVRGHARVSSLTLKDVQLTDAGRYDCE 80

                  ....*....
gi 281359561 4760 ATNTSGKDS 4768
Cdd:cd05732    81 ASNRIGGDQ 89
IgI_4_Robo cd05726
Fourth immunoglobulin (Ig)-like domain in Robo (roundabout) receptors; member of the I-set of ...
2312-2397 6.01e-04

Fourth immunoglobulin (Ig)-like domain in Robo (roundabout) receptors; member of the I-set of Ig superfamily (IgSF) domains; Members here are composed the fourth immunoglobulin (Ig)-like domain in Robo (roundabout) receptors. Robo receptors play a role in the development of the central nervous system (CNS), and are receptors of Slit protein. Slit is a repellant secreted by the neural cells in the midline. Slit acts through Robo to prevent most neurons from crossing the midline from either side. Three mammalian Robo homologs (Robo1, Robo2, Robo3), and three mammalian Slit homologs (Slit-1, Slit-2, Slit-3), have been identified. Commissural axons, which cross the midline, express low levels of Robo; longitudinal axons, which avoid the midline, express high levels of Robo. Robo1, Robo2, and Robo3 are expressed by commissural neurons in the vertebrate spinal cord and Slit-1, Slit-2, and Slit-3 are expressed at the ventral midline. Robo-3 is a divergent member of the Robo family which instead of being a positive regulator of Slit responsiveness, antagonizes Slit responsiveness in precrossing axons. The Slit-Robo interaction is mediated by the second leucine-rich repeat (LRR) domain of Slit and the two N-terminal Ig domains of Robo, Ig1 and Ig2. The primary Robo binding site for Slit2 has been shown by surface plasmon resonance experiments and mutational analysis to be the Ig1 domain, while the Ig2 domain has been proposed to harbor a weak secondary binding site. This group belongs to the I-set of IgSF domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand, but lack a C" strand.


Pssm-ID: 409391 [Multi-domain]  Cd Length: 98  Bit Score: 43.02  E-value: 6.01e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 2312 KNVTVKKGQTIRFDIKYDGEPEPAATWVK-GTDNLKFDNQ------RICLDQlerNSSITIKKSVRKDTGKYKLVLSNSS 2384
Cdd:cd05726     7 RDQVVALGRTVTFQCETKGNPQPAIFWQKeGSQNLLFPYQppqpssRFSVSP---TGDLTITNVQRSDVGYYICQALNVA 83
                          90
                  ....*....|...
gi 281359561 2385 GTIESEAQVVVLD 2397
Cdd:cd05726    84 GSILAKAQLEVTD 96
IgI_2_Palladin_C cd20990
Second C-terminal immunoglobulin (Ig)-like domain of palladin; member of the I-set of Ig ...
4694-4775 6.08e-04

Second C-terminal immunoglobulin (Ig)-like domain of palladin; member of the I-set of Ig superfamily (IgSF) domains; The members here are composed of the C-terminal immunoglobulin (Ig)-like domain of palladin. Palladin belongs to the palladin-myotilin-myopalladin family. Proteins belonging to this family contain multiple Ig-like domains and function as scaffolds, modulating actin cytoskeleton. Palladin binds to alpha-actinin ezrin, vasodilator-stimulated phosphoprotein VASP, SPIN90 (also known as DIP or mDia interacting protein), and Src. Palladin also binds F-actin directly, via its Ig3 domain. Palladin is expressed as several alternatively spliced isoforms, having various combinations of Ig-like domains, in a cell-type-specific manner. It has been suggested that palladin's different Ig-like domains may be specialized for distinct functions. This group belongs to the I-set of IgSF domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand, but lack a C" strand.


Pssm-ID: 409582  Cd Length: 91  Bit Score: 42.78  E-value: 6.08e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 4694 NITLSSGTALKLDANITGEPAPKVEWKLSNYHLQ--SGKNVTIETPDYYTkLVIRPTQRSDSGEYLVTATNTSGKDSVLV 4771
Cdd:cd20990     9 DLTVQEGKLCRMDCKVSGLPTPDLSWQLDGKPIRpdSAHKMLVRENGVHS-LIIEPVTSRDAGIYTCIATNRAGQNSFNL 87

                  ....
gi 281359561 4772 NVVI 4775
Cdd:cd20990    88 ELVV 91
IgI_titin_I1-like cd20951
Immunoglobulin domain I1 of the titin I-band and similar proteins; a member of the I-set of ...
4685-4775 6.08e-04

Immunoglobulin domain I1 of the titin I-band and similar proteins; a member of the I-set of IgSF domains; The members here are composed of the immunoglobulin domain I1 of the titin I-band and similar proteins. Titin is a key component in the assembly and functioning of vertebrate striated muscles. By providing connections at the level of individual microfilaments, it contributes to the fine balance of forces between the two halves of the sarcomere. The Ig superfamily (IgSF) is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. The two sheets are linked together by a conserved disulfide bond between B strand and F strand. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. The Ig I1 domain of the titin I-band is a member of the I-set Ig domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand but lack a C" strand. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors, the hemolymph protein hemolin, the muscle proteins titin, telokin, and twitchin, the neuronal adhesion molecule axonin-1, and the signaling molecule semaphorin 4D that is involved in axonal guidance, immune function and angiogenesis.


Pssm-ID: 409543 [Multi-domain]  Cd Length: 94  Bit Score: 42.79  E-value: 6.08e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 4685 PKIDRRnLRNITLSSGTALKLDANITGEPAPKVEW-----KLSNyhLQSGKNVTIETPDYYTKLVIRPTQRSDSGEYLVT 4759
Cdd:cd20951     1 PEFIIR-LQSHTVWEKSDAKLRVEVQGKPDPEVKWykngvPIDP--SSIPGKYKIESEYGVHVLHIRRVTVEDSAVYSAV 77
                          90
                  ....*....|....*.
gi 281359561 4760 ATNTSGKDSVLVNVVI 4775
Cdd:cd20951    78 AKNIHGEASSSASVVV 93
IgI_4_hemolin-like cd20978
Fourth immunoglobulin (Ig)-like domain of hemolin, and similar domains; a member of the I-set ...
4685-4773 6.18e-04

Fourth immunoglobulin (Ig)-like domain of hemolin, and similar domains; a member of the I-set of IgSF domains; The members here are composed of the fourth immunoglobulin (Ig)-like domain of hemolin and similar proteins. Hemolin, an insect immunoglobulin superfamily (IgSF) member containing four Ig-like domains, is a lipopolysaccharide-binding immune protein induced during bacterial infection. Hemolin shares significant sequence similarity with the first four Ig-like domains of the transmembrane cell adhesion molecules (CAMs) of the L1 family. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. The fourth Ig-like domain of hemolin is a member of the I-set Ig domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set domains, members of the I-set have a discontinuous A strand but lack a C" strand. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors, the muscle proteins titin, telokin, and twitchin, the neuronal adhesion molecule axonin-1, and the signaling molecule semaphorin 4D that is involved in axonal guidance, immune function and angiogenesis.


Pssm-ID: 409570 [Multi-domain]  Cd Length: 88  Bit Score: 42.38  E-value: 6.18e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 4685 PKIDRRNLRNITLSSGTALKLDANITGEPAPKVEWklsnyhLQSGKNVTIETPDY-YTK--LVIRPTQRSDSGEYLVTAT 4761
Cdd:cd20978     1 PKFIQKPEKNVVVKGGQDVTLPCQVTGVPQPKITW------LHNGKPLQGPMERAtVEDgtLTIINVQPEDTGYYGCVAT 74
                          90
                  ....*....|....
gi 281359561 4762 NTSGK--DSVLVNV 4773
Cdd:cd20978    75 NEIGDiyTETLLHV 88
IgI_APEG-1_like cd20975
Immunoglobulin-like domain of human Aortic Preferentially Expressed Protein-1 (APEG-1) and ...
5570-5660 6.23e-04

Immunoglobulin-like domain of human Aortic Preferentially Expressed Protein-1 (APEG-1) and similar proteins; a member of the I-set of IgSF domains; The members here are composed of the immunoglobulin I-set (IgI) domain of the Human Aortic Preferentially Expressed Protein-1 (APEG-1) and similar proteins. APEG-1 is a novel specific smooth muscle differentiation marker predicted to play a role in the growth and differentiation of arterial smooth muscle cells (SMCs). The Ig superfamily (IgSF) is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. Unlike the V-set, one of the distinctive features of I-set domains is the lack of a C" strand. The structure of the human APEG-1 lacks this strand and thus it belongs to the I-set of the IgSF. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors, the hemolymph protein hemolin, the muscle proteins titin, telokin, and twitchin, the neuronal adhesion molecule axonin-1, and the signaling molecule semaphorin 4D that is involved in axonal guidance, immune function and angiogenesis.


Pssm-ID: 409567  Cd Length: 91  Bit Score: 42.46  E-value: 6.23e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 5570 PFFDKSLLnDITVHAGKRLGWTLPIEASPRPLITWLYNGKEIGSNSR-----GESGLFQneltFEIVSSLRSDEGRYTLI 5644
Cdd:cd20975     1 PTFKVSLM-DQSVREGQDVIMSIRVQGEPKPVVSWLRNRQPVRPDQRrfaeeAEGGLCR----LRILAAERGDAGFYTCK 75
                          90
                  ....*....|....*.
gi 281359561 5645 LKNEHGSFDASAHATV 5660
Cdd:cd20975    76 AVNEYGARQCEARLEV 91
IgI_Myomesin_like_C cd05737
C-terminal immunoglobulin (Ig)-like domain of myomesin and M-protein; member of the I-set of ...
7650-7737 6.31e-04

C-terminal immunoglobulin (Ig)-like domain of myomesin and M-protein; member of the I-set of Ig superfamily (IgSF) domains; The members here are composed of the C-terminal immunoglobulin (Ig)-like domain of myomesin and M-protein (also known as myomesin-2). Myomesin and M-protein are both structural proteins localized to the M-band, a transverse structure in the center of the sarcomere, and are candidates for M-band bridges. Both proteins are modular, consisting mainly of repetitive Ig-like and fibronectin type III (FnIII) domains. Myomesin is expressed in all types of vertebrate striated muscle; M-protein has a muscle-type specific expression pattern. Myomesin is present in both slow and fast fibers; M-protein is present only in fast fibers. It has been suggested that myomesin acts as a molecular spring with alternative splicing as a means of modifying its elasticity.


Pssm-ID: 319300  Cd Length: 92  Bit Score: 42.58  E-value: 6.31e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 7650 IVKPLRDANCIQNHNA-QFTCTINGVPKPTISWYKGAREISNGARYHM-YSEGDNHFLNINDVFGEDADEYVCRAVNKAG 7727
Cdd:cd05737     3 VLGGLPDVVTIMEGKTlNLTCNVWGDPPPEVSWLKNDQALAFLDHCNLkVEAGRTVYFTINGVSSEDSGKYGLVVKNKYG 82
                          90
                  ....*....|
gi 281359561 7728 AKSTRATLAI 7737
Cdd:cd05737    83 SETSDVTVSV 92
Ig4_Contactin-2-like cd05728
Fourth Ig domain of the neural cell adhesion molecule contactin-2, and similar domains; The ...
2617-2693 6.85e-04

Fourth Ig domain of the neural cell adhesion molecule contactin-2, and similar domains; The members here are composed of the fourth Ig domain of the neural cell adhesion molecule contactin-2. Contactins are comprised of six Ig domains followed by four fibronectin type III (FnIII) domains anchored to the membrane by glycosylphosphatidylinositol. Contactin-2 (also called TAG-1, axonin-1) facilitates cell adhesion by homophilic binding between molecules in apposed membranes. The first four Ig domains form the intermolecular binding fragment which arranges as a compact U-shaped module by contacts between Ig domains 1 and 4, and domains 2 and 3. It has been proposed that a linear zipper-like array forms, from contactin-2 molecules alternatively provided by the two apposed membranes.


Pssm-ID: 143205 [Multi-domain]  Cd Length: 85  Bit Score: 42.20  E-value: 6.85e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 281359561 2617 GRTHKWSVDVLGEPIPELHWsWRDDIPLTNGDRIKIENvdyhTDFSITNVLRKDSGFYTLKAENRNGIDRETVELVV 2693
Cdd:cd05728    14 GSSLRWECKASGNPRPAYRW-LKNGQPLASENRIEVEA----GDLRITKLSLSDSGMYQCVAENKHGTIYASAELAV 85
IgI_4_MYLK-like cd20976
Fourth Ig-like domain from smooth muscle myosin light chain kinase and similar domains ; a ...
5575-5660 7.22e-04

Fourth Ig-like domain from smooth muscle myosin light chain kinase and similar domains ; a member of the I-set of IgSF domains; The members here are composed of the fourth immunoglobulin (Ig)-like domain from smooth muscle myosin light chain kinase (MYLK) and similar domains. The Ig superfamily (IgSF) is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. Unlike the V-set, one of the distinctive features of I-set domains is the lack of a C" strand. The structure of this group shows that the fourth Ig-like domain from myosin light chain kinase lacks this strand and thus belongs to the I-set of the IgSF. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors, the hemolymph protein hemolin, the muscle proteins titin, telokin, and twitchin, the neuronal adhesion molecule axonin-1, and the signaling molecule semaphorin 4D that is involved in axonal guidance, immune function and angiogenesis.


Pssm-ID: 409568 [Multi-domain]  Cd Length: 90  Bit Score: 42.24  E-value: 7.22e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 5575 SLLNDITVHAGKRLGWTLPIEASPRPLITWLYNGKEI---GSNSRGESGLfqNELTfeIVSSLRSDEGRYTLILKNEHGS 5651
Cdd:cd20976     6 SVPKDLEAVEGQDFVAQCSARGKPVPRITWIRNAQPLqyaADRSTCEAGV--GELH--IQDVLPEDHGTYTCLAKNAAGQ 81

                  ....*....
gi 281359561 5652 FDASAHATV 5660
Cdd:cd20976    82 VSCSAWVTV 90
Ig_3 pfam13927
Immunoglobulin domain; This family contains immunoglobulin-like domains.
656-721 7.27e-04

Immunoglobulin domain; This family contains immunoglobulin-like domains.


Pssm-ID: 464046 [Multi-domain]  Cd Length: 78  Bit Score: 41.78  E-value: 7.27e-04
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 281359561   656 TVVIECTVASKFEPKCTWYKEtSTVKESKRHVYQVEQTKEGEfavkLEINDVEESDKGAYKLVASN 721
Cdd:pfam13927   18 TVTLTCEATGSPPPTITWYKN-GEPISSGSTRSRSLSGSNST----LTISNVTRSDAGTYTCVASN 78
Ig cd00096
Immunoglobulin domain; The members here are composed of the immunoglobulin (Ig) domain found ...
3522-3581 7.35e-04

Immunoglobulin domain; The members here are composed of the immunoglobulin (Ig) domain found in the Ig superfamily. The Ig superfamily is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. Members of this group are components of immunoglobulin, neuroglia, cell surface glycoproteins, including T-cell receptors, CD2, CD4, CD8, and membrane glycoproteins, including butyrophilin and chondroitin sulfate proteoglycan core protein. A predominant feature of most Ig domains is a disulfide bridge connecting the two beta-sheets with a tryptophan residue packed against the disulfide bond. Ig superfamily (IgSF) domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. Typically, the V-set domains have A, B, E, and D strands in one sheet and A', G, F, C, C' and C" in the other. The structures in C1-set are smaller than those in the V-set; they have one beta sheet that is formed by strands A, B, E, and D and the other by strands G, F, C, and C'. Moreover, a C1-set Ig domain contains a short C' strand (three residues) and lacks A' and C" strand. Unlike other Ig domain sets, C2-set structures do not have a D strand. Like the V-set Ig domains, members of the I-set have a discontinuous A strand, but lack a C" strand.


Pssm-ID: 409353 [Multi-domain]  Cd Length: 70  Bit Score: 41.55  E-value: 7.35e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 3522 NIRGEPAPKVEWFFNNSSVTSDEHSvKIDNVDYNTKFFVMRAQRSQSGKYIIKATNEVGE 3581
Cdd:cd00096     6 SASGNPPPTITWYKNGKPLPPSSRD-SRRSELGNGTLTISNVTLEDSGTYTCVASNSAGG 64
Ig_C5_MyBP-C cd05894
C5 immunoglobulin (Ig) domain of cardiac myosin binding protein C (MyBP-C); The members here ...
2612-2693 8.04e-04

C5 immunoglobulin (Ig) domain of cardiac myosin binding protein C (MyBP-C); The members here are composed of the C5 immunoglobulin (Ig) domain of cardiac myosin binding protein C (MyBP-C). MyBP-C consists of repeated domains, Ig and fibronectin type 3, and various linkers. Three isoforms of MYBP-C exist: slow-skeletal (ssMyBP-C), fast-skeletal (fsMyBP-C), and cardiac (cMyBP-C). cMYBP-C has insertions between and inside domains and an additional cardiac-specific Ig domain at the N-terminus. For cMYBP_C an interaction has been demonstrated between this C5 domain and the Ig C8 domain.


Pssm-ID: 409475  Cd Length: 86  Bit Score: 42.13  E-value: 8.04e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 2612 VTIKSGRTHKWSVDVLGEPIPELHWSwRDDIPLTNGD-RIKIENVDYHTDFSITNVLRKDSGFYTLKAENRNGIDRETVE 2690
Cdd:cd05894     5 IVVVAGNKLRLDVPISGEPAPTVTWS-RGDKAFTATEgRVRVESYKDLSSFVIEGAEREDEGVYTITVTNPVGEDHASLF 83

                  ...
gi 281359561 2691 LVV 2693
Cdd:cd05894    84 VKV 86
IgI_telokin-like cd20973
immunoglobulin-like domain of telokin and similar proteins; a member of the I-set of IgSF ...
2917-2995 8.05e-04

immunoglobulin-like domain of telokin and similar proteins; a member of the I-set of IgSF domains; The members here are composed of the immunoglobulin (Ig) domain in telokin, the C-terminal domain of myosin light chain kinase which is identical to telokin, and similar proteins. The Ig superfamily (IgSF) is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. Unlike the V-set, one of the distinctive features of I-set domains is the lack of a C" strand. The structure of the telokin Ig domain lacks this strand and thus it belongs to the I-set of the IgSF. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors, the hemolymph protein hemolin, the muscle proteins titin, telokin, and twitchin, the neuronal adhesion molecule axonin-1, and the signaling molecule semaphorin 4D that is involved in axonal guidance, immune function and angiogenesis.


Pssm-ID: 409565 [Multi-domain]  Cd Length: 88  Bit Score: 42.18  E-value: 8.05e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 2917 GKPIRYDVNVRGEPAPVITWYQNDKELKpeelpSSSEIKNI---PYNTKISIIETVRKHTGIYKIIAVNEHGQDEATVEV 2993
Cdd:cd20973    12 GSAARFDCKVEGYPDPEVKWMKDDNPIV-----ESRRFQIDqdeDGLCSLIISDVCGDDSGKYTCKAVNSLGEATCSAEL 86

                  ..
gi 281359561 2994 NI 2995
Cdd:cd20973    87 TV 88
Ig cd00096
Immunoglobulin domain; The members here are composed of the immunoglobulin (Ig) domain found ...
5874-5944 8.60e-04

Immunoglobulin domain; The members here are composed of the immunoglobulin (Ig) domain found in the Ig superfamily. The Ig superfamily is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. Members of this group are components of immunoglobulin, neuroglia, cell surface glycoproteins, including T-cell receptors, CD2, CD4, CD8, and membrane glycoproteins, including butyrophilin and chondroitin sulfate proteoglycan core protein. A predominant feature of most Ig domains is a disulfide bridge connecting the two beta-sheets with a tryptophan residue packed against the disulfide bond. Ig superfamily (IgSF) domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. Typically, the V-set domains have A, B, E, and D strands in one sheet and A', G, F, C, C' and C" in the other. The structures in C1-set are smaller than those in the V-set; they have one beta sheet that is formed by strands A, B, E, and D and the other by strands G, F, C, and C'. Moreover, a C1-set Ig domain contains a short C' strand (three residues) and lacks A' and C" strand. Unlike other Ig domain sets, C2-set structures do not have a D strand. Like the V-set Ig domains, members of the I-set have a discontinuous A strand, but lack a C" strand.


Pssm-ID: 409353 [Multi-domain]  Cd Length: 70  Bit Score: 41.55  E-value: 8.60e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 281359561 5874 VRIKCglifhtdiHFIGEPAPEATWTLNSNPLLSNDRSTITSIGHHSVVHTVNCQRSDSGIYHLLLRNSSG 5944
Cdd:cd00096     1 VTLTC--------SASGNPPPTITWYKNGKPLPPSSRDSRRSELGNGTLTISNVTLEDSGTYTCVASNSAG 63
IgI_NCAM-1_like cd05732
Immunoglobulin (Ig)-like I-set domain of Neural Cell Adhesion Molecule 1 (NCAM-1) and similar ...
443-532 8.61e-04

Immunoglobulin (Ig)-like I-set domain of Neural Cell Adhesion Molecule 1 (NCAM-1) and similar proteins; The members here are composed of the fourth immunoglobulin (Ig)-like domain of Neural Cell Adhesion Molecule (NCAM-1). NCAM plays important roles in the development and regeneration of the central nervous system, in synaptogenesis and neural migration. NCAM mediates cell-cell and cell-substratum recognition and adhesion via homophilic (NCAM-NCAM), and heterophilic (NCAM-non-NCAM), interactions. NCAM is expressed as three major isoforms having different intracellular extensions. The extracellular portion of NCAM has five N-terminal Ig-like domains and two fibronectin type III domains. The double zipper adhesion complex model for NCAM homophilic binding involves Ig1, Ig2, and Ig3. By this model, Ig1 and Ig2 mediate dimerization of NCAM molecules situated on the same cell surface (cis interactions), and Ig3 domains mediate interactions between NCAM molecules expressed on the surface of opposing cells (trans interactions), through binding to the Ig1 and Ig2 domains. The adhesive ability of NCAM is modulated by the addition of polysialic acid chains to the fifth Ig-like domain. Also included in this group is NCAM-2 (also known as OCAM/mamFas II and RNCAM) NCAM-2 is differentially expressed in the developing and mature olfactory epithelium (OE). One of the unique features of I-set domains is the lack of a C" strand. The structures of this group show that the Ig domain lacks this strand and thus is a member of the I-set of Ig domains.


Pssm-ID: 409395 [Multi-domain]  Cd Length: 96  Bit Score: 42.13  E-value: 8.61e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561  443 KPRIIPNESGTL-----ITMKCKCKAKPEPTVTWYRGQDLVEKSKKIKINTTVIAEDTYELTLEIKDPGATDGGTYRCNV 517
Cdd:cd05732     2 QPKITYLENQTAveleqITLTCEAEGDPIPEITWRRATRGISFEEGDLDGRIVVRGHARVSSLTLKDVQLTDAGRYDCEA 81
                          90
                  ....*....|....*
gi 281359561  518 KNEYGESNANLNLNI 532
Cdd:cd05732    82 SNRIGGDQQSMYLEV 96
IgI_5_Robo cd20952
Fifth Ig-like domain of Roundabout (Robo) homolog 1/2, and similar domains; a member of the ...
11-101 8.96e-04

Fifth Ig-like domain of Roundabout (Robo) homolog 1/2, and similar domains; a member of the I-set of IgSF domains; The members here are composed of the fifth Ig-like domain of Roundabout (Robo) homolog 1/2 and similar domains. Robo receptors play a role in the development of the central nervous system (CNS), and are receptors of Slit protein. Slit is a repellant secreted by the neural cells in the midline. Slit acts through Robo to prevent most neurons from crossing the midline from either side. Three mammalian Robo homologs (Robo1, -2, and -3), and three mammalian Slit homologs (Slit-1,-2, -3), have been identified. Commissural axons, which cross the midline, express low levels of Robo; longitudinal axons, which avoid the midline, express high levels of Robo. Robo1, -2, and -3 are expressed by commissural neurons in the vertebrate spinal cord and Slits 1, -2, -3 are expressed at the ventral midline. Robo-3 is a divergent member of the Robo family which instead of being a positive regulator of slit responsiveness, antagonizes slit responsiveness in precrossing axons. The Slit-Robo interaction is mediated by the second leucine-rich repeat (LRR) domain of Slit and the two N-terminal Ig domains of Robo, Ig1 and Ig2. The primary Robo binding site for Slit2 has been shown by surface plasmon resonance experiments and mutational analysis to be is the Ig1 domain, while the Ig2 domain has been proposed to harbor a weak secondary binding site. The fifth Ig-like domain of Robo 1 and 2 is a member of the I-set Ig domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand but lack a C" strand. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors


Pssm-ID: 409544 [Multi-domain]  Cd Length: 87  Bit Score: 42.10  E-value: 8.96e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561   11 FVKKPQLHQEDDGNRLIFECQLLSSPKPDIEWFRSDNKV-VEDVRtkFKIQPVGenkytvVLELDDVVETDAGLYKVKAK 89
Cdd:cd20952     2 ILQGPQNQTVAVGGTVVLNCQATGEPVPTISWLKDGVPLlGKDER--ITTLENG------SLQIKGAEKSDTGEYTCVAL 73
                          90
                  ....*....|..
gi 281359561   90 NKSGEVSASINL 101
Cdd:cd20952    74 NLSGEATWSAVL 85
IgI_4_hemolin-like cd20978
Fourth immunoglobulin (Ig)-like domain of hemolin, and similar domains; a member of the I-set ...
2917-2993 9.14e-04

Fourth immunoglobulin (Ig)-like domain of hemolin, and similar domains; a member of the I-set of IgSF domains; The members here are composed of the fourth immunoglobulin (Ig)-like domain of hemolin and similar proteins. Hemolin, an insect immunoglobulin superfamily (IgSF) member containing four Ig-like domains, is a lipopolysaccharide-binding immune protein induced during bacterial infection. Hemolin shares significant sequence similarity with the first four Ig-like domains of the transmembrane cell adhesion molecules (CAMs) of the L1 family. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. The fourth Ig-like domain of hemolin is a member of the I-set Ig domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set domains, members of the I-set have a discontinuous A strand but lack a C" strand. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors, the muscle proteins titin, telokin, and twitchin, the neuronal adhesion molecule axonin-1, and the signaling molecule semaphorin 4D that is involved in axonal guidance, immune function and angiogenesis.


Pssm-ID: 409570 [Multi-domain]  Cd Length: 88  Bit Score: 41.99  E-value: 9.14e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 281359561 2917 GKPIRYDVNVRGEPAPVITWYQNDKELKpeelpSSSEIKNIPYNTkISIIETVRKHTGIYKIIAVNEHG--QDEATVEV 2993
Cdd:cd20978    16 GQDVTLPCQVTGVPQPKITWLHNGKPLQ-----GPMERATVEDGT-LTIINVQPEDTGYYGCVATNEIGdiYTETLLHV 88
IgI_1_MuSK cd20970
agrin-responsive first immunoglobulin-like domains (Ig1) of the MuSK ectodomain; a member of ...
3509-3590 9.23e-04

agrin-responsive first immunoglobulin-like domains (Ig1) of the MuSK ectodomain; a member of the I-set of IgSF domains; The members here are composed of the first immunoglobulin-like domains (Ig1) of the Muscle-specific kinase (MuSK). MuSK is a receptor tyrosine kinase specifically expressed in skeletal muscle, where it plays a central role in the formation and maintenance of the neuromuscular junction (NMJ). MuSK is activated by agrin, a neuron-derived heparan sulfate proteoglycan. The activation of MUSK in myotubes regulates the formation of NMJs through the regulation of different processes including the specific expression of genes in subsynaptic nuclei, the reorganization of the actin cytoskeleton and the clustering of the acetylcholine receptors (AChR) in the postsynaptic membrane. The Ig superfamily (IgSF) is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. Unlike the V-set, one of the distinctive features of I-set domains is the lack of a C" strand. The structure of the MuSK lacks this strand and thus it belongs to the I-set of the IgSF. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors, the hemolymph protein hemolin, the muscle proteins titin, telokin, and twitchin, the neuronal adhesion molecule axonin-1, and the signaling molecule semaphorin 4D that is involved in axonal guidance, immune function and angiogenesis.


Pssm-ID: 409562 [Multi-domain]  Cd Length: 92  Bit Score: 42.11  E-value: 9.23e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 3509 VIVKTGLSISLDINIRGEPAPKVEWFFNNSSV--TSDEHSVKIDNvdynTKFFVMRAQRSQSGKYIIKATNEV-GEDEAE 3585
Cdd:cd20970    12 VTAREGENATFMCRAEGSPEPEISWTRNGNLIieFNTRYIVRENG----TTLTIRNIRRSDMGIYLCIASNGVpGSVEKR 87

                  ....*
gi 281359561 3586 LEVTV 3590
Cdd:cd20970    88 ITLQV 92
Ig_Pro_neuregulin cd05750
Immunoglobulin (Ig)-like domain in neuregulins; The members here are composed of the ...
7670-7737 9.48e-04

Immunoglobulin (Ig)-like domain in neuregulins; The members here are composed of the immunoglobulin (Ig)-like domain in neuregulins (NRGs). NRGs are signaling molecules which participate in cell-cell interactions in the nervous system, breast, heart, and other organ systems, and are implicated in the pathology of diseases including schizophrenia, multiple sclerosis, and breast cancer. There are four members of the neuregulin gene family (NRG-1, NRG-2, NRG-3, and NRG-4). The NRG-1 protein, binds to and activates the tyrosine kinases receptors ErbB3 and ErbB4, initiating signaling cascades. The other NRGs proteins bind one or the other or both of these ErbBs. NRG-1 has multiple functions: in the brain it regulates various processes such as radial glia formation and neuronal migration, dendritic development, and expression of neurotransmitters receptors, while in the peripheral nervous system NRG-1 regulates processes such as target cell differentiation, and Schwann cell survival. There are many NRG-1 isoforms which arise from the alternative splicing of mRNA. Less is known of the functions of the other NRGs. NRG-2 and NRG-3 are expressed predominantly in the nervous system. NRG-2 is expressed by motor neurons and terminal Schwann cells, and is concentrated near synaptic sites and may be a signal that regulates synaptic differentiation. NRG-4 has been shown to direct pancreatic islet cell development towards the delta-cell lineage.


Pssm-ID: 409408 [Multi-domain]  Cd Length: 92  Bit Score: 42.11  E-value: 9.48e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 7670 TINGVPKPTISWYKGAREISNGARYHMYSEGD--NHFLNINDVFGEDADEYVCRAVNKAGAKSTRATLAI 7737
Cdd:cd05750    23 ATSENPSPRYRWFKDGKELNRKRPKNIKIRNKkkNSELQINKAKLEDSGEYTCVVENILGKDTVTGNVTV 92
IgI_1_Titin_Z1z2-like cd20974
First Ig-like domain of the giant muscle protein titin Z1z2 in the sarcomeric Z-disk and ...
7254-7339 9.62e-04

First Ig-like domain of the giant muscle protein titin Z1z2 in the sarcomeric Z-disk and similar proteins; a member of the I-set of IgSF domains; The members here are composed of the first immunoglobulin (Ig)-like domain of the giant muscle protein titin Z1z2 in the sarcomeric Z-disk and similar proteins. Titin is a key component in the assembly and functioning of vertebrate striated muscles. By providing connections at the level of individual microfilaments, it contributes to the fine balance of forces between the two halves of the sarcomere. The Ig superfamily (IgSF) is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. Unlike the V-set, one of the distinctive features of I-set domains is the lack of a C" strand. The structure of the titin Z1z2 lacks this strand and thus it belongs to the I-set of the IgSF. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors, the hemolymph protein hemolin, the muscle proteins titin, telokin, and twitchin, the neuronal adhesion molecule axonin-1, and the signaling molecule semaphorin 4D that is involved in axonal guidance, immune function and angiogenesis.


Pssm-ID: 409566 [Multi-domain]  Cd Length: 93  Bit Score: 41.95  E-value: 9.62e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 7254 PDWITRLQDKVAPFGKDYTLQCAASGKPSPTARWLRNGKEIQMNGG-RMTCDSKDGVFRLHISNVQTGDDGDYTCEAMNS 7332
Cdd:cd20974     1 PVFTQPLQSVVVLEGSTATFEAHVSGKPVPEVSWFRDGQVISTSTLpGVQISFSDGRAKLSIPAVTKANSGRYSLTATNG 80

                  ....*...
gi 281359561 7333 LG-FVNTS 7339
Cdd:cd20974    81 SGqATSTA 88
Ig_C5_MyBP-C cd05894
C5 immunoglobulin (Ig) domain of cardiac myosin binding protein C (MyBP-C); The members here ...
557-636 1.05e-03

C5 immunoglobulin (Ig) domain of cardiac myosin binding protein C (MyBP-C); The members here are composed of the C5 immunoglobulin (Ig) domain of cardiac myosin binding protein C (MyBP-C). MyBP-C consists of repeated domains, Ig and fibronectin type 3, and various linkers. Three isoforms of MYBP-C exist: slow-skeletal (ssMyBP-C), fast-skeletal (fsMyBP-C), and cardiac (cMyBP-C). cMYBP-C has insertions between and inside domains and an additional cardiac-specific Ig domain at the N-terminus. For cMYBP_C an interaction has been demonstrated between this C5 domain and the Ig C8 domain.


Pssm-ID: 409475  Cd Length: 86  Bit Score: 41.75  E-value: 1.05e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561  557 GKLVIMECKVKADPKPDVIWFRNGEVIKESNKiKTFIEQRGDQYYIKLELldPQLEDSGLYKCNIKNTLGELNANLTLNI 636
Cdd:cd05894    10 GNKLRLDVPISGEPAPTVTWSRGDKAFTATEG-RVRVESYKDLSSFVIEG--AEREDEGVYTITVTNPVGEDHASLFVKV 86
IgI_Myotilin_C_like cd05744
Immunoglobulin (Ig)-like domain of myotilin, palladin, and myopalladin; member of the I-set of ...
5890-5954 1.05e-03

Immunoglobulin (Ig)-like domain of myotilin, palladin, and myopalladin; member of the I-set of Ig superfamily (IgSF) domains; The members here are composed of the immunoglobulin (Ig)-like domain in myotilin, palladin, and myopalladin. Myotilin, palladin, and myopalladin function as scaffolds that regulate actin organization. Myotilin and myopalladin are most abundant in skeletal and cardiac muscle; palladin is ubiquitously expressed in the organs of developing vertebrates and plays a key role in cellular morphogenesis. The three family members each interact with specific molecular partners with all three binding to alpha-actinin; In addition, palladin also binds to vasodilator-stimulated phosphoprotein (VASP) and ezrin, myotilin binds to filamin and actin, and myopalladin also binds to nebulin and cardiac ankyrin repeat protein (CARP). This group belongs to the I-set of IgSF domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand, but lack a C" strand.


Pssm-ID: 409405 [Multi-domain]  Cd Length: 91  Bit Score: 42.10  E-value: 1.05e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 281359561 5890 GEPAPEATWTLNSNPLLSNDRSTI--TSIGHHSVVHTvNCQRSDSGIYHLLLRNSSGIDEGSFELVV 5954
Cdd:cd05744    26 GLPTPDLFWQLNGKPVRPDSAHKMlvRENGRHSLIIE-PVTKRDAGIYTCIARNRAGENSFNAELVV 91
Ig_Titin_like cd05748
Immunoglobulin (Ig)-like domain of titin and similar proteins; The members here are composed ...
7671-7730 1.07e-03

Immunoglobulin (Ig)-like domain of titin and similar proteins; The members here are composed of the immunoglobulin (Ig)-like domain found in titin-like proteins and similar proteins. Titin (also called connectin) is a fibrous sarcomeric protein specifically found in vertebrate striated muscle. Titin is a giant protein; depending on isoform composition, it ranges from 2970 to 3700 kDa, and is of a length that spans half a sarcomere. Titin largely consists of multiple repeats of Ig-like and fibronectin type 3 (FN-III)-like domains. Titin connects the ends of myosin thick filaments to Z disks and extends along the thick filament to the H zone. It appears to function similarly to an elastic band, keeping the myosin filaments centered in the sarcomere during muscle contraction or stretching. Within the sarcomere, titin is also attached to or is associated with myosin binding protein C (MyBP-C). MyBP-C appears to contribute to the generation of passive tension by titin and like titin has repeated Ig-like and FN-III domains. Also included in this group are worm twitchin and insect projectin, thick filament proteins of invertebrate muscle which also have repeated Ig-like and FN-III domains.


Pssm-ID: 409406 [Multi-domain]  Cd Length: 82  Bit Score: 41.42  E-value: 1.07e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 7671 INGVPKPTISWYKGAREISNGARYHMYSEGDNHFLNINDVFGEDADEYVCRAVNKAGAKS 7730
Cdd:cd05748    16 IKGRPTPTVTWSKDGQPLKETGRVQIETTASSTSLVIKNAKRSDSGKYTLTLKNSAGEKS 75
IgI_M-protein_C cd05891
C-terminal immunoglobulin (Ig)-like domain of M-protein; member of the I-set of Ig superfamily ...
8751-8831 1.07e-03

C-terminal immunoglobulin (Ig)-like domain of M-protein; member of the I-set of Ig superfamily (IgSF) domains; The members here are composed of the C-terminal immunoglobulin (Ig)-like domain of M-protein (also known as myomesin-2). M-protein is a structural protein localized to the M-band, a transverse structure in the center of the sarcomere, and is a candidate for M-band bridges. M-protein is modular consisting mainly of repetitive IG-like and fibronectin type III (FnIII) domains and has a muscle-type specific expression pattern. M-protein is present in fast fibers.


Pssm-ID: 143299  Cd Length: 92  Bit Score: 41.82  E-value: 1.07e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 8751 VRDGDAVNLACRIIGAQHFDVVWLHNNKEIKPSKDFQYTNEANIY-RLQIAEIFPEDGGTYTCEAFNDIGESfstcTINV 8829
Cdd:cd05891    13 IMEGKTLNLTCTVFGNPDPEVIWFKNDQDIELSEHYSVKLEQGKYaSLTIKGVTSEDSGKYSINVKNKYGGE----TVDV 88

                  ..
gi 281359561 8830 TV 8831
Cdd:cd05891    89 TV 90
Ig_Titin_like cd05748
Immunoglobulin (Ig)-like domain of titin and similar proteins; The members here are composed ...
7278-7334 1.11e-03

Immunoglobulin (Ig)-like domain of titin and similar proteins; The members here are composed of the immunoglobulin (Ig)-like domain found in titin-like proteins and similar proteins. Titin (also called connectin) is a fibrous sarcomeric protein specifically found in vertebrate striated muscle. Titin is a giant protein; depending on isoform composition, it ranges from 2970 to 3700 kDa, and is of a length that spans half a sarcomere. Titin largely consists of multiple repeats of Ig-like and fibronectin type 3 (FN-III)-like domains. Titin connects the ends of myosin thick filaments to Z disks and extends along the thick filament to the H zone. It appears to function similarly to an elastic band, keeping the myosin filaments centered in the sarcomere during muscle contraction or stretching. Within the sarcomere, titin is also attached to or is associated with myosin binding protein C (MyBP-C). MyBP-C appears to contribute to the generation of passive tension by titin and like titin has repeated Ig-like and FN-III domains. Also included in this group are worm twitchin and insect projectin, thick filament proteins of invertebrate muscle which also have repeated Ig-like and FN-III domains.


Pssm-ID: 409406 [Multi-domain]  Cd Length: 82  Bit Score: 41.42  E-value: 1.11e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 281359561 7278 SGKPSPTARWLRNGKEIqMNGGRMTCDSKDGVFRLHISNVQTGDDGDYTCEAMNSLG 7334
Cdd:cd05748    17 KGRPTPTVTWSKDGQPL-KETGRVQIETTASSTSLVIKNAKRSDSGKYTLTLKNSAG 72
IgI_Myotilin_C_like cd05744
Immunoglobulin (Ig)-like domain of myotilin, palladin, and myopalladin; member of the I-set of ...
1827-1897 1.11e-03

Immunoglobulin (Ig)-like domain of myotilin, palladin, and myopalladin; member of the I-set of Ig superfamily (IgSF) domains; The members here are composed of the immunoglobulin (Ig)-like domain in myotilin, palladin, and myopalladin. Myotilin, palladin, and myopalladin function as scaffolds that regulate actin organization. Myotilin and myopalladin are most abundant in skeletal and cardiac muscle; palladin is ubiquitously expressed in the organs of developing vertebrates and plays a key role in cellular morphogenesis. The three family members each interact with specific molecular partners with all three binding to alpha-actinin; In addition, palladin also binds to vasodilator-stimulated phosphoprotein (VASP) and ezrin, myotilin binds to filamin and actin, and myopalladin also binds to nebulin and cardiac ankyrin repeat protein (CARP). This group belongs to the I-set of IgSF domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand, but lack a C" strand.


Pssm-ID: 409405 [Multi-domain]  Cd Length: 91  Bit Score: 41.71  E-value: 1.11e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 281359561 1827 FVKVLKSQQCIEKDTVTLACEID-DAMGEVQWLRNGEEIKPDKRIQ-IVKDGRKRKLVIKDCKVTDAGQFKCT 1897
Cdd:cd05744     3 FLQAPGDLEVQEGRLCRFDCKVSgLPTPDLFWQLNGKPVRPDSAHKmLVRENGRHSLIIEPVTKRDAGIYTCI 75
IgI_5_Robo cd20952
Fifth Ig-like domain of Roundabout (Robo) homolog 1/2, and similar domains; a member of the ...
1506-1588 1.14e-03

Fifth Ig-like domain of Roundabout (Robo) homolog 1/2, and similar domains; a member of the I-set of IgSF domains; The members here are composed of the fifth Ig-like domain of Roundabout (Robo) homolog 1/2 and similar domains. Robo receptors play a role in the development of the central nervous system (CNS), and are receptors of Slit protein. Slit is a repellant secreted by the neural cells in the midline. Slit acts through Robo to prevent most neurons from crossing the midline from either side. Three mammalian Robo homologs (Robo1, -2, and -3), and three mammalian Slit homologs (Slit-1,-2, -3), have been identified. Commissural axons, which cross the midline, express low levels of Robo; longitudinal axons, which avoid the midline, express high levels of Robo. Robo1, -2, and -3 are expressed by commissural neurons in the vertebrate spinal cord and Slits 1, -2, -3 are expressed at the ventral midline. Robo-3 is a divergent member of the Robo family which instead of being a positive regulator of slit responsiveness, antagonizes slit responsiveness in precrossing axons. The Slit-Robo interaction is mediated by the second leucine-rich repeat (LRR) domain of Slit and the two N-terminal Ig domains of Robo, Ig1 and Ig2. The primary Robo binding site for Slit2 has been shown by surface plasmon resonance experiments and mutational analysis to be is the Ig1 domain, while the Ig2 domain has been proposed to harbor a weak secondary binding site. The fifth Ig-like domain of Robo 1 and 2 is a member of the I-set Ig domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand but lack a C" strand. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors


Pssm-ID: 409544 [Multi-domain]  Cd Length: 87  Bit Score: 41.71  E-value: 1.14e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 1506 YSVVEDSTAYLTVGVEGSPAPTFKFYK-GVSEILEGGRFKFLTDGqtntiTLCMRKCKPNDESKYKIVVSNIHGEDSAEM 1584
Cdd:cd20952     9 QTVAVGGTVVLNCQATGEPVPTISWLKdGVPLLGKDERITTLENG-----SLQIKGAEKSDTGEYTCVALNLSGEATWSA 83

                  ....
gi 281359561 1585 QLYV 1588
Cdd:cd20952    84 VLDV 87
Ig_2 pfam13895
Immunoglobulin domain; This domain contains immunoglobulin-like domains.
8451-8515 1.16e-03

Immunoglobulin domain; This domain contains immunoglobulin-like domains.


Pssm-ID: 464026 [Multi-domain]  Cd Length: 79  Bit Score: 41.23  E-value: 1.16e-03
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 281359561  8451 RDTCKLLCCLSGKPVPNVRWYKDGRELSKYEYAMTHSdgvVTmeiidckPSDSGKYSCKATNCHG 8515
Cdd:pfam13895   14 GEPVTLTCSAPGNPPPSYTWYKDGSAISSSPNFFTLS---VS-------AEDSGTYTCVARNGRG 68
IgI_C2_MyBP-C-like cd20967
Domain C2 of human cardiac Myosin Binding Protein C and similar domains; a member of the I-set ...
8455-8510 1.24e-03

Domain C2 of human cardiac Myosin Binding Protein C and similar domains; a member of the I-set of IgSF domains; The members here are composed of the immunoglobulin (Ig) Domain C2 of human cardiac Myosin Binding Protein C (MyBP-C) and similar domains. MyBP-C is a thick filament protein involved in the regulation of muscle contraction. Mutations in cardiac MyBP-C gene are the second most frequent cause of hypertrophic cardiomyopathy. MyBP-C binds to myosin with two binding sites, one at its C-terminus and another at its N-terminus. The N-terminal binding site, consisting of immunoglobulin (lg) domains C1 and C2 connected by a flexible linker, interacts with the S2 segment of myosin in a phosphorylation-regulated manner. The C1 and C2 Ig domains can bind to and activate or inhibit the thin filament. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. Unlike the V-set, one of the distinctive features of I-set domains is the lack of a C" strand. The structures of the Ig domains of MyBP-C lack this strand and thus belong to the I-set of Ig superfamily domains. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors.


Pssm-ID: 409559  Cd Length: 82  Bit Score: 41.46  E-value: 1.24e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 281359561 8455 KLLCCLSGKPVPnVRWYKDGREL-SKYEYAMTHSDGVVTMEIIDCKPSDSGKYSCKA 8510
Cdd:cd20967    16 RLTVELADPDAE-VKWYKDGQELqSSSKVIFESIGAKRTLTVQQASLADAGEYQCVA 71
IgI_2_Palladin_C cd20990
Second C-terminal immunoglobulin (Ig)-like domain of palladin; member of the I-set of Ig ...
335-425 1.25e-03

Second C-terminal immunoglobulin (Ig)-like domain of palladin; member of the I-set of Ig superfamily (IgSF) domains; The members here are composed of the C-terminal immunoglobulin (Ig)-like domain of palladin. Palladin belongs to the palladin-myotilin-myopalladin family. Proteins belonging to this family contain multiple Ig-like domains and function as scaffolds, modulating actin cytoskeleton. Palladin binds to alpha-actinin ezrin, vasodilator-stimulated phosphoprotein VASP, SPIN90 (also known as DIP or mDia interacting protein), and Src. Palladin also binds F-actin directly, via its Ig3 domain. Palladin is expressed as several alternatively spliced isoforms, having various combinations of Ig-like domains, in a cell-type-specific manner. It has been suggested that palladin's different Ig-like domains may be specialized for distinct functions. This group belongs to the I-set of IgSF domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand, but lack a C" strand.


Pssm-ID: 409582  Cd Length: 91  Bit Score: 41.62  E-value: 1.25e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561  335 PRFPKKP--TIRQEEDLLIMECVLEAHPVPDIVWYCSEKEIcnnqRTKMTRKAITKDSYILTLEIQNPTKEDGGNYRCNA 412
Cdd:cd20990     1 PHFLQAPgdLTVQEGKLCRMDCKVSGLPTPDLSWQLDGKPI----RPDSAHKMLVRENGVHSLIIEPVTSRDAGIYTCIA 76
                          90
                  ....*....|...
gi 281359561  413 INMYGESNANIAL 425
Cdd:cd20990    77 TNRAGQNSFNLEL 89
IgI_Myomesin_like_C cd05737
C-terminal immunoglobulin (Ig)-like domain of myomesin and M-protein; member of the I-set of ...
3509-3590 1.28e-03

C-terminal immunoglobulin (Ig)-like domain of myomesin and M-protein; member of the I-set of Ig superfamily (IgSF) domains; The members here are composed of the C-terminal immunoglobulin (Ig)-like domain of myomesin and M-protein (also known as myomesin-2). Myomesin and M-protein are both structural proteins localized to the M-band, a transverse structure in the center of the sarcomere, and are candidates for M-band bridges. Both proteins are modular, consisting mainly of repetitive Ig-like and fibronectin type III (FnIII) domains. Myomesin is expressed in all types of vertebrate striated muscle; M-protein has a muscle-type specific expression pattern. Myomesin is present in both slow and fast fibers; M-protein is present only in fast fibers. It has been suggested that myomesin acts as a molecular spring with alternative splicing as a means of modifying its elasticity.


Pssm-ID: 319300  Cd Length: 92  Bit Score: 41.81  E-value: 1.28e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 3509 VIVKTGLSISLDINIRGEPAPKVEWFFNNSSVTSDEH-SVKIDNVDYNTkFFVMRAQRSQSGKYIIKATNEVGEDEAELE 3587
Cdd:cd05737    11 VTIMEGKTLNLTCNVWGDPPPEVSWLKNDQALAFLDHcNLKVEAGRTVY-FTINGVSSEDSGKYGLVVKNKYGSETSDVT 89

                  ...
gi 281359561 3588 VTV 3590
Cdd:cd05737    90 VSV 92
Ig_Titin_like cd05748
Immunoglobulin (Ig)-like domain of titin and similar proteins; The members here are composed ...
1516-1582 1.31e-03

Immunoglobulin (Ig)-like domain of titin and similar proteins; The members here are composed of the immunoglobulin (Ig)-like domain found in titin-like proteins and similar proteins. Titin (also called connectin) is a fibrous sarcomeric protein specifically found in vertebrate striated muscle. Titin is a giant protein; depending on isoform composition, it ranges from 2970 to 3700 kDa, and is of a length that spans half a sarcomere. Titin largely consists of multiple repeats of Ig-like and fibronectin type 3 (FN-III)-like domains. Titin connects the ends of myosin thick filaments to Z disks and extends along the thick filament to the H zone. It appears to function similarly to an elastic band, keeping the myosin filaments centered in the sarcomere during muscle contraction or stretching. Within the sarcomere, titin is also attached to or is associated with myosin binding protein C (MyBP-C). MyBP-C appears to contribute to the generation of passive tension by titin and like titin has repeated Ig-like and FN-III domains. Also included in this group are worm twitchin and insect projectin, thick filament proteins of invertebrate muscle which also have repeated Ig-like and FN-III domains.


Pssm-ID: 409406 [Multi-domain]  Cd Length: 82  Bit Score: 41.42  E-value: 1.31e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 281359561 1516 LTVGVEGSPAPTFKFYKGVSEILEGGRFKFLTdGQTNTiTLCMRKCKPNDESKYKIVVSNIHGEDSA 1582
Cdd:cd05748    12 LDIPIKGRPTPTVTWSKDGQPLKETGRVQIET-TASST-SLVIKNAKRSDSGKYTLTLKNSAGEKSA 76
IgI_2_Robo cd05724
Second immunoglobulin (Ig)-like domain in Robo (roundabout) receptors; member of the I-set of ...
8845-8924 1.32e-03

Second immunoglobulin (Ig)-like domain in Robo (roundabout) receptors; member of the I-set of Ig superfamily (IgSF) domains; The members here are composed of the second immunoglobulin (Ig)-like domain in Robo (roundabout) receptors. Robo receptors play a role in the development of the central nervous system (CNS), and are receptors of the Slit protein. Slit is a repellant secreted by the neural cells in the midline. Slit acts through Robo to prevent most neurons from crossing the midline from either side. Three mammalian Robo homologs (Robo1, Robo2, and Robo3), and three mammalian Slit homologs (Slit-1,Slit-2, Slit-3), have been identified. Commissural axons, which cross the midline, express low levels of Robo; longitudinal axons, which avoid the midline, express high levels of Robo. Robo1, Robo2, and Robo3 are expressed by commissural neurons in the vertebrate spinal cord and Slit-1, Slit-2, Slit-3 are expressed at the ventral midline. Robo-3 is a divergent member of the Robo family which instead of being a positive regulator of Slit responsiveness, antagonizes Slit responsiveness in precrossing axons. The Slit-Robo interaction is mediated by the second leucine-rich repeat (LRR) domain of Slit and the two N-terminal Ig domains of Robo, Ig1 and Ig2. The primary Robo binding site for Slit-2 has been shown by surface plasmon resonance experiments and mutational analysis to be the Ig1 domain, while the Ig2 domain has been proposed to harbor a weak secondary binding site. This group belongs to the I-set of IgSF domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand, but lack a C" strand.


Pssm-ID: 409389 [Multi-domain]  Cd Length: 87  Bit Score: 41.62  E-value: 1.32e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 8845 PTSVSVLEGEGTTFECE--IDSELLNLVWLKDGKPIDETLPRYSFTKDGhrySFAVAKCNMDDVGQYQAKA--VSGKAES 8920
Cdd:cd05724     4 PSDTQVAVGEMAVLECSppRGHPEPTVSWRKDGQPLNLDNERVRIVDDG---NLLIAEARKSDEGTYKCVAtnMVGERES 80

                  ....
gi 281359561 8921 ICAF 8924
Cdd:cd05724    81 RAAR 84
IgI_telokin-like cd20973
immunoglobulin-like domain of telokin and similar proteins; a member of the I-set of IgSF ...
6862-6946 1.41e-03

immunoglobulin-like domain of telokin and similar proteins; a member of the I-set of IgSF domains; The members here are composed of the immunoglobulin (Ig) domain in telokin, the C-terminal domain of myosin light chain kinase which is identical to telokin, and similar proteins. The Ig superfamily (IgSF) is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. Unlike the V-set, one of the distinctive features of I-set domains is the lack of a C" strand. The structure of the telokin Ig domain lacks this strand and thus it belongs to the I-set of the IgSF. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors, the hemolymph protein hemolin, the muscle proteins titin, telokin, and twitchin, the neuronal adhesion molecule axonin-1, and the signaling molecule semaphorin 4D that is involved in axonal guidance, immune function and angiogenesis.


Pssm-ID: 409565 [Multi-domain]  Cd Length: 88  Bit Score: 41.41  E-value: 1.41e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 6862 SIRDMTVIAGDEFRITVPYHASPRPTASWSLNGLEVIPGERIKFDSN-DY-ASMYYNKSAKRDEtGSYTITLTNNKGSDT 6939
Cdd:cd20973     3 TLRDKEVVEGSAARFDCKVEGYPDPEVKWMKDDNPIVESRRFQIDQDeDGlCSLIISDVCGDDS-GKYTCKAVNSLGEAT 81

                  ....*..
gi 281359561 6940 ASCHVTV 6946
Cdd:cd20973    82 CSAELTV 88
Ig_2 pfam13895
Immunoglobulin domain; This domain contains immunoglobulin-like domains.
443-532 1.54e-03

Immunoglobulin domain; This domain contains immunoglobulin-like domains.


Pssm-ID: 464026 [Multi-domain]  Cd Length: 79  Bit Score: 41.23  E-value: 1.54e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561   443 KPRIIPNES----GTLITMKCKCKAKPEPTVTWYRGQDLVEKSKKIKINTTViaedtyeltleikdpgATDGGTYRCNVK 518
Cdd:pfam13895    1 KPVLTPSPTvvteGEPVTLTCSAPGNPPPSYTWYKDGSAISSSPNFFTLSVS----------------AEDSGTYTCVAR 64
                           90
                   ....*....|....*
gi 281359561   519 NE-YGESNANLNLNI 532
Cdd:pfam13895   65 NGrGGKVSNPVELTV 79
IgI_NCAM-1_like cd05732
Immunoglobulin (Ig)-like I-set domain of Neural Cell Adhesion Molecule 1 (NCAM-1) and similar ...
548-636 1.56e-03

Immunoglobulin (Ig)-like I-set domain of Neural Cell Adhesion Molecule 1 (NCAM-1) and similar proteins; The members here are composed of the fourth immunoglobulin (Ig)-like domain of Neural Cell Adhesion Molecule (NCAM-1). NCAM plays important roles in the development and regeneration of the central nervous system, in synaptogenesis and neural migration. NCAM mediates cell-cell and cell-substratum recognition and adhesion via homophilic (NCAM-NCAM), and heterophilic (NCAM-non-NCAM), interactions. NCAM is expressed as three major isoforms having different intracellular extensions. The extracellular portion of NCAM has five N-terminal Ig-like domains and two fibronectin type III domains. The double zipper adhesion complex model for NCAM homophilic binding involves Ig1, Ig2, and Ig3. By this model, Ig1 and Ig2 mediate dimerization of NCAM molecules situated on the same cell surface (cis interactions), and Ig3 domains mediate interactions between NCAM molecules expressed on the surface of opposing cells (trans interactions), through binding to the Ig1 and Ig2 domains. The adhesive ability of NCAM is modulated by the addition of polysialic acid chains to the fifth Ig-like domain. Also included in this group is NCAM-2 (also known as OCAM/mamFas II and RNCAM) NCAM-2 is differentially expressed in the developing and mature olfactory epithelium (OE). One of the unique features of I-set domains is the lack of a C" strand. The structures of this group show that the Ig domain lacks this strand and thus is a member of the I-set of Ig domains.


Pssm-ID: 409395 [Multi-domain]  Cd Length: 96  Bit Score: 41.74  E-value: 1.56e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561  548 KPRIVSENN-----GKLVIMECKVKADPKPDVIWFRNGEVIKESNK-IKTFIEQRGDQYYIKLELLDPQLEDSGLYKCNI 621
Cdd:cd05732     2 QPKITYLENqtaveLEQITLTCEAEGDPIPEITWRRATRGISFEEGdLDGRIVVRGHARVSSLTLKDVQLTDAGRYDCEA 81
                          90
                  ....*....|....*
gi 281359561  622 KNTLGELNANLTLNI 636
Cdd:cd05732    82 SNRIGGDQQSMYLEV 96
Ig_Titin_like cd05748
Immunoglobulin (Ig)-like domain of titin and similar proteins; The members here are composed ...
669-726 1.56e-03

Immunoglobulin (Ig)-like domain of titin and similar proteins; The members here are composed of the immunoglobulin (Ig)-like domain found in titin-like proteins and similar proteins. Titin (also called connectin) is a fibrous sarcomeric protein specifically found in vertebrate striated muscle. Titin is a giant protein; depending on isoform composition, it ranges from 2970 to 3700 kDa, and is of a length that spans half a sarcomere. Titin largely consists of multiple repeats of Ig-like and fibronectin type 3 (FN-III)-like domains. Titin connects the ends of myosin thick filaments to Z disks and extends along the thick filament to the H zone. It appears to function similarly to an elastic band, keeping the myosin filaments centered in the sarcomere during muscle contraction or stretching. Within the sarcomere, titin is also attached to or is associated with myosin binding protein C (MyBP-C). MyBP-C appears to contribute to the generation of passive tension by titin and like titin has repeated Ig-like and FN-III domains. Also included in this group are worm twitchin and insect projectin, thick filament proteins of invertebrate muscle which also have repeated Ig-like and FN-III domains.


Pssm-ID: 409406 [Multi-domain]  Cd Length: 82  Bit Score: 41.04  E-value: 1.56e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 281359561  669 PKCTWYKETSTVKESKRhvYQVEQTKEgefAVKLEINDVEESDKGAYKLVASNEKGEA 726
Cdd:cd05748    22 PTVTWSKDGQPLKETGR--VQIETTAS---STSLVIKNAKRSDSGKYTLTLKNSAGEK 74
IgI_telokin-like cd20973
immunoglobulin-like domain of telokin and similar proteins; a member of the I-set of IgSF ...
1508-1588 1.61e-03

immunoglobulin-like domain of telokin and similar proteins; a member of the I-set of IgSF domains; The members here are composed of the immunoglobulin (Ig) domain in telokin, the C-terminal domain of myosin light chain kinase which is identical to telokin, and similar proteins. The Ig superfamily (IgSF) is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. Unlike the V-set, one of the distinctive features of I-set domains is the lack of a C" strand. The structure of the telokin Ig domain lacks this strand and thus it belongs to the I-set of the IgSF. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors, the hemolymph protein hemolin, the muscle proteins titin, telokin, and twitchin, the neuronal adhesion molecule axonin-1, and the signaling molecule semaphorin 4D that is involved in axonal guidance, immune function and angiogenesis.


Pssm-ID: 409565 [Multi-domain]  Cd Length: 88  Bit Score: 41.41  E-value: 1.61e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 1508 VVEDSTAYLTVGVEGSPAPTFKFYKGVSEILEGGRFKFLTDGQTNTiTLCMRKCKPNDESKYKIVVSNIHGEDSAEMQLY 1587
Cdd:cd20973     9 VVEGSAARFDCKVEGYPDPEVKWMKDDNPIVESRRFQIDQDEDGLC-SLIISDVCGDDSGKYTCKAVNSLGEATCSAELT 87

                  .
gi 281359561 1588 V 1588
Cdd:cd20973    88 V 88
IgI_Myomesin_like_C cd05737
C-terminal immunoglobulin (Ig)-like domain of myomesin and M-protein; member of the I-set of ...
2612-2693 1.63e-03

C-terminal immunoglobulin (Ig)-like domain of myomesin and M-protein; member of the I-set of Ig superfamily (IgSF) domains; The members here are composed of the C-terminal immunoglobulin (Ig)-like domain of myomesin and M-protein (also known as myomesin-2). Myomesin and M-protein are both structural proteins localized to the M-band, a transverse structure in the center of the sarcomere, and are candidates for M-band bridges. Both proteins are modular, consisting mainly of repetitive Ig-like and fibronectin type III (FnIII) domains. Myomesin is expressed in all types of vertebrate striated muscle; M-protein has a muscle-type specific expression pattern. Myomesin is present in both slow and fast fibers; M-protein is present only in fast fibers. It has been suggested that myomesin acts as a molecular spring with alternative splicing as a means of modifying its elasticity.


Pssm-ID: 319300  Cd Length: 92  Bit Score: 41.42  E-value: 1.63e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 2612 VTIKSGRTHKWSVDVLGEPIPELHWSWRD-DIPLTNGDRIKIENVDYHTdFSITNVLRKDSGFYTLKAENRNGidRETVE 2690
Cdd:cd05737    11 VTIMEGKTLNLTCNVWGDPPPEVSWLKNDqALAFLDHCNLKVEAGRTVY-FTINGVSSEDSGKYGLVVKNKYG--SETSD 87

                  ...
gi 281359561 2691 LVV 2693
Cdd:cd05737    88 VTV 90
Ig_2 pfam13895
Immunoglobulin domain; This domain contains immunoglobulin-like domains.
7661-7732 1.65e-03

Immunoglobulin domain; This domain contains immunoglobulin-like domains.


Pssm-ID: 464026 [Multi-domain]  Cd Length: 79  Bit Score: 40.84  E-value: 1.65e-03
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 281359561  7661 QNHNAQFTCTINGVPKPTISWYKGAREISNGARYHmysegdnhflnINDVFGEDADEYVCRAVNKAGAKSTR 7732
Cdd:pfam13895   13 EGEPVTLTCSAPGNPPPSYTWYKDGSAISSSPNFF-----------TLSVSAEDSGTYTCVARNGRGGKVSN 73
IgI_Myotilin_C cd05892
C-terminal immunoglobulin (Ig)-like domain of myotilin; member of the I-set of Ig superfamily ...
438-532 1.68e-03

C-terminal immunoglobulin (Ig)-like domain of myotilin; member of the I-set of Ig superfamily (IgSF) domains; The members here are composed of the C-terminal immunoglobulin (Ig)-like domain of myotilin. Mytolin belongs to the palladin-myotilin-myopalladin family. Proteins belonging to the latter family contain multiple Ig-like domains and function as scaffolds, modulating the actin cytoskeleton. Myotilin is most abundant in skeletal and cardiac muscle and is involved in maintaining sarcomere integrity. It binds to alpha-actinin, filamin, and actin. Mutations in myotilin lead to muscle disorders. This group belongs to the I-set of IgSF domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand, but lack a C" strand.


Pssm-ID: 409473  Cd Length: 92  Bit Score: 41.29  E-value: 1.68e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561  438 PSFIEKPRIIPNESGTLITMKCKCKAKPEPTVTWYRGQDLVekskkiKINTTVIA---EDTYELTLEIKDPGATDGGTYR 514
Cdd:cd05892     1 PMFIQKPQNKKVLEGDPVRLECQISAIPPPQIFWKKNNEML------QYNTDRISlyqDNCGRICLLIQNANKKDAGWYT 74
                          90
                  ....*....|....*...
gi 281359561  515 CNVKNEYGESNANLNLNI 532
Cdd:cd05892    75 VSAVNEAGVVSCNARLDV 92
IgI_4_Dscam cd20956
Fourth immunoglobulin domain of the Drosophila melanogaster Dscam protein, and similar domains; ...
8456-8516 1.84e-03

Fourth immunoglobulin domain of the Drosophila melanogaster Dscam protein, and similar domains; a member of the I-set of IgSF domains; The members here are composed of the fourth immunoglobulin domain of the Drosophila melanogaster Down syndrome cell adhesion molecule (DSCAM) protein and similar proteins. Down syndrome cell adhesion molecule (DSCAM) is a cell adhesion molecule that plays critical roles in neural development, including axon guidance and branching, axon target recognition, self-avoidance and synaptic formation. DSCAM belongs to the immunoglobulin superfamily and contributes to defects in the central nervous system in Down syndrome patients. Vertebrate DSCAMs differ from Drosophila Dscam1 in that they lack the extensive alternative splicing that occurs in the insect gene. Drosophila melanogaster Dscam has 38,016 isoforms generated by the alternative splicing of four variable exon clusters, which allows every neuron in the fly to display a distinctive set of Dscam proteins on its cell surface. Drosophila Dscam1 is a cell-surface protein that plays important roles in neural development and axon tiling of neurons. It is shown that thousands of isoforms bind themselves through specific homophilic (self-binding) interactions, a process which mediates cellular self-recognition. Drosophila Dscam2 is also alternatively spliced and plays a key role in the development of two visual system neurons, monopolar cells L1 and L2. This group is a member of the I-set Ig domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand but lack a C" strand.


Pssm-ID: 409548 [Multi-domain]  Cd Length: 96  Bit Score: 41.39  E-value: 1.84e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 281359561 8456 LLCCLSGKPVPNVRWYKDGRELSKY------EYaMThSDGVVT--MEIIDCKPSDSGKYSCKATNCHGT 8516
Cdd:cd20956    21 LKCVASGNPLPQITWTLDGFPIPESprfrvgDY-VT-SDGDVVsyVNISSVRVEDGGEYTCTATNDVGS 87
Ig_Pro_neuregulin cd05750
Immunoglobulin (Ig)-like domain in neuregulins; The members here are composed of the ...
8461-8525 1.88e-03

Immunoglobulin (Ig)-like domain in neuregulins; The members here are composed of the immunoglobulin (Ig)-like domain in neuregulins (NRGs). NRGs are signaling molecules which participate in cell-cell interactions in the nervous system, breast, heart, and other organ systems, and are implicated in the pathology of diseases including schizophrenia, multiple sclerosis, and breast cancer. There are four members of the neuregulin gene family (NRG-1, NRG-2, NRG-3, and NRG-4). The NRG-1 protein, binds to and activates the tyrosine kinases receptors ErbB3 and ErbB4, initiating signaling cascades. The other NRGs proteins bind one or the other or both of these ErbBs. NRG-1 has multiple functions: in the brain it regulates various processes such as radial glia formation and neuronal migration, dendritic development, and expression of neurotransmitters receptors, while in the peripheral nervous system NRG-1 regulates processes such as target cell differentiation, and Schwann cell survival. There are many NRG-1 isoforms which arise from the alternative splicing of mRNA. Less is known of the functions of the other NRGs. NRG-2 and NRG-3 are expressed predominantly in the nervous system. NRG-2 is expressed by motor neurons and terminal Schwann cells, and is concentrated near synaptic sites and may be a signal that regulates synaptic differentiation. NRG-4 has been shown to direct pancreatic islet cell development towards the delta-cell lineage.


Pssm-ID: 409408 [Multi-domain]  Cd Length: 92  Bit Score: 41.34  E-value: 1.88e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 281359561 8461 SGKPVPNVRWYKDGRELSKY---EYAMTHSDGVVTMEIIDCKPSDSGKYSCKATNCHGTDETDCVVIV 8525
Cdd:cd05750    25 SENPSPRYRWFKDGKELNRKrpkNIKIRNKKKNSELQINKAKLEDSGEYTCVVENILGKDTVTGNVTV 92
IgI_Myotilin_C cd05892
C-terminal immunoglobulin (Ig)-like domain of myotilin; member of the I-set of Ig superfamily ...
4692-4765 1.94e-03

C-terminal immunoglobulin (Ig)-like domain of myotilin; member of the I-set of Ig superfamily (IgSF) domains; The members here are composed of the C-terminal immunoglobulin (Ig)-like domain of myotilin. Mytolin belongs to the palladin-myotilin-myopalladin family. Proteins belonging to the latter family contain multiple Ig-like domains and function as scaffolds, modulating the actin cytoskeleton. Myotilin is most abundant in skeletal and cardiac muscle and is involved in maintaining sarcomere integrity. It binds to alpha-actinin, filamin, and actin. Mutations in myotilin lead to muscle disorders. This group belongs to the I-set of IgSF domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand, but lack a C" strand.


Pssm-ID: 409473  Cd Length: 92  Bit Score: 41.29  E-value: 1.94e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 281359561 4692 LRNITLSSGTALKLDANITGEPAPKVEWKLSNYHLQ-SGKNVTIETPDY-YTKLVIRPTQRSDSGEYLVTATNTSG 4765
Cdd:cd05892     7 PQNKKVLEGDPVRLECQISAIPPPQIFWKKNNEMLQyNTDRISLYQDNCgRICLLIQNANKKDAGWYTVSAVNEAG 82
IgI_2_Titin_Z1z2-like cd20972
Second Ig-like domain of the giant muscle protein titin Z1z2 in the sarcomeric Z-disk, and ...
3208-3292 1.96e-03

Second Ig-like domain of the giant muscle protein titin Z1z2 in the sarcomeric Z-disk, and similar domains; a member of the I-set of IgSF domains; The members here are composed of the second immunoglobulin (Ig)-like domain of the giant muscle protein titin Z1z2 in the sarcomeric Z-disk and similar proteins. Titin is a key component in the assembly and functioning of vertebrate striated muscles. By providing connections at the level of individual microfilaments, it contributes to the fine balance of forces between the two halves of the sarcomere. The Ig superfamily (IgSF) is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. Unlike the V-set, one of the distinctive features of I-set domains is the lack of a C" strand. The structure of the titin Z1z2 lacks this strand and thus it belongs to the I-set of the IgSF. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors, the hemolymph protein hemolin, the muscle proteins titin, telokin, and twitchin, the neuronal adhesion molecule axonin-1, and the signaling molecule semaphorin 4D that is involved in axonal guidance, immune function and angiogenesis.


Pssm-ID: 409564 [Multi-domain]  Cd Length: 91  Bit Score: 41.03  E-value: 1.96e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 3208 KMKPIKVRAGQPVKFDVDVKGEPAPSLTWFLKETELTSTGQVRLENIDYNTKLTLLDTDRKQSGQYKLRAENINGVDEAV 3287
Cdd:cd20972     7 KLRSQEVAEGSKVRLECRVTGNPTPVVRWFCEGKELQNSPDIQIHQEGDLHSLIIAEAFEEDTGRYSCLATNSVGSDTTS 86

                  ....*
gi 281359561 3288 VEVII 3292
Cdd:cd20972    87 AEIFV 91
IgI_Twitchin_like cd20949
C-terminal immunoglobulin-like domain of the myosin-associated giant protein kinase Twitchin, ...
3212-3289 2.11e-03

C-terminal immunoglobulin-like domain of the myosin-associated giant protein kinase Twitchin, and similar domains; member of the I-set IgSF domains; The members here are composed of the C-terminal immunoglobulin-like domain of the myosin-associated giant protein kinase Twitchin and similar proteins, including Caenorhabditis elegans and Aplysia californica Twitchin, Drosophila melanogaster Projectin, and similar proteins. These are very large muscle proteins containing multiple immunoglobulin (Ig)-like and fibronectin type III (FN3) domains and a single kinase domain near the C-terminus. In humans these proteins are called Titin. The Ig superfamily (IgSF) is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. The Ig-like domain of the Twitchin is a member of the I-set IgSF domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand but lack a C" strand. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors, the hemolymph protein hemolin, the muscle proteins (titin, telokin, and twitchin), the neuronal adhesion molecule axonin-1, and the signaling molecule semaphorin 4D.


Pssm-ID: 409541 [Multi-domain]  Cd Length: 89  Bit Score: 41.16  E-value: 2.11e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 3212 IKVRAGQPVKFDVDVKGEPAPSLTWFLKETELTSTGQ--VRLENIDYNtkLTLLDTDRKQSGQYKLRAENINGVDEAVVE 3289
Cdd:cd20949     9 TTVKEGQSATILCEVKGEPQPNVTWHFNGQPISASVAdmSKYRILADG--LLINKVTQDDTGEYTCRAYQVNSIASDMQE 86
Ig_Titin_like cd05748
Immunoglobulin (Ig)-like domain of titin and similar proteins; The members here are composed ...
36-101 2.12e-03

Immunoglobulin (Ig)-like domain of titin and similar proteins; The members here are composed of the immunoglobulin (Ig)-like domain found in titin-like proteins and similar proteins. Titin (also called connectin) is a fibrous sarcomeric protein specifically found in vertebrate striated muscle. Titin is a giant protein; depending on isoform composition, it ranges from 2970 to 3700 kDa, and is of a length that spans half a sarcomere. Titin largely consists of multiple repeats of Ig-like and fibronectin type 3 (FN-III)-like domains. Titin connects the ends of myosin thick filaments to Z disks and extends along the thick filament to the H zone. It appears to function similarly to an elastic band, keeping the myosin filaments centered in the sarcomere during muscle contraction or stretching. Within the sarcomere, titin is also attached to or is associated with myosin binding protein C (MyBP-C). MyBP-C appears to contribute to the generation of passive tension by titin and like titin has repeated Ig-like and FN-III domains. Also included in this group are worm twitchin and insect projectin, thick filament proteins of invertebrate muscle which also have repeated Ig-like and FN-III domains.


Pssm-ID: 409406 [Multi-domain]  Cd Length: 82  Bit Score: 40.65  E-value: 2.12e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 281359561   36 PKPDIEWFRSDNKVVEDVRTKfkiqpVGENKYTVVLELDDVVETDAGLYKVKAKNKSGEVSASINL 101
Cdd:cd05748    20 PTPTVTWSKDGQPLKETGRVQ-----IETTASSTSLVIKNAKRSDSGKYTLTLKNSAGEKSATINV 80
ig pfam00047
Immunoglobulin domain; Members of the immunoglobulin superfamily are found in hundreds of ...
1750-1808 2.19e-03

Immunoglobulin domain; Members of the immunoglobulin superfamily are found in hundreds of proteins of different functions. Examples include antibodies, the giant muscle kinase titin and receptor tyrosine kinases. Immunoglobulin-like domains may be involved in protein-protein and protein-ligand interactions.


Pssm-ID: 395002  Cd Length: 86  Bit Score: 41.03  E-value: 2.19e-03
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 281359561  1750 TLECSVS--SSMANVHWFKNNTKLESDDPRYLISKDINGNLKLIIKDSvLDDAGLYRCQLD 1808
Cdd:pfam00047   15 TLTCSAStgSPGPDVTWSKEGGTLIESLKVKHDNGRTTQSSLLISNVT-KEDAGTYTCVVN 74
IgI_5_Robo cd20952
Fifth Ig-like domain of Roundabout (Robo) homolog 1/2, and similar domains; a member of the ...
137-210 2.23e-03

Fifth Ig-like domain of Roundabout (Robo) homolog 1/2, and similar domains; a member of the I-set of IgSF domains; The members here are composed of the fifth Ig-like domain of Roundabout (Robo) homolog 1/2 and similar domains. Robo receptors play a role in the development of the central nervous system (CNS), and are receptors of Slit protein. Slit is a repellant secreted by the neural cells in the midline. Slit acts through Robo to prevent most neurons from crossing the midline from either side. Three mammalian Robo homologs (Robo1, -2, and -3), and three mammalian Slit homologs (Slit-1,-2, -3), have been identified. Commissural axons, which cross the midline, express low levels of Robo; longitudinal axons, which avoid the midline, express high levels of Robo. Robo1, -2, and -3 are expressed by commissural neurons in the vertebrate spinal cord and Slits 1, -2, -3 are expressed at the ventral midline. Robo-3 is a divergent member of the Robo family which instead of being a positive regulator of slit responsiveness, antagonizes slit responsiveness in precrossing axons. The Slit-Robo interaction is mediated by the second leucine-rich repeat (LRR) domain of Slit and the two N-terminal Ig domains of Robo, Ig1 and Ig2. The primary Robo binding site for Slit2 has been shown by surface plasmon resonance experiments and mutational analysis to be is the Ig1 domain, while the Ig2 domain has been proposed to harbor a weak secondary binding site. The fifth Ig-like domain of Robo 1 and 2 is a member of the I-set Ig domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand but lack a C" strand. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors


Pssm-ID: 409544 [Multi-domain]  Cd Length: 87  Bit Score: 40.94  E-value: 2.23e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 281359561  137 LFECRVNADPIPAIIWFHNGAAVKESERHKITVDKdvhsyfATLEILNVTVEDAGKYKVNAKNELGESNATISL 210
Cdd:cd20952    18 VLNCQATGEPVPTISWLKDGVPLLGKDERITTLEN------GSLQIKGAEKSDTGEYTCVALNLSGEATWSAVL 85
IgI_Myomesin_like_C cd05737
C-terminal immunoglobulin (Ig)-like domain of myomesin and M-protein; member of the I-set of ...
2314-2395 2.25e-03

C-terminal immunoglobulin (Ig)-like domain of myomesin and M-protein; member of the I-set of Ig superfamily (IgSF) domains; The members here are composed of the C-terminal immunoglobulin (Ig)-like domain of myomesin and M-protein (also known as myomesin-2). Myomesin and M-protein are both structural proteins localized to the M-band, a transverse structure in the center of the sarcomere, and are candidates for M-band bridges. Both proteins are modular, consisting mainly of repetitive Ig-like and fibronectin type III (FnIII) domains. Myomesin is expressed in all types of vertebrate striated muscle; M-protein has a muscle-type specific expression pattern. Myomesin is present in both slow and fast fibers; M-protein is present only in fast fibers. It has been suggested that myomesin acts as a molecular spring with alternative splicing as a means of modifying its elasticity.


Pssm-ID: 319300  Cd Length: 92  Bit Score: 41.04  E-value: 2.25e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 2314 VTVKKGQTIRFDIKYDGEPEPAATWVKGTDNLKF-DNQRICLDQlERNSSITIKKSVRKDTGKYKLVLSNSSGTIESEAQ 2392
Cdd:cd05737    11 VTIMEGKTLNLTCNVWGDPPPEVSWLKNDQALAFlDHCNLKVEA-GRTVYFTINGVSSEDSGKYGLVVKNKYGSETSDVT 89

                  ...
gi 281359561 2393 VVV 2395
Cdd:cd05737    90 VSV 92
IgI_1_Titin_Z1z2-like cd20974
First Ig-like domain of the giant muscle protein titin Z1z2 in the sarcomeric Z-disk and ...
557-636 2.25e-03

First Ig-like domain of the giant muscle protein titin Z1z2 in the sarcomeric Z-disk and similar proteins; a member of the I-set of IgSF domains; The members here are composed of the first immunoglobulin (Ig)-like domain of the giant muscle protein titin Z1z2 in the sarcomeric Z-disk and similar proteins. Titin is a key component in the assembly and functioning of vertebrate striated muscles. By providing connections at the level of individual microfilaments, it contributes to the fine balance of forces between the two halves of the sarcomere. The Ig superfamily (IgSF) is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. Unlike the V-set, one of the distinctive features of I-set domains is the lack of a C" strand. The structure of the titin Z1z2 lacks this strand and thus it belongs to the I-set of the IgSF. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors, the hemolymph protein hemolin, the muscle proteins titin, telokin, and twitchin, the neuronal adhesion molecule axonin-1, and the signaling molecule semaphorin 4D that is involved in axonal guidance, immune function and angiogenesis.


Pssm-ID: 409566 [Multi-domain]  Cd Length: 93  Bit Score: 41.18  E-value: 2.25e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561  557 GKLVIMECKVKADPKPDVIWFRNGEVIKESNKIKTFIEQRGDQyyIKLELLDPQLEDSGLYKCNIKNTLGELNANLTLNI 636
Cdd:cd20974    15 GSTATFEAHVSGKPVPEVSWFRDGQVISTSTLPGVQISFSDGR--AKLSIPAVTKANSGRYSLTATNGSGQATSTAELLV 92
IgI_Myotilin_C cd05892
C-terminal immunoglobulin (Ig)-like domain of myotilin; member of the I-set of Ig superfamily ...
544-636 2.25e-03

C-terminal immunoglobulin (Ig)-like domain of myotilin; member of the I-set of Ig superfamily (IgSF) domains; The members here are composed of the C-terminal immunoglobulin (Ig)-like domain of myotilin. Mytolin belongs to the palladin-myotilin-myopalladin family. Proteins belonging to the latter family contain multiple Ig-like domains and function as scaffolds, modulating the actin cytoskeleton. Myotilin is most abundant in skeletal and cardiac muscle and is involved in maintaining sarcomere integrity. It binds to alpha-actinin, filamin, and actin. Mutations in myotilin lead to muscle disorders. This group belongs to the I-set of IgSF domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand, but lack a C" strand.


Pssm-ID: 409473  Cd Length: 92  Bit Score: 40.91  E-value: 2.25e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561  544 TFIEKPRIVSENNGKLVIMECKVKADPKPDVIWFRNGEVIK-ESNKIKTFIEQRGdqyYIKLELLDPQLEDSGLYKCNIK 622
Cdd:cd05892     2 MFIQKPQNKKVLEGDPVRLECQISAIPPPQIFWKKNNEMLQyNTDRISLYQDNCG---RICLLIQNANKKDAGWYTVSAV 78
                          90
                  ....*....|....
gi 281359561  623 NTLGELNANLTLNI 636
Cdd:cd05892    79 NEAGVVSCNARLDV 92
Ig_C5_MyBP-C cd05894
C5 immunoglobulin (Ig) domain of cardiac myosin binding protein C (MyBP-C); The members here ...
465-532 2.27e-03

C5 immunoglobulin (Ig) domain of cardiac myosin binding protein C (MyBP-C); The members here are composed of the C5 immunoglobulin (Ig) domain of cardiac myosin binding protein C (MyBP-C). MyBP-C consists of repeated domains, Ig and fibronectin type 3, and various linkers. Three isoforms of MYBP-C exist: slow-skeletal (ssMyBP-C), fast-skeletal (fsMyBP-C), and cardiac (cMyBP-C). cMYBP-C has insertions between and inside domains and an additional cardiac-specific Ig domain at the N-terminus. For cMYBP_C an interaction has been demonstrated between this C5 domain and the Ig C8 domain.


Pssm-ID: 409475  Cd Length: 86  Bit Score: 40.98  E-value: 2.27e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 281359561  465 PEPTVTWYRGQDLV-EKSKKIKINTTViaeDTYELTLEIKDpgATDGGTYRCNVKNEYGESNANLNLNI 532
Cdd:cd05894    23 PAPTVTWSRGDKAFtATEGRVRVESYK---DLSSFVIEGAE--REDEGVYTITVTNPVGEDHASLFVKV 86
Ig_3 pfam13927
Immunoglobulin domain; This family contains immunoglobulin-like domains.
5864-5935 2.29e-03

Immunoglobulin domain; This family contains immunoglobulin-like domains.


Pssm-ID: 464046 [Multi-domain]  Cd Length: 78  Bit Score: 40.63  E-value: 2.29e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561  5864 PPKIITPLNE--------VRIKCglifhtdiHFIGEPAPEATWTLNSNPLLSNDRSTITSIGHHSVVHTVNCQRSDSGIY 5935
Cdd:pfam13927    1 KPVITVSPSSvtvregetVTLTC--------EATGSPPPTITWYKNGEPISSGSTRSRSLSGSNSTLTISNVTRSDAGTY 72
IgI_8_hMLCK_like cd05762
Eighth immunoglobulin (Ig)-like domain of human myosin light-chain kinase (MLCK) and similar ...
5864-5961 2.32e-03

Eighth immunoglobulin (Ig)-like domain of human myosin light-chain kinase (MLCK) and similar protein; member of the I-set of IgSF domains; The members here are composed of the eighth immunoglobulin (Ig)-like domain of human myosin light-chain kinase (MLCK) and similar proteins. Myosin light-chain kinase (MLCK) is a key regulator of different forms of cell motility involving actin and myosin II. Agonist stimulation of smooth muscle cells increases cytosolic Ca2+ which binds calmodulin. This Ca2+-calmodulin complex in turn binds to and activates MLCK. Activated MLCK leads to the phosphorylation of the 20 kDa myosin regulatory light chain (RLC) of myosin II and the stimulation of actin-activated myosin MgATPase activity. MLCK is widely present in vertebrate tissues; it phosphorylates the 20 kDa RLC of both smooth and nonmuscle myosin II. Phosphorylation leads to the activation of the myosin motor domain and altered structural properties of myosin II. In smooth muscle MLCK it is involved in initiating contraction. In nonmuscle cells, MLCK may participate in cell division and cell motility; it has been suggested MLCK plays a role in cardiomyocyte differentiation and contraction through regulation of nonmuscle myosin II.


Pssm-ID: 409419  Cd Length: 99  Bit Score: 41.09  E-value: 2.32e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 5864 PPKIITPLNEVRIKCGLIFHTDIHFIGEPAPEATWTLNSNPLLSNDRSTITSIGHHSVVHTVNCQRSDSGIYHLLLRNSS 5943
Cdd:cd05762     1 PPQIIQFPEDMKVRAGESVELFCKVTGTQPITCTWMKFRKQIQEGEGIKIENTENSSKLTITEGQQEHCGCYTLEVENKL 80
                          90
                  ....*....|....*...
gi 281359561 5944 GIDEGSFELVVLDRPGPP 5961
Cdd:cd05762    81 GSRQAQVNLTVVDKPDPP 98
Ig_2 pfam13895
Immunoglobulin domain; This domain contains immunoglobulin-like domains.
4979-5069 2.40e-03

Immunoglobulin domain; This domain contains immunoglobulin-like domains.


Pssm-ID: 464026 [Multi-domain]  Cd Length: 79  Bit Score: 40.46  E-value: 2.40e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561  4979 PIIDRSSLVevrIKAGQSFTFDCKVSGEPAPQTKWllkkkevYSKDNVkvtnVDYNTKLKVNSATRSDSGIYTVFAENAN 5058
Cdd:pfam13895    2 PVLTPSPTV---VTEGEPVTLTCSAPGNPPPSYTW-------YKDGSA----ISSSPNFFTLSVSAEDSGTYTCVARNGR 67
                           90
                   ....*....|..
gi 281359561  5059 G-EDSADVKVTV 5069
Cdd:pfam13895   68 GgKVSNPVELTV 79
IG_like smart00410
Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.
7354-7440 2.41e-03

Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.


Pssm-ID: 214653 [Multi-domain]  Cd Length: 85  Bit Score: 40.57  E-value: 2.41e-03
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561   7354 PSELKLPEGDNSKIKIFYSGDQPLTVILKKNNEVICDSNDDTHVKVNifDDYVAIYIRNIVKSDGGPYQIEFTNESGSAT 7433
Cdd:smart00410    1 PPSVTVKEGESVTLSCEASGSPPPEVTWYKQGGKLLAESGRFSVSRS--GSTSTLTISNVTPEDSGTYTCAATNSSGSAS 78

                    ....*..
gi 281359561   7434 GEFYVHI 7440
Cdd:smart00410   79 SGTTLTV 85
Ig5_Contactin cd04969
Fifth immunoglobulin (Ig) domain of contactin; The members here are composed of the fifth ...
5302-5357 2.54e-03

Fifth immunoglobulin (Ig) domain of contactin; The members here are composed of the fifth immunoglobulin (Ig) domain of contactins. Contactins are neural cell adhesion molecules and are comprised of six Ig domains followed by four fibronectin type III (FnIII) domains anchored to the membrane by glycosylphosphatidylinositol. The first four Ig domains form the intermolecular binding fragment, which arranges as a compact U-shaped module via contacts between Ig domains 1 and 4, and between Ig domains 2 and 3. Contactin-2 (TAG-1, axonin-1) may play a part in the neuronal processes of neurite outgrowth, axon guidance and fasciculation, and neuronal migration. This group also includes contactin-1 and contactin-5. The different contactins show different expression patterns in the central nervous system. During development and in adulthood, contactin-2 is transiently expressed in subsets of central and peripheral neurons. Contactin-5 is expressed specifically in the rat postnatal nervous system, peaking at about 3 weeks postnatal, and a lack of contactin-5 (NB-2) results in an impairment of neuronal activity in the rat auditory system. Contactin-5 is highly expressed in the adult human brain in the occipital lobe and in the amygdala. Contactin-1 is differentially expressed in tumor tissues and may, through a RhoA mechanism, facilitate invasion and metastasis of human lung adenocarcinoma.


Pssm-ID: 409358 [Multi-domain]  Cd Length: 89  Bit Score: 40.91  E-value: 2.54e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 281359561 5302 GEPLPSKDWTHEGNMIINTDRVKIsnFDDRTkIRILDAKRSDTGVYTLTARNINGT 5357
Cdd:cd04969    28 ASPKPTISWSKGTELLTNSSRICI--LPDGS-LKIKNVTKSDEGKYTCFAVNFFGK 80
IgI_Myomesin_like_C cd05737
C-terminal immunoglobulin (Ig)-like domain of myomesin and M-protein; member of the I-set of ...
8447-8525 2.63e-03

C-terminal immunoglobulin (Ig)-like domain of myomesin and M-protein; member of the I-set of Ig superfamily (IgSF) domains; The members here are composed of the C-terminal immunoglobulin (Ig)-like domain of myomesin and M-protein (also known as myomesin-2). Myomesin and M-protein are both structural proteins localized to the M-band, a transverse structure in the center of the sarcomere, and are candidates for M-band bridges. Both proteins are modular, consisting mainly of repetitive Ig-like and fibronectin type III (FnIII) domains. Myomesin is expressed in all types of vertebrate striated muscle; M-protein has a muscle-type specific expression pattern. Myomesin is present in both slow and fast fibers; M-protein is present only in fast fibers. It has been suggested that myomesin acts as a molecular spring with alternative splicing as a means of modifying its elasticity.


Pssm-ID: 319300  Cd Length: 92  Bit Score: 40.65  E-value: 2.63e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 8447 VMQARDTCkLLCCLSGKPVPNVRWYKDGRELSKYE-YAMTHSDG-VVTMEIIDCKPSDSGKYSCKATNCHGTDETDCVVI 8524
Cdd:cd05737    13 IMEGKTLN-LTCNVWGDPPPEVSWLKNDQALAFLDhCNLKVEAGrTVYFTINGVSSEDSGKYGLVVKNKYGSETSDVTVS 91

                  .
gi 281359561 8525 V 8525
Cdd:cd05737    92 V 92
IgI_4_MYLK-like cd20976
Fourth Ig-like domain from smooth muscle myosin light chain kinase and similar domains ; a ...
6173-6255 2.67e-03

Fourth Ig-like domain from smooth muscle myosin light chain kinase and similar domains ; a member of the I-set of IgSF domains; The members here are composed of the fourth immunoglobulin (Ig)-like domain from smooth muscle myosin light chain kinase (MYLK) and similar domains. The Ig superfamily (IgSF) is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. Unlike the V-set, one of the distinctive features of I-set domains is the lack of a C" strand. The structure of this group shows that the fourth Ig-like domain from myosin light chain kinase lacks this strand and thus belongs to the I-set of the IgSF. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors, the hemolymph protein hemolin, the muscle proteins titin, telokin, and twitchin, the neuronal adhesion molecule axonin-1, and the signaling molecule semaphorin 4D that is involved in axonal guidance, immune function and angiogenesis.


Pssm-ID: 409568 [Multi-domain]  Cd Length: 90  Bit Score: 40.70  E-value: 2.67e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 6173 KRIKVRAGEPVNLNIPISGAPTPTIEWKRGDLKLE-EGKRISyeTNSERTLFRIDDSNRRDSGKYTVTAANEFGKDTADI 6251
Cdd:cd20976     9 KDLEAVEGQDFVAQCSARGKPVPRITWIRNAQPLQyAADRST--CEAGVGELHIQDVLPEDHGTYTCLAKNAAGQVSCSA 86

                  ....
gi 281359561 6252 EVIV 6255
Cdd:cd20976    87 WVTV 90
IgI_M-protein_C cd05891
C-terminal immunoglobulin (Ig)-like domain of M-protein; member of the I-set of Ig superfamily ...
3509-3590 2.71e-03

C-terminal immunoglobulin (Ig)-like domain of M-protein; member of the I-set of Ig superfamily (IgSF) domains; The members here are composed of the C-terminal immunoglobulin (Ig)-like domain of M-protein (also known as myomesin-2). M-protein is a structural protein localized to the M-band, a transverse structure in the center of the sarcomere, and is a candidate for M-band bridges. M-protein is modular consisting mainly of repetitive IG-like and fibronectin type III (FnIII) domains and has a muscle-type specific expression pattern. M-protein is present in fast fibers.


Pssm-ID: 143299  Cd Length: 92  Bit Score: 40.66  E-value: 2.71e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 3509 VIVKTGLSISLDINIRGEPAPKVEWFFNNSSVTSDEH-SVKIDNVDYnTKFFVMRAQRSQSGKYIIKATNEVGEDEAELE 3587
Cdd:cd05891    11 VTIMEGKTLNLTCTVFGNPDPEVIWFKNDQDIELSEHySVKLEQGKY-ASLTIKGVTSEDSGKYSINVKNKYGGETVDVT 89

                  ...
gi 281359561 3588 VTV 3590
Cdd:cd05891    90 VSV 92
IgI_telokin-like cd20973
immunoglobulin-like domain of telokin and similar proteins; a member of the I-set of IgSF ...
451-524 2.76e-03

immunoglobulin-like domain of telokin and similar proteins; a member of the I-set of IgSF domains; The members here are composed of the immunoglobulin (Ig) domain in telokin, the C-terminal domain of myosin light chain kinase which is identical to telokin, and similar proteins. The Ig superfamily (IgSF) is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. Unlike the V-set, one of the distinctive features of I-set domains is the lack of a C" strand. The structure of the telokin Ig domain lacks this strand and thus it belongs to the I-set of the IgSF. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors, the hemolymph protein hemolin, the muscle proteins titin, telokin, and twitchin, the neuronal adhesion molecule axonin-1, and the signaling molecule semaphorin 4D that is involved in axonal guidance, immune function and angiogenesis.


Pssm-ID: 409565 [Multi-domain]  Cd Length: 88  Bit Score: 40.64  E-value: 2.76e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 281359561  451 SGTLITMKCKCKAKPEPTVTWYRGQDLVEKSKKIKINTtviaEDTYELTLEIKDPGATDGGTYRCNVKNEYGES 524
Cdd:cd20973    11 EGSAARFDCKVEGYPDPEVKWMKDDNPIVESRRFQIDQ----DEDGLCSLIISDVCGDDSGKYTCKAVNSLGEA 80
ig pfam00047
Immunoglobulin domain; Members of the immunoglobulin superfamily are found in hundreds of ...
338-425 2.91e-03

Immunoglobulin domain; Members of the immunoglobulin superfamily are found in hundreds of proteins of different functions. Examples include antibodies, the giant muscle kinase titin and receptor tyrosine kinases. Immunoglobulin-like domains may be involved in protein-protein and protein-ligand interactions.


Pssm-ID: 395002  Cd Length: 86  Bit Score: 40.64  E-value: 2.91e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561   338 PKKPTIRQEEDLLIMEC-VLEAHPVPDIVWYcSEKEICNNQRTKMTrkaITKDSYILTLEIQNPTKEDGGNYRCNAINMY 416
Cdd:pfam00047    2 APPTVTVLEGDSATLTCsASTGSPGPDVTWS-KEGGTLIESLKVKH---DNGRTTQSSLLISNVTKEDAGTYTCVVNNPG 77

                   ....*....
gi 281359561   417 GESNANIAL 425
Cdd:pfam00047   78 GSATLSTSL 86
IgI_1_MuSK cd20970
agrin-responsive first immunoglobulin-like domains (Ig1) of the MuSK ectodomain; a member of ...
452-524 2.92e-03

agrin-responsive first immunoglobulin-like domains (Ig1) of the MuSK ectodomain; a member of the I-set of IgSF domains; The members here are composed of the first immunoglobulin-like domains (Ig1) of the Muscle-specific kinase (MuSK). MuSK is a receptor tyrosine kinase specifically expressed in skeletal muscle, where it plays a central role in the formation and maintenance of the neuromuscular junction (NMJ). MuSK is activated by agrin, a neuron-derived heparan sulfate proteoglycan. The activation of MUSK in myotubes regulates the formation of NMJs through the regulation of different processes including the specific expression of genes in subsynaptic nuclei, the reorganization of the actin cytoskeleton and the clustering of the acetylcholine receptors (AChR) in the postsynaptic membrane. The Ig superfamily (IgSF) is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. Unlike the V-set, one of the distinctive features of I-set domains is the lack of a C" strand. The structure of the MuSK lacks this strand and thus it belongs to the I-set of the IgSF. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors, the hemolymph protein hemolin, the muscle proteins titin, telokin, and twitchin, the neuronal adhesion molecule axonin-1, and the signaling molecule semaphorin 4D that is involved in axonal guidance, immune function and angiogenesis.


Pssm-ID: 409562 [Multi-domain]  Cd Length: 92  Bit Score: 40.57  E-value: 2.92e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 281359561  452 GTLITMKCKCKAKPEPTVTWYRGQDLVEkskkiKINTTVIA-EDTYELT-LEIKDpgaTDGGTYRCNVKNEYGES 524
Cdd:cd20970    17 GENATFMCRAEGSPEPEISWTRNGNLII-----EFNTRYIVrENGTTLTiRNIRR---SDMGIYLCIASNGVPGS 83
IgI_2_Palladin_C cd20990
Second C-terminal immunoglobulin (Ig)-like domain of palladin; member of the I-set of Ig ...
8448-8525 2.96e-03

Second C-terminal immunoglobulin (Ig)-like domain of palladin; member of the I-set of Ig superfamily (IgSF) domains; The members here are composed of the C-terminal immunoglobulin (Ig)-like domain of palladin. Palladin belongs to the palladin-myotilin-myopalladin family. Proteins belonging to this family contain multiple Ig-like domains and function as scaffolds, modulating actin cytoskeleton. Palladin binds to alpha-actinin ezrin, vasodilator-stimulated phosphoprotein VASP, SPIN90 (also known as DIP or mDia interacting protein), and Src. Palladin also binds F-actin directly, via its Ig3 domain. Palladin is expressed as several alternatively spliced isoforms, having various combinations of Ig-like domains, in a cell-type-specific manner. It has been suggested that palladin's different Ig-like domains may be specialized for distinct functions. This group belongs to the I-set of IgSF domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand, but lack a C" strand.


Pssm-ID: 409582  Cd Length: 91  Bit Score: 40.85  E-value: 2.96e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 8448 MQARDTCKLLCCLSGKPVPNVRWYKDGREL--SKYEYAMTHSDGVVTMEIIDCKPSDSGKYSCKATNCHGTDETDCVVIV 8525
Cdd:cd20990    12 VQEGKLCRMDCKVSGLPTPDLSWQLDGKPIrpDSAHKMLVRENGVHSLIIEPVTSRDAGIYTCIATNRAGQNSFNLELVV 91
IgI_M-protein_C cd05891
C-terminal immunoglobulin (Ig)-like domain of M-protein; member of the I-set of Ig superfamily ...
8447-8525 2.99e-03

C-terminal immunoglobulin (Ig)-like domain of M-protein; member of the I-set of Ig superfamily (IgSF) domains; The members here are composed of the C-terminal immunoglobulin (Ig)-like domain of M-protein (also known as myomesin-2). M-protein is a structural protein localized to the M-band, a transverse structure in the center of the sarcomere, and is a candidate for M-band bridges. M-protein is modular consisting mainly of repetitive IG-like and fibronectin type III (FnIII) domains and has a muscle-type specific expression pattern. M-protein is present in fast fibers.


Pssm-ID: 143299  Cd Length: 92  Bit Score: 40.66  E-value: 2.99e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 8447 VMQARdTCKLLCCLSGKPVPNVRWYKDGR--ELSKYEYAMTHSDGVVTMEIIDCKPSDSGKYSCKATNCHGTDETDCVVI 8524
Cdd:cd05891    13 IMEGK-TLNLTCTVFGNPDPEVIWFKNDQdiELSEHYSVKLEQGKYASLTIKGVTSEDSGKYSINVKNKYGGETVDVTVS 91

                  .
gi 281359561 8525 V 8525
Cdd:cd05891    92 V 92
IgI_Twitchin_like cd20949
C-terminal immunoglobulin-like domain of the myosin-associated giant protein kinase Twitchin, ...
439-522 3.03e-03

C-terminal immunoglobulin-like domain of the myosin-associated giant protein kinase Twitchin, and similar domains; member of the I-set IgSF domains; The members here are composed of the C-terminal immunoglobulin-like domain of the myosin-associated giant protein kinase Twitchin and similar proteins, including Caenorhabditis elegans and Aplysia californica Twitchin, Drosophila melanogaster Projectin, and similar proteins. These are very large muscle proteins containing multiple immunoglobulin (Ig)-like and fibronectin type III (FN3) domains and a single kinase domain near the C-terminus. In humans these proteins are called Titin. The Ig superfamily (IgSF) is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. The Ig-like domain of the Twitchin is a member of the I-set IgSF domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand but lack a C" strand. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors, the hemolymph protein hemolin, the muscle proteins (titin, telokin, and twitchin), the neuronal adhesion molecule axonin-1, and the signaling molecule semaphorin 4D.


Pssm-ID: 409541 [Multi-domain]  Cd Length: 89  Bit Score: 40.39  E-value: 3.03e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561  439 SFIEKPRIIPNESGTLITMKCKCKAKPEPTVTWYR-GQDL---VEKSKKIKINttviaedTYELTleIKDPGATDGGTYR 514
Cdd:cd20949     1 TFTENAYVTTVKEGQSATILCEVKGEPQPNVTWHFnGQPIsasVADMSKYRIL-------ADGLL--INKVTQDDTGEYT 71

                  ....*...
gi 281359561  515 CNVKNEYG 522
Cdd:cd20949    72 CRAYQVNS 79
Ig5_Contactin cd04969
Fifth immunoglobulin (Ig) domain of contactin; The members here are composed of the fifth ...
7757-7831 3.12e-03

Fifth immunoglobulin (Ig) domain of contactin; The members here are composed of the fifth immunoglobulin (Ig) domain of contactins. Contactins are neural cell adhesion molecules and are comprised of six Ig domains followed by four fibronectin type III (FnIII) domains anchored to the membrane by glycosylphosphatidylinositol. The first four Ig domains form the intermolecular binding fragment, which arranges as a compact U-shaped module via contacts between Ig domains 1 and 4, and between Ig domains 2 and 3. Contactin-2 (TAG-1, axonin-1) may play a part in the neuronal processes of neurite outgrowth, axon guidance and fasciculation, and neuronal migration. This group also includes contactin-1 and contactin-5. The different contactins show different expression patterns in the central nervous system. During development and in adulthood, contactin-2 is transiently expressed in subsets of central and peripheral neurons. Contactin-5 is expressed specifically in the rat postnatal nervous system, peaking at about 3 weeks postnatal, and a lack of contactin-5 (NB-2) results in an impairment of neuronal activity in the rat auditory system. Contactin-5 is highly expressed in the adult human brain in the occipital lobe and in the amygdala. Contactin-1 is differentially expressed in tumor tissues and may, through a RhoA mechanism, facilitate invasion and metastasis of human lung adenocarcinoma.


Pssm-ID: 409358 [Multi-domain]  Cd Length: 89  Bit Score: 40.52  E-value: 3.12e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 281359561 7757 KGENVVIKIPFTGFPKPRIHWVRDGENIESGGHYTVeVKERHavLIIRDGSHLDSGPYRITAENELG--SDTAIIQV 7831
Cdd:cd04969    16 KGGDVIIECKPKASPKPTISWSKGTELLTNSSRICI-LPDGS--LKIKNVTKSDEGKYTCFAVNFFGkaNSTGSLSV 89
Ig_C5_MyBP-C cd05894
C5 immunoglobulin (Ig) domain of cardiac myosin binding protein C (MyBP-C); The members here ...
133-210 3.23e-03

C5 immunoglobulin (Ig) domain of cardiac myosin binding protein C (MyBP-C); The members here are composed of the C5 immunoglobulin (Ig) domain of cardiac myosin binding protein C (MyBP-C). MyBP-C consists of repeated domains, Ig and fibronectin type 3, and various linkers. Three isoforms of MYBP-C exist: slow-skeletal (ssMyBP-C), fast-skeletal (fsMyBP-C), and cardiac (cMyBP-C). cMYBP-C has insertions between and inside domains and an additional cardiac-specific Ig domain at the N-terminus. For cMYBP_C an interaction has been demonstrated between this C5 domain and the Ig C8 domain.


Pssm-ID: 409475  Cd Length: 86  Bit Score: 40.21  E-value: 3.23e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 281359561  133 GKRLLFECRVNADPIPAIIWFHNGAAVKESE-RHKITVDKDVhsyfATLEILNVTVEDAGKYKVNAKNELGESNATISL 210
Cdd:cd05894    10 GNKLRLDVPISGEPAPTVTWSRGDKAFTATEgRVRVESYKDL----SSFVIEGAEREDEGVYTITVTNPVGEDHASLFV 84
IgI_Myomesin_like_C cd05737
C-terminal immunoglobulin (Ig)-like domain of myomesin and M-protein; member of the I-set of ...
8325-8401 3.26e-03

C-terminal immunoglobulin (Ig)-like domain of myomesin and M-protein; member of the I-set of Ig superfamily (IgSF) domains; The members here are composed of the C-terminal immunoglobulin (Ig)-like domain of myomesin and M-protein (also known as myomesin-2). Myomesin and M-protein are both structural proteins localized to the M-band, a transverse structure in the center of the sarcomere, and are candidates for M-band bridges. Both proteins are modular, consisting mainly of repetitive Ig-like and fibronectin type III (FnIII) domains. Myomesin is expressed in all types of vertebrate striated muscle; M-protein has a muscle-type specific expression pattern. Myomesin is present in both slow and fast fibers; M-protein is present only in fast fibers. It has been suggested that myomesin acts as a molecular spring with alternative splicing as a means of modifying its elasticity.


Pssm-ID: 319300  Cd Length: 92  Bit Score: 40.65  E-value: 3.26e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 281359561 8325 EGQSVKFYCRCIAIATPTLTWSHNNIELRQSVKF-MKRYVGDDYYFIINRVKLDDRGEYIIRAENHYGSREEVVFLNV 8401
Cdd:cd05737    15 EGKTLNLTCNVWGDPPPEVSWLKNDQALAFLDHCnLKVEAGRTVYFTINGVSSEDSGKYGLVVKNKYGSETSDVTVSV 92
IgI_APEG-1_like cd20975
Immunoglobulin-like domain of human Aortic Preferentially Expressed Protein-1 (APEG-1) and ...
553-626 3.28e-03

Immunoglobulin-like domain of human Aortic Preferentially Expressed Protein-1 (APEG-1) and similar proteins; a member of the I-set of IgSF domains; The members here are composed of the immunoglobulin I-set (IgI) domain of the Human Aortic Preferentially Expressed Protein-1 (APEG-1) and similar proteins. APEG-1 is a novel specific smooth muscle differentiation marker predicted to play a role in the growth and differentiation of arterial smooth muscle cells (SMCs). The Ig superfamily (IgSF) is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. Unlike the V-set, one of the distinctive features of I-set domains is the lack of a C" strand. The structure of the human APEG-1 lacks this strand and thus it belongs to the I-set of the IgSF. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors, the hemolymph protein hemolin, the muscle proteins titin, telokin, and twitchin, the neuronal adhesion molecule axonin-1, and the signaling molecule semaphorin 4D that is involved in axonal guidance, immune function and angiogenesis.


Pssm-ID: 409567  Cd Length: 91  Bit Score: 40.53  E-value: 3.28e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 281359561  553 SENNGKLVIMECKVKADPKPDVIWFRNGEVIKESNkiKTFIEQRGDQyYIKLELLDPQLEDSGLYKCNIKNTLG 626
Cdd:cd20975    11 SVREGQDVIMSIRVQGEPKPVVSWLRNRQPVRPDQ--RRFAEEAEGG-LCRLRILAAERGDAGFYTCKAVNEYG 81
IgI_1_MuSK cd20970
agrin-responsive first immunoglobulin-like domains (Ig1) of the MuSK ectodomain; a member of ...
2926-2993 3.38e-03

agrin-responsive first immunoglobulin-like domains (Ig1) of the MuSK ectodomain; a member of the I-set of IgSF domains; The members here are composed of the first immunoglobulin-like domains (Ig1) of the Muscle-specific kinase (MuSK). MuSK is a receptor tyrosine kinase specifically expressed in skeletal muscle, where it plays a central role in the formation and maintenance of the neuromuscular junction (NMJ). MuSK is activated by agrin, a neuron-derived heparan sulfate proteoglycan. The activation of MUSK in myotubes regulates the formation of NMJs through the regulation of different processes including the specific expression of genes in subsynaptic nuclei, the reorganization of the actin cytoskeleton and the clustering of the acetylcholine receptors (AChR) in the postsynaptic membrane. The Ig superfamily (IgSF) is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. Unlike the V-set, one of the distinctive features of I-set domains is the lack of a C" strand. The structure of the MuSK lacks this strand and thus it belongs to the I-set of the IgSF. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors, the hemolymph protein hemolin, the muscle proteins titin, telokin, and twitchin, the neuronal adhesion molecule axonin-1, and the signaling molecule semaphorin 4D that is involved in axonal guidance, immune function and angiogenesis.


Pssm-ID: 409562 [Multi-domain]  Cd Length: 92  Bit Score: 40.57  E-value: 3.38e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 281359561 2926 VRGEPAPVITWYQNDKelKPEELPSSSEIKNIpyNTKISIIETVRKHTGIYKIIAVNEHG---QDEATVEV 2993
Cdd:cd20970    26 AEGSPEPEISWTRNGN--LIIEFNTRYIVREN--GTTLTIRNIRRSDMGIYLCIASNGVPgsvEKRITLQV 92
IgI_Twitchin_like cd20949
C-terminal immunoglobulin-like domain of the myosin-associated giant protein kinase Twitchin, ...
7268-7334 3.51e-03

C-terminal immunoglobulin-like domain of the myosin-associated giant protein kinase Twitchin, and similar domains; member of the I-set IgSF domains; The members here are composed of the C-terminal immunoglobulin-like domain of the myosin-associated giant protein kinase Twitchin and similar proteins, including Caenorhabditis elegans and Aplysia californica Twitchin, Drosophila melanogaster Projectin, and similar proteins. These are very large muscle proteins containing multiple immunoglobulin (Ig)-like and fibronectin type III (FN3) domains and a single kinase domain near the C-terminus. In humans these proteins are called Titin. The Ig superfamily (IgSF) is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. The Ig-like domain of the Twitchin is a member of the I-set IgSF domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand but lack a C" strand. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors, the hemolymph protein hemolin, the muscle proteins (titin, telokin, and twitchin), the neuronal adhesion molecule axonin-1, and the signaling molecule semaphorin 4D.


Pssm-ID: 409541 [Multi-domain]  Cd Length: 89  Bit Score: 40.39  E-value: 3.51e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 281359561 7268 GKDYTLQCAASGKPSPTARWLRNGKEIQMNGGRMTcDSKDGVFRLHISNVQTGDDGDYTCEAMNSLG 7334
Cdd:cd20949    14 GQSATILCEVKGEPQPNVTWHFNGQPISASVADMS-KYRILADGLLINKVTQDDTGEYTCRAYQVNS 79
IgI_2_Robo cd05724
Second immunoglobulin (Ig)-like domain in Robo (roundabout) receptors; member of the I-set of ...
451-523 3.52e-03

Second immunoglobulin (Ig)-like domain in Robo (roundabout) receptors; member of the I-set of Ig superfamily (IgSF) domains; The members here are composed of the second immunoglobulin (Ig)-like domain in Robo (roundabout) receptors. Robo receptors play a role in the development of the central nervous system (CNS), and are receptors of the Slit protein. Slit is a repellant secreted by the neural cells in the midline. Slit acts through Robo to prevent most neurons from crossing the midline from either side. Three mammalian Robo homologs (Robo1, Robo2, and Robo3), and three mammalian Slit homologs (Slit-1,Slit-2, Slit-3), have been identified. Commissural axons, which cross the midline, express low levels of Robo; longitudinal axons, which avoid the midline, express high levels of Robo. Robo1, Robo2, and Robo3 are expressed by commissural neurons in the vertebrate spinal cord and Slit-1, Slit-2, Slit-3 are expressed at the ventral midline. Robo-3 is a divergent member of the Robo family which instead of being a positive regulator of Slit responsiveness, antagonizes Slit responsiveness in precrossing axons. The Slit-Robo interaction is mediated by the second leucine-rich repeat (LRR) domain of Slit and the two N-terminal Ig domains of Robo, Ig1 and Ig2. The primary Robo binding site for Slit-2 has been shown by surface plasmon resonance experiments and mutational analysis to be the Ig1 domain, while the Ig2 domain has been proposed to harbor a weak secondary binding site. This group belongs to the I-set of IgSF domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand, but lack a C" strand.


Pssm-ID: 409389 [Multi-domain]  Cd Length: 87  Bit Score: 40.46  E-value: 3.52e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 281359561  451 SGTLITMKCKC-KAKPEPTVTWYR-GQDLVEKSKKIKINTtviaedtyELTLEIKDPGATDGGTYRCNVKNEYGE 523
Cdd:cd05724    11 VGEMAVLECSPpRGHPEPTVSWRKdGQPLNLDNERVRIVD--------DGNLLIAEARKSDEGTYKCVATNMVGE 77
IgI_telokin-like cd20973
immunoglobulin-like domain of telokin and similar proteins; a member of the I-set of IgSF ...
3214-3279 3.53e-03

immunoglobulin-like domain of telokin and similar proteins; a member of the I-set of IgSF domains; The members here are composed of the immunoglobulin (Ig) domain in telokin, the C-terminal domain of myosin light chain kinase which is identical to telokin, and similar proteins. The Ig superfamily (IgSF) is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. Unlike the V-set, one of the distinctive features of I-set domains is the lack of a C" strand. The structure of the telokin Ig domain lacks this strand and thus it belongs to the I-set of the IgSF. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors, the hemolymph protein hemolin, the muscle proteins titin, telokin, and twitchin, the neuronal adhesion molecule axonin-1, and the signaling molecule semaphorin 4D that is involved in axonal guidance, immune function and angiogenesis.


Pssm-ID: 409565 [Multi-domain]  Cd Length: 88  Bit Score: 40.25  E-value: 3.53e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 281359561 3214 VRAGQPVKFDVDVKGEPAPSLTWFLKETELTSTGQVRLE-NIDYNTKLTLLDTDRKQSGQYKLRAEN 3279
Cdd:cd20973     9 VVEGSAARFDCKVEGYPDPEVKWMKDDNPIVESRRFQIDqDEDGLCSLIISDVCGDDSGKYTCKAVN 75
IgI_2_Palladin_C cd20990
Second C-terminal immunoglobulin (Ig)-like domain of palladin; member of the I-set of Ig ...
2912-2993 3.56e-03

Second C-terminal immunoglobulin (Ig)-like domain of palladin; member of the I-set of Ig superfamily (IgSF) domains; The members here are composed of the C-terminal immunoglobulin (Ig)-like domain of palladin. Palladin belongs to the palladin-myotilin-myopalladin family. Proteins belonging to this family contain multiple Ig-like domains and function as scaffolds, modulating actin cytoskeleton. Palladin binds to alpha-actinin ezrin, vasodilator-stimulated phosphoprotein VASP, SPIN90 (also known as DIP or mDia interacting protein), and Src. Palladin also binds F-actin directly, via its Ig3 domain. Palladin is expressed as several alternatively spliced isoforms, having various combinations of Ig-like domains, in a cell-type-specific manner. It has been suggested that palladin's different Ig-like domains may be specialized for distinct functions. This group belongs to the I-set of IgSF domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand, but lack a C" strand.


Pssm-ID: 409582  Cd Length: 91  Bit Score: 40.47  E-value: 3.56e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 2912 LLIRAGKPIRYDVNVRGEPAPVITWYQNDKELKPEelpSSSEIKNIPYNTKISIIETV-RKHTGIYKIIAVNEHGQDEAT 2990
Cdd:cd20990    10 LTVQEGKLCRMDCKVSGLPTPDLSWQLDGKPIRPD---SAHKMLVRENGVHSLIIEPVtSRDAGIYTCIATNRAGQNSFN 86

                  ...
gi 281359561 2991 VEV 2993
Cdd:cd20990    87 LEL 89
IgI_titin_I1-like cd20951
Immunoglobulin domain I1 of the titin I-band and similar proteins; a member of the I-set of ...
335-428 3.63e-03

Immunoglobulin domain I1 of the titin I-band and similar proteins; a member of the I-set of IgSF domains; The members here are composed of the immunoglobulin domain I1 of the titin I-band and similar proteins. Titin is a key component in the assembly and functioning of vertebrate striated muscles. By providing connections at the level of individual microfilaments, it contributes to the fine balance of forces between the two halves of the sarcomere. The Ig superfamily (IgSF) is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. The two sheets are linked together by a conserved disulfide bond between B strand and F strand. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. The Ig I1 domain of the titin I-band is a member of the I-set Ig domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand but lack a C" strand. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors, the hemolymph protein hemolin, the muscle proteins titin, telokin, and twitchin, the neuronal adhesion molecule axonin-1, and the signaling molecule semaphorin 4D that is involved in axonal guidance, immune function and angiogenesis.


Pssm-ID: 409543 [Multi-domain]  Cd Length: 94  Bit Score: 40.48  E-value: 3.63e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561  335 PRFPKKP---TIRQEEDLlIMECVLEAHPVPDIVWYCSEKEIcnnQRTKMTRK-AITKDSYILTLEIQNPTKEDGGNYRC 410
Cdd:cd20951     1 PEFIIRLqshTVWEKSDA-KLRVEVQGKPDPEVKWYKNGVPI---DPSSIPGKyKIESEYGVHVLHIRRVTVEDSAVYSA 76
                          90
                  ....*....|....*...
gi 281359561  411 NAINMYGESNANIALNFQ 428
Cdd:cd20951    77 VAKNIHGEASSSASVVVE 94
ig pfam00047
Immunoglobulin domain; Members of the immunoglobulin superfamily are found in hundreds of ...
7659-7735 3.69e-03

Immunoglobulin domain; Members of the immunoglobulin superfamily are found in hundreds of proteins of different functions. Examples include antibodies, the giant muscle kinase titin and receptor tyrosine kinases. Immunoglobulin-like domains may be involved in protein-protein and protein-ligand interactions.


Pssm-ID: 395002  Cd Length: 86  Bit Score: 40.26  E-value: 3.69e-03
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 281359561  7659 CIQNHNAQFTCTIN-GVPKPTISWYKGAREISNGARYHMYSEGDNHF-LNINDVFGEDADEYVCRAVNKAGAKSTRATL 7735
Cdd:pfam00047    8 VLEGDSATLTCSAStGSPGPDVTWSKEGGTLIESLKVKHDNGRTTQSsLLISNVTKEDAGTYTCVVNNPGGSATLSTSL 86
IgI_1_MuSK cd20970
agrin-responsive first immunoglobulin-like domains (Ig1) of the MuSK ectodomain; a member of ...
2313-2395 3.84e-03

agrin-responsive first immunoglobulin-like domains (Ig1) of the MuSK ectodomain; a member of the I-set of IgSF domains; The members here are composed of the first immunoglobulin-like domains (Ig1) of the Muscle-specific kinase (MuSK). MuSK is a receptor tyrosine kinase specifically expressed in skeletal muscle, where it plays a central role in the formation and maintenance of the neuromuscular junction (NMJ). MuSK is activated by agrin, a neuron-derived heparan sulfate proteoglycan. The activation of MUSK in myotubes regulates the formation of NMJs through the regulation of different processes including the specific expression of genes in subsynaptic nuclei, the reorganization of the actin cytoskeleton and the clustering of the acetylcholine receptors (AChR) in the postsynaptic membrane. The Ig superfamily (IgSF) is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. Unlike the V-set, one of the distinctive features of I-set domains is the lack of a C" strand. The structure of the MuSK lacks this strand and thus it belongs to the I-set of the IgSF. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors, the hemolymph protein hemolin, the muscle proteins titin, telokin, and twitchin, the neuronal adhesion molecule axonin-1, and the signaling molecule semaphorin 4D that is involved in axonal guidance, immune function and angiogenesis.


Pssm-ID: 409562 [Multi-domain]  Cd Length: 92  Bit Score: 40.18  E-value: 3.84e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 2313 NVTVKKGQTIRFDIKYDGEPEPAATWvkgtdnLKFDNQRICLDQ----LERNSSITIKKSVRKDTGKYKLVLSN-SSGTI 2387
Cdd:cd20970    11 TVTAREGENATFMCRAEGSPEPEISW------TRNGNLIIEFNTryivRENGTTLTIRNIRRSDMGIYLCIASNgVPGSV 84

                  ....*...
gi 281359561 2388 ESEAQVVV 2395
Cdd:cd20970    85 EKRITLQV 92
COG4733 COG4733
Phage-related protein, tail protein J [Mobilome: prophages, transposons];
7469-7634 3.91e-03

Phage-related protein, tail protein J [Mobilome: prophages, transposons];


Pssm-ID: 443767 [Multi-domain]  Cd Length: 978  Bit Score: 44.55  E-value: 3.91e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 7469 SYDGGLKVSHYVIE-RKDvsSPHWITVSSTcKDTAFNVQGLIENQeYIFRVMAVNENGMGPPLEGLNPIRAKDPIDPPSP 7547
Cdd:COG4733   557 SWDAPAGAVAYEVEwRRD--DGNWVSVPRT-SGTSFEVPGIYAGD-YEVRVRAINALGVSSAWAASSETTVTGKTAPPPA 632
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 7548 PGSpqITEIGGDF-VHLEWEKPESDGGAHIQGYWidkrevgSNTWQRVNATIC----AANQINCINLIEGRQYEFRIFAQ 7622
Cdd:COG4733   633 PTG--LTATGGLGgITLSWSFPVDADTLRTEIRY-------STTGDWASATVAqalyPGNTYTLAGLKAGQTYYYRARAV 703
                         170
                  ....*....|..
gi 281359561 7623 NVAGLSTESSAS 7634
Cdd:COG4733   704 DRSGNVSAWWVS 715
IgI_2_Palladin_C cd20990
Second C-terminal immunoglobulin (Ig)-like domain of palladin; member of the I-set of Ig ...
7669-7737 4.20e-03

Second C-terminal immunoglobulin (Ig)-like domain of palladin; member of the I-set of Ig superfamily (IgSF) domains; The members here are composed of the C-terminal immunoglobulin (Ig)-like domain of palladin. Palladin belongs to the palladin-myotilin-myopalladin family. Proteins belonging to this family contain multiple Ig-like domains and function as scaffolds, modulating actin cytoskeleton. Palladin binds to alpha-actinin ezrin, vasodilator-stimulated phosphoprotein VASP, SPIN90 (also known as DIP or mDia interacting protein), and Src. Palladin also binds F-actin directly, via its Ig3 domain. Palladin is expressed as several alternatively spliced isoforms, having various combinations of Ig-like domains, in a cell-type-specific manner. It has been suggested that palladin's different Ig-like domains may be specialized for distinct functions. This group belongs to the I-set of IgSF domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand, but lack a C" strand.


Pssm-ID: 409582  Cd Length: 91  Bit Score: 40.08  E-value: 4.20e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 7669 CTINGVPKPTISWYKGAREIS-NGARYHMYSEGDNHFLNINDVFGEDADEYVCRAVNKAGAKSTRATLAI 7737
Cdd:cd20990    22 CKVSGLPTPDLSWQLDGKPIRpDSAHKMLVRENGVHSLIIEPVTSRDAGIYTCIATNRAGQNSFNLELVV 91
Ig_Titin_like cd05748
Immunoglobulin (Ig)-like domain of titin and similar proteins; The members here are composed ...
8340-8401 4.41e-03

Immunoglobulin (Ig)-like domain of titin and similar proteins; The members here are composed of the immunoglobulin (Ig)-like domain found in titin-like proteins and similar proteins. Titin (also called connectin) is a fibrous sarcomeric protein specifically found in vertebrate striated muscle. Titin is a giant protein; depending on isoform composition, it ranges from 2970 to 3700 kDa, and is of a length that spans half a sarcomere. Titin largely consists of multiple repeats of Ig-like and fibronectin type 3 (FN-III)-like domains. Titin connects the ends of myosin thick filaments to Z disks and extends along the thick filament to the H zone. It appears to function similarly to an elastic band, keeping the myosin filaments centered in the sarcomere during muscle contraction or stretching. Within the sarcomere, titin is also attached to or is associated with myosin binding protein C (MyBP-C). MyBP-C appears to contribute to the generation of passive tension by titin and like titin has repeated Ig-like and FN-III domains. Also included in this group are worm twitchin and insect projectin, thick filament proteins of invertebrate muscle which also have repeated Ig-like and FN-III domains.


Pssm-ID: 409406 [Multi-domain]  Cd Length: 82  Bit Score: 39.88  E-value: 4.41e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 281359561 8340 TPTLTWSHNNIELRQSVKFMKRYVGDDYYFIINRVKLDDRGEYIIRAENHYGSREEVVFLNV 8401
Cdd:cd05748    21 TPTVTWSKDGQPLKETGRVQIETTASSTSLVIKNAKRSDSGKYTLTLKNSAGEKSATINVKV 82
IgI_4_hemolin-like cd20978
Fourth immunoglobulin (Ig)-like domain of hemolin, and similar domains; a member of the I-set ...
3202-3290 4.46e-03

Fourth immunoglobulin (Ig)-like domain of hemolin, and similar domains; a member of the I-set of IgSF domains; The members here are composed of the fourth immunoglobulin (Ig)-like domain of hemolin and similar proteins. Hemolin, an insect immunoglobulin superfamily (IgSF) member containing four Ig-like domains, is a lipopolysaccharide-binding immune protein induced during bacterial infection. Hemolin shares significant sequence similarity with the first four Ig-like domains of the transmembrane cell adhesion molecules (CAMs) of the L1 family. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. The fourth Ig-like domain of hemolin is a member of the I-set Ig domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set domains, members of the I-set have a discontinuous A strand but lack a C" strand. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors, the muscle proteins titin, telokin, and twitchin, the neuronal adhesion molecule axonin-1, and the signaling molecule semaphorin 4D that is involved in axonal guidance, immune function and angiogenesis.


Pssm-ID: 409570 [Multi-domain]  Cd Length: 88  Bit Score: 40.07  E-value: 4.46e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 3202 PYINRDKMKPIKVRAGQPVKFDVDVKGEPAPSLTWFLKETELTStgqvRLENIDY-NTKLTLLDTDRKQSGQYKLRAENI 3280
Cdd:cd20978     1 PKFIQKPEKNVVVKGGQDVTLPCQVTGVPQPKITWLHNGKPLQG----PMERATVeDGTLTIINVQPEDTGYYGCVATNE 76
                          90
                  ....*....|..
gi 281359561 3281 NG--VDEAVVEV 3290
Cdd:cd20978    77 IGdiYTETLLHV 88
IgI_Myomesin_like_C cd05737
C-terminal immunoglobulin (Ig)-like domain of myomesin and M-protein; member of the I-set of ...
4405-4480 4.50e-03

C-terminal immunoglobulin (Ig)-like domain of myomesin and M-protein; member of the I-set of Ig superfamily (IgSF) domains; The members here are composed of the C-terminal immunoglobulin (Ig)-like domain of myomesin and M-protein (also known as myomesin-2). Myomesin and M-protein are both structural proteins localized to the M-band, a transverse structure in the center of the sarcomere, and are candidates for M-band bridges. Both proteins are modular, consisting mainly of repetitive Ig-like and fibronectin type III (FnIII) domains. Myomesin is expressed in all types of vertebrate striated muscle; M-protein has a muscle-type specific expression pattern. Myomesin is present in both slow and fast fibers; M-protein is present only in fast fibers. It has been suggested that myomesin acts as a molecular spring with alternative splicing as a means of modifying its elasticity.


Pssm-ID: 319300  Cd Length: 92  Bit Score: 40.27  E-value: 4.50e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 281359561 4405 GEPIFLDINISGEPAPDVTWNQNNKSVQTTSFSHIENLPYNTKYIN-NNPERKDTGLYKISAHNFYGQDQVEFQINI 4480
Cdd:cd05737    16 GKTLNLTCNVWGDPPPEVSWLKNDQALAFLDHCNLKVEAGRTVYFTiNGVSSEDSGKYGLVVKNKYGSETSDVTVSV 92
Ig3_Peroxidasin cd05745
Third immunoglobulin (Ig)-like domain of peroxidasin; The members here are composed of the ...
2318-2395 4.68e-03

Third immunoglobulin (Ig)-like domain of peroxidasin; The members here are composed of the third immunoglobulin (Ig)-like domain in peroxidasin. Peroxidasin has a peroxidase domain and interacting extracellular motifs containing four Ig-like domains. It has been suggested that peroxidasin is secreted and has functions related to the stabilization of the extracellular matrix. It may play a part in various other important processes such as removal and destruction of cells which have undergone programmed cell death and protection of the organism against non-self.


Pssm-ID: 143222 [Multi-domain]  Cd Length: 74  Bit Score: 39.54  E-value: 4.68e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 281359561 2318 KGQTIRFDIKYDGEPEPAATWVKGTDNLKFDNQRICLDqlerNSSITIKKSVRKDTGKYKLVLSNSSGTIESEAQVVV 2395
Cdd:cd05745     1 EGQTVDFLCEAQGYPQPVIAWTKGGSQLSVDRRHLVLS----SGTLRISRVALHDQGQYECQAVNIVGSQRTVAQLTV 74
IgI_4_Dscam cd20956
Fourth immunoglobulin domain of the Drosophila melanogaster Dscam protein, and similar domains; ...
6177-6246 4.78e-03

Fourth immunoglobulin domain of the Drosophila melanogaster Dscam protein, and similar domains; a member of the I-set of IgSF domains; The members here are composed of the fourth immunoglobulin domain of the Drosophila melanogaster Down syndrome cell adhesion molecule (DSCAM) protein and similar proteins. Down syndrome cell adhesion molecule (DSCAM) is a cell adhesion molecule that plays critical roles in neural development, including axon guidance and branching, axon target recognition, self-avoidance and synaptic formation. DSCAM belongs to the immunoglobulin superfamily and contributes to defects in the central nervous system in Down syndrome patients. Vertebrate DSCAMs differ from Drosophila Dscam1 in that they lack the extensive alternative splicing that occurs in the insect gene. Drosophila melanogaster Dscam has 38,016 isoforms generated by the alternative splicing of four variable exon clusters, which allows every neuron in the fly to display a distinctive set of Dscam proteins on its cell surface. Drosophila Dscam1 is a cell-surface protein that plays important roles in neural development and axon tiling of neurons. It is shown that thousands of isoforms bind themselves through specific homophilic (self-binding) interactions, a process which mediates cellular self-recognition. Drosophila Dscam2 is also alternatively spliced and plays a key role in the development of two visual system neurons, monopolar cells L1 and L2. This group is a member of the I-set Ig domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand but lack a C" strand.


Pssm-ID: 409548 [Multi-domain]  Cd Length: 96  Bit Score: 40.24  E-value: 4.78e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 281359561 6177 VRAGEPVNLNIPISGAPTPTIEWKRGDLKLEEGKRIS---YETNSERTL--FRIDDSNRRDSGKYTVTAANEFGK 6246
Cdd:cd20956    13 LQPGPSVSLKCVASGNPLPQITWTLDGFPIPESPRFRvgdYVTSDGDVVsyVNISSVRVEDGGEYTCTATNDVGS 87
Ig3_Peroxidasin cd05745
Third immunoglobulin (Ig)-like domain of peroxidasin; The members here are composed of the ...
132-211 4.82e-03

Third immunoglobulin (Ig)-like domain of peroxidasin; The members here are composed of the third immunoglobulin (Ig)-like domain in peroxidasin. Peroxidasin has a peroxidase domain and interacting extracellular motifs containing four Ig-like domains. It has been suggested that peroxidasin is secreted and has functions related to the stabilization of the extracellular matrix. It may play a part in various other important processes such as removal and destruction of cells which have undergone programmed cell death and protection of the organism against non-self.


Pssm-ID: 143222 [Multi-domain]  Cd Length: 74  Bit Score: 39.54  E-value: 4.82e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561  132 DGKRLLFECRVNADPIPAIIWFHNGAAVKESERHKITVDkdvhsyfATLEILNVTVEDAGKYKVNAKNELGESNATISLN 211
Cdd:cd05745     1 EGQTVDFLCEAQGYPQPVIAWTKGGSQLSVDRRHLVLSS-------GTLRISRVALHDQGQYECQAVNIVGSQRTVAQLT 73
IgI_NCAM-1_like cd05732
Immunoglobulin (Ig)-like I-set domain of Neural Cell Adhesion Molecule 1 (NCAM-1) and similar ...
7651-7727 4.84e-03

Immunoglobulin (Ig)-like I-set domain of Neural Cell Adhesion Molecule 1 (NCAM-1) and similar proteins; The members here are composed of the fourth immunoglobulin (Ig)-like domain of Neural Cell Adhesion Molecule (NCAM-1). NCAM plays important roles in the development and regeneration of the central nervous system, in synaptogenesis and neural migration. NCAM mediates cell-cell and cell-substratum recognition and adhesion via homophilic (NCAM-NCAM), and heterophilic (NCAM-non-NCAM), interactions. NCAM is expressed as three major isoforms having different intracellular extensions. The extracellular portion of NCAM has five N-terminal Ig-like domains and two fibronectin type III domains. The double zipper adhesion complex model for NCAM homophilic binding involves Ig1, Ig2, and Ig3. By this model, Ig1 and Ig2 mediate dimerization of NCAM molecules situated on the same cell surface (cis interactions), and Ig3 domains mediate interactions between NCAM molecules expressed on the surface of opposing cells (trans interactions), through binding to the Ig1 and Ig2 domains. The adhesive ability of NCAM is modulated by the addition of polysialic acid chains to the fifth Ig-like domain. Also included in this group is NCAM-2 (also known as OCAM/mamFas II and RNCAM) NCAM-2 is differentially expressed in the developing and mature olfactory epithelium (OE). One of the unique features of I-set domains is the lack of a C" strand. The structures of this group show that the Ig domain lacks this strand and thus is a member of the I-set of Ig domains.


Pssm-ID: 409395 [Multi-domain]  Cd Length: 96  Bit Score: 40.20  E-value: 4.84e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 7651 VKP----LRDANCIQNHNAQFTCTINGVPKPTISWYKGAREISNGA-----RYHMYSEGDNHFLNINDVFGEDADEYVCR 7721
Cdd:cd05732     1 VQPkityLENQTAVELEQITLTCEAEGDPIPEITWRRATRGISFEEgdldgRIVVRGHARVSSLTLKDVQLTDAGRYDCE 80

                  ....*.
gi 281359561 7722 AVNKAG 7727
Cdd:cd05732    81 ASNRIG 86
IgI_Myomesin_like_C cd05737
C-terminal immunoglobulin (Ig)-like domain of myomesin and M-protein; member of the I-set of ...
7751-7834 4.86e-03

C-terminal immunoglobulin (Ig)-like domain of myomesin and M-protein; member of the I-set of Ig superfamily (IgSF) domains; The members here are composed of the C-terminal immunoglobulin (Ig)-like domain of myomesin and M-protein (also known as myomesin-2). Myomesin and M-protein are both structural proteins localized to the M-band, a transverse structure in the center of the sarcomere, and are candidates for M-band bridges. Both proteins are modular, consisting mainly of repetitive Ig-like and fibronectin type III (FnIII) domains. Myomesin is expressed in all types of vertebrate striated muscle; M-protein has a muscle-type specific expression pattern. Myomesin is present in both slow and fast fibers; M-protein is present only in fast fibers. It has been suggested that myomesin acts as a molecular spring with alternative splicing as a means of modifying its elasticity.


Pssm-ID: 319300  Cd Length: 92  Bit Score: 39.88  E-value: 4.86e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 7751 DTAYFDKGENVVIKIPFTGFPKPRIHWVRDGENIESGGHYTVEVKE-RHAVLIIRDGSHLDSGPYRITAENELGSDTaiI 7829
Cdd:cd05737     9 DVVTIMEGKTLNLTCNVWGDPPPEVSWLKNDQALAFLDHCNLKVEAgRTVYFTINGVSSEDSGKYGLVVKNKYGSET--S 86

                  ....*
gi 281359561 7830 QVQIS 7834
Cdd:cd05737    87 DVTVS 91
IgI_Twitchin_like cd20949
C-terminal immunoglobulin-like domain of the myosin-associated giant protein kinase Twitchin, ...
2612-2693 4.89e-03

C-terminal immunoglobulin-like domain of the myosin-associated giant protein kinase Twitchin, and similar domains; member of the I-set IgSF domains; The members here are composed of the C-terminal immunoglobulin-like domain of the myosin-associated giant protein kinase Twitchin and similar proteins, including Caenorhabditis elegans and Aplysia californica Twitchin, Drosophila melanogaster Projectin, and similar proteins. These are very large muscle proteins containing multiple immunoglobulin (Ig)-like and fibronectin type III (FN3) domains and a single kinase domain near the C-terminus. In humans these proteins are called Titin. The Ig superfamily (IgSF) is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. The Ig-like domain of the Twitchin is a member of the I-set IgSF domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand but lack a C" strand. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors, the hemolymph protein hemolin, the muscle proteins (titin, telokin, and twitchin), the neuronal adhesion molecule axonin-1, and the signaling molecule semaphorin 4D.


Pssm-ID: 409541 [Multi-domain]  Cd Length: 89  Bit Score: 40.01  E-value: 4.89e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 2612 VTIKSGRTHKWSVDVLGEPIPELHWSwRDDIPLTNG--DRIKIENVDYhtDFSITNVLRKDSGFYTLKAENRNGIDRETV 2689
Cdd:cd20949     9 TTVKEGQSATILCEVKGEPQPNVTWH-FNGQPISASvaDMSKYRILAD--GLLINKVTQDDTGEYTCRAYQVNSIASDMQ 85

                  ....
gi 281359561 2690 ELVV 2693
Cdd:cd20949    86 ERTV 89
IgI_Myotilin_C cd05892
C-terminal immunoglobulin (Ig)-like domain of myotilin; member of the I-set of Ig superfamily ...
4405-4470 5.16e-03

C-terminal immunoglobulin (Ig)-like domain of myotilin; member of the I-set of Ig superfamily (IgSF) domains; The members here are composed of the C-terminal immunoglobulin (Ig)-like domain of myotilin. Mytolin belongs to the palladin-myotilin-myopalladin family. Proteins belonging to the latter family contain multiple Ig-like domains and function as scaffolds, modulating the actin cytoskeleton. Myotilin is most abundant in skeletal and cardiac muscle and is involved in maintaining sarcomere integrity. It binds to alpha-actinin, filamin, and actin. Mutations in myotilin lead to muscle disorders. This group belongs to the I-set of IgSF domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand, but lack a C" strand.


Pssm-ID: 409473  Cd Length: 92  Bit Score: 40.14  E-value: 5.16e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 281359561 4405 GEPIFLDINISGEPAPDVTWNQNNKSVQTTSfSHIENLPYNTKYIN---NNPERKDTGLYKISAHNFYG 4470
Cdd:cd05892    15 GDPVRLECQISAIPPPQIFWKKNNEMLQYNT-DRISLYQDNCGRIClliQNANKKDAGWYTVSAVNEAG 82
Ig5_Contactin cd04969
Fifth immunoglobulin (Ig) domain of contactin; The members here are composed of the fifth ...
655-728 5.25e-03

Fifth immunoglobulin (Ig) domain of contactin; The members here are composed of the fifth immunoglobulin (Ig) domain of contactins. Contactins are neural cell adhesion molecules and are comprised of six Ig domains followed by four fibronectin type III (FnIII) domains anchored to the membrane by glycosylphosphatidylinositol. The first four Ig domains form the intermolecular binding fragment, which arranges as a compact U-shaped module via contacts between Ig domains 1 and 4, and between Ig domains 2 and 3. Contactin-2 (TAG-1, axonin-1) may play a part in the neuronal processes of neurite outgrowth, axon guidance and fasciculation, and neuronal migration. This group also includes contactin-1 and contactin-5. The different contactins show different expression patterns in the central nervous system. During development and in adulthood, contactin-2 is transiently expressed in subsets of central and peripheral neurons. Contactin-5 is expressed specifically in the rat postnatal nervous system, peaking at about 3 weeks postnatal, and a lack of contactin-5 (NB-2) results in an impairment of neuronal activity in the rat auditory system. Contactin-5 is highly expressed in the adult human brain in the occipital lobe and in the amygdala. Contactin-1 is differentially expressed in tumor tissues and may, through a RhoA mechanism, facilitate invasion and metastasis of human lung adenocarcinoma.


Pssm-ID: 409358 [Multi-domain]  Cd Length: 89  Bit Score: 39.75  E-value: 5.25e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 281359561  655 RTVVIECTVASKFEPKCTWYKETSTVKESKRhvyqVEQTKEGefavKLEINDVEESDKGAYKLVASNEKGEAVS 728
Cdd:cd04969    18 GDVIIECKPKASPKPTISWSKGTELLTNSSR----ICILPDG----SLKIKNVTKSDEGKYTCFAVNFFGKANS 83
IgI_8_hMLCK_like cd05762
Eighth immunoglobulin (Ig)-like domain of human myosin light-chain kinase (MLCK) and similar ...
2643-2700 5.31e-03

Eighth immunoglobulin (Ig)-like domain of human myosin light-chain kinase (MLCK) and similar protein; member of the I-set of IgSF domains; The members here are composed of the eighth immunoglobulin (Ig)-like domain of human myosin light-chain kinase (MLCK) and similar proteins. Myosin light-chain kinase (MLCK) is a key regulator of different forms of cell motility involving actin and myosin II. Agonist stimulation of smooth muscle cells increases cytosolic Ca2+ which binds calmodulin. This Ca2+-calmodulin complex in turn binds to and activates MLCK. Activated MLCK leads to the phosphorylation of the 20 kDa myosin regulatory light chain (RLC) of myosin II and the stimulation of actin-activated myosin MgATPase activity. MLCK is widely present in vertebrate tissues; it phosphorylates the 20 kDa RLC of both smooth and nonmuscle myosin II. Phosphorylation leads to the activation of the myosin motor domain and altered structural properties of myosin II. In smooth muscle MLCK it is involved in initiating contraction. In nonmuscle cells, MLCK may participate in cell division and cell motility; it has been suggested MLCK plays a role in cardiomyocyte differentiation and contraction through regulation of nonmuscle myosin II.


Pssm-ID: 409419  Cd Length: 99  Bit Score: 40.32  E-value: 5.31e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 281359561 2643 PLTNGDRIKIENVDYHTDFSITNVLRKDSGFYTLKAENRNGIDRETVELVVLGKPSSP 2700
Cdd:cd05762    41 QIQEGEGIKIENTENSSKLTITEGQQEHCGCYTLEVENKLGSRQAQVNLTVVDKPDPP 98
IgI_Twitchin_like cd20949
C-terminal immunoglobulin-like domain of the myosin-associated giant protein kinase Twitchin, ...
3807-3885 5.34e-03

C-terminal immunoglobulin-like domain of the myosin-associated giant protein kinase Twitchin, and similar domains; member of the I-set IgSF domains; The members here are composed of the C-terminal immunoglobulin-like domain of the myosin-associated giant protein kinase Twitchin and similar proteins, including Caenorhabditis elegans and Aplysia californica Twitchin, Drosophila melanogaster Projectin, and similar proteins. These are very large muscle proteins containing multiple immunoglobulin (Ig)-like and fibronectin type III (FN3) domains and a single kinase domain near the C-terminus. In humans these proteins are called Titin. The Ig superfamily (IgSF) is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. The Ig-like domain of the Twitchin is a member of the I-set IgSF domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand but lack a C" strand. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors, the hemolymph protein hemolin, the muscle proteins (titin, telokin, and twitchin), the neuronal adhesion molecule axonin-1, and the signaling molecule semaphorin 4D.


Pssm-ID: 409541 [Multi-domain]  Cd Length: 89  Bit Score: 40.01  E-value: 5.34e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 3807 MRSGQMLHIDALIKAEPPAKVTWTYNKTEIK--TSDHIKIENEDYKTTfiMPKVKRADRGIYIVTAKNDSGSDTVEVELE 3884
Cdd:cd20949    11 VKEGQSATILCEVKGEPQPNVTWHFNGQPISasVADMSKYRILADGLL--INKVTQDDTGEYTCRAYQVNSIASDMQERT 88

                  .
gi 281359561 3885 V 3885
Cdd:cd20949    89 V 89
IgI_M-protein_C cd05891
C-terminal immunoglobulin (Ig)-like domain of M-protein; member of the I-set of Ig superfamily ...
2314-2385 5.37e-03

C-terminal immunoglobulin (Ig)-like domain of M-protein; member of the I-set of Ig superfamily (IgSF) domains; The members here are composed of the C-terminal immunoglobulin (Ig)-like domain of M-protein (also known as myomesin-2). M-protein is a structural protein localized to the M-band, a transverse structure in the center of the sarcomere, and is a candidate for M-band bridges. M-protein is modular consisting mainly of repetitive IG-like and fibronectin type III (FnIII) domains and has a muscle-type specific expression pattern. M-protein is present in fast fibers.


Pssm-ID: 143299  Cd Length: 92  Bit Score: 39.89  E-value: 5.37e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 281359561 2314 VTVKKGQTIRFDIKYDGEPEPAATWVKGTDNLKFDNQ-RICLDQlERNSSITIKKSVRKDTGKYKLVLSNSSG 2385
Cdd:cd05891    11 VTIMEGKTLNLTCTVFGNPDPEVIWFKNDQDIELSEHySVKLEQ-GKYASLTIKGVTSEDSGKYSINVKNKYG 82
IgI_4_hemolin-like cd20978
Fourth immunoglobulin (Ig)-like domain of hemolin, and similar domains; a member of the I-set ...
3506-3590 5.42e-03

Fourth immunoglobulin (Ig)-like domain of hemolin, and similar domains; a member of the I-set of IgSF domains; The members here are composed of the fourth immunoglobulin (Ig)-like domain of hemolin and similar proteins. Hemolin, an insect immunoglobulin superfamily (IgSF) member containing four Ig-like domains, is a lipopolysaccharide-binding immune protein induced during bacterial infection. Hemolin shares significant sequence similarity with the first four Ig-like domains of the transmembrane cell adhesion molecules (CAMs) of the L1 family. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. The fourth Ig-like domain of hemolin is a member of the I-set Ig domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set domains, members of the I-set have a discontinuous A strand but lack a C" strand. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors, the muscle proteins titin, telokin, and twitchin, the neuronal adhesion molecule axonin-1, and the signaling molecule semaphorin 4D that is involved in axonal guidance, immune function and angiogenesis.


Pssm-ID: 409570 [Multi-domain]  Cd Length: 88  Bit Score: 39.68  E-value: 5.42e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 3506 LKPVIVKTGLSISLDINIRGEPAPKVEWFFNNSSVTSD-------EHSVKIDNVdyntkffvmraQRSQSGKYIIKATNE 3578
Cdd:cd20978     8 EKNVVVKGGQDVTLPCQVTGVPQPKITWLHNGKPLQGPmeratveDGTLTIINV-----------QPEDTGYYGCVATNE 76
                          90
                  ....*....|..
gi 281359561 3579 VGEDEAELEVTV 3590
Cdd:cd20978    77 IGDIYTETLLHV 88
Ig_2 pfam13895
Immunoglobulin domain; This domain contains immunoglobulin-like domains.
8313-8392 5.85e-03

Immunoglobulin domain; This domain contains immunoglobulin-like domains.


Pssm-ID: 464026 [Multi-domain]  Cd Length: 79  Bit Score: 39.30  E-value: 5.85e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561  8313 RFVIRPSSQFCYEGQSVKFYCRCIAIATPTLTWSHNNIELRQSVKfmkryvgddyyFIINRVKLDDRGEYIIRAENHYGS 8392
Cdd:pfam13895    1 KPVLTPSPTVVTEGEPVTLTCSAPGNPPPSYTWYKDGSAISSSPN-----------FFTLSVSAEDSGTYTCVARNGRGG 69
Ig_Pro_neuregulin cd05750
Immunoglobulin (Ig)-like domain in neuregulins; The members here are composed of the ...
1828-1909 5.89e-03

Immunoglobulin (Ig)-like domain in neuregulins; The members here are composed of the immunoglobulin (Ig)-like domain in neuregulins (NRGs). NRGs are signaling molecules which participate in cell-cell interactions in the nervous system, breast, heart, and other organ systems, and are implicated in the pathology of diseases including schizophrenia, multiple sclerosis, and breast cancer. There are four members of the neuregulin gene family (NRG-1, NRG-2, NRG-3, and NRG-4). The NRG-1 protein, binds to and activates the tyrosine kinases receptors ErbB3 and ErbB4, initiating signaling cascades. The other NRGs proteins bind one or the other or both of these ErbBs. NRG-1 has multiple functions: in the brain it regulates various processes such as radial glia formation and neuronal migration, dendritic development, and expression of neurotransmitters receptors, while in the peripheral nervous system NRG-1 regulates processes such as target cell differentiation, and Schwann cell survival. There are many NRG-1 isoforms which arise from the alternative splicing of mRNA. Less is known of the functions of the other NRGs. NRG-2 and NRG-3 are expressed predominantly in the nervous system. NRG-2 is expressed by motor neurons and terminal Schwann cells, and is concentrated near synaptic sites and may be a signal that regulates synaptic differentiation. NRG-4 has been shown to direct pancreatic islet cell development towards the delta-cell lineage.


Pssm-ID: 409408 [Multi-domain]  Cd Length: 92  Bit Score: 39.80  E-value: 5.89e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 1828 VKVLKSQQCIEKDTVTLACEiddAMGE-----VQWLRNGEEI--KPDKRIQIVKDGRKRKLVIKDCKVTDAGQFKCTTNA 1900
Cdd:cd05750     3 LKEMKSQTVQEGSKLVLKCE---ATSEnpsprYRWFKDGKELnrKRPKNIKIRNKKKNSELQINKAKLEDSGEYTCVVEN 79
                          90
                  ....*....|...
gi 281359561 1901 ----DTTESEIII 1909
Cdd:cd05750    80 ilgkDTVTGNVTV 92
IgI_Myomesin_like_C cd05737
C-terminal immunoglobulin (Ig)-like domain of myomesin and M-protein; member of the I-set of ...
5580-5651 6.45e-03

C-terminal immunoglobulin (Ig)-like domain of myomesin and M-protein; member of the I-set of Ig superfamily (IgSF) domains; The members here are composed of the C-terminal immunoglobulin (Ig)-like domain of myomesin and M-protein (also known as myomesin-2). Myomesin and M-protein are both structural proteins localized to the M-band, a transverse structure in the center of the sarcomere, and are candidates for M-band bridges. Both proteins are modular, consisting mainly of repetitive Ig-like and fibronectin type III (FnIII) domains. Myomesin is expressed in all types of vertebrate striated muscle; M-protein has a muscle-type specific expression pattern. Myomesin is present in both slow and fast fibers; M-protein is present only in fast fibers. It has been suggested that myomesin acts as a molecular spring with alternative splicing as a means of modifying its elasticity.


Pssm-ID: 319300  Cd Length: 92  Bit Score: 39.88  E-value: 6.45e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 281359561 5580 ITVHAGKRLGWTLPIEASPRPLITWLYNGKEIGSNSRGESGLFQ-NELTFEIVSSLRSDEGRYTLILKNEHGS 5651
Cdd:cd05737    11 VTIMEGKTLNLTCNVWGDPPPEVSWLKNDQALAFLDHCNLKVEAgRTVYFTINGVSSEDSGKYGLVVKNKYGS 83
Ig cd00096
Immunoglobulin domain; The members here are composed of the immunoglobulin (Ig) domain found ...
4113-4176 6.50e-03

Immunoglobulin domain; The members here are composed of the immunoglobulin (Ig) domain found in the Ig superfamily. The Ig superfamily is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. Members of this group are components of immunoglobulin, neuroglia, cell surface glycoproteins, including T-cell receptors, CD2, CD4, CD8, and membrane glycoproteins, including butyrophilin and chondroitin sulfate proteoglycan core protein. A predominant feature of most Ig domains is a disulfide bridge connecting the two beta-sheets with a tryptophan residue packed against the disulfide bond. Ig superfamily (IgSF) domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. Typically, the V-set domains have A, B, E, and D strands in one sheet and A', G, F, C, C' and C" in the other. The structures in C1-set are smaller than those in the V-set; they have one beta sheet that is formed by strands A, B, E, and D and the other by strands G, F, C, and C'. Moreover, a C1-set Ig domain contains a short C' strand (three residues) and lacks A' and C" strand. Unlike other Ig domain sets, C2-set structures do not have a D strand. Like the V-set Ig domains, members of the I-set have a discontinuous A strand, but lack a C" strand.


Pssm-ID: 409353 [Multi-domain]  Cd Length: 70  Bit Score: 39.23  E-value: 6.50e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 281359561 4113 KVSGEPPATKVWLHNKARLENDDsNYNIDMESYRTKLTVPISKRFHSGKYTLKAENESGRDEAS 4176
Cdd:cd00096     6 SASGNPPPTITWYKNGKPLPPSS-RDSRRSELGNGTLTISNVTLEDSGTYTCVASNSAGGSASA 68
IgI_telokin-like cd20973
immunoglobulin-like domain of telokin and similar proteins; a member of the I-set of IgSF ...
242-320 6.59e-03

immunoglobulin-like domain of telokin and similar proteins; a member of the I-set of IgSF domains; The members here are composed of the immunoglobulin (Ig) domain in telokin, the C-terminal domain of myosin light chain kinase which is identical to telokin, and similar proteins. The Ig superfamily (IgSF) is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. Unlike the V-set, one of the distinctive features of I-set domains is the lack of a C" strand. The structure of the telokin Ig domain lacks this strand and thus it belongs to the I-set of the IgSF. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors, the hemolymph protein hemolin, the muscle proteins titin, telokin, and twitchin, the neuronal adhesion molecule axonin-1, and the signaling molecule semaphorin 4D that is involved in axonal guidance, immune function and angiogenesis.


Pssm-ID: 409565 [Multi-domain]  Cd Length: 88  Bit Score: 39.48  E-value: 6.59e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 281359561  242 GGNVTFECRCVGDPTPTVTWSHGETELNESNRYKmsltMDQKLYHIACLEISSVVSSDQGEYRAQAKNKHGSGVATINL 320
Cdd:cd20973    12 GSAARFDCKVEGYPDPEVKWMKDDNPIVESRRFQ----IDQDEDGLCSLIISDVCGDDSGKYTCKAVNSLGEATCSAEL 86
IgI_Twitchin_like cd20949
C-terminal immunoglobulin-like domain of the myosin-associated giant protein kinase Twitchin, ...
10-102 6.75e-03

C-terminal immunoglobulin-like domain of the myosin-associated giant protein kinase Twitchin, and similar domains; member of the I-set IgSF domains; The members here are composed of the C-terminal immunoglobulin-like domain of the myosin-associated giant protein kinase Twitchin and similar proteins, including Caenorhabditis elegans and Aplysia californica Twitchin, Drosophila melanogaster Projectin, and similar proteins. These are very large muscle proteins containing multiple immunoglobulin (Ig)-like and fibronectin type III (FN3) domains and a single kinase domain near the C-terminus. In humans these proteins are called Titin. The Ig superfamily (IgSF) is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. The Ig-like domain of the Twitchin is a member of the I-set IgSF domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand but lack a C" strand. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors, the hemolymph protein hemolin, the muscle proteins (titin, telokin, and twitchin), the neuronal adhesion molecule axonin-1, and the signaling molecule semaphorin 4D.


Pssm-ID: 409541 [Multi-domain]  Cd Length: 89  Bit Score: 39.62  E-value: 6.75e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561   10 SFVKKPQLHQEDDGNRLIFECQLLSSPKPDIEWFRSDNKVVEDVR--TKFKIQPVGenkytvvLELDDVVETDAGLYKVK 87
Cdd:cd20949     1 TFTENAYVTTVKEGQSATILCEVKGEPQPNVTWHFNGQPISASVAdmSKYRILADG-------LLINKVTQDDTGEYTCR 73
                          90
                  ....*....|....*
gi 281359561   88 AKNKSGEVSASINLN 102
Cdd:cd20949    74 AYQVNSIASDMQERT 88
Ig cd00096
Immunoglobulin domain; The members here are composed of the immunoglobulin (Ig) domain found ...
777-831 7.04e-03

Immunoglobulin domain; The members here are composed of the immunoglobulin (Ig) domain found in the Ig superfamily. The Ig superfamily is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. Members of this group are components of immunoglobulin, neuroglia, cell surface glycoproteins, including T-cell receptors, CD2, CD4, CD8, and membrane glycoproteins, including butyrophilin and chondroitin sulfate proteoglycan core protein. A predominant feature of most Ig domains is a disulfide bridge connecting the two beta-sheets with a tryptophan residue packed against the disulfide bond. Ig superfamily (IgSF) domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. Typically, the V-set domains have A, B, E, and D strands in one sheet and A', G, F, C, C' and C" in the other. The structures in C1-set are smaller than those in the V-set; they have one beta sheet that is formed by strands A, B, E, and D and the other by strands G, F, C, and C'. Moreover, a C1-set Ig domain contains a short C' strand (three residues) and lacks A' and C" strand. Unlike other Ig domain sets, C2-set structures do not have a D strand. Like the V-set Ig domains, members of the I-set have a discontinuous A strand, but lack a C" strand.


Pssm-ID: 409353 [Multi-domain]  Cd Length: 70  Bit Score: 38.85  E-value: 7.04e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 281359561  777 KVEWYKGSTVIRETKDITTTFDGTTARLTFSSARTEHTSNYKVIVTNEVGKDESS 831
Cdd:cd00096    14 TITWYKNGKPLPPSSRDSRRSELGNGTLTISNVTLEDSGTYTCVASNSAGGSASA 68
IgI_titin_I1-like cd20951
Immunoglobulin domain I1 of the titin I-band and similar proteins; a member of the I-set of ...
6176-6255 8.08e-03

Immunoglobulin domain I1 of the titin I-band and similar proteins; a member of the I-set of IgSF domains; The members here are composed of the immunoglobulin domain I1 of the titin I-band and similar proteins. Titin is a key component in the assembly and functioning of vertebrate striated muscles. By providing connections at the level of individual microfilaments, it contributes to the fine balance of forces between the two halves of the sarcomere. The Ig superfamily (IgSF) is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. The two sheets are linked together by a conserved disulfide bond between B strand and F strand. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. The Ig I1 domain of the titin I-band is a member of the I-set Ig domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand but lack a C" strand. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors, the hemolymph protein hemolin, the muscle proteins titin, telokin, and twitchin, the neuronal adhesion molecule axonin-1, and the signaling molecule semaphorin 4D that is involved in axonal guidance, immune function and angiogenesis.


Pssm-ID: 409543 [Multi-domain]  Cd Length: 94  Bit Score: 39.33  E-value: 8.08e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 6176 KVRAGEPVNLNIPISGAPTPTIEWKRGDLKLE---EGKRISYETNSERTLFRIDDSNRRDSGKYTVTAANEFGKDTADIE 6252
Cdd:cd20951    11 TVWEKSDAKLRVEVQGKPDPEVKWYKNGVPIDpssIPGKYKIESEYGVHVLHIRRVTVEDSAVYSAVAKNIHGEASSSAS 90

                  ...
gi 281359561 6253 VIV 6255
Cdd:cd20951    91 VVV 93
Ig_3 pfam13927
Immunoglobulin domain; This family contains immunoglobulin-like domains.
8839-8910 8.35e-03

Immunoglobulin domain; This family contains immunoglobulin-like domains.


Pssm-ID: 464046 [Multi-domain]  Cd Length: 78  Bit Score: 39.09  E-value: 8.35e-03
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 281359561  8839 PSFVKFPTSVSVLEGEGTTFECEIDSE-LLNLVWLKDGKPIDETlPRYSFTKDGHRYSFAVAKCNMDDVGQYQ 8910
Cdd:pfam13927    2 PVITVSPSSVTVREGETVTLTCEATGSpPPTITWYKNGEPISSG-STRSRSLSGSNSTLTISNVTRSDAGTYT 73
IgI_2_Palladin_C cd20990
Second C-terminal immunoglobulin (Ig)-like domain of palladin; member of the I-set of Ig ...
9-101 8.41e-03

Second C-terminal immunoglobulin (Ig)-like domain of palladin; member of the I-set of Ig superfamily (IgSF) domains; The members here are composed of the C-terminal immunoglobulin (Ig)-like domain of palladin. Palladin belongs to the palladin-myotilin-myopalladin family. Proteins belonging to this family contain multiple Ig-like domains and function as scaffolds, modulating actin cytoskeleton. Palladin binds to alpha-actinin ezrin, vasodilator-stimulated phosphoprotein VASP, SPIN90 (also known as DIP or mDia interacting protein), and Src. Palladin also binds F-actin directly, via its Ig3 domain. Palladin is expressed as several alternatively spliced isoforms, having various combinations of Ig-like domains, in a cell-type-specific manner. It has been suggested that palladin's different Ig-like domains may be specialized for distinct functions. This group belongs to the I-set of IgSF domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand, but lack a C" strand.


Pssm-ID: 409582  Cd Length: 91  Bit Score: 39.31  E-value: 8.41e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561    9 PSFVKKPQLHQEDDGNRLIFECQLLSSPKPDIEWFRSDNKVVEDVRTKFKIQPVGENKytvvLELDDVVETDAGLYKVKA 88
Cdd:cd20990     1 PHFLQAPGDLTVQEGKLCRMDCKVSGLPTPDLSWQLDGKPIRPDSAHKMLVRENGVHS----LIIEPVTSRDAGIYTCIA 76
                          90
                  ....*....|...
gi 281359561   89 KNKSGEVSASINL 101
Cdd:cd20990    77 TNRAGQNSFNLEL 89
IgI_2_Robo cd05724
Second immunoglobulin (Ig)-like domain in Robo (roundabout) receptors; member of the I-set of ...
547-627 8.65e-03

Second immunoglobulin (Ig)-like domain in Robo (roundabout) receptors; member of the I-set of Ig superfamily (IgSF) domains; The members here are composed of the second immunoglobulin (Ig)-like domain in Robo (roundabout) receptors. Robo receptors play a role in the development of the central nervous system (CNS), and are receptors of the Slit protein. Slit is a repellant secreted by the neural cells in the midline. Slit acts through Robo to prevent most neurons from crossing the midline from either side. Three mammalian Robo homologs (Robo1, Robo2, and Robo3), and three mammalian Slit homologs (Slit-1,Slit-2, Slit-3), have been identified. Commissural axons, which cross the midline, express low levels of Robo; longitudinal axons, which avoid the midline, express high levels of Robo. Robo1, Robo2, and Robo3 are expressed by commissural neurons in the vertebrate spinal cord and Slit-1, Slit-2, Slit-3 are expressed at the ventral midline. Robo-3 is a divergent member of the Robo family which instead of being a positive regulator of Slit responsiveness, antagonizes Slit responsiveness in precrossing axons. The Slit-Robo interaction is mediated by the second leucine-rich repeat (LRR) domain of Slit and the two N-terminal Ig domains of Robo, Ig1 and Ig2. The primary Robo binding site for Slit-2 has been shown by surface plasmon resonance experiments and mutational analysis to be the Ig1 domain, while the Ig2 domain has been proposed to harbor a weak secondary binding site. This group belongs to the I-set of IgSF domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand, but lack a C" strand.


Pssm-ID: 409389 [Multi-domain]  Cd Length: 87  Bit Score: 39.31  E-value: 8.65e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561  547 EKPRIVSENNGKLVIMECKV-KADPKPDVIWFRNGEVIKESNKIKTFIEQRgdqyyiKLELLDPQLEDSGLYKCNIKNTL 625
Cdd:cd05724     2 VEPSDTQVAVGEMAVLECSPpRGHPEPTVSWRKDGQPLNLDNERVRIVDDG------NLLIAEARKSDEGTYKCVATNMV 75

                  ..
gi 281359561  626 GE 627
Cdd:cd05724    76 GE 77
IgI_3_Robo cd05725
Third immunoglobulin (Ig)-like domain in Robo (roundabout) receptors; member of the I-set of ...
5284-5357 8.68e-03

Third immunoglobulin (Ig)-like domain in Robo (roundabout) receptors; member of the I-set of Ig superfamily (IgSF) domains; The members here are composed of the third immunoglobulin (Ig)-like domain in Robo (roundabout) receptors. Robo receptors play a role in the development of the central nervous system (CNS), and are receptors of Slit protein. Slit is a repellant secreted by the neural cells in the midline. Slit acts through Robo to prevent most neurons from crossing the midline from either side. Three mammalian Robo homologs (Robo1, Robo2, Robo3), and three mammalian Slit homologs (Slit-1,Slit-2, Slit-3), have been identified. Commissural axons, which cross the midline, express low levels of Robo; longitudinal axons, which avoid the midline, express high levels of Robo. Robo1, Robo2, and Robo3 are expressed by commissural neurons in the vertebrate spinal cord and Slit-1, Slit-2, and Slit-3 are expressed at the ventral midline. Robo-3 is a divergent member of the Robo family which instead of being a positive regulator of Slit responsiveness, antagonizes Slit responsiveness in precrossing axons. The Slit-Robo interaction is mediated by the second leucine-rich repeat (LRR) domain of Slit and the two N-terminal Ig domains of Robo, Ig1 and Ig2. The primary Robo binding site for Slit2 has been shown by surface plasmon resonance experiments and mutational analysis to be the Ig1 domain, while the Ig2 domain has been proposed to harbor a weak secondary binding site. This group belongs to the I-set of IgSF domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand, but lack a C" strand.


Pssm-ID: 409390 [Multi-domain]  Cd Length: 83  Bit Score: 38.92  E-value: 8.68e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 281359561 5284 SDIKIKAGNVFEFDVPVTGEPLPSKDWTHE-GNMIINtdRVKIsnFDDRTkIRILDAKRSDTGVYTLTARNINGT 5357
Cdd:cd05725     5 QNQVVLVDDSAEFQCEVGGDPVPTVRWRKEdGELPKG--RYEI--LDDHS-LKIRKVTAGDMGSYTCVAENMVGK 74
Ig5_Contactin cd04969
Fifth immunoglobulin (Ig) domain of contactin; The members here are composed of the fifth ...
4992-5059 8.81e-03

Fifth immunoglobulin (Ig) domain of contactin; The members here are composed of the fifth immunoglobulin (Ig) domain of contactins. Contactins are neural cell adhesion molecules and are comprised of six Ig domains followed by four fibronectin type III (FnIII) domains anchored to the membrane by glycosylphosphatidylinositol. The first four Ig domains form the intermolecular binding fragment, which arranges as a compact U-shaped module via contacts between Ig domains 1 and 4, and between Ig domains 2 and 3. Contactin-2 (TAG-1, axonin-1) may play a part in the neuronal processes of neurite outgrowth, axon guidance and fasciculation, and neuronal migration. This group also includes contactin-1 and contactin-5. The different contactins show different expression patterns in the central nervous system. During development and in adulthood, contactin-2 is transiently expressed in subsets of central and peripheral neurons. Contactin-5 is expressed specifically in the rat postnatal nervous system, peaking at about 3 weeks postnatal, and a lack of contactin-5 (NB-2) results in an impairment of neuronal activity in the rat auditory system. Contactin-5 is highly expressed in the adult human brain in the occipital lobe and in the amygdala. Contactin-1 is differentially expressed in tumor tissues and may, through a RhoA mechanism, facilitate invasion and metastasis of human lung adenocarcinoma.


Pssm-ID: 409358 [Multi-domain]  Cd Length: 89  Bit Score: 39.37  E-value: 8.81e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 281359561 4992 KAGQSFTFDCKVSGEPAPQTKWllKKKEVYSKDNVKVTNVDyNTKLKVNSATRSDSGIYTVFAENANG 5059
Cdd:cd04969    15 AKGGDVIIECKPKASPKPTISW--SKGTELLTNSSRICILP-DGSLKIKNVTKSDEGKYTCFAVNFFG 79
IgI_2_Robo cd05724
Second immunoglobulin (Ig)-like domain in Robo (roundabout) receptors; member of the I-set of ...
3524-3588 9.45e-03

Second immunoglobulin (Ig)-like domain in Robo (roundabout) receptors; member of the I-set of Ig superfamily (IgSF) domains; The members here are composed of the second immunoglobulin (Ig)-like domain in Robo (roundabout) receptors. Robo receptors play a role in the development of the central nervous system (CNS), and are receptors of the Slit protein. Slit is a repellant secreted by the neural cells in the midline. Slit acts through Robo to prevent most neurons from crossing the midline from either side. Three mammalian Robo homologs (Robo1, Robo2, and Robo3), and three mammalian Slit homologs (Slit-1,Slit-2, Slit-3), have been identified. Commissural axons, which cross the midline, express low levels of Robo; longitudinal axons, which avoid the midline, express high levels of Robo. Robo1, Robo2, and Robo3 are expressed by commissural neurons in the vertebrate spinal cord and Slit-1, Slit-2, Slit-3 are expressed at the ventral midline. Robo-3 is a divergent member of the Robo family which instead of being a positive regulator of Slit responsiveness, antagonizes Slit responsiveness in precrossing axons. The Slit-Robo interaction is mediated by the second leucine-rich repeat (LRR) domain of Slit and the two N-terminal Ig domains of Robo, Ig1 and Ig2. The primary Robo binding site for Slit-2 has been shown by surface plasmon resonance experiments and mutational analysis to be the Ig1 domain, while the Ig2 domain has been proposed to harbor a weak secondary binding site. This group belongs to the I-set of IgSF domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand, but lack a C" strand.


Pssm-ID: 409389 [Multi-domain]  Cd Length: 87  Bit Score: 38.92  E-value: 9.45e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 281359561 3524 RGEPAPKVEWFFNNSSVTSDEHSVKIdnVDyNTKFFVMRAQRSQSGKYIIKATNEVGEDE---AELEV 3588
Cdd:cd05724    23 RGHPEPTVSWRKDGQPLNLDNERVRI--VD-DGNLLIAEARKSDEGTYKCVATNMVGEREsraARLSV 87
IgI_Myotilin_C cd05892
C-terminal immunoglobulin (Ig)-like domain of myotilin; member of the I-set of Ig superfamily ...
8740-8831 9.55e-03

C-terminal immunoglobulin (Ig)-like domain of myotilin; member of the I-set of Ig superfamily (IgSF) domains; The members here are composed of the C-terminal immunoglobulin (Ig)-like domain of myotilin. Mytolin belongs to the palladin-myotilin-myopalladin family. Proteins belonging to the latter family contain multiple Ig-like domains and function as scaffolds, modulating the actin cytoskeleton. Myotilin is most abundant in skeletal and cardiac muscle and is involved in maintaining sarcomere integrity. It binds to alpha-actinin, filamin, and actin. Mutations in myotilin lead to muscle disorders. This group belongs to the I-set of IgSF domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand, but lack a C" strand.


Pssm-ID: 409473  Cd Length: 92  Bit Score: 39.37  E-value: 9.55e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 8740 PKIVSHLESRFVRDGDAVNLACRIIGAQHFDVVWLHNNKEIKPSKD--FQYTNEANIYRLQIAEIFPEDGGTYTCEAFND 8817
Cdd:cd05892     1 PMFIQKPQNKKVLEGDPVRLECQISAIPPPQIFWKKNNEMLQYNTDriSLYQDNCGRICLLIQNANKKDAGWYTVSAVNE 80
                          90
                  ....*....|....
gi 281359561 8818 IGesFSTCTINVTV 8831
Cdd:cd05892    81 AG--VVSCNARLDV 92
IgI_5_Dscam cd20958
Fifth immunoglobulin domain of the Drosophila melanogaster Dscam protein, and similar domains; ...
5283-5366 9.68e-03

Fifth immunoglobulin domain of the Drosophila melanogaster Dscam protein, and similar domains; a member of the I-set of IgSF domains; The members here are composed of the fifth immunoglobulin domain of the Drosophila melanogaster Down syndrome cell adhesion molecule (DSCAM) protein and similar proteins. Down syndrome cell adhesion molecule (DSCAM) is a cell adhesion molecule that plays critical roles in neural development, including axon guidance and branching, axon target recognition, self-avoidance and synaptic formation. DSCAM belongs to the immunoglobulin superfamily and contributes to defects in the central nervous system in Down syndrome patients. Vertebrate DSCAMs differ from Drosophila Dscam1 in that they lack the extensive alternative splicing that occurs in the insect gene. Drosophila melanogaster Dscam has 38,016 isoforms generated by the alternative splicing of four variable exon clusters, which allows every neuron in the fly to display a distinctive set of Dscam proteins on its cell surface. Drosophila Dscam1 is a cell-surface protein that plays important roles in neural development and axon tiling of neurons. It is shown that thousands of isoforms bind themselves through specific homophilic (self-binding) interactions, a process which mediates cellular self-recognition. Drosophila Dscam2 is also alternatively spliced and plays a key role in the development of two visual system neurons, monopolar cells L1 and L2. This group is a member of the I-set Ig domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand but lack a C" strand.


Pssm-ID: 409550 [Multi-domain]  Cd Length: 89  Bit Score: 39.09  E-value: 9.68e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359561 5283 MSDIKIKAGNVFEFDVPVTGEPLPSKDWTHEGNMIINTDRVKIsnFDDRT-KIRILDaKRSDTGVYTLTARNING-TDRH 5360
Cdd:cd20958     7 MGNLTAVAGQTLRLHCPVAGYPISSITWEKDGRRLPLNHRQRV--FPNGTlVIENVQ-RSSDEGEYTCTARNQQGqSASR 83

                  ....*.
gi 281359561 5361 NVKVTI 5366
Cdd:cd20958    84 SVFVKV 89
IgI_2_Robo cd05724
Second immunoglobulin (Ig)-like domain in Robo (roundabout) receptors; member of the I-set of ...
2330-2391 9.92e-03

Second immunoglobulin (Ig)-like domain in Robo (roundabout) receptors; member of the I-set of Ig superfamily (IgSF) domains; The members here are composed of the second immunoglobulin (Ig)-like domain in Robo (roundabout) receptors. Robo receptors play a role in the development of the central nervous system (CNS), and are receptors of the Slit protein. Slit is a repellant secreted by the neural cells in the midline. Slit acts through Robo to prevent most neurons from crossing the midline from either side. Three mammalian Robo homologs (Robo1, Robo2, and Robo3), and three mammalian Slit homologs (Slit-1,Slit-2, Slit-3), have been identified. Commissural axons, which cross the midline, express low levels of Robo; longitudinal axons, which avoid the midline, express high levels of Robo. Robo1, Robo2, and Robo3 are expressed by commissural neurons in the vertebrate spinal cord and Slit-1, Slit-2, Slit-3 are expressed at the ventral midline. Robo-3 is a divergent member of the Robo family which instead of being a positive regulator of Slit responsiveness, antagonizes Slit responsiveness in precrossing axons. The Slit-Robo interaction is mediated by the second leucine-rich repeat (LRR) domain of Slit and the two N-terminal Ig domains of Robo, Ig1 and Ig2. The primary Robo binding site for Slit-2 has been shown by surface plasmon resonance experiments and mutational analysis to be the Ig1 domain, while the Ig2 domain has been proposed to harbor a weak secondary binding site. This group belongs to the I-set of IgSF domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand, but lack a C" strand.


Pssm-ID: 409389 [Multi-domain]  Cd Length: 87  Bit Score: 38.92  E-value: 9.92e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 281359561 2330 GEPEPAATWVKGTDNLKFDNQRIcldQLERNSSITIKKSVRKDTGKYKLVLSNSSGTIESEA 2391
Cdd:cd05724    24 GHPEPTVSWRKDGQPLNLDNERV---RIVDDGNLLIAEARKSDEGTYKCVATNMVGERESRA 82
IgI_5_Dscam cd20958
Fifth immunoglobulin domain of the Drosophila melanogaster Dscam protein, and similar domains; ...
6179-6255 9.97e-03

Fifth immunoglobulin domain of the Drosophila melanogaster Dscam protein, and similar domains; a member of the I-set of IgSF domains; The members here are composed of the fifth immunoglobulin domain of the Drosophila melanogaster Down syndrome cell adhesion molecule (DSCAM) protein and similar proteins. Down syndrome cell adhesion molecule (DSCAM) is a cell adhesion molecule that plays critical roles in neural development, including axon guidance and branching, axon target recognition, self-avoidance and synaptic formation. DSCAM belongs to the immunoglobulin superfamily and contributes to defects in the central nervous system in Down syndrome patients. Vertebrate DSCAMs differ from Drosophila Dscam1 in that they lack the extensive alternative splicing that occurs in the insect gene. Drosophila melanogaster Dscam has 38,016 isoforms generated by the alternative splicing of four variable exon clusters, which allows every neuron in the fly to display a distinctive set of Dscam proteins on its cell surface. Drosophila Dscam1 is a cell-surface protein that plays important roles in neural development and axon tiling of neurons. It is shown that thousands of isoforms bind themselves through specific homophilic (self-binding) interactions, a process which mediates cellular self-recognition. Drosophila Dscam2 is also alternatively spliced and plays a key role in the development of two visual system neurons, monopolar cells L1 and L2. This group is a member of the I-set Ig domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand but lack a C" strand.


Pssm-ID: 409550 [Multi-domain]  Cd Length: 89  Bit Score: 39.09  E-value: 9.97e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 281359561 6179 AGEPVNLNIPISGAPTPTIEWKRGDLKLEEGKRISYETNSERTLFRIDdsNRRDSGKYTVTAANEFG-KDTADIEVIV 6255
Cdd:cd20958    14 AGQTLRLHCPVAGYPISSITWEKDGRRLPLNHRQRVFPNGTLVIENVQ--RSSDEGEYTCTARNQQGqSASRSVFVKV 89
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH