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Conserved domains on  [gi|442627668|ref|NP_523559|]
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kekkon 1, isoform B [Drosophila melanogaster]

Protein Classification

leucine-rich repeat domain-containing protein; toll-like receptor( domain architecture ID 11471532)

leucine-rich repeat (LRR) domain-containing protein may participate in protein-protein interactions| toll-like receptor (TLR) is involved in the recognition of microbial pathogens by the innate immune system, which recognize different pathogen-associated molecular patterns

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
LRR COG4886
Leucine-rich repeat (LRR) protein [Transcription];
122-277 1.21e-27

Leucine-rich repeat (LRR) protein [Transcription];


:

Pssm-ID: 443914 [Multi-domain]  Cd Length: 414  Bit Score: 116.57  E-value: 1.21e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627668 122 NTQVLDMSGNKLQTLSNEqfIrANLLNLQKLYLRNCKIGEIErETFKGLTNLVELDLSHNLLVTVPSlALGHIPSLRELT 201
Cdd:COG4886  114 NLESLDLSGNQLTDLPEE--L-ANLTNLKELDLSNNQLTDLP-EPLGNLTNLKSLDLSNNQLTDLPE-ELGNLTNLKELD 188

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 442627668 202 LASNHIHKIeSQAFGNTPSLHKLDLSHCDIQTISAqAFGGLQGLTLLRLNGNKLSELlpKTIETLSRLHGIELHDN 277
Cdd:COG4886  189 LSNNQITDL-PEPLGNLTNLEELDLSGNQLTDLPE-PLANLTNLETLDLSNNQLTDL--PELGNLTNLEELDLSNN 260
IG_like smart00410
Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.
 338-429 1.64e-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: 63.68  E-value: 1.64e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627668   338 VEAAMGENASITCRARAVPAANINWYWNGRLLANNSaftayQRIHMLEQveggfEKRSKLVLTNAQETDSSEFYCVAENR 417
Cdd:smart00410   4 VTVKEGESVTLSCEASGSPPPEVTWYKQGGKLLAES-----GRFSVSRS-----GSTSTLTISNVTPEDSGTYTCAATNS 73

                           90
                   ....*....|..
gi 442627668   418 AGMAEANFTLHV 429
Cdd:smart00410  74 SGSASSGTTLTV 85
LRRCT smart00082
Leucine rich repeat C-terminal domain;
277-327 5.57e-09

Leucine rich repeat C-terminal domain;


:

Pssm-ID: 214507 [Multi-domain]  Cd Length: 51  Bit Score: 52.82  E-value: 5.57e-09
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|..
gi 442627668   277 NPWLCDCRLRDTKLWLM-KRNIPYPVAPVCSgGPERIIDRSFADLHvDEFAC 327
Cdd:smart00082   1 NPFICDCELRWLLRWLQaNEHLQDPVDLRCA-SPSSLRGPLLELLH-SEFKC 50
 
Name Accession Description Interval E-value
LRR COG4886
Leucine-rich repeat (LRR) protein [Transcription];
122-277 1.21e-27

Leucine-rich repeat (LRR) protein [Transcription];


Pssm-ID: 443914 [Multi-domain]  Cd Length: 414  Bit Score: 116.57  E-value: 1.21e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627668 122 NTQVLDMSGNKLQTLSNEqfIrANLLNLQKLYLRNCKIGEIErETFKGLTNLVELDLSHNLLVTVPSlALGHIPSLRELT 201
Cdd:COG4886  114 NLESLDLSGNQLTDLPEE--L-ANLTNLKELDLSNNQLTDLP-EPLGNLTNLKSLDLSNNQLTDLPE-ELGNLTNLKELD 188

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 442627668 202 LASNHIHKIeSQAFGNTPSLHKLDLSHCDIQTISAqAFGGLQGLTLLRLNGNKLSELlpKTIETLSRLHGIELHDN 277
Cdd:COG4886  189 LSNNQITDL-PEPLGNLTNLEELDLSGNQLTDLPE-PLANLTNLETLDLSNNQLTDL--PELGNLTNLEELDLSNN 260
LRR_8 pfam13855
Leucine rich repeat;
148-207 5.61e-15

Leucine rich repeat;


Pssm-ID: 404697 [Multi-domain]  Cd Length: 61  Bit Score: 69.86  E-value: 5.61e-15
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627668  148 NLQKLYLRNCKIGEIERETFKGLTNLVELDLSHNLLVTVPSLALGHIPSLRELTLASNHI 207
Cdd:pfam13855   2 NLRSLDLSNNRLTSLDDGAFKGLSNLKVLDLSNNLLTTLSPGAFSGLPSLRYLDLSGNRL 61
PPP1R42 cd21340
protein phosphatase 1 regulatory subunit 42; Protein phosphatase 1 regulatory subunit 42 ...
 121-278 2.46e-13

protein phosphatase 1 regulatory subunit 42; Protein phosphatase 1 regulatory subunit 42 (PPP1R42), also known as leucine-rich repeat-containing protein 67 (lrrc67) or testis leucine-rich repeat (TLRR) protein, plays a role in centrosome separation. PPP1R42 has been shown to interact with the well-conserved signaling protein phosphatase-1 (PP1) and thereby increasing PP1's activity, which counters centrosome separation. Inhibition of PPP1R42 expression increases the number of centrosomes per cell while its depletion reduces the activity of PP1 leading to activation of NEK2, the kinase responsible for phosphorylation of centrosomal linker proteins promoting centrosome separation.


Pssm-ID: 411060 [Multi-domain]  Cd Length: 220  Bit Score: 70.20  E-value: 2.46e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627668 121 PNTQVLDMSGNKLQTLSNEQFiranLLNLQKLYLRNCKIGEIERetFKGLTNLVELDLSHNLLVTVPSlaLGHIPSLREL 200
Cdd:cd21340   24 KNLKVLYLYDNKITKIENLEF----LTNLTHLYLQNNQIEKIEN--LENLVNLKKLYLGGNRISVVEG--LENLTNLEEL 95

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627668 201 TLASNHIHKIESQAFGN------TPSLHKLDLSHCDIQTISaqAFGGLQGLTLLRLNGNKLSEL--LPKTIETLSRLHGI 272
Cdd:cd21340   96 HIENQRLPPGEKLTFDPrslaalSNSLRVLNISGNNIDSLE--PLAPLRNLEQLDASNNQISDLeeLLDLLSSWPSLREL 173


                 ....*.
gi 442627668 273 ELHDNP 278
Cdd:cd21340  174 DLTGNP 179
IG_like smart00410
Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.
 338-429 1.64e-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: 63.68  E-value: 1.64e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627668   338 VEAAMGENASITCRARAVPAANINWYWNGRLLANNSaftayQRIHMLEQveggfEKRSKLVLTNAQETDSSEFYCVAENR 417
Cdd:smart00410   4 VTVKEGESVTLSCEASGSPPPEVTWYKQGGKLLAES-----GRFSVSRS-----GSTSTLTISNVTPEDSGTYTCAATNS 73

                           90
                   ....*....|..
gi 442627668   418 AGMAEANFTLHV 429
Cdd:smart00410  74 SGSASSGTTLTV 85
I-set pfam07679
Immunoglobulin I-set domain;
329-429 3.62e-10

Immunoglobulin I-set domain;


Pssm-ID: 400151 [Multi-domain]  Cd Length: 90  Bit Score: 57.27  E-value: 3.62e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627668  329 PEMLPISHYVEAAMGENASITCRARAVPAANINWYWNGRLLANNsaftayQRIHMLEQveggfEKRSKLVLTNAQETDSS 408
Cdd:pfam07679   1 PKFTQKPKDVEVQEGESARFTCTVTGTPDPEVSWFKDGQPLRSS------DRFKVTYE-----GGTYTLTISNVQPDDSG 69

                          90       100
                  ....*....|....*....|.
gi 442627668  409 EFYCVAENRAGMAEANFTLHV 429
Cdd:pfam07679  70 KYTCVATNSAGEAEASAELTV 90
LRRCT smart00082
Leucine rich repeat C-terminal domain;
277-327 5.57e-09

Leucine rich repeat C-terminal domain;


Pssm-ID: 214507 [Multi-domain]  Cd Length: 51  Bit Score: 52.82  E-value: 5.57e-09
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|..
gi 442627668   277 NPWLCDCRLRDTKLWLM-KRNIPYPVAPVCSgGPERIIDRSFADLHvDEFAC 327
Cdd:smart00082   1 NPFICDCELRWLLRWLQaNEHLQDPVDLRCA-SPSSLRGPLLELLH-SEFKC 50
IgI_4_hemolin-like cd20978
Fourth immunoglobulin (Ig)-like domain of hemolin, and similar domains; a member of the I-set ...
 343-429 9.45e-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: 50.47  E-value: 9.45e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627668 343 GENASITCRARAVPAANINWYWNGRLLANNSaftayQRIHMleqveggfeKRSKLVLTNAQETDSSEFYCVAENRAGMAE 422
Cdd:cd20978   16 GQDVTLPCQVTGVPQPKITWLHNGKPLQGPM-----ERATV---------EDGTLTIINVQPEDTGYYGCVATNEIGDIY 81


                 ....*..
gi 442627668 423 ANFTLHV 429
Cdd:cd20978   82 TETLLHV 88
PLN00113 PLN00113
leucine-rich repeat receptor-like protein kinase; Provisional
 81-277 6.89e-07

leucine-rich repeat receptor-like protein kinase; Provisional


Pssm-ID: 215061 [Multi-domain]  Cd Length: 968  Bit Score: 53.31  E-value: 6.89e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627668  81 DPPAQQQSTCQTVCACKWKG----GKQTVECIDRHLIQIPEHIDPNT------QVLDMSGNKLQ---------------- 134
Cdd:PLN00113  43 DPLKYLSNWNSSADVCLWQGitcnNSSRVVSIDLSGKNISGKISSAIfrlpyiQTINLSNNQLSgpipddifttssslry 122

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627668 135 -TLSNEQFI----RANLLNLQKLYLRNCKI-GEIEREtFKGLTNLVELDLSHNLLVTVPSLALGHIPSLRELTLASNH-- 206
Cdd:PLN00113 123 lNLSNNNFTgsipRGSIPNLETLDLSNNMLsGEIPND-IGSFSSLKVLDLGGNVLVGKIPNSLTNLTSLEFLTLASNQlv 201

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627668 207 ------IHKIES----------------QAFGNTPSLHKLDLSHCDIQTISAQAFGGLQGLTLLRLNGNKLSELLPKTIE 264
Cdd:PLN00113 202 gqipreLGQMKSlkwiylgynnlsgeipYEIGGLTSLNHLDLVYNNLTGPIPSSLGNLKNLQYLFLYQNKLSGPIPPSIF 281

                        250
                 ....*....|...
gi 442627668 265 TLSRLHGIELHDN 277
Cdd:PLN00113 282 SLQKLISLDLSDN 294
 
Name Accession Description Interval E-value
LRR COG4886
Leucine-rich repeat (LRR) protein [Transcription];
122-277 1.21e-27

Leucine-rich repeat (LRR) protein [Transcription];


Pssm-ID: 443914 [Multi-domain]  Cd Length: 414  Bit Score: 116.57  E-value: 1.21e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627668 122 NTQVLDMSGNKLQTLSNEqfIrANLLNLQKLYLRNCKIGEIErETFKGLTNLVELDLSHNLLVTVPSlALGHIPSLRELT 201
Cdd:COG4886  114 NLESLDLSGNQLTDLPEE--L-ANLTNLKELDLSNNQLTDLP-EPLGNLTNLKSLDLSNNQLTDLPE-ELGNLTNLKELD 188

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 442627668 202 LASNHIHKIeSQAFGNTPSLHKLDLSHCDIQTISAqAFGGLQGLTLLRLNGNKLSELlpKTIETLSRLHGIELHDN 277
Cdd:COG4886  189 LSNNQITDL-PEPLGNLTNLEELDLSGNQLTDLPE-PLANLTNLETLDLSNNQLTDL--PELGNLTNLEELDLSNN 260
LRR COG4886
Leucine-rich repeat (LRR) protein [Transcription];
112-277 6.21e-20

Leucine-rich repeat (LRR) protein [Transcription];


Pssm-ID: 443914 [Multi-domain]  Cd Length: 414  Bit Score: 93.46  E-value: 6.21e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627668 112 LIQIPEHID--PNTQVLDMSGNKLQTLSNEqfIrANLLNLQKLYLRNCKIGEIEREtFKGLTNLVELDLSHNLLVTVPSl 189
Cdd:COG4886  171 LTDLPEELGnlTNLKELDLSNNQITDLPEP--L-GNLTNLEELDLSGNQLTDLPEP-LANLTNLETLDLSNNQLTDLPE- 245

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627668 190 aLGHIPSLRELTLASNHIHKIESqaFGNTPSLHKLDLSHCDIQTISAQAFGGLQGLTLLRLNGNKLSELLPKTIETLSRL 269
Cdd:COG4886  246 -LGNLTNLEELDLSNNQLTDLPP--LANLTNLKTLDLSNNQLTDLKLKELELLLGLNSLLLLLLLLNLLELLILLLLLTT 322


                 ....*...
gi 442627668 270 HGIELHDN 277
Cdd:COG4886  323 LLLLLLLL 330
LRR COG4886
Leucine-rich repeat (LRR) protein [Transcription];
119-277 6.55e-19

Leucine-rich repeat (LRR) protein [Transcription];


Pssm-ID: 443914 [Multi-domain]  Cd Length: 414  Bit Score: 90.38  E-value: 6.55e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627668 119 IDPNTQVLDMSGNKLQTLSNEQFIRANLLNLQKLYLRNCkigeierETFKGLTNLVELDLSHNLLVTVPSlALGHIPSLR 198
Cdd:COG4886   68 LLSLLLLLLLSLLLLSLLLLGLTDLGDLTNLTELDLSGN-------EELSNLTNLESLDLSGNQLTDLPE-ELANLTNLK 139

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 442627668 199 ELTLASNHIHKIESqAFGNTPSLHKLDLSHCDIQTISAqAFGGLQGLTLLRLNGNKLSElLPKTIETLSRLHGIELHDN 277
Cdd:COG4886  140 ELDLSNNQLTDLPE-PLGNLTNLKSLDLSNNQLTDLPE-ELGNLTNLKELDLSNNQITD-LPEPLGNLTNLEELDLSGN 215
LRR_8 pfam13855
Leucine rich repeat;
148-207 5.61e-15

Leucine rich repeat;


Pssm-ID: 404697 [Multi-domain]  Cd Length: 61  Bit Score: 69.86  E-value: 5.61e-15
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627668  148 NLQKLYLRNCKIGEIERETFKGLTNLVELDLSHNLLVTVPSLALGHIPSLRELTLASNHI 207
Cdd:pfam13855   2 NLRSLDLSNNRLTSLDDGAFKGLSNLKVLDLSNNLLTTLSPGAFSGLPSLRYLDLSGNRL 61
LRR COG4886
Leucine-rich repeat (LRR) protein [Transcription];
129-278 1.77e-14

Leucine-rich repeat (LRR) protein [Transcription];


Pssm-ID: 443914 [Multi-domain]  Cd Length: 414  Bit Score: 76.51  E-value: 1.77e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627668 129 SGNKLQTLSNEQFIRANLLNLQKLYLRNCKIGEIERETFKGLTNLVELDLSHNllvtvpsLALGHIPSLRELTLASNHIH 208
Cdd:COG4886   54 SLLLRDLLLSSLLLLLSLLLLLLLSLLLLSLLLLGLTDLGDLTNLTELDLSGN-------EELSNLTNLESLDLSGNQLT 126

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627668 209 KIEsQAFGNTPSLHKLDLSHCDIQTISAqAFGGLQGLTLLRLNGNKLSElLPKTIETLSRLHGIELHDNP 278
Cdd:COG4886  127 DLP-EELANLTNLKELDLSNNQLTDLPE-PLGNLTNLKSLDLSNNQLTD-LPEELGNLTNLKELDLSNNQ 193
PPP1R42 cd21340
protein phosphatase 1 regulatory subunit 42; Protein phosphatase 1 regulatory subunit 42 ...
 121-278 2.46e-13

protein phosphatase 1 regulatory subunit 42; Protein phosphatase 1 regulatory subunit 42 (PPP1R42), also known as leucine-rich repeat-containing protein 67 (lrrc67) or testis leucine-rich repeat (TLRR) protein, plays a role in centrosome separation. PPP1R42 has been shown to interact with the well-conserved signaling protein phosphatase-1 (PP1) and thereby increasing PP1's activity, which counters centrosome separation. Inhibition of PPP1R42 expression increases the number of centrosomes per cell while its depletion reduces the activity of PP1 leading to activation of NEK2, the kinase responsible for phosphorylation of centrosomal linker proteins promoting centrosome separation.


Pssm-ID: 411060 [Multi-domain]  Cd Length: 220  Bit Score: 70.20  E-value: 2.46e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627668 121 PNTQVLDMSGNKLQTLSNEQFiranLLNLQKLYLRNCKIGEIERetFKGLTNLVELDLSHNLLVTVPSlaLGHIPSLREL 200
Cdd:cd21340   24 KNLKVLYLYDNKITKIENLEF----LTNLTHLYLQNNQIEKIEN--LENLVNLKKLYLGGNRISVVEG--LENLTNLEEL 95

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627668 201 TLASNHIHKIESQAFGN------TPSLHKLDLSHCDIQTISaqAFGGLQGLTLLRLNGNKLSEL--LPKTIETLSRLHGI 272
Cdd:cd21340   96 HIENQRLPPGEKLTFDPrslaalSNSLRVLNISGNNIDSLE--PLAPLRNLEQLDASNNQISDLeeLLDLLSSWPSLREL 173


                 ....*.
gi 442627668 273 ELHDNP 278
Cdd:cd21340  174 DLTGNP 179
IG_like smart00410
Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.
 338-429 1.64e-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: 63.68  E-value: 1.64e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627668   338 VEAAMGENASITCRARAVPAANINWYWNGRLLANNSaftayQRIHMLEQveggfEKRSKLVLTNAQETDSSEFYCVAENR 417
Cdd:smart00410   4 VTVKEGESVTLSCEASGSPPPEVTWYKQGGKLLAES-----GRFSVSRS-----GSTSTLTISNVTPEDSGTYTCAATNS 73

                           90
                   ....*....|..
gi 442627668   418 AGMAEANFTLHV 429
Cdd:smart00410  74 SGSASSGTTLTV 85
LRR_8 pfam13855
Leucine rich repeat;
195-255 1.69e-12

Leucine rich repeat;


Pssm-ID: 404697 [Multi-domain]  Cd Length: 61  Bit Score: 62.93  E-value: 1.69e-12
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 442627668  195 PSLRELTLASNHIHKIESQAFGNTPSLHKLDLSHCDIQTISAQAFGGLQGLTLLRLNGNKL 255
Cdd:pfam13855   1 PNLRSLDLSNNRLTSLDDGAFKGLSNLKVLDLSNNLLTTLSPGAFSGLPSLRYLDLSGNRL 61
I-set pfam07679
Immunoglobulin I-set domain;
329-429 3.62e-10

Immunoglobulin I-set domain;


Pssm-ID: 400151 [Multi-domain]  Cd Length: 90  Bit Score: 57.27  E-value: 3.62e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627668  329 PEMLPISHYVEAAMGENASITCRARAVPAANINWYWNGRLLANNsaftayQRIHMLEQveggfEKRSKLVLTNAQETDSS 408
Cdd:pfam07679   1 PKFTQKPKDVEVQEGESARFTCTVTGTPDPEVSWFKDGQPLRSS------DRFKVTYE-----GGTYTLTISNVQPDDSG 69

                          90       100
                  ....*....|....*....|.
gi 442627668  409 EFYCVAENRAGMAEANFTLHV 429
Cdd:pfam07679  70 KYTCVATNSAGEAEASAELTV 90
LRR_8 pfam13855
Leucine rich repeat;
121-183 5.15e-10

Leucine rich repeat;


Pssm-ID: 404697 [Multi-domain]  Cd Length: 61  Bit Score: 55.99  E-value: 5.15e-10
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 442627668  121 PNTQVLDMSGNKLQTLSNEQFirANLLNLQKLYLRNCKIGEIERETFKGLTNLVELDLSHNLL 183
Cdd:pfam13855   1 PNLRSLDLSNNRLTSLDDGAF--KGLSNLKVLDLSNNLLTTLSPGAFSGLPSLRYLDLSGNRL 61
LRR_8 pfam13855
Leucine rich repeat;
171-231 1.23e-09

Leucine rich repeat;


Pssm-ID: 404697 [Multi-domain]  Cd Length: 61  Bit Score: 54.84  E-value: 1.23e-09
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 442627668  171 TNLVELDLSHNLLVTVPSLALGHIPSLRELTLASNHIHKIESQAFGNTPSLHKLDLSHCDI 231
Cdd:pfam13855   1 PNLRSLDLSNNRLTSLDDGAFKGLSNLKVLDLSNNLLTTLSPGAFSGLPSLRYLDLSGNRL 61
LRR_RI cd00116
Leucine-rich repeats (LRRs), ribonuclease inhibitor (RI)-like subfamily. LRRs are 20-29 ...
 119-277 1.56e-09

Leucine-rich repeats (LRRs), ribonuclease inhibitor (RI)-like subfamily. LRRs are 20-29 residue sequence motifs present in many proteins that participate in protein-protein interactions and have different functions and cellular locations. LRRs correspond to structural units consisting of a beta strand (LxxLxLxxN/CxL conserved pattern) and an alpha helix. This alignment contains 12 strands corresponding to 11 full repeats, consistent with the extent observed in the subfamily acting as Ran GTPase Activating Proteins (RanGAP1).


Pssm-ID: 238064 [Multi-domain]  Cd Length: 319  Bit Score: 60.45  E-value: 1.56e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627668 119 IDPNTQVLDM---SGNKLQTLS---------NEQFIRANLLN--LQKLYLRNCKIG-EIERETFKGLT----NLVELDLS 179
Cdd:cd00116   66 IPRGLQSLLQgltKGCGLQELDlsdnalgpdGCGVLESLLRSssLQELKLNNNGLGdRGLRLLAKGLKdlppALEKLVLG 145

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627668 180 HNLLVTVPSLALG----HIPSLRELTLASNHIHK--IES--QAFGNTPSLHKLDLSHCDIQTISAQAFGG----LQGLTL 247
Cdd:cd00116  146 RNRLEGASCEALAkalrANRDLKELNLANNGIGDagIRAlaEGLKANCNLEVLDLNNNGLTDEGASALAEtlasLKSLEV 225

                        170       180       190
                 ....*....|....*....|....*....|....*
gi 442627668 248 LRLNGNKL-----SELLPKTIETLSRLHGIELHDN 277
Cdd:cd00116  226 LNLGDNNLtdagaAALASALLSPNISLLTLSLSCN 260
Ig_3 pfam13927
Immunoglobulin domain; This family contains immunoglobulin-like domains.
 338-416 2.91e-09

Immunoglobulin domain; This family contains immunoglobulin-like domains.


Pssm-ID: 464046 [Multi-domain]  Cd Length: 78  Bit Score: 54.49  E-value: 2.91e-09
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 442627668  338 VEAAMGENASITCRARAVPAANINWYWNGRLLANNSaftayqrihmlEQVEGGFEKRSKLVLTNAQETDSSEFYCVAEN 416
Cdd:pfam13927  11 VTVREGETVTLTCEATGSPPPTITWYKNGEPISSGS-----------TRSRSLSGSNSTLTISNVTRSDAGTYTCVASN 78
LRRCT smart00082
Leucine rich repeat C-terminal domain;
277-327 5.57e-09

Leucine rich repeat C-terminal domain;


Pssm-ID: 214507 [Multi-domain]  Cd Length: 51  Bit Score: 52.82  E-value: 5.57e-09
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|..
gi 442627668   277 NPWLCDCRLRDTKLWLM-KRNIPYPVAPVCSgGPERIIDRSFADLHvDEFAC 327
Cdd:smart00082   1 NPFICDCELRWLLRWLQaNEHLQDPVDLRCA-SPSSLRGPLLELLH-SEFKC 50
IgI_4_hemolin-like cd20978
Fourth immunoglobulin (Ig)-like domain of hemolin, and similar domains; a member of the I-set ...
 343-429 9.45e-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: 50.47  E-value: 9.45e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627668 343 GENASITCRARAVPAANINWYWNGRLLANNSaftayQRIHMleqveggfeKRSKLVLTNAQETDSSEFYCVAENRAGMAE 422
Cdd:cd20978   16 GQDVTLPCQVTGVPQPKITWLHNGKPLQGPM-----ERATV---------EDGTLTIINVQPEDTGYYGCVATNEIGDIY 81


                 ....*..
gi 442627668 423 ANFTLHV 429
Cdd:cd20978   82 TETLLHV 88
Ig cd00096
Immunoglobulin domain; The members here are composed of the immunoglobulin (Ig) domain found ...
 346-419 9.73e-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: 49.64  E-value: 9.73e-08
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 442627668 346 ASITCRARAVPAANINWYWNGRLLANNSAFTAYQRIHmleqveggfekRSKLVLTNAQETDSSEFYCVAENRAG 419
Cdd:cd00096    1 VTLTCSASGNPPPTITWYKNGKPLPPSSRDSRRSELG-----------NGTLTISNVTLEDSGTYTCVASNSAG 63
LRR_8 pfam13855
Leucine rich repeat;
219-278 1.58e-07

Leucine rich repeat;


Pssm-ID: 404697 [Multi-domain]  Cd Length: 61  Bit Score: 48.67  E-value: 1.58e-07
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627668  219 PSLHKLDLSHCDIQTISAQAFGGLQGLTLLRLNGNKLSELLPKTIETLSRLHGIELHDNP 278
Cdd:pfam13855   1 PNLRSLDLSNNRLTSLDDGAFKGLSNLKVLDLSNNLLTTLSPGAFSGLPSLRYLDLSGNR 60
PLN00113 PLN00113
leucine-rich repeat receptor-like protein kinase; Provisional
 81-277 6.89e-07

leucine-rich repeat receptor-like protein kinase; Provisional


Pssm-ID: 215061 [Multi-domain]  Cd Length: 968  Bit Score: 53.31  E-value: 6.89e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627668  81 DPPAQQQSTCQTVCACKWKG----GKQTVECIDRHLIQIPEHIDPNT------QVLDMSGNKLQ---------------- 134
Cdd:PLN00113  43 DPLKYLSNWNSSADVCLWQGitcnNSSRVVSIDLSGKNISGKISSAIfrlpyiQTINLSNNQLSgpipddifttssslry 122

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627668 135 -TLSNEQFI----RANLLNLQKLYLRNCKI-GEIEREtFKGLTNLVELDLSHNLLVTVPSLALGHIPSLRELTLASNH-- 206
Cdd:PLN00113 123 lNLSNNNFTgsipRGSIPNLETLDLSNNMLsGEIPND-IGSFSSLKVLDLGGNVLVGKIPNSLTNLTSLEFLTLASNQlv 201

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627668 207 ------IHKIES----------------QAFGNTPSLHKLDLSHCDIQTISAQAFGGLQGLTLLRLNGNKLSELLPKTIE 264
Cdd:PLN00113 202 gqipreLGQMKSlkwiylgynnlsgeipYEIGGLTSLNHLDLVYNNLTGPIPSSLGNLKNLQYLFLYQNKLSGPIPPSIF 281

                        250
                 ....*....|...
gi 442627668 265 TLSRLHGIELHDN 277
Cdd:PLN00113 282 SLQKLISLDLSDN 294
Ig4_L1-NrCAM_like cd04978
Fourth immunoglobulin (Ig)-like domain of L1, Ng-CAM (Neuron-glia CAM cell adhesion molecule), ...
 343-429 8.64e-07

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: 47.83  E-value: 8.64e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627668 343 GENASITCRARAVPAANINWYWNGRLLANNSAftayqriHMLEQVEGGfekrsKLVLTNAQETDSSEFYCVAENRAGMAE 422
Cdd:cd04978   14 GETGELICEAEGNPQPTITWRLNGVPIEPAPE-------DMRRTVDGR-----TLIFSNLQPNDTAVYQCNASNVHGYLL 81


                 ....*..
gi 442627668 423 ANFTLHV 429
Cdd:cd04978   82 ANAFLHV 88
IgC2_3_Dscam cd20957
Third immunoglobulin domain of the Drosophila melanogaster Dscam protein, and similar domains; ...
 342-423 1.05e-06

Third immunoglobulin domain of the Drosophila melanogaster Dscam protein, and similar domains; a member of the Constant 2 (C2)-set of IgSF domains; The members here are composed of the third 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. 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. This group belongs to the C2-set of IgSF domains, having A, B, and E strands in one beta-sheet and A', G, F, C, and C' in the other. Unlike other Ig domain sets, the C2-set lacks the D strand.


Pssm-ID: 409549 [Multi-domain]  Cd Length: 88  Bit Score: 47.53  E-value: 1.05e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627668 342 MGENASITCRARAVPAANINWYWNGRLLANNSaftayqRIHMLEqveggfekRSKLVLTNAQETDSSEFYCVAENRAGMA 421
Cdd:cd20957   15 FGRTAVFNCSVTGNPIHTVLWMKDGKPLGHSS------RVQILS--------EDVLVIPSVKREDKGMYQCFVRNDGDSA 80


                 ..
gi 442627668 422 EA 423
Cdd:cd20957   81 QA 82
RNA1 COG5238
Ran GTPase-activating protein (RanGAP) involved in mRNA processing and transport [Translation, ...
 112-278 1.08e-06

Ran GTPase-activating protein (RanGAP) involved in mRNA processing and transport [Translation, ribosomal structure and biogenesis];


Pssm-ID: 444072 [Multi-domain]  Cd Length: 434  Bit Score: 52.10  E-value: 1.08e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627668 112 LIQIPEHIDPNTQVLDMSGNKLQTLSNEQFIRANLLN--LQKLYLRNCKIGEIERETF----KGLTNLVELDLSHN---- 181
Cdd:COG5238  171 ISMAKALQNNSVETVYLGCNQIGDEGIEELAEALTQNttVTTLWLKRNPIGDEGAEILaealKGNKSLTTLDLSNNqigd 250

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627668 182 --LLVTVPSLALGHipSLRELTLASNHIH----KIESQAFGNTPSLHKLDLSHCDIQTISAQAFG-GLQG---LTLLRLN 251
Cdd:COG5238  251 egVIALAEALKNNT--TVETLYLSGNQIGaegaIALAKALQGNTTLTSLDLSVNRIGDEGAIALAeGLQGnktLHTLNLA 328

                        170       180       190
                 ....*....|....*....|....*....|.
gi 442627668 252 GNKLS----ELLPKTIETLSRLHGIELHDNP 278
Cdd:COG5238  329 YNGIGaqgaIALAKALQENTTLHSLDLSDNQ 359
Ig5_Contactin-1 cd05852
Fifth immunoglobulin (Ig) domain of contactin-1; The members here are composed of the fifth ...
 330-429 1.69e-06

Fifth immunoglobulin (Ig) domain of contactin-1; The members here are composed of the fifth immunoglobulin (Ig) domain of the neural cell adhesion molecule contactin-1. Contactins are comprised of six Ig domains followed by four fibronectin type III (FnIII) domains anchored to the membrane by glycosylphosphatidylinositol. Contactin-1 is differentially expressed in tumor tissues and may through a RhoA mechanism, facilitate invasion and metastasis of human lung adenocarcinoma.


Pssm-ID: 409438  Cd Length: 89  Bit Score: 46.92  E-value: 1.69e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627668 330 EMLPISHYVEAAMGENASITCRARAVPAANINWYWNGRLLANNSaftayqRIHMLEqvEGGFEkrsklvLTNAQETDSSE 409
Cdd:cd05852    4 EFNPMKKKILAAKGGRVIIECKPKAAPKPKFSWSKGTELLVNNS------RISIWD--DGSLE------ILNITKLDEGS 69

                         90       100
                 ....*....|....*....|
gi 442627668 410 FYCVAENRAGMAEANFTLHV 429
Cdd:cd05852   70 YTCFAENNRGKANSTGVLSV 89
PLN03150 PLN03150
hypothetical protein; Provisional
 194-281 1.83e-06

hypothetical protein; Provisional


Pssm-ID: 178695 [Multi-domain]  Cd Length: 623  Bit Score: 51.74  E-value: 1.83e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627668 194 IPSLREL---TLASNHIHKIESQAFGNTPSLHKLDLSHCDIQTISAQAFGGLQGLTLLRLNGNKLSELLPKTIETLSrLH 270
Cdd:PLN03150 438 ISKLRHLqsiNLSGNSIRGNIPPSLGSITSLEVLDLSYNSFNGSIPESLGQLTSLRILNLNGNSLSGRVPAALGGRL-LH 516

                         90
                 ....*....|...
gi 442627668 271 GIELH--DNPWLC 281
Cdd:PLN03150 517 RASFNftDNAGLC 529
Ig5_Contactin cd04969
Fifth immunoglobulin (Ig) domain of contactin; The members here are composed of the fifth ...
 333-429 1.85e-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: 46.68  E-value: 1.85e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627668 333 PISHYVEAAMGENASITCRARAVPAANINWYWNGRLLANNSaftayqRIHMLEQveggfekrSKLVLTNAQETDSSEFYC 412
Cdd:cd04969    7 PVKKKILAAKGGDVIIECKPKASPKPTISWSKGTELLTNSS------RICILPD--------GSLKIKNVTKSDEGKYTC 72

                         90
                 ....*....|....*..
gi 442627668 413 VAENRAGMAEANFTLHV 429
Cdd:cd04969   73 FAVNFFGKANSTGSLSV 89
IgI_Myotilin_C_like cd05744
Immunoglobulin (Ig)-like domain of myotilin, palladin, and myopalladin; member of the I-set of ...
 343-429 2.55e-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: 46.33  E-value: 2.55e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627668 343 GENASITCRARAVPAANINWYWNGRLLANNSAFTAYQRihmleqvEGGfekRSKLVLTNAQETDSSEFYCVAENRAGMAE 422
Cdd:cd05744   15 GRLCRFDCKVSGLPTPDLFWQLNGKPVRPDSAHKMLVR-------ENG---RHSLIIEPVTKRDAGIYTCIARNRAGENS 84


                 ....*..
gi 442627668 423 ANFTLHV 429
Cdd:cd05744   85 FNAELVV 91
PLN00113 PLN00113
leucine-rich repeat receptor-like protein kinase; Provisional
 126-277 3.08e-06

leucine-rich repeat receptor-like protein kinase; Provisional


Pssm-ID: 215061 [Multi-domain]  Cd Length: 968  Bit Score: 51.00  E-value: 3.08e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627668 126 LDMSGNKLQTLSNEQfiRANLLNLQKLYL-RNCKIGEIERetFKGLTNLVELDLSHNLLVTVPSLALGHIPSLRELTLAS 204
Cdd:PLN00113 433 LDISNNNLQGRINSR--KWDMPSLQMLSLaRNKFFGGLPD--SFGSKRLENLDLSRNQFSGAVPRKLGSLSELMQLKLSE 508

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 442627668 205 NHIHKIESQAFGNTPSLHKLDLSHCDIQTISAQAFGGLQGLTLLRLNGNKLSELLPKTIETLSRLHGIELHDN 277
Cdd:PLN00113 509 NKLSGEIPDELSSCKKLVSLDLSHNQLSGQIPASFSEMPVLSQLDLSQNQLSGEIPKNLGNVESLVQVNISHN 581
LRR_RI cd00116
Leucine-rich repeats (LRRs), ribonuclease inhibitor (RI)-like subfamily. LRRs are 20-29 ...
 110-257 4.12e-06

Leucine-rich repeats (LRRs), ribonuclease inhibitor (RI)-like subfamily. LRRs are 20-29 residue sequence motifs present in many proteins that participate in protein-protein interactions and have different functions and cellular locations. LRRs correspond to structural units consisting of a beta strand (LxxLxLxxN/CxL conserved pattern) and an alpha helix. This alignment contains 12 strands corresponding to 11 full repeats, consistent with the extent observed in the subfamily acting as Ran GTPase Activating Proteins (RanGAP1).


Pssm-ID: 238064 [Multi-domain]  Cd Length: 319  Bit Score: 49.66  E-value: 4.12e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627668 110 RHLIQIPEHIDPNTQVLDMSGNKLQTLSNEQFirANLL----NLQKLYLRNCKIGE--IER--ETFKGLTNLVELDLSHN 181
Cdd:cd00116  126 RLLAKGLKDLPPALEKLVLGRNRLEGASCEAL--AKALranrDLKELNLANNGIGDagIRAlaEGLKANCNLEVLDLNNN 203

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627668 182 LLVTVPSLALGHIP----SLRELTLASNHI-----HKIESQAFGNTPSLHKLDLSHCDIQTISAQAFGGLQG----LTLL 248
Cdd:cd00116  204 GLTDEGASALAETLaslkSLEVLNLGDNNLtdagaAALASALLSPNISLLTLSLSCNDITDDGAKDLAEVLAekesLLEL 283


                 ....*....
gi 442627668 249 RLNGNKLSE 257
Cdd:cd00116  284 DLRGNKFGE 292
PPP1R42 cd21340
protein phosphatase 1 regulatory subunit 42; Protein phosphatase 1 regulatory subunit 42 ...
 118-225 4.18e-06

protein phosphatase 1 regulatory subunit 42; Protein phosphatase 1 regulatory subunit 42 (PPP1R42), also known as leucine-rich repeat-containing protein 67 (lrrc67) or testis leucine-rich repeat (TLRR) protein, plays a role in centrosome separation. PPP1R42 has been shown to interact with the well-conserved signaling protein phosphatase-1 (PP1) and thereby increasing PP1's activity, which counters centrosome separation. Inhibition of PPP1R42 expression increases the number of centrosomes per cell while its depletion reduces the activity of PP1 leading to activation of NEK2, the kinase responsible for phosphorylation of centrosomal linker proteins promoting centrosome separation.


Pssm-ID: 411060 [Multi-domain]  Cd Length: 220  Bit Score: 48.63  E-value: 4.18e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627668 118 HID----PNTQVLDMSGNKLQTLSNeqfiranllNLQKLYLRNCKIGEIEreTFKGLTNLVELDLSHNLLVTVPSLA--L 191
Cdd:cd21340   96 HIEnqrlPPGEKLTFDPRSLAALSN---------SLRVLNISGNNIDSLE--PLAPLRNLEQLDASNNQISDLEELLdlL 164

                         90       100       110
                 ....*....|....*....|....*....|....*..
gi 442627668 192 GHIPSLRELTLASNHI---HKIESQAFGNTPSLHKLD 225
Cdd:cd21340  165 SSWPSLRELDLTGNPVckkPKYRDKIILASKSLEVLD 201
Ig4_L1-CAM_like cd05867
Fourth immunoglobulin (Ig)-like domain of the L1 cell adhesion molecule (CAM); The members ...
 343-429 4.46e-06

Fourth immunoglobulin (Ig)-like domain of the L1 cell adhesion molecule (CAM); The members here are composed of the fourth immunoglobulin (Ig)-like domain of the L1 cell adhesion molecule (CAM). L1 is comprised of an extracellular region having six Ig-like domains and five fibronectin type III domains, a transmembrane region, and an intracellular domain. L1 is primarily expressed in the nervous system and is involved in its development and function. L1 is associated with an X-linked recessive disorder, X-linked hydrocephalus, MASA syndrome, and spastic paraplegia type 1, that involves abnormalities of axonal growth. This group also contains the chicken neuron-glia cell adhesion molecule, Ng-CAM.


Pssm-ID: 409453 [Multi-domain]  Cd Length: 89  Bit Score: 45.66  E-value: 4.46e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627668 343 GENASITCRARAVPAANINWYWNGRLLAnnsAFTAYQRIHMleqveggfeKRSKLVLTNAQETDSSEFYCVAENRAGMAE 422
Cdd:cd05867   14 GETARLDCQVEGIPTPNITWSINGAPIE---GTDPDPRRHV---------SSGALILTDVQPSDTAVYQCEARNRHGNLL 81


                 ....*..
gi 442627668 423 ANFTLHV 429
Cdd:cd05867   82 ANAHVHV 88
IgI_3_NCAM-1 cd05730
Third immunoglobulin (Ig)-like domain of Neural Cell Adhesion Molecule 1 (NCAM-1); member of ...
 340-429 1.02e-05

Third immunoglobulin (Ig)-like domain of Neural Cell Adhesion Molecule 1 (NCAM-1); member of the I-set of IgSF domains; The members here are composed of the third 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.


Pssm-ID: 143207 [Multi-domain]  Cd Length: 95  Bit Score: 44.92  E-value: 1.02e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627668 340 AAMGENASITCRARAVPAANINWYWNGrllannsaftayqrihmlEQVEGGFEK------RSKLVLTNAQETDSSEFYCV 413
Cdd:cd05730   15 ANLGQSVTLACDADGFPEPTMTWTKDG------------------EPIESGEEKysfnedGSEMTILDVDKLDEAEYTCI 76

                         90
                 ....*....|....*.
gi 442627668 414 AENRAGMAEANFTLHV 429
Cdd:cd05730   77 AENKAGEQEAEIHLKV 92
LRR_4 pfam12799
Leucine Rich repeats (2 copies); Leucine rich repeats are short sequence motifs present in a ...
 148-185 1.14e-05

Leucine Rich repeats (2 copies); Leucine rich repeats are short sequence motifs present in a number of proteins with diverse functions and cellular locations. These repeats are usually involved in protein-protein interactions. Each Leucine Rich Repeat is composed of a beta-alpha unit. These units form elongated non-globular structures. Leucine Rich Repeats are often flanked by cysteine rich domains.


Pssm-ID: 463713 [Multi-domain]  Cd Length: 44  Bit Score: 43.00  E-value: 1.14e-05
                          10        20        30
                  ....*....|....*....|....*....|....*...
gi 442627668  148 NLQKLYLRNCKIGEIEreTFKGLTNLVELDLSHNLLVT 185
Cdd:pfam12799   2 NLEVLDLSNNQITDIP--PLAKLPNLETLDLSGNNKIT 37
Ig4_Contactin-2-like cd05728
Fourth Ig domain of the neural cell adhesion molecule contactin-2, and similar domains; The ...
 339-429 4.80e-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: 42.59  E-value: 4.80e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627668 339 EAAMGENASITCRARAVPAANINWYWNGRLLANNsaftayQRIhmleQVEGGFEKRSKLVLTnaqetDSSEFYCVAENRA 418
Cdd:cd05728   10 EADIGSSLRWECKASGNPRPAYRWLKNGQPLASE------NRI----EVEAGDLRITKLSLS-----DSGMYQCVAENKH 74

                         90
                 ....*....|.
gi 442627668 419 GMAEANFTLHV 429
Cdd:cd05728   75 GTIYASAELAV 85
RNA1 COG5238
Ran GTPase-activating protein (RanGAP) involved in mRNA processing and transport [Translation, ...
 109-277 5.77e-05

Ran GTPase-activating protein (RanGAP) involved in mRNA processing and transport [Translation, ribosomal structure and biogenesis];


Pssm-ID: 444072 [Multi-domain]  Cd Length: 434  Bit Score: 46.71  E-value: 5.77e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627668 109 DRHLIQIPEHIDPNTQV--LDMSGNKLqtlSNEQFIR-ANLL----NLQKLYLRNCKIGE--IER--ETFKGLTNLVELD 177
Cdd:COG5238  222 DEGAEILAEALKGNKSLttLDLSNNQI---GDEGVIAlAEALknntTVETLYLSGNQIGAegAIAlaKALQGNTTLTSLD 298

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627668 178 LSHNLL----VTVPSLALGHIPSLRELTLASNHIHKIESQAFGNT----PSLHKLDLSHCDIQTISAQAFG----GLQGL 245
Cdd:COG5238  299 LSVNRIgdegAIALAEGLQGNKTLHTLNLAYNGIGAQGAIALAKAlqenTTLHSLDLSDNQIGDEGAIALAkyleGNTTL 378

                        170       180       190
                 ....*....|....*....|....*....|....*.
gi 442627668 246 TLLRLNGNKLSEL----LPKTIETlSRLHGIELHDN 277
Cdd:COG5238  379 RELNLGKNNIGKQgaeaLIDALQT-NRLHTLILDGN 413
IgI_titin_I1-like cd20951
Immunoglobulin domain I1 of the titin I-band and similar proteins; a member of the I-set of ...
 329-429 9.81e-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: 42.02  E-value: 9.81e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627668 329 PEML--PISHYVEAamGENASITCRARAVPAANINWYWNGRLLANNSAFTAYQrihmleqveggFEKRS---KLVLTNAQ 403
Cdd:cd20951    1 PEFIirLQSHTVWE--KSDAKLRVEVQGKPDPEVKWYKNGVPIDPSSIPGKYK-----------IESEYgvhVLHIRRVT 67

                         90       100
                 ....*....|....*....|....*.
gi 442627668 404 ETDSSEFYCVAENRAGMAEANFTLHV 429
Cdd:cd20951   68 VEDSAVYSAVAKNIHGEASSSASVVV 93
IgI_1_MuSK cd20970
agrin-responsive first immunoglobulin-like domains (Ig1) of the MuSK ectodomain; a member of ...
 338-429 1.15e-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: 41.72  E-value: 1.15e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627668 338 VEAAMGENASITCRARAVPAANINWYWNGRLlannsaftayqrihmLEQVEGGFEKRSK---LVLTNAQETDSSEFYCVA 414
Cdd:cd20970   12 VTAREGENATFMCRAEGSPEPEISWTRNGNL---------------IIEFNTRYIVRENgttLTIRNIRRSDMGIYLCIA 76

                         90
                 ....*....|....*.
gi 442627668 415 ENRA-GMAEANFTLHV 429
Cdd:cd20970   77 SNGVpGSVEKRITLQV 92
LRR COG4886
Leucine-rich repeat (LRR) protein [Transcription];
121-274 1.92e-04

Leucine-rich repeat (LRR) protein [Transcription];


Pssm-ID: 443914 [Multi-domain]  Cd Length: 414  Bit Score: 44.92  E-value: 1.92e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627668 121 PNTQVLDMSGNKLQTLSNEqfirANLLNLQKLYLRNCKIGEIERETF---KGLTNLVELDLSHNLLVTVPSLALGHIPSL 197
Cdd:COG4886  250 TNLEELDLSNNQLTDLPPL----ANLTNLKTLDLSNNQLTDLKLKELellLGLNSLLLLLLLLNLLELLILLLLLTTLLL 325

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 442627668 198 RELTLASNHIHKIESQAFGNTPSLHKLDLSHCDIQTISAQAFGGLQGLTLLRLNGNKLSELLPKTIETLSRLHGIEL 274
Cdd:COG4886  326 LLLLLKGLLVTLTTLALSLSLLALLTLLLLLNLLSLLLTLLLTLGLLGLLEATLLTLALLLLTLLLLLLTTTAGVLL 402
IgI_SALM5_like cd05764
Immunoglobulin domain of human Synaptic Adhesion-Like Molecule 5 (SALM5) and similar proteins; ...
 335-429 2.03e-04

Immunoglobulin domain of human Synaptic Adhesion-Like Molecule 5 (SALM5) and similar proteins; member of the I-set of IgSF domains; This group contains the immunoglobulin domain of human Synaptic Adhesion-Like Molecule 5 (SALM5) and similar proteins. The SALM (for synaptic adhesion-like molecules; also known as Lrfn for leucine-rich repeat and fibronectin type III domain containing) family of adhesion molecules consists of five known members: SALM1/Lrfn2, SALM2/Lrfn1, SALM3/Lrfn4, SALM4/Lrfn3, and SALM5/Lrfn5. SALMs share a similar domain structure, containing leucine-rich repeats (LRRs), an immunoglobulin (Ig) domain, and a fibronectin III (FNIII) domain, followed by a transmembrane domain and a C-terminal PDZ-binding motif. SALM5 is implicated in autism spectrum disorders (ASDs) and schizophrenia, induces presynaptic differentiation in contacting axons. SALM5 interacts with the Ig domains of LAR (Leukocyte common Antigen-Related) family receptor protein tyrosine phosphatases (LAR-RPTPs; LAR, PTPdelta, and PTPsigma). In addition, PTPdelta is implicated in ASDs, ADHD, bipolar disorder, and restless leg syndrome. Studies have shown that LAR-RPTPs are novel and splicing-dependent presynaptic ligands for SALM5, and that they mediate SALM5-dependent presynaptic differentiation. Furthermore, SALM5 maintains AMPA receptor (AMPAR)-mediated excitatory synaptic transmission through mechanisms involving the interaction of SALM5 with LAR-RPTPs. This group belongs to the I-set of immunoglobulin superfamily (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: 409421 [Multi-domain]  Cd Length: 88  Bit Score: 40.92  E-value: 2.03e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627668 335 SHYVEAAMGENASITCRARAVPAANINWYW-NGRLLANNSAFTAYQrihmleqvEGGFEkrskLVLTNAQetDSSEFYCV 413
Cdd:cd05764    7 THELRVLEGQRATLRCKARGDPEPAIHWISpEGKLISNSSRTLVYD--------NGTLD----ILITTVK--DTGAFTCI 72

                         90
                 ....*....|....*.
gi 442627668 414 AENRAGMAEANFTLHV 429
Cdd:cd05764   73 ASNPAGEATARVELHI 88
IgC_1_Robo cd07693
First immunoglobulin (Ig)-like constant domain in Robo (roundabout) receptors, and similar ...
 343-430 6.80e-04

First immunoglobulin (Ig)-like constant domain in Robo (roundabout) receptors, and similar domains; The members here are composed of the first immunoglobulin (Ig)-like domain in Roundabout (Robo) 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, and Robo3), and three mammalian Slit homologs (Slit1, Slit2, Slit3), 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 Slit1, Slit2,and Slit3 are expressed at the ventral midline. Robo3 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.


Pssm-ID: 409490 [Multi-domain]  Cd Length: 99  Bit Score: 39.84  E-value: 6.80e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627668 343 GENASITCRARAVPAANINWYWNGRLLANNSAFTAYQRIhMLEQVEGGFekrSKLVLTNAQETDSSEFYCVAENRAGMA- 421
Cdd:cd07693   15 GDPATLNCKAEGRPTPTIQWLKNGQPLETDKDDPRSHRI-VLPSGSLFF---LRVVHGRKGRSDEGVYVCVAHNSLGEAv 90


                 ....*....
gi 442627668 422 EANFTLHVS 430
Cdd:cd07693   91 SRNASLEVA 99
IgI_Twitchin_like cd20949
C-terminal immunoglobulin-like domain of the myosin-associated giant protein kinase Twitchin, ...
 338-422 7.19e-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: 39.62  E-value: 7.19e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627668 338 VEAAMGENASITCRARAVPAANINWYWNGRLLANNSAFTAYQRIHmleqveggfekRSKLVLTNAQETDSSEFYCVAENR 417
Cdd:cd20949    9 TTVKEGQSATILCEVKGEPQPNVTWHFNGQPISASVADMSKYRIL-----------ADGLLINKVTQDDTGEYTCRAYQV 77


                 ....*
gi 442627668 418 AGMAE 422
Cdd:cd20949   78 NSIAS 82
IgI_LRIG1-like cd05763
Immunoglobulin (Ig)-like ectodomain of the LRIG1 (Leucine-rich Repeats And Immunoglobulin-like ...
 334-429 7.45e-04

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: 39.53  E-value: 7.45e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627668 334 ISHYVEAAMGENASITCRARAVPAANINWYWNGrllANNSAFTAYQRIHMLEQVEGGFekrsklvLTNAQETDSSEFYCV 413
Cdd:cd05763    5 TPHDITIRAGSTARLECAATGHPTPQIAWQKDG---GTDFPAARERRMHVMPEDDVFF-------IVDVKIEDTGVYSCT 74

                         90
                 ....*....|....*.
gi 442627668 414 AENRAGMAEANFTLHV 429
Cdd:cd05763   75 AQNSAGSISANATLTV 90
PPP1R42 cd21340
protein phosphatase 1 regulatory subunit 42; Protein phosphatase 1 regulatory subunit 42 ...
 152-275 1.10e-03

protein phosphatase 1 regulatory subunit 42; Protein phosphatase 1 regulatory subunit 42 (PPP1R42), also known as leucine-rich repeat-containing protein 67 (lrrc67) or testis leucine-rich repeat (TLRR) protein, plays a role in centrosome separation. PPP1R42 has been shown to interact with the well-conserved signaling protein phosphatase-1 (PP1) and thereby increasing PP1's activity, which counters centrosome separation. Inhibition of PPP1R42 expression increases the number of centrosomes per cell while its depletion reduces the activity of PP1 leading to activation of NEK2, the kinase responsible for phosphorylation of centrosomal linker proteins promoting centrosome separation.


Pssm-ID: 411060 [Multi-domain]  Cd Length: 220  Bit Score: 41.31  E-value: 1.10e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627668 152 LYLRNCKIGEIEretfkgltnlvELDLSHNLLVtvpslalghipslreLTLASNHIHKIESqaFGNTPSLHKLDLSHCDI 231
Cdd:cd21340    7 LYLNDKNITKID-----------NLSLCKNLKV---------------LYLYDNKITKIEN--LEFLTNLTHLYLQNNQI 58

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*
gi 442627668 232 QTIsaQAFGGLQGLTLLRLNGNKLSellpkTIETLSRLHGI-ELH 275
Cdd:cd21340   59 EKI--ENLENLVNLKKLYLGGNRIS-----VVEGLENLTNLeELH 96
LRR_4 pfam12799
Leucine Rich repeats (2 copies); Leucine rich repeats are short sequence motifs present in a ...
 195-236 1.12e-03

Leucine Rich repeats (2 copies); Leucine rich repeats are short sequence motifs present in a number of proteins with diverse functions and cellular locations. These repeats are usually involved in protein-protein interactions. Each Leucine Rich Repeat is composed of a beta-alpha unit. These units form elongated non-globular structures. Leucine Rich Repeats are often flanked by cysteine rich domains.


Pssm-ID: 463713 [Multi-domain]  Cd Length: 44  Bit Score: 37.61  E-value: 1.12e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|...
gi 442627668  195 PSLRELTLASNHIHKIEsqAFGNTPSLHKLDLSHCD-IQTISA 236
Cdd:pfam12799   1 PNLEVLDLSNNQITDIP--PLAKLPNLETLDLSGNNkITDLSD 41
RNA1 COG5238
Ran GTPase-activating protein (RanGAP) involved in mRNA processing and transport [Translation, ...
 109-231 1.28e-03

Ran GTPase-activating protein (RanGAP) involved in mRNA processing and transport [Translation, ribosomal structure and biogenesis];


Pssm-ID: 444072 [Multi-domain]  Cd Length: 434  Bit Score: 42.08  E-value: 1.28e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627668 109 DRHLIQIPEHIDPNTQV--LDMSGNKL---------QTLSNEQFIRANLLN---------------------LQKLYLRN 156
Cdd:COG5238  250 DEGVIALAEALKNNTTVetLYLSGNQIgaegaialaKALQGNTTLTSLDLSvnrigdegaialaeglqgnktLHTLNLAY 329

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627668 157 CKIGEIER----ETFKGLTNLVELDLSHNLLVTVPSLALGHI----PSLRELTLASNHIHKIESQAFG---NTPSLHKLD 225
Cdd:COG5238  330 NGIGAQGAialaKALQENTTLHSLDLSDNQIGDEGAIALAKYlegnTTLRELNLGKNNIGKQGAEALIdalQTNRLHTLI 409


                 ....*.
gi 442627668 226 LSHCDI 231
Cdd:COG5238  410 LDGNLI 415
Ig_Perlecan_like cd05743
Immunoglobulin (Ig)-like domain of the human basement membrane heparan sulfate proteoglycan ...
 343-424 1.40e-03

Immunoglobulin (Ig)-like domain of the human basement membrane heparan sulfate proteoglycan perlecan and similar proteins; The members here are composed of the immunoglobulin (Ig)-like domain of the human basement membrane heparan sulfate proteoglycan perlecan, also known as HSPG2, and similar proteins. Perlecan consists of five domains: domain I has three putative heparan sulfate attachment sites, domain II has four LDL receptor-like repeats, and one Ig-like repeat, domain III resembles the short arm of laminin chains, domain IV has multiple Ig-like repeats (21 repeats in human perlecan), and domain V resembles the globular G domain of the laminin A chain and internal repeats of EGF. Perlecan may participate in a variety of biological functions including cell binding, LDL-metabolism, basement membrane assembly and selective permeability, calcium binding, and growth- and neurite-promoting activities.


Pssm-ID: 143220  Cd Length: 78  Bit Score: 38.24  E-value: 1.40e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627668 343 GENASITCRARAVPAANINWywngRLlaNNSAFTAYQRIHMLEqvEGGfekRSKLVLTNAQETDSSEFYCVAENRAGMAE 422
Cdd:cd05743    1 GETVEFTCVATGVPTPIINW----RL--NWGHVPDSARVSITS--EGG---YGTLTIRDVKESDQGAYTCEAINTRGMVF 69


                 ..
gi 442627668 423 AN 424
Cdd:cd05743   70 GI 71
PLN00113 PLN00113
leucine-rich repeat receptor-like protein kinase; Provisional
 114-277 1.43e-03

leucine-rich repeat receptor-like protein kinase; Provisional


Pssm-ID: 215061 [Multi-domain]  Cd Length: 968  Bit Score: 42.53  E-value: 1.43e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627668 114 QIPEHID--PNTQVLDMSGNKLQ----------------TLSNEQFI------RANLLNLQKLYL-RNCKIGEIEREtFK 168
Cdd:PLN00113 155 EIPNDIGsfSSLKVLDLGGNVLVgkipnsltnltsleflTLASNQLVgqipreLGQMKSLKWIYLgYNNLSGEIPYE-IG 233

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627668 169 GLTNLVELDLSHNLLV-TVPSlALGHIPSLRELTLASNHIH-KIESQAFGNTpSLHKLDLSHCDIQTISAQAFGGLQGLT 246
Cdd:PLN00113 234 GLTSLNHLDLVYNNLTgPIPS-SLGNLKNLQYLFLYQNKLSgPIPPSIFSLQ-KLISLDLSDNSLSGEIPELVIQLQNLE 311

                        170       180       190
                 ....*....|....*....|....*....|.
gi 442627668 247 LLRLNGNKLSELLPKTIETLSRLHGIELHDN 277
Cdd:PLN00113 312 ILHLFSNNFTGKIPVALTSLPRLQVLQLWSN 342
LRR_5 pfam13306
BspA type Leucine rich repeat region (6 copies); This family includes a number of leucine rich ...
 148-267 1.63e-03

BspA type Leucine rich repeat region (6 copies); This family includes a number of leucine rich repeats. This family contains a large number of BSPA-like surface antigens from Trichomonas vaginalis.


Pssm-ID: 463839 [Multi-domain]  Cd Length: 127  Bit Score: 39.45  E-value: 1.63e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627668  148 NLQKLYLRNcKIGEIERETFKGLTNLVELDLSHNlLVTVPSLALGHIpSLRELTLASNhIHKIESQAFGNTPSLHKLDLS 227
Cdd:pfam13306  12 SLTSITIPS-SLTSIGEYAFSNCTSLKSITLPSS-LTSIGSYAFYNC-SLTSITIPSS-LTSIGEYAFSNCSNLKSITLP 87

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 442627668  228 HcDIQTISAQAFgglqgltllrlNGNKLSEL-LPKTIETLS 267
Cdd:pfam13306  88 S-NLTSIGSYAF-----------SNCSLKSItIPSSVTTIG 116
IgI_4_MYLK-like cd20976
Fourth Ig-like domain from smooth muscle myosin light chain kinase and similar domains ; a ...
 329-429 1.77e-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: 38.39  E-value: 1.77e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627668 329 PEMLPISHYVEAAMGENASITCRARAVPAANINWYWNGRLLANNSAFTayqrihmleQVEGGFekrSKLVLTNAQETDSS 408
Cdd:cd20976    2 PSFSSVPKDLEAVEGQDFVAQCSARGKPVPRITWIRNAQPLQYAADRS---------TCEAGV---GELHIQDVLPEDHG 69

                         90       100
                 ....*....|....*....|.
gi 442627668 409 EFYCVAENRAGMAEANFTLHV 429
Cdd:cd20976   70 TYTCLAKNAAGQVSCSAWVTV 90
LRR_4 pfam12799
Leucine Rich repeats (2 copies); Leucine rich repeats are short sequence motifs present in a ...
 171-211 2.04e-03

Leucine Rich repeats (2 copies); Leucine rich repeats are short sequence motifs present in a number of proteins with diverse functions and cellular locations. These repeats are usually involved in protein-protein interactions. Each Leucine Rich Repeat is composed of a beta-alpha unit. These units form elongated non-globular structures. Leucine Rich Repeats are often flanked by cysteine rich domains.


Pssm-ID: 463713 [Multi-domain]  Cd Length: 44  Bit Score: 36.84  E-value: 2.04e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|..
gi 442627668  171 TNLVELDLSHNLLVTVPSLAlgHIPSLRELTLASN-HIHKIE 211
Cdd:pfam12799   1 PNLEVLDLSNNQITDIPPLA--KLPNLETLDLSGNnKITDLS 40
IgI_Myotilin_C cd05892
C-terminal immunoglobulin (Ig)-like domain of myotilin; member of the I-set of Ig superfamily ...
 340-429 2.22e-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: 38.21  E-value: 2.22e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627668 340 AAMGENASITCRARAVPAANINWYWNGRLLANNSaftayQRIHMLEQVEGgfekRSKLVLTNAQETDSSEFYCVAENRAG 419
Cdd:cd05892   12 VLEGDPVRLECQISAIPPPQIFWKKNNEMLQYNT-----DRISLYQDNCG----RICLLIQNANKKDAGWYTVSAVNEAG 82

                         90
                 ....*....|
gi 442627668 420 MAEANFTLHV 429
Cdd:cd05892   83 VVSCNARLDV 92
IgI_1_Contactin-2 cd05850
First immunoglobulin (Ig) domain of contactin-2; member of the I-set of Ig superfamily domains; ...
 337-419 3.49e-03

First immunoglobulin (Ig) domain of contactin-2; member of the I-set of Ig superfamily domains; The members here are composed of the first immunoglobulin (Ig) domain of the neural cell adhesion molecule contactin-2-like. Contactins are comprised of six Ig domains followed by four fibronectin type III (FnIII) domains anchored to the membrane by glycosylphosphatidylinositol. Contactin-2 (TAG-1, axonin-1) facilitates cell adhesion by homophilic binding between molecules in apposed membranes. It may play a part in the neuronal processes of neurite outgrowth, axon guidance and fasciculation, and neuronal migration. 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. 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-2 is also expressed in retinal amacrine cells in the developing chick retina, corresponding to the period of formation and maturation of AC processes. This group belongs to the I-set of IgSF domains.


Pssm-ID: 409437 [Multi-domain]  Cd Length: 97  Bit Score: 37.60  E-value: 3.49e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627668 337 YVEAAMGENASITCRARAVPAANINWYWNGRLL--ANNSAFTayqrihmleQVEGgfekrsKLVLTNAQET-DSSEFYCV 413
Cdd:cd05850   14 FPEGSAEEKVTLACRARASPPATYRWKMNGTELkmEPDSRYR---------LVAG------NLVISNPVKAkDAGSYQCL 78


                 ....*.
gi 442627668 414 AENRAG 419
Cdd:cd05850   79 ASNRRG 84
ig pfam00047
Immunoglobulin domain; Members of the immunoglobulin superfamily are found in hundreds of ...
 333-427 4.82e-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: 37.17  E-value: 4.82e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627668  333 PISHYVEAAMGENASITCRAR-AVPAANINWYWNGrllannsaftayQRIHMLEQVEGGFEKRSKLVLT--NAQETDSSE 409
Cdd:pfam00047   1 SAPPTVTVLEGDSATLTCSAStGSPGPDVTWSKEG------------GTLIESLKVKHDNGRTTQSSLLisNVTKEDAGT 68

                          90
                  ....*....|....*...
gi 442627668  410 FYCVAENRAGMAEANFTL 427
Cdd:pfam00047  69 YTCVVNNPGGSATLSTSL 86
Ig6_Contactin cd04970
Sixth immunoglobulin (Ig) domain of contactin; The members here are composed of the sixth ...
 333-429 5.14e-03

Sixth immunoglobulin (Ig) domain of contactin; The members here are composed of the sixth 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: 409359  Cd Length: 102  Bit Score: 37.53  E-value: 5.14e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627668 333 PISHYVEaaMGENASITCRARAVPAANINWYW--NGRLLANNSAFTAYQRIHMLEQVeggfekrSKLVLTNAQETDSSEF 410
Cdd:cd04970    9 PSNADIT--VGENATLQCHASHDPTLDLTFTWsfNGVPIDLEKIEGHYRRRYGKDSN-------GDLEIVNAQLKHAGRY 79

                         90
                 ....*....|....*....
gi 442627668 411 YCVAENRAGMAEANFTLHV 429
Cdd:cd04970   80 TCTAQTVVDSDSASATLVV 98
 
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.
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