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Conserved domains on  [gi|1159648420|gb|OPJ77732|]
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kinesin-like protein KIF21A isoform F [Patagioenas fasciata monilis]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
GH31_MGAM_SI_GAA cd06602
maltase-glucoamylase, sucrase-isomaltase, lysosomal acid alpha-glucosidase; This subgroup ...
 1936-2296 0e+00

maltase-glucoamylase, sucrase-isomaltase, lysosomal acid alpha-glucosidase; This subgroup includes the following three closely related glycosyl hydrolase family 31 (GH31) enzymes: maltase-glucoamylase (MGAM), sucrase-isomaltase (SI), and lysosomal acid alpha-glucosidase (GAA), also known as acid-maltase. MGAM is one of the two enzymes responsible for catalyzing the last glucose-releasing step in starch digestion. SI is implicated in the digestion of dietary starch and major disaccharides such as sucrose and isomaltose, while GAA degrades glycogen in the lysosome, cleaving both alpha-1,4 and alpha-1,6 glucosidic linkages. MGAM and SI are anchored to small-intestinal brush-border epithelial cells. The absence of SI from the brush border membrane or its malfunction is associated with malabsorption disorders such as congenital sucrase-isomaltase deficiency (CSID). The domain architectures of MGAM and SI include two tandem GH31 catalytic domains, an N-terminal domain found near the membrane-bound end, and a C-terminal luminal domain. Both of the tandem GH31 domains of MGAM and SI are included in this family. The domain architecture of GAA includes an N-terminal TFF (trefoil factor family) domain in addition to the GH31 catalytic domain. Deficient GAA expression causes Pompe disease, an autosomal recessive genetic disorder also known as glycogen storage disease type II (GSDII).


:

Pssm-ID: 269888  Cd Length: 367  Bit Score: 655.74  E-value: 0e+00
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159648420 1936 GRPHMPAYWSLGFHLSRWGYGSIDVLKETVNRMHYYDIPYDVQHLDIDYMERYMDFTYDKVNYAGLPEYIQKLKRKGMHN 2015
Cdd:cd06602      1 GRPAMPPYWSLGFHLCRWGYKNLDELKEVVERYRAAGIPLDVQWNDIDYMDRYRDFTLDPVNFPGLPAFVDDLHANGQHY 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159648420 2016 VVILDPFITKdEEPGTYRPYDLGEEMGVWVNNSDGvTPAVGKAWPpGDSVFPDYTNPRTAEWWTQMCLEFKDVLDYDGIW 2095
Cdd:cd06602     81 VPILDPGISA-NESGGYPPYDRGLEMDVFIKNDDG-SPYVGKVWP-GYTVFPDFTNPNTQEWWTEEIKDFHDQVPFDGLW 157

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159648420 2096 IDMNEPSNFLTG------QYPGCAVNDLNNPPYVPSIS-DHSLAQKTLCPDSKTYLGE-HYNTHSLFGWSQTAPTFHAAQ 2167
Cdd:cd06602    158 IDMNEPSNFCTGscgnspNAPGCPDNKLNNPPYVPNNLgGGSLSDKTICMDAVHYDGGlHYDVHNLYGLSEAIATYKALK 237

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159648420 2168 QA-TGKRAFVLSRSTFVGSGKHGGHWLGDNFSQWKDMHRSIVGILEFNLFGIPYIGADICGFNHNTTYELCLRWMQLGSF 2246
Cdd:cd06602    238 EIfPGKRPFIISRSTFPGSGKYAGHWLGDNYSTWEDMRYSIPGMLEFNLFGIPMVGADICGFNGNTTEELCARWMQLGAF 317

                          330       340       350       360       370
                   ....*....|....*....|....*....|....*....|....*....|
gi 1159648420 2247 YPFSRNHNAEGNREQDPAVFGAEFAEISRATLRIRYSLLPYLYTLFYESH 2296
Cdd:cd06602    318 YPFSRNHNDIGAIDQEPYVWGPSVADASRKALLIRYSLLPYLYTLFYRAH 367
KISc_KIF4 cd01372
Kinesin motor domain, KIF4-like subfamily; Kinesin motor domain, KIF4-like subfamily. Members ...
 8-372 0e+00

Kinesin motor domain, KIF4-like subfamily; Kinesin motor domain, KIF4-like subfamily. Members of this group seem to perform a variety of functions, and have been implicated in neuronal organelle transport and chromosome segregation during mitosis. This catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Kinesins are microtubule-dependent molecular motors that play important roles in intracellular transport and in cell division. In most kinesins, the motor domain is found at the N-terminus (N-type). N-type kinesins are (+) end-directed motors, i.e. they transport cargo towards the (+) end of the microtubule. Kinesin motor domains hydrolyze ATP at a rate of about 80 per second, and move along the microtubule at a speed of about 6400 Angstroms per second. To achieve that, kinesin head groups work in pairs. Upon replacing ADP with ATP, a kinesin motor domain increases its affinity for microtubule binding and locks in place. Also, the neck linker binds to the motor domain, which repositions the other head domain through the coiled-coil domain close to a second tubulin dimer, about 80 Angstroms along the microtubule. Meanwhile, ATP hydrolysis takes place, and when the second head domain binds to the microtubule, the first domain again replaces ADP with ATP, triggering a conformational change that pulls the first domain forward.


:

Pssm-ID: 276823 [Multi-domain]  Cd Length: 341  Bit Score: 631.29  E-value: 0e+00
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159648420    8 SSVRVAVRIRPQLAKEKIEGCHICTSVTPGEPQVFLGKDKAFTFDYVFNIDSQQEEIYVQCIEKLIEGCFEGYNATVFAY 87
Cdd:cd01372      1 SSVRVAVRVRPLLPKEIIEGCRICVSFVPGEPQVTVGTDKSFTFDYVFDPSTEQEEVYNTCVAPLVDGLFEGYNATVLAY 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159648420   88 GQTGAGKTYTMGTGFDVNITEEEQGIISRAVKHLFRCIEEKKQAaikqglppPDFKVNAQFLELYNEEILDLFDTTRDid 167
Cdd:cd01372     81 GQTGSGKTYTMGTAYTAEEDEEQVGIIPRAIQHIFKKIEKKKDT--------FEFQLKVSFLEIYNEEIRDLLDPETD-- 150

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159648420  168 aknKKSNIKIHEDSAGGIYTVGVTTRTVNGESEMMQCLKLGALSRTTASTQMNVQSSRSHAIFTIHLCQTRVCPPfntdn 247
Cdd:cd01372    151 ---KKPTISIREDSKGGITIVGLTEVTVLSAEDMMSCLEQGSLSRTTASTAMNSQSSRSHAIFTITLEQTKKNGP----- 222

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159648420  248 atdnriISESSEMNEFETLTAKFHFVDLAGSERLKRTGATGERAKEGISINCGLLALGNVISALGDKSKKATHVPYRDSK 327
Cdd:cd01372    223 ------IAPMSADDKNSTFTSKFHFVDLAGSERLKRTGATGDRLKEGISINSGLLALGNVISALGDESKKGAHVPYRDSK 296

                          330       340       350       360
                   ....*....|....*....|....*....|....*....|....*
gi 1159648420  328 LTRLLQDSLGGNSQTLMIACVSPSDRDFMETLNTLKYANRARNIK 372
Cdd:cd01372    297 LTRLLQDSLGGNSHTLMIACVSPADSNFEETLNTLKYANRARNIK 341
WD40 cd00200
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ...
 1316-1629 1.13e-60

WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions including adaptor/regulatory modules in signal transduction, pre-mRNA processing and cytoskeleton assembly; typically contains a GH dipeptide 11-24 residues from its N-terminus and the WD dipeptide at its C-terminus and is 40 residues long, hence the name WD40; between GH and WD lies a conserved core; serves as a stable propeller-like platform to which proteins can bind either stably or reversibly; forms a propeller-like structure with several blades where each blade is composed of a four-stranded anti-parallel b-sheet; instances with few detectable copies are hypothesized to form larger structures by dimerization; each WD40 sequence repeat forms the first three strands of one blade and the last strand in the next blade; the last C-terminal WD40 repeat completes the blade structure of the first WD40 repeat to create the closed ring propeller-structure; residues on the top and bottom surface of the propeller are proposed to coordinate interactions with other proteins and/or small ligands; 7 copies of the repeat are present in this alignment.


:

Pssm-ID: 238121 [Multi-domain]  Cd Length: 289  Bit Score: 210.65  E-value: 1.13e-60
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159648420 1316 CIYTAEGHTKAVLCVDATDD--LLFTGSKDRTCKVWNLVTGQEIMSLGGHPNNVVSIKYCNYTSLVFTVST-SYIKVWDI 1392
Cdd:cd00200      1 LRRTLKGHTGGVTCVAFSPDgkLLATGSGDGTIKVWDLETGELLRTLKGHTGPVRDVAASADGTYLASGSSdKTIRLWDL 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159648420 1393 RDSaKCIRTLTSSgqampgdvcsastnrtvaipagENQINQIALNPTGTFLYAAAG-NSVRMWDLKRFQSTGKLTGHQGP 1471
Cdd:cd00200     81 ETG-ECVRTLTGH----------------------TSYVSSVAFSPDGRILSSSSRdKTIKVWDVETGKCLTTLRGHTDW 137

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159648420 1472 VMCLTVDRisnGQDLIVTGSKDHYIKMFDVTEGalgsvSPTHNFEpPHYDGIEALAIMGDN--LFSGSRDNGIKKWDLAQ 1549
Cdd:cd00200    138 VNSVAFSP---DGTFVASSSQDGTIKLWDLRTG-----KCVATLT-GHTGEVNSVAFSPDGekLLSSSSDGTIKLWDLST 208

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159648420 1550 KDLLQQVPnAHKDWVCALGLVPGAPVLLSGCRGGNIKLWNVETFAPIGEMKGHDSPINAIC--TNSSQIFTAADDRTVRI 1627
Cdd:cd00200    209 GKCLGTLR-GHENGVNSVAFSPDGYLLASGSEDGTIRVWDLRTGECVQTLSGHTNSVTSLAwsPDGKRLASGSADGTIRI 287


                   ..
gi 1159648420 1628 WK 1629
Cdd:cd00200    288 WD 289
Rcc_KIF21A cd22263
regulatory coiled-coil domain found in kinesin-like protein KIF21A; KIF21A, also called ...
 920-1003 1.46e-47

regulatory coiled-coil domain found in kinesin-like protein KIF21A; KIF21A, also called kinesin-like protein KIF2 or renal carcinoma antigen NY-REN-62, is a microtubule-binding motor protein involved in neuronal axonal transport. It works as a microtubule stabilizer that regulates axonal morphology, suppressing cortical microtubule dynamics in neurons. Mutations in KIF21A cause congenital fibrosis of the extraocular muscles type 1 (CFEOM1). In vitro, it has a plus-end directed motor activity. This model corresponds to the regulatory coiled-coil domain of KIF21A, which folds into an intramolecular antiparallel coiled-coil monomer in solution, but crystallizes into a dimeric domain-swapped antiparallel coiled-coil.


:

Pssm-ID: 410204 [Multi-domain]  Cd Length: 82  Bit Score: 165.10  E-value: 1.46e-47
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159648420  920 QRMTISNMEADMNRLLTQREELTKRREKLSKRREKLMKDGGgsETDRNVQNINEEMESLTANIDYINDSISDCQANIMQM 999
Cdd:cd22263      1 QRMTISNMEADMNRLLKQREELTKRREKLSKKREKIIKENG--EGDKNVHNINEEMESLTANIDYINDSISDCQANIMQM 78


                   ....
gi 1159648420 1000 EEAK 1003
Cdd:cd22263     79 EEAK 82
NtCtMGAM_N pfam16863
N-terminal barrel of NtMGAM and CtMGAM, maltase-glucoamylase; NtCtMGAM_N is a beta-barrel-like ...
 1722-1830 2.97e-37

N-terminal barrel of NtMGAM and CtMGAM, maltase-glucoamylase; NtCtMGAM_N is a beta-barrel-like structure just N-terminal to the catalytic domain of maltase-glucoamylase in eukaryotes. It contributes to the architecture of the substrate-binding site, by donating a loop that comes into close contact with two regions in the catalytic domain thereby creating the site. This family is frequently found at the N-terminus of Glycosyl hydrolase 31, pfam01055.to which it contributes as above.


:

Pssm-ID: 465286  Cd Length: 113  Bit Score: 136.84  E-value: 2.97e-37
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159648420 1722 GWRVTLNKRQAL-SLFGNDISPIVLEVEFQTRDRLRFKLYDPNSQRFEVP---LQIDSPGVAADEANYDVELVEGSSHFR 1797
Cdd:pfam16863    1 GLTADLTLAGSPcNLYGNDIETLKLTVEYQTDNRLHVKITDPNNKRYEVPeelLPRPSPSSSASDSLYEFEYTNEPFGFK 80

                           90       100       110
                   ....*....|....*....|....*....|...
gi 1159648420 1798 IKRKSTGTVLWDSPLVDLFFSNQYLQITTTVPS 1830
Cdd:pfam16863   81 VTRKSTGEVLFDTSGGPLVFEDQFLQLSTRLPS 113
GH31_N cd14752
N-terminal domain of glycosyl hydrolase family 31 (GH31); This family is found N-terminal to ...
 1829-1936 1.12e-25

N-terminal domain of glycosyl hydrolase family 31 (GH31); This family is found N-terminal to the glycosyl-hydrolase domain of Glycoside hydrolase family 31 (GH31). GH31 includes the glycoside hydrolases alpha-glucosidase (EC 3.2.1.20), alpha-1,3-glucosidase (EC 3.2.1.84), alpha-xylosidase (EC 3.2.1.177), sucrase-isomaltase (EC 3.2.1.48 and EC 3.2.1.10), as well as alpha-glucan lyase (EC 4.2.2.13). All GH31 enzymes cleave a terminal carbohydrate moiety from a substrate that varies considerably in size, depending on the enzyme, and may be either a starch or a glycoprotein. In most cases, the pyranose moiety recognized in subsite-1 of the substrate binding site is an alpha-D-glucose, though some GH31 family members show a preference for alpha-D-xylose. Several GH31 enzymes can accommodate both glucose and xylose and different levels of discrimination between the two have been observed. Most characterized GH31 enzymes are alpha-glucosidases. In mammals, GH31 members with alpha-glucosidase activity are implicated in at least three distinct biological processes. The lysosomal acid alpha-glucosidase (GAA) is essential for glycogen degradation and a deficiency or malfunction of this enzyme causes glycogen storage disease II, also known as Pompe disease. In the endoplasmic reticulum, alpha-glucosidase II catalyzes the second step in the N-linked oligosaccharide processing pathway that constitutes part of the quality control system for glycoprotein folding and maturation. The intestinal enzymes sucrase-isomaltase (SI) and maltase-glucoamylase (MGAM) play key roles in the final stage of carbohydrate digestion, making alpha-glucosidase inhibitors useful in the treatment of type 2 diabetes. GH31 alpha-glycosidases are retaining enzymes that cleave their substrates via an acid/base-catalyzed, double-displacement mechanism involving a covalent glycosyl-enzyme intermediate. Two aspartic acid residues of the catalytic domain have been identified as the catalytic nucleophile and the acid/base, respectively. A loop of the N-terminal beta-sandwich domain is part of the active site pocket.


:

Pssm-ID: 270212 [Multi-domain]  Cd Length: 122  Bit Score: 103.80  E-value: 1.12e-25
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159648420 1829 PSTSVYGFGEQEHESFKHSMdfvTYGMFSRDQAPTPLV--NLYGVHPFYMCveadSNAHGVLLLNSNAQDVSLSPD--PS 1904
Cdd:cd14752     18 PDEHFYGLGERFGGLNKRGK---RYRLWNTDQGGYRGStdPLYGSIPFYLS----SKGYGVFLDNPSRTEFDFGSEdsDE 90

                           90       100       110
                   ....*....|....*....|....*....|..
gi 1159648420 1905 VTFRTIGGILDFYVFLGPTPENVVQQYTEAIG 1936
Cdd:cd14752     91 LTFSSEGGDLDYYFFAGPTPKEVIEQYTELTG 122
SCP-1 super family cl30946
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ...
 389-1024 2.96e-16

Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major component of the transverse filaments of the synaptonemal complex. Synaptonemal complexes are structures that are formed between homologous chromosomes during meiotic prophase.


The actual alignment was detected with superfamily member pfam05483:

Pssm-ID: 114219 [Multi-domain]  Cd Length: 787  Bit Score: 85.54  E-value: 2.96e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159648420  389 LRSEIARLQMELMEYKTGKRI--IDEEGVESINDMFHENAMLQTENNNLRVRIKAMQETVDALRaritqlmsDQANQVLA 466
Cdd:pfam05483  204 VQAENARLEMHFKLKEDHEKIqhLEEEYKKEINDKEKQVSLLLIQITEKENKMKDLTFLLEESR--------DKANQLEE 275

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159648420  467 RAGEGNEEISNMI---HNYIKEIEDLRAKLLESEAVNENLRRNLSRAsTRSTYfggpsafsasMLSSEKET-LEILDIAK 542
Cdd:pfam05483  276 KTKLQDENLKELIekkDHLTKELEDIKMSLQRSMSTQKALEEDLQIA-TKTIC----------QLTEEKEAqMEELNKAK 344

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159648420  543 KDLEKLKKKERKKKKSVkedntdnEQEKRDEKGSSERENNELE--AEEIQEASDREDEEEEDdededdmevvessdesds 620
Cdd:pfam05483  345 AAHSFVVTEFEATTCSL-------EELLRTEQQRLEKNEDQLKiiTMELQKKSSELEEMTKF------------------ 399

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159648420  621 dsdeKENYQADLANITCEIAIKQKLIDELENSQRRLQTLKRQYEEKLMMLQHKIRDTQLERDQVLQNLGSVETYSEEkAK 700
Cdd:pfam05483  400 ----KNNKEVELEELKKILAEDEKLLDEKKQFEKIAEELKGKEQELIFLLQAREKEIHDLEIQLTAIKTSEEHYLKE-VE 474

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159648420  701 KIKSEYEKKlQTMNKEL-QRLQTAQKEHARLLKNQSQYEKQLKKLQQEVTEMKKTKVRLMKQMKEEQEkarmTESRRNRE 779
Cdd:pfam05483  475 DLKTELEKE-KLKNIELtAHCDKLLLENKELTQEASDMTLELKKHQEDIINCKKQEERMLKQIENLEE----KEMNLRDE 549

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159648420  780 IAQLKKE--QRKREHQLKL--LEAQKRNQEVILRRKTEEVTALRRQVRPLSDKVAGKVS--RKLSLPEHPIQEPSSSSSV 853
Cdd:pfam05483  550 LESVREEfiQKGDEVKCKLdkSEENARSIEYEVLKKEKQMKILENKCNNLKKQIENKNKniEELHQENKALKKKGSAENK 629

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159648420  854 EHDGSRIAAqQKMRIPVARVQALSVTATNGTGRKYQRKAVTSRVYSSRAARMKWQLLE----RRVTDIIMQRmTISNMEA 929
Cdd:pfam05483  630 QLNAYEIKV-NKLELELASAKQKFEEIIDNYQKEIEDKKISEEKLLEEVEKAKAIADEavklQKEIDKRCQH-KIAEMVA 707

                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159648420  930 DMNRLLTQREELTKRREK---LSKRREKLMKDGGGS-ETDrnVQNINEEMESLTAnidyindsisdcqanimQMEEAKEE 1005
Cdd:pfam05483  708 LMEKHKHQYDKIIEERDSelgLYKNKEQEQSSAKAAlEIE--LSNIKAELLSLKK-----------------QLEIEKEE 768

                          650
                   ....*....|....*....
gi 1159648420 1006 GETLDVTAVINACTLTEAR 1024
Cdd:pfam05483  769 KEKLKMEAKENTAILKDKK 787
Trefoil pfam00088
Trefoil (P-type) domain;
1664-1703 2.54e-11

Trefoil (P-type) domain;


:

Pssm-ID: 459666  Cd Length: 43  Bit Score: 60.41  E-value: 2.54e-11
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|
gi 1159648420 1664 AVQKRIDCHPqPGASQEACEAQGCTWCATDVANAPWCFFS 1703
Cdd:pfam00088    5 PPSDRFDCGY-PGITQEECEARGCCWDPSVDPGVPWCFYP 43
 
Name Accession Description Interval E-value
GH31_MGAM_SI_GAA cd06602
maltase-glucoamylase, sucrase-isomaltase, lysosomal acid alpha-glucosidase; This subgroup ...
 1936-2296 0e+00

maltase-glucoamylase, sucrase-isomaltase, lysosomal acid alpha-glucosidase; This subgroup includes the following three closely related glycosyl hydrolase family 31 (GH31) enzymes: maltase-glucoamylase (MGAM), sucrase-isomaltase (SI), and lysosomal acid alpha-glucosidase (GAA), also known as acid-maltase. MGAM is one of the two enzymes responsible for catalyzing the last glucose-releasing step in starch digestion. SI is implicated in the digestion of dietary starch and major disaccharides such as sucrose and isomaltose, while GAA degrades glycogen in the lysosome, cleaving both alpha-1,4 and alpha-1,6 glucosidic linkages. MGAM and SI are anchored to small-intestinal brush-border epithelial cells. The absence of SI from the brush border membrane or its malfunction is associated with malabsorption disorders such as congenital sucrase-isomaltase deficiency (CSID). The domain architectures of MGAM and SI include two tandem GH31 catalytic domains, an N-terminal domain found near the membrane-bound end, and a C-terminal luminal domain. Both of the tandem GH31 domains of MGAM and SI are included in this family. The domain architecture of GAA includes an N-terminal TFF (trefoil factor family) domain in addition to the GH31 catalytic domain. Deficient GAA expression causes Pompe disease, an autosomal recessive genetic disorder also known as glycogen storage disease type II (GSDII).


Pssm-ID: 269888  Cd Length: 367  Bit Score: 655.74  E-value: 0e+00
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159648420 1936 GRPHMPAYWSLGFHLSRWGYGSIDVLKETVNRMHYYDIPYDVQHLDIDYMERYMDFTYDKVNYAGLPEYIQKLKRKGMHN 2015
Cdd:cd06602      1 GRPAMPPYWSLGFHLCRWGYKNLDELKEVVERYRAAGIPLDVQWNDIDYMDRYRDFTLDPVNFPGLPAFVDDLHANGQHY 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159648420 2016 VVILDPFITKdEEPGTYRPYDLGEEMGVWVNNSDGvTPAVGKAWPpGDSVFPDYTNPRTAEWWTQMCLEFKDVLDYDGIW 2095
Cdd:cd06602     81 VPILDPGISA-NESGGYPPYDRGLEMDVFIKNDDG-SPYVGKVWP-GYTVFPDFTNPNTQEWWTEEIKDFHDQVPFDGLW 157

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159648420 2096 IDMNEPSNFLTG------QYPGCAVNDLNNPPYVPSIS-DHSLAQKTLCPDSKTYLGE-HYNTHSLFGWSQTAPTFHAAQ 2167
Cdd:cd06602    158 IDMNEPSNFCTGscgnspNAPGCPDNKLNNPPYVPNNLgGGSLSDKTICMDAVHYDGGlHYDVHNLYGLSEAIATYKALK 237

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159648420 2168 QA-TGKRAFVLSRSTFVGSGKHGGHWLGDNFSQWKDMHRSIVGILEFNLFGIPYIGADICGFNHNTTYELCLRWMQLGSF 2246
Cdd:cd06602    238 EIfPGKRPFIISRSTFPGSGKYAGHWLGDNYSTWEDMRYSIPGMLEFNLFGIPMVGADICGFNGNTTEELCARWMQLGAF 317

                          330       340       350       360       370
                   ....*....|....*....|....*....|....*....|....*....|
gi 1159648420 2247 YPFSRNHNAEGNREQDPAVFGAEFAEISRATLRIRYSLLPYLYTLFYESH 2296
Cdd:cd06602    318 YPFSRNHNDIGAIDQEPYVWGPSVADASRKALLIRYSLLPYLYTLFYRAH 367
Glyco_hydro_31 pfam01055
Glycosyl hydrolases family 31; Glycosyl hydrolases are key enzymes of carbohydrate metabolism. ...
 1917-2388 0e+00

Glycosyl hydrolases family 31; Glycosyl hydrolases are key enzymes of carbohydrate metabolism. Family 31 comprises of enzymes that are, or similar to, alpha- galactosidases.


Pssm-ID: 460044 [Multi-domain]  Cd Length: 443  Bit Score: 643.46  E-value: 0e+00
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159648420 1917 YVFLGPTPENVVQQYTEAIGRPHMPAYWSLGFHLSRWGYGSIDVLKETVNRMHYYDIPYDVQHLDIDYMERYMDFTYDKV 1996
Cdd:pfam01055    1 YFFLGPTPKDVVKQYTELTGRPPLPPYWALGYHQSRWGYKSEEEVLEVVDGFRERDIPLDVIWLDIDYMDGYRDFTWDPE 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159648420 1997 NYAGLPEYIQKLKRKGMHNVVILDPFITKDEEPgtYRPYDLGEEMGVWVNNSDGvTPAVGKaWPpGDSVFPDYTNPRTAE 2076
Cdd:pfam01055   81 RFPDPKGMVDELHAKGQKLVVIIDPGIKKVDPG--YPPYDEGLEKGYFVKNPDG-SLYVGG-WP-GMSAFPDFTNPEARD 155

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159648420 2077 WWTQMCLEFKDVLDYDGIWIDMNEPSNFltGQYPGCAVNDLNNPPYVPSisdhslaqktlcpdsktylgEHYNTHSLFGW 2156
Cdd:pfam01055  156 WWADQLFKFLLDMGVDGIWNDMNEPSVF--CGSGPEDTVAKDNDPGGGV--------------------EHYDVHNLYGL 213

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159648420 2157 SQTAPTFHAAQQATG-KRAFVLSRSTFVGSGKHGGHWLGDNFSQWKDMHRSIVGILEFNLFGIPYIGADICGFNHNTTYE 2235
Cdd:pfam01055  214 LMAKATYEGLREKRPnKRPFVLTRSGFAGSQRYAAHWSGDNTSTWEHLRFSIPGGLSLGLSGIPFWGADIGGFFNPTTPE 293

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159648420 2236 LCLRWMQLGSFYPFSRNHNAEGNREQDPAVFGAEFAEISRATLRIRYSLLPYLYTLFYESHVHGNTVARSLMHEFTSDQE 2315
Cdd:pfam01055  294 LYVRWYQLGAFSPFFRNHSSIDTRRREPWLFGEEVEEIIRKAIRLRYRLLPYLYTLFYEAHETGLPVMRPLFLEFPDDPN 373

                          410       420       430       440       450       460       470
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1159648420 2316 THGIDTAFLWGPAFMIAPVLQEGARSVDVYFPEATWFDYYTGHKVPstwKKNYATVAAPLSKIPLFIRGGYIL 2388
Cdd:pfam01055  374 TFDIDDQFMFGPSLLVAPVLEEGATSVDVYLPGGRWYDFWTGERYE---GGGTVPVTAPLDRIPLFVRGGSII 443
KISc_KIF4 cd01372
Kinesin motor domain, KIF4-like subfamily; Kinesin motor domain, KIF4-like subfamily. Members ...
 8-372 0e+00

Kinesin motor domain, KIF4-like subfamily; Kinesin motor domain, KIF4-like subfamily. Members of this group seem to perform a variety of functions, and have been implicated in neuronal organelle transport and chromosome segregation during mitosis. This catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Kinesins are microtubule-dependent molecular motors that play important roles in intracellular transport and in cell division. In most kinesins, the motor domain is found at the N-terminus (N-type). N-type kinesins are (+) end-directed motors, i.e. they transport cargo towards the (+) end of the microtubule. Kinesin motor domains hydrolyze ATP at a rate of about 80 per second, and move along the microtubule at a speed of about 6400 Angstroms per second. To achieve that, kinesin head groups work in pairs. Upon replacing ADP with ATP, a kinesin motor domain increases its affinity for microtubule binding and locks in place. Also, the neck linker binds to the motor domain, which repositions the other head domain through the coiled-coil domain close to a second tubulin dimer, about 80 Angstroms along the microtubule. Meanwhile, ATP hydrolysis takes place, and when the second head domain binds to the microtubule, the first domain again replaces ADP with ATP, triggering a conformational change that pulls the first domain forward.


Pssm-ID: 276823 [Multi-domain]  Cd Length: 341  Bit Score: 631.29  E-value: 0e+00
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159648420    8 SSVRVAVRIRPQLAKEKIEGCHICTSVTPGEPQVFLGKDKAFTFDYVFNIDSQQEEIYVQCIEKLIEGCFEGYNATVFAY 87
Cdd:cd01372      1 SSVRVAVRVRPLLPKEIIEGCRICVSFVPGEPQVTVGTDKSFTFDYVFDPSTEQEEVYNTCVAPLVDGLFEGYNATVLAY 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159648420   88 GQTGAGKTYTMGTGFDVNITEEEQGIISRAVKHLFRCIEEKKQAaikqglppPDFKVNAQFLELYNEEILDLFDTTRDid 167
Cdd:cd01372     81 GQTGSGKTYTMGTAYTAEEDEEQVGIIPRAIQHIFKKIEKKKDT--------FEFQLKVSFLEIYNEEIRDLLDPETD-- 150

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159648420  168 aknKKSNIKIHEDSAGGIYTVGVTTRTVNGESEMMQCLKLGALSRTTASTQMNVQSSRSHAIFTIHLCQTRVCPPfntdn 247
Cdd:cd01372    151 ---KKPTISIREDSKGGITIVGLTEVTVLSAEDMMSCLEQGSLSRTTASTAMNSQSSRSHAIFTITLEQTKKNGP----- 222

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159648420  248 atdnriISESSEMNEFETLTAKFHFVDLAGSERLKRTGATGERAKEGISINCGLLALGNVISALGDKSKKATHVPYRDSK 327
Cdd:cd01372    223 ------IAPMSADDKNSTFTSKFHFVDLAGSERLKRTGATGDRLKEGISINSGLLALGNVISALGDESKKGAHVPYRDSK 296

                          330       340       350       360
                   ....*....|....*....|....*....|....*....|....*
gi 1159648420  328 LTRLLQDSLGGNSQTLMIACVSPSDRDFMETLNTLKYANRARNIK 372
Cdd:cd01372    297 LTRLLQDSLGGNSHTLMIACVSPADSNFEETLNTLKYANRARNIK 341
Kinesin pfam00225
Kinesin motor domain;
15-371 5.97e-140

Kinesin motor domain;


Pssm-ID: 459720 [Multi-domain]  Cd Length: 326  Bit Score: 440.09  E-value: 5.97e-140
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159648420   15 RIRPQLAKEKIEGCHICTSVTPGEPQVFL-------GKDKAFTFDYVFNIDSQQEEIYVQCIEKLIEGCFEGYNATVFAY 87
Cdd:pfam00225    1 RVRPLNEREKERGSSVIVSVESVDSETVEsshltnkNRTKTFTFDKVFDPEATQEDVYEETAKPLVESVLEGYNVTIFAY 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159648420   88 GQTGAGKTYTMGTgfdvniTEEEQGIISRAVKHLFRCIEEKKQaaikqglpPPDFKVNAQFLELYNEEILDLFDTTrdid 167
Cdd:pfam00225   81 GQTGSGKTYTMEG------SDEQPGIIPRALEDLFDRIQKTKE--------RSEFSVKVSYLEIYNEKIRDLLSPS---- 142

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159648420  168 aKNKKSNIKIHEDSAGGIYTVGVTTRTVNGESEMMQCLKLGALSRTTASTQMNVQSSRSHAIFTIHLCQTRVcppfntdn 247
Cdd:pfam00225  143 -NKNKRKLRIREDPKKGVYVKGLTEVEVSSAEEVLELLQLGNKNRTVAATKMNEESSRSHAIFTITVEQRNR-------- 213

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159648420  248 atdnriisesSEMNEFETLTAKFHFVDLAGSERLKRTG-ATGERAKEGISINCGLLALGNVISALGDKSKKatHVPYRDS 326
Cdd:pfam00225  214 ----------STGGEESVKTGKLNLVDLAGSERASKTGaAGGQRLKEAANINKSLSALGNVISALADKKSK--HIPYRDS 281

                          330       340       350       360
                   ....*....|....*....|....*....|....*....|....*
gi 1159648420  327 KLTRLLQDSLGGNSQTLMIACVSPSDRDFMETLNTLKYANRARNI 371
Cdd:pfam00225  282 KLTRLLQDSLGGNSKTLMIANISPSSSNYEETLSTLRFASRAKNI 326
KISc smart00129
Kinesin motor, catalytic domain. ATPase; Microtubule-dependent molecular motors that play ...
 9-378 1.57e-138

Kinesin motor, catalytic domain. ATPase; Microtubule-dependent molecular motors that play important roles in intracellular transport of organelles and in cell division.


Pssm-ID: 214526 [Multi-domain]  Cd Length: 335  Bit Score: 436.23  E-value: 1.57e-138
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159648420     9 SVRVAVRIRPQLAKEKIEGCHICTSVTPGEPQV-------FLGKDKAFTFDYVFNIDSQQEEIYVQCIEKLIEGCFEGYN 81
Cdd:smart00129    1 NIRVVVRVRPLNKREKSRKSPSVVPFPDKVGKTltvrspkNRQGEKKFTFDKVFDATASQEDVFEETAAPLVDSVLEGYN 80

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159648420    82 ATVFAYGQTGAGKTYTMGTgfdvniTEEEQGIISRAVKHLFRCIEEKKqaaikqglPPPDFKVNAQFLELYNEEILDLFD 161
Cdd:smart00129   81 ATIFAYGQTGSGKTYTMIG------TPDSPGIIPRALKDLFEKIDKRE--------EGWQFSVKVSYLEIYNEKIRDLLN 146

                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159648420   162 TTrdidaknkKSNIKIHEDSAGGIYTVGVTTRTVNGESEMMQCLKLGALSRTTASTQMNVQSSRSHAIFTIHLcqtrvcp 241
Cdd:smart00129  147 PS--------SKKLEIREDEKGGVYVKGLTEISVSSFEEVYNLLEKGNKNRTVAATKMNEESSRSHAVFTITV------- 211

                           250       260       270       280       290       300       310       320
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159648420   242 pfntdnatDNRIISESSEmnefETLTAKFHFVDLAGSERLKRTGATGERAKEGISINCGLLALGNVISALGDKSKKaTHV 321
Cdd:smart00129  212 --------EQKIKNSSSG----SGKASKLNLVDLAGSERAKKTGAEGDRLKEAGNINKSLSALGNVINALAQHSKS-RHI 278

                           330       340       350       360       370
                    ....*....|....*....|....*....|....*....|....*....|....*..
gi 1159648420   322 PYRDSKLTRLLQDSLGGNSQTLMIACVSPSDRDFMETLNTLKYANRARNIKNKVMVN 378
Cdd:smart00129  279 PYRDSKLTRLLQDSLGGNSKTLMIANVSPSSSNLEETLSTLRFASRAKEIKNKPIVN 335
YicI COG1501
Alpha-glucosidase/xylosidase, GH31 family [Carbohydrate transport and metabolism];
1829-2429 3.11e-102

Alpha-glucosidase/xylosidase, GH31 family [Carbohydrate transport and metabolism];


Pssm-ID: 441110 [Multi-domain]  Cd Length: 609  Bit Score: 342.91  E-value: 3.11e-102
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159648420 1829 PSTSVYGFGEQEHESFKHSMDFVTYGMfsrDQAPTPLV-NLYGVHPFYMcveaDSNAHGVLLlNSN---AQDVSLSPDPS 1904
Cdd:COG1501     60 LGEQIYGLGERFTTLHKRGRIVVNWNL---DHGGHKDNgNTYAPIPFYV----SSKGYGVFV-NSAsyvTFDVGSAYSDL 131

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159648420 1905 VTFRTIGGILDFYVFLGPTPENVVQQYTEAIGRPHMPAYWSLGFHLSRWGYGSIDVLKETVNRMHYYDIPYDVQHLDIDY 1984
Cdd:COG1501    132 VEFTVPGDSLEFYVIEGPSPEDVLEKYTELTGKPPLPPRWAFGYWQSRKSYYDQDQVLAFADEFRDRGFPLDVIHLDIRW 211

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159648420 1985 MERYM--DFTYDKVNYAGLPEYIQKLKRKGMHNVVILDPFItkDEEPGTYRpydlgEEMGVWVNNSDGvTPAVGKAWPpG 2062
Cdd:COG1501    212 MDKYYwgDFEWDPRRFPDPKAMVKELHDRGVKLVLWINPYV--APDSAIFA-----EGMANFVKIASG-TVFVGKMWP-G 282

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159648420 2063 DSVFPDYTNPRTAEWWtQMCLEfKDVLDY--DGIWIDMNEpsnfltgqypgcavndlnNPPYVPSISDHSLAQKTlcpds 2140
Cdd:COG1501    283 TTGLLDFTRPDAREWF-WAGLE-KELLSIgvDGIKLDMNE------------------GWPTDVATFPSNVPQQM----- 337

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159648420 2141 ktylgehyntHSLFGWSQTAPTFHAAQQATGKRAFVLSRSTFVGSGKHGGHWLGDNFSQWKDMHRSIVGILEFNLFGIPY 2220
Cdd:COG1501    338 ----------RNLYGLLEAKATFEGFRTSRNNRTFILTRSGFAGGQRYPVIWTGDNTSSWESLEDQLTQGLNLSLSGVPF 407

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159648420 2221 IGADICGFNHNTTYELCLRWMQLGSFYPFSRNHNAEGNREqdPAVFGAEFAEISRATLRIRYSLLPYLYTLFYESHVHGN 2300
Cdd:COG1501    408 WTPDIGGFFGSPSRELWIRWFQVGAFSPFARIHGWASSTE--PWFFDEEAKQIVKEYAQLRYRLLPYIYSLFAKASTDGT 485

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159648420 2301 TVARSLMHEFTSDQETHGIDTAFLWGPAFMIAPVLqEGARSVDVYFPEATWFDYYTGHKVP-STWkknyATVAAPLSKIP 2379
Cdd:COG1501    486 PVIRPLFLEFPDDPTTRFIDDQYMFGEYLLVAPIF-AGTESRLVYLPKGKWYDFWTGELIEgGQW----ITVTAPLDRLP 560

                          570       580       590       600       610
                   ....*....|....*....|....*....|....*....|....*....|.
gi 1159648420 2380 LFIRGGYILPeQAPASTTTK-SRLNPFGLIIALDehGEASGSLFWDDGDSI 2429
Cdd:COG1501    561 LYVRDGSIIP-LGPVSLRPSmQKIDGIELRVYGS--GETAYTLYDDDGETV 608
alpha_gluc_MalA NF040948
alpha-glucosidase MalA;
1833-2389 2.68e-97

alpha-glucosidase MalA;


Pssm-ID: 468879 [Multi-domain]  Cd Length: 626  Bit Score: 328.91  E-value: 2.68e-97
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159648420 1833 VYGFGEQEHESFKHSMDFVTY----GMFSRDQAPtplvnLYGVHPFYMCVEaDSNAHGvLLLNSNAQ---DVSLS----- 1900
Cdd:NF040948    63 VLGLGEKAFELDRRRGRFIMYnvdaGAYTKYSDP-----LYVSIPFFISVK-GGKATG-YFVNSPSKlifDIGLErydkv 135

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159648420 1901 ----PDPSVtfrtiggilDFYVFLGPTPENVVQQYTEAIGRPHMPAYWSLGFHLSRWGYGSIDVLKETVNRMHYYDIPYD 1976
Cdd:NF040948   136 kitiPENSV---------ELYVIEGPTIEEVLETYSELTGKPFLPPKWALGYQISRYSYYPQDAVVEVVDELRKEGFPVS 206

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159648420 1977 VQHLDIDYMERYMDFTYDKVNYAGLPEYIQKLKRKGMHNVVILDPFITKDEepgTYRPYDLGeeMGVWVNNSDGvTPAVG 2056
Cdd:NF040948   207 AVYLDIDYMDSYKLFTWDKEKFPDPRKFIEELHSRGVKVITIVDPSVKADQ---NYEVFRSG--LGKYCETENG-ELYVG 280

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159648420 2057 KAWPpGDSVFPDYTNPRTAEWWTQMCLEFKDVLDYDGIWIDMNEPSNF-LTGQYPGCAVNDLNNPPYVPSISDHSLAQkt 2135
Cdd:NF040948   281 KLWP-GNSVFPDFLNEETREWWAELVEEWVKQYGVDGIWLDMNEPTDFtEDIERAALGPHQLREDRLLYTFPPGAVHR-- 357

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159648420 2136 LCPDSKTYLGEHYNTHSLFgwsQTAPTFHAAQQATGKRAFVLSRSTFVGSGKHGGHWLGDNFSQWKDMHRSIVGILEFNL 2215
Cdd:NF040948   358 LDDGKKVKHEKVRNAYPYF---EAMATYEGLKRAGKDEPFILSRSGYAGIQRYAAIWTGDNTSSWDDLKLQLQLVLGLSI 434

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159648420 2216 FGIPYIGADICGF-----NHNTTYELCLRWMQLGSFYPFSRNHNAEGNREQDPAVFGAEFAEISRATLRIRYSLLPYLYT 2290
Cdd:NF040948   435 SGVPYVGCDIGGFagrsfPIDNSPELLVRYYQAALFFPLFRTHKSKDGNDQEPYFLPSKYKEKVKRVIKLRYKFLPYLYS 514

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159648420 2291 LFYESHVHGNTVARSLMHEFTSDQETHGIDTAFLWGPAFMIAPVLQEGARSVDVYFPEATWFDYYTG--HKVPStWKKNY 2368
Cdd:NF040948   515 LAWEAHETGHPIIRPLFYEFQDDEDAYRIEDEYMVGKYLLYAPQIYPKEESRDVYLPRGKWLDFWTGeeYEGPS-WIESE 593

                          570       580
                   ....*....|....*....|.
gi 1159648420 2369 AtvaaplsKIPLFIRGGYILP 2389
Cdd:NF040948   594 A-------ELPIYIREGSAVP 607
PLN02763 PLN02763
hydrolase, hydrolyzing O-glycosyl compounds
 1829-2442 6.02e-96

hydrolase, hydrolyzing O-glycosyl compounds


Pssm-ID: 215408 [Multi-domain]  Cd Length: 978  Bit Score: 335.32  E-value: 6.02e-96
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159648420 1829 PSTSVYGFGEQEHESFKHSMDFVTYGMFSRDQAP-TPlvNLYGVHPFYMCVEADSNAHGVLLLNSNAQDVSL-------- 1899
Cdd:PLN02763    72 SGTSFYGTGEVSGPLERTGKRVYTWNTDAWGYGQnTT--SLYQSHPWVFVVLPNGEALGVLADTTRRCEIDLrkesiiri 149

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159648420 1900 ---SPDPSVTFrtiggildfyvflGP--TPENVVQQYTEAIGRPHMPAYWSLGFHLSRWGYGSIDVLKETVNRMHYYDIP 1974
Cdd:PLN02763   150 iapASYPVITF-------------GPfpSPEALLTSLSHAIGTVFMPPKWALGYQQCRWSYESAKRVAEIARTFREKKIP 216

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159648420 1975 YDVQHLDIDYMERYMDFTYDKVNYAGLPEYIQKLKRKGMHNVVILDPFITKDEEpgtYRPYDLGEEMGVWVNNSDGvTPA 2054
Cdd:PLN02763   217 CDVVWMDIDYMDGFRCFTFDKERFPDPKGLADDLHSIGFKAIWMLDPGIKAEEG---YFVYDSGCENDVWIQTADG-KPF 292

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159648420 2055 VGKAWPpGDSVFPDYTNPRTAEWWTQMCLEFKDVlDYDGIWIDMNEPSNFLTGQYPGCAVNDLNNPPYVPSISDHSlaqk 2134
Cdd:PLN02763   293 VGEVWP-GPCVFPDFTNKKTRSWWANLVKDFVSN-GVDGIWNDMNEPAVFKTVTKTMPETNIHRGDEELGGVQNHS---- 366

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159648420 2135 tlcpdsktylgeHYntHSLFGWSQTAPTFHAAQQA-TGKRAFVLSRSTFVGSGKHGGHWLGDNFSQWKDMHRSIVGILEF 2213
Cdd:PLN02763   367 ------------HY--HNVYGMLMARSTYEGMLLAnKNKRPFVLTRAGFIGSQRYAATWTGDNLSNWEHLHMSIPMVLQL 432

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159648420 2214 NLFGIPYIGADICGFNHNTTYELCLRWMQLGSFYPFSRNHNAEGNREQDPAVFGAEFAEISRATLRIRYSLLPYLYTLFY 2293
Cdd:PLN02763   433 GLSGQPLSGPDIGGFAGDATPKLFGRWMGVGAMFPFARGHSEQGTIDHEPWSFGEECEEVCRLALKRRYRLLPHFYTLFY 512

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159648420 2294 ESHVHGNTVARSLMHEFTSDQETHGIDTAFLWGPAFMIAPVL-QEGARSVDVYFPEATW--FDYYTGHkvPSTwkknyat 2370
Cdd:PLN02763   513 KAHTTGLPVMTPIFFADPKDPSLRKVENSFLLGPLLISASTLpDQGSDNLQHVLPKGIWqrFDFDDSH--PDL------- 583

                          570       580       590       600       610       620       630
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1159648420 2371 vaaPLskipLFIRGGYILPEQAPASTTTKSRL-NPFGLIIALDEHGEASGSLFWDDGDSIDtIENENYFLAKY 2442
Cdd:PLN02763   584 ---PL----LYLQGGSIIPLGPPIQHVGEASLsDDLTLLIALDENGKAEGVLYEDDGDGFG-YTKGDYLLTHY 648
KIP1 COG5059
Kinesin-like protein [Cytoskeleton];
44-509 4.27e-95

Kinesin-like protein [Cytoskeleton];


Pssm-ID: 227392 [Multi-domain]  Cd Length: 568  Bit Score: 320.53  E-value: 4.27e-95
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159648420   44 GKDKAFTFDYVFNIDSQQEEIYVQCIEKLIEGCFEGYNATVFAYGQTGAGKTYTMgTGfdvniTEEEQGIISRAVKHLFR 123
Cdd:COG5059     53 SKEGTYAFDKVFGPSATQEDVYEETIKPLIDSLLLGYNCTVFAYGQTGSGKTYTM-SG-----TEEEPGIIPLSLKELFS 126

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159648420  124 CIEEKKQAAikqglpppDFKVNAQFLELYNEEILDLFDttrdidakNKKSNIKIHEDSAGGIYTVGVTTRTVNGESEMMQ 203
Cdd:COG5059    127 KLEDLSMTK--------DFAVSISYLEIYNEKIYDLLS--------PNEESLNIREDSLLGVKVAGLTEKHVSSKEEILD 190

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159648420  204 CLKLGALSRTTASTQMNVQSSRSHAIFTIHLcqtrvcppfntdnatdnriisESSEMNEFETLTAKFHFVDLAGSERLKR 283
Cdd:COG5059    191 LLRKGEKNRTTASTEINDESSRSHSIFQIEL---------------------ASKNKVSGTSETSKLSLVDLAGSERAAR 249

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159648420  284 TGATGERAKEGISINCGLLALGNVISALGDKsKKATHVPYRDSKLTRLLQDSLGGNSQTLMIACVSPSDRDFMETLNTLK 363
Cdd:COG5059    250 TGNRGTRLKEGASINKSLLTLGNVINALGDK-KKSGHIPYRESKLTRLLQDSLGGNCNTRVICTISPSSNSFEETINTLK 328

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159648420  364 YANRARNIKNKVMVNQDRASQ-QINALRSEIARLQMELMEYKTGKRIID------------EEGVESINDMFHENAMLQT 430
Cdd:COG5059    329 FASRAKSIKNKIQVNSSSDSSrEIEEIKFDLSEDRSEIEILVFREQSQLsqsslsgifaymQSLKKETETLKSRIDLIMK 408

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159648420  431 EN--------NNLRVRIKAMQETVDALRARITQLMSDQAnqvlaragEGNEEISNMIHNYIKEIEDLRAKL----LESEA 498
Cdd:COG5059    409 SIisgtferkKLLKEEGWKYKSTLQFLRIEIDRLLLLRE--------EELSKKKTKIHKLNKLRHDLSSLLssipEETSD 480

                          490
                   ....*....|.
gi 1159648420  499 VNENLRRNLSR 509
Cdd:COG5059    481 RVESEKASKLR 491
PLN03188 PLN03188
kinesin-12 family protein; Provisional
 7-404 1.56e-67

kinesin-12 family protein; Provisional


Pssm-ID: 215621 [Multi-domain]  Cd Length: 1320  Bit Score: 252.93  E-value: 1.56e-67
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159648420    7 ESSVRVAVRIRPQLAKEkiEGCHICTSVTPGEPQVflgKDKAFTFDYVFNIDSQQEEIYVQCIEKLIEGCFEGYNATVFA 86
Cdd:PLN03188    97 DSGVKVIVRMKPLNKGE--EGEMIVQKMSNDSLTI---NGQTFTFDSIADPESTQEDIFQLVGAPLVENCLAGFNSSVFA 171

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159648420   87 YGQTGAGKTYTM-GTG---FDVNITEEEQGIISRAVKHLF-RCIEEKKQAAIKQglppPDFKVNAQFLELYNEEILDLFD 161
Cdd:PLN03188   172 YGQTGSGKTYTMwGPAnglLEEHLSGDQQGLTPRVFERLFaRINEEQIKHADRQ----LKYQCRCSFLEIYNEQITDLLD 247

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159648420  162 TTrdidaknkKSNIKIHEDSAGGIYTVGVTTRTVNGESEMMQCLKLGALSRTTASTQMNVQSSRSHAIFTihlcqtrvCp 241
Cdd:PLN03188   248 PS--------QKNLQIREDVKSGVYVENLTEEYVKTMKDVTQLLIKGLSNRRTGATSINAESSRSHSVFT--------C- 310

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159648420  242 pfntdnATDNRIISESSEMNEFETltAKFHFVDLAGSERLKRTGATGERAKEGISINCGLLALGNVISALGDKSK--KAT 319
Cdd:PLN03188   311 ------VVESRCKSVADGLSSFKT--SRINLVDLAGSERQKLTGAAGDRLKEAGNINRSLSQLGNLINILAEISQtgKQR 382

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159648420  320 HVPYRDSKLTRLLQDSLGGNSQTLMIACVSPSDRDFMETLNTLKYANRARNIKNKVMVNQDrASQQINALRSEIARLQME 399
Cdd:PLN03188   383 HIPYRDSRLTFLLQESLGGNAKLAMVCAISPSQSCKSETFSTLRFAQRAKAIKNKAVVNEV-MQDDVNFLREVIRQLRDE 461


                   ....*
gi 1159648420  400 LMEYK 404
Cdd:PLN03188   462 LQRVK 466
WD40 cd00200
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ...
 1316-1629 1.13e-60

WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions including adaptor/regulatory modules in signal transduction, pre-mRNA processing and cytoskeleton assembly; typically contains a GH dipeptide 11-24 residues from its N-terminus and the WD dipeptide at its C-terminus and is 40 residues long, hence the name WD40; between GH and WD lies a conserved core; serves as a stable propeller-like platform to which proteins can bind either stably or reversibly; forms a propeller-like structure with several blades where each blade is composed of a four-stranded anti-parallel b-sheet; instances with few detectable copies are hypothesized to form larger structures by dimerization; each WD40 sequence repeat forms the first three strands of one blade and the last strand in the next blade; the last C-terminal WD40 repeat completes the blade structure of the first WD40 repeat to create the closed ring propeller-structure; residues on the top and bottom surface of the propeller are proposed to coordinate interactions with other proteins and/or small ligands; 7 copies of the repeat are present in this alignment.


Pssm-ID: 238121 [Multi-domain]  Cd Length: 289  Bit Score: 210.65  E-value: 1.13e-60
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159648420 1316 CIYTAEGHTKAVLCVDATDD--LLFTGSKDRTCKVWNLVTGQEIMSLGGHPNNVVSIKYCNYTSLVFTVST-SYIKVWDI 1392
Cdd:cd00200      1 LRRTLKGHTGGVTCVAFSPDgkLLATGSGDGTIKVWDLETGELLRTLKGHTGPVRDVAASADGTYLASGSSdKTIRLWDL 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159648420 1393 RDSaKCIRTLTSSgqampgdvcsastnrtvaipagENQINQIALNPTGTFLYAAAG-NSVRMWDLKRFQSTGKLTGHQGP 1471
Cdd:cd00200     81 ETG-ECVRTLTGH----------------------TSYVSSVAFSPDGRILSSSSRdKTIKVWDVETGKCLTTLRGHTDW 137

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159648420 1472 VMCLTVDRisnGQDLIVTGSKDHYIKMFDVTEGalgsvSPTHNFEpPHYDGIEALAIMGDN--LFSGSRDNGIKKWDLAQ 1549
Cdd:cd00200    138 VNSVAFSP---DGTFVASSSQDGTIKLWDLRTG-----KCVATLT-GHTGEVNSVAFSPDGekLLSSSSDGTIKLWDLST 208

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159648420 1550 KDLLQQVPnAHKDWVCALGLVPGAPVLLSGCRGGNIKLWNVETFAPIGEMKGHDSPINAIC--TNSSQIFTAADDRTVRI 1627
Cdd:cd00200    209 GKCLGTLR-GHENGVNSVAFSPDGYLLASGSEDGTIRVWDLRTGECVQTLSGHTNSVTSLAwsPDGKRLASGSADGTIRI 287


                   ..
gi 1159648420 1628 WK 1629
Cdd:cd00200    288 WD 289
WD40 COG2319
WD40 repeat [General function prediction only];
1315-1632 2.94e-49

WD40 repeat [General function prediction only];


Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 181.65  E-value: 2.94e-49
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159648420 1315 QCIYTAEGHTKAVLCVDATDD--LLFTGSKDRTCKVWNLVTGQEIMSLGGHPNNVvsikycnyTSLVFT------VSTSY 1386
Cdd:COG2319    111 LLLRTLTGHTGAVRSVAFSPDgkTLASGSADGTVRLWDLATGKLLRTLTGHSGAV--------TSVAFSpdgkllASGSD 182

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159648420 1387 ---IKVWDIrDSAKCIRTLTssgqampgdvcsastnrtvaipAGENQINQIALNPTGTFL-YAAAGNSVRMWDLKRFQST 1462
Cdd:COG2319    183 dgtVRLWDL-ATGKLLRTLT----------------------GHTGAVRSVAFSPDGKLLaSGSADGTVRLWDLATGKLL 239

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159648420 1463 GKLTGHQGPVMCLTVDriSNGQdLIVTGSKDHYIKMFDVTEGALGSVSPTHNfepphyDGIEALAI--MGDNLFSGSRDN 1540
Cdd:COG2319    240 RTLTGHSGSVRSVAFS--PDGR-LLASGSADGTVRLWDLATGELLRTLTGHS------GGVNSVAFspDGKLLASGSDDG 310

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159648420 1541 GIKKWDLAQKDLLQqVPNAHKDWVCALGLVPGAPVLLSGCRGGNIKLWNVETFAPIGEMKGHDSPINAIC--TNSSQIFT 1618
Cdd:COG2319    311 TVRLWDLATGKLLR-TLTGHTGAVRSVAFSPDGKTLASGSDDGTVRLWDLATGELLRTLTGHTGAVTSVAfsPDGRTLAS 389

                          330
                   ....*....|....
gi 1159648420 1619 AADDRTVRIWKARN 1632
Cdd:COG2319    390 GSADGTVRLWDLAT 403
Rcc_KIF21A cd22263
regulatory coiled-coil domain found in kinesin-like protein KIF21A; KIF21A, also called ...
 920-1003 1.46e-47

regulatory coiled-coil domain found in kinesin-like protein KIF21A; KIF21A, also called kinesin-like protein KIF2 or renal carcinoma antigen NY-REN-62, is a microtubule-binding motor protein involved in neuronal axonal transport. It works as a microtubule stabilizer that regulates axonal morphology, suppressing cortical microtubule dynamics in neurons. Mutations in KIF21A cause congenital fibrosis of the extraocular muscles type 1 (CFEOM1). In vitro, it has a plus-end directed motor activity. This model corresponds to the regulatory coiled-coil domain of KIF21A, which folds into an intramolecular antiparallel coiled-coil monomer in solution, but crystallizes into a dimeric domain-swapped antiparallel coiled-coil.


Pssm-ID: 410204 [Multi-domain]  Cd Length: 82  Bit Score: 165.10  E-value: 1.46e-47
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159648420  920 QRMTISNMEADMNRLLTQREELTKRREKLSKRREKLMKDGGgsETDRNVQNINEEMESLTANIDYINDSISDCQANIMQM 999
Cdd:cd22263      1 QRMTISNMEADMNRLLKQREELTKRREKLSKKREKIIKENG--EGDKNVHNINEEMESLTANIDYINDSISDCQANIMQM 78


                   ....
gi 1159648420 1000 EEAK 1003
Cdd:cd22263     79 EEAK 82
NtCtMGAM_N pfam16863
N-terminal barrel of NtMGAM and CtMGAM, maltase-glucoamylase; NtCtMGAM_N is a beta-barrel-like ...
 1722-1830 2.97e-37

N-terminal barrel of NtMGAM and CtMGAM, maltase-glucoamylase; NtCtMGAM_N is a beta-barrel-like structure just N-terminal to the catalytic domain of maltase-glucoamylase in eukaryotes. It contributes to the architecture of the substrate-binding site, by donating a loop that comes into close contact with two regions in the catalytic domain thereby creating the site. This family is frequently found at the N-terminus of Glycosyl hydrolase 31, pfam01055.to which it contributes as above.


Pssm-ID: 465286  Cd Length: 113  Bit Score: 136.84  E-value: 2.97e-37
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159648420 1722 GWRVTLNKRQAL-SLFGNDISPIVLEVEFQTRDRLRFKLYDPNSQRFEVP---LQIDSPGVAADEANYDVELVEGSSHFR 1797
Cdd:pfam16863    1 GLTADLTLAGSPcNLYGNDIETLKLTVEYQTDNRLHVKITDPNNKRYEVPeelLPRPSPSSSASDSLYEFEYTNEPFGFK 80

                           90       100       110
                   ....*....|....*....|....*....|...
gi 1159648420 1798 IKRKSTGTVLWDSPLVDLFFSNQYLQITTTVPS 1830
Cdd:pfam16863   81 VTRKSTGEVLFDTSGGPLVFEDQFLQLSTRLPS 113
GH31_N cd14752
N-terminal domain of glycosyl hydrolase family 31 (GH31); This family is found N-terminal to ...
 1829-1936 1.12e-25

N-terminal domain of glycosyl hydrolase family 31 (GH31); This family is found N-terminal to the glycosyl-hydrolase domain of Glycoside hydrolase family 31 (GH31). GH31 includes the glycoside hydrolases alpha-glucosidase (EC 3.2.1.20), alpha-1,3-glucosidase (EC 3.2.1.84), alpha-xylosidase (EC 3.2.1.177), sucrase-isomaltase (EC 3.2.1.48 and EC 3.2.1.10), as well as alpha-glucan lyase (EC 4.2.2.13). All GH31 enzymes cleave a terminal carbohydrate moiety from a substrate that varies considerably in size, depending on the enzyme, and may be either a starch or a glycoprotein. In most cases, the pyranose moiety recognized in subsite-1 of the substrate binding site is an alpha-D-glucose, though some GH31 family members show a preference for alpha-D-xylose. Several GH31 enzymes can accommodate both glucose and xylose and different levels of discrimination between the two have been observed. Most characterized GH31 enzymes are alpha-glucosidases. In mammals, GH31 members with alpha-glucosidase activity are implicated in at least three distinct biological processes. The lysosomal acid alpha-glucosidase (GAA) is essential for glycogen degradation and a deficiency or malfunction of this enzyme causes glycogen storage disease II, also known as Pompe disease. In the endoplasmic reticulum, alpha-glucosidase II catalyzes the second step in the N-linked oligosaccharide processing pathway that constitutes part of the quality control system for glycoprotein folding and maturation. The intestinal enzymes sucrase-isomaltase (SI) and maltase-glucoamylase (MGAM) play key roles in the final stage of carbohydrate digestion, making alpha-glucosidase inhibitors useful in the treatment of type 2 diabetes. GH31 alpha-glycosidases are retaining enzymes that cleave their substrates via an acid/base-catalyzed, double-displacement mechanism involving a covalent glycosyl-enzyme intermediate. Two aspartic acid residues of the catalytic domain have been identified as the catalytic nucleophile and the acid/base, respectively. A loop of the N-terminal beta-sandwich domain is part of the active site pocket.


Pssm-ID: 270212 [Multi-domain]  Cd Length: 122  Bit Score: 103.80  E-value: 1.12e-25
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159648420 1829 PSTSVYGFGEQEHESFKHSMdfvTYGMFSRDQAPTPLV--NLYGVHPFYMCveadSNAHGVLLLNSNAQDVSLSPD--PS 1904
Cdd:cd14752     18 PDEHFYGLGERFGGLNKRGK---RYRLWNTDQGGYRGStdPLYGSIPFYLS----SKGYGVFLDNPSRTEFDFGSEdsDE 90

                           90       100       110
                   ....*....|....*....|....*....|..
gi 1159648420 1905 VTFRTIGGILDFYVFLGPTPENVVQQYTEAIG 1936
Cdd:cd14752     91 LTFSSEGGDLDYYFFAGPTPKEVIEQYTELTG 122
SCP-1 pfam05483
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ...
 389-1024 2.96e-16

Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major component of the transverse filaments of the synaptonemal complex. Synaptonemal complexes are structures that are formed between homologous chromosomes during meiotic prophase.


Pssm-ID: 114219 [Multi-domain]  Cd Length: 787  Bit Score: 85.54  E-value: 2.96e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159648420  389 LRSEIARLQMELMEYKTGKRI--IDEEGVESINDMFHENAMLQTENNNLRVRIKAMQETVDALRaritqlmsDQANQVLA 466
Cdd:pfam05483  204 VQAENARLEMHFKLKEDHEKIqhLEEEYKKEINDKEKQVSLLLIQITEKENKMKDLTFLLEESR--------DKANQLEE 275

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159648420  467 RAGEGNEEISNMI---HNYIKEIEDLRAKLLESEAVNENLRRNLSRAsTRSTYfggpsafsasMLSSEKET-LEILDIAK 542
Cdd:pfam05483  276 KTKLQDENLKELIekkDHLTKELEDIKMSLQRSMSTQKALEEDLQIA-TKTIC----------QLTEEKEAqMEELNKAK 344

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159648420  543 KDLEKLKKKERKKKKSVkedntdnEQEKRDEKGSSERENNELE--AEEIQEASDREDEEEEDdededdmevvessdesds 620
Cdd:pfam05483  345 AAHSFVVTEFEATTCSL-------EELLRTEQQRLEKNEDQLKiiTMELQKKSSELEEMTKF------------------ 399

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159648420  621 dsdeKENYQADLANITCEIAIKQKLIDELENSQRRLQTLKRQYEEKLMMLQHKIRDTQLERDQVLQNLGSVETYSEEkAK 700
Cdd:pfam05483  400 ----KNNKEVELEELKKILAEDEKLLDEKKQFEKIAEELKGKEQELIFLLQAREKEIHDLEIQLTAIKTSEEHYLKE-VE 474

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159648420  701 KIKSEYEKKlQTMNKEL-QRLQTAQKEHARLLKNQSQYEKQLKKLQQEVTEMKKTKVRLMKQMKEEQEkarmTESRRNRE 779
Cdd:pfam05483  475 DLKTELEKE-KLKNIELtAHCDKLLLENKELTQEASDMTLELKKHQEDIINCKKQEERMLKQIENLEE----KEMNLRDE 549

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159648420  780 IAQLKKE--QRKREHQLKL--LEAQKRNQEVILRRKTEEVTALRRQVRPLSDKVAGKVS--RKLSLPEHPIQEPSSSSSV 853
Cdd:pfam05483  550 LESVREEfiQKGDEVKCKLdkSEENARSIEYEVLKKEKQMKILENKCNNLKKQIENKNKniEELHQENKALKKKGSAENK 629

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159648420  854 EHDGSRIAAqQKMRIPVARVQALSVTATNGTGRKYQRKAVTSRVYSSRAARMKWQLLE----RRVTDIIMQRmTISNMEA 929
Cdd:pfam05483  630 QLNAYEIKV-NKLELELASAKQKFEEIIDNYQKEIEDKKISEEKLLEEVEKAKAIADEavklQKEIDKRCQH-KIAEMVA 707

                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159648420  930 DMNRLLTQREELTKRREK---LSKRREKLMKDGGGS-ETDrnVQNINEEMESLTAnidyindsisdcqanimQMEEAKEE 1005
Cdd:pfam05483  708 LMEKHKHQYDKIIEERDSelgLYKNKEQEQSSAKAAlEIE--LSNIKAELLSLKK-----------------QLEIEKEE 768

                          650
                   ....*....|....*....
gi 1159648420 1006 GETLDVTAVINACTLTEAR 1024
Cdd:pfam05483  769 KEKLKMEAKENTAILKDKK 787
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 625-1017 8.04e-14

chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]


Pssm-ID: 274009 [Multi-domain]  Cd Length: 1164  Bit Score: 77.80  E-value: 8.04e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159648420  625 KENYQADLANITCEIAIKQKLIDELENsqrRLQTLKRQYEEKlmmlqhkirdtqlERDQVLQnlgsvetyseekakKIKS 704
Cdd:TIGR02169  172 KEKALEELEEVEENIERLDLIIDEKRQ---QLERLRREREKA-------------ERYQALL--------------KEKR 221

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159648420  705 EYEKKLQtmnkeLQRLQTAQKEHARLLKNQSQYEKQLKKLQQEVTEMKKTKVRLMKQMKEEQEK-ARMTESRRNR----- 778
Cdd:TIGR02169  222 EYEGYEL-----LKEKEALERQKEAIERQLASLEEELEKLTEEISELEKRLEEIEQLLEELNKKiKDLGEEEQLRvkeki 296

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159648420  779 -----EIAQLKKEQRKREHQLKLLEAQKRNQEVILRRKTEEVTALRRQVRPLSDKVAgKVSRKLslpehpiqepsssssv 853
Cdd:TIGR02169  297 geleaEIASLERSIAEKERELEDAEERLAKLEAEIDKLLAEIEELEREIEEERKRRD-KLTEEY---------------- 359

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159648420  854 ehdgsrIAAQQKMRIPVARVQALSvtATNGTGR----KYQRK--AVTSRVYSSRAARMKWQ-LLERRVTDIIMQRMTISN 926
Cdd:TIGR02169  360 ------AELKEELEDLRAELEEVD--KEFAETRdelkDYREKleKLKREINELKRELDRLQeELQRLSEELADLNAAIAG 431

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159648420  927 MEADMNRLLTQREELtkrREKLSKRREKLMkdgggsETDRNVQNINEEMESLTANIDYINDSISDCQANIMQMEEAK--- 1003
Cdd:TIGR02169  432 IEAKINELEEEKEDK---ALEIKKQEWKLE------QLAADLSKYEQELYDLKEEYDRVEKELSKLQRELAEAEAQAras 502

                          410
                   ....*....|....*.
gi 1159648420 1004 --EEGETLDVTAVINA 1017
Cdd:TIGR02169  503 eeRVRGGRAVEEVLKA 518
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 625-836 1.09e-12

Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 443969 [Multi-domain]  Cd Length: 377  Bit Score: 72.49  E-value: 1.09e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159648420  625 KENYQADLANITCEIAIKQKLIDELENSQRRLQTLKRQYEEKLMMLQHKIRDTQLERDQVLQNLGSVETySEEKAKKIKS 704
Cdd:COG4942     22 AAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEK-EIAELRAELE 100

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159648420  705 EYEKKLQTMNKELQR-------------------------LQTAQKEHARLLKNQSQYEKQLKKLQQEVTEMKKTKVRLM 759
Cdd:COG4942    101 AQKEELAELLRALYRlgrqpplalllspedfldavrrlqyLKYLAPARREQAEELRADLAELAALRAELEAERAELEALL 180

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159648420  760 KQMKEEQEKARMTESRRNREIAQLKKEQRKREHQLKLLEAQKRNQEVILRRKTEEVTALRRQVRPLSDK---------VA 830
Cdd:COG4942    181 AELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAERTPAAGFAalkgklpwpVS 260


                   ....*.
gi 1159648420  831 GKVSRK 836
Cdd:COG4942    261 GRVVRR 266
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
363-1009 2.49e-12

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 72.79  E-value: 2.49e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159648420  363 KYANRARNIKNKVMVNQDR---ASQQINALRSEIARLQMELMEYKTGKRIIdEEGVESINDMFHENAMLQTENNNLRVRI 439
Cdd:PRK03918   183 KFIKRTENIEELIKEKEKEleeVLREINEISSELPELREELEKLEKEVKEL-EELKEEIEELEKELESLEGSKRKLEEKI 261

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159648420  440 KAMQETVDALRARITQLmSDQANQV--LARAGEGNEEISNMIHNYIKEIEDLRAKL--LESEAvnENLRRNLSRastrst 515
Cdd:PRK03918   262 RELEERIEELKKEIEEL-EEKVKELkeLKEKAEEYIKLSEFYEEYLDELREIEKRLsrLEEEI--NGIEERIKE------ 332

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159648420  516 yfggpsafsasmLSSEKETLEildiakkdleklkkkerkkkksvkedntdnEQEKRDEKgsSERENNELE--AEEIQEAs 593
Cdd:PRK03918   333 ------------LEEKEERLE------------------------------ELKKKLKE--LEKRLEELEerHELYEEA- 367

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159648420  594 dredeeeeddededdmevvessdesDSDSDEKENYQADLANITCEiaikqKLIDELENSQRRlqtlKRQYEEKLMMLQHK 673
Cdd:PRK03918   368 -------------------------KAKKEELERLKKRLTGLTPE-----KLEKELEELEKA----KEEIEEEISKITAR 413

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159648420  674 IRDTQLERDQVLQNLGSVET-----------YSEEKAKKIKSEYEKKLQTMNKELQRLQTAQKEharLLKNQSQYEKQLK 742
Cdd:PRK03918   414 IGELKKEIKELKKAIEELKKakgkcpvcgreLTEEHRKELLEEYTAELKRIEKELKEIEEKERK---LRKELRELEKVLK 490

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159648420  743 KlQQEVTEMKKTkVRLMKQMKEEQEKARMTE-SRRNREIAQLKKEQRKREHQLKLLEaqkrnqevilrRKTEEVTALRRQ 821
Cdd:PRK03918   491 K-ESELIKLKEL-AEQLKELEEKLKKYNLEElEKKAEEYEKLKEKLIKLKGEIKSLK-----------KELEKLEELKKK 557

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159648420  822 VRPLSDKVaGKVSRKLSLPEHPIQEPSSSSSVEHDGsriaaqqkmripvaRVQALsvtatngtgRKYQRKAVTSRVYSSR 901
Cdd:PRK03918   558 LAELEKKL-DELEEELAELLKELEELGFESVEELEE--------------RLKEL---------EPFYNEYLELKDAEKE 613

                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159648420  902 AARMKwQLLERRVTDIIMQRMTISNMEADMNRLLTQREELTKR--REKLSKRREKLMkdgggsETDRNVQNINEEMESLT 979
Cdd:PRK03918   614 LEREE-KELKKLEEELDKAFEELAETEKRLEELRKELEELEKKysEEEYEELREEYL------ELSRELAGLRAELEELE 686

                          650       660       670
                   ....*....|....*....|....*....|
gi 1159648420  980 ANIDYINDSISDCQANIMQMEEAKEEGETL 1009
Cdd:PRK03918   687 KRREEIKKTLEKLKEELEEREKAKKELEKL 716
Trefoil pfam00088
Trefoil (P-type) domain;
1664-1703 2.54e-11

Trefoil (P-type) domain;


Pssm-ID: 459666  Cd Length: 43  Bit Score: 60.41  E-value: 2.54e-11
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|
gi 1159648420 1664 AVQKRIDCHPqPGASQEACEAQGCTWCATDVANAPWCFFS 1703
Cdd:pfam00088    5 PPSDRFDCGY-PGITQEECEARGCCWDPSVDPGVPWCFYP 43
PD smart00018
P or trefoil or TFF domain; Proposed role in renewal and pathology of mucous epithelia.
 1659-1702 7.26e-11

P or trefoil or TFF domain; Proposed role in renewal and pathology of mucous epithelia.


Pssm-ID: 197472  Cd Length: 46  Bit Score: 59.32  E-value: 7.26e-11
                            10        20        30        40
                    ....*....|....*....|....*....|....*....|....
gi 1159648420  1659 EQCTGAVQKRIDCHPqPGASQEACEAQGCTWCATDVaNAPWCFF 1702
Cdd:smart00018    1 AQCSVPPSERINCGP-PGITEAECEARGCCFDSSIS-GVPWCFY 42
Trefoil cd00111
P or trefoil or TFF domain; Trefoil factor family domain peptides are mucin-associated ...
 1659-1702 2.03e-10

P or trefoil or TFF domain; Trefoil factor family domain peptides are mucin-associated molecules, largely found in epithelia of gastrointestinal tissues. Function is not known but it was originally identified from mucosal tissues, where it may have a regulatory or structural role and has also been implicated as a growth fractor in other tissues.The domain is found in 1 to 6 copies where it occurs.


Pssm-ID: 238059  Cd Length: 44  Bit Score: 57.74  E-value: 2.03e-10
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....
gi 1159648420 1659 EQCTGAVQKRIDCHPqPGASQEACEAQGCTWcATDVANAPWCFF 1702
Cdd:cd00111      1 EWCSVPPSERIDCGP-PGITQEECEARGCCF-DPSISGVPWCFY 42
WD40 pfam00400
WD domain, G-beta repeat;
1315-1350 1.55e-06

WD domain, G-beta repeat;


Pssm-ID: 459801 [Multi-domain]  Cd Length: 39  Bit Score: 46.57  E-value: 1.55e-06
                           10        20        30
                   ....*....|....*....|....*....|....*...
gi 1159648420 1315 QCIYTAEGHTKAVLCVDATDD--LLFTGSKDRTCKVWN 1350
Cdd:pfam00400    2 KLLKTLEGHTGSVTSLAFSPDgkLLASGSDDGTVKVWD 39
WD40 smart00320
WD40 repeats; Note that these repeats are permuted with respect to the structural repeats ...
 1313-1350 5.37e-06

WD40 repeats; Note that these repeats are permuted with respect to the structural repeats (blades) of the beta propeller domain.


Pssm-ID: 197651 [Multi-domain]  Cd Length: 40  Bit Score: 45.38  E-value: 5.37e-06
                            10        20        30        40
                    ....*....|....*....|....*....|....*....|
gi 1159648420  1313 PLQCIYTAEGHTKAVLCVDATDD--LLFTGSKDRTCKVWN 1350
Cdd:smart00320    1 SGELLKTLKGHTGPVTSVAFSPDgkYLASGSDDGTIKLWD 40
Spc7 smart00787
Spc7 kinetochore protein; This domain is found in cell division proteins which are required ...
 690-842 3.05e-05

Spc7 kinetochore protein; This domain is found in cell division proteins which are required for kinetochore-spindle association.


Pssm-ID: 197874 [Multi-domain]  Cd Length: 312  Bit Score: 48.48  E-value: 3.05e-05
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159648420   690 SVETYSEEKAKK------------IKSEYEKKLQTMNKELQRL----QTAQKEHARLLKNQSQYEKQLKKLQQEVTEMKK 753
Cdd:smart00787  121 LVKTFARLEAKKmwyewrmkllegLKEGLDENLEGLKEDYKLLmkelELLNSIKPKLRDRKDALEEELRQLKQLEDELED 200

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159648420   754 TKVRLMKQMKEEQEKARMTESRRNREIAQLkkEQRKREHQLKLleAQKRNQEVILRRKTEEVTALRRQVRPLSDKVAGKV 833
Cdd:smart00787  201 CDPTELDRAKEKLKKLLQEIMIKVKKLEEL--EEELQELESKI--EDLTNKKSELNTEIAEAEKKLEQCRGFTFKEIEKL 276


                    ....*....
gi 1159648420   834 SRKLSLPEH 842
Cdd:smart00787  277 KEQLKLLQS 285
iSH2_PI3K_IA_R cd12923
Inter-Src homology 2 (iSH2) helical domain of Class IA Phosphoinositide 3-kinase Regulatory ...
 696-810 4.65e-05

Inter-Src homology 2 (iSH2) helical domain of Class IA Phosphoinositide 3-kinase Regulatory subunits; PI3Ks catalyze the transfer of the gamma-phosphoryl group from ATP to the 3-hydroxyl of the inositol ring of D-myo-phosphatidylinositol (PtdIns) or its derivatives. They play an important role in a variety of fundamental cellular processes, including cell motility, the Ras pathway, vesicle trafficking and secretion, immune cell activation, and apoptosis. They are classified according to their substrate specificity, regulation, and domain structure. Class IA PI3Ks are heterodimers of a p110 catalytic (C) subunit and a p85-related regulatory (R) subunit. The R subunit down-regulates PI3K basal activity, stabilizes the C subunit, and plays a role in the activation downstream of tyrosine kinases. All R subunits contain two SH2 domains that flank an intervening helical domain (iSH2), which binds to the N-terminal adaptor-binding domain (ABD) of the catalytic subunit. In vertebrates, there are three genes (PIK3R1, PIK3R2, and PIK3R3) that encode for different Class IA PI3K R subunits.


Pssm-ID: 214016 [Multi-domain]  Cd Length: 152  Bit Score: 45.68  E-value: 4.65e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159648420  696 EEKAKKIKsEYEKKLQTMNKELQRLQ--------------TAQ----------KEHARLL-----KNQSQYEKQL----K 742
Cdd:cd12923      4 EKLAKKLK-EINKEYLDKSREYDELYekynklsqeiqlkrQALeafeeavkmfEEQLRTQekfqkEAQPHEKQRLmennE 82

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1159648420  743 KLQQEVTEMKKTKVRLMKQMKEEQEKARMTESRRN---REIAQLKKEqrkREHQLKLLEAQKRNQEVILRR 810
Cdd:cd12923     83 LLKSRLKELEESKEQLEEDLRKQVAYNRELEREMNslkPELMQLRKQ---KDQYLRWLKRKGVSQEEINQL 150
Spc7 smart00787
Spc7 kinetochore protein; This domain is found in cell division proteins which are required ...
 939-1033 3.28e-03

Spc7 kinetochore protein; This domain is found in cell division proteins which are required for kinetochore-spindle association.


Pssm-ID: 197874 [Multi-domain]  Cd Length: 312  Bit Score: 42.31  E-value: 3.28e-03
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159648420   939 EELTKRREKLSKRREKLMkdgggsETDRNVQNINEEMESLTANIDYINDSISDCQANIMQMEEAKEEgetldvtavINAC 1018
Cdd:smart00787  204 TELDRAKEKLKKLLQEIM------IKVKKLEELEEELQELESKIEDLTNKKSELNTEIAEAEKKLEQ---------CRGF 268

                            90
                    ....*....|....*
gi 1159648420  1019 TLTEARYLLDHFLTM 1033
Cdd:smart00787  269 TFKEIEKLKEQLKLL 283
Gal_mutarotas_2 pfam13802
Galactose mutarotase-like; This family is found N-terminal to glycosyl-hydrolase domains, and ...
 1833-1892 4.15e-03

Galactose mutarotase-like; This family is found N-terminal to glycosyl-hydrolase domains, and appears to be similar to the galactose mutarotase superfamily.


Pssm-ID: 463987 [Multi-domain]  Cd Length: 67  Bit Score: 37.83  E-value: 4.15e-03
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1159648420 1833 VYGFGEqehesfkHSMDFV----TYGMFSRDQAPTPL--VNLYGVHPFYMCVEaDSNAHGVLLLNS 1892
Cdd:pfam13802    4 VYGLGE-------RAGPLNkrgtRYRLWNTDAFGYELdtDPLYKSIPFYISHN-GGRGYGVFWDNP 61
 
Name Accession Description Interval E-value
GH31_MGAM_SI_GAA cd06602
maltase-glucoamylase, sucrase-isomaltase, lysosomal acid alpha-glucosidase; This subgroup ...
 1936-2296 0e+00

maltase-glucoamylase, sucrase-isomaltase, lysosomal acid alpha-glucosidase; This subgroup includes the following three closely related glycosyl hydrolase family 31 (GH31) enzymes: maltase-glucoamylase (MGAM), sucrase-isomaltase (SI), and lysosomal acid alpha-glucosidase (GAA), also known as acid-maltase. MGAM is one of the two enzymes responsible for catalyzing the last glucose-releasing step in starch digestion. SI is implicated in the digestion of dietary starch and major disaccharides such as sucrose and isomaltose, while GAA degrades glycogen in the lysosome, cleaving both alpha-1,4 and alpha-1,6 glucosidic linkages. MGAM and SI are anchored to small-intestinal brush-border epithelial cells. The absence of SI from the brush border membrane or its malfunction is associated with malabsorption disorders such as congenital sucrase-isomaltase deficiency (CSID). The domain architectures of MGAM and SI include two tandem GH31 catalytic domains, an N-terminal domain found near the membrane-bound end, and a C-terminal luminal domain. Both of the tandem GH31 domains of MGAM and SI are included in this family. The domain architecture of GAA includes an N-terminal TFF (trefoil factor family) domain in addition to the GH31 catalytic domain. Deficient GAA expression causes Pompe disease, an autosomal recessive genetic disorder also known as glycogen storage disease type II (GSDII).


Pssm-ID: 269888  Cd Length: 367  Bit Score: 655.74  E-value: 0e+00
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159648420 1936 GRPHMPAYWSLGFHLSRWGYGSIDVLKETVNRMHYYDIPYDVQHLDIDYMERYMDFTYDKVNYAGLPEYIQKLKRKGMHN 2015
Cdd:cd06602      1 GRPAMPPYWSLGFHLCRWGYKNLDELKEVVERYRAAGIPLDVQWNDIDYMDRYRDFTLDPVNFPGLPAFVDDLHANGQHY 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159648420 2016 VVILDPFITKdEEPGTYRPYDLGEEMGVWVNNSDGvTPAVGKAWPpGDSVFPDYTNPRTAEWWTQMCLEFKDVLDYDGIW 2095
Cdd:cd06602     81 VPILDPGISA-NESGGYPPYDRGLEMDVFIKNDDG-SPYVGKVWP-GYTVFPDFTNPNTQEWWTEEIKDFHDQVPFDGLW 157

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159648420 2096 IDMNEPSNFLTG------QYPGCAVNDLNNPPYVPSIS-DHSLAQKTLCPDSKTYLGE-HYNTHSLFGWSQTAPTFHAAQ 2167
Cdd:cd06602    158 IDMNEPSNFCTGscgnspNAPGCPDNKLNNPPYVPNNLgGGSLSDKTICMDAVHYDGGlHYDVHNLYGLSEAIATYKALK 237

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159648420 2168 QA-TGKRAFVLSRSTFVGSGKHGGHWLGDNFSQWKDMHRSIVGILEFNLFGIPYIGADICGFNHNTTYELCLRWMQLGSF 2246
Cdd:cd06602    238 EIfPGKRPFIISRSTFPGSGKYAGHWLGDNYSTWEDMRYSIPGMLEFNLFGIPMVGADICGFNGNTTEELCARWMQLGAF 317

                          330       340       350       360       370
                   ....*....|....*....|....*....|....*....|....*....|
gi 1159648420 2247 YPFSRNHNAEGNREQDPAVFGAEFAEISRATLRIRYSLLPYLYTLFYESH 2296
Cdd:cd06602    318 YPFSRNHNDIGAIDQEPYVWGPSVADASRKALLIRYSLLPYLYTLFYRAH 367
Glyco_hydro_31 pfam01055
Glycosyl hydrolases family 31; Glycosyl hydrolases are key enzymes of carbohydrate metabolism. ...
 1917-2388 0e+00

Glycosyl hydrolases family 31; Glycosyl hydrolases are key enzymes of carbohydrate metabolism. Family 31 comprises of enzymes that are, or similar to, alpha- galactosidases.


Pssm-ID: 460044 [Multi-domain]  Cd Length: 443  Bit Score: 643.46  E-value: 0e+00
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159648420 1917 YVFLGPTPENVVQQYTEAIGRPHMPAYWSLGFHLSRWGYGSIDVLKETVNRMHYYDIPYDVQHLDIDYMERYMDFTYDKV 1996
Cdd:pfam01055    1 YFFLGPTPKDVVKQYTELTGRPPLPPYWALGYHQSRWGYKSEEEVLEVVDGFRERDIPLDVIWLDIDYMDGYRDFTWDPE 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159648420 1997 NYAGLPEYIQKLKRKGMHNVVILDPFITKDEEPgtYRPYDLGEEMGVWVNNSDGvTPAVGKaWPpGDSVFPDYTNPRTAE 2076
Cdd:pfam01055   81 RFPDPKGMVDELHAKGQKLVVIIDPGIKKVDPG--YPPYDEGLEKGYFVKNPDG-SLYVGG-WP-GMSAFPDFTNPEARD 155

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159648420 2077 WWTQMCLEFKDVLDYDGIWIDMNEPSNFltGQYPGCAVNDLNNPPYVPSisdhslaqktlcpdsktylgEHYNTHSLFGW 2156
Cdd:pfam01055  156 WWADQLFKFLLDMGVDGIWNDMNEPSVF--CGSGPEDTVAKDNDPGGGV--------------------EHYDVHNLYGL 213

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159648420 2157 SQTAPTFHAAQQATG-KRAFVLSRSTFVGSGKHGGHWLGDNFSQWKDMHRSIVGILEFNLFGIPYIGADICGFNHNTTYE 2235
Cdd:pfam01055  214 LMAKATYEGLREKRPnKRPFVLTRSGFAGSQRYAAHWSGDNTSTWEHLRFSIPGGLSLGLSGIPFWGADIGGFFNPTTPE 293

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159648420 2236 LCLRWMQLGSFYPFSRNHNAEGNREQDPAVFGAEFAEISRATLRIRYSLLPYLYTLFYESHVHGNTVARSLMHEFTSDQE 2315
Cdd:pfam01055  294 LYVRWYQLGAFSPFFRNHSSIDTRRREPWLFGEEVEEIIRKAIRLRYRLLPYLYTLFYEAHETGLPVMRPLFLEFPDDPN 373

                          410       420       430       440       450       460       470
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1159648420 2316 THGIDTAFLWGPAFMIAPVLQEGARSVDVYFPEATWFDYYTGHKVPstwKKNYATVAAPLSKIPLFIRGGYIL 2388
Cdd:pfam01055  374 TFDIDDQFMFGPSLLVAPVLEEGATSVDVYLPGGRWYDFWTGERYE---GGGTVPVTAPLDRIPLFVRGGSII 443
KISc_KIF4 cd01372
Kinesin motor domain, KIF4-like subfamily; Kinesin motor domain, KIF4-like subfamily. Members ...
 8-372 0e+00

Kinesin motor domain, KIF4-like subfamily; Kinesin motor domain, KIF4-like subfamily. Members of this group seem to perform a variety of functions, and have been implicated in neuronal organelle transport and chromosome segregation during mitosis. This catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Kinesins are microtubule-dependent molecular motors that play important roles in intracellular transport and in cell division. In most kinesins, the motor domain is found at the N-terminus (N-type). N-type kinesins are (+) end-directed motors, i.e. they transport cargo towards the (+) end of the microtubule. Kinesin motor domains hydrolyze ATP at a rate of about 80 per second, and move along the microtubule at a speed of about 6400 Angstroms per second. To achieve that, kinesin head groups work in pairs. Upon replacing ADP with ATP, a kinesin motor domain increases its affinity for microtubule binding and locks in place. Also, the neck linker binds to the motor domain, which repositions the other head domain through the coiled-coil domain close to a second tubulin dimer, about 80 Angstroms along the microtubule. Meanwhile, ATP hydrolysis takes place, and when the second head domain binds to the microtubule, the first domain again replaces ADP with ATP, triggering a conformational change that pulls the first domain forward.


Pssm-ID: 276823 [Multi-domain]  Cd Length: 341  Bit Score: 631.29  E-value: 0e+00
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159648420    8 SSVRVAVRIRPQLAKEKIEGCHICTSVTPGEPQVFLGKDKAFTFDYVFNIDSQQEEIYVQCIEKLIEGCFEGYNATVFAY 87
Cdd:cd01372      1 SSVRVAVRVRPLLPKEIIEGCRICVSFVPGEPQVTVGTDKSFTFDYVFDPSTEQEEVYNTCVAPLVDGLFEGYNATVLAY 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159648420   88 GQTGAGKTYTMGTGFDVNITEEEQGIISRAVKHLFRCIEEKKQAaikqglppPDFKVNAQFLELYNEEILDLFDTTRDid 167
Cdd:cd01372     81 GQTGSGKTYTMGTAYTAEEDEEQVGIIPRAIQHIFKKIEKKKDT--------FEFQLKVSFLEIYNEEIRDLLDPETD-- 150

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159648420  168 aknKKSNIKIHEDSAGGIYTVGVTTRTVNGESEMMQCLKLGALSRTTASTQMNVQSSRSHAIFTIHLCQTRVCPPfntdn 247
Cdd:cd01372    151 ---KKPTISIREDSKGGITIVGLTEVTVLSAEDMMSCLEQGSLSRTTASTAMNSQSSRSHAIFTITLEQTKKNGP----- 222

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159648420  248 atdnriISESSEMNEFETLTAKFHFVDLAGSERLKRTGATGERAKEGISINCGLLALGNVISALGDKSKKATHVPYRDSK 327
Cdd:cd01372    223 ------IAPMSADDKNSTFTSKFHFVDLAGSERLKRTGATGDRLKEGISINSGLLALGNVISALGDESKKGAHVPYRDSK 296

                          330       340       350       360
                   ....*....|....*....|....*....|....*....|....*
gi 1159648420  328 LTRLLQDSLGGNSQTLMIACVSPSDRDFMETLNTLKYANRARNIK 372
Cdd:cd01372    297 LTRLLQDSLGGNSHTLMIACVSPADSNFEETLNTLKYANRARNIK 341
Kinesin pfam00225
Kinesin motor domain;
15-371 5.97e-140

Kinesin motor domain;


Pssm-ID: 459720 [Multi-domain]  Cd Length: 326  Bit Score: 440.09  E-value: 5.97e-140
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159648420   15 RIRPQLAKEKIEGCHICTSVTPGEPQVFL-------GKDKAFTFDYVFNIDSQQEEIYVQCIEKLIEGCFEGYNATVFAY 87
Cdd:pfam00225    1 RVRPLNEREKERGSSVIVSVESVDSETVEsshltnkNRTKTFTFDKVFDPEATQEDVYEETAKPLVESVLEGYNVTIFAY 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159648420   88 GQTGAGKTYTMGTgfdvniTEEEQGIISRAVKHLFRCIEEKKQaaikqglpPPDFKVNAQFLELYNEEILDLFDTTrdid 167
Cdd:pfam00225   81 GQTGSGKTYTMEG------SDEQPGIIPRALEDLFDRIQKTKE--------RSEFSVKVSYLEIYNEKIRDLLSPS---- 142

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159648420  168 aKNKKSNIKIHEDSAGGIYTVGVTTRTVNGESEMMQCLKLGALSRTTASTQMNVQSSRSHAIFTIHLCQTRVcppfntdn 247
Cdd:pfam00225  143 -NKNKRKLRIREDPKKGVYVKGLTEVEVSSAEEVLELLQLGNKNRTVAATKMNEESSRSHAIFTITVEQRNR-------- 213

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159648420  248 atdnriisesSEMNEFETLTAKFHFVDLAGSERLKRTG-ATGERAKEGISINCGLLALGNVISALGDKSKKatHVPYRDS 326
Cdd:pfam00225  214 ----------STGGEESVKTGKLNLVDLAGSERASKTGaAGGQRLKEAANINKSLSALGNVISALADKKSK--HIPYRDS 281

                          330       340       350       360
                   ....*....|....*....|....*....|....*....|....*
gi 1159648420  327 KLTRLLQDSLGGNSQTLMIACVSPSDRDFMETLNTLKYANRARNI 371
Cdd:pfam00225  282 KLTRLLQDSLGGNSKTLMIANISPSSSNYEETLSTLRFASRAKNI 326
GH31_GANC_GANAB_alpha cd06603
neutral alpha-glucosidase C, neutral alpha-glucosidase AB; This subgroup includes the closely ...
 1936-2428 1.40e-139

neutral alpha-glucosidase C, neutral alpha-glucosidase AB; This subgroup includes the closely related glycosyl hydrolase family 31 (GH31) isozymes, neutral alpha-glucosidase C (GANC) and the alpha subunit of heterodimeric neutral alpha-glucosidase AB (GANAB). Initially distinguished on the basis of differences in electrophoretic mobility in starch gel, GANC and GANAB have been shown to have other differences, including those of substrate specificity. GANC and GANAB are key enzymes in glycogen metabolism that hydrolyze terminal, non-reducing 1,4-linked alpha-D-glucose residues from glycogen in the endoplasmic reticulum. The GANC/GANAB family includes the alpha-glucosidase II (ModA) from Dictyostelium discoideum as well as the alpha-glucosidase II (GLS2, or ROT2 - Reversal of TOR2 lethality protein 2) from Saccharomyces cerevisiae.


Pssm-ID: 269889  Cd Length: 467  Bit Score: 445.04  E-value: 1.40e-139
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159648420 1936 GRPHMPAYWSLGFHLSRWGYGSIDVLKETVNRMHYYDIPYDVQHLDIDYMERYMDFTYDKVNYAGLPEYIQKLKRKGMHN 2015
Cdd:cd06603      1 GTPPLPPLFALGYHQCRWNYNDQEDVLEVDANFDEHDIPYDVIWLDIEHTDGKRYFTWDKKKFPDPKKMQEKLASKGRKL 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159648420 2016 VVILDPFITKDEEpgtYRPYDLGEEMGVWVNNSDGvTPAVGKAWPpGDSVFPDYTNPRTAEWWTQMCL--EFKDVLDYDG 2093
Cdd:cd06603     81 VTIVDPHIKRDDD---YFVYKEAKEKDYFVKDSDG-KDFEGWCWP-GSSSWPDFLNPEVRDWWASLFSydKYKGSTENLY 155

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159648420 2094 IWIDMNEPSNFltgqypgcavndlNNPpyvpsisdhslaQKTLCPDSKTYLG-EHYNTHSLFGWSQTAPTF--HAAQQAT 2170
Cdd:cd06603    156 IWNDMNEPSVF-------------NGP------------EITMPKDAIHYGGvEHRDVHNIYGLYMHMATFegLLKRSNG 210

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159648420 2171 GKRAFVLSRSTFVGSGKHGGHWLGDNFSQWKDMHRSIVGILEFNLFGIPYIGADICGFNHNTTYELCLRWMQLGSFYPFS 2250
Cdd:cd06603    211 KKRPFVLTRSFFAGSQRYGAVWTGDNMATWEHLKISIPMLLSLSIAGIPFVGADVGGFFGNPDEELLVRWYQAGAFYPFF 290

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159648420 2251 RNHNAEGNREQDPAVFGAEFAEISRATLRIRYSLLPYLYTLFYESHVHGNTVARSLMHEFTSDQETHGIDTAFLWGPAFM 2330
Cdd:cd06603    291 RAHAHIDTKRREPWLFGEETTEIIREAIRLRYRLLPYWYTLFYEASRTGLPIMRPLWYEFPEDESTFDIDDQFMLGDSLL 370

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159648420 2331 IAPVLQEGARSVDVYFPEAT-WFDYYTGHKVPSTwkkNYATVAAPLSKIPLFIRGGYILPEQ-APASTTTKSRLNPFGLI 2408
Cdd:cd06603    371 VKPVVEEGATSVTVYLPGGEvWYDYFTGQRVTGG---GTKTVPVPLDSIPVFQRGGSIIPRKeRVRRSSKLMRNDPYTLV 447

                          490       500
                   ....*....|....*....|
gi 1159648420 2409 IALDEHGEASGSLFWDDGDS 2428
Cdd:cd06603    448 VALDENGEAEGELYLDDGES 467
KISc smart00129
Kinesin motor, catalytic domain. ATPase; Microtubule-dependent molecular motors that play ...
 9-378 1.57e-138

Kinesin motor, catalytic domain. ATPase; Microtubule-dependent molecular motors that play important roles in intracellular transport of organelles and in cell division.


Pssm-ID: 214526 [Multi-domain]  Cd Length: 335  Bit Score: 436.23  E-value: 1.57e-138
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159648420     9 SVRVAVRIRPQLAKEKIEGCHICTSVTPGEPQV-------FLGKDKAFTFDYVFNIDSQQEEIYVQCIEKLIEGCFEGYN 81
Cdd:smart00129    1 NIRVVVRVRPLNKREKSRKSPSVVPFPDKVGKTltvrspkNRQGEKKFTFDKVFDATASQEDVFEETAAPLVDSVLEGYN 80

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159648420    82 ATVFAYGQTGAGKTYTMGTgfdvniTEEEQGIISRAVKHLFRCIEEKKqaaikqglPPPDFKVNAQFLELYNEEILDLFD 161
Cdd:smart00129   81 ATIFAYGQTGSGKTYTMIG------TPDSPGIIPRALKDLFEKIDKRE--------EGWQFSVKVSYLEIYNEKIRDLLN 146

                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159648420   162 TTrdidaknkKSNIKIHEDSAGGIYTVGVTTRTVNGESEMMQCLKLGALSRTTASTQMNVQSSRSHAIFTIHLcqtrvcp 241
Cdd:smart00129  147 PS--------SKKLEIREDEKGGVYVKGLTEISVSSFEEVYNLLEKGNKNRTVAATKMNEESSRSHAVFTITV------- 211

                           250       260       270       280       290       300       310       320
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159648420   242 pfntdnatDNRIISESSEmnefETLTAKFHFVDLAGSERLKRTGATGERAKEGISINCGLLALGNVISALGDKSKKaTHV 321
Cdd:smart00129  212 --------EQKIKNSSSG----SGKASKLNLVDLAGSERAKKTGAEGDRLKEAGNINKSLSALGNVINALAQHSKS-RHI 278

                           330       340       350       360       370
                    ....*....|....*....|....*....|....*....|....*....|....*..
gi 1159648420   322 PYRDSKLTRLLQDSLGGNSQTLMIACVSPSDRDFMETLNTLKYANRARNIKNKVMVN 378
Cdd:smart00129  279 PYRDSKLTRLLQDSLGGNSKTLMIANVSPSSSNLEETLSTLRFASRAKEIKNKPIVN 335
KISc cd00106
Kinesin motor domain; Kinesin motor domain. This catalytic (head) domain has ATPase activity ...
 9-369 7.97e-122

Kinesin motor domain; Kinesin motor domain. This catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Kinesins are microtubule-dependent molecular motors that play important roles in intracellular transport and in cell division. In most kinesins, the motor domain is found at the N-terminus (N-type), in some its is found in the middle (M-type), or C-terminal (C-type). N-type and M-type kinesins are (+) end-directed motors, while C-type kinesins are (-) end-directed motors, i.e. they transport cargo towards the (-) end of the microtubule. Kinesin motor domains hydrolyze ATP at a rate of about 80 per second, and move along the microtubule at a speed of about 6400 Angstroms per second. To achieve that, kinesin head groups work in pairs. Upon replacing ADP with ATP, a kinesin motor domain increases its affinity for microtubule binding and locks in place. Also, the neck linker binds to the motor domain, which repositions the other head domain through the coiled-coil domain close to a second tubulin dimer, about 80 Angstroms along the microtubule. Meanwhile, ATP hydrolysis takes place, and when the second head domain binds to the microtubule, the first domain again replaces ADP with ATP, triggering a conformational change that pulls the first domain forward.


Pssm-ID: 276812 [Multi-domain]  Cd Length: 326  Bit Score: 388.15  E-value: 7.97e-122
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159648420    9 SVRVAVRIRPQLAKEKiEGCHICTSVTPG------EPQVFLGKDKAFTFDYVFNIDSQQEEIYVQCIEKLIEGCFEGYNA 82
Cdd:cd00106      1 NVRVAVRVRPLNGREA-RSAKSVISVDGGksvvldPPKNRVAPPKTFAFDAVFDSTSTQEEVYEGTAKPLVDSALEGYNG 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159648420   83 TVFAYGQTGAGKTYTMGtgfdvNITEEEQGIISRAVKHLFRCIEEKKqaaikqgLPPPDFKVNAQFLELYNEEILDLFDt 162
Cdd:cd00106     80 TIFAYGQTGSGKTYTML-----GPDPEQRGIIPRALEDIFERIDKRK-------ETKSSFSVSASYLEIYNEKIYDLLS- 146

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159648420  163 trdidaKNKKSNIKIHEDSAGGIYTVGVTTRTVNGESEMMQCLKLGALSRTTASTQMNVQSSRSHAIFTIHLcqtrvcpp 242
Cdd:cd00106    147 ------PVPKKPLSLREDPKRGVYVKGLTEVEVGSLEDALELLDAGNKNRTTASTNMNEHSSRSHAVFTIHV-------- 212

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159648420  243 fntdnatDNRIISESSEMnefeTLTAKFHFVDLAGSERLKRTGATGERAKEGISINCGLLALGNVISALGDKSKKatHVP 322
Cdd:cd00106    213 -------KQRNREKSGES----VTSSKLNLVDLAGSERAKKTGAEGDRLKEGGNINKSLSALGKVISALADGQNK--HIP 279

                          330       340       350       360
                   ....*....|....*....|....*....|....*....|....*..
gi 1159648420  323 YRDSKLTRLLQDSLGGNSQTLMIACVSPSDRDFMETLNTLKYANRAR 369
Cdd:cd00106    280 YRDSKLTRLLQDSLGGNSKTIMIACISPSSENFEETLSTLRFASRAK 326
GH31_glucosidase_II_MalA cd06604
Alpha-glucosidase II-like; Alpha-glucosidase II (alpha-D-glucoside glucohydrolase) is a ...
 1936-2296 4.62e-113

Alpha-glucosidase II-like; Alpha-glucosidase II (alpha-D-glucoside glucohydrolase) is a glycosyl hydrolase family 31 (GH31) enzyme, found in bacteria and plants, which has exo-alpha-1,4-glucosidase and oligo-1,6-glucosidase activities. Alpha-glucosidase II has been characterized in Bacillus thermoamyloliquefaciens where it forms a homohexamer. This subgroup also includes the MalA alpha-glucosidase from Sulfolobus solfataricus and the AglA alpha-glucosidase from Picrophilus torridus. MalA is part of the carbohydrate-metabolizing machinery that allows this organism to utilize carbohydrates, such as maltose, as the sole carbon and energy source.


Pssm-ID: 269890 [Multi-domain]  Cd Length: 339  Bit Score: 363.37  E-value: 4.62e-113
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159648420 1936 GRPHMPAYWSLGFHLSRWGYGSIDVLKETVNRMHYYDIPYDVQHLDIDYMERYMDFTYDKVNYAGLPEYIQKLKRKGMHN 2015
Cdd:cd06604      1 GRPPLPPKWALGYQQSRWSYYPEEEVREVAKGFRERDIPCDAIYLDIDYMDGYRVFTWDKERFPDPKELIKELHEQGFRL 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159648420 2016 VVILDPFITKDEEpgtYRPYDLGEEMGVWVNNSDGvTPAVGKAWPpGDSVFPDYTNPRTAEWWTQmclEFKDVLDY--DG 2093
Cdd:cd06604     81 VTIVDPGVKVDPG---YEVYEEGLENDYFVKDPDG-ELYVGKVWP-GKSVFPDFTNPEVREWWGD---LYKELVDLgvDG 152

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159648420 2094 IWIDMNEPsnfltgqypgcAVNDLNNPPYVPSISDHSLAQKTlcpdsktylGEHYNTHSLFGWSQTAPTFHA-AQQATGK 2172
Cdd:cd06604    153 IWNDMNEP-----------AVFNAPGGTTMPLDAVHRLDGGK---------ITHEEVHNLYGLLMARATYEGlRRLRPNK 212

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159648420 2173 RAFVLSRSTFVGSGKHGGHWLGDNFSQWKDMHRSIVGILEFNLFGIPYIGADICGFNHNTTYELCLRWMQLGSFYPFSRN 2252
Cdd:cd06604    213 RPFVLSRAGYAGIQRYAAIWTGDNSSSWEHLRLSIPMLLNLGLSGVPFVGADIGGFAGDPSPELLARWYQLGAFFPFFRN 292

                          330       340       350       360
                   ....*....|....*....|....*....|....*....|....
gi 1159648420 2253 HNAEGNREQDPAVFGAEFAEISRATLRIRYSLLPYLYTLFYESH 2296
Cdd:cd06604    293 HSAKGTRDQEPWAFGEEVEEIARKAIELRYRLLPYLYTLFYEAH 336
KISc_KIF3 cd01371
Kinesin motor domain, kinesins II or KIF3_like proteins; Kinesin motor domain, kinesins II or ...
 9-371 3.06e-107

Kinesin motor domain, kinesins II or KIF3_like proteins; Kinesin motor domain, kinesins II or KIF3_like proteins. Subgroup of kinesins, which form heterotrimers composed of 2 kinesins and one non-motor accessory subunit. Kinesins II play important roles in ciliary transport, and have been implicated in neuronal transport, melanosome transport, the secretory pathway, and mitosis. This catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Kinesins are microtubule-dependent molecular motors that play important roles in intracellular transport and in cell division. In this group the motor domain is found at the N-terminus (N-type). N-type kinesins are (+) end-directed motors, i.e. they transport cargo towards the (+) end of the microtubule. Kinesin motor domains hydrolyze ATP at a rate of about 80 per second, and move along the microtubule at a speed of about 6400 Angstroms per second. To achieve that, kinesin head groups work in pairs. Upon replacing ADP with ATP, a kinesin motor domain increases its affinity for microtubule binding and locks in place. Also, the neck linker binds to the motor domain, which repositions the other head domain through the coiled-coil domain close to a second tubulin dimer, about 80 Angstroms along the microtubule. Meanwhile, ATP hydrolysis takes place, and when the second head domain binds to the microtubule, the first domain again replaces ADP with ATP, triggering a conformational change that pulls the first domain forward.


Pssm-ID: 276822 [Multi-domain]  Cd Length: 334  Bit Score: 346.37  E-value: 3.06e-107
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159648420    9 SVRVAVRIRPQLAKEKIEGCHICTSVTPGEPQVFLGKDKA--------FTFDYVFNIDSQQEEIYVQCIEKLIEGCFEGY 80
Cdd:cd01371      2 NVKVVVRCRPLNGKEKAAGALQIVDVDEKRGQVSVRNPKAtaneppktFTFDAVFDPNSKQLDVYDETARPLVDSVLEGY 81

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159648420   81 NATVFAYGQTGAGKTYTMGtGFDVNitEEEQGIISRAVKHLFRCIEEKKQAAikqglpppDFKVNAQFLELYNEEIldlf 160
Cdd:cd01371     82 NGTIFAYGQTGTGKTYTME-GKRED--PELRGIIPNSFAHIFGHIARSQNNQ--------QFLVRVSYLEIYNEEI---- 146

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159648420  161 dttRDIDAKNKKSNIKIHEDSAGGIYTVGVTTRTVNGESEMMQCLKLGALSRTTASTQMNVQSSRSHAIFTIhlcqTRVC 240
Cdd:cd01371    147 ---RDLLGKDQTKRLELKERPDTGVYVKDLSMFVVKNADEMEHVMNLGNKNRSVGATNMNEDSSRSHAIFTI----TIEC 219

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159648420  241 ppfntdnatdnriiSESSEMNEFETLTAKFHFVDLAGSERLKRTGATGERAKEGISINCGLLALGNVISALGDKskKATH 320
Cdd:cd01371    220 --------------SEKGEDGENHIRVGKLNLVDLAGSERQSKTGATGERLKEATKINLSLSALGNVISALVDG--KSTH 283

                          330       340       350       360       370
                   ....*....|....*....|....*....|....*....|....*....|.
gi 1159648420  321 VPYRDSKLTRLLQDSLGGNSQTLMIACVSPSDRDFMETLNTLKYANRARNI 371
Cdd:cd01371    284 IPYRDSKLTRLLQDSLGGNSKTVMCANIGPADYNYDETLSTLRYANRAKNI 334
KISc_C_terminal cd01366
Kinesin motor domain, KIFC2/KIFC3/ncd-like carboxy-terminal kinesins; Kinesin motor domain, ...
 10-373 9.97e-105

Kinesin motor domain, KIFC2/KIFC3/ncd-like carboxy-terminal kinesins; Kinesin motor domain, KIFC2/KIFC3/ncd-like carboxy-terminal kinesins. Ncd is a spindle motor protein necessary for chromosome segregation in meiosis. KIFC2/KIFC3-like kinesins have been implicated in motility of the Golgi apparatus as well as dentritic and axonal transport in neurons. This catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Kinesins are microtubule-dependent molecular motors that play important roles in intracellular transport and in cell division. In this subgroup the motor domain is found at the C-terminus (C-type). C-type kinesins are (-) end-directed motors, i.e. they transport cargo towards the (-) end of the microtubule. Kinesin motor domains hydrolyze ATP at a rate of about 80 per second, and move along the microtubule at a speed of about 6400 Angstroms per second. To achieve that, kinesin head groups work in pairs. Upon replacing ADP with ATP, a kinesin motor domain increases its affinity for microtubule binding and locks in place. Also, the neck linker binds to the motor domain, which repositions the other head domain through the coiled-coil domain close to a second tubulin dimer, about 80 Angstroms along the microtubule. Meanwhile, ATP hydrolysis takes place, and when the second head domain binds to the microtubule, the first domain again replaces ADP with ATP, triggering a conformational change that pulls the first domain forward.


Pssm-ID: 276817 [Multi-domain]  Cd Length: 329  Bit Score: 339.18  E-value: 9.97e-105
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159648420   10 VRVAVRIRPQLAKEKIE-GCHICTSVTPGEPQVFLGKD---KAFTFDYVFNIDSQQEEIYVQcIEKLIEGCFEGYNATVF 85
Cdd:cd01366      4 IRVFCRVRPLLPSEENEdTSHITFPDEDGQTIELTSIGakqKEFSFDKVFDPEASQEDVFEE-VSPLVQSALDGYNVCIF 82

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159648420   86 AYGQTGAGKTYTMgTGfdvniTEEEQGIISRAVKHLFRCIEEKKQAAIKqglpppdFKVNAQFLELYNEEILDLFDTTRd 165
Cdd:cd01366     83 AYGQTGSGKTYTM-EG-----PPESPGIIPRALQELFNTIKELKEKGWS-------YTIKASMLEIYNETIRDLLAPGN- 148

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159648420  166 idAKNKKSNIKiHEDSAGGIYTVGVTTRTVNGESEMMQCLKLGALSRTTASTQMNVQSSRSHAIFTIHLcqtrvcppfnt 245
Cdd:cd01366    149 --APQKKLEIR-HDSEKGDTTVTNLTEVKVSSPEEVRQLLKKASKNRSTASTAMNEHSSRSHSVFILHI----------- 214

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159648420  246 dnatdnRIISESSEmnefETLTAKFHFVDLAGSERLKRTGATGERAKEGISINCGLLALGNVISALgdkSKKATHVPYRD 325
Cdd:cd01366    215 ------SGRNLQTG----EISVGKLNLVDLAGSERLNKSGATGDRLKETQAINKSLSALGDVISAL---RQKQSHIPYRN 281

                          330       340       350       360
                   ....*....|....*....|....*....|....*....|....*...
gi 1159648420  326 SKLTRLLQDSLGGNSQTLMIACVSPSDRDFMETLNTLKYANRARNIKN 373
Cdd:cd01366    282 SKLTYLLQDSLGGNSKTLMFVNISPAESNLNETLNSLRFASKVNSCEL 329
KISc_KIP3_like cd01370
Kinesin motor domain, KIP3-like subgroup; Kinesin motor domain, KIP3-like subgroup. The yeast ...
 9-371 5.35e-104

Kinesin motor domain, KIP3-like subgroup; Kinesin motor domain, KIP3-like subgroup. The yeast kinesin KIP3 plays a role in positioning the mitotic spindle. This catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Kinesins are microtubule-dependent molecular motors that play important roles in intracellular transport and in cell division. In most kinesins, the motor domain is found at the N-terminus (N-type). N-type kinesins are (+) end-directed motors, i.e. they transport cargo towards the (+) end of the microtubule. Kinesin motor domains hydrolyze ATP at a rate of about 80 per second, and move along the microtubule at a speed of about 6400 Angstroms per second. To achieve that, kinesin head groups work in pairs. Upon replacing ADP with ATP, a kinesin motor domain increases its affinity for microtubule binding and locks in place. Also, the neck linker binds to the motor domain, which repositions the other head domain through the coiled-coil domain close to a second tubulin dimer, about 80 Angstroms along the microtubule. Meanwhile, ATP hydrolysis takes place, and when the second head domain binds to the microtubule, the first domain again replaces ADP with ATP, triggering a conformational change that pulls the first domain forward.


Pssm-ID: 276821 [Multi-domain]  Cd Length: 345  Bit Score: 337.78  E-value: 5.35e-104
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159648420    9 SVRVAVRIRPQLAKEKIEGCHICTSVTPGEPQVF----------------------LGKDKAFTFDYVFNIDSQQEEIYV 66
Cdd:cd01370      1 SLTVAVRVRPFSEKEKNEGFRRIVKVMDNHMLVFdpkdeedgffhggsnnrdrrkrRNKELKYVFDRVFDETSTQEEVYE 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159648420   67 QCIEKLIEGCFEGYNATVFAYGQTGAGKTYTMgTGfdvniTEEEQGIISRAVKHLFRCIEEKKQAAikqglpppDFKVNA 146
Cdd:cd01370     81 ETTKPLVDGVLNGYNATVFAYGATGAGKTHTM-LG-----TPQEPGLMVLTMKELFKRIESLKDEK--------EFEVSM 146

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159648420  147 QFLELYNEEILDLFdttrdidaKNKKSNIKIHEDSAGGIYTVGVTTRTVNGESEMMQCLKLGALSRTTASTQMNVQSSRS 226
Cdd:cd01370    147 SYLEIYNETIRDLL--------NPSSGPLELREDAQNGIVVAGLTEHSPKSAEEILELLMKGNRNRTQEPTDANATSSRS 218

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159648420  227 HAIFTIHLCQTRvcppfNTDNATDNriisessemnefeTLTAKFHFVDLAGSERLKRTGATGERAKEGISINCGLLALGN 306
Cdd:cd01370    219 HAVLQITVRQQD-----KTASINQQ-------------VRQGKLSLIDLAGSERASATNNRGQRLKEGANINRSLLALGN 280

                          330       340       350       360       370       380
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1159648420  307 VISALGDKSKKATHVPYRDSKLTRLLQDSLGGNSQTLMIACVSPSDRDFMETLNTLKYANRARNI 371
Cdd:cd01370    281 CINALADPGKKNKHIPYRDSKLTRLLKDSLGGNCRTVMIANISPSSSSYEETHNTLKYANRAKNI 345
YicI COG1501
Alpha-glucosidase/xylosidase, GH31 family [Carbohydrate transport and metabolism];
1829-2429 3.11e-102

Alpha-glucosidase/xylosidase, GH31 family [Carbohydrate transport and metabolism];


Pssm-ID: 441110 [Multi-domain]  Cd Length: 609  Bit Score: 342.91  E-value: 3.11e-102
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159648420 1829 PSTSVYGFGEQEHESFKHSMDFVTYGMfsrDQAPTPLV-NLYGVHPFYMcveaDSNAHGVLLlNSN---AQDVSLSPDPS 1904
Cdd:COG1501     60 LGEQIYGLGERFTTLHKRGRIVVNWNL---DHGGHKDNgNTYAPIPFYV----SSKGYGVFV-NSAsyvTFDVGSAYSDL 131

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159648420 1905 VTFRTIGGILDFYVFLGPTPENVVQQYTEAIGRPHMPAYWSLGFHLSRWGYGSIDVLKETVNRMHYYDIPYDVQHLDIDY 1984
Cdd:COG1501    132 VEFTVPGDSLEFYVIEGPSPEDVLEKYTELTGKPPLPPRWAFGYWQSRKSYYDQDQVLAFADEFRDRGFPLDVIHLDIRW 211

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159648420 1985 MERYM--DFTYDKVNYAGLPEYIQKLKRKGMHNVVILDPFItkDEEPGTYRpydlgEEMGVWVNNSDGvTPAVGKAWPpG 2062
Cdd:COG1501    212 MDKYYwgDFEWDPRRFPDPKAMVKELHDRGVKLVLWINPYV--APDSAIFA-----EGMANFVKIASG-TVFVGKMWP-G 282

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159648420 2063 DSVFPDYTNPRTAEWWtQMCLEfKDVLDY--DGIWIDMNEpsnfltgqypgcavndlnNPPYVPSISDHSLAQKTlcpds 2140
Cdd:COG1501    283 TTGLLDFTRPDAREWF-WAGLE-KELLSIgvDGIKLDMNE------------------GWPTDVATFPSNVPQQM----- 337

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159648420 2141 ktylgehyntHSLFGWSQTAPTFHAAQQATGKRAFVLSRSTFVGSGKHGGHWLGDNFSQWKDMHRSIVGILEFNLFGIPY 2220
Cdd:COG1501    338 ----------RNLYGLLEAKATFEGFRTSRNNRTFILTRSGFAGGQRYPVIWTGDNTSSWESLEDQLTQGLNLSLSGVPF 407

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159648420 2221 IGADICGFNHNTTYELCLRWMQLGSFYPFSRNHNAEGNREqdPAVFGAEFAEISRATLRIRYSLLPYLYTLFYESHVHGN 2300
Cdd:COG1501    408 WTPDIGGFFGSPSRELWIRWFQVGAFSPFARIHGWASSTE--PWFFDEEAKQIVKEYAQLRYRLLPYIYSLFAKASTDGT 485

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159648420 2301 TVARSLMHEFTSDQETHGIDTAFLWGPAFMIAPVLqEGARSVDVYFPEATWFDYYTGHKVP-STWkknyATVAAPLSKIP 2379
Cdd:COG1501    486 PVIRPLFLEFPDDPTTRFIDDQYMFGEYLLVAPIF-AGTESRLVYLPKGKWYDFWTGELIEgGQW----ITVTAPLDRLP 560

                          570       580       590       600       610
                   ....*....|....*....|....*....|....*....|....*....|.
gi 1159648420 2380 LFIRGGYILPeQAPASTTTK-SRLNPFGLIIALDehGEASGSLFWDDGDSI 2429
Cdd:COG1501    561 LYVRDGSIIP-LGPVSLRPSmQKIDGIELRVYGS--GETAYTLYDDDGETV 608
KISc_KIF1A_KIF1B cd01365
Kinesin motor domain, KIF1_like proteins; Kinesin motor domain, KIF1_like proteins. KIF1A ...
 8-378 1.18e-100

Kinesin motor domain, KIF1_like proteins; Kinesin motor domain, KIF1_like proteins. KIF1A (Unc104) transports synaptic vesicles to the nerve terminal, KIF1B has been implicated in transport of mitochondria. Both proteins are expressed in neurons. This catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Kinesins are microtubule-dependent molecular motors that play important roles in intracellular transport and in cell division. In most kinesins, the motor domain is found at the N-terminus (N-type). N-type kinesins are (+) end-directed motors, i.e. they transport cargo towards the (+) end of the microtubule. In contrast to the majority of dimeric kinesins, most KIF1A/Unc104 kinesins are monomeric motors. A lysine-rich loop in KIF1A binds to the negatively charged C-terminus of tubulin and compensates for the lack of a second motor domain, allowing KIF1A to move processively.


Pssm-ID: 276816 [Multi-domain]  Cd Length: 361  Bit Score: 328.54  E-value: 1.18e-100
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159648420    8 SSVRVAVRIRPQLAKEKIEGCHIC-------TSVTPGEPQVFLGKD-----KAFTFDYVF-NIDSQ------QEEIYvQC 68
Cdd:cd01365      1 ANVKVAVRVRPFNSREKERNSKCIvqmsgkeTTLKNPKQADKNNKAtrevpKSFSFDYSYwSHDSEdpnyasQEQVY-ED 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159648420   69 I-EKLIEGCFEGYNATVFAYGQTGAGKTYTMgTGFDvniteEEQGIISRAVKHLFRCIEEKKQAAIKqglpppdFKVNAQ 147
Cdd:cd01365     80 LgEELLQHAFEGYNVCLFAYGQTGSGKSYTM-MGTQ-----EQPGIIPRLCEDLFSRIADTTNQNMS-------YSVEVS 146

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159648420  148 FLELYNEEILDLFDTtrdiDAKNKKSNIKIHEDSAGGIYTVGVTTRTVNGESEMMQCLKLGALSRTTASTQMNVQSSRSH 227
Cdd:cd01365    147 YMEIYNEKVRDLLNP----KPKKNKGNLKVREHPVLGPYVEDLSKLAVTSYEDIQDLMDEGNKSRTVAATNMNDTSSRSH 222

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159648420  228 AIFTIHLCQTRvcppfnTDNATDNRIiSESSEMNefetltakfhFVDLAGSERLKRTGATGERAKEGISINCGLLALGNV 307
Cdd:cd01365    223 AVFTIVLTQKR------HDAETNLTT-EKVSKIS----------LVDLAGSERASSTGATGDRLKEGANINKSLTTLGKV 285

                          330       340       350       360       370       380       390
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1159648420  308 ISALGD-----KSKKATHVPYRDSKLTRLLQDSLGGNSQTLMIACVSPSDRDFMETLNTLKYANRARNIKNKVMVN 378
Cdd:cd01365    286 ISALADmssgkSKKKSSFIPYRDSVLTWLLKENLGGNSKTAMIAAISPADINYEETLSTLRYADRAKKIVNRAVVN 361
KISc_BimC_Eg5 cd01364
Kinesin motor domain, BimC/Eg5 spindle pole proteins; Kinesin motor domain, BimC/Eg5 spindle ...
 7-380 4.05e-98

Kinesin motor domain, BimC/Eg5 spindle pole proteins; Kinesin motor domain, BimC/Eg5 spindle pole proteins, participate in spindle assembly and chromosome segregation during cell division. This catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Kinesins are microtubule-dependent molecular motors that play important roles in intracellular transport and in cell division. In most kinesins, the motor domain is found at the N-terminus (N-type), N-type kinesins are (+) end-directed motors, i.e. they transport cargo towards the (+) end of the microtubule. Kinesin motor domains hydrolyze ATP at a rate of about 80 per second, and move along the microtubule at a speed of about 6400 Angstroms per second. To achieve that, kinesin head groups work in pairs. Upon replacing ADP with ATP, a kinesin motor domain increases its affinity for microtubule binding and locks in place. Also, the neck linker binds to the motor domain, which repositions the other head domain through the coiled-coil domain close to a second tubulin dimer, about 80 Angstroms along the microtubule. Meanwhile, ATP hydrolysis takes place, and when the second head domain binds to the microtubule, the first domain again replaces ADP with ATP, triggering a conformational change that pulls the first domain forward.


Pssm-ID: 276815 [Multi-domain]  Cd Length: 353  Bit Score: 321.20  E-value: 4.05e-98
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159648420    7 ESSVRVAVRIRPQLAKEKIEGCHICTSVTPGEPQVFL--------GKDKAFTFDYVFNIDSQQEEIYVQCIEKLIEGCFE 78
Cdd:cd01364      1 GKNIQVVVRCRPFNLRERKASSHSVVEVDPVRKEVSVrtggladkSSTKTYTFDMVFGPEAKQIDVYRSVVCPILDEVLM 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159648420   79 GYNATVFAYGQTGAGKTYTM----GTGFDVNITE-EEQGIISRAVKHLFRCIEEKKQaaikqglpppDFKVNAQFLELYN 153
Cdd:cd01364     81 GYNCTIFAYGQTGTGKTYTMegdrSPNEEYTWELdPLAGIIPRTLHQLFEKLEDNGT----------EYSVKVSYLEIYN 150

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159648420  154 EEILDLFDttrdiDAKNKKSNIKIHEDSA--GGIYTVGVTTRTVNGESEMMQCLKLGALSRTTASTQMNVQSSRSHAIFT 231
Cdd:cd01364    151 EELFDLLS-----PSSDVSERLRMFDDPRnkRGVIIKGLEEITVHNKDEVYQILEKGAAKRKTAATLMNAQSSRSHSVFS 225

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159648420  232 IHLcqtrvcppfntdnatdnrIISESSEMNEFETLTAKFHFVDLAGSERLKRTGATGERAKEGISINCGLLALGNVISAL 311
Cdd:cd01364    226 ITI------------------HIKETTIDGEELVKIGKLNLVDLAGSENIGRSGAVDKRAREAGNINQSLLTLGRVITAL 287

                          330       340       350       360       370       380
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1159648420  312 GDKSKkatHVPYRDSKLTRLLQDSLGGNSQTLMIACVSPSDRDFMETLNTLKYANRARNIKNKVMVNQD 380
Cdd:cd01364    288 VERAP---HVPYRESKLTRLLQDSLGGRTKTSIIATISPASVNLEETLSTLEYAHRAKNIKNKPEVNQK 353
alpha_gluc_MalA NF040948
alpha-glucosidase MalA;
1833-2389 2.68e-97

alpha-glucosidase MalA;


Pssm-ID: 468879 [Multi-domain]  Cd Length: 626  Bit Score: 328.91  E-value: 2.68e-97
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159648420 1833 VYGFGEQEHESFKHSMDFVTY----GMFSRDQAPtplvnLYGVHPFYMCVEaDSNAHGvLLLNSNAQ---DVSLS----- 1900
Cdd:NF040948    63 VLGLGEKAFELDRRRGRFIMYnvdaGAYTKYSDP-----LYVSIPFFISVK-GGKATG-YFVNSPSKlifDIGLErydkv 135

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159648420 1901 ----PDPSVtfrtiggilDFYVFLGPTPENVVQQYTEAIGRPHMPAYWSLGFHLSRWGYGSIDVLKETVNRMHYYDIPYD 1976
Cdd:NF040948   136 kitiPENSV---------ELYVIEGPTIEEVLETYSELTGKPFLPPKWALGYQISRYSYYPQDAVVEVVDELRKEGFPVS 206

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159648420 1977 VQHLDIDYMERYMDFTYDKVNYAGLPEYIQKLKRKGMHNVVILDPFITKDEepgTYRPYDLGeeMGVWVNNSDGvTPAVG 2056
Cdd:NF040948   207 AVYLDIDYMDSYKLFTWDKEKFPDPRKFIEELHSRGVKVITIVDPSVKADQ---NYEVFRSG--LGKYCETENG-ELYVG 280

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159648420 2057 KAWPpGDSVFPDYTNPRTAEWWTQMCLEFKDVLDYDGIWIDMNEPSNF-LTGQYPGCAVNDLNNPPYVPSISDHSLAQkt 2135
Cdd:NF040948   281 KLWP-GNSVFPDFLNEETREWWAELVEEWVKQYGVDGIWLDMNEPTDFtEDIERAALGPHQLREDRLLYTFPPGAVHR-- 357

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159648420 2136 LCPDSKTYLGEHYNTHSLFgwsQTAPTFHAAQQATGKRAFVLSRSTFVGSGKHGGHWLGDNFSQWKDMHRSIVGILEFNL 2215
Cdd:NF040948   358 LDDGKKVKHEKVRNAYPYF---EAMATYEGLKRAGKDEPFILSRSGYAGIQRYAAIWTGDNTSSWDDLKLQLQLVLGLSI 434

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159648420 2216 FGIPYIGADICGF-----NHNTTYELCLRWMQLGSFYPFSRNHNAEGNREQDPAVFGAEFAEISRATLRIRYSLLPYLYT 2290
Cdd:NF040948   435 SGVPYVGCDIGGFagrsfPIDNSPELLVRYYQAALFFPLFRTHKSKDGNDQEPYFLPSKYKEKVKRVIKLRYKFLPYLYS 514

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159648420 2291 LFYESHVHGNTVARSLMHEFTSDQETHGIDTAFLWGPAFMIAPVLQEGARSVDVYFPEATWFDYYTG--HKVPStWKKNY 2368
Cdd:NF040948   515 LAWEAHETGHPIIRPLFYEFQDDEDAYRIEDEYMVGKYLLYAPQIYPKEESRDVYLPRGKWLDFWTGeeYEGPS-WIESE 593

                          570       580
                   ....*....|....*....|.
gi 1159648420 2369 AtvaaplsKIPLFIRGGYILP 2389
Cdd:NF040948   594 A-------ELPIYIREGSAVP 607
KISc_KHC_KIF5 cd01369
Kinesin motor domain, kinesin heavy chain (KHC) or KIF5-like subgroup; Kinesin motor domain, ...
 7-371 5.65e-97

Kinesin motor domain, kinesin heavy chain (KHC) or KIF5-like subgroup; Kinesin motor domain, kinesin heavy chain (KHC) or KIF5-like subgroup. Members of this group have been associated with organelle transport. This catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Kinesins are microtubule-dependent molecular motors that play important roles in intracellular transport and in cell division. In most kinesins, the motor domain is found at the N-terminus (N-type). N-type kinesins are (+) end-directed motors, i.e. they transport cargo towards the (+) end of the microtubule. Kinesin motor domains hydrolyze ATP at a rate of about 80 per second, and move along the microtubule at a speed of about 6400 Angstroms per second. To achieve that, kinesin head groups work in pairs. Upon replacing ADP with ATP, a kinesin motor domain increases its affinity for microtubule binding and locks in place. Also, the neck linker binds to the motor domain, which repositions the other head domain through the coiled-coil domain close to a second tubulin dimer, about 80 Angstroms along the microtubule. Meanwhile, ATP hydrolysis takes place, and when the second head domain binds to the microtubule, the first domain again replaces ADP with ATP, triggering a conformational change that pulls the first domain forward.


Pssm-ID: 276820 [Multi-domain]  Cd Length: 325  Bit Score: 316.58  E-value: 5.65e-97
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159648420    7 ESSVRVAVRIRPQLAKEKIEGCHICTSVTPGEPQVFLGKD--KAFTFDYVFNIDSQQEEIYVQCIEKLIEGCFEGYNATV 84
Cdd:cd01369      1 ECNIKVVCRFRPLNELEVLQGSKSIVKFDPEDTVVIATSEtgKTFSFDRVFDPNTTQEDVYNFAAKPIVDDVLNGYNGTI 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159648420   85 FAYGQTGAGKTYTMgtgFDVNITEEEQGIISRAVKHLFRCIEEKKQAAikqglpppDFKVNAQFLELYNEEILDLFDTTR 164
Cdd:cd01369     81 FAYGQTSSGKTYTM---EGKLGDPESMGIIPRIVQDIFETIYSMDENL--------EFHVKVSYFEIYMEKIRDLLDVSK 149

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159648420  165 DidaknkksNIKIHEDSAGGIYTVGVTTRTVNGESEMMQCLKLGALSRTTASTQMNVQSSRSHAIFTIHLCQtrvcppfn 244
Cdd:cd01369    150 T--------NLSVHEDKNRGPYVKGATERFVSSPEEVLDVIDEGKSNRHVAVTNMNEESSRSHSIFLINVKQ-------- 213

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159648420  245 tDNATDNRIisessemnefetLTAKFHFVDLAGSERLKRTGATGERAKEGISINCGLLALGNVISALGDKSKkaTHVPYR 324
Cdd:cd01369    214 -ENVETEKK------------KSGKLYLVDLAGSEKVSKTGAEGAVLDEAKKINKSLSALGNVINALTDGKK--THIPYR 278

                          330       340       350       360
                   ....*....|....*....|....*....|....*....|....*..
gi 1159648420  325 DSKLTRLLQDSLGGNSQTLMIACVSPSDRDFMETLNTLKYANRARNI 371
Cdd:cd01369    279 DSKLTRILQDSLGGNSRTTLIICCSPSSYNESETLSTLRFGQRAKTI 325
PLN02763 PLN02763
hydrolase, hydrolyzing O-glycosyl compounds
 1829-2442 6.02e-96

hydrolase, hydrolyzing O-glycosyl compounds


Pssm-ID: 215408 [Multi-domain]  Cd Length: 978  Bit Score: 335.32  E-value: 6.02e-96
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159648420 1829 PSTSVYGFGEQEHESFKHSMDFVTYGMFSRDQAP-TPlvNLYGVHPFYMCVEADSNAHGVLLLNSNAQDVSL-------- 1899
Cdd:PLN02763    72 SGTSFYGTGEVSGPLERTGKRVYTWNTDAWGYGQnTT--SLYQSHPWVFVVLPNGEALGVLADTTRRCEIDLrkesiiri 149

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159648420 1900 ---SPDPSVTFrtiggildfyvflGP--TPENVVQQYTEAIGRPHMPAYWSLGFHLSRWGYGSIDVLKETVNRMHYYDIP 1974
Cdd:PLN02763   150 iapASYPVITF-------------GPfpSPEALLTSLSHAIGTVFMPPKWALGYQQCRWSYESAKRVAEIARTFREKKIP 216

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159648420 1975 YDVQHLDIDYMERYMDFTYDKVNYAGLPEYIQKLKRKGMHNVVILDPFITKDEEpgtYRPYDLGEEMGVWVNNSDGvTPA 2054
Cdd:PLN02763   217 CDVVWMDIDYMDGFRCFTFDKERFPDPKGLADDLHSIGFKAIWMLDPGIKAEEG---YFVYDSGCENDVWIQTADG-KPF 292

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159648420 2055 VGKAWPpGDSVFPDYTNPRTAEWWTQMCLEFKDVlDYDGIWIDMNEPSNFLTGQYPGCAVNDLNNPPYVPSISDHSlaqk 2134
Cdd:PLN02763   293 VGEVWP-GPCVFPDFTNKKTRSWWANLVKDFVSN-GVDGIWNDMNEPAVFKTVTKTMPETNIHRGDEELGGVQNHS---- 366

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159648420 2135 tlcpdsktylgeHYntHSLFGWSQTAPTFHAAQQA-TGKRAFVLSRSTFVGSGKHGGHWLGDNFSQWKDMHRSIVGILEF 2213
Cdd:PLN02763   367 ------------HY--HNVYGMLMARSTYEGMLLAnKNKRPFVLTRAGFIGSQRYAATWTGDNLSNWEHLHMSIPMVLQL 432

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159648420 2214 NLFGIPYIGADICGFNHNTTYELCLRWMQLGSFYPFSRNHNAEGNREQDPAVFGAEFAEISRATLRIRYSLLPYLYTLFY 2293
Cdd:PLN02763   433 GLSGQPLSGPDIGGFAGDATPKLFGRWMGVGAMFPFARGHSEQGTIDHEPWSFGEECEEVCRLALKRRYRLLPHFYTLFY 512

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159648420 2294 ESHVHGNTVARSLMHEFTSDQETHGIDTAFLWGPAFMIAPVL-QEGARSVDVYFPEATW--FDYYTGHkvPSTwkknyat 2370
Cdd:PLN02763   513 KAHTTGLPVMTPIFFADPKDPSLRKVENSFLLGPLLISASTLpDQGSDNLQHVLPKGIWqrFDFDDSH--PDL------- 583

                          570       580       590       600       610       620       630
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1159648420 2371 vaaPLskipLFIRGGYILPEQAPASTTTKSRL-NPFGLIIALDEHGEASGSLFWDDGDSIDtIENENYFLAKY 2442
Cdd:PLN02763   584 ---PL----LYLQGGSIIPLGPPIQHVGEASLsDDLTLLIALDENGKAEGVLYEDDGDGFG-YTKGDYLLTHY 648
GH31_MGAM-like cd06600
maltase-glucoamylase (MGAM)-like; This family includes the following closely related glycosyl ...
 1936-2284 8.92e-96

maltase-glucoamylase (MGAM)-like; This family includes the following closely related glycosyl hydrolase family 31 (GH31) enzymes: maltase-glucoamylase (MGAM), sucrase-isomaltase (SI), lysosomal acid alpha-glucosidase (GAA), neutral alpha-glucosidase C (GANC), the alpha subunit of neutral alpha-glucosidase AB (GANAB), and alpha-glucosidase II. MGAM is one of the two enzymes responsible for catalyzing the last glucose-releasing step in starch digestion. SI is implicated in the digestion of dietary starch and major disaccharides such as sucrose and isomaltose, while GAA degrades glycogen in the lysosome, cleaving both alpha-1,4 and alpha-1,6 glucosidic linkages. MGAM and SI are anchored to small-intestinal brush-border epithelial cells. The absence of SI from the brush border membrane or its malfunction is associated with malabsorption disorders such as congenital sucrase-isomaltase deficiency (CSID). The domain architectures of MGAM and SI include two tandem GH31 catalytic domains, an N-terminal domain found near the membrane-bound end and a C-terminal luminal domain. Both of the tandem GH31 domains of MGAM and SI are included in this family. The domain architecture of GAA includes an N-terminal TFF (trefoil factor family) domain in addition to the GH31 catalytic domain. Deficient GAA expression causes Pompe disease, an autosomal recessive genetic disorder also known as glycogen storage disease type II (GSDII). GANC and GANAB are key enzymes in glycogen metabolism that hydrolyze terminal, non-reducing 1,4-linked alpha-D-glucose residues from glycogen in the endoplasmic reticulum. Alpha-glucosidase II is a GH31 enzyme, found in bacteria and plants, which has exo-alpha-1,4-glucosidase and oligo-1,6-glucosidase activities. Alpha-glucosidase II has been characterized in Bacillus thermoamyloliquefaciens where it forms a homohexamer. This family also includes the MalA alpha-glucosidase from Sulfolobus solfataricus and the AglA alpha-glucosidase from Picrophilus torridus. MalA is part of the carbohydrate-metabolizing machinery that allows this organism to utilize carbohydrates, such as maltose, as the sole carbon and energy source. The MGAM-like family corresponds to subgroup 1 in the Ernst et al classification of GH31 enzymes.


Pssm-ID: 269886 [Multi-domain]  Cd Length: 256  Bit Score: 310.19  E-value: 8.92e-96
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159648420 1936 GRPHMPAYWSLGFHLSRWGYGSIDVLKETVNRMHYYDIPYDVQHLDIDYMERYMDFTYDKVNYAGLPEYIQKLKRKGMHN 2015
Cdd:cd06600      1 GRPALPPYWAFGYHQSRYSYYDQDKVVEVVDIMQEAGIPYDVMWLDIDYMDSYKDFTWDPVRFPEPKKFVDELHKNGQKL 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159648420 2016 VVILDPFITkdeepgtyrpydlgeemgvwvnnsdgvtpavgkawppgdsvfpdytnprtAEWWTQMCLEFKDVLDYDGIW 2095
Cdd:cd06600     81 VTIVDPGIT--------------------------------------------------REWWAGLISEFLYSQGIDGIW 110

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159648420 2096 IDMNEPSNFltgqypgcavndlnnppyvpsisdhslaqktlcpdsktylgehYNTHSLFGWSQTAPTFHAAQQATGKRAF 2175
Cdd:cd06600    111 IDMNEPSNF-------------------------------------------YKVHNLYGFYEAMATAEGLRTSHNERPF 147

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159648420 2176 VLSRSTFVGSGKHGGHWLGDNFSQWKDMHRSIVGILEFNLFGIPYIGADICGFNHNTTYELCLRWMQLGSFYPFSRNHNA 2255
Cdd:cd06600    148 ILSRSTFAGSQKYAAHWTGDNTASWDDLKLSIPLVLGLSLSGIPFVGADIGGFAGDTSEELLVRWYQLGAFYPFSRSHKA 227

                          330       340
                   ....*....|....*....|....*....
gi 1159648420 2256 EGNREQDPAVFGAEFAEISRATLRIRYSL 2284
Cdd:cd06600    228 TDTKDQEPVLFPEYYKESVREILELRYKL 256
KIP1 COG5059
Kinesin-like protein [Cytoskeleton];
44-509 4.27e-95

Kinesin-like protein [Cytoskeleton];


Pssm-ID: 227392 [Multi-domain]  Cd Length: 568  Bit Score: 320.53  E-value: 4.27e-95
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159648420   44 GKDKAFTFDYVFNIDSQQEEIYVQCIEKLIEGCFEGYNATVFAYGQTGAGKTYTMgTGfdvniTEEEQGIISRAVKHLFR 123
Cdd:COG5059     53 SKEGTYAFDKVFGPSATQEDVYEETIKPLIDSLLLGYNCTVFAYGQTGSGKTYTM-SG-----TEEEPGIIPLSLKELFS 126

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159648420  124 CIEEKKQAAikqglpppDFKVNAQFLELYNEEILDLFDttrdidakNKKSNIKIHEDSAGGIYTVGVTTRTVNGESEMMQ 203
Cdd:COG5059    127 KLEDLSMTK--------DFAVSISYLEIYNEKIYDLLS--------PNEESLNIREDSLLGVKVAGLTEKHVSSKEEILD 190

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159648420  204 CLKLGALSRTTASTQMNVQSSRSHAIFTIHLcqtrvcppfntdnatdnriisESSEMNEFETLTAKFHFVDLAGSERLKR 283
Cdd:COG5059    191 LLRKGEKNRTTASTEINDESSRSHSIFQIEL---------------------ASKNKVSGTSETSKLSLVDLAGSERAAR 249

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159648420  284 TGATGERAKEGISINCGLLALGNVISALGDKsKKATHVPYRDSKLTRLLQDSLGGNSQTLMIACVSPSDRDFMETLNTLK 363
Cdd:COG5059    250 TGNRGTRLKEGASINKSLLTLGNVINALGDK-KKSGHIPYRESKLTRLLQDSLGGNCNTRVICTISPSSNSFEETINTLK 328

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159648420  364 YANRARNIKNKVMVNQDRASQ-QINALRSEIARLQMELMEYKTGKRIID------------EEGVESINDMFHENAMLQT 430
Cdd:COG5059    329 FASRAKSIKNKIQVNSSSDSSrEIEEIKFDLSEDRSEIEILVFREQSQLsqsslsgifaymQSLKKETETLKSRIDLIMK 408

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159648420  431 EN--------NNLRVRIKAMQETVDALRARITQLMSDQAnqvlaragEGNEEISNMIHNYIKEIEDLRAKL----LESEA 498
Cdd:COG5059    409 SIisgtferkKLLKEEGWKYKSTLQFLRIEIDRLLLLRE--------EELSKKKTKIHKLNKLRHDLSSLLssipEETSD 480

                          490
                   ....*....|.
gi 1159648420  499 VNENLRRNLSR 509
Cdd:COG5059    481 RVESEKASKLR 491
KISc_KLP2_like cd01373
Kinesin motor domain, KIF15-like subgroup; Kinesin motor domain, KIF15-like subgroup. Members ...
 10-380 1.73e-94

Kinesin motor domain, KIF15-like subgroup; Kinesin motor domain, KIF15-like subgroup. Members of this subgroup seem to play a role in mitosis and meiosis. This catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Kinesins are microtubule-dependent molecular motors that play important roles in intracellular transport and in cell division. In most kinesins, the motor domain is found at the N-terminus (N-type). N-type kinesins are (+) end-directed motors, i.e. they transport cargo towards the (+) end of the microtubule. Kinesin motor domains hydrolyze ATP at a rate of about 80 per second, and move along the microtubule at a speed of about 6400 Angstroms per second. To achieve that, kinesin head groups work in pairs. Upon replacing ADP with ATP, a kinesin motor domain increases its affinity for microtubule binding and locks in place. Also, the neck linker binds to the motor domain, which repositions the other head domain through the coiled-coil domain close to a second tubulin dimer, about 80 Angstroms along the microtubule. Meanwhile, ATP hydrolysis takes place, and when the second head domain binds to the microtubule, the first domain again replaces ADP with ATP, triggering a conformational change that pulls the first domain forward.


Pssm-ID: 276824 [Multi-domain]  Cd Length: 347  Bit Score: 310.21  E-value: 1.73e-94
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159648420   10 VRVAVRIRPQLAKEKIEGCHICTSVTPGEPQVFLGK-DKAFTFDYVFNIDSQQEEIYVQCIEKLIEGCFEGYNATVFAYG 88
Cdd:cd01373      3 VKVFVRIRPPAEREGDGEYGQCLKKLSSDTLVLHSKpPKTFTFDHVADSNTNQESVFQSVGKPIVESCLSGYNGTIFAYG 82

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159648420   89 QTGAGKTYTM--GTGFDVNITEEEQGIISRAVKHLFRCIEEKKQAAIKQglppPDFKVNAQFLELYNEEILDLFDTTrdi 166
Cdd:cd01373     83 QTGSGKTYTMwgPSESDNESPHGLRGVIPRIFEYLFSLIQREKEKAGEG----KSFLCKCSFLEIYNEQIYDLLDPA--- 155

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159648420  167 daknkKSNIKIHEDSAGGIYTVGVTTRTVNGESEMMQCLKLGALSRTTASTQMNVQSSRSHAIFTIhlcqtrvcppfntd 246
Cdd:cd01373    156 -----SRNLKLREDIKKGVYVENLVEEYVTSAEDVYQVLSKGWSNRKVAATSMNRESSRSHAVFTC-------------- 216

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159648420  247 natdnrIISESSEMNEFETL-TAKFHFVDLAGSERLKRTGATGERAKEGISINCGLLALGNVISALGDKSK-KATHVPYR 324
Cdd:cd01373    217 ------TIESWEKKACFVNIrTSRLNLVDLAGSERQKDTHAEGVRLKEAGNINKSLSCLGHVINALVDVAHgKQRHVCYR 290

                          330       340       350       360       370
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 1159648420  325 DSKLTRLLQDSLGGNSQTLMIACVSPSDRDFMETLNTLKYANRARNIKNKVMVNQD 380
Cdd:cd01373    291 DSKLTFLLRDSLGGNAKTAIIANVHPSSKCFGETLSTLRFAQRAKLIKNKAVVNED 346
KISc_CENP_E cd01374
Kinesin motor domain, CENP-E/KIP2-like subgroup; Kinesin motor domain, CENP-E/KIP2-like ...
 9-371 1.09e-90

Kinesin motor domain, CENP-E/KIP2-like subgroup; Kinesin motor domain, CENP-E/KIP2-like subgroup, involved in chromosome movement and/or spindle elongation during mitosis. This catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Kinesins are microtubule-dependent molecular motors that play important roles in intracellular transport and in cell division. In most kinesins, the motor domain is found at the N-terminus (N-type). N-type kinesins are (+) end-directed motors, i.e. they transport cargo towards the (+) end of the microtubule. Kinesin motor domains hydrolyze ATP at a rate of about 80 per second, and move along the microtubule at a speed of about 6400 Angstroms per second. To achieve that, kinesin head groups work in pairs. Upon replacing ADP with ATP, a kinesin motor domain increases its affinity for microtubule binding and locks in place. Also, the neck linker binds to the motor domain, which repositions the other head domain through the coiled-coil domain close to a second tubulin dimer, about 80 Angstroms along the microtubule. Meanwhile, ATP hydrolysis takes place, and when the second head domain binds to the microtubule, the first domain again replaces ADP with ATP, triggering a conformational change that pulls the first domain forward.


Pssm-ID: 276825 [Multi-domain]  Cd Length: 321  Bit Score: 298.48  E-value: 1.09e-90
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159648420    9 SVRVAVRIRPQLAKEKIEGCHICTSVTPG----EPQVFlgkdKAFTFDYVFNIDSQQEEIYVQCIEKLIEGCFEGYNATV 84
Cdd:cd01374      1 KITVTVRVRPLNSREIGINEQVAWEIDNDtiylVEPPS----TSFTFDHVFGGDSTNREVYELIAKPVVKSALEGYNGTI 76

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159648420   85 FAYGQTGAGKTYTMgTGfdvniTEEEQGIISRAVKHLFRCIEEKkqaaikqglPPPDFKVNAQFLELYNEEILDLFDTTr 164
Cdd:cd01374     77 FAYGQTSSGKTFTM-SG-----DEDEPGIIPLAIRDIFSKIQDT---------PDREFLLRVSYLEIYNEKINDLLSPT- 140

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159648420  165 didaknkKSNIKIHEDSAGGIYTVGVTTRTVNGESEMMQCLKLGALSRTTASTQMNVQSSRSHAIFtihlcqtrvcppfn 244
Cdd:cd01374    141 -------SQNLKIRDDVEKGVYVAGLTEEIVSSPEHALSLIARGEKNRHVGETDMNERSSRSHTIF-------------- 199

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159648420  245 tdnatdnRIISESSEMNEFETLTAKF---HFVDLAGSERLKRTGATGERAKEGISINCGLLALGNVISALGDkSKKATHV 321
Cdd:cd01374    200 -------RITIESSERGELEEGTVRVstlNLIDLAGSERAAQTGAAGVRRKEGSHINKSLLTLGTVISKLSE-GKVGGHI 271

                          330       340       350       360       370
                   ....*....|....*....|....*....|....*....|....*....|
gi 1159648420  322 PYRDSKLTRLLQDSLGGNSQTLMIACVSPSDRDFMETLNTLKYANRARNI 371
Cdd:cd01374    272 PYRDSKLTRILQPSLGGNSRTAIICTITPAESHVEETLNTLKFASRAKKI 321
KISc_KID_like cd01376
Kinesin motor domain, KIF22/Kid-like subgroup; Kinesin motor domain, KIF22/Kid-like subgroup. ...
 10-369 4.30e-72

Kinesin motor domain, KIF22/Kid-like subgroup; Kinesin motor domain, KIF22/Kid-like subgroup. Members of this group might play a role in regulating chromosomal movement along microtubules in mitosis. This catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Kinesins are microtubule-dependent molecular motors that play important roles in intracellular transport and in cell division. In most kinesins, the motor domain is found at the N-terminus (N-type). N-type kinesins are (+) end-directed motors, i.e. they transport cargo towards the (+) end of the microtubule. Kinesin motor domains hydrolyze ATP at a rate of about 80 per second, and move along the microtubule at a speed of about 6400 Angstroms per second. To achieve that, kinesin head groups work in pairs. Upon replacing ADP with ATP, a kinesin motor domain increases its affinity for microtubule binding and locks in place. Also, the neck linker binds to the motor domain, which repositions the other head domain through the coiled-coil domain close to a second tubulin dimer, about 80 Angstroms along the microtubule. Meanwhile, ATP hydrolysis takes place, and when the second head domain binds to the microtubule, the first domain again replaces ADP with ATP, triggering a conformational change that pulls the first domain forward.


Pssm-ID: 276827 [Multi-domain]  Cd Length: 319  Bit Score: 244.72  E-value: 4.30e-72
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159648420   10 VRVAVRIRPQLAKEKIEGCHICTSVTpGEPQVFL------GKDKAFTFDYVFNIDSQQEEIYVQCIEKLIEGCFEGYNAT 83
Cdd:cd01376      2 VRVAVRVRPFVDGTAGASDPSCVSGI-DSCSVELadprnhGETLKYQFDAFYGEESTQEDIYAREVQPIVPHLLEGQNAT 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159648420   84 VFAYGQTGAGKTYTMgTGfdvniTEEEQGIISRAVKHLFRCIEEKKQAaikqglpppdFKVNAQFLELYNEEILDLFDTt 163
Cdd:cd01376     81 VFAYGSTGAGKTFTM-LG-----SPEQPGLMPLTVMDLLQMTRKEAWA----------LSFTMSYLEIYQEKILDLLEP- 143

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159648420  164 rdidaknKKSNIKIHEDSAGGIYTVGVTTRTVNGESEMMQCLKLGALSRTTASTQMNVQSSRSHAIFTIHlcqtrvcppf 243
Cdd:cd01376    144 -------ASKELVIREDKDGNILIPGLSSKPIKSMAEFEEAFLPASKNRTVAATRLNDNSSRSHAVLLIK---------- 206

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159648420  244 ntdnatdnriISESSEMNEFETLTAKFHFVDLAGSERLKRTGATGERAKEGISINCGLLALGNVISALgdkSKKATHVPY 323
Cdd:cd01376    207 ----------VDQRERLAPFRQRTGKLNLIDLAGSEDNRRTGNEGIRLKESGAINSSLFVLSKVVNAL---NKNLPRIPY 273

                          330       340       350       360
                   ....*....|....*....|....*....|....*....|....*.
gi 1159648420  324 RDSKLTRLLQDSLGGNSQTLMIACVSPSDRDFMETLNTLKYANRAR 369
Cdd:cd01376    274 RDSKLTRLLQDSLGGGSRCIMVANIAPERTFYQDTLSTLNFAARSR 319
KISc_KIF2_like cd01367
Kinesin motor domain, KIF2-like group; Kinesin motor domain, KIF2-like group. KIF2 is a ...
 10-367 1.18e-70

Kinesin motor domain, KIF2-like group; Kinesin motor domain, KIF2-like group. KIF2 is a protein expressed in neurons, which has been associated with axonal transport and neuron development; alternative splice forms have been implicated in lysosomal translocation. This catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Kinesins are microtubule-dependent molecular motors that play important roles in intracellular transport and in cell division. In this subgroup the motor domain is found in the middle (M-type) of the protein chain. M-type kinesins are (+) end-directed motors, i.e. they transport cargo towards the (+) end of the microtubule. Kinesin motor domains hydrolyze ATP at a rate of about 80 per second, and move along the microtubule at a speed of about 6400 Angstroms per second (KIF2 may be slower). To achieve that, kinesin head groups work in pairs. Upon replacing ADP with ATP, a kinesin motor domain increases its affinity for microtubule binding and locks in place. Also, the neck linker binds to the motor domain, which repositions the other head domain through the coiled-coil domain close to a second tubulin dimer, about 80 Angstroms along the microtubule. Meanwhile, ATP hydrolysis takes place, and when the second head domain binds to the microtubule, the first domain again replaces ADP with ATP, triggering a conformational change that pulls the first domain forward.


Pssm-ID: 276818 [Multi-domain]  Cd Length: 328  Bit Score: 241.05  E-value: 1.18e-70
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159648420   10 VRVAVRIRPQLAKEKIEG------CHICTSVTPGEPQ--VFLGK---DKAFTFDYVFNIDSQQEEIYVQCIEKLIEGCFE 78
Cdd:cd01367      2 IKVCVRKRPLNKKEVAKKeidvvsVPSKLTLIVHEPKlkVDLTKyieNHTFRFDYVFDESSSNETVYRSTVKPLVPHIFE 81

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159648420   79 GYNATVFAYGQTGAGKTYTMGTGFdvNITEEEQGIISRAVKHLFRCIEEKKQAAikqglpppDFKVNAQFLELYNEEILD 158
Cdd:cd01367     82 GGKATCFAYGQTGSGKTYTMGGDF--SGQEESKGIYALAARDVFRLLNKLPYKD--------NLGVTVSFFEIYGGKVFD 151

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159648420  159 LFdttrdidakNKKSNIKIHEDSAGGIYTVGVTTRTVNGESEMMQCLKLGALSRTTASTQMNVQSSRSHAIFTIHLcqtr 238
Cdd:cd01367    152 LL---------NRKKRVRLREDGKGEVQVVGLTEKPVTSAEELLELIESGSSLRTTGQTSANSQSSRSHAILQIIL---- 218

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159648420  239 vcppfntdnatdnriisessEMNEFETLTAKFHFVDLAGSER-LKRTGATGERAKEGISINCGLLALGNVISALGDKSkk 317
Cdd:cd01367    219 --------------------RDRGTNKLHGKLSFVDLAGSERgADTSSADRQTRMEGAEINKSLLALKECIRALGQNK-- 276

                          330       340       350       360       370
                   ....*....|....*....|....*....|....*....|....*....|.
gi 1159648420  318 aTHVPYRDSKLTRLLQDSL-GGNSQTLMIACVSPSDRDFMETLNTLKYANR 367
Cdd:cd01367    277 -AHIPFRGSKLTQVLKDSFiGENSKTCMIATISPGASSCEHTLNTLRYADR 326
KISc_KIF9_like cd01375
Kinesin motor domain, KIF9-like subgroup; Kinesin motor domain, KIF9-like subgroup; might play ...
 46-369 1.57e-68

Kinesin motor domain, KIF9-like subgroup; Kinesin motor domain, KIF9-like subgroup; might play a role in cell shape remodeling. This catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Kinesins are microtubule-dependent molecular motors that play important roles in intracellular transport and in cell division. In most kinesins, the motor domain is found at the N-terminus (N-type). N-type kinesins are (+) end-directed motors, i.e. they transport cargo towards the (+) end of the microtubule. Kinesin motor domains hydrolyze ATP at a rate of about 80 per second, and move along the microtubule at a speed of about 6400 Angstroms per second. To achieve that, kinesin head groups work in pairs. Upon replacing ADP with ATP, a kinesin motor domain increases its affinity for microtubule binding and locks in place. Also, the neck linker binds to the motor domain, which repositions the other head domain through the coiled-coil domain close to a second tubulin dimer, about 80 Angstroms along the microtubule. Meanwhile, ATP hydrolysis takes place, and when the second head domain binds to the microtubule, the first domain again replaces ADP with ATP, triggering a conformational change that pulls the first domain forward.


Pssm-ID: 276826 [Multi-domain]  Cd Length: 334  Bit Score: 235.17  E-value: 1.57e-68
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159648420   46 DKAFTFDYVFNiDSQQEEIYVQCIEKLIEGCFEGYNATVFAYGQTGAGKTYTMgTGFDVNITEeeQGIISRAVKHLFRCI 125
Cdd:cd01375     47 DWSFKFDGVLH-NASQELVYETVAKDVVSSALAGYNGTIFAYGQTGAGKTFTM-TGGTENYKH--RGIIPRALQQVFRMI 122

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159648420  126 EEKKQAAIKqglpppdfkVNAQFLELYNEEILDLFDTTRDIDAKNKKsnIKIHEDSAGGIYTVGVTTRTVNGESEMMQCL 205
Cdd:cd01375    123 EERPTKAYT---------VHVSYLEIYNEQLYDLLSTLPYVGPSVTP--MTILEDSPQNIFIKGLSLHLTSQEEEALSLL 191

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159648420  206 KLGALSRTTASTQMNVQSSRSHAIFTIHLCqtrvcppfntdnatdnriiSESSEMNEFETLTAKFHFVDLAGSERLKRTG 285
Cdd:cd01375    192 FLGETNRIIASHTMNKNSSRSHCIFTIHLE-------------------AHSRTLSSEKYITSKLNLVDLAGSERLSKTG 252

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159648420  286 ATGERAKEGISINCGLLALGNVISALGDKskKATHVPYRDSKLTRLLQDSLGGNSQTLMIACVSPSDRDFMETLNTLKYA 365
Cdd:cd01375    253 VEGQVLKEATYINKSLSFLEQAIIALSDK--DRTHVPFRQSKLTHVLRDSLGGNCNTVMVANIYGEAAQLEETLSTLRFA 330


                   ....
gi 1159648420  366 NRAR 369
Cdd:cd01375    331 SRVK 334
PLN03188 PLN03188
kinesin-12 family protein; Provisional
 7-404 1.56e-67

kinesin-12 family protein; Provisional


Pssm-ID: 215621 [Multi-domain]  Cd Length: 1320  Bit Score: 252.93  E-value: 1.56e-67
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159648420    7 ESSVRVAVRIRPQLAKEkiEGCHICTSVTPGEPQVflgKDKAFTFDYVFNIDSQQEEIYVQCIEKLIEGCFEGYNATVFA 86
Cdd:PLN03188    97 DSGVKVIVRMKPLNKGE--EGEMIVQKMSNDSLTI---NGQTFTFDSIADPESTQEDIFQLVGAPLVENCLAGFNSSVFA 171

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159648420   87 YGQTGAGKTYTM-GTG---FDVNITEEEQGIISRAVKHLF-RCIEEKKQAAIKQglppPDFKVNAQFLELYNEEILDLFD 161
Cdd:PLN03188   172 YGQTGSGKTYTMwGPAnglLEEHLSGDQQGLTPRVFERLFaRINEEQIKHADRQ----LKYQCRCSFLEIYNEQITDLLD 247

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159648420  162 TTrdidaknkKSNIKIHEDSAGGIYTVGVTTRTVNGESEMMQCLKLGALSRTTASTQMNVQSSRSHAIFTihlcqtrvCp 241
Cdd:PLN03188   248 PS--------QKNLQIREDVKSGVYVENLTEEYVKTMKDVTQLLIKGLSNRRTGATSINAESSRSHSVFT--------C- 310

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159648420  242 pfntdnATDNRIISESSEMNEFETltAKFHFVDLAGSERLKRTGATGERAKEGISINCGLLALGNVISALGDKSK--KAT 319
Cdd:PLN03188   311 ------VVESRCKSVADGLSSFKT--SRINLVDLAGSERQKLTGAAGDRLKEAGNINRSLSQLGNLINILAEISQtgKQR 382

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159648420  320 HVPYRDSKLTRLLQDSLGGNSQTLMIACVSPSDRDFMETLNTLKYANRARNIKNKVMVNQDrASQQINALRSEIARLQME 399
Cdd:PLN03188   383 HIPYRDSRLTFLLQESLGGNAKLAMVCAISPSQSCKSETFSTLRFAQRAKAIKNKAVVNEV-MQDDVNFLREVIRQLRDE 461


                   ....*
gi 1159648420  400 LMEYK 404
Cdd:PLN03188   462 LQRVK 466
KISc_KIF23_like cd01368
Kinesin motor domain, KIF23-like subgroup; Kinesin motor domain, KIF23-like subgroup. Members ...
 10-365 9.75e-66

Kinesin motor domain, KIF23-like subgroup; Kinesin motor domain, KIF23-like subgroup. Members of this group may play a role in mitosis. This catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Kinesins are microtubule-dependent molecular motors that play important roles in intracellular transport and in cell division. In most kinesins, the motor domain is found at the N-terminus (N-type). N-type kinesins are (+) end-directed motors, i.e. they transport cargo towards the (+) end of the microtubule. Kinesin motor domains hydrolyze ATP at a rate of about 80 per second, and move along the microtubule at a speed of about 6400 Angstroms per second. To achieve that, kinesin head groups work in pairs. Upon replacing ADP with ATP, a kinesin motor domain increases its affinity for microtubule binding and locks in place. Also, the neck linker binds to the motor domain, which repositions the other head domain through the coiled-coil domain close to a second tubulin dimer, about 80 Angstroms along the microtubule. Meanwhile, ATP hydrolysis takes place, and when the second head domain binds to the microtubule, the first domain again replaces ADP with ATP, triggering a conformational change that pulls the first domain forward.


Pssm-ID: 276819 [Multi-domain]  Cd Length: 345  Bit Score: 227.66  E-value: 9.75e-66
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159648420   10 VRVAVRIRPQLAKEKI---EGC-HI--CTSVTPGEPQVFLG---------KDKAFTFDYVFNIDSQQEEIYVQCIEKLIE 74
Cdd:cd01368      3 VKVYLRVRPLSKDELEsedEGCiEVinSTTVVLHPPKGSAAnksernggqKETKFSFSKVFGPNTTQKEFFQGTALPLVQ 82

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159648420   75 GCFEGYNATVFAYGQTGAGKTYTMgTGfdvniTEEEQGIISRAVKHLFRCIeekkqaaikqglppPDFKVNAQFLELYNE 154
Cdd:cd01368     83 DLLHGKNGLLFTYGVTNSGKTYTM-QG-----SPGDGGILPRSLDVIFNSI--------------GGYSVFVSYIEIYNE 142

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159648420  155 EILDLFDTTRDIDAKNKKSnIKIHEDSAGGIYTVGVTTRTVNGESEMMQCLKLGALSRTTASTQMNVQSSRSHAIFTIHL 234
Cdd:cd01368    143 YIYDLLEPSPSSPTKKRQS-LRLREDHNGNMYVAGLTEIEVKSTEEARKVLKRGQKNRSVAGTKLNRESSRSHSVFTIKL 221

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159648420  235 CQTRVCPPFNTDNATDNRIISESSemnefetltakfhFVDLAGSERLKRTGATGERAKEGISINCGLLALGNVISAL--G 312
Cdd:cd01368    222 VQAPGDSDGDVDQDKDQITVSQLS-------------LVDLAGSERTSRTQNTGERLKEAGNINTSLMTLGTCIEVLreN 288

                          330       340       350       360       370
                   ....*....|....*....|....*....|....*....|....*....|...
gi 1159648420  313 DKSKKATHVPYRDSKLTRLLQDSLGGNSQTLMIACVSPSDRDFMETLNTLKYA 365
Cdd:cd01368    289 QLQGTNKMVPFRDSKLTHLFQNYFDGEGKASMIVNVNPCASDYDETLHVMKFS 341
WD40 cd00200
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ...
 1316-1629 1.13e-60

WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions including adaptor/regulatory modules in signal transduction, pre-mRNA processing and cytoskeleton assembly; typically contains a GH dipeptide 11-24 residues from its N-terminus and the WD dipeptide at its C-terminus and is 40 residues long, hence the name WD40; between GH and WD lies a conserved core; serves as a stable propeller-like platform to which proteins can bind either stably or reversibly; forms a propeller-like structure with several blades where each blade is composed of a four-stranded anti-parallel b-sheet; instances with few detectable copies are hypothesized to form larger structures by dimerization; each WD40 sequence repeat forms the first three strands of one blade and the last strand in the next blade; the last C-terminal WD40 repeat completes the blade structure of the first WD40 repeat to create the closed ring propeller-structure; residues on the top and bottom surface of the propeller are proposed to coordinate interactions with other proteins and/or small ligands; 7 copies of the repeat are present in this alignment.


Pssm-ID: 238121 [Multi-domain]  Cd Length: 289  Bit Score: 210.65  E-value: 1.13e-60
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159648420 1316 CIYTAEGHTKAVLCVDATDD--LLFTGSKDRTCKVWNLVTGQEIMSLGGHPNNVVSIKYCNYTSLVFTVST-SYIKVWDI 1392
Cdd:cd00200      1 LRRTLKGHTGGVTCVAFSPDgkLLATGSGDGTIKVWDLETGELLRTLKGHTGPVRDVAASADGTYLASGSSdKTIRLWDL 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159648420 1393 RDSaKCIRTLTSSgqampgdvcsastnrtvaipagENQINQIALNPTGTFLYAAAG-NSVRMWDLKRFQSTGKLTGHQGP 1471
Cdd:cd00200     81 ETG-ECVRTLTGH----------------------TSYVSSVAFSPDGRILSSSSRdKTIKVWDVETGKCLTTLRGHTDW 137

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159648420 1472 VMCLTVDRisnGQDLIVTGSKDHYIKMFDVTEGalgsvSPTHNFEpPHYDGIEALAIMGDN--LFSGSRDNGIKKWDLAQ 1549
Cdd:cd00200    138 VNSVAFSP---DGTFVASSSQDGTIKLWDLRTG-----KCVATLT-GHTGEVNSVAFSPDGekLLSSSSDGTIKLWDLST 208

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159648420 1550 KDLLQQVPnAHKDWVCALGLVPGAPVLLSGCRGGNIKLWNVETFAPIGEMKGHDSPINAIC--TNSSQIFTAADDRTVRI 1627
Cdd:cd00200    209 GKCLGTLR-GHENGVNSVAFSPDGYLLASGSEDGTIRVWDLRTGECVQTLSGHTNSVTSLAwsPDGKRLASGSADGTIRI 287


                   ..
gi 1159648420 1628 WK 1629
Cdd:cd00200    288 WD 289
GH31 cd06589
glycosyl hydrolase family 31 (GH31); GH31 enzymes occur in prokaryotes, eukaryotes, and ...
 1936-2275 5.10e-52

glycosyl hydrolase family 31 (GH31); GH31 enzymes occur in prokaryotes, eukaryotes, and archaea with a wide range of hydrolytic activities, including alpha-glucosidase (glucoamylase and sucrase-isomaltase), alpha-xylosidase, 6-alpha-glucosyltransferase, 3-alpha-isomaltosyltransferase and alpha-1,4-glucan lyase. All GH31 enzymes cleave a terminal carbohydrate moiety from a substrate that varies considerably in size, depending on the enzyme, and may be either a starch or a glycoprotein. In most cases, the pyranose moiety recognized in subsite -1 of the substrate binding site is an alpha-D-glucose, though some GH31 family members show a preference for alpha-D-xylose. Several GH31 enzymes can accommodate both glucose and xylose and different levels of discrimination between the two have been observed. Most characterized GH31 enzymes are alpha-glucosidases. In mammals, GH31 members with alpha-glucosidase activity are implicated in at least three distinct biological processes. The lysosomal acid alpha-glucosidase (GAA) is essential for glycogen degradation and a deficiency or malfunction of this enzyme causes glycogen storage disease II, also known as Pompe disease. In the endoplasmic reticulum, alpha-glucosidase II catalyzes the second step in the N-linked oligosaccharide processing pathway that constitutes part of the quality control system for glycoprotein folding and maturation. The intestinal enzymes sucrase-isomaltase (SI) and maltase-glucoamylase (MGAM) play key roles in the final stage of carbohydrate digestion, making alpha-glucosidase inhibitors useful in the treatment of type 2 diabetes. GH31 alpha-glycosidases are retaining enzymes that cleave their substrates via an acid/base-catalyzed, double-displacement mechanism involving a covalent glycosyl-enzyme intermediate. Two aspartic acid residues have been identified as the catalytic nucleophile and the acid/base, respectively.


Pssm-ID: 269876 [Multi-domain]  Cd Length: 265  Bit Score: 184.86  E-value: 5.10e-52
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159648420 1936 GRPHMPAYWSLGFHLSRWGYGSIDVLKETVNRMHYYDIPYDVQHLDIDYMER---YMDFTYDKVNYAGLPEYIQKLKRKG 2012
Cdd:cd06589      1 GRPPLLPKWALGFWNSRYGYYSEDEVEELVDRYREEGIPLDGFVLDSDWMDWggnWGGFTWNREKFPDPKGMIDELHDKG 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159648420 2013 MHNVVILDPFItkdeepgtyrpydlgeemgvwvnnsdgvtpavgkawppgdsvfpdytnprtAEWWTQMCLEFKDVLDYD 2092
Cdd:cd06589     81 VKLGLIVKPRL---------------------------------------------------RDWWWENIKKLLLEQGVD 109

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159648420 2093 GIWIDMNEPSNFLTGqypgcavndlnnppyvpsISDHSLAQKTLcpdsktylgehyntHSLFGWSQTAPTFHAAQQATG- 2171
Cdd:cd06589    110 GWWTDMGEPLPFDDA------------------TFHNGGKAQKI--------------HNAYPLNMAEATYEGQKKTFPn 157

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159648420 2172 KRAFVLSRSTFVGSGKHGGHWLGDNFSQWKDMHRSIVGILEFNLFGIPYIGADICGFN-HNTTYELCLRWMQLGSFYPFS 2250
Cdd:cd06589    158 KRPFILSRSGYAGAQRYPAIWSGDNTTTWDSLAFQIRAGLSASLSGVGYWGHDIGGFTgGDPDKELYTRWVQFGAFSPIF 237

                          330       340
                   ....*....|....*....|....*
gi 1159648420 2251 RNHNAEGNREQDPAVFGAEFAEISR 2275
Cdd:cd06589    238 RLHGDNSPRDKEPWVYGEEALAIFR 262
WD40 COG2319
WD40 repeat [General function prediction only];
1315-1632 2.94e-49

WD40 repeat [General function prediction only];


Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 181.65  E-value: 2.94e-49
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159648420 1315 QCIYTAEGHTKAVLCVDATDD--LLFTGSKDRTCKVWNLVTGQEIMSLGGHPNNVvsikycnyTSLVFT------VSTSY 1386
Cdd:COG2319    111 LLLRTLTGHTGAVRSVAFSPDgkTLASGSADGTVRLWDLATGKLLRTLTGHSGAV--------TSVAFSpdgkllASGSD 182

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159648420 1387 ---IKVWDIrDSAKCIRTLTssgqampgdvcsastnrtvaipAGENQINQIALNPTGTFL-YAAAGNSVRMWDLKRFQST 1462
Cdd:COG2319    183 dgtVRLWDL-ATGKLLRTLT----------------------GHTGAVRSVAFSPDGKLLaSGSADGTVRLWDLATGKLL 239

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159648420 1463 GKLTGHQGPVMCLTVDriSNGQdLIVTGSKDHYIKMFDVTEGALGSVSPTHNfepphyDGIEALAI--MGDNLFSGSRDN 1540
Cdd:COG2319    240 RTLTGHSGSVRSVAFS--PDGR-LLASGSADGTVRLWDLATGELLRTLTGHS------GGVNSVAFspDGKLLASGSDDG 310

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159648420 1541 GIKKWDLAQKDLLQqVPNAHKDWVCALGLVPGAPVLLSGCRGGNIKLWNVETFAPIGEMKGHDSPINAIC--TNSSQIFT 1618
Cdd:COG2319    311 TVRLWDLATGKLLR-TLTGHTGAVRSVAFSPDGKTLASGSDDGTVRLWDLATGELLRTLTGHTGAVTSVAfsPDGRTLAS 389

                          330
                   ....*....|....
gi 1159648420 1619 AADDRTVRIWKARN 1632
Cdd:COG2319    390 GSADGTVRLWDLAT 403
Rcc_KIF21A cd22263
regulatory coiled-coil domain found in kinesin-like protein KIF21A; KIF21A, also called ...
 920-1003 1.46e-47

regulatory coiled-coil domain found in kinesin-like protein KIF21A; KIF21A, also called kinesin-like protein KIF2 or renal carcinoma antigen NY-REN-62, is a microtubule-binding motor protein involved in neuronal axonal transport. It works as a microtubule stabilizer that regulates axonal morphology, suppressing cortical microtubule dynamics in neurons. Mutations in KIF21A cause congenital fibrosis of the extraocular muscles type 1 (CFEOM1). In vitro, it has a plus-end directed motor activity. This model corresponds to the regulatory coiled-coil domain of KIF21A, which folds into an intramolecular antiparallel coiled-coil monomer in solution, but crystallizes into a dimeric domain-swapped antiparallel coiled-coil.


Pssm-ID: 410204 [Multi-domain]  Cd Length: 82  Bit Score: 165.10  E-value: 1.46e-47
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159648420  920 QRMTISNMEADMNRLLTQREELTKRREKLSKRREKLMKDGGgsETDRNVQNINEEMESLTANIDYINDSISDCQANIMQM 999
Cdd:cd22263      1 QRMTISNMEADMNRLLKQREELTKRREKLSKKREKIIKENG--EGDKNVHNINEEMESLTANIDYINDSISDCQANIMQM 78


                   ....
gi 1159648420 1000 EEAK 1003
Cdd:cd22263     79 EEAK 82
GH31_xylosidase_YicI cd06593
alpha-xylosidase YicI-like; YicI alpha-xylosidase is a glycosyl hydrolase family 31 (GH31) ...
 1936-2284 1.71e-44

alpha-xylosidase YicI-like; YicI alpha-xylosidase is a glycosyl hydrolase family 31 (GH31) enzyme that catalyzes the release of an alpha-xylosyl residue from the non-reducing end of alpha-xyloside substrates such as alpha-xylosyl fluoride and isoprimeverose. YicI forms a homohexamer (a trimer of dimers). All GH31 enzymes cleave a terminal carbohydrate moiety from a substrate that varies considerably in size, depending on the enzyme, and may be either a starch or a glycoprotein. The YicI family corresponds to subgroup 4 in the Ernst et al classification of GH31 enzymes.


Pssm-ID: 269879 [Multi-domain]  Cd Length: 308  Bit Score: 164.66  E-value: 1.71e-44
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159648420 1936 GRPHMPAYWSLGFHLSRWGYGSIDVLKETVNRMHYYDIPYDVQHLDIDYMERYM--DFTYDKVNYAGLPEYIQKLKRKGM 2013
Cdd:cd06593      1 GRPPLPPAWSFGLWLSRSFYYSEEEVLEVADGMRERGIPCDVIHLDCFWMKEDWwcDFEWDEERFPDPEGMIARLKEKGF 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159648420 2014 HNVVILDPFITKDEEPgtyrpYDLGEEMGVWVNNSDGVTPAVGKAWPPGDSVFpDYTNPRTAEWWtQMCLefKDVLD--Y 2091
Cdd:cd06593     81 KVCLWINPYISQDSPL-----FKEAAEKGYLVKNPDGSPWHQWDGWQPGMGII-DFTNPEAVAWY-KEKL--KRLLDmgV 151

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159648420 2092 DGIWIDMNEpsnfltgqypgcavndlnnppYVPsisdhslaqktlcPDSKTYLGEHY-NTHSLFG--WSQTAptFHAAQQ 2168
Cdd:cd06593    152 DVIKTDFGE---------------------RIP-------------EDAVYYDGSDGrKMHNLYPllYNKAV--YEATKE 195

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159648420 2169 ATGKRAFVLSRSTFVGSGKHGGHWLGDNFSQWKDMHRSIVGILEFNLFGIPYIGADICGFNHNTTYELCLRWMQLGSFYP 2248
Cdd:cd06593    196 VKGEEAVLWARSAWAGSQRYPVHWGGDSESTFEGMAASLRGGLSLGLSGFGFWSHDIGGFEGTPSPELYKRWTQFGLLSS 275

                          330       340       350
                   ....*....|....*....|....*....|....*.
gi 1159648420 2249 FSRNHnaeGNREQDPAVFGAEFAEISRATLRIRYSL 2284
Cdd:cd06593    276 HSRLH---GSTPREPWEYGEEALDVVRKFAKLRYRL 308
GH31_lyase_GLase cd06601
alpha-1,4-glucan lyase; GLases (alpha-1,4-glucan lyases) are glycosyl hydrolase family 31 ...
 1936-2299 1.24e-41

alpha-1,4-glucan lyase; GLases (alpha-1,4-glucan lyases) are glycosyl hydrolase family 31 (GH31) enzymes that degrade alpha-1,4-glucans and maltooligosaccharides via a nonhydrolytic pathway to yield 1,5-D-anhydrofructose from the nonreducing end. GLases cleave the bond between C1 and O1 of the nonreducing sugar residue of alpha-glucans to generate a monosaccharide product with a double bond between C1 and C2. This family corresponds to subgroup 2 in the Ernst et al classification of GH31 enzymes.


Pssm-ID: 269887 [Multi-domain]  Cd Length: 347  Bit Score: 157.96  E-value: 1.24e-41
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159648420 1936 GRPHMPAYWSLGFHLSRWGYGSIDVLKETVNRMHYYDIPYDVQHLDIDYMERYMDFTYDKVNYAGLPEYIQKLKRKGMHN 2015
Cdd:cd06601      1 GRSRMKPRYVFGYHQGCYGYSSRESLEVVVQSYRDANIPLDGLHIDVDFQDNYRTFTTSKDKFPNPKEMFSNLHAQGFKC 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159648420 2016 VVILDPFITKdeepgtyrPYDLGEEMGVWVnNSDGvtpavgkawppgdsVFPDYTNPRTAEWWTQ-------MCLEFkdv 2088
Cdd:cd06601     81 STNITPIITD--------PYIGGVNYGGGL-GSPG--------------FYPDLGRPEVREWWGQqykylfdMGLEM--- 134

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159648420 2089 ldydgIWIDMNEPSnFLTGQYPGCA-----------VND--LNNPPYVPSISDHSLAQKTLCpdSKTYLGehynthslfg 2155
Cdd:cd06601    135 -----VWQDMTTPA-IAPHKINGYGdmktfplrllvTDDsvKNEHTYKPAATLWNLYAYNLH--KATYHG---------- 196

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159648420 2156 wsqtaptFHAAQQATGKRAFVLSRSTFVGSGKHGGHWLGDNFSQWKDMHRSIVGILEFNLFGIPYIGADICGF------- 2228
Cdd:cd06601    197 -------LNRLNARPNRRNFIIGRGGYAGAQRFAGLWTGDNASTWDFLQINIPQVLNLGLSGVPISGSDIGGFasgsden 269

                          330       340       350       360       370       380       390
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1159648420 2229 -NHNTTYELCLRWMQLGSFYPFSRNHNAEGNREQDPAVFGAEFA------EISRATLRIRYSLLPYLYTLFYESHVHG 2299
Cdd:cd06601    270 eGKWCDPELLIRWVQAGAFLPWFRNHYDRYIKKKQQEKLYEPYYyyepvlPICRKYVELRYRLMQVFYDAMYENTQNG 347
GH31_transferase_CtsZ cd06598
CtsZ (cyclic tetrasaccharide-synthesizing enzyme Z)-like; CtsZ is a bacterial ...
 1936-2294 1.81e-40

CtsZ (cyclic tetrasaccharide-synthesizing enzyme Z)-like; CtsZ is a bacterial 6-alpha-glucosyltransferase, first identified in Arthrobacter globiformis, that produces cyclic tetrasaccharides together with a closely related enzyme CtsY. CtsZ and CtsY both have a glycosyl hydrolase family 31 (GH31) catalytic domain; CtsY belongs to a different subfamily. All GH31 enzymes cleave a terminal carbohydrate moiety from a substrate that varies considerably in size, depending on the enzyme, and may be either a starch or a glycoprotein.


Pssm-ID: 269884  Cd Length: 332  Bit Score: 153.99  E-value: 1.81e-40
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159648420 1936 GRPHMPAYWSLGFHLSRWGYGSIDVLKETVNRMHYYDIPYDVQHLD-------IDYMERYM-DFTYDKVNYAGLPEYIQK 2007
Cdd:cd06598      1 GRPPLPPKWAFGLWQSEFGYDNWAEVDELVDTLRQKDFPLDGVVLDlywfggiIASPDGPMgDLDWDRKAFPDPAKMIAD 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159648420 2008 LKRKGMHNVVILDPFITKdeepGTYRPYDLGEEmGVWVNNSDG-VTPAVGKAWPpGDSVFPDYTNPRTAEWWTQmclEFK 2086
Cdd:cd06598     81 LKQQGVGTILIEEPYVLK----NSDEYDELVKK-GLLAKDKAGkPEPTLFNFWF-GEGGMIDWSDPEARAWWHD---RYK 151

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159648420 2087 DVLDY--DGIWIDMNEPSNfltgqYPgcavndlnnppyvpsisdhslaqktlcPDSKTYLGEHYNTHSLFG--WSQTAPT 2162
Cdd:cd06598    152 DLIDMgvAGWWTDLGEPEM-----HP---------------------------PDMVHADGDAADVHNIYNllWAKSIYD 199

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159648420 2163 FHAaQQATGKRAFVLSRSTFVGSGKHG-GHWLGDNFSQWKDMHRSIVGILEFNLFGIPYIGADICGFNHNTTY--ELCLR 2239
Cdd:cd06598    200 GYQ-RNFPEQRPFIMSRSGTAGSQRYGvIPWSGDIGRTWGGLASQINLQLHMSLSGIDYYGSDIGGFARGETLdpELYTR 278

                          330       340       350       360       370
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1159648420 2240 WMQLGSFYPFSRNHNAEGNREQdPAVFGAEFAEISRATLRIRYSLLPYLYTLFYE 2294
Cdd:cd06598    279 WFQYGAFDPPVRPHGQNLCNPE-TAPDREGTKAINRENIKLRYQLLPYYYSLAYR 332
PRK10658 PRK10658
putative alpha-glucosidase; Provisional
 1905-2385 1.96e-40

putative alpha-glucosidase; Provisional


Pssm-ID: 236731 [Multi-domain]  Cd Length: 665  Bit Score: 161.60  E-value: 1.96e-40
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159648420 1905 VTFRTIGGILDFYVFLGPTPENVVQQYTEAIGRPHMPAYWSLGFHLSRWGYGSIDvlKETVNR----MHYYDIPYDVQHL 1980
Cdd:PRK10658   227 VQFSVEGEYLEYFVIDGPTPKEVLDRYTALTGRPALPPAWSFGLWLTTSFTTNYD--EATVNSfidgMAERDLPLHVFHF 304

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159648420 1981 DIDYMERY--MDFTYDKVNY---AGLpeyIQKLKRKGMHNVVILDPFITKDEepgtyRPYDLGEEMGVWVNNSDGvtpAV 2055
Cdd:PRK10658   305 DCFWMKEFqwCDFEWDPRTFpdpEGM---LKRLKAKGLKICVWINPYIAQKS-----PLFKEGKEKGYLLKRPDG---SV 373

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159648420 2056 GK--AWPPGDSVFpDYTNPRTAEWWTQMcLE---------FK---------DVLDYDGiwidmnepsnfltgqypgcavn 2115
Cdd:PRK10658   374 WQwdKWQPGMAIV-DFTNPDACKWYADK-LKglldmgvdcFKtdfgeriptDVVWFDG---------------------- 429

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159648420 2116 dlnnppyvpsiSD----HSLAqktlcpdskTYLgehYNthslfgwsQTapTFHAAQQATGKR-AFVLSRSTFVGSGKHGG 2190
Cdd:PRK10658   430 -----------SDpqkmHNYY---------TYL---YN--------KT--VFDVLKETRGEGeAVLFARSATVGGQQFPV 476

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159648420 2191 HWLGDNFSQWKDMHRSIVGILEFNLFGIPYIGADICGFNHNTTYELCLRWMQLGSFYPFSRNHNAEGNREqdPAVFGAEF 2270
Cdd:PRK10658   477 HWGGDCYSNYESMAESLRGGLSLGLSGFGFWSHDIGGFENTATADVYKRWCAFGLLSSHSRLHGSKSYRV--PWAYDEEA 554

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159648420 2271 AEISRATLRIRYSLLPYLYTLFYESHVHGNTVARSLMHEFTSDQETHGIDTAFLWGPAFMIAPVLQEgARSVDVYFPEAT 2350
Cdd:PRK10658   555 VDVVRFFTKLKCRLMPYLYREAAEAHERGTPMMRAMVLEFPDDPACDYLDRQYMLGDSLLVAPVFSE-AGDVEYYLPEGR 633

                          490       500       510
                   ....*....|....*....|....*....|....*....
gi 1159648420 2351 WFDYYTGHKV-PSTWKK---NYATvaaplskIPLFIRGG 2385
Cdd:PRK10658   634 WTHLLTGEEVeGGRWHKeqhDFLS-------LPLLVRPN 665
WD40 cd00200
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ...
 1315-1546 2.54e-37

WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions including adaptor/regulatory modules in signal transduction, pre-mRNA processing and cytoskeleton assembly; typically contains a GH dipeptide 11-24 residues from its N-terminus and the WD dipeptide at its C-terminus and is 40 residues long, hence the name WD40; between GH and WD lies a conserved core; serves as a stable propeller-like platform to which proteins can bind either stably or reversibly; forms a propeller-like structure with several blades where each blade is composed of a four-stranded anti-parallel b-sheet; instances with few detectable copies are hypothesized to form larger structures by dimerization; each WD40 sequence repeat forms the first three strands of one blade and the last strand in the next blade; the last C-terminal WD40 repeat completes the blade structure of the first WD40 repeat to create the closed ring propeller-structure; residues on the top and bottom surface of the propeller are proposed to coordinate interactions with other proteins and/or small ligands; 7 copies of the repeat are present in this alignment.


Pssm-ID: 238121 [Multi-domain]  Cd Length: 289  Bit Score: 143.24  E-value: 2.54e-37
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159648420 1315 QCIYTAEGHTKAVLCVDATDD--LLFTGSKDRTCKVWNLVTGQEIMSLGGHPNNVVSIKYCNYTSLVFTVST-SYIKVWD 1391
Cdd:cd00200     84 ECVRTLTGHTSYVSSVAFSPDgrILSSSSRDKTIKVWDVETGKCLTTLRGHTDWVNSVAFSPDGTFVASSSQdGTIKLWD 163

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159648420 1392 IRdSAKCIRTLTSSgqampgdvcsastnrtvaipagENQINQIALNPTGTFLYAAAG-NSVRMWDLKRFQSTGKLTGHQG 1470
Cdd:cd00200    164 LR-TGKCVATLTGH----------------------TGEVNSVAFSPDGEKLLSSSSdGTIKLWDLSTGKCLGTLRGHEN 220

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1159648420 1471 PVMCLTVdriSNGQDLIVTGSKDHYIKMFDVTEGALGSVSPTHNfepphyDGIEALAIMGDN--LFSGSRDNGIKKWD 1546
Cdd:cd00200    221 GVNSVAF---SPDGYLLASGSEDGTIRVWDLRTGECVQTLSGHT------NSVTSLAWSPDGkrLASGSADGTIRIWD 289
NtCtMGAM_N pfam16863
N-terminal barrel of NtMGAM and CtMGAM, maltase-glucoamylase; NtCtMGAM_N is a beta-barrel-like ...
 1722-1830 2.97e-37

N-terminal barrel of NtMGAM and CtMGAM, maltase-glucoamylase; NtCtMGAM_N is a beta-barrel-like structure just N-terminal to the catalytic domain of maltase-glucoamylase in eukaryotes. It contributes to the architecture of the substrate-binding site, by donating a loop that comes into close contact with two regions in the catalytic domain thereby creating the site. This family is frequently found at the N-terminus of Glycosyl hydrolase 31, pfam01055.to which it contributes as above.


Pssm-ID: 465286  Cd Length: 113  Bit Score: 136.84  E-value: 2.97e-37
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159648420 1722 GWRVTLNKRQAL-SLFGNDISPIVLEVEFQTRDRLRFKLYDPNSQRFEVP---LQIDSPGVAADEANYDVELVEGSSHFR 1797
Cdd:pfam16863    1 GLTADLTLAGSPcNLYGNDIETLKLTVEYQTDNRLHVKITDPNNKRYEVPeelLPRPSPSSSASDSLYEFEYTNEPFGFK 80

                           90       100       110
                   ....*....|....*....|....*....|...
gi 1159648420 1798 IKRKSTGTVLWDSPLVDLFFSNQYLQITTTVPS 1830
Cdd:pfam16863   81 VTRKSTGEVLFDTSGGPLVFEDQFLQLSTRLPS 113
GH31_NET37 cd06592
glucosidase NET37; NET37 (also known as KIAA1161) is a human lamina-associated nuclear ...
 1971-2351 6.45e-36

glucosidase NET37; NET37 (also known as KIAA1161) is a human lamina-associated nuclear envelope transmembrane protein. A member of the glycosyl hydrolase family 31 (GH31) , it has been shown to be required for myogenic differentiation of C2C12 cells. Related proteins are found in eukaryotes and prokaryotes. Enzymes of the GH31 family possess a wide range of different hydrolytic activities including alpha-glucosidase (glucoamylase and sucrase-isomaltase), alpha-xylosidase, 6-alpha-glucosyltransferase, 3-alpha-isomaltosyltransferase and alpha-1,4-glucan lyase. All GH31 enzymes cleave a terminal carbohydrate moiety from a substrate that varies considerably in size, depending on the enzyme, and may be either a starch or a glycoprotein.


Pssm-ID: 269878 [Multi-domain]  Cd Length: 364  Bit Score: 141.59  E-value: 6.45e-36
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159648420 1971 YDIPYDVQHLDIDYMERYMDFTYDKVNYAGLPEYIQKLKRKGMHNVVILDPFITKDEEPgtyrpYDLGEEMGVWVNNSDG 2050
Cdd:cd06592     30 NGFPPSVIEIDDGWQTYYGDFEFDPEKFPDPKGMIDKLHEMGFRVTLWVHPFINPDSPN-----FRELRDKGYLVKEDSG 104

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159648420 2051 VTPAVGKaWPPGDSVFPDYTNPRTAEWWTQMCLEFKDVLDYDGIWIDMNEPSNfltgqYPgcavndlNNPPYVPSISDHS 2130
Cdd:cd06592    105 GPPLIVK-WWNGYGAVLDFTNPEARDWFKERLRELQEDYGIDGFKFDAGEASY-----LP-------ADPATFPSGLNPN 171

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159648420 2131 laqktlcPDSKTY--LGEHYNTHSlfgwsqtapTFHAAQQATGKRAFVLSRSTFvgsgKHGGHWLGdnfsqwkdMHRSIV 2208
Cdd:cd06592    172 -------EYTTLYaeLAAEFGLLN---------EVRSGWKSQGLPLFVRMSDKD----SHWGYWNG--------LRSLIP 223

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159648420 2209 GILEFNLFGIPYIGADICG----FNHNTTYELCLRWMQLGSFYP---FSrnhnaegnreqdPA---VFGAEFAEISRATL 2278
Cdd:cd06592    224 TALTQGLLGYPFVLPDMIGgnayGNFPPDKELYIRWLQLSAFMPamqFS------------VApwrNYDEEVVDIARKLA 291

                          330       340       350       360       370       380       390
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1159648420 2279 RIRYSLLPYLYTLFYESHVHGNTVARSLMHEFTSDQETHGIDTAFLWGPAFMIAPVLQEGARSVDVYFPEATW 2351
Cdd:cd06592    292 KLREKLLPYIYELAAEAVDTGEPIIRPLWWIAPEDEEALTIDDQFLLGDDILVAPVLEKGARSRDVYLPKGRW 364
PRK10426 PRK10426
alpha-glucosidase; Provisional
 1774-2385 6.62e-34

alpha-glucosidase; Provisional


Pssm-ID: 236691 [Multi-domain]  Cd Length: 635  Bit Score: 140.90  E-value: 6.62e-34
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159648420 1774 DSPGVAADEANYDVELVEGssHFRIKRKSTGTVlwdsPLVDlffsNQYLQITTTVPSTSVYGFGEQehesFKHSM----- 1848
Cdd:PRK10426    35 DNPCLWIGSGVADIDMYRG--NFSIKDKLTEKI----ALTD----NRIWLRLAADPDEHIYGCGEQ----FSYFDlrgkp 100

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159648420 1849 ---------------DFVTYGMFSRDQAPTPLVNLYGVHPFYMcveaDSNAHGVLLLNSNAQDVSLSPDPSVTFRTIGGI 1913
Cdd:PRK10426   101 fplwtseqgvgrnkqTYVTWQADCKENAGGDYYWTYFPQPTFV----SSQKYYCHVDNSAYMNFDFSAPEYHELELWEDK 176

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159648420 1914 LDFYVFLGPTPENVVQQYTEAIGRphMPAywslgfhLSRWGY--------GSIDVLKETVNRMHYYDIPydVQHLDI-DY 1984
Cdd:PRK10426   177 ATLRFECADTYISLLEKLTALFGR--QPE-------LPDWAYdgvtlgiqGGTEVVQKKLDTMRNAGVK--VNGIWAqDW 245

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159648420 1985 MERYM---------DFTYDKVNYAGLPEYIQKLKRKGMHNVVILDPFITKDeepgtyRP-YDLGEEMGVWVNNSDGVTPA 2054
Cdd:PRK10426   246 SGIRMtsfgkrlmwNWKWDSERYPQLDSRIKQLNEEGIQFLGYINPYLASD------GDlCEEAAEKGYLAKDADGGDYL 319

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159648420 2055 VgkawPPGDsvFP----DYTNPRTAEWWTQMCLefKDVLDY--DGIWIDMNEpsnfltgqypgcavndlnnppYVPSisD 2128
Cdd:PRK10426   320 V----EFGE--FYagvvDLTNPEAYEWFKEVIK--KNMIGLgcSGWMADFGE---------------------YLPT--D 368

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159648420 2129 HSLAQKTlcpdSKTYLGEHYNTHslfgWsqtAPTFHAAQQATGK--RAFVLSRSTFVGSGKHGG-HWLGDNFSQWkDMH- 2204
Cdd:PRK10426   369 AYLHNGV----SAEIMHNAWPAL----W---AKCNYEALEETGKlgEILFFMRAGYTGSQKYSTlFWAGDQNVDW-SLDd 436

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159648420 2205 ---RSIVGILEFNLFGIPYIGADICG----FNHNTTYELCLRWMQLGSFYPFSRNHnaEGNREQD-PAVFG-----AEFA 2271
Cdd:PRK10426   437 glaSVVPAALSLGMSGHGLHHSDIGGyttlFGMKRTKELLLRWCEFSAFTPVMRTH--EGNRPGDnWQFDSdaetiAHFA 514

                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159648420 2272 EISRatlrIRYSLLPYLYTLFYESHVHGNTVARSLMHEFTSDQETHGIDTAFLWGPAFMIAPVLQEGARSVDVYFPEATW 2351
Cdd:PRK10426   515 RMTR----VFTTLKPYLKELVAEAAKTGLPVMRPLFLHYEDDAATYTLKYQYLLGRDLLVAPVHEEGRTDWTVYLPEDKW 590

                          650       660       670
                   ....*....|....*....|....*....|....*...
gi 1159648420 2352 FDYYTGhkvpstwkKNYA----TVAAPLSKIPLFIRGG 2385
Cdd:PRK10426   591 VHLWTG--------EAFAggeiTVEAPIGKPPVFYRAG 620
GH31_glycosidase_Aec37 cd06599
E.coli Aec37-like; Glycosyl hydrolase family 31 (GH31) domain of a bacterial protein family ...
 1936-2250 6.03e-33

E.coli Aec37-like; Glycosyl hydrolase family 31 (GH31) domain of a bacterial protein family represented by Escherichia coli protein Aec37. The gene encoding Aec37 (aec-37) is located within a genomic island (AGI-3) isolated from the extraintestinal avian pathogenic Escherichia coli strain BEN2908. The function of Aec37 and its orthologs is unknown; however, deletion of a region of the genome that includes aec-37 affects the assimilation of seven carbohydrates, decreases growth rate of the strain in minimal medium containing galacturonate or trehalose, and attenuates the virulence of E. coli BEN2908 in chickens. All GH31 enzymes cleave a terminal carbohydrate moiety from a substrate that varies considerably in size, depending on the enzyme, and may be either a starch or a glycoprotein.


Pssm-ID: 269885 [Multi-domain]  Cd Length: 319  Bit Score: 131.57  E-value: 6.03e-33
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159648420 1936 GRPHMPAYWSLGFHLSRWGYG----SIDVLKETVNRMHYYDIPYDVQHLDIDYM-----ERYMdFTYDKVNYAGLPEYIQ 2006
Cdd:cd06599      1 GRPALPPRWSLGYLGSTMYYTeapdAQEQILDFIDTCREHDIPCDGFHLSSGYTsiedgKRYV-FNWNKDKFPDPKAFFR 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159648420 2007 KLKRKGMHNVVILDPFITKDEePgtyrPYDLGEEMGVWVNNSDGVTPAVGKAWPpGDSVFPDYTNPRTAEWWTQMCLEfk 2086
Cdd:cd06599     80 KFHERGIRLVANIKPGLLTDH-P----HYDELAEKGAFIKDDDGGEPAVGRFWG-GGGSYLDFTNPEGREWWKEGLKE-- 151

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159648420 2087 DVLDY--DGIWIDMNEpsnfltgqYPGCAVNDLnnppyvpsisdhslaqktLCPDSKTYLGEHYN-THSLFgwsqTAPTF 2163
Cdd:cd06599    152 QLLDYgiDSVWNDNNE--------YEIWDDDAA------------------CCGFGKGGPISELRpIQPLL----MARAS 201

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159648420 2164 HAAQQAT--GKRAFVLSRSTFVGSGKHGGHWLGDNFSQWKDMHRSIVGILEFNLFGIPYIGADICGFNHNT-TYELCLRW 2240
Cdd:cd06599    202 REAQLEHapNKRPFVISRSGCAGIQRYAQTWSGDNRTSWKTLKYNIAMGLGMSLSGVANYGHDIGGFAGPApEPELFVRW 281

                          330
                   ....*....|.
gi 1159648420 2241 MQLGSFYP-FS 2250
Cdd:cd06599    282 VQNGIFQPrFS 292
Rcc_KIF21 cd22248
regulatory coiled-coil domain found in the kinesin-like KIF21 family; The KIF21 family ...
 920-1003 5.45e-31

regulatory coiled-coil domain found in the kinesin-like KIF21 family; The KIF21 family includes KIF21A and KIF21B. KIF21A (also called kinesin-like protein KIF2, or renal carcinoma antigen NY-REN-62) is a microtubule-binding motor protein involved in neuronal axonal transport. It works as a microtubule stabilizer that regulates axonal morphology, suppressing cortical microtubule dynamics in neurons. Mutations in KIF21A cause congenital fibrosis of the extraocular muscles type 1 (CFEOM1). In vitro, it has a plus-end directed motor activity. KIF21B is a plus-end directed microtubule-dependent motor protein which displays processive activity. It is involved in regulation of microtubule dynamics, synapse function, and neuronal morphology, including dendritic tree branching and spine formation. KIF21B plays a role in learning and memory. It is involved in the delivery of gamma-aminobutyric acid (GABA(A)) receptors to the cell surface. This model corresponds to the regulatory coiled-coil domain of KIF21A/KIF21B, which folds into an intramolecular antiparallel coiled-coil monomer in solution but crystallizes into a dimeric domain-swapped antiparallel coiled-coil.


Pssm-ID: 410202 [Multi-domain]  Cd Length: 81  Bit Score: 117.69  E-value: 5.45e-31
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159648420  920 QRMTISNMEADMNRLLTQREELTKRREKLSKRREKLMKDGggsETDRNVQNINEEMESLTANIDYINDSISDCQANIMQM 999
Cdd:cd22248      1 NKQTISNLERDMERWLKEREKLSKELEKLEKKRERALDEG---KDESVLRDLEEEIDSLKANIDYVQENITECQSNIMQM 77


                   ....
gi 1159648420 1000 EEAK 1003
Cdd:cd22248     78 EESK 81
Rcc_KIF21B cd22262
regulatory coiled-coil domain found in kinesin-like protein KIF21B; KIF21B is a plus-end ...
 920-1003 7.15e-31

regulatory coiled-coil domain found in kinesin-like protein KIF21B; KIF21B is a plus-end directed microtubule-dependent motor protein which displays processive activity. It is involved in regulation of microtubule dynamics, synapse function, and neuronal morphology, including dendritic tree branching and spine formation. KIF21B plays a role in learning and memory. It is involved in the delivery of gamma-aminobutyric acid (GABA(A)) receptors to the cell surface. This model corresponds to a conserved region of KIF21B, which shows high sequence similarity to the regulatory coiled-coil domain of KIF21A.


Pssm-ID: 410203 [Multi-domain]  Cd Length: 82  Bit Score: 117.21  E-value: 7.15e-31
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159648420  920 QRMTISNMEADMNRLLTQREELTKRREKLSKRREKLMKDGGGSEtdRNVQNINEEMESLTANIDYINDSISDCQANIMQM 999
Cdd:cd22262      1 QRMTIINLEADMERLLKKREELSLLQEALVRKRQKLLSESPEEE--KGVQELNEEIEVLNANIDYINDSISDCQATIVQI 78


                   ....
gi 1159648420 1000 EEAK 1003
Cdd:cd22262     79 EETK 82
GH31_CPE1046 cd06596
Clostridium CPE1046-like; CPE1046 is an uncharacterized Clostridium perfringens protein with a ...
 2170-2357 5.57e-30

Clostridium CPE1046-like; CPE1046 is an uncharacterized Clostridium perfringens protein with a glycosyl hydrolase family 31 (GH31) domain. The domain architecture of CPE1046 and its orthologs includes a C-terminal fibronectin type 3 (FN3) domain and a coagulation factor 5/8 type C domain in addition to the GH31 domain. Enzymes of the GH31 family possess a wide range of different hydrolytic activities including alpha-glucosidase (glucoamylase and sucrase-isomaltase), alpha-xylosidase, 6-alpha-glucosyltransferase, 3-alpha-isomaltosyltransferase and alpha-1,4-glucan lyase. All GH31 enzymes cleave a terminal carbohydrate moiety from a substrate that varies considerably in size, depending on the enzyme, and may be either a starch or a glycoprotein.


Pssm-ID: 269882  Cd Length: 334  Bit Score: 123.22  E-value: 5.57e-30
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159648420 2170 TGKRAFVLSRSTFVGSGKHGGHWLGDNFSQWKDMHRSIVGILEFNLFGIPYIGADICG-FNHNTtyELCLRWMQLGSFYP 2248
Cdd:cd06596    142 SNARPFIWTVDGWAGTQRYAVIWTGDQSGSWEYIRFHIPTYIGSGLSGQAYATSDVDGiFGGSP--ETYTRDLQWKAFTP 219

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159648420 2249 FSRNHNAEGNREQDPAVFGAEFAEISRATLRIRYSLLPYLYTLFYESHVHGNTVARSLMHEFTSDQETHGIDTA--FLWG 2326
Cdd:cd06596    220 VLMNMSGWAANDKQPWVFGEPYTSINRKYLKLKMRLMPYIYTYAREASVTGLPMVRAMFLEYPNDPTAYGTATQyqFMWG 299

                          170       180       190
                   ....*....|....*....|....*....|....*
gi 1159648420 2327 PAFMIAPVLQEGARSVDV----YFPEATWFDYYTG 2357
Cdd:cd06596    300 PDFLVAPVYQNTAAGNDVrngiYLPAGTWIDYWTG 334
GH31_xylosidase_XylS cd06591
xylosidase XylS-like; XylS is a glycosyl hydrolase family 31 (GH31) alpha-xylosidase found in ...
 1936-2281 6.01e-29

xylosidase XylS-like; XylS is a glycosyl hydrolase family 31 (GH31) alpha-xylosidase found in prokaryotes, eukaryotes, and archaea, that catalyzes the release of alpha-xylose from the non-reducing terminal side of the alpha-xyloside substrate. XylS has been characterized in Sulfolobus solfataricus where it hydrolyzes isoprimeverose, the p-nitrophenyl-beta derivative of isoprimeverose, and xyloglucan oligosaccharides, and has transxylosidic activity. All GH31 enzymes cleave a terminal carbohydrate moiety from a substrate that varies considerably in size, depending on the enzyme, and may be either a starch or a glycoprotein. The XylS family corresponds to subgroup 3 in the Ernst et al classification of GH31 enzymes.


Pssm-ID: 269877 [Multi-domain]  Cd Length: 322  Bit Score: 119.97  E-value: 6.01e-29
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159648420 1936 GRPHMPAYWSLGFHLSRWGYGSIDVLKETVNRMHYYDIPYDVQHLDIDYMERYM--DFTYDKVNYAGLPEYIQKLKRKGM 2013
Cdd:cd06591      1 GKAPMLPKWALGFWQSKERYKTQEELLEVAREYRERGIPLDVIVQDWFYWTEQGwgDMKFDPERFPDPKGMVDELHKMNV 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159648420 2014 HNVVILDPFITKDEEpgTYRPYDlgeEMGVWVNNsdgvtpAVGKAWPPGDSVFPDYTNPRTAEW-WTQMclefKDVL-DY 2091
Cdd:cd06591     81 KLMISVWPTFGPGSE--NYKELD---EKGLLLRT------NRGNGGFGGGTAFYDATNPEAREIyWKQL----KDNYfDK 145

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159648420 2092 --DGIWIDMNEPSNFltgqypgcaVNDLNNPpyvpsisdhslaqktlcpDSKTYLG---EHYNTHSLFgwsqTAPTFHAA 2166
Cdd:cd06591    146 giDAWWLDATEPELD---------PYDFDNY------------------DGRTALGpgaEVGNAYPLM----HAKGIYEG 194

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159648420 2167 QQATG--KRAFVLSRSTFVGSGKHGGH-WLGDNFSQWKDMHRSIVGILEFNLFGIPYIGADICGF-----NHNTTY---- 2234
Cdd:cd06591    195 QRATGpdKRVVILTRSAFAGQQRYGAAvWSGDISSSWETLRRQIPAGLNFGASGIPYWTTDIGGFfggdpEPGEDDpayr 274

                          330       340       350       360
                   ....*....|....*....|....*....|....*....|....*...
gi 1159648420 2235 ELCLRWMQLGSFYPFSRNHNAEGNREQD-PAVFGAEFAEISRATLRIR 2281
Cdd:cd06591    275 ELYVRWFQFGAFCPIFRSHGTRPPREPNeIWSYGEEAYDILVKYIKLR 322
GH31_transferase_CtsY cd06597
CtsY (cyclic tetrasaccharide-synthesizing enzyme Y)-like; CtsY is a bacterial ...
 1936-2283 8.11e-27

CtsY (cyclic tetrasaccharide-synthesizing enzyme Y)-like; CtsY is a bacterial 3-alpha-isomaltosyltransferase, first identified in Arthrobacter globiformis, that produces cyclic tetrasaccharides together with a closely related enzyme CtsZ. CtsY and CtsZ both have a glycosyl hydrolase family 31 (GH31) catalytic domain; CtsZ belongs to a different subfamily. All GH31 enzymes cleave a terminal carbohydrate moiety from a substrate that varies considerably in size, depending on the enzyme, and may be either a starch or a glycoprotein.


Pssm-ID: 269883 [Multi-domain]  Cd Length: 326  Bit Score: 113.95  E-value: 8.11e-27
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159648420 1936 GRPHMPAYWSlgFHLSRWG--YGSIDVLKETVNRMHYYDIPYDVqhLDIDY---MERYMDFTYDKVNYAGLPEYIQKLKR 2010
Cdd:cd06597      1 GRAALPPKWA--FGHWVSAneWNSQAEVLELVEEYLAYDIPVGA--VVIEAwsdEATFYIFNDATGKWPDPKGMIDSLHE 76

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159648420 2011 KGMHNVVILDPFITKDEEP-GTYRP-YDLGEEMGVWVNNSDGvTPAVGKAWPPGDSVFPDYTNPRTAEWWT-QMclefKD 2087
Cdd:cd06597     77 QGIKVILWQTPVVKTDGTDhAQKSNdYAEAIAKGYYVKNGDG-TPYIPEGWWFGGGSLIDFTNPEAVAWWHdQR----DY 151

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159648420 2088 VLDYDGI--WidmnepsnfltgqypgcavndlnnppyvpsisdhslaqktlcpdsKTYLGEHYNTHSL-FGWSQTAPT-- 2162
Cdd:cd06597    152 LLDELGIdgF---------------------------------------------KTDGGEPYWGEDLiFSDGKKGREmr 186

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159648420 2163 ----------FHAAQQATGKRAFVLSRSTFVGSGKHGGHWLGDNFSQWKDMHRSIVGILEFNLFGIPYIGADICGFNHNT 2232
Cdd:cd06597    187 neypnlyykaYFDYIREIGNDGVLFSRAGDSGAQRYPIGWVGDQDSTFEGLQSALKAGLSAAWSGYPFWGWDIGGFSGPL 266

                          330       340       350       360       370       380
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1159648420 2233 -TYELCLRWMQLGSFYPFSRNHNaEGNREQDP---------AVFGAEFAEISRATLRIRYS 2283
Cdd:cd06597    267 pTAELYLRWTQLAAFSPIMQNHS-EKNHRPWSeerrwnvaeRTGDPEVLDIYRKYVKLRME 326
WD40 cd00200
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ...
 1461-1632 5.73e-26

WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions including adaptor/regulatory modules in signal transduction, pre-mRNA processing and cytoskeleton assembly; typically contains a GH dipeptide 11-24 residues from its N-terminus and the WD dipeptide at its C-terminus and is 40 residues long, hence the name WD40; between GH and WD lies a conserved core; serves as a stable propeller-like platform to which proteins can bind either stably or reversibly; forms a propeller-like structure with several blades where each blade is composed of a four-stranded anti-parallel b-sheet; instances with few detectable copies are hypothesized to form larger structures by dimerization; each WD40 sequence repeat forms the first three strands of one blade and the last strand in the next blade; the last C-terminal WD40 repeat completes the blade structure of the first WD40 repeat to create the closed ring propeller-structure; residues on the top and bottom surface of the propeller are proposed to coordinate interactions with other proteins and/or small ligands; 7 copies of the repeat are present in this alignment.


Pssm-ID: 238121 [Multi-domain]  Cd Length: 289  Bit Score: 110.50  E-value: 5.73e-26
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159648420 1461 STGKLTGHQGPVMCLtvdRISNGQDLIVTGSKDHYIKMFDVTEGALGSVSPTHnfepphYDGIEALAIMGDN--LFSGSR 1538
Cdd:cd00200      1 LRRTLKGHTGGVTCV---AFSPDGKLLATGSGDGTIKVWDLETGELLRTLKGH------TGPVRDVAASADGtyLASGSS 71

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159648420 1539 DNGIKKWDLAQKDLLQQVpNAHKDWVCALGLVPGAPVLLSGCRGGNIKLWNVETFAPIGEMKGHDSPINAICTNSSQ--I 1616
Cdd:cd00200     72 DKTIRLWDLETGECVRTL-TGHTSYVSSVAFSPDGRILSSSSRDKTIKVWDVETGKCLTTLRGHTDWVNSVAFSPDGtfV 150

                          170
                   ....*....|....*.
gi 1159648420 1617 FTAADDRTVRIWKARN 1632
Cdd:cd00200    151 ASSSQDGTIKLWDLRT 166
GH31_N cd14752
N-terminal domain of glycosyl hydrolase family 31 (GH31); This family is found N-terminal to ...
 1829-1936 1.12e-25

N-terminal domain of glycosyl hydrolase family 31 (GH31); This family is found N-terminal to the glycosyl-hydrolase domain of Glycoside hydrolase family 31 (GH31). GH31 includes the glycoside hydrolases alpha-glucosidase (EC 3.2.1.20), alpha-1,3-glucosidase (EC 3.2.1.84), alpha-xylosidase (EC 3.2.1.177), sucrase-isomaltase (EC 3.2.1.48 and EC 3.2.1.10), as well as alpha-glucan lyase (EC 4.2.2.13). All GH31 enzymes cleave a terminal carbohydrate moiety from a substrate that varies considerably in size, depending on the enzyme, and may be either a starch or a glycoprotein. In most cases, the pyranose moiety recognized in subsite-1 of the substrate binding site is an alpha-D-glucose, though some GH31 family members show a preference for alpha-D-xylose. Several GH31 enzymes can accommodate both glucose and xylose and different levels of discrimination between the two have been observed. Most characterized GH31 enzymes are alpha-glucosidases. In mammals, GH31 members with alpha-glucosidase activity are implicated in at least three distinct biological processes. The lysosomal acid alpha-glucosidase (GAA) is essential for glycogen degradation and a deficiency or malfunction of this enzyme causes glycogen storage disease II, also known as Pompe disease. In the endoplasmic reticulum, alpha-glucosidase II catalyzes the second step in the N-linked oligosaccharide processing pathway that constitutes part of the quality control system for glycoprotein folding and maturation. The intestinal enzymes sucrase-isomaltase (SI) and maltase-glucoamylase (MGAM) play key roles in the final stage of carbohydrate digestion, making alpha-glucosidase inhibitors useful in the treatment of type 2 diabetes. GH31 alpha-glycosidases are retaining enzymes that cleave their substrates via an acid/base-catalyzed, double-displacement mechanism involving a covalent glycosyl-enzyme intermediate. Two aspartic acid residues of the catalytic domain have been identified as the catalytic nucleophile and the acid/base, respectively. A loop of the N-terminal beta-sandwich domain is part of the active site pocket.


Pssm-ID: 270212 [Multi-domain]  Cd Length: 122  Bit Score: 103.80  E-value: 1.12e-25
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159648420 1829 PSTSVYGFGEQEHESFKHSMdfvTYGMFSRDQAPTPLV--NLYGVHPFYMCveadSNAHGVLLLNSNAQDVSLSPD--PS 1904
Cdd:cd14752     18 PDEHFYGLGERFGGLNKRGK---RYRLWNTDQGGYRGStdPLYGSIPFYLS----SKGYGVFLDNPSRTEFDFGSEdsDE 90

                           90       100       110
                   ....*....|....*....|....*....|..
gi 1159648420 1905 VTFRTIGGILDFYVFLGPTPENVVQQYTEAIG 1936
Cdd:cd14752     91 LTFSSEGGDLDYYFFAGPTPKEVIEQYTELTG 122
Microtub_bd pfam16796
Microtubule binding; This motor homology domain binds microtubules and lacks an ATP-binding ...
 9-159 2.49e-21

Microtubule binding; This motor homology domain binds microtubules and lacks an ATP-binding site.


Pssm-ID: 465274 [Multi-domain]  Cd Length: 144  Bit Score: 92.28  E-value: 2.49e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159648420    9 SVRVAVRIRPQLAKEkiegCHICTSVTPGEPQVFLGKDKAFTFDYVFNIDSQQEEIYvQCIEKLIEGCFEGYNATVFAYG 88
Cdd:pfam16796   21 NIRVFARVRPELLSE----AQIDYPDETSSDGKIGSKNKSFSFDRVFPPESEQEDVF-QEISQLVQSCLDGYNVCIFAYG 95

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1159648420   89 QTGAGKTYTMgtgfdvniteeeqgiISRAVKHLFRCIEEKKQAaikqglppPDFKVNAQFLELYNEEILDL 159
Cdd:pfam16796   96 QTGSGSNDGM---------------IPRAREQIFRFISSLKKG--------WKYTIELQFVEIYNESSQDL 143
WD40 cd00200
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ...
 1314-1455 4.06e-19

WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions including adaptor/regulatory modules in signal transduction, pre-mRNA processing and cytoskeleton assembly; typically contains a GH dipeptide 11-24 residues from its N-terminus and the WD dipeptide at its C-terminus and is 40 residues long, hence the name WD40; between GH and WD lies a conserved core; serves as a stable propeller-like platform to which proteins can bind either stably or reversibly; forms a propeller-like structure with several blades where each blade is composed of a four-stranded anti-parallel b-sheet; instances with few detectable copies are hypothesized to form larger structures by dimerization; each WD40 sequence repeat forms the first three strands of one blade and the last strand in the next blade; the last C-terminal WD40 repeat completes the blade structure of the first WD40 repeat to create the closed ring propeller-structure; residues on the top and bottom surface of the propeller are proposed to coordinate interactions with other proteins and/or small ligands; 7 copies of the repeat are present in this alignment.


Pssm-ID: 238121 [Multi-domain]  Cd Length: 289  Bit Score: 90.09  E-value: 4.06e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159648420 1314 LQCIYTAEGHTKAVLCVDATDD--LLFTGSKDRTCKVWNLVTGQEIMSLGGHPNNVVSIKYCNYTSLVFTVST-SYIKVW 1390
Cdd:cd00200    167 GKCVATLTGHTGEVNSVAFSPDgeKLLSSSSDGTIKLWDLSTGKCLGTLRGHENGVNSVAFSPDGYLLASGSEdGTIRVW 246

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1159648420 1391 DIRdSAKCIRTLTssgqampgdvcsastnrtvaipAGENQINQIALNPTGTFLYAAAG-NSVRMWD 1455
Cdd:cd00200    247 DLR-TGECVQTLS----------------------GHTNSVTSLAWSPDGKRLASGSAdGTIRIWD 289
GH31_u1 cd06595
glycosyl hydrolase family 31 (GH31); uncharacterized subgroup; This family represents an ...
 1936-2288 1.23e-16

glycosyl hydrolase family 31 (GH31); uncharacterized subgroup; This family represents an uncharacterized GH31 enzyme subgroup found in bacteria and eukaryotes. Enzymes of the GH31 family possess a wide range of different hydrolytic activities including alpha-glucosidase (glucoamylase and sucrase-isomaltase), alpha-xylosidase, 6-alpha-glucosyltransferase, 3-alpha-isomaltosyltransferase and alpha-1,4-glucan lyase. All GH31 enzymes cleave a terminal carbohydrate moiety from a substrate that varies considerably in size, depending on the enzyme, and may be either a starch or a glycoprotein.


Pssm-ID: 269881 [Multi-domain]  Cd Length: 304  Bit Score: 83.02  E-value: 1.23e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159648420 1936 GRPHMPAYWSLGFHLSR-WGYGSIDVlKETVNRMHYYDIPYDVQHLDIDYMERYMD-------FTYDKVNYAGLPEYIQK 2007
Cdd:cd06595      2 GKPPLIPRYALGNWWSRyWAYSDDDI-LDLVDNFKRNEIPLSVLVLDMDWHITDKKykngwtgYTWNKELFPDPKGFLDW 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159648420 2008 LKRKGMHNVVILDPF--ITKDEEPgtYRpyDLGEEMGVwvnnsdgvTPAVGKAWPpgdsvFpDYTNPRTAEWWTQMCLEF 2085
Cdd:cd06595     81 LHERGLRVGLNLHPAegIRPHEEA--YA--EFAKYLGI--------DPAKIIPIP-----F-DVTDPKFLDAYFKLLIHP 142

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159648420 2086 KDVLDYDGIWIDMNEP-SNFLTGQYPGCAVNDLnnppyvpsisdhslaqktlcpdsktylgeHYNTHSLFGwsqtaptfh 2164
Cdd:cd06595    143 LEKQGVDFWWLDWQQGkDSPLAGLDPLWWLNHY-----------------------------HYLDSGRNG--------- 184

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159648420 2165 aaqqatGKRAFVLSRSTFVGSGKHGGHWLGDNFSQWKdmhrSIVGILEFNL----FGIPYIGADICGFNHNTT-YELCLR 2239
Cdd:cd06595    185 ------KRRPLILSRWGGLGSHRYPIGFSGDTEVSWE----TLAFQPYFTAtaanVGYSWWSHDIGGHKGGIEdPELYLR 254

                          330       340       350       360       370
                   ....*....|....*....|....*....|....*....|....*....|
gi 1159648420 2240 WMQLGSFYPFSRNHNAEGNR-EQDPAVFGAEFAEISRATLRIRYSLLPYL 2288
Cdd:cd06595    255 WVQFGVFSPILRLHSDKGPYyKREPWLWDAKTFEIAKDYLRLRHRLIPYL 304
SCP-1 pfam05483
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ...
 389-1024 2.96e-16

Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major component of the transverse filaments of the synaptonemal complex. Synaptonemal complexes are structures that are formed between homologous chromosomes during meiotic prophase.


Pssm-ID: 114219 [Multi-domain]  Cd Length: 787  Bit Score: 85.54  E-value: 2.96e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159648420  389 LRSEIARLQMELMEYKTGKRI--IDEEGVESINDMFHENAMLQTENNNLRVRIKAMQETVDALRaritqlmsDQANQVLA 466
Cdd:pfam05483  204 VQAENARLEMHFKLKEDHEKIqhLEEEYKKEINDKEKQVSLLLIQITEKENKMKDLTFLLEESR--------DKANQLEE 275

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159648420  467 RAGEGNEEISNMI---HNYIKEIEDLRAKLLESEAVNENLRRNLSRAsTRSTYfggpsafsasMLSSEKET-LEILDIAK 542
Cdd:pfam05483  276 KTKLQDENLKELIekkDHLTKELEDIKMSLQRSMSTQKALEEDLQIA-TKTIC----------QLTEEKEAqMEELNKAK 344

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159648420  543 KDLEKLKKKERKKKKSVkedntdnEQEKRDEKGSSERENNELE--AEEIQEASDREDEEEEDdededdmevvessdesds 620
Cdd:pfam05483  345 AAHSFVVTEFEATTCSL-------EELLRTEQQRLEKNEDQLKiiTMELQKKSSELEEMTKF------------------ 399

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159648420  621 dsdeKENYQADLANITCEIAIKQKLIDELENSQRRLQTLKRQYEEKLMMLQHKIRDTQLERDQVLQNLGSVETYSEEkAK 700
Cdd:pfam05483  400 ----KNNKEVELEELKKILAEDEKLLDEKKQFEKIAEELKGKEQELIFLLQAREKEIHDLEIQLTAIKTSEEHYLKE-VE 474

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159648420  701 KIKSEYEKKlQTMNKEL-QRLQTAQKEHARLLKNQSQYEKQLKKLQQEVTEMKKTKVRLMKQMKEEQEkarmTESRRNRE 779
Cdd:pfam05483  475 DLKTELEKE-KLKNIELtAHCDKLLLENKELTQEASDMTLELKKHQEDIINCKKQEERMLKQIENLEE----KEMNLRDE 549

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159648420  780 IAQLKKE--QRKREHQLKL--LEAQKRNQEVILRRKTEEVTALRRQVRPLSDKVAGKVS--RKLSLPEHPIQEPSSSSSV 853
Cdd:pfam05483  550 LESVREEfiQKGDEVKCKLdkSEENARSIEYEVLKKEKQMKILENKCNNLKKQIENKNKniEELHQENKALKKKGSAENK 629

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159648420  854 EHDGSRIAAqQKMRIPVARVQALSVTATNGTGRKYQRKAVTSRVYSSRAARMKWQLLE----RRVTDIIMQRmTISNMEA 929
Cdd:pfam05483  630 QLNAYEIKV-NKLELELASAKQKFEEIIDNYQKEIEDKKISEEKLLEEVEKAKAIADEavklQKEIDKRCQH-KIAEMVA 707

                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159648420  930 DMNRLLTQREELTKRREK---LSKRREKLMKDGGGS-ETDrnVQNINEEMESLTAnidyindsisdcqanimQMEEAKEE 1005
Cdd:pfam05483  708 LMEKHKHQYDKIIEERDSelgLYKNKEQEQSSAKAAlEIE--LSNIKAELLSLKK-----------------QLEIEKEE 768

                          650
                   ....*....|....*....
gi 1159648420 1006 GETLDVTAVINACTLTEAR 1024
Cdd:pfam05483  769 KEKLKMEAKENTAILKDKK 787
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 625-1017 8.04e-14

chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]


Pssm-ID: 274009 [Multi-domain]  Cd Length: 1164  Bit Score: 77.80  E-value: 8.04e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159648420  625 KENYQADLANITCEIAIKQKLIDELENsqrRLQTLKRQYEEKlmmlqhkirdtqlERDQVLQnlgsvetyseekakKIKS 704
Cdd:TIGR02169  172 KEKALEELEEVEENIERLDLIIDEKRQ---QLERLRREREKA-------------ERYQALL--------------KEKR 221

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159648420  705 EYEKKLQtmnkeLQRLQTAQKEHARLLKNQSQYEKQLKKLQQEVTEMKKTKVRLMKQMKEEQEK-ARMTESRRNR----- 778
Cdd:TIGR02169  222 EYEGYEL-----LKEKEALERQKEAIERQLASLEEELEKLTEEISELEKRLEEIEQLLEELNKKiKDLGEEEQLRvkeki 296

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159648420  779 -----EIAQLKKEQRKREHQLKLLEAQKRNQEVILRRKTEEVTALRRQVRPLSDKVAgKVSRKLslpehpiqepsssssv 853
Cdd:TIGR02169  297 geleaEIASLERSIAEKERELEDAEERLAKLEAEIDKLLAEIEELEREIEEERKRRD-KLTEEY---------------- 359

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159648420  854 ehdgsrIAAQQKMRIPVARVQALSvtATNGTGR----KYQRK--AVTSRVYSSRAARMKWQ-LLERRVTDIIMQRMTISN 926
Cdd:TIGR02169  360 ------AELKEELEDLRAELEEVD--KEFAETRdelkDYREKleKLKREINELKRELDRLQeELQRLSEELADLNAAIAG 431

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159648420  927 MEADMNRLLTQREELtkrREKLSKRREKLMkdgggsETDRNVQNINEEMESLTANIDYINDSISDCQANIMQMEEAK--- 1003
Cdd:TIGR02169  432 IEAKINELEEEKEDK---ALEIKKQEWKLE------QLAADLSKYEQELYDLKEEYDRVEKELSKLQRELAEAEAQAras 502

                          410
                   ....*....|....*.
gi 1159648420 1004 --EEGETLDVTAVINA 1017
Cdd:TIGR02169  503 eeRVRGGRAVEEVLKA 518
GH31_glucosidase_YihQ cd06594
alpha-glucosidase YihQ-like; YihQ is a bacterial alpha-glucosidase with a conserved glycosyl ...
 1993-2262 1.17e-13

alpha-glucosidase YihQ-like; YihQ is a bacterial alpha-glucosidase with a conserved glycosyl hydrolase family 31 (GH31) domain that catalyzes the release of an alpha-glucosyl residue from the non-reducing end of alpha-glucoside substrates such as alpha-glucosyl fluoride. Orthologs of YihQ that have not yet been functionally characterized are present in plants and fungi. YihQ has sequence similarity to other GH31 enzymes such as CtsZ, a 6-alpha-glucosyltransferase from Bacillus globisporus, and YicI, an alpha-xylosidase from Echerichia coli. These latter two belong to different GH31 subfamilies than YihQ. In bacteria, YihQ (along with YihO) is important for bacterial O-antigen capsule assembly and translocation.


Pssm-ID: 269880 [Multi-domain]  Cd Length: 325  Bit Score: 74.54  E-value: 1.17e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159648420 1993 YDKVNYAGLPEYIQKLKRKGMHNVVILDPFITKDEEPGTYRPydlGEEMGVWVNNSDGVTPAVGKAwpPGDSVFPDYTNP 2072
Cdd:cd06594     65 WDEELYPGWDELVKELKEQGIRVLGYINPFLANVGPLYSYKE---AEEKGYLVKNKTGEPYLVDFG--EFDAGLVDLTNP 139

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159648420 2073 RTAEWwtqmcleFKDVLdydgiwIDMNEPSN-------FltGQYpgcavndLnnpPYVPSISDHSlaqktlcpDSKTYlg 2145
Cdd:cd06594    140 EARRW-------FKEVI------KENMIDFGlsgwmadF--GEY-------L---PFDAVLHSGE--------DAALY-- 184

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159648420 2146 ehyntHSLFG--WSQTAptfHAAQQATGK--RAFVLSRSTFVGSGKHGG-HWLGD---NFSQWKDMHRSIVGILEFNLFG 2217
Cdd:cd06594    185 -----HNRYPelWARLN---REAVEEAGKegEIVFFMRSGYTGSPRYSTlFWAGDqnvDWSRDDGLKSVIPGALSSGLSG 256

                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|...
gi 1159648420 2218 IPYIGADICGF--------NHNTTYELCLRWMQLGSFYPFSRNHnaEGNREQD 2262
Cdd:cd06594    257 FSLTHSDIGGYttlfnplvGYKRSKELLMRWAEMAAFTPVMRTH--EGNRPDD 307
Motor_domain cd01363
Myosin and Kinesin motor domain; Myosin and Kinesin motor domain. These ATPases belong to the ...
 12-350 3.13e-13

Myosin and Kinesin motor domain; Myosin and Kinesin motor domain. These ATPases belong to the P-loop NTPase family and provide the driving force in myosin and kinesin mediated processes. Some of the names do not match with what is given in the sequence list. This is because they are based on the current nomenclature by Kollmar/Sebe-Pedros.


Pssm-ID: 276814 [Multi-domain]  Cd Length: 170  Bit Score: 70.07  E-value: 3.13e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159648420   12 VAVRIRPQLAKEKIEGCHIctsvtpgepqvflgkdkaFTFDYVFNIDSQQEEIYVQCiEKLIEGCFEGYN-ATVFAYGQT 90
Cdd:cd01363      1 VLVRVNPFKELPIYRDSKI------------------IVFYRGFRRSESQPHVFAIA-DPAYQSMLDGYNnQSIFAYGES 61

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159648420   91 GAGKTYTMgtgfdvniteeeQGIISRAVKHLFRCIEEKKQAAikqglpppdfkvnaqflelyneeildlfdttrdidakn 170
Cdd:cd01363     62 GAGKTETM------------KGVIPYLASVAFNGINKGETEG-------------------------------------- 91

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159648420  171 kksnikihedsaggiyTVGVTTRTVNGESEMMQCLKLGALSRtTASTQMNVQSSRSHAIFTIhlcqtrvcppfntdnatd 250
Cdd:cd01363     92 ----------------WVYLTEITVTLEDQILQANPILEAFG-NAKTTRNENSSRFGKFIEI------------------ 136

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159648420  251 nriisessemnefetltakfhFVDLAGSERlkrtgatgerakegisINCGLLALGNVISAlgdkskkathvpyrdskltr 330
Cdd:cd01363    137 ---------------------LLDIAGFEI----------------INESLNTLMNVLRA-------------------- 159

                          330       340
                   ....*....|....*....|
gi 1159648420  331 llqdslggnSQTLMIACVSP 350
Cdd:cd01363    160 ---------TRPHFVRCISP 170
CCDC158 pfam15921
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ...
 434-1086 6.42e-13

Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.


Pssm-ID: 464943 [Multi-domain]  Cd Length: 1112  Bit Score: 74.77  E-value: 6.42e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159648420  434 NLRVRIKAMQETVDAL---RARITQLMSDQANQVLARAGEGNEEIS---NMIHNYIKEIEDLRAKLLESEAVNENLRR-- 505
Cdd:pfam15921  114 DLQTKLQEMQMERDAMadiRRRESQSQEDLRNQLQNTVHELEAAKClkeDMLEDSNTQIEQLRKMMLSHEGVLQEIRSil 193

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159648420  506 -NLSRASTRSTY------------FGgpSAFSASM--LSSE-----------KETLEILDIAKKDLEKLKKKERKKKKSV 559
Cdd:pfam15921  194 vDFEEASGKKIYehdsmstmhfrsLG--SAISKILreLDTEisylkgrifpvEDQLEALKSESQNKIELLLQQHQDRIEQ 271

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159648420  560 KEDNTDNEQEKRDEKGSSER-ENNELEA--EEIQEASDREDEEeeddededdmevvessdesdsdsdekenYQADLANIT 636
Cdd:pfam15921  272 LISEHEVEITGLTEKASSARsQANSIQSqlEIIQEQARNQNSM----------------------------YMRQLSDLE 323

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159648420  637 CEIAikqKLIDELENSQRRLQTLKRQYEEKLMMLQHKIRDTQLERDQVLQNLGSVEtyseekakkikSEYEKKLQTMNKE 716
Cdd:pfam15921  324 STVS---QLRSELREAKRMYEDKIEELEKQLVLANSELTEARTERDQFSQESGNLD-----------DQLQKLLADLHKR 389

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159648420  717 LQRLQTAQKEHARLLKNQSQYEKQLKKLQQEVTEMKKTKVRL---MKQMKEEqekarmTESRRNREIAQLKKEQRKREhQ 793
Cdd:pfam15921  390 EKELSLEKEQNKRLWDRDTGNSITIDHLRRELDDRNMEVQRLealLKAMKSE------CQGQMERQMAAIQGKNESLE-K 462

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159648420  794 LKLLEAQKRNQEVILRRKTEEVTA----LRRQVRPLSD--------------------KVAGKVSRKLSLPEHPIQEPSS 849
Cdd:pfam15921  463 VSSLTAQLESTKEMLRKVVEELTAkkmtLESSERTVSDltaslqekeraieatnaeitKLRSRVDLKLQELQHLKNEGDH 542

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159648420  850 SSSV--EHDGSRIAAQQKMR-IPVARVQALSVTATNG-----TGRKYQRKAVTSRVYSSRaaRMKWQ----LLERRVTDI 917
Cdd:pfam15921  543 LRNVqtECEALKLQMAEKDKvIEILRQQIENMTQLVGqhgrtAGAMQVEKAQLEKEINDR--RLELQefkiLKDKKDAKI 620

                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159648420  918 IMQRMTISNMEADMNRLLTQREELTKRREKLSKRREKLMKDGGGSETD------------RNVQNINEEMESLTANIDyi 985
Cdd:pfam15921  621 RELEARVSDLELEKVKLVNAGSERLRAVKDIKQERDQLLNEVKTSRNElnslsedyevlkRNFRNKSEEMETTTNKLK-- 698

                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159648420  986 ndsisdcqaniMQMEEAKEEGETldvtaviNACTLTEARYLLDHFLTMGINKGLQAAQKEAQIKVLEGRLKQTE--ITSA 1063
Cdd:pfam15921  699 -----------MQLKSAQSELEQ-------TRNTLKSMEGSDGHAMKVAMGMQKQITAKRGQIDALQSKIQFLEeaMTNA 760

                          730       740
                   ....*....|....*....|....
gi 1159648420 1064 TQNQllfHMLKE-KAELNPELDAL 1086
Cdd:pfam15921  761 NKEK---HFLKEeKNKLSQELSTV 781
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 625-836 1.09e-12

Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 443969 [Multi-domain]  Cd Length: 377  Bit Score: 72.49  E-value: 1.09e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159648420  625 KENYQADLANITCEIAIKQKLIDELENSQRRLQTLKRQYEEKLMMLQHKIRDTQLERDQVLQNLGSVETySEEKAKKIKS 704
Cdd:COG4942     22 AAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEK-EIAELRAELE 100

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159648420  705 EYEKKLQTMNKELQR-------------------------LQTAQKEHARLLKNQSQYEKQLKKLQQEVTEMKKTKVRLM 759
Cdd:COG4942    101 AQKEELAELLRALYRlgrqpplalllspedfldavrrlqyLKYLAPARREQAEELRADLAELAALRAELEAERAELEALL 180

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159648420  760 KQMKEEQEKARMTESRRNREIAQLKKEQRKREHQLKLLEAQKRNQEVILRRKTEEVTALRRQVRPLSDK---------VA 830
Cdd:COG4942    181 AELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAERTPAAGFAalkgklpwpVS 260


                   ....*.
gi 1159648420  831 GKVSRK 836
Cdd:COG4942    261 GRVVRR 266
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
363-1009 2.49e-12

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 72.79  E-value: 2.49e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159648420  363 KYANRARNIKNKVMVNQDR---ASQQINALRSEIARLQMELMEYKTGKRIIdEEGVESINDMFHENAMLQTENNNLRVRI 439
Cdd:PRK03918   183 KFIKRTENIEELIKEKEKEleeVLREINEISSELPELREELEKLEKEVKEL-EELKEEIEELEKELESLEGSKRKLEEKI 261

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159648420  440 KAMQETVDALRARITQLmSDQANQV--LARAGEGNEEISNMIHNYIKEIEDLRAKL--LESEAvnENLRRNLSRastrst 515
Cdd:PRK03918   262 RELEERIEELKKEIEEL-EEKVKELkeLKEKAEEYIKLSEFYEEYLDELREIEKRLsrLEEEI--NGIEERIKE------ 332

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159648420  516 yfggpsafsasmLSSEKETLEildiakkdleklkkkerkkkksvkedntdnEQEKRDEKgsSERENNELE--AEEIQEAs 593
Cdd:PRK03918   333 ------------LEEKEERLE------------------------------ELKKKLKE--LEKRLEELEerHELYEEA- 367

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159648420  594 dredeeeeddededdmevvessdesDSDSDEKENYQADLANITCEiaikqKLIDELENSQRRlqtlKRQYEEKLMMLQHK 673
Cdd:PRK03918   368 -------------------------KAKKEELERLKKRLTGLTPE-----KLEKELEELEKA----KEEIEEEISKITAR 413

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159648420  674 IRDTQLERDQVLQNLGSVET-----------YSEEKAKKIKSEYEKKLQTMNKELQRLQTAQKEharLLKNQSQYEKQLK 742
Cdd:PRK03918   414 IGELKKEIKELKKAIEELKKakgkcpvcgreLTEEHRKELLEEYTAELKRIEKELKEIEEKERK---LRKELRELEKVLK 490

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159648420  743 KlQQEVTEMKKTkVRLMKQMKEEQEKARMTE-SRRNREIAQLKKEQRKREHQLKLLEaqkrnqevilrRKTEEVTALRRQ 821
Cdd:PRK03918   491 K-ESELIKLKEL-AEQLKELEEKLKKYNLEElEKKAEEYEKLKEKLIKLKGEIKSLK-----------KELEKLEELKKK 557

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159648420  822 VRPLSDKVaGKVSRKLSLPEHPIQEPSSSSSVEHDGsriaaqqkmripvaRVQALsvtatngtgRKYQRKAVTSRVYSSR 901
Cdd:PRK03918   558 LAELEKKL-DELEEELAELLKELEELGFESVEELEE--------------RLKEL---------EPFYNEYLELKDAEKE 613

                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159648420  902 AARMKwQLLERRVTDIIMQRMTISNMEADMNRLLTQREELTKR--REKLSKRREKLMkdgggsETDRNVQNINEEMESLT 979
Cdd:PRK03918   614 LEREE-KELKKLEEELDKAFEELAETEKRLEELRKELEELEKKysEEEYEELREEYL------ELSRELAGLRAELEELE 686

                          650       660       670
                   ....*....|....*....|....*....|
gi 1159648420  980 ANIDYINDSISDCQANIMQMEEAKEEGETL 1009
Cdd:PRK03918   687 KRREEIKKTLEKLKEELEEREKAKKELEKL 716
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 625-831 4.92e-12

chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 72.01  E-value: 4.92e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159648420  625 KENYQADLANITCEIAIKQKLIDELENSQRRLQTLKRQYEEKLMMLQHKIRDTQLERDQVLQNLGSVETYSEEKAKKIKs 704
Cdd:TIGR02168  283 IEELQKELYALANEISRLEQQKQILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELE- 361

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159648420  705 EYEKKLQTMNkelQRLQTAQKEHARLLKNQSQYEKQLKKLQQEVTEMKKTKVRL---MKQMKEEQEKARMTESRRN---- 777
Cdd:TIGR02168  362 ELEAELEELE---SRLEELEEQLETLRSKVAQLELQIASLNNEIERLEARLERLedrRERLQQEIEELLKKLEEAElkel 438

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1159648420  778 -REIAQLKKEQRKREHQLKLLEAQKRNQEVILRRKTEEVTALRRQVRPLSDKVAG 831
Cdd:TIGR02168  439 qAELEELEEELEELQEELERLEEALEELREELEEAEQALDAAERELAQLQARLDS 493
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
638-1007 1.41e-11

Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 70.18  E-value: 1.41e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159648420  638 EIAIKQKLIDELENSQRRLQTL---KRQYEEKLMMLQHKIRDTQLERDQVLQNLGSVETYSEEKAKkikseyEKKLQTMN 714
Cdd:COG4717     72 ELKELEEELKEAEEKEEEYAELqeeLEELEEELEELEAELEELREELEKLEKLLQLLPLYQELEAL------EAELAELP 145

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159648420  715 KELQRLQTAQKEHARLlknqsqyEKQLKKLQQEVTEMKKTKVRLM-----------KQMKEEQEKARMTESRRNREIAQL 783
Cdd:COG4717    146 ERLEELEERLEELREL-------EEELEELEAELAELQEELEELLeqlslateeelQDLAEELEELQQRLAELEEELEEA 218

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159648420  784 KKEQRKREHQLKLLEAQKRNQEviLRRKTEE-------------VTALRRQVRPLSDKVAG--------------KVSRK 836
Cdd:COG4717    219 QEELEELEEELEQLENELEAAA--LEERLKEarlllliaaallaLLGLGGSLLSLILTIAGvlflvlgllallflLLARE 296

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159648420  837 LSLPEHPIQEPSSSSSVEhdgsRIAAQQKMRIpVARV---QALSVTATNGTGRKYQRKAVTSRVYSSRAARMKWQLLERR 913
Cdd:COG4717    297 KASLGKEAEELQALPALE----ELEEEELEEL-LAALglpPDLSPEELLELLDRIEELQELLREAEELEEELQLEELEQE 371

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159648420  914 VtDIIMQRMTISNmEADMNRLLTQ---REELTKRREKLSKRREKLMKDGGGSETDRNVQNINEEMESLTANIDYINDSIS 990
Cdd:COG4717    372 I-AALLAEAGVED-EEELRAALEQaeeYQELKEELEELEEQLEELLGELEELLEALDEEELEEELEELEEELEELEEELE 449

                          410       420
                   ....*....|....*....|.
gi 1159648420  991 DCQANI----MQMEEAKEEGE 1007
Cdd:COG4717    450 ELREELaeleAELEQLEEDGE 470
rad50 TIGR00606
rad50; All proteins in this family for which functions are known are involvedin recombination, ...
 581-1066 1.49e-11

rad50; All proteins in this family for which functions are known are involvedin recombination, recombinational repair, and/or non-homologous end joining.They are components of an exonuclease complex with MRE11 homologs. This family is distantly related to the SbcC family of bacterial proteins.This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University).


Pssm-ID: 129694 [Multi-domain]  Cd Length: 1311  Bit Score: 70.46  E-value: 1.49e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159648420  581 NNELEAEEIQEASDREDEEEEDDEDEDDMEVVESSDESdsdsdekENYQADLANITCEIAIKQKLIDEL--ENS------ 652
Cdd:TIGR00606  611 NNELESKEEQLSSYEDKLFDVCGSQDEESDLERLKEEI-------EKSSKQRAMLAGATAVYSQFITQLtdENQsccpvc 683

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159648420  653 QR-------------RLQTLKRQYEEKLMMLQHKIRDTQLERDQVLQNLGSVETYSEEKAKKIKsEYEKKLQTMNKELQR 719
Cdd:TIGR00606  684 QRvfqteaelqefisDLQSKLRLAPDKLKSTESELKKKEKRRDEMLGLAPGRQSIIDLKEKEIP-ELRNKLQKVNRDIQR 762

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159648420  720 LQTAQKEHARLLKNQSQYEKQLKKLQQEVTEMKktkvRLMKQMKE-----EQEKARMTESRRNREIAQLKKEQRKREHQL 794
Cdd:TIGR00606  763 LKNDIEEQETLLGTIMPEEESAKVCLTDVTIME----RFQMELKDverkiAQQAAKLQGSDLDRTVQQVNQEKQEKQHEL 838

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159648420  795 KlleaqKRNQEVILRRKTEEvtALRRQVRPLSDKVAGKVSRKLSLPEHPIQEPSSSSSVEHDGSRIaaQQKMR-IPVARV 873
Cdd:TIGR00606  839 D-----TVVSKIELNRKLIQ--DQQEQIQHLKSKTNELKSEKLQIGTNLQRRQQFEEQLVELSTEV--QSLIReIKDAKE 909

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159648420  874 QALSVTATNGTGRKYQRKAVTSRVYSSRAARMKWQLLERRVTDIIMQRMTISNMEAD-MNRLLTQRE-ELTKRREKLS-- 949
Cdd:TIGR00606  910 QDSPLETFLEKDQQEKEELISSKETSNKKAQDKVNDIKEKVKNIHGYMKDIENKIQDgKDDYLKQKEtELNTVNAQLEec 989

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159648420  950 -KRREKLMKDGGGSETDRNVQNINEEM--ESLTANIdyINDSIS---------DCQANIMQMEEAKEEGETLDvtavina 1017
Cdd:TIGR00606  990 eKHQEKINEDMRLMRQDIDTQKIQERWlqDNLTLRK--RENELKeveeelkqhLKEMGQMQVLQMKQEHQKLE------- 1060

                          490       500       510       520       530
                   ....*....|....*....|....*....|....*....|....*....|
gi 1159648420 1018 ctlTEARYL-LDHFLTMGINKGLqaaqkEAQIKVLEGRLKQTEITSATQN 1066
Cdd:TIGR00606 1061 ---ENIDLIkRNHVLALGRQKGY-----EKEIKHFKKELREPQFRDAEEK 1102
Trefoil pfam00088
Trefoil (P-type) domain;
1664-1703 2.54e-11

Trefoil (P-type) domain;


Pssm-ID: 459666  Cd Length: 43  Bit Score: 60.41  E-value: 2.54e-11
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|
gi 1159648420 1664 AVQKRIDCHPqPGASQEACEAQGCTWCATDVANAPWCFFS 1703
Cdd:pfam00088    5 PPSDRFDCGY-PGITQEECEARGCCWDPSVDPGVPWCFYP 43
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
673-989 2.62e-11

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 68.00  E-value: 2.62e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159648420  673 KIRDTQLERDQVLQNLGSVETYSEEKAKKIKSEYEKKLQTMNKELQRLQTAQKEHARLLKNQSQYEKQLKKLQQEVTEMK 752
Cdd:COG4372      7 KVGKARLSLFGLRPKTGILIAALSEQLRKALFELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEELEELN 86

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159648420  753 K---TKVRLMKQMKEEQEKARMTESRRNREIAQLKKEQRKREHQLKLLEAQKRNQEVILRRKTEEVTALRRQVRPLSDKV 829
Cdd:COG4372     87 EqlqAAQAELAQAQEELESLQEEAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEEL 166

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159648420  830 AGKVSRKLSLPEHPIQEPSSSSSVEHD-----GSRIAAQQKMRIPVARVQALSVTATNGTGRKYQRKAVTSRVYSSRAAR 904
Cdd:COG4372    167 AALEQELQALSEAEAEQALDELLKEANrnaekEEELAEAEKLIESLPRELAEELLEAKDSLEAKLGLALSALLDALELEE 246

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159648420  905 MKWQLLERRVTDIIMQRMTISNMEADMNRLLTQREELTKRREKLSKRREKLMKDGGGSETDRNVQNINEEMESLTANIDY 984
Cdd:COG4372    247 DKEELLEEVILKEIEELELAILVEKDTEEEELEIAALELEALEEAALELKLLALLLNLAALSLIGALEDALLAALLELAK 326


                   ....*
gi 1159648420  985 INDSI 989
Cdd:COG4372    327 KLELA 331
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 645-823 3.09e-11

Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 69.20  E-value: 3.09e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159648420  645 LIDELEnsqRRLQTLKRQ------YEE--------KLMMLQHKIRDTQLERDQVLQNLGSVETYSEEKAKKIkSEYEKKL 710
Cdd:COG1196    194 ILGELE---RQLEPLERQaekaerYRElkeelkelEAELLLLKLRELEAELEELEAELEELEAELEELEAEL-AELEAEL 269

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159648420  711 QTMNKELQRLQ----TAQKEHARLLKNQSQYEKQLKKLQQEVTEMKKTKVRLMKQMKEEQEKARMTESRRNREIAQLKKE 786
Cdd:COG1196    270 EELRLELEELEleleEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEA 349

                          170       180       190
                   ....*....|....*....|....*....|....*..
gi 1159648420  787 QRKREHQLKLLEAQKRNQEVILRRKTEEVTALRRQVR 823
Cdd:COG1196    350 EEELEEAEAELAEAEEALLEAEAELAEAEEELEELAE 386
PD smart00018
P or trefoil or TFF domain; Proposed role in renewal and pathology of mucous epithelia.
 1659-1702 7.26e-11

P or trefoil or TFF domain; Proposed role in renewal and pathology of mucous epithelia.


Pssm-ID: 197472  Cd Length: 46  Bit Score: 59.32  E-value: 7.26e-11
                            10        20        30        40
                    ....*....|....*....|....*....|....*....|....
gi 1159648420  1659 EQCTGAVQKRIDCHPqPGASQEACEAQGCTWCATDVaNAPWCFF 1702
Cdd:smart00018    1 AQCSVPPSERINCGP-PGITEAECEARGCCFDSSIS-GVPWCFY 42
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 626-839 1.28e-10

Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 67.27  E-value: 1.28e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159648420  626 ENYQADLANITCEIAIKQKLIDELENSQRRLQTLKRQYEEKLMMLQHKIRDTQLERDQV---LQNLGSVETYSEEKAKKI 702
Cdd:COG1196    284 EEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELeeeLEEAEEELEEAEAELAEA 363

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159648420  703 KSEYEKKLQTMNKELQRLQTAQKEHARLLKNQSQYEKQLKKLQQEVTEMKKTKVRLMKQMKEEQEKArmtESRRNREIAQ 782
Cdd:COG1196    364 EEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEAL---AELEEEEEEE 440

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 1159648420  783 LKKEQRKREHQLKLLEAQKRNQEVILRRKTEEvTALRRQVRPLSDKVAGKVSRKLSL 839
Cdd:COG1196    441 EEALEEAAEEEAELEEEEEALLELLAELLEEA-ALLEAALAELLEELAEAAARLLLL 496
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 626-830 1.36e-10

chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 67.39  E-value: 1.36e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159648420  626 ENYQADLANITCEIAIKQKLIDELENSQRRLQTLKRQYEEKLMMLQHKIRDTQLERDQVLQNLGSVETYSEEKAKKIKSE 705
Cdd:TIGR02168  708 EELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEEL 787

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159648420  706 yEKKLQTMNKELQ----RLQTAQKEHARLLKNQSQYEKQLKKLQQEVTEMKKTKVRLMKQMKEEQEK-ARMTESRRN--- 777
Cdd:TIGR02168  788 -EAQIEQLKEELKalreALDELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDiESLAAEIEElee 866

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 1159648420  778 ------REIAQLKKEQRKREHQLKLLEAQKRNQEVILRRKTEEVTALRRQVRPLSDKVA 830
Cdd:TIGR02168  867 lieeleSELEALLNERASLEEALALLRSELEELSEELRELESKRSELRRELEELREKLA 925
WD40 COG2319
WD40 repeat [General function prediction only];
1525-1637 1.72e-10

WD40 repeat [General function prediction only];


Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 65.70  E-value: 1.72e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159648420 1525 ALAIMGDNLFSGSRDNGIKKWDLAQKDLLQQVPnAHKDWVCALGLVPGAPVLLSGCRGGNIKLWNVETFAPIGEMKGHDS 1604
Cdd:COG2319     43 AASPDGARLAAGAGDLTLLLLDAAAGALLATLL-GHTAAVLSVAFSPDGRLLASASADGTVRLWDLATGLLLRTLTGHTG 121

                           90       100       110
                   ....*....|....*....|....*....|....*
gi 1159648420 1605 PINAICT--NSSQIFTAADDRTVRIWkarNVLDGQ 1637
Cdd:COG2319    122 AVRSVAFspDGKTLASGSADGTVRLW---DLATGK 153
Trefoil cd00111
P or trefoil or TFF domain; Trefoil factor family domain peptides are mucin-associated ...
 1659-1702 2.03e-10

P or trefoil or TFF domain; Trefoil factor family domain peptides are mucin-associated molecules, largely found in epithelia of gastrointestinal tissues. Function is not known but it was originally identified from mucosal tissues, where it may have a regulatory or structural role and has also been implicated as a growth fractor in other tissues.The domain is found in 1 to 6 copies where it occurs.


Pssm-ID: 238059  Cd Length: 44  Bit Score: 57.74  E-value: 2.03e-10
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....
gi 1159648420 1659 EQCTGAVQKRIDCHPqPGASQEACEAQGCTWcATDVANAPWCFF 1702
Cdd:cd00111      1 EWCSVPPSERIDCGP-PGITQEECEARGCCF-DPSISGVPWCFY 42
TPH pfam13868
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ...
 642-811 3.23e-10

Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of eukaryotic proteins. Trichoplein or mitostatin, was first defined as a meiosis-specific nuclear structural protein. It has since been linked with mitochondrial movement. It is associated with the mitochondrial outer membrane, and over-expression leads to reduction in mitochondrial motility whereas lack of it enhances mitochondrial movement. The activity appears to be mediated through binding the mitochondria to the actin intermediate filaments (IFs). The family is in the trichohyalin-plectin-homology domain.


Pssm-ID: 464007 [Multi-domain]  Cd Length: 341  Bit Score: 64.17  E-value: 3.23e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159648420  642 KQKLIDELENSQRRLQTLKRQYEEKLMMLQHKIRDTQLERDQVLQNLGsVETYSEEKAKKIKSEYEKKLQtMNKELQRLQ 721
Cdd:pfam13868  164 KAEREEEREAEREEIEEEKEREIARLRAQQEKAQDEKAERDELRAKLY-QEEQERKERQKEREEAEKKAR-QRQELQQAR 241

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159648420  722 TAQKEHARLLKnqsqyEKQLKKLQQEVTEMKKTKVRLMKQMKEEQEKARMTESRRNREIAQL---KKEQRKREHQLKLLE 798
Cdd:pfam13868  242 EEQIELKERRL-----AEEAEREEEEFERMLRKQAEDEEIEQEEAEKRRMKRLEHRRELEKQieeREEQRAAEREEELEE 316

                          170
                   ....*....|...
gi 1159648420  799 AQKRNQEVILRRK 811
Cdd:pfam13868  317 GERLREEEAERRE 329
Myosin_tail_1 pfam01576
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ...
 643-1005 3.52e-10

Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.


Pssm-ID: 460256 [Multi-domain]  Cd Length: 1081  Bit Score: 65.97  E-value: 3.52e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159648420  643 QKLIDEL---ENSQRRL----QTLKRQYEEKLmmlqhKIRDTQLE--RDQVLQNLGSVETYSEE--KAKKIKSEYEKKLQ 711
Cdd:pfam01576  702 EELEDELqatEDAKLRLevnmQALKAQFERDL-----QARDEQGEekRRQLVKQVRELEAELEDerKQRAQAVAAKKKLE 776

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159648420  712 TMNKELQrlqtAQKEHARllKNQSQYEKQLKKLQQEvtemkktkvrlMKQMKEEQEKARMteSRRnrEIAQLKKEQRKRe 791
Cdd:pfam01576  777 LDLKELE----AQIDAAN--KGREEAVKQLKKLQAQ-----------MKDLQRELEEARA--SRD--EILAQSKESEKK- 834

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159648420  792 hqLKLLEAQkrnqeviLRRKTEEVTA---LRRQVR----PLSDKVAGKVSRKLSLP-------------EHPIQEPSSSS 851
Cdd:pfam01576  835 --LKNLEAE-------LLQLQEDLAAserARRQAQqerdELADEIASGASGKSALQdekrrleariaqlEEELEEEQSNT 905

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159648420  852 SVEHDGSRIAAQQkmripvarvqALSVTATNGTGRKYQRKAVTSRVYSSRA---ARMKWQLLERRVTDiiMQRMTISNME 928
Cdd:pfam01576  906 ELLNDRLRKSTLQ----------VEQLTTELAAERSTSQKSESARQQLERQnkeLKAKLQEMEGTVKS--KFKSSIAALE 973

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159648420  929 ADMNRLLTQREELTKRRE---KLSKRREKLMKDGGGSETD--RNVQNINEEMESLTANIDYINdsisdcqaniMQMEEAK 1003
Cdd:pfam01576  974 AKIAQLEEQLEQESRERQaanKLVRRTEKKLKEVLLQVEDerRHADQYKDQAEKGNSRMKQLK----------RQLEEAE 1043


                   ..
gi 1159648420 1004 EE 1005
Cdd:pfam01576 1044 EE 1045
DUF5401 pfam17380
Family of unknown function (DUF5401); This is a family of unknown function found in ...
 660-822 3.99e-10

Family of unknown function (DUF5401); This is a family of unknown function found in Chromadorea.


Pssm-ID: 375164 [Multi-domain]  Cd Length: 722  Bit Score: 65.53  E-value: 3.99e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159648420  660 KRQYEEKL-MMLQHKIRDT------QLERDQVLQNLGSVETYSEEKAKKIKSEYEKKLQTMNKELQRLQtaQKEHARLLK 732
Cdd:pfam17380  286 ERQQQEKFeKMEQERLRQEkeekarEVERRRKLEEAEKARQAEMDRQAAIYAEQERMAMERERELERIR--QEERKRELE 363

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159648420  733 NQSQYE--------KQLKKLQ-----------QEVTEMKKTKV-------------RLMKQMKEEQEKARMTESR----- 775
Cdd:pfam17380  364 RIRQEEiameisrmRELERLQmerqqknervrQELEAARKVKIleeerqrkiqqqkVEMEQIRAEQEEARQREVRrleee 443

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|...
gi 1159648420  776 RNREIAQLKKEQRKREHQLKLL---EAQKRNQEVIL---RRKTEEVTALRRQV 822
Cdd:pfam17380  444 RAREMERVRLEEQERQQQVERLrqqEEERKRKKLELekeKRDRKRAEEQRRKI 496
COG1340 COG1340
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
638-815 4.14e-10

Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];


Pssm-ID: 440951 [Multi-domain]  Cd Length: 297  Bit Score: 63.39  E-value: 4.14e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159648420  638 EIAIKQKLIDELENSQRRLQTLKRQYEEKLMMLQHKIRDTQLERDQVLQnlgsVETYSE--EKAKKIKsEYEKKLQTMNK 715
Cdd:COG1340     93 ELDELRKELAELNKAGGSIDKLRKEIERLEWRQQTEVLSPEEEKELVEK----IKELEKelEKAKKAL-EKNEKLKELRA 167

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159648420  716 ELQRLQTAQKEHARLLK---NQSQ-YEKQLKKLQQEVTEMKKTKVRLMKQMKEEQEKARMTesrrNREIAQLKKEQRKRE 791
Cdd:COG1340    168 ELKELRKEAEEIHKKIKelaEEAQeLHEEMIELYKEADELRKEADELHKEIVEAQEKADEL----HEEIIELQKELRELR 243

                          170       180
                   ....*....|....*....|....*....
gi 1159648420  792 HQL-----KLLEAQKRNQEVILRRKTEEV 815
Cdd:COG1340    244 KELkklrkKQRALKREKEKEELEEKAEEI 272
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
643-823 4.78e-10

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 64.15  E-value: 4.78e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159648420  643 QKLIDELENSQRRLQTLKRQYEEklmmlqhkirdTQLERDQVLQNLgsvetyseEKAKKIKSEYEKKLQTMNKELQRLQT 722
Cdd:COG4372     34 RKALFELDKLQEELEQLREELEQ-----------AREELEQLEEEL--------EQARSELEQLEEELEELNEQLQAAQA 94

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159648420  723 AQKEHARLLKnqsQYEKQLKKLQQEVTEMKKTKVRLM---KQMKEEQEKARMTESRRNREIAQLKKEQRKREHQLKLLEA 799
Cdd:COG4372     95 ELAQAQEELE---SLQEEAEELQEELEELQKERQDLEqqrKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAALEQ 171

                          170       180
                   ....*....|....*....|....
gi 1159648420  800 QkrNQEVILRRKTEEVTALRRQVR 823
Cdd:COG4372    172 E--LQALSEAEAEQALDELLKEAN 193
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 651-958 5.62e-10

chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]


Pssm-ID: 274009 [Multi-domain]  Cd Length: 1164  Bit Score: 65.09  E-value: 5.62e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159648420  651 NSQRRLQTLKRQYEEKLMMLQHKIRDTQLERDQVLQNLGSVETYSEEKAKKIkSEYEKKLQTMNKELQRLQtaqKEHARL 730
Cdd:TIGR02169  660 RAPRGGILFSRSEPAELQRLRERLEGLKRELSSLQSELRRIENRLDELSQEL-SDASRKIGEIEKEIEQLE---QEEEKL 735

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159648420  731 LKNQSQYEKQLKKLQQEVTEMKKTKVRLMKQMKEEQEK--------ARMTESRRNREIAQLKKEQRKREHQLKLLEAQKR 802
Cdd:TIGR02169  736 KERLEELEEDLSSLEQEIENVKSELKELEARIEELEEDlhkleealNDLEARLSHSRIPEIQAELSKLEEEVSRIEARLR 815

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159648420  803 NQEVILRRKT-------EEVTALRRQVRPLSDKVA----------GKVSRKLS-LPEHPIQEPSSSSSVEH-DGSRIAAQ 863
Cdd:TIGR02169  816 EIEQKLNRLTlekeyleKEIQELQEQRIDLKEQIKsiekeienlnGKKEELEEeLEELEAALRDLESRLGDlKKERDELE 895

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159648420  864 QKMRIPVARVQALSVTATNGTGRKYQRKAVTSRVYSSRAA--RMKWQLLERRVTDIIMQ--RMTISNMEADMNRL----- 934
Cdd:TIGR02169  896 AQLRELERKIEELEAQIEKKRKRLSELKAKLEALEEELSEieDPKGEDEEIPEEELSLEdvQAELQRVEEEIRALepvnm 975

                          330       340
                   ....*....|....*....|....*.
gi 1159648420  935 --LTQREELTKRREKLSKRREKLMKD 958
Cdd:TIGR02169  976 laIQEYEEVLKRLDELKEKRAKLEEE 1001
DR0291 COG1579
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ...
 646-800 7.75e-10

Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];


Pssm-ID: 441187 [Multi-domain]  Cd Length: 236  Bit Score: 61.48  E-value: 7.75e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159648420  646 IDELENSQRRLQTLKRQYEEKLMMLQHKIRDTQLERDQVLQNLGSVETYSEEKAKKIKsEYEKKLQTM--NKELQRLQta 723
Cdd:COG1579     19 LDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIK-KYEEQLGNVrnNKEYEALQ-- 95

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1159648420  724 qKEHARLLKNQSQYEKQLKKLQQEVTEMKKTKVRLMKQMKEEQEKARMTESRRNREIAQLKKEQRKREHQLKLLEAQ 800
Cdd:COG1579     96 -KEIESLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEELAELEAELEELEAEREELAAK 171
ERM_helical pfam20492
Ezrin/radixin/moesin, alpha-helical domain; The ERM family consists of three closely-related ...
 697-823 9.05e-10

Ezrin/radixin/moesin, alpha-helical domain; The ERM family consists of three closely-related proteins, ezrin, radixin and moesin. Ezrin was first identified as a constituent of microvilli, radixin as a barbed, end-capping actin-modulating protein from isolated junctional fractions, and moesin as a heparin binding protein. A tumour suppressor molecule responsible for neurofibromatosis type 2 (NF2) is highly similar to ERM proteins and has been designated merlin (moesin-ezrin-radixin-like protein). ERM molecules contain 3 domains, an N-terminal globular domain, an extended alpha-helical domain and a charged C-terminal domain (pfam00769). Ezrin, radixin and merlin also contain a polyproline linker region between the helical and C-terminal domains. The N-terminal domain is highly conserved and is also found in merlin, band 4.1 proteins and members of the band 4.1 superfamily, designated the FERM domain. ERM proteins crosslink actin filaments with plasma membranes. They co-localize with CD44 at actin filament plasma membrane interaction sites, associating with CD44 via their N-terminal domains and with actin filaments via their C-terminal domains. This is the alpha-helical domain, which is involved in intramolecular masking of protein-protein interaction sites, regulating the activity of this proteins.


Pssm-ID: 466641 [Multi-domain]  Cd Length: 120  Bit Score: 58.39  E-value: 9.05e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159648420  697 EKAKKIKSEYEKKLQTMNKELQRLQTA---QKEHARLLknqsqyEKQLKKLQQEVTEMKKtkvrlmKQMKEEQEKARMTE 773
Cdd:pfam20492    2 EEAEREKQELEERLKQYEEETKKAQEEleeSEETAEEL------EEERRQAEEEAERLEQ------KRQEAEEEKERLEE 69

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|
gi 1159648420  774 SRRNREIAQLKKEQRKREHQlklLEAQKRNQEVilRRKTEEVTALRRQVR 823
Cdd:pfam20492   70 SAEMEAEEKEQLEAELAEAQ---EEIARLEEEV--ERKEEEARRLQEELE 114
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
626-1102 3.48e-09

Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 62.63  E-value: 3.48e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159648420  626 ENYQADLANITCEIAIKQKLIDELENSqrrLQTLKRQYEE----KLMMLQHKIRDTQLERDQVLQNLGSVET-------- 693
Cdd:COG4913    298 EELRAELARLEAELERLEARLDALREE---LDELEAQIRGnggdRLEQLEREIERLERELEERERRRARLEAllaalglp 374

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159648420  694 --YSEEKAKKIKSEYEKKLQTMNKELQRLQTAQkehARLLKNQSQYEKQLKKLQQEVTEMKKTKVRLMKQMkeEQEKARM 771
Cdd:COG4913    375 lpASAEEFAALRAEAAALLEALEEELEALEEAL---AEAEAALRDLRRELRELEAEIASLERRKSNIPARL--LALRDAL 449

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159648420  772 TESRRNREIA--------QLKKEQRK---------REHQLKLLEAQKRNQEVI-------LRRK--TEEV-TALRRQVRP 824
Cdd:COG4913    450 AEALGLDEAElpfvgeliEVRPEEERwrgaiervlGGFALTLLVPPEHYAAALrwvnrlhLRGRlvYERVrTGLPDPERP 529

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159648420  825 LSDkvAGKVSRKLSLPEHPIQEpssssSVEHdgsRIaAQQKMRIPVARVQAL-----SVTAT-----NGT-GRKYQRKAV 893
Cdd:COG4913    530 RLD--PDSLAGKLDFKPHPFRA-----WLEA---EL-GRRFDYVCVDSPEELrrhprAITRAgqvkgNGTrHEKDDRRRI 598

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159648420  894 TSR-VYSSRAARmKWQLLERRVTDIimqrmtisnmEADMNRLLTQREELTKRREKLSKRREKLMKDGGGSETDRNVQNIN 972
Cdd:COG4913    599 RSRyVLGFDNRA-KLAALEAELAEL----------EEELAEAEERLEALEAELDALQERREALQRLAEYSWDEIDVASAE 667

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159648420  973 EEMESLTANIDYINDSISDCQANIMQMEEAKEEGETLDvtAVINACTLTEARylLDHfltmginkglQAAQKEAQIKVLE 1052
Cdd:COG4913    668 REIAELEAELERLDASSDDLAALEEQLEELEAELEELE--EELDELKGEIGR--LEK----------ELEQAEEELDELQ 733

                          490       500       510       520       530
                   ....*....|....*....|....*....|....*....|....*....|
gi 1159648420 1053 GRLKQTEItsatqnqllfhmlKEKAELNPELDALLGHALQDNLEDSTDED 1102
Cdd:COG4913    734 DRLEAAED-------------LARLELRALLEERFAAALGDAVERELREN 770
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 698-1103 3.73e-09

chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 62.38  E-value: 3.73e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159648420  698 KAKKIKSEYEKKLQTMNKELQRLQTAQKEHARLLKN---QSQYEKQLKKLQQEVTEMKKT-KVRLMKQMKEEQEKARMTE 773
Cdd:TIGR02168  169 KYKERRKETERKLERTRENLDRLEDILNELERQLKSlerQAEKAERYKELKAELRELELAlLVLRLEELREELEELQEEL 248

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159648420  774 SRRNREIAQLKKEQRKREHQLKLLEAQKRNQEvilRRKTEEVTALRRQVRPLSDKVAGKVSRKLSLPEHPIQEPSSSSSV 853
Cdd:TIGR02168  249 KEAEEELEELTAELQELEEKLEELRLEVSELE---EEIEELQKELYALANEISRLEQQKQILRERLANLERQLEELEAQL 325

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159648420  854 EHDGSR------IAAQQKMRIPVARVQALSvtatngtgrkyQRKAVTsrvyssrAARMKWQLLERRVTDiimQRMTISNM 927
Cdd:TIGR02168  326 EELESKldelaeELAELEEKLEELKEELES-----------LEAELE-------ELEAELEELESRLEE---LEEQLETL 384

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159648420  928 EADMNRLLTQREELTKRREKLSKRREKLmkdgggsetDRNVQNINEEMESLTANIDyiNDSISDCQANIMQMEEAKEEGE 1007
Cdd:TIGR02168  385 RSKVAQLELQIASLNNEIERLEARLERL---------EDRRERLQQEIEELLKKLE--EAELKELQAELEELEEELEELQ 453

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159648420 1008 TLDVTAVINACTLTEARYLLDHFLTMGINKGLQAAQKEAQIKVLEGRLK--QTEITSATQNQLLFH----MLKEKAELNP 1081
Cdd:TIGR02168  454 EELERLEEALEELREELEEAEQALDAAERELAQLQARLDSLERLQENLEgfSEGVKALLKNQSGLSgilgVLSELISVDE 533

                          410       420
                   ....*....|....*....|....*.
gi 1159648420 1082 E----LDALLGHALQdNLEDSTDEDA 1103
Cdd:TIGR02168  534 GyeaaIEAALGGRLQ-AVVVENLNAA 558
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 652-1028 1.30e-08

chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 60.84  E-value: 1.30e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159648420  652 SQRRLQTLKRQYE-----EKLMMLQHKIRDTQLERDQVLQNLGSVETySEEKAKKIKSEYEKKLQTMNKELQRLQtaqKE 726
Cdd:TIGR02168  666 AKTNSSILERRREieeleEKIEELEEKIAELEKALAELRKELEELEE-ELEQLRKELEELSRQISALRKDLARLE---AE 741

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159648420  727 HARLLKNQSQYEKQLKKLQQEVTEMKktkvrlmkqmkEEQEKARMTESRRNREIAQLKKEQRKREHQLKLLEaqkrnqev 806
Cdd:TIGR02168  742 VEQLEERIAQLSKELTELEAEIEELE-----------ERLEEAEEELAEAEAEIEELEAQIEQLKEELKALR-------- 802

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159648420  807 ilrrktEEVTALRRQVRPLSDKVAGKVSR------KLSLPEHPIQEPSSSSSV-EHDGSRIAAQQ-KMRIPVARVQAlsv 878
Cdd:TIGR02168  803 ------EALDELRAELTLLNEEAANLRERleslerRIAATERRLEDLEEQIEElSEDIESLAAEIeELEELIEELES--- 873

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159648420  879 tatngtgrkyQRKAVTSRVYSSRAARMKWQLLERRVTDiimqrmTISNMEADMNRLLTQREELTKRREKLSKRREKLMkd 958
Cdd:TIGR02168  874 ----------ELEALLNERASLEEALALLRSELEELSE------ELRELESKRSELRRELEELREKLAQLELRLEGLE-- 935

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159648420  959 gggSETDRNVQNINEE----MESLTANIDYINDSISDCQA---------------NIMQMEEAKEEGETLD-VTAVINac 1018
Cdd:TIGR02168  936 ---VRIDNLQERLSEEysltLEEAEALENKIEDDEEEARRrlkrlenkikelgpvNLAAIEEYEELKERYDfLTAQKE-- 1010

                          410
                   ....*....|
gi 1159648420 1019 TLTEARYLLD 1028
Cdd:TIGR02168 1011 DLTEAKETLE 1020
SMC_N pfam02463
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ...
 642-1102 1.31e-08

RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The SMC (structural maintenance of chromosomes) superfamily proteins have ATP-binding domains at the N- and C-termini, and two extended coiled-coil domains separated by a hinge in the middle. The eukaryotic SMC proteins form two kind of heterodimers: the SMC1/SMC3 and the SMC2/SMC4 types. These heterodimers constitute an essential part of higher order complexes, which are involved in chromatin and DNA dynamics. This family also includes the RecF and RecN proteins that are involved in DNA metabolism and recombination.


Pssm-ID: 426784 [Multi-domain]  Cd Length: 1161  Bit Score: 60.76  E-value: 1.31e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159648420  642 KQKLIDELENSQRR-LQTLKRQYEEKLMMLQ-HKIRDTQLERDQVLQNLGSVETYSEEKAKKIKSE-YEKKLQTMNKELQ 718
Cdd:pfam02463  287 ELKLLAKEEEELKSeLLKLERRKVDDEEKLKeSEKEKKKAEKELKKEKEEIEELEKELKELEIKREaEEEEEEELEKLQE 366

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159648420  719 RLQTAQKEHARLLKNQSQYEKQLKKLQQEVTEMKKTKVRLMK------QMKEEQEKARMTESRRNREIAQ---------- 782
Cdd:pfam02463  367 KLEQLEEELLAKKKLESERLSSAAKLKEEELELKSEEEKEAQlllelaRQLEDLLKEEKKEELEILEEEEesielkqgkl 446

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159648420  783 ---------LKKEQRKREHQLKLLEAQ-KRNQEVILRRKTEEVTALRRQVRPLSDKVAGKVSRKLSLPEHPIQEPSSSSS 852
Cdd:pfam02463  447 teekeelekQELKLLKDELELKKSEDLlKETQLVKLQEQLELLLSRQKLEERSQKESKARSGLKVLLALIKDGVGGRIIS 526

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159648420  853 VEHDGSR---IAAQQKMRIPVARVQALSVTATNGTGRKYQRKAVT-------SRVYSSRAARMKWQLLERRVTDIIMQRM 922
Cdd:pfam02463  527 AHGRLGDlgvAVENYKVAISTAVIVEVSATADEVEERQKLVRALTelplgarKLRLLIPKLKLPLKSIAVLEIDPILNLA 606

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159648420  923 TISNMEADMNRLLTQREELTKRREKLSKRREKLMKDGGGSETDRNVQNINEEMESLTANidyINDSISDCQANIMQMEEA 1002
Cdd:pfam02463  607 QLDKATLEADEDDKRAKVVEGILKDTELTKLKESAKAKESGLRKGVSLEEGLAEKSEVK---ASLSELTKELLEIQELQE 683

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159648420 1003 KEEGETLdvTAVINACTLTEARYLLdHFLTMGINKGLQAAQKEAQIKVLEGRLKQTEITSATQNQLLFHMLKEKAEL-NP 1081
Cdd:pfam02463  684 KAESELA--KEEILRRQLEIKKKEQ-REKEELKKLKLEAEELLADRVQEAQDKINEELKLLKQKIDEEEEEEEKSRLkKE 760

                          490       500
                   ....*....|....*....|.
gi 1159648420 1082 ELDALLGHALQDNLEDSTDED 1102
Cdd:pfam02463  761 EKEEEKSELSLKEKELAEERE 781
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
638-1003 1.57e-08

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 60.46  E-value: 1.57e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159648420  638 EIAIKQKL-IDELENSQRRLQTLKRQYEEKLMMLQHKIRdtqlerdqvlqnlgsvetySEEKAKKIKSEYEKKLQTMNKE 716
Cdd:PRK03918   148 EKVVRQILgLDDYENAYKNLGEVIKEIKRRIERLEKFIK-------------------RTENIEELIKEKEKELEEVLRE 208

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159648420  717 LQRLQTAQKEHARLLKNQSQYEKQLKKLQQEVTEMKKTKVRLMKQMKEEQEKARMTESRrnreIAQLKKEQRKREHQLKL 796
Cdd:PRK03918   209 INEISSELPELREELEKLEKEVKELEELKEEIEELEKELESLEGSKRKLEEKIRELEER----IEELKKEIEELEEKVKE 284

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159648420  797 LEAQKRNQE--VILRRKTEEVTALRRQVrplsDKVAGKVSRKLSLPEHPIQEPSS-SSSVEHDGSRIAAQQKmripvaRV 873
Cdd:PRK03918   285 LKELKEKAEeyIKLSEFYEEYLDELREI----EKRLSRLEEEINGIEERIKELEEkEERLEELKKKLKELEK------RL 354

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159648420  874 QALSVTAtngtgRKYQRkavtsrvyssraARMKWQLLERrvtdiIMQRMTISNMeadmnrlltqrEELTKRREKLSKRRE 953
Cdd:PRK03918   355 EELEERH-----ELYEE------------AKAKKEELER-----LKKRLTGLTP-----------EKLEKELEELEKAKE 401

                          330       340       350       360       370
                   ....*....|....*....|....*....|....*....|....*....|
gi 1159648420  954 KLMkdgggsetdrnvqninEEMESLTANIDYINDSISDCQANIMQMEEAK 1003
Cdd:PRK03918   402 EIE----------------EEISKITARIGELKKEIKELKKAIEELKKAK 435
Mplasa_alph_rch TIGR04523
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
 357-812 1.73e-08

helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.


Pssm-ID: 275316 [Multi-domain]  Cd Length: 745  Bit Score: 60.03  E-value: 1.73e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159648420  357 ETLNTLKyaNRARNIKNKVMVNQ---DRASQQINALRSEIARLQMELMEYKTGK-RIIDEEGVESINDMFHENAMLQTEN 432
Cdd:TIGR04523  253 TQLNQLK--DEQNKIKKQLSEKQkelEQNNKKIKELEKQLNQLKSEISDLNNQKeQDWNKELKSELKNQEKKLEEIQNQI 330

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159648420  433 NNLRVRIKAMQETVDALRARITQLMSD---------QANQVLARAGEGNEEISNMIHNYIKEIEDLRAKLLESEAVNENL 503
Cdd:TIGR04523  331 SQNNKIISQLNEQISQLKKELTNSESEnsekqreleEKQNEIEKLKKENQSYKQEIKNLESQINDLESKIQNQEKLNQQK 410

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159648420  504 RRNLSRastrstyfggpsafsasmLSSEKETL--EILDIakkdleklkkkerkkkksvKEDNTDNEQEKRD---EKGSSE 578
Cdd:TIGR04523  411 DEQIKK------------------LQQEKELLekEIERL-------------------KETIIKNNSEIKDltnQDSVKE 453

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159648420  579 RENNELEA-EEIQEasdredeeeeddededdmevvessDESDSDSDEKENYQADLANITCEIAIKQKLIDEL--ENSQ-- 653
Cdd:TIGR04523  454 LIIKNLDNtRESLE------------------------TQLKVLSRSINKIKQNLEQKQKELKSKEKELKKLneEKKEle 509

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159648420  654 RRLQTLKRQYEEklmmLQHKIRDTQLERDQVLQNLGSVETYSEE-KAKKIKSEYEKKLQTMNKELQRLQTAQKEharLLK 732
Cdd:TIGR04523  510 EKVKDLTKKISS----LKEKIEKLESEKKEKESKISDLEDELNKdDFELKKENLEKEIDEKNKEIEELKQTQKS---LKK 582

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159648420  733 NQSQYEKQLKKLQQEVTEMKKtkvrlmkqmkeEQEKARMTESRRNREIAQLKKEQRKREHQLKLLEAQKR--NQEVILRR 810
Cdd:TIGR04523  583 KQEEKQELIDQKEKEKKDLIK-----------EIEEKEKKISSLEKELEKAKKENEKLSSIIKNIKSKKNklKQEVKQIK 651


                   ..
gi 1159648420  811 KT 812
Cdd:TIGR04523  652 ET 653
CwlO1 COG3883
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ...
 625-905 1.74e-08

Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];


Pssm-ID: 443091 [Multi-domain]  Cd Length: 379  Bit Score: 59.07  E-value: 1.74e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159648420  625 KENYQADLANITCEIaikQKLIDELENSQRRLQTLKRQYEEklmmLQHKIRDTQLERDQVLQNL----GSVETYSEEKAK 700
Cdd:COG3883     18 IQAKQKELSELQAEL---EAAQAELDALQAELEELNEEYNE----LQAELEALQAEIDKLQAEIaeaeAEIEERREELGE 90

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159648420  701 KIKSEYE--------------KKLQTMNKELQRLQTAQKEHARLLKNQSQYEKQLKKLQQEVTEMKKTKVRLMKQMKEEQ 766
Cdd:COG3883     91 RARALYRsggsvsyldvllgsESFSDFLDRLSALSKIADADADLLEELKADKAELEAKKAELEAKLAELEALKAELEAAK 170

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159648420  767 EKARMTESRRNREIAQLKKEQRKREHQLKLLEAQKRNQEVILRRKTEEVTAlRRQVRPLSDKVAGKVSRKLSLPEHPIQE 846
Cdd:COG3883    171 AELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAA-AAAAAAAAAAAAAAAAAAAAAAASAAGA 249

                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 1159648420  847 PSSSSSVEHDGSRIAAQQKMRIPVARVQALSVTATNGTGRKYQRKAVTSRVYSSRAARM 905
Cdd:COG3883    250 GAAGAAGAAAGSAGAAGAAAGAAGAGAAAASAAGGGAGGAGGGGGGGGAASGGSGGGSG 308
TPH pfam13868
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ...
 642-823 2.22e-08

Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of eukaryotic proteins. Trichoplein or mitostatin, was first defined as a meiosis-specific nuclear structural protein. It has since been linked with mitochondrial movement. It is associated with the mitochondrial outer membrane, and over-expression leads to reduction in mitochondrial motility whereas lack of it enhances mitochondrial movement. The activity appears to be mediated through binding the mitochondria to the actin intermediate filaments (IFs). The family is in the trichohyalin-plectin-homology domain.


Pssm-ID: 464007 [Multi-domain]  Cd Length: 341  Bit Score: 58.78  E-value: 2.22e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159648420  642 KQKLIDELENSQRRLQTLKRQYEEKLMMLQHKIRDTQLERDQVLQNLgsvetysEEKAKKIKSEYEKKLQTMNKELQRLQ 721
Cdd:pfam13868  125 QRQLREEIDEFNEEQAEWKELEKEEEREEDERILEYLKEKAEREEER-------EAEREEIEEEKEREIARLRAQQEKAQ 197

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159648420  722 TAQKEH--ARLLKNQSQYEKQLKKLQQEvtemkktkvrlmKQMKEEQEKARMTESRRN--REIAQLKKEQRKRE------ 791
Cdd:pfam13868  198 DEKAERdeLRAKLYQEEQERKERQKERE------------EAEKKARQRQELQQAREEqiELKERRLAEEAEREeeefer 265

                          170       180       190
                   ....*....|....*....|....*....|....*
gi 1159648420  792 ---HQLKLLEAQKRNQEVILRRKTEEVTALRRQVR 823
Cdd:pfam13868  266 mlrKQAEDEEIEQEEAEKRRMKRLEHRRELEKQIE 300
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 647-832 3.24e-08

Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 443969 [Multi-domain]  Cd Length: 377  Bit Score: 58.24  E-value: 3.24e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159648420  647 DELENSQRRLQTLKRQYEEklmmLQHKIRDTQLERDQVLQNLGSVETYSEEKAKKIKsEYEKKLQTMNKELQRLQTAQKE 726
Cdd:COG4942     20 DAAAEAEAELEQLQQEIAE----LEKELAALKKEEKALLKQLAALERRIAALARRIR-ALEQELAALEAELAELEKEIAE 94

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159648420  727 -HARLLKNQSQYEKQLKKLQQEvteMKKTKVRLMKQMKEEQEKARMTESrrnreIAQLKKEQRKR----EHQLKLLEAQK 801
Cdd:COG4942     95 lRAELEAQKEELAELLRALYRL---GRQPPLALLLSPEDFLDAVRRLQY-----LKYLAPARREQaeelRADLAELAALR 166

                          170       180       190
                   ....*....|....*....|....*....|.
gi 1159648420  802 RNQEVILRRKTEEVTALRRQVRPLSDKVAGK 832
Cdd:COG4942    167 AELEAERAELEALLAELEEERAALEALKAER 197
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 378-1057 4.13e-08

chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 58.91  E-value: 4.13e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159648420  378 NQDRASQQINALRSEIARLQMELMEYKT-----GKRIID-----EEGVESINDMFHENAMLQTENNNLRVRIKAMQETVD 447
Cdd:TIGR02168  261 ELQELEEKLEELRLEVSELEEEIEELQKelyalANEISRleqqkQILRERLANLERQLEELEAQLEELESKLDELAEELA 340

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159648420  448 ALRARITQLMSDQANQV--LARAGEGNEEISNMIHNYIKEIEDLRAK---LLESEAVNENLRRNLSRASTRstyfggpsa 522
Cdd:TIGR02168  341 ELEEKLEELKEELESLEaeLEELEAELEELESRLEELEEQLETLRSKvaqLELQIASLNNEIERLEARLER--------- 411

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159648420  523 fSASMLSSEKETLEILDIAKKDLEKLKKKERKKKKSVKEDNTDNEQEKRDEKGSSERENNELEAEEIQEASDREDEEEED 602
Cdd:TIGR02168  412 -LEDRRERLQQEIEELLKKLEEAELKELQAELEELEEELEELQEELERLEEALEELREELEEAEQALDAAERELAQLQAR 490

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159648420  603 DEDEDDMEVVESSDESDSDSDEKENYQ--------ADLanITC----EIAIK-------QKLIDELENSQRR-LQTLKRQ 662
Cdd:TIGR02168  491 LDSLERLQENLEGFSEGVKALLKNQSGlsgilgvlSEL--ISVdegyEAAIEaalggrlQAVVVENLNAAKKaIAFLKQN 568

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159648420  663 YEEKLMMLQHK-IRDTQLE--RDQVLQNLGSVETYSEEkAKKIKSEYEKKLQTM-------------------NKELQRL 720
Cdd:TIGR02168  569 ELGRVTFLPLDsIKGTEIQgnDREILKNIEGFLGVAKD-LVKFDPKLRKALSYLlggvlvvddldnalelakkLRPGYRI 647

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159648420  721 QT----------------AQKEHARLLKNQS--QYEKQLKKLQQEVTEMKKTKVRLMKQ---MKEEQEKARMTESRRNRE 779
Cdd:TIGR02168  648 VTldgdlvrpggvitggsAKTNSSILERRREieELEEKIEELEEKIAELEKALAELRKEleeLEEELEQLRKELEELSRQ 727

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159648420  780 IAQLKKEQRKREHQLKLLEAQKRNQEVILRRKTEEVTALRRQVRPLSDKVAGKVSRKLSLpEHPIQEpsSSSSVEHDGSR 859
Cdd:TIGR02168  728 ISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEEL-EAQIEQ--LKEELKALREA 804

                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159648420  860 IAAQQkmripvARVQALSVTATNGTGRkyQRKAVTSRVYSSRAARMKWQLLERRVTDIIMQRMTISNMEADMNRLLTQRE 939
Cdd:TIGR02168  805 LDELR------AELTLLNEEAANLRER--LESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELE 876

                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159648420  940 ELTKRREKLSKRREKLMKDggGSETDRNVQNINEEMESLTANIDYINDSISDcqaniMQMEEAKEEGETLDVTAVINAct 1019
Cdd:TIGR02168  877 ALLNERASLEEALALLRSE--LEELSEELRELESKRSELRRELEELREKLAQ-----LELRLEGLEVRIDNLQERLSE-- 947

                          730       740       750
                   ....*....|....*....|....*....|....*...
gi 1159648420 1020 ltEARYLLDHFLTMGINKGLQAAQKEAQIKVLEGRLKQ 1057
Cdd:TIGR02168  948 --EYSLTLEEAEALENKIEDDEEEARRRLKRLENKIKE 983
PRK12704 PRK12704
phosphodiesterase; Provisional
 671-814 4.53e-08

phosphodiesterase; Provisional


Pssm-ID: 237177 [Multi-domain]  Cd Length: 520  Bit Score: 58.25  E-value: 4.53e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159648420  671 QHKIRDTQLERDQVLQN-LGSVETYSEEK-------AKKIKSEYEKKLQTMNKELQRLQTAQKEHARLLKNQSQY----E 738
Cdd:PRK12704    30 EAKIKEAEEEAKRILEEaKKEAEAIKKEAlleakeeIHKLRNEFEKELRERRNELQKLEKRLLQKEENLDRKLELlekrE 109

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1159648420  739 KQLKKLQQEVTEMKKTkvrlMKQMKEEQEKARMTESRRNREIAQLKKEQRKREhQLKLLEAQKRNQEVILRRKTEE 814
Cdd:PRK12704   110 EELEKKEKELEQKQQE----LEKKEEELEELIEEQLQELERISGLTAEEAKEI-LLEKVEEEARHEAAVLIKEIEE 180
Caldesmon pfam02029
Caldesmon;
638-821 8.67e-08

Caldesmon;


Pssm-ID: 460421 [Multi-domain]  Cd Length: 495  Bit Score: 57.57  E-value: 8.67e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159648420  638 EIAIKQKLIDELENSQRRLQTLKRQYEEKLmmlQHKIRDTQLERDQVLQNLGSVETYSEEKAKKIKSEYEKKL------- 710
Cdd:pfam02029  127 RYKEEETEIREKEYQENKWSTEVRQAEEEG---EEEEDKSEEAEEVPTENFAKEEVKDEKIKKEKKVKYESKVfldqkrg 203

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159648420  711 ----QTMNKELQRLQTAQKEHARLLKNQSQYEKQLKKLQQEVTEMKKTKVRLMKQMKEEQE------------------K 768
Cdd:pfam02029  204 hpevKSQNGEEEVTKLKVTTKRRQGGLSQSQEREEEAEVFLEAEQKLEELRRRRQEKESEEfeklrqkqqeaeleleelK 283

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|...
gi 1159648420  769 ARMTESRRNREIAQLKKEQRKREHQLKLLEAQKRNQEVILRRKTEevTALRRQ 821
Cdd:pfam02029  284 KKREERRKLLEEEEQRRKQEEAERKLREEEEKRRMKEEIERRRAE--AAEKRQ 334
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 367-1007 9.90e-08

chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]


Pssm-ID: 274009 [Multi-domain]  Cd Length: 1164  Bit Score: 57.77  E-value: 9.90e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159648420  367 RARNIKNKVMVNQDRASQQINALRSEIARLQME---LMEYKT-GKRIIDEEGVEsindMFHENAMLQTENNNLRVRIKAM 442
Cdd:TIGR02169  174 KALEELEEVEENIERLDLIIDEKRQQLERLRRErekAERYQAlLKEKREYEGYE----LLKEKEALERQKEAIERQLASL 249

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159648420  443 QETVDALRARITQLM--SDQANQVLAragEGNEEISNMIHNyikEIEDLRAKLLESEAVNENLRRNLSRASTRSTYFGGP 520
Cdd:TIGR02169  250 EEELEKLTEEISELEkrLEEIEQLLE---ELNKKIKDLGEE---EQLRVKEKIGELEAEIASLERSIAEKERELEDAEER 323

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159648420  521 SAFSASMLSSEKETLEILDiakkdleklkkkerkkkksvkednTDNEQEKR------DEKGSSERENNELEAEeIQEASD 594
Cdd:TIGR02169  324 LAKLEAEIDKLLAEIEELE------------------------REIEEERKrrdkltEEYAELKEELEDLRAE-LEEVDK 378

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159648420  595 REDEEEEDDEDeddmevvessdesdsdsdekenYQADLANITCEIaikqkliDELENSQRRLQTLKRQYEEKLMMLQHKI 674
Cdd:TIGR02169  379 EFAETRDELKD----------------------YREKLEKLKREI-------NELKRELDRLQEELQRLSEELADLNAAI 429

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159648420  675 RDtqlerdqVLQNLGSVETYSEEKAKKIKsEYEKKLQTMNKELQrlqTAQKEHARLLKNQSQYEKQLKKLQQEVTEMKKT 754
Cdd:TIGR02169  430 AG-------IEAKINELEEEKEDKALEIK-KQEWKLEQLAADLS---KYEQELYDLKEEYDRVEKELSKLQRELAEAEAQ 498

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159648420  755 KvrlmKQMKEEQEkarmtESRRNRE------------IAQLKKeqRKREHQLKL-LEAQKRNQEVILrrKTEEVTAlrRQ 821
Cdd:TIGR02169  499 A----RASEERVR-----GGRAVEEvlkasiqgvhgtVAQLGS--VGERYATAIeVAAGNRLNNVVV--EDDAVAK--EA 563

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159648420  822 VRPLSDKvagKVSRKLSLPEHPIQEPSSSSS--------------VEHD-----------GSRIAAQqkmRIPVARVQAL 876
Cdd:TIGR02169  564 IELLKRR---KAGRATFLPLNKMRDERRDLSilsedgvigfavdlVEFDpkyepafkyvfGDTLVVE---DIEAARRLMG 637

                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159648420  877 S---VT----------ATNGTGRKYQRKAVTSRVYSSRAARMKWQL--LERRVTDIIMQRMTIsnmEADMNRLLTQREEL 941
Cdd:TIGR02169  638 KyrmVTlegelfeksgAMTGGSRAPRGGILFSRSEPAELQRLRERLegLKRELSSLQSELRRI---ENRLDELSQELSDA 714

                          650       660       670       680       690       700       710
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1159648420  942 TKRREKLSKRREKLMKDGGGS-----ETDRNVQNINEEMESLTANIDYINDSISDCQANIMQMEEAKEEGE 1007
Cdd:TIGR02169  715 SRKIGEIEKEIEQLEQEEEKLkerleELEEDLSSLEQEIENVKSELKELEARIEELEEDLHKLEEALNDLE 785
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
379-830 1.06e-07

Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 57.47  E-value: 1.06e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159648420  379 QDRASQQINALRSEIARLQMELM------EYKTGKRIIDE--EGVESINDMFHENAMLQTENNNLRVRIKAMQETVDALR 450
Cdd:COG4717    104 LEELEAELEELREELEKLEKLLQllplyqELEALEAELAElpERLEELEERLEELRELEEELEELEAELAELQEELEELL 183

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159648420  451 ARITQLMSDQANQVLARAGEGNEEISNMIHNYIK---EIEDLRAKL--LESEAVNENLRRNLSRASTRSTYFGGPSAFSA 525
Cdd:COG4717    184 EQLSLATEEELQDLAEELEELQQRLAELEEELEEaqeELEELEEELeqLENELEAAALEERLKEARLLLLIAAALLALLG 263

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159648420  526 SMLSSEKETLEILDIAKKDLEKLKKKERKKKKSVkednTDNEQEKRDEKGSSEREnnELEAEEIQEasdredeeeedded 605
Cdd:COG4717    264 LGGSLLSLILTIAGVLFLVLGLLALLFLLLAREK----ASLGKEAEELQALPALE--ELEEEELEE-------------- 323

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159648420  606 eddmevvessdesdsdsdekenyqaDLANITCEIAIKQKLIDELENSQRRLQTLKRQYEEklMMLQHKIRDTQLERDQVL 685
Cdd:COG4717    324 -------------------------LLAALGLPPDLSPEELLELLDRIEELQELLREAEE--LEEELQLEELEQEIAALL 376

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159648420  686 QNLGSVetySEEkakkiksEYEKKLqtmnKELQRLQTAQKEHARLlknQSQYEKQLKKLQQEVTEMKKTkvrlmkQMKEE 765
Cdd:COG4717    377 AEAGVE---DEE-------ELRAAL----EQAEEYQELKEELEEL---EEQLEELLGELEELLEALDEE------ELEEE 433

                          410       420       430       440       450       460
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1159648420  766 QEKARMTESRRNREIAQLKKEQRKREHQLKLLEAQKRNQEviLRRKTEEvtaLRRQVRPLSDKVA 830
Cdd:COG4717    434 LEELEEELEELEEELEELREELAELEAELEQLEEDGELAE--LLQELEE---LKAELRELAEEWA 493
Lebercilin pfam15619
Ciliary protein causing Leber congenital amaurosis disease; Lebercilin is a family of ...
 636-832 1.68e-07

Ciliary protein causing Leber congenital amaurosis disease; Lebercilin is a family of eukaryotic ciliary proteins. Mutations in the gene, LCA5, are implicated in the disease Leber congenital amaurosis. In photoreceptors, lebercilin is uniquely localized at the cilium that bridges the inner and outer segments. Lebercilin functions as an integral element of selective protein transport through photoreceptor cilia. Lebercilin specifically interacts with the intraflagellar transport (IFT), and disruption of IFT can lead to Leber congenital amaurosis.


Pssm-ID: 464776 [Multi-domain]  Cd Length: 193  Bit Score: 53.75  E-value: 1.68e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159648420  636 TCEIAIKQKLIDELENSQRRLQTLKRQYEEKLmmlqHKIRDTQLERDQVLQNL-GSVETYSEE--KAKKIKSEYEKKLQT 712
Cdd:pfam15619   17 QNELAELQSKLEELRKENRLLKRLQKRQEKAL----GKYEGTESELPQLIARHnEEVRVLRERlrRLQEKERDLERKLKE 92

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159648420  713 MNKELQRLQTAQKEHARLLKNQSQYEKQlkKLQQEVTEMKKTKVRLMKQMKEEQEKARMTESRRNREIAQLKKeqrkreh 792
Cdd:pfam15619   93 KEAELLRLRDQLKRLEKLSEDKNLAERE--ELQKKLEQLEAKLEDKDEKIQDLERKLELENKSFRRQLAAEKK------- 163

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|
gi 1159648420  793 qlKLLEAQkrnqevilrrktEEVTALRRQVRPLSDKVAGK 832
Cdd:pfam15619  164 --KHKEAQ------------EEVKILQEEIERLQQKLKEK 189
Rabaptin pfam03528
Rabaptin;
642-801 1.86e-07

Rabaptin;


Pssm-ID: 367545 [Multi-domain]  Cd Length: 486  Bit Score: 56.27  E-value: 1.86e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159648420  642 KQKLidELENSQRRLQtLKRQY---EEKLMMLQHKIRDTQLERDQV----------LQNLGSVETYSEEKAKKIKSEYEK 708
Cdd:pfam03528   24 KQQL--EAEFNQKRAK-FKELYlakEEDLKRQNAVLQEAQVELDALqnqlalaraeMENIKAVATVSENTKQEAIDEVKS 100

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159648420  709 KLQtmnKELQRLQTAQKE---------HARLLKNQSQYEKQLKKLQQEVTEMKKtkvRL------------MKQMKEEQE 767
Cdd:pfam03528  101 QWQ---EEVASLQAIMKEtvreyevqfHRRLEQERAQWNQYRESAEREIADLRR---RLsegqeeenledeMKKAQEDAE 174

                          170       180       190
                   ....*....|....*....|....*....|....
gi 1159648420  768 KARMTESRRNREIAQLKKEQRKREHQLKLLEAQK 801
Cdd:pfam03528  175 KLRSVVMPMEKEIAALKAKLTEAEDKIKELEASK 208
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 385-764 1.91e-07

chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]


Pssm-ID: 274009 [Multi-domain]  Cd Length: 1164  Bit Score: 57.00  E-value: 1.91e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159648420  385 QINALRSEIARLQMELMEYKtgKRIIDEEgvESINDMFHENAMLQTENNNLRVRIKAMQETVDALRARITQLMSDQAnQV 464
Cdd:TIGR02169  689 ELSSLQSELRRIENRLDELS--QELSDAS--RKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQEIENVKSELK-EL 763

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159648420  465 LARAGEGNEEIsnmiHNYIKEIEDLRAKLLES---------EAVNENLRRNLSRAST--RSTyfgGPSAFSASMLSSEKE 533
Cdd:TIGR02169  764 EARIEELEEDL----HKLEEALNDLEARLSHSripeiqaelSKLEEEVSRIEARLREieQKL---NRLTLEKEYLEKEIQ 836

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159648420  534 TLEILDIAkkdleklkkkerkkkksvkEDNTDNEQEKRDEKGSSERENNELEAEEIQEAsdredeeeeddededdmevve 613
Cdd:TIGR02169  837 ELQEQRID-------------------LKEQIKSIEKEIENLNGKKEELEEELEELEAA--------------------- 876

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159648420  614 ssdesdsdsdeKENYQADLANITCEIaikQKLIDELENSQRRLQTLKRQYEEK---LMMLQHKIRDTQLERDQVLQNLGS 690
Cdd:TIGR02169  877 -----------LRDLESRLGDLKKER---DELEAQLRELERKIEELEAQIEKKrkrLSELKAKLEALEEELSEIEDPKGE 942

                          330       340       350       360       370       380       390
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1159648420  691 VETYSEEKAkkIKSEYEKKLQTMNKELQRLQT----AQKEHARLLKNQSQYEKQLKKLQQEVTEMKKTKVRLMKQMKE 764
Cdd:TIGR02169  943 DEEIPEEEL--SLEDVQAELQRVEEEIRALEPvnmlAIQEYEEVLKRLDELKEKRAKLEEERKAILERIEEYEKKKRE 1018
Nup88 pfam10168
Nuclear pore component; Nup88 can be divided into two structural domains; the N-terminal ...
 655-823 2.31e-07

Nuclear pore component; Nup88 can be divided into two structural domains; the N-terminal two-thirds of the protein has no obvious structural motifs but is the region for binding to Nup98, one of the components of the nuclear pore. the C-terminal end is a predicted coiled-coil domain. Nup88 is overexpressed in tumour cells.


Pssm-ID: 462975 [Multi-domain]  Cd Length: 713  Bit Score: 56.21  E-value: 2.31e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159648420  655 RLQTLKRQY---EEklmmLQHKIRDTQLERDQVLQNLGSVETYSE----------EKAKKIKSEYEKKLQTMNKELQRLQ 721
Cdd:pfam10168  545 REEYLKKHDlarEE----IQKRVKLLKLQKEQQLQELQSLEEERKslseraeklaEKYEEIKDKQEKLMRRCKKVLQRLN 620

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159648420  722 TAqkeharlLKNQSQYEKQLKKlqqEVTEMKKTkvrlMKQMKEEQEKARMTESRRNREIAQLKKEQRKREHQLKllEAQK 801
Cdd:pfam10168  621 SQ-------LPVLSDAEREMKK---ELETINEQ----LKHLANAIKQAKKKMNYQRYQIAKSQSIRKKSSLSLS--EKQR 684

                          170       180
                   ....*....|....*....|..
gi 1159648420  802 RNQEVILRRKTEEVTALRRQVR 823
Cdd:pfam10168  685 KTIKEILKQLGSEIDELIKQVK 706
DR0291 COG1579
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ...
 709-823 2.40e-07

Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];


Pssm-ID: 441187 [Multi-domain]  Cd Length: 236  Bit Score: 54.16  E-value: 2.40e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159648420  709 KLQTMNKELQRLQTAQKEH----ARLLKNQSQYEKQLKKLQQEVTEMKKTKVRLMKQMKEEQEK-----ARMTESRRNR- 778
Cdd:COG1579     11 DLQELDSELDRLEHRLKELpaelAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARikkyeEQLGNVRNNKe 90

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|.
gi 1159648420  779 ------EIAQLKKEQRKREHQLKLLEAQKRNQEVILRRKTEEVTALRRQVR 823
Cdd:COG1579     91 yealqkEIESLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELE 141
CCDC34 pfam13904
Coiled-coil domain-containing protein 3; This family is found in eukaryotes; it has several ...
 668-811 2.70e-07

Coiled-coil domain-containing protein 3; This family is found in eukaryotes; it has several conserved tryptophan residues. The function is not known.


Pssm-ID: 464032 [Multi-domain]  Cd Length: 221  Bit Score: 53.94  E-value: 2.70e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159648420  668 MMLQHKIRDTQLERdqvlqnlGSVETYSEEKAKKiKSEYEKKLQtMNKELQRLQTAQKEhARLLKNQSQYEKQLKKLQQE 747
Cdd:pfam13904   38 LTYARKLEGLKLER-------QPLEAYENWLAAK-QRQRQKELQ-AQKEEREKEEQEAE-LRKRLAKEKYQEWLQRKARQ 107

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1159648420  748 vtemkKTKVRLMKQMKEEQEKARMTESRRNREIAQ-----------LKKEQRKREHQLKLLEAQKRNQEVILRRK 811
Cdd:pfam13904  108 -----QTKKREESHKQKAAESASKSLAKPERKVSQeeakevlqeweRKKLEQQQRKREEEQREQLKKEEEEQERK 177
TPH pfam13868
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ...
 566-823 3.40e-07

Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of eukaryotic proteins. Trichoplein or mitostatin, was first defined as a meiosis-specific nuclear structural protein. It has since been linked with mitochondrial movement. It is associated with the mitochondrial outer membrane, and over-expression leads to reduction in mitochondrial motility whereas lack of it enhances mitochondrial movement. The activity appears to be mediated through binding the mitochondria to the actin intermediate filaments (IFs). The family is in the trichohyalin-plectin-homology domain.


Pssm-ID: 464007 [Multi-domain]  Cd Length: 341  Bit Score: 54.92  E-value: 3.40e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159648420  566 NEQEKRDEkgssERENNELEAEEIQEASDRedeeeeddededdmevveSSDESDSDSDEKENYQADLanitceiaIKQkl 645
Cdd:pfam13868   34 IKAEEKEE----ERRLDEMMEEERERALEE------------------EEEKEEERKEERKRYRQEL--------EEQ-- 81

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159648420  646 IDELEnsQRRLQTLKRQYEEKLMMLQHkIRDTQLERDQVLQNLgsvetysEEKAKKIKSEYEK--KLQTMNKELQRLQtA 723
Cdd:pfam13868   82 IEERE--QKRQEEYEEKLQEREQMDEI-VERIQEEDQAEAEEK-------LEKQRQLREEIDEfnEEQAEWKELEKEE-E 150

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159648420  724 QKEHARLLKNQSQYEKQLKKLQQEVTEMKKTKVRLM-----KQMKEEQEKARMTESRRNREIAQLKKEQRKREHQlklLE 798
Cdd:pfam13868  151 REEDERILEYLKEKAEREEEREAEREEIEEEKEREIarlraQQEKAQDEKAERDELRAKLYQEEQERKERQKERE---EA 227

                          250       260
                   ....*....|....*....|....*
gi 1159648420  799 AQKRNQEVILRRKTEEVTALRRQVR 823
Cdd:pfam13868  228 EKKARQRQELQQAREEQIELKERRL 252
DUF5401 pfam17380
Family of unknown function (DUF5401); This is a family of unknown function found in ...
 642-865 3.81e-07

Family of unknown function (DUF5401); This is a family of unknown function found in Chromadorea.


Pssm-ID: 375164 [Multi-domain]  Cd Length: 722  Bit Score: 55.51  E-value: 3.81e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159648420  642 KQKLIDELENSQR-------RLQTLKRQ---YEEKLMMLQHKIR--------DTQLERDQVLQNLGSVETYSEEKAKKIK 703
Cdd:pfam17380  305 KEEKAREVERRRKleeaekaRQAEMDRQaaiYAEQERMAMERERelerirqeERKRELERIRQEEIAMEISRMRELERLQ 384

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159648420  704 SEYEKKLQTMNKELQ---RLQTAQKEHARLLKNQSQYEKQLKKLQQEVTEMKKTkvRLMKQMKEEQEKARMTESRRNREI 780
Cdd:pfam17380  385 MERQQKNERVRQELEaarKVKILEEERQRKIQQQKVEMEQIRAEQEEARQREVR--RLEEERAREMERVRLEEQERQQQV 462

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159648420  781 AQLKKEQRKREHQLKLLEAQKRNQEVI--LRRKTEEVTALRRQVRPLSDKvagkvsRKLSLPEHPIQEpSSSSSVEHDGS 858
Cdd:pfam17380  463 ERLRQQEEERKRKKLELEKEKRDRKRAeeQRRKILEKELEERKQAMIEEE------RKRKLLEKEMEE-RQKAIYEEERR 535


                   ....*..
gi 1159648420  859 RIAAQQK 865
Cdd:pfam17380  536 REAEEER 542
PTZ00121 PTZ00121
MAEBL; Provisional
 566-815 4.06e-07

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 55.92  E-value: 4.06e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159648420  566 NEQEKRDEKGSSERENnelEAEEIQEAsdredeeeeddededdmevvessdesdsdsdeKENYQADlanitceiaiKQKL 645
Cdd:PTZ00121  1519 EEAKKADEAKKAEEAK---KADEAKKA--------------------------------EEKKKAD----------ELKK 1553

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159648420  646 IDELENSQ--RRLQTLKRQYEEKLMMLQHKIRDTQLERDQVLQNLGSVETYSEEKAKKIKSEYEKKLQTmnKELQRLQTA 723
Cdd:PTZ00121  1554 AEELKKAEekKKAEEAKKAEEDKNMALRKAEEAKKAEEARIEEVMKLYEEEKKMKAEEAKKAEEAKIKA--EELKKAEEE 1631

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159648420  724 QKEHARLLKNQSQYEKQLKKLQQEVTEMKKTKVRLMKqmKEEQEKARMTESRRNREiaqlkkEQRKREHQLKLLEAQKRN 803
Cdd:PTZ00121  1632 KKKVEQLKKKEAEEKKKAEELKKAEEENKIKAAEEAK--KAEEDKKKAEEAKKAEE------DEKKAAEALKKEAEEAKK 1703

                          250
                   ....*....|..
gi 1159648420  804 QEVILRRKTEEV 815
Cdd:PTZ00121  1704 AEELKKKEAEEK 1715
mukB PRK04863
chromosome partition protein MukB;
643-955 4.30e-07

chromosome partition protein MukB;


Pssm-ID: 235316 [Multi-domain]  Cd Length: 1486  Bit Score: 55.73  E-value: 4.30e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159648420  643 QKLIDELENSQRRLQ-------TLKRQY---EEKLMMLQHKIRDTqlerDQVLQNlgsVETYSEEKAKKI---KSEYEKK 709
Cdd:PRK04863   917 GNALAQLEPIVSVLQsdpeqfeQLKQDYqqaQQTQRDAKQQAFAL----TEVVQR---RAHFSYEDAAEMlakNSDLNEK 989

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159648420  710 LQTMNKELQRLQTAQKEHARLLKNQ-SQYEKQLKKLQQEVTEMKKTKVRLMKQMKE--------EQEKARmteSRRNREI 780
Cdd:PRK04863   990 LRQRLEQAEQERTRAREQLRQAQAQlAQYNQVLASLKSSYDAKRQMLQELKQELQDlgvpadsgAEERAR---ARRDELH 1066

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159648420  781 AQLKKEQRKR---EHQLKLLEAQKRNQEVILRRKTEEVTALRRQVRPlsdKVAGK-----------VSRKL---SLPEHP 843
Cdd:PRK04863  1067 ARLSANRSRRnqlEKQLTFCEAEMDNLTKKLRKLERDYHEMREQVVN---AKAGWcavlrlvkdngVERRLhrrELAYLS 1143

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159648420  844 IQEPSSSSSVehdgsriaAQQKMRIPVARVQALS-VTATNGTGRKYQRKAVT-SRVYssraarmkwQLLERRV-TDIIMQ 920
Cdd:PRK04863  1144 ADELRSMSDK--------ALGALRLAVADNEHLRdVLRLSEDPKRPERKVQFyIAVY---------QHLRERIrQDIIRT 1206

                          330       340       350
                   ....*....|....*....|....*....|....*...
gi 1159648420  921 ---RMTISNMEADMNRLltqREELTKRREKLSKRREKL 955
Cdd:PRK04863  1207 ddpVEAIEQMEIELSRL---TEELTSREQKLAISSESV 1241
Myosin_tail_1 pfam01576
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ...
 646-991 4.33e-07

Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.


Pssm-ID: 460256 [Multi-domain]  Cd Length: 1081  Bit Score: 55.57  E-value: 4.33e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159648420  646 IDELENSQRRLQTLK-------RQYEEKLMMLQHKIRDTQLERDQVLQNLGSVETY---SEEKAKKIkSEYEKKLQTMNK 715
Cdd:pfam01576  112 LDEEEAARQKLQLEKvtteakiKKLEEDILLLEDQNSKLSKERKLLEERISEFTSNlaeEEEKAKSL-SKLKNKHEAMIS 190

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159648420  716 ELQ-RLQTAQKEHARLLKNQSQYEKQLKKLQQEVTEMKKTKVRLMKQMKEEQEKARMTESRRNREIAQLKKEQRK-REHQ 793
Cdd:pfam01576  191 DLEeRLKKEEKGRQELEKAKRKLEGESTDLQEQIAELQAQIAELRAQLAKKEEELQAALARLEEETAQKNNALKKiRELE 270

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159648420  794 LKLLEAQK--------RNQEVILRRK-TEEVTALRRQVRPLSDKVAGKvsrklslpehpiQEPSSSSSVEHDGSRIAAQQ 864
Cdd:pfam01576  271 AQISELQEdleseraaRNKAEKQRRDlGEELEALKTELEDTLDTTAAQ------------QELRSKREQEVTELKKALEE 338

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159648420  865 KMRIPVARVQALsvtatngtgRKYQRKAV---TSRVYSSRAARMKW----QLLERRVtdiimqrmtiSNMEADMNRLLTQ 937
Cdd:pfam01576  339 ETRSHEAQLQEM---------RQKHTQALeelTEQLEQAKRNKANLekakQALESEN----------AELQAELRTLQQA 399

                          330       340       350       360       370
                   ....*....|....*....|....*....|....*....|....*....|....
gi 1159648420  938 REELTKRREKLSKRREKLMkdGGGSETDRNVQNINEEMESLTANIDYINDSISD 991
Cdd:pfam01576  400 KQDSEHKRKKLEGQLQELQ--ARLSESERQRAELAEKLSKLQSELESVSSLLNE 451
DUF5401 pfam17380
Family of unknown function (DUF5401); This is a family of unknown function found in ...
 678-977 5.05e-07

Family of unknown function (DUF5401); This is a family of unknown function found in Chromadorea.


Pssm-ID: 375164 [Multi-domain]  Cd Length: 722  Bit Score: 55.13  E-value: 5.05e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159648420  678 QLERDQVLQNLG-SVETYSEEKAKKikseYEKKLQTMNKEL-QRLQTAQkeHARLLKNQSQYEKQLKKLQQEVTEMKKTK 755
Cdd:pfam17380  235 KMERRKESFNLAeDVTTMTPEYTVR----YNGQTMTENEFLnQLLHIVQ--HQKAVSERQQQEKFEKMEQERLRQEKEEK 308

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159648420  756 VRLMKQMK--EEQEKARMTE---------------SRRNREIAQLKKEQRKREHQlklleaQKRNQEV---ILRRKTEEV 815
Cdd:pfam17380  309 AREVERRRklEEAEKARQAEmdrqaaiyaeqermaMERERELERIRQEERKRELE------RIRQEEIameISRMRELER 382

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159648420  816 TALRRQVRPLSDKVAGKVSRKLSLPEHPIQepsssssvehdgsRIAAQQKMRIPVARVQalsvtatngtgRKYQRKAVTS 895
Cdd:pfam17380  383 LQMERQQKNERVRQELEAARKVKILEEERQ-------------RKIQQQKVEMEQIRAE-----------QEEARQREVR 438

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159648420  896 RVYSSRAARMKwqllerRVTDIIMQRmtisnmEADMNRLLTQREEltKRREKLSKRREKlMKDGGGSETDRNVqnINEEM 975
Cdd:pfam17380  439 RLEEERAREME------RVRLEEQER------QQQVERLRQQEEE--RKRKKLELEKEK-RDRKRAEEQRRKI--LEKEL 501


                   ..
gi 1159648420  976 ES 977
Cdd:pfam17380  502 EE 503
DUF3584 pfam12128
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ...
 713-1010 5.52e-07

Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. Proteins in this family are typically between 943 to 1234 amino acids in length. This family contains a P-loop motif suggesting it is a nucleotide binding protein. It may be involved in replication.


Pssm-ID: 432349 [Multi-domain]  Cd Length: 1191  Bit Score: 55.23  E-value: 5.52e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159648420  713 MNKELQR--------LQTAQKEHARLLKNQSQYEKQLKKLQQEVTEMKK-------TKVRLMKQMkeEQEKARMTESRRn 777
Cdd:pfam12128  598 SEEELRErldkaeeaLQSAREKQAAAEEQLVQANGELEKASREETFARTalknarlDLRRLFDEK--QSEKDKKNKALA- 674

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159648420  778 REIAQLKKEQRKREHQLKLLEaqkRNQEVILRRKTEEVTALRRQVRPLSDKVAGKVSRKLSLpehpIQEPSSSSSVEHDG 857
Cdd:pfam12128  675 ERKDSANERLNSLEAQLKQLD---KKHQAWLEEQKEQKREARTEKQAYWQVVEGALDAQLAL----LKAAIAARRSGAKA 747

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159648420  858 SRIAAQQKMRIPVArvqALSVTATNGTGRKYQRKAVTSRVysSRAARMKWQLLERRVtdiIMQ----------RMTISNM 927
Cdd:pfam12128  748 ELKALETWYKRDLA---SLGVDPDVIAKLKREIRTLERKI--ERIAVRRQEVLRYFD---WYQetwlqrrprlATQLSNI 819

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159648420  928 EADMNRLltqREELTKRREKLSKRREKLMKDGGGSEtDRNVQnINEEMESLTANIDYINDSISDCQANimqmEEAKEEGE 1007
Cdd:pfam12128  820 ERAISEL---QQQLARLIADTKLRRAKLEMERKASE-KQQVR-LSENLRGLRCEMSKLATLKEDANSE----QAQGSIGE 890


                   ...
gi 1159648420 1008 TLD 1010
Cdd:pfam12128  891 RLA 893
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
643-842 6.57e-07

Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 55.31  E-value: 6.57e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159648420  643 QKLIDELENSQRRLQTLKRQYEeklmMLQHkIRDTQLERDQVLQNLGSVETYSE----EKAKKIKSEYEKKLQTMNKELQ 718
Cdd:COG4913    231 VEHFDDLERAHEALEDAREQIE----LLEP-IRELAERYAAARERLAELEYLRAalrlWFAQRRLELLEAELEELRAELA 305

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159648420  719 RLQTAQKEHARLLKNQSQYE------------KQLKKLQQEVTEMKKTKVRLMKQMKEEQEKARMTESRRNREIAQLKKE 786
Cdd:COG4913    306 RLEAELERLEARLDALREELdeleaqirgnggDRLEQLEREIERLERELEERERRRARLEALLAALGLPLPASAEEFAAL 385

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 1159648420  787 QRKREHQLKLLEAQKRNQEVILRRKTEEVTALRRQVRPLSDKVAGKVSRKLSLPEH 842
Cdd:COG4913    386 RAEAAALLEALEEELEALEEALAEAEAALRDLRRELRELEAEIASLERRKSNIPAR 441
PKK pfam12474
Polo kinase kinase; This domain family is found in eukaryotes, and is approximately 140 amino ...
 657-790 7.15e-07

Polo kinase kinase; This domain family is found in eukaryotes, and is approximately 140 amino acids in length. The family is found in association with pfam00069. Polo-like kinase 1 (Plx1) is essential during mitosis for the activation of Cdc25C, for spindle assembly, and for cyclin B degradation. This family is Polo kinase kinase (PKK) which phosphorylates Polo kinase and Polo-like kinase to activate them. PKK is a serine/threonine kinase.


Pssm-ID: 463600 [Multi-domain]  Cd Length: 139  Bit Score: 50.64  E-value: 7.15e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159648420  657 QTLKRQYEEKL--MMLQHKIRDTQLERDQvLQNLGsvetyseEKAKKIKSEYEKklqtmnkELQRLQTAQKEHARLLKNQ 734
Cdd:pfam12474   17 QQLKKRYEKELeqLERQQKQQIEKLEQRQ-TQELR-------RLPKRIRAEQKK-------RLKMFRESLKQEKKELKQE 81

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 1159648420  735 sqyEKQLKKLQ-QEVTEMKKTKVRLMKQMKEEQEKARMTESRRnREIAQLKKEQRKR 790
Cdd:pfam12474   82 ---VEKLPKFQrKEAKRQRKEELELEQKHEELEFLQAQSEALE-RELQQLQNEKRKE 134
Mplasa_alph_rch TIGR04523
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
 638-841 7.88e-07

helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.


Pssm-ID: 275316 [Multi-domain]  Cd Length: 745  Bit Score: 54.64  E-value: 7.88e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159648420  638 EIAIKQKLIDELENSQRRLQTLKRQYEEKLMMLQHKirDTQLERdqVLQNLGSVETYSEEKAKKIKSEYEKKLQTMNKEL 717
Cdd:TIGR04523  413 QIKKLQQEKELLEKEIERLKETIIKNNSEIKDLTNQ--DSVKEL--IIKNLDNTRESLETQLKVLSRSINKIKQNLEQKQ 488

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159648420  718 QRLQTAQKEHARLLKNQSQYEKQLKKLQQEVTEMKKtkvrlmKQMKEEQEKarmteSRRNREIAQLKKEQRKREHQLK-- 795
Cdd:TIGR04523  489 KELKSKEKELKKLNEEKKELEEKVKDLTKKISSLKE------KIEKLESEK-----KEKESKISDLEDELNKDDFELKke 557

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*.
gi 1159648420  796 LLEAQKRNQEVILRRKTEEVTALRRQVRPLSDKVAGKVSRKLSLPE 841
Cdd:TIGR04523  558 NLEKEIDEKNKEIEELKQTQKSLKKKQEEKQELIDQKEKEKKDLIK 603
DUF4670 pfam15709
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins ...
 629-817 8.22e-07

Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins in this family are typically between 373 and 763 amino acids in length.


Pssm-ID: 464815 [Multi-domain]  Cd Length: 522  Bit Score: 54.19  E-value: 8.22e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159648420  629 QADLANITCEIAIKQKLIDElENSQRRLQT-LKRQYEEKlmmlQHKIRDTQLERDQVLQNLGSVET---YSEEKAKKIKS 704
Cdd:pfam15709  322 KALLEKREQEKASRDRLRAE-RAEMRRLEVeRKRREQEE----QRRLQQEQLERAEKMREELELEQqrrFEEIRLRKQRL 396

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159648420  705 EYEKKLQTMNKELQRLQ-TAQKEHARLlkNQSQYEKQLKKLQQevtemkktkvrlmKQMKEEQEKARMTESRRNREIAQL 783
Cdd:pfam15709  397 EEERQRQEEEERKQRLQlQAAQERARQ--QQEEFRRKLQELQR-------------KKQQEEAERAEAEKQRQKELEMQL 461

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....
gi 1159648420  784 KKEQR---------KREHQLKLLEAQ-KRNQEVILRRKTEEVTA 817
Cdd:pfam15709  462 AEEQKrlmemaeeeRLEYQRQKQEAEeKARLEAEERRQKEEEAA 505
CCDC158 pfam15921
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ...
 349-1011 1.06e-06

Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.


Pssm-ID: 464943 [Multi-domain]  Cd Length: 1112  Bit Score: 54.35  E-value: 1.06e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159648420  349 SPSDRDFMETL-NTLKYANRARNIKNKVMVNqdrASQQINALRS----------EIARLQMELmEYKTGKRIIDEEGVES 417
Cdd:pfam15921  137 SQSQEDLRNQLqNTVHELEAAKCLKEDMLED---SNTQIEQLRKmmlshegvlqEIRSILVDF-EEASGKKIYEHDSMST 212

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159648420  418 ---------INDMFHEnamLQTENNNLRVRIKAMQETVDALRA---------------RITQLMSD-------------- 459
Cdd:pfam15921  213 mhfrslgsaISKILRE---LDTEISYLKGRIFPVEDQLEALKSesqnkielllqqhqdRIEQLISEheveitgltekass 289

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159648420  460 ---QANQVLARAGEGNEEISNMIHNYIKEIEDLrakllesEAVNENLRRNLSRAstRSTYFGGPSAFSASMLSSEKETLE 536
Cdd:pfam15921  290 arsQANSIQSQLEIIQEQARNQNSMYMRQLSDL-------ESTVSQLRSELREA--KRMYEDKIEELEKQLVLANSELTE 360

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159648420  537 ildiakkdleklkKKERKKKKSVKEDNTDNEQEK-------RDEKGSSERENN-------------------ELEAE--E 588
Cdd:pfam15921  361 -------------ARTERDQFSQESGNLDDQLQKlladlhkREKELSLEKEQNkrlwdrdtgnsitidhlrrELDDRnmE 427

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159648420  589 IQ--EASDREDEEEEDDEDEDDMEVVESSDESDsdsdekENYQADLANITCEIAIKQKLIDELENSQRRLQTLKRQYEEK 666
Cdd:pfam15921  428 VQrlEALLKAMKSECQGQMERQMAAIQGKNESL------EKVSSLTAQLESTKEMLRKVVEELTAKKMTLESSERTVSDL 501

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159648420  667 LMMLQHKIRdtqlerdqvlqnlgSVETYSEEkAKKIKSEYEKKLQTMN---KELQRLQTAQKEHARLLKNQSQYEKQLKK 743
Cdd:pfam15921  502 TASLQEKER--------------AIEATNAE-ITKLRSRVDLKLQELQhlkNEGDHLRNVQTECEALKLQMAEKDKVIEI 566

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159648420  744 LQQEVTEMKK---TKVRLMKQMKEEQEKARMTESRRNREIAQLKKEQRKREHQLKLLEA--------------------- 799
Cdd:pfam15921  567 LRQQIENMTQlvgQHGRTAGAMQVEKAQLEKEINDRRLELQEFKILKDKKDAKIRELEArvsdlelekvklvnagserlr 646

                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159648420  800 ------QKRNQ---EVILRRK-----TEEVTALRRQVRPLSDKVAgKVSRKLSLpehpiQEPSSSSSVEHdgsriaaqqk 865
Cdd:pfam15921  647 avkdikQERDQllnEVKTSRNelnslSEDYEVLKRNFRNKSEEME-TTTNKLKM-----QLKSAQSELEQ---------- 710

                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159648420  866 mripvARVQALSVTATNGTGRKY---QRKAVTSRVYSSRAARMKWQLLErrvtdiimQRMTISNMEADMnrlltQREELT 942
Cdd:pfam15921  711 -----TRNTLKSMEGSDGHAMKVamgMQKQITAKRGQIDALQSKIQFLE--------EAMTNANKEKHF-----LKEEKN 772

                          730       740       750       760       770       780       790
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1159648420  943 KRREKLSKRREKLMKDGGGSETDRNVQ-NINEEMESLTANIDYINDSISDCQaNIMQMEEAK----EEGETLDV 1011
Cdd:pfam15921  773 KLSQELSTVATEKNKMAGELEVLRSQErRLKEKVANMEVALDKASLQFAECQ-DIIQRQEQEsvrlKLQHTLDV 845
Cast pfam10174
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ...
 643-1052 1.32e-06

RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part of the CAZ (cytomatrix at the active zone) complex which is involved in determining the site of synaptic vesicle fusion. The C-terminus is a PDZ-binding motif that binds directly to RIM (a small G protein Rab-3A effector). The family also contains four coiled-coil domains.


Pssm-ID: 431111 [Multi-domain]  Cd Length: 766  Bit Score: 54.06  E-value: 1.32e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159648420  643 QKLIDELENSQRRLQTLKRQYEEKLMMLQHKIRDTQLERDQVLQNLGSVETYSE---EKAKKIKSEYEKK---------- 709
Cdd:pfam10174  232 QTVIEMKDTKISSLERNIRDLEDEVQMLKTNGLLHTEDREEEIKQMEVYKSHSKfmkNKIDQLKQELSKKesellalqtk 311

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159648420  710 LQTMN-------------------KElQRLQTAQKE----HARLLKNQSQYEKQLKKLQqEVTEMKKT---KVRLMKQMK 763
Cdd:pfam10174  312 LETLTnqnsdckqhievlkesltaKE-QRAAILQTEvdalRLRLEEKESFLNKKTKQLQ-DLTEEKSTlagEIRDLKDML 389

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159648420  764 EEQEKARMTESRRnreIAQLKKEQRKREHQL--------------------------------KLLEAQKRNQEVILRRK 811
Cdd:pfam10174  390 DVKERKINVLQKK---IENLQEQLRDKDKQLaglkervkslqtdssntdtalttleealsekeRIIERLKEQREREDRER 466

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159648420  812 TEEVTALRRQVRPLSDKV----AGKVSRKLSLPEHPIQEPSSSSSVEHDGSR-----IAAQQKMRipvarvqalSVTATN 882
Cdd:pfam10174  467 LEELESLKKENKDLKEKVsalqPELTEKESSLIDLKEHASSLASSGLKKDSKlksleIAVEQKKE---------ECSKLE 537

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159648420  883 GTGRKYQRKAVTSRVYSSRAARMKwqLLERRVTdiiMQRMTISNMEADMNRLL-----TQREELTKRR--EKLSKRREKL 955
Cdd:pfam10174  538 NQLKKAHNAEEAVRTNPEINDRIR--LLEQEVA---RYKEESGKAQAEVERLLgilreVENEKNDKDKkiAELESLTLRQ 612

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159648420  956 MKDggGSETDRNVQNINEEMESLTANID----YINDSISDCQANImQMEEAKEEGE----TLDVTAVINACT-------- 1019
Cdd:pfam10174  613 MKE--QNKKVANIKHGQQEMKKKGAQLLeearRREDNLADNSQQL-QLEELMGALEktrqELDATKARLSSTqqslaekd 689

                          490       500       510       520
                   ....*....|....*....|....*....|....*....|.
gi 1159648420 1020 --LT----EARYLLDHFLTMGiNKGLQAA--QKEAQIKVLE 1052
Cdd:pfam10174  690 ghLTnlraERRKQLEEILEMK-QEALLAAisEKDANIALLE 729
CAF-1_p150 pfam11600
Chromatin assembly factor 1 complex p150 subunit, N-terminal; CAF-1_p150 is a polypeptide ...
 695-802 1.35e-06

Chromatin assembly factor 1 complex p150 subunit, N-terminal; CAF-1_p150 is a polypeptide subunit of CAF-1, which functions in depositing newly synthesized and acetylated histones H3/H4 into chromatin during DNA replication and repair. CAF-1_p150 includes the HP1 interaction site, the PEST, KER and ED interacting sites. CAF-1_p150 interacts directly with newly synthesized and acetylated histones through the acidic KER and ED domains. The PEST domain is associated with proteins that undergo rapid proteolysis.


Pssm-ID: 402959 [Multi-domain]  Cd Length: 164  Bit Score: 50.46  E-value: 1.35e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159648420  695 SEEKAK------KIKSEYEKKLQTMNKELQRLQTAQKEHARLLKNQSQYEKQLKKLQQEvtemkktKVRLMKQMKEEQEK 768
Cdd:pfam11600   10 QEEKEKqrlekdKERLRRQLKLEAEKEEKERLKEEAKAEKERAKEEARRKKEEEKELKE-------KERREKKEKDEKEK 82

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|
gi 1159648420  769 A---RMTESRRNREIAQLK---KEQRKREHQLKLLEAQKR 802
Cdd:pfam11600   83 AeklRLKEEKRKEKQEALEaklEEKRKKEEEKRLKEEEKR 122
DUF4515 pfam14988
Domain of unknown function (DUF4515); This family of proteins is found in bacteria and ...
 700-836 1.42e-06

Domain of unknown function (DUF4515); This family of proteins is found in bacteria and eukaryotes. Proteins in this family are typically between 198 and 469 amino acids in length. There are two completely conserved L residues that may be functionally important.


Pssm-ID: 405647 [Multi-domain]  Cd Length: 206  Bit Score: 51.31  E-value: 1.42e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159648420  700 KKIKSEYEKKLQTM-NKELQRLQTAQKEHARLLknqSQYEKQLKKLQQEVTEMKKTKVRLMKQMKEEQEKARMTESrRNR 778
Cdd:pfam14988   10 AKKTEEKQKKIEKLwNQYVQECEEIERRRQELA---SRYTQQTAELQTQLLQKEKEQASLKKELQALRPFAKLKES-QER 85

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159648420  779 EIAQLKKEQRK--REHQLKLLEAQKRnqevILRRKteevTALRRQVRPLSDKVAGKVSRK 836
Cdd:pfam14988   86 EIQDLEEEKEKvrAETAEKDREAHLQ----FLKEK----ALLEKQLQELRILELGERATR 137
rad50 TIGR00606
rad50; All proteins in this family for which functions are known are involvedin recombination, ...
 638-978 1.43e-06

rad50; All proteins in this family for which functions are known are involvedin recombination, recombinational repair, and/or non-homologous end joining.They are components of an exonuclease complex with MRE11 homologs. This family is distantly related to the SbcC family of bacterial proteins.This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University).


Pssm-ID: 129694 [Multi-domain]  Cd Length: 1311  Bit Score: 53.90  E-value: 1.43e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159648420  638 EIAIKQKLIDELENSQRRLQTLKRQYEEKLMMLQHkIRDTQLERDQVLQNLGSVETySEEKAKKIKSEYEKKLQTMN--- 714
Cdd:TIGR00606  177 EIFSATRYIKALETLRQVRQTQGQKVQEHQMELKY-LKQYKEKACEIRDQITSKEA-QLESSREIVKSYENELDPLKnrl 254

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159648420  715 KELQRLQTAQKEHARLLKNQSQYEKQLKKLQQEVTE-MKKTKVRLMKQMKEEQEKARMTESRRNREIAQLKKEQRKREHQ 793
Cdd:TIGR00606  255 KEIEHNLSKIMKLDNEIKALKSRKKQMEKDNSELELkMEKVFQGTDEQLNDLYHNHQRTVREKERELVDCQRELEKLNKE 334

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159648420  794 LKLLEAQKrnQEVILRRKTEEVTALRRQVRplsdkvagkvSRKLSLPEHPIQEPSSSSSVEHDG-SRIAAQQKMRIPVAR 872
Cdd:TIGR00606  335 RRLLNQEK--TELLVEQGRLQLQADRHQEH----------IRARDSLIQSLATRLELDGFERGPfSERQIKNFHTLVIER 402

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159648420  873 VQALSVTATNGTG------RKYQRKAVTSRVYSSRAAR---MKWQLLERRVTDIIMQRMTISNMEADMNRLLTQREELTK 943
Cdd:TIGR00606  403 QEDEAKTAAQLCAdlqskeRLKQEQADEIRDEKKGLGRtieLKKEILEKKQEELKFVIKELQQLEGSSDRILELDQELRK 482

                          330       340       350       360
                   ....*....|....*....|....*....|....*....|....*.
gi 1159648420  944 RREKLS-----------KRREKLMKDgGGSETDRNVQNINEEMESL 978
Cdd:TIGR00606  483 AERELSkaeknsltetlKKEVKSLQN-EKADLDRKLRKLDQEMEQL 527
WD40 pfam00400
WD domain, G-beta repeat;
1315-1350 1.55e-06

WD domain, G-beta repeat;


Pssm-ID: 459801 [Multi-domain]  Cd Length: 39  Bit Score: 46.57  E-value: 1.55e-06
                           10        20        30
                   ....*....|....*....|....*....|....*...
gi 1159648420 1315 QCIYTAEGHTKAVLCVDATDD--LLFTGSKDRTCKVWN 1350
Cdd:pfam00400    2 KLLKTLEGHTGSVTSLAFSPDgkLLASGSDDGTVKVWD 39
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
639-835 1.73e-06

Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 53.77  E-value: 1.73e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159648420  639 IAIKQKLIDELEnsqRRLQTLKRQYEEklmmLQhKIRDTQLERDQVLQNLgsvETYSEEKaKKIKSeYEKKLQTMNKELQ 718
Cdd:COG4913    612 LAALEAELAELE---EELAEAEERLEA----LE-AELDALQERREALQRL---AEYSWDE-IDVAS-AEREIAELEAELE 678

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159648420  719 RLQTAQKEHARLLKNQSQYEKQLKKLQQEVTEMKKTKVRL---MKQMKEEQEKARMTESRRnreiaqlkkEQRKREHQLK 795
Cdd:COG4913    679 RLDASSDDLAALEEQLEELEAELEELEEELDELKGEIGRLekeLEQAEEELDELQDRLEAA---------EDLARLELRA 749

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*.
gi 1159648420  796 LLEA------QKRNQEVILRRKTEEVTALRRQVRPLSDKVAGKVSR 835
Cdd:COG4913    750 LLEErfaaalGDAVERELRENLEERIDALRARLNRAEEELERAMRA 795
PTZ00121 PTZ00121
MAEBL; Provisional
 624-976 2.07e-06

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 53.61  E-value: 2.07e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159648420  624 EKENYQADLAnitceiaiKQKlideLENSQRRLQTLKRQYEEKLMMLQHKIRDTQLERDQVLQnlgsvetySEEKA---K 700
Cdd:PTZ00121  1311 AEEAKKADEA--------KKK----AEEAKKKADAAKKKAEEAKKAAEAAKAEAEAAADEAEA--------AEEKAeaaE 1370

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159648420  701 KIKSEYEKKLQTMNK---------ELQRLQTAQKEHARLLKNQSQYEK---QLKKLQQEVTEMKKTKVRLMKQMKEEQEK 768
Cdd:PTZ00121  1371 KKKEEAKKKADAAKKkaeekkkadEAKKKAEEDKKKADELKKAAAAKKkadEAKKKAEEKKKADEAKKKAEEAKKADEAK 1450

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159648420  769 ARMTESRRNREIAQLKKEQRKREHQLKLLEAQKRNQEviLRRKTEEVTALRRQVRPLSD-KVAGKVSRKLSLPEHPIQEP 847
Cdd:PTZ00121  1451 KKAEEAKKAEEAKKKAEEAKKADEAKKKAEEAKKADE--AKKKAEEAKKKADEAKKAAEaKKKADEAKKAEEAKKADEAK 1528

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159648420  848 SSSSSVEHDGSRIAAQQKMRIPVARVQALSvTATNGTGRKYQRKAVTSRVYSSRAARMKWQLLERRVTDIIMQRMTISNM 927
Cdd:PTZ00121  1529 KAEEAKKADEAKKAEEKKKADELKKAEELK-KAEEKKKAEEAKKAEEDKNMALRKAEEAKKAEEARIEEVMKLYEEEKKM 1607

                          330       340       350       360       370
                   ....*....|....*....|....*....|....*....|....*....|..
gi 1159648420  928 EADMNRLLTQ---REELTKRREKLSKRREKLMKDggGSETDRNVQNINEEME 976
Cdd:PTZ00121  1608 KAEEAKKAEEakiKAEELKKAEEEKKKVEQLKKK--EAEEKKKAEELKKAEE 1657
235kDa-fam TIGR01612
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in ...
 628-1030 2.19e-06

reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in plasmodium species alternately annotated as reticulocyte binding protein, 235-kDa family protein and rhoptry protein. Rhoptry protein is localized on the cell surface and is extremely large (although apparently lacking in repeat structure) and is important for the process of invasion of the RBCs by the parasite. These proteins are found in P. falciparum, P. vivax and P. yoelii.


Pssm-ID: 130673 [Multi-domain]  Cd Length: 2757  Bit Score: 53.52  E-value: 2.19e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159648420  628 YQADLANITCEIA--IKQKLIDELENsQRRLQTLKRQYEEKLMMLQHkirdtqLERDQVLQNLGSVETYSE-------EK 698
Cdd:TIGR01612  669 YEDDIDALYNELSsiVKENAIDNTED-KAKLDDLKSKIDKEYDKIQN------METATVELHLSNIENKKNelldiivEI 741

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159648420  699 AKKIKSEYEKKLqtmNKELQRLQTAQKEHARLLKNQSQYEKQLKKLQQEVTEMKK--TKVRLMKQMKEEQEKARMTESRR 776
Cdd:TIGR01612  742 KKHIHGEINKDL---NKILEDFKNKEKELSNKINDYAKEKDELNKYKSKISEIKNhyNDQINIDNIKDEDAKQNYDKSKE 818

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159648420  777 NREIAQLKK-EQRKREHQLKLLEAQ---KRNQEVILRRK-TEEVTALRRQVRPLSDKVAGKVS-RKLSLPEHPIQEPSS- 849
Cdd:TIGR01612  819 YIKTISIKEdEIFKIINEMKFMKDDflnKVDKFINFENNcKEKIDSEHEQFAELTNKIKAEISdDKLNDYEKKFNDSKSl 898

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159648420  850 ----SSSVEHDGSRIAAQQKMR--IPVARVQALSVTATNGTGRKYQRK--------AVTSRVYSSRAARMKWQLLERRVT 915
Cdd:TIGR01612  899 ineiNKSIEEEYQNINTLKKVDeyIKICENTKESIEKFHNKQNILKEIlnknidtiKESNLIEKSYKDKFDNTLIDKINE 978

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159648420  916 -DIIMQRMTISNMEADMNRLLTQREELtkrREKLSKRREKLMKDgGGSETDRNVQNINEEMESLTANIDYINDSISDCQA 994
Cdd:TIGR01612  979 lDKAFKDASLNDYEAKNNELIKYFNDL---KANLGKNKENMLYH-QFDEKEKATNDIEQKIEDANKNIPNIEIAIHTSIY 1054

                          410       420       430
                   ....*....|....*....|....*....|....*.
gi 1159648420  995 NIMQmEEAKEEGETLDvtaVINACTLTEARYLLDHF 1030
Cdd:TIGR01612 1055 NIID-EIEKEIGKNIE---LLNKEILEEAEINITNF 1086
DUF612 pfam04747
Protein of unknown function, DUF612; This family includes several uncharacterized proteins ...
 641-1005 2.30e-06

Protein of unknown function, DUF612; This family includes several uncharacterized proteins from Caenorhabditis elegans.


Pssm-ID: 282585 [Multi-domain]  Cd Length: 511  Bit Score: 52.76  E-value: 2.30e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159648420  641 IKQKLIDELENSQRRLQTLKRQYEEKLM--MLQHKIRDtqlERDQVLQNLGSVEtySEEKAKKIKSEYEKKLQtmnKELQ 718
Cdd:pfam04747   12 IRQQLTNRRKNLGRVAKSQRNQFRQWLLtaVLPNSIND---QRKEAFASLELTE--QPQQVEKVKKSEKKKAQ---KQIA 83

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159648420  719 RLQTAQKEharlLKNQSQYEKQLKKLQQEVTEmKKTKVRLMKQMKEEQEKarmtesrrnreiaqLKKEQRKREHQLKLLE 798
Cdd:pfam04747   84 KDHEAEQK----VNAKKAAEKEARRAEAEAKK-RAAQEEEHKQWKAEQER--------------IQKEQEKKEADLKKLQ 144

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159648420  799 AQKRNQEVILRRKTEEVTALRRQVRPL---SDKVAGKVSRKLSLPehPIQEPSSSSSVEHDgsriaaqqkmriPVARVQA 875
Cdd:pfam04747  145 AEKKKEKAVKAEKAEKAEKTKKASTPApveEEIVVKKVANDRSAA--PAPEPKTPTNTPAE------------PAEQVQE 210

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159648420  876 LsvtatngTGRKYQRKAVTSRVYSSRAARMKWQLLE--RRVTDIIMQRMTISNMEADMNRLLTQREELTKRREK------ 947
Cdd:pfam04747  211 I-------TGKKNKKNKKKSESEATAAPASVEQVVEqpKVVTEEPHQQAAPQEKKNKKNKRKSESENVPAASETpvepvv 283

                          330       340       350       360       370       380
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1159648420  948 -----LSKRREKLMKDGGGSETDRNVQnineemESLTANIDYINDSISDCQANIMQMEEAKEE 1005
Cdd:pfam04747  284 ettppASENQKKNKKDKKKSESEKVVE------EPVQAEAPKSKKPTADDNMDFLDFVTAKEE 340
CCDC158 pfam15921
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ...
 641-897 2.36e-06

Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.


Pssm-ID: 464943 [Multi-domain]  Cd Length: 1112  Bit Score: 53.20  E-value: 2.36e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159648420  641 IKQ---KLIDELENSQRRLQTLKRQYE----------EKLMM----LQHKIRDTQLERDQVLQNLGSVETySEEKAKKIK 703
Cdd:pfam15921  651 IKQerdQLLNEVKTSRNELNSLSEDYEvlkrnfrnksEEMETttnkLKMQLKSAQSELEQTRNTLKSMEG-SDGHAMKVA 729

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159648420  704 SEYEKKLQTMNKELQRLQTAQK--EHARLLKNQSQY--EKQLKKLQQEVTEMKKTKvrlmKQMKEEQEKARMTESRRNRE 779
Cdd:pfam15921  730 MGMQKQITAKRGQIDALQSKIQflEEAMTNANKEKHflKEEKNKLSQELSTVATEK----NKMAGELEVLRSQERRLKEK 805

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159648420  780 IAQLKKEQRKRehQLKLLEAQKrnqevILRRKTEEVTALRRQ----VRPL-------SDKVAGKVSRKLSLPEHPIQEPS 848
Cdd:pfam15921  806 VANMEVALDKA--SLQFAECQD-----IIQRQEQESVRLKLQhtldVKELqgpgytsNSSMKPRLLQPASFTRTHSNVPS 878

                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1159648420  849 SSSS-------------VEHDGSRIAAQ--QKMRIPVARVQALSVTATNGTGRKYQRKAVTSRV 897
Cdd:pfam15921  879 SQSTasflshhsrktnaLKEDPTRDLKQllQELRSVINEEPTVQLSKAEDKGRAPSLGALDDRV 942
PRK00409 PRK00409
recombination and DNA strand exchange inhibitor protein; Reviewed
 625-755 2.48e-06

recombination and DNA strand exchange inhibitor protein; Reviewed


Pssm-ID: 234750 [Multi-domain]  Cd Length: 782  Bit Score: 52.91  E-value: 2.48e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159648420  625 KENYQADLANItceiaikQKLIDELENSQRRLQT-------LKRQYEEKLMMLQHKIRDTQLERDQVLQNLgsvetysEE 697
Cdd:PRK00409   508 KKLIGEDKEKL-------NELIASLEELERELEQkaeeaeaLLKEAEKLKEELEEKKEKLQEEEDKLLEEA-------EK 573

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1159648420  698 KAKKI----KSEYEKKLQTMNKELQRLQTAQKEHaRLLKNQSQYEKQLKKLQQEVTEMKKTK 755
Cdd:PRK00409   574 EAQQAikeaKKEADEIIKELRQLQKGGYASVKAH-ELIEARKRLNKANEKKEKKKKKQKEKQ 634
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 366-790 2.61e-06

chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 53.14  E-value: 2.61e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159648420  366 NRARNIKNkvmvnqdrASQQINALRSEIARLQMELMEYKTGKRIIDEEGVEsindmfhenamLQTENNNLRVRIKAMQET 445
Cdd:TIGR02168  674 ERRREIEE--------LEEKIEELEEKIAELEKALAELRKELEELEEELEQ-----------LRKELEELSRQISALRKD 734

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159648420  446 VDALRARITQLmsdqaNQVLARAGEGNEEISNMIHNYIKEIEDLRAKLLESEAVNENLRRNLSRASTRSTYFGgpsafsa 525
Cdd:TIGR02168  735 LARLEAEVEQL-----EERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALR------- 802

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159648420  526 SMLSSEKETLEILDIAKKDLEKLKKKERKKKKSVKEDNTDNEQEKRDEKGSSERENNELEAEEIQEAsdredeeeedded 605
Cdd:TIGR02168  803 EALDELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIE------------- 869

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159648420  606 eddmevvESSDESDSDSDEKENYQADLANITCEIAIKQKLIDELENsqrRLQTLKRQYEEklmmLQHKIRDTQLERDQVL 685
Cdd:TIGR02168  870 -------ELESELEALLNERASLEEALALLRSELEELSEELRELES---KRSELRRELEE----LREKLAQLELRLEGLE 935

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159648420  686 QNLgsvetysEEKAKKIKSEYEkklqtMNkelqrLQTAQKEHARLLKNQSQYEKQLKKLQQEVTEMKktKVRLM-----K 760
Cdd:TIGR02168  936 VRI-------DNLQERLSEEYS-----LT-----LEEAEALENKIEDDEEEARRRLKRLENKIKELG--PVNLAaieeyE 996

                          410       420       430
                   ....*....|....*....|....*....|....*..
gi 1159648420  761 QMKE-----EQEKARMTESRRNRE--IAQLKKEQRKR 790
Cdd:TIGR02168  997 ELKErydflTAQKEDLTEAKETLEeaIEEIDREARER 1033
COG2433 COG2433
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
696-838 2.73e-06

Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];


Pssm-ID: 441980 [Multi-domain]  Cd Length: 644  Bit Score: 52.94  E-value: 2.73e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159648420  696 EEKAKKIKSEYEKKLQTMNKELQRLQtaqKEHARLlknqsqyEKQLKKLQQEVTEMKKT------KVRLMKQmkEEQEKA 769
Cdd:COG2433    394 EPEAEREKEHEERELTEEEEEIRRLE---EQVERL-------EAEVEELEAELEEKDERierlerELSEARS--EERREI 461

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1159648420  770 RMTE--SRRNREIAQLKKEqrkrehqlkLLEAQKRNQEviLRRKTEEVTALRRQVRpLSDKVAGKVSRKLS 838
Cdd:COG2433    462 RKDReiSRLDREIERLERE---------LEEERERIEE--LKRKLERLKELWKLEH-SGELVPVKVVEKFT 520
Myosin_tail_1 pfam01576
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ...
 642-1099 2.94e-06

Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.


Pssm-ID: 460256 [Multi-domain]  Cd Length: 1081  Bit Score: 52.87  E-value: 2.94e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159648420  642 KQKLIDELENSQRRLQTLKrqyEEKlMMLQHKIR-DTQL----------------ERDQVLQNLGSVETYSEEKAKKIKS 704
Cdd:pfam01576   21 QQKAESELKELEKKHQQLC---EEK-NALQEQLQaETELcaeaeemrarlaarkqELEEILHELESRLEEEEERSQQLQN 96

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159648420  705 EyEKKLQTMNKELQRlQTAQKEHARllkNQSQYEK-----QLKKLQQEVTEMKKTKVRLMK--------------QMKEE 765
Cdd:pfam01576   97 E-KKKMQQHIQDLEE-QLDEEEAAR---QKLQLEKvtteaKIKKLEEDILLLEDQNSKLSKerklleeriseftsNLAEE 171

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159648420  766 QEKARMTESRRNRE---IAQLKKEQRKREHQLKLLEAQKRNQEvilrrktEEVTALRRQVRPLSDKVAgKVSRKLSLPEH 842
Cdd:pfam01576  172 EEKAKSLSKLKNKHeamISDLEERLKKEEKGRQELEKAKRKLE-------GESTDLQEQIAELQAQIA-ELRAQLAKKEE 243

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159648420  843 PIQEPSSSSSvEHDGSRIAAQQKMRIPVARVQALsvtatngtgrkyQRKAVTSRVYSSRAARMKWQL---LERRVTDiim 919
Cdd:pfam01576  244 ELQAALARLE-EETAQKNNALKKIRELEAQISEL------------QEDLESERAARNKAEKQRRDLgeeLEALKTE--- 307

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159648420  920 qrmtisnMEADMNRLLTQREELTKRREKLSkrrekLMKDGGGSETDRNVQNINEEMESLTANIDYINDSISDCQANIMQM 999
Cdd:pfam01576  308 -------LEDTLDTTAAQQELRSKREQEVT-----ELKKALEEETRSHEAQLQEMRQKHTQALEELTEQLEQAKRNKANL 375

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159648420 1000 EEAKE--EGETLDVTAVINacTLTEARYLLDHfltmginkglQAAQKEAQIKVLEGRLKQTEitsatqnqllfhmlKEKA 1077
Cdd:pfam01576  376 EKAKQalESENAELQAELR--TLQQAKQDSEH----------KRKKLEGQLQELQARLSESE--------------RQRA 429

                          490       500
                   ....*....|....*....|..
gi 1159648420 1078 ELNPELdallgHALQDNLEDST 1099
Cdd:pfam01576  430 ELAEKL-----SKLQSELESVS 446
DUF4686 pfam15742
Domain of unknown function (DUF4686); This family of proteins is found in eukaryotes. Proteins ...
 637-805 3.50e-06

Domain of unknown function (DUF4686); This family of proteins is found in eukaryotes. Proteins in this family are typically between 498 and 775 amino acids in length. There is a conserved DLK sequence motif.


Pssm-ID: 464838 [Multi-domain]  Cd Length: 384  Bit Score: 51.99  E-value: 3.50e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159648420  637 CEIAIKQKLidELENSQRRLQTLKRQYEE---KLMMLQHKIRDTQLERDQVLQNLGSV----ETYSEEKAKKIKSEyEKK 709
Cdd:pfam15742   54 QEENIKIKA--ELKQAQQKLLDSTKMCSSltaEWKHCQQKIRELELEVLKQAQSIKSQnslqEKLAQEKSRVADAE-EKI 130

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159648420  710 LqtmnkELQRlqtaQKEHARLLKNQSQYEKQLKKLQQEVTEMKKTKVRLMKQMKEEQEK-----ARMTESRRNREIAQLK 784
Cdd:pfam15742  131 L-----ELQQ----KLEHAHKVCLTDTCILEKKQLEERIKEASENEAKLKQQYQEEQQKrklldQNVNELQQQVRSLQDK 201

                          170       180       190
                   ....*....|....*....|....*....|...
gi 1159648420  785 KEQRKR------------EHQLKLLEAQKRNQE 805
Cdd:pfam15742  202 EAQLEMtnsqqqlriqqqEAQLKQLENEKRKSD 234
TolA COG3064
Membrane protein TolA involved in colicin uptake [Cell wall/membrane/envelope biogenesis];
643-1008 3.82e-06

Membrane protein TolA involved in colicin uptake [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 442298 [Multi-domain]  Cd Length: 485  Bit Score: 51.96  E-value: 3.82e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159648420  643 QKLIDELENSQRRLQTLKRQYEEKLmmLQHKIRDTQLERDQvlqnlgsvetysEEKAKKIKSEYEKKLQTMNKEL-QRLQ 721
Cdd:COG3064     15 QERLEQAEAEKRAAAEAEQKAKEEA--EEERLAELEAKRQA------------EEEAREAKAEAEQRAAELAAEAaKKLA 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159648420  722 TAQKEHARLlknQSQYEKQLKKLQQEvTEMKKTKvrlmKQMKEEQEKARMTESRRNREI-AQLKKEQRKREHQLKLLEAQ 800
Cdd:COG3064     81 EAEKAAAEA---EKKAAAEKAKAAKE-AEAAAAA----EKAAAAAEKEKAEEAKRKAEEeAKRKAEEERKAAEAEAAAKA 152

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159648420  801 KRNQEVILRRKTEEVTALRRQVRPLSDKVAGKVSRKLSLPEHPIQEPSSSSSVEHDGSRIAAQQKMRIPVARVQALSVTA 880
Cdd:COG3064    153 EAEAARAAAAAAAAAAAAAARAAAGAAAALVAAAAAAVEAADTAAAAAAALAAAAAAAAADAALLALAVAARAAAASREA 232

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159648420  881 TNGTGRKYQRKAVTSRVYSSRAARMKWQLLERRVTDIIMQRMTISNMEADMNRLLTQREELTKRREKLSKRREKLMKDGG 960
Cdd:COG3064    233 ALAAVEATEEAALGGAEEAADLAAVGVLGAALAAAAAGAAALSSGLVVVAAALAGLAAAAAGLVLDDSAALAAELLGAVA 312

                          330       340       350       360
                   ....*....|....*....|....*....|....*....|....*...
gi 1159648420  961 GSETDRNVQNINEEMESLTANIDYINDSISDCQANIMQMEEAKEEGET 1008
Cdd:COG3064    313 AEEAVLAAAAAAGALVVRGGGAASLEAALSLLAAGAAAAAAGAGALAT 360
YscO-like pfam16789
YscO-like protein; This family of proteins is similar to the type III secretion protein YscO. ...
 641-791 4.07e-06

YscO-like protein; This family of proteins is similar to the type III secretion protein YscO. The family includes Chlamydia trachomatis CT670 which is found in a type III secretion gene cluster. CT670 interacts with CT671, a putative YscP homolog and CT670 and CT671 may form a chaperone-effector pair.


Pssm-ID: 435583 [Multi-domain]  Cd Length: 160  Bit Score: 49.06  E-value: 4.07e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159648420  641 IKQKLIDELE----NSQRRL----QTLKRQYEEKLMMLQHKIRDTQLERDQVLQNLGSvetyseEKAKKIKsEYEKKLQT 712
Cdd:pfam16789   11 IKKKRVEEAEkvvkDKKRALekekEKLAELEAERDKVRKHKKAKMQQLRDEMDRGTTS------DKILQMK-RYIKVVKE 83

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159648420  713 MNKELQRLQTAQKEHARLL-KNQSQYEKQLKKLQQEVTEMKKTKVRLMKQMKEEQEKArmtESRRNREIAQLKKEQRKRE 791
Cdd:pfam16789   84 RLKQEEKKVQDQKEQVRTAaRNLEIAREELKKKRQEVEKLEKHKKEWVKEMKKEEEDQ---EEREQDEIGSALHLANQRK 160
PKK pfam12474
Polo kinase kinase; This domain family is found in eukaryotes, and is approximately 140 amino ...
 678-814 4.75e-06

Polo kinase kinase; This domain family is found in eukaryotes, and is approximately 140 amino acids in length. The family is found in association with pfam00069. Polo-like kinase 1 (Plx1) is essential during mitosis for the activation of Cdc25C, for spindle assembly, and for cyclin B degradation. This family is Polo kinase kinase (PKK) which phosphorylates Polo kinase and Polo-like kinase to activate them. PKK is a serine/threonine kinase.


Pssm-ID: 463600 [Multi-domain]  Cd Length: 139  Bit Score: 48.33  E-value: 4.75e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159648420  678 QLERDQVLqnlgsvETYSEEKAKKIKSeYEKKLQTMnkelQRLQTAQKEhaRLLKNQSQYEKQLKKLQ---QEvTEMKKT 754
Cdd:pfam12474    2 QLQKEQQK------DRFEQERQQLKKR-YEKELEQL----ERQQKQQIE--KLEQRQTQELRRLPKRIraeQK-KRLKMF 67

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1159648420  755 KVRLMKQMKEE-QEKARMTESRRNREIAQLK--KEQRKREHQLKLLEAQKRNQEVILRRKTEE 814
Cdd:pfam12474   68 RESLKQEKKELkQEVEKLPKFQRKEAKRQRKeeLELEQKHEELEFLQAQSEALERELQQLQNE 130
WD40 smart00320
WD40 repeats; Note that these repeats are permuted with respect to the structural repeats ...
 1313-1350 5.37e-06

WD40 repeats; Note that these repeats are permuted with respect to the structural repeats (blades) of the beta propeller domain.


Pssm-ID: 197651 [Multi-domain]  Cd Length: 40  Bit Score: 45.38  E-value: 5.37e-06
                            10        20        30        40
                    ....*....|....*....|....*....|....*....|
gi 1159648420  1313 PLQCIYTAEGHTKAVLCVDATDD--LLFTGSKDRTCKVWN 1350
Cdd:smart00320    1 SGELLKTLKGHTGPVTSVAFSPDgkYLASGSDDGTIKLWD 40
DUF4670 pfam15709
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins ...
 684-821 5.79e-06

Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins in this family are typically between 373 and 763 amino acids in length.


Pssm-ID: 464815 [Multi-domain]  Cd Length: 522  Bit Score: 51.49  E-value: 5.79e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159648420  684 VLQNLGSVETYSEEKAKK---IKSEYEKKLQtmnkelQRLQTAQKEHARL---LKNQSQYEKqlKKLQQEVTE-MKKTKV 756
Cdd:pfam15709  305 VTGNMESEEERSEEDPSKallEKREQEKASR------DRLRAERAEMRRLeveRKRREQEEQ--RRLQQEQLErAEKMRE 376

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1159648420  757 RLMKQMKEEQEKARMTESRRNREIAQLKKEQRKREHQLKLLEAQKRNQEVILRRKTEEVTALRRQ 821
Cdd:pfam15709  377 ELELEQQRRFEEIRLRKQRLEEERQRQEEEERKQRLQLQAAQERARQQQEEFRRKLQELQRKKQQ 441
MAD pfam05557
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ...
 637-1051 7.11e-06

Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint (Mitotic arrest deficient or MAD) proteins. The mitotic spindle checkpoint monitors proper attachment of the bipolar spindle to the kinetochores of aligned sister chromatids and causes a cell cycle arrest in prometaphase when failures occur. Multiple components of the mitotic spindle checkpoint have been identified in yeast and higher eukaryotes. In S.cerevisiae, the existence of a Mad1-dependent complex containing Mad2, Mad3, Bub3 and Cdc20 has been demonstrated.


Pssm-ID: 461677 [Multi-domain]  Cd Length: 660  Bit Score: 51.67  E-value: 7.11e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159648420  637 CEIAIKQKLIDELENSQrrlqtLKRQYEEKLMMLQHKIRDTQLERDQVLQNLGSvETySEEKAKKIKSEYEkkLQTMNKE 716
Cdd:pfam05557   63 REAEAEEALREQAELNR-----LKKKYLEALNKKLNEKESQLADAREVISCLKN-EL-SELRRQIQRAELE--LQSTNSE 133

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159648420  717 LQRLQTAQKEHARLLKNQSQYEKQLKKLQQEVTE----MKKTKVRLMKQmkeEQEKARMTESR-RNREIAQLKKEQRKRE 791
Cdd:pfam05557  134 LEELQERLDLLKAKASEAEQLRQNLEKQQSSLAEaeqrIKELEFEIQSQ---EQDSEIVKNSKsELARIPELEKELERLR 210

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159648420  792 HQLKLLEAQKRNQEVIlrrkTEEVTALRRQVRPLSDKVAGKVSRKLSLpEHPIQEPSSSSSVEHDGSriaaqQKMRIPVA 871
Cdd:pfam05557  211 EHNKHLNENIENKLLL----KEEVEDLKRKLEREEKYREEAATLELEK-EKLEQELQSWVKLAQDTG-----LNLRSPED 280

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159648420  872 ---RVQALSvtatngtgrkyQRKAV-TSRVYSSRaarmkwqllerrvTDIIMQRMTISNMEADMNRLLTQREELTKRREK 947
Cdd:pfam05557  281 lsrRIEQLQ-----------QREIVlKEENSSLT-------------SSARQLEKARRELEQELAQYLKKIEDLNKKLKR 336

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159648420  948 LSKRREKLmkdgggsetDRNVQNINEEMESLTANIDYINDSISDCQANIMQMEEAKEEGETLDVTAVINActltEARYLL 1027
Cdd:pfam05557  337 HKALVRRL---------QRRVLLLTKERDGYRAILESYDKELTMSNYSPQLLERIEEAEDMTQKMQAHNE----EMEAQL 403

                          410       420
                   ....*....|....*....|....
gi 1159648420 1028 DHFLTMGINKGLQAAQKEAQIKVL 1051
Cdd:pfam05557  404 SVAEEELGGYKQQAQTLERELQAL 427
CALCOCO1 pfam07888
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ...
 625-816 7.18e-06

Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are similar to the coiled-coil transcriptional coactivator protein coexpressed by Mus musculus (CoCoA/CALCOCO1). This protein binds to a highly conserved N-terminal domain of p160 coactivators, such as GRIP1, and thus enhances transcriptional activation by a number of nuclear receptors. CALCOCO1 has a central coiled-coil region with three leucine zipper motifs, which is required for its interaction with GRIP1 and may regulate the autonomous transcriptional activation activity of the C-terminal region.


Pssm-ID: 462303 [Multi-domain]  Cd Length: 488  Bit Score: 51.05  E-value: 7.18e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159648420  625 KENYQADLANITCEIAIKQKLIDELENSQRRLQTLKRQYEEKLMMLQHKIRDTQ---LERDQVLQNLGSVE---TYSEEK 698
Cdd:pfam07888  173 RKQLQAKLQQTEEELRSLSKEFQELRNSLAQRDTQVLQLQDTITTLTQKLTTAHrkeAENEALLEELRSLQerlNASERK 252

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159648420  699 AKKIKSE---------------YEKKLQTMNKELQ---------------------RLQTAQKEHARLLKNQSQYEKQLK 742
Cdd:pfam07888  253 VEGLGEElssmaaqrdrtqaelHQARLQAAQLTLQladaslalregrarwaqeretLQQSAEADKDRIEKLSAELQRLEE 332

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1159648420  743 KLQQEVTEMKKTKVRLMKqmkeEQEKARMTESRRNREIAQLKKEQRKREHQLKLLEAQKrnQEVI-----LRRKTEEVT 816
Cdd:pfam07888  333 RLQEERMEREKLEVELGR----EKDCNRVQLSESRRELQELKASLRVAQKEKEQLQAEK--QELLeyirqLEQRLETVA 405
SMC_N pfam02463
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ...
 278-805 8.43e-06

RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The SMC (structural maintenance of chromosomes) superfamily proteins have ATP-binding domains at the N- and C-termini, and two extended coiled-coil domains separated by a hinge in the middle. The eukaryotic SMC proteins form two kind of heterodimers: the SMC1/SMC3 and the SMC2/SMC4 types. These heterodimers constitute an essential part of higher order complexes, which are involved in chromatin and DNA dynamics. This family also includes the RecF and RecN proteins that are involved in DNA metabolism and recombination.


Pssm-ID: 426784 [Multi-domain]  Cd Length: 1161  Bit Score: 51.51  E-value: 8.43e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159648420  278 SERLKRTGATGERAKEGISINCGLLALGNVISALGDKSKKATHVPYRDSKLTRLLQDSLGGNsQTLMIACVSPSDRDFME 357
Cdd:pfam02463  528 HGRLGDLGVAVENYKVAISTAVIVEVSATADEVEERQKLVRALTELPLGARKLRLLIPKLKL-PLKSIAVLEIDPILNLA 606

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159648420  358 TLNtlKYANRARNIKNKVMVNQDRASQQINALRSE-IARLQMELMEYKTGKRIIDEE-----GVESINDMFHENAMLQT- 430
Cdd:pfam02463  607 QLD--KATLEADEDDKRAKVVEGILKDTELTKLKEsAKAKESGLRKGVSLEEGLAEKsevkaSLSELTKELLEIQELQEk 684

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159648420  431 -ENNNLRVRIKAMQETVDALRARITQLM---SDQANQVLARAGEGNEEISNMIhnYIKEIEDLRAKLLESEAVNENLRRN 506
Cdd:pfam02463  685 aESELAKEEILRRQLEIKKKEQREKEELkklKLEAEELLADRVQEAQDKINEE--LKLLKQKIDEEEEEEEKSRLKKEEK 762

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159648420  507 LSRASTRSTYFggpsafsaSMLSSEKETLEILdiakkdlEKLKKKERKKKKSVKEDNTDNEQEKRDEKGSSERENNELEA 586
Cdd:pfam02463  763 EEEKSELSLKE--------KELAEEREKTEKL-------KVEEEKEEKLKAQEEELRALEEELKEEAELLEEEQLLIEQE 827

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159648420  587 EEIQEAsdredeeeeddedEDDMEVVESSDESDSDSDEKENYQADLANITCEIAIKQKLIDELENSQRRlqtlKRQYEEK 666
Cdd:pfam02463  828 EKIKEE-------------ELEELALELKEEQKLEKLAEEELERLEEEITKEELLQELLLKEEELEEQK----LKDELES 890

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159648420  667 LMMLQHKIRDTQLERDQVLQNLGSVETYSEEKAKKIKsEYEKKLQTMNKELQRLQTAQKEhaRLLKNQSQYEKQLKKLQQ 746
Cdd:pfam02463  891 KEEKEKEEKKELEEESQKLNLLEEKENEIEERIKEEA-EILLKYEEEPEELLLEEADEKE--KEENNKEEEEERNKRLLL 967

                          490       500       510       520       530       540
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1159648420  747 EVTEMKKTKVRLMKQMKEEQE--------KARMTESRR--NREIAQLKKEQRKREHQLKLLEAQKRNQE 805
Cdd:pfam02463  968 AKEELGKVNLMAIEEFEEKEErynkdeleKERLEEEKKklIRAIIEETCQRLKEFLELFVSINKGWNKV 1036
DUF4659 pfam15558
Domain of unknown function (DUF4659); This family of proteins is found in eukaryotes. Proteins ...
 650-957 8.55e-06

Domain of unknown function (DUF4659); This family of proteins is found in eukaryotes. Proteins in this family are typically between 427 and 674 amino acids in length. There are two completely conserved residues (D and I) that may be functionally important.


Pssm-ID: 464768 [Multi-domain]  Cd Length: 374  Bit Score: 50.81  E-value: 8.55e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159648420  650 ENSQRRLQT--------LKRQYEEKLMMLQHkirdtqlERDQVLQNlgSVETYSEEKAK-KIKSEYE-------KKLQTM 713
Cdd:pfam15558   20 EQRMRELQQqaalaweeLRRRDQKRQETLER-------ERRLLLQQ--SQEQWQAEKEQrKARLGREerrradrREKQVI 90

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159648420  714 NKELQ-RLQTAQKEHARLLKNQS-QYEKQLKKLQQEvtemkktkvrlmkQMKEEQEKARMTESRRNREIAQLKKEQRKRE 791
Cdd:pfam15558   91 EKESRwREQAEDQENQRQEKLERaRQEAEQRKQCQE-------------QRLKEKEEELQALREQNSLQLQERLEEACHK 157

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159648420  792 HQLKLLEAQKRNQEvilRRKTEEVTALRRQVRPLSDKVAGKVSRKLSLpehpiqEPSSSSSVE-HDGSRIAAQQKMRIPV 870
Cdd:pfam15558  158 RQLKEREEQKKVQE---NNLSELLNHQARKVLVDCQAKAEELLRRLSL------EQSLQRSQEnYEQLVEERHRELREKA 228

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159648420  871 ARVQALSVTATNGTGRKYQ----RKAVTSRVySSRAARMKWQLLERRVTDiIMQRMTISNMEAD----MNRLLTQREELT 942
Cdd:pfam15558  229 QKEEEQFQRAKWRAEEKEEerqeHKEALAEL-ADRKIQQARQVAHKTVQD-KAQRARELNLEREknhhILKLKVEKEEKC 306

                          330
                   ....*....|....*
gi 1159648420  943 KRREKLSKRREKLMK 957
Cdd:pfam15558  307 HREGIKEAIKKKEQR 321
PTZ00121 PTZ00121
MAEBL; Provisional
 483-1007 1.00e-05

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 51.30  E-value: 1.00e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159648420  483 IKEIEDLRAKLLESEAVnENLRRNLSRASTRSTYFGGPSAFSASMLSSEKETLEIL---------DIAKKDLEKLKKKER 553
Cdd:PTZ00121  1229 VKKAEEAKKDAEEAKKA-EEERNNEEIRKFEEARMAHFARRQAAIKAEEARKADELkkaeekkkaDEAKKAEEKKKADEA 1307

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159648420  554 KKKKSVKedNTDNEQEKRDEKGSSERENNELEAEEIQEASDREDEEEEDDEDEDDMEVVESSDESDSDSDEKEnyQADLA 633
Cdd:PTZ00121  1308 KKKAEEA--KKADEAKKKAEEAKKKADAAKKKAEEAKKAAEAAKAEAEAAADEAEAAEEKAEAAEKKKEEAKK--KADAA 1383

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159648420  634 NITCEiaiKQKLIDEL----ENSQRRLQTLKRQYEEKLMMLQHKIRDTQLERDQVLQNLGSvETYSEEKAKKiKSEYEKK 709
Cdd:PTZ00121  1384 KKKAE---EKKKADEAkkkaEEDKKKADELKKAAAAKKKADEAKKKAEEKKKADEAKKKAE-EAKKADEAKK-KAEEAKK 1458

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159648420  710 LQTMNKELQrlqtaQKEHARLLKNQSQYEKQLKKLQQEVTEMKKTKVRLMK--QMKEEQEKARMTESRRNREIAQlKKEQ 787
Cdd:PTZ00121  1459 AEEAKKKAE-----EAKKADEAKKKAEEAKKADEAKKKAEEAKKKADEAKKaaEAKKKADEAKKAEEAKKADEAK-KAEE 1532

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159648420  788 RKREHQLKLLEAQKRNQEVilrRKTEEVTAlRRQVRPLSDKVAGKVSRKLSLPEHPIQEPSSSSSVEHDGSRIAAQQKMR 867
Cdd:PTZ00121  1533 AKKADEAKKAEEKKKADEL---KKAEELKK-AEEKKKAEEAKKAEEDKNMALRKAEEAKKAEEARIEEVMKLYEEEKKMK 1608

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159648420  868 IPVAR-VQALSVTATNGTGRKYQRKAVTSRVYSSRAARMKWQLLERRVTDIIMQRMTISNMEADMNRlltQREELTKRRE 946
Cdd:PTZ00121  1609 AEEAKkAEEAKIKAEELKKAEEEKKKVEQLKKKEAEEKKKAEELKKAEEENKIKAAEEAKKAEEDKK---KAEEAKKAEE 1685

                          490       500       510       520       530       540
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1159648420  947 KLSKRREKLMKDgggSETDRNVQNINEEMESLTANIDYINDSIsdcQANIMQMEEAKEEGE 1007
Cdd:PTZ00121  1686 DEKKAAEALKKE---AEEAKKAEELKKKEAEEKKKAEELKKAE---EENKIKAEEAKKEAE 1740
PRK00409 PRK00409
recombination and DNA strand exchange inhibitor protein; Reviewed
 647-796 1.35e-05

recombination and DNA strand exchange inhibitor protein; Reviewed


Pssm-ID: 234750 [Multi-domain]  Cd Length: 782  Bit Score: 50.60  E-value: 1.35e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159648420  647 DELENSQRRLQTLKRQYEEKLMMLQHKIRDTQLERDQVlqnlgsvetysEEKAKKIKSEYEKKLQTMNKELQ-RLQTAQK 725
Cdd:PRK00409   516 EKLNELIASLEELERELEQKAEEAEALLKEAEKLKEEL-----------EEKKEKLQEEEDKLLEEAEKEAQqAIKEAKK 584

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1159648420  726 EHARLLKNQSQYEKQLKKLQ--QEVTEMKKtkvRLMKQMKEEQEKarmtesrrnreiaqlKKEQRKREHQLKL 796
Cdd:PRK00409   585 EADEIIKELRQLQKGGYASVkaHELIEARK---RLNKANEKKEKK---------------KKKQKEKQEELKV 639
SCP-1 pfam05483
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ...
 369-811 1.49e-05

Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major component of the transverse filaments of the synaptonemal complex. Synaptonemal complexes are structures that are formed between homologous chromosomes during meiotic prophase.


Pssm-ID: 114219 [Multi-domain]  Cd Length: 787  Bit Score: 50.49  E-value: 1.49e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159648420  369 RNIKNKVMVNQDrasqQINALRSEIARLQMELME---YKTGKriidEEGVESINDMFHENAMLQTENNNLRVRIKAM--- 442
Cdd:pfam05483  366 RTEQQRLEKNED----QLKIITMELQKKSSELEEmtkFKNNK----EVELEELKKILAEDEKLLDEKKQFEKIAEELkgk 437

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159648420  443 -QETVDALRARITQLmSDQANQVLAragegneeISNMIHNYIKEIEDLRAKLLESEAVNENLRRNLSRAStrstyfggps 521
Cdd:pfam05483  438 eQELIFLLQAREKEI-HDLEIQLTA--------IKTSEEHYLKEVEDLKTELEKEKLKNIELTAHCDKLL---------- 498

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159648420  522 afsasmLSSEKETLEILDIAKKDLEKLKKKerkkkksvkedNTDNEQEKRDEKGSSERENNEL----EAEEIQEASDRED 597
Cdd:pfam05483  499 ------LENKELTQEASDMTLELKKHQEDI-----------INCKKQEERMLKQIENLEEKEMnlrdELESVREEFIQKG 561

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159648420  598 EEEEDDEDEDDMEVVESSDESDSDSDEKENYQADLANITCEIAIKQKLIDELENSQRRLQTLKRQYEEKLMMLQHKIRDT 677
Cdd:pfam05483  562 DEVKCKLDKSEENARSIEYEVLKKEKQMKILENKCNNLKKQIENKNKNIEELHQENKALKKKGSAENKQLNAYEIKVNKL 641

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159648420  678 QLERDQVLQNLGSV-ETYSEE-KAKKIKS-----EYEKKLQT------MNKEL-QRLQTAQKEHARLL-KNQSQYEKqlk 742
Cdd:pfam05483  642 ELELASAKQKFEEIiDNYQKEiEDKKISEeklleEVEKAKAIadeavkLQKEIdKRCQHKIAEMVALMeKHKHQYDK--- 718

                          410       420       430       440       450       460       470
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1159648420  743 klqqeVTEMKKTKVRLMKQMKEEQEKARM---TE-SRRNREIAQLKKE-QRKREHQLKLLEAQKRNQEVILRRK 811
Cdd:pfam05483  719 -----IIEERDSELGLYKNKEQEQSSAKAaleIElSNIKAELLSLKKQlEIEKEEKEKLKMEAKENTAILKDKK 787
PRK12704 PRK12704
phosphodiesterase; Provisional
 696-818 1.69e-05

phosphodiesterase; Provisional


Pssm-ID: 237177 [Multi-domain]  Cd Length: 520  Bit Score: 50.16  E-value: 1.69e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159648420  696 EEKAKKIKSEYEKKLQTMNKElqRLQTAQKEharLLKNQSQYEKQLKKLQQEVTEMKKtkvRLmkQMKEEQEKARMTE-S 774
Cdd:PRK12704    37 EEEAKRILEEAKKEAEAIKKE--ALLEAKEE---IHKLRNEFEKELRERRNELQKLEK---RL--LQKEENLDRKLELlE 106

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....
gi 1159648420  775 RRNREIAQLKKEQRKREHQLKLLEAQKRNQEVILRRKTEEVTAL 818
Cdd:PRK12704   107 KREEELEKKEKELEQKQQELEKKEEELEELIEEQLQELERISGL 150
GumC COG3206
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
643-774 1.85e-05

Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 442439 [Multi-domain]  Cd Length: 687  Bit Score: 50.02  E-value: 1.85e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159648420  643 QKLIDELENSQRRLQTLKRQYEEklmmlQH-KIRDTQLERDQVLQNLgsvetysEEKAKKIKSEYEKKLQTMNKELQRLQ 721
Cdd:COG3206    266 QQLRAQLAELEAELAELSARYTP-----NHpDVIALRAQIAALRAQL-------QQEAQRILASLEAELEALQAREASLQ 333

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|...
gi 1159648420  722 TAQKEHARLLKNQSQYEKQLKKLQQEVtemkKTKVRLMKQMKEEQEKARMTES 774
Cdd:COG3206    334 AQLAQLEARLAELPELEAELRRLEREV----EVARELYESLLQRLEEARLAEA 382
PRK12704 PRK12704
phosphodiesterase; Provisional
 649-816 2.03e-05

phosphodiesterase; Provisional


Pssm-ID: 237177 [Multi-domain]  Cd Length: 520  Bit Score: 49.78  E-value: 2.03e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159648420  649 LENSQRRLQTLKRQYE----EKLMMLQHKIRDTQLERDQVLQNLgsvetysEEKAKKIKSEYEKKLQTMNKELQRLQTAQ 724
Cdd:PRK12704    44 LEEAKKEAEAIKKEALleakEEIHKLRNEFEKELRERRNELQKL-------EKRLLQKEENLDRKLELLEKREEELEKKE 116

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159648420  725 KEHARLLKNQSQYEKQLKKLQQE-VTEMKK--------TKVRLMKQMKEE--QEKARMTesrrnREIAQLKKEqrkrehq 793
Cdd:PRK12704   117 KELEQKQQELEKKEEELEELIEEqLQELERisgltaeeAKEILLEKVEEEarHEAAVLI-----KEIEEEAKE------- 184

                          170       180
                   ....*....|....*....|....*..
gi 1159648420  794 lkllEAQKRNQEVIL----RRKTEEVT 816
Cdd:PRK12704   185 ----EADKKAKEILAqaiqRCAADHVA 207
FAM184 pfam15665
Family with sequence similarity 184, A and B; The function of FAM184 is not known.
 647-822 2.31e-05

Family with sequence similarity 184, A and B; The function of FAM184 is not known.


Pssm-ID: 464788 [Multi-domain]  Cd Length: 211  Bit Score: 47.73  E-value: 2.31e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159648420  647 DELENSqrrLQTLKRQYEEKLmmlQHKIRDTqleRDQVLQNLGSVETYSEEKaKKIKS------EYEK-KLQTMNK-ELQ 718
Cdd:pfam15665   10 DEHEAE---IQALKEAHEEEI---QQILAET---REKILQYKSKIGEELDLK-RRIQTleesleQHERmKRQALTEfEQY 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159648420  719 RLQTAQKEharlLKNQSQYEKQLKKLQQEVTEMKKT---KVR-LMKQMKE-EQEKARMTESRR---NREIAQLKKEQRKR 790
Cdd:pfam15665   80 KRRVEERE----LKAEAEHRQRVVELSREVEEAKRAfeeKLEsFEQLQAQfEQEKRKALEELRakhRQEIQELLTTQRAQ 155

                          170       180       190
                   ....*....|....*....|....*....|....*...
gi 1159648420  791 -----EHQLKLLEAQKrnQEVI-LRRKTEEVTALRRQV 822
Cdd:pfam15665  156 sasslAEQEKLEELHK--AELEsLRKEVEDLRKEKKKL 191
CCDC34 pfam13904
Coiled-coil domain-containing protein 3; This family is found in eukaryotes; it has several ...
 660-795 2.63e-05

Coiled-coil domain-containing protein 3; This family is found in eukaryotes; it has several conserved tryptophan residues. The function is not known.


Pssm-ID: 464032 [Multi-domain]  Cd Length: 221  Bit Score: 47.78  E-value: 2.63e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159648420  660 KRQYEEKLMMLQHKirdtQLERDQvlqnlgsvetYSEEKAKKIKSEYEKKLQtmNKELQRLQTAQKEHARLLKNQSQyeK 739
Cdd:pfam13904   65 QRQRQKELQAQKEE----REKEEQ----------EAELRKRLAKEKYQEWLQ--RKARQQTKKREESHKQKAAESAS--K 126

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 1159648420  740 QLKKLQQEVTEmKKTKVRLMK--QMKEEQEKARMTESRRNREIAQLKKEQRKREHQLK 795
Cdd:pfam13904  127 SLAKPERKVSQ-EEAKEVLQEweRKKLEQQQRKREEEQREQLKKEEEEQERKQLAEKA 183
Borrelia_P83 pfam05262
Borrelia P83/100 protein; This family consists of several Borrelia P83/P100 antigen proteins.
 669-817 2.72e-05

Borrelia P83/100 protein; This family consists of several Borrelia P83/P100 antigen proteins.


Pssm-ID: 114011 [Multi-domain]  Cd Length: 489  Bit Score: 49.23  E-value: 2.72e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159648420  669 MLQHKIRDTQLERDQVlqNLGSVEtySEEKAKK---IKSEYEKKLQTMNKELQRLQTAQKEHARLLKNQSQYEKQLKKLQ 745
Cdd:pfam05262  186 LREDNEKGVNFRRDMT--DLKERE--SQEDAKRaqqLKEELDKKQIDADKAQQKADFAQDNADKQRDEVRQKQQEAKNLP 261

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159648420  746 QEV-TEMKKTKVRLMKQMKEEQEKARMtESRRNREIAQ---------LKKE---QRKREHQlKLLEAQKRNQEVI--LRR 810
Cdd:pfam05262  262 KPAdTSSPKEDKQVAENQKREIEKAQI-EIKKNDEEALkakdhkafdLKQEskaSEKEAED-KELEAQKKREPVAedLQK 339


                   ....*..
gi 1159648420  811 KTEEVTA 817
Cdd:pfam05262  340 TKPQVEA 346
TACC_C pfam05010
Transforming acidic coiled-coil-containing protein (TACC), C-terminal; This entry represents a ...
 627-807 2.79e-05

Transforming acidic coiled-coil-containing protein (TACC), C-terminal; This entry represents a C-terminal domain found in the the proteins TACC 1, 2 and 3 (TACC1-3). TACC1 is found concentrated in the centrosomes of eukaryotes which may play a conserved role in organizing centrosomal microtubules. The human TACC proteins have been linked to cancer and TACC2 has been identified as a possible tumour suppressor (AZU-1). TACC 3 from Xenopus laevis, also known as maskin, associates XMAP215 and promotes efficient microtubule elongation during mitosis. Maskin is also found to bind CPEB and elF-4E. Interestingly, the functional homolog (Alp7) in Schizosaccharomyces pombe (not included in this entry) has been shown to be required for organization of bipolar spindles.


Pssm-ID: 461517 [Multi-domain]  Cd Length: 201  Bit Score: 47.36  E-value: 2.79e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159648420  627 NYQADLANITCEIAIKQKLIDEL----ENSQRRLQTLKR---QYEE--KLMM---------LQHKIRDTQLERDQVLQNL 688
Cdd:pfam05010    5 DMDAALEKARNEIEEKELEINELkakyEELRRENLEMRKivaEFEKtiAQMIeekqkqkelEHAEIQKVLEEKDQALADL 84

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159648420  689 GSVET-YSE-----EKAKKIKSEYEKKLQTMNKELQR-LQTAQKEHARL--LKNQSqyEKQLKKLQQEVTEMKKtkvrlm 759
Cdd:pfam05010   85 NSVEKsFSDlfkryEKQKEVISGYKKNEESLKKCAQDyLARIKKEEQRYqaLKAHA--EEKLDQANEEIAQVRS------ 156

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*....
gi 1159648420  760 kqmKEEQEKARMTesrrnreiAQLKKEQRKREHQLKLLEAQ-KRNQEVI 807
Cdd:pfam05010  157 ---KAKAETAALQ--------ASLRKEQMKVQSLERQLEQKtKENEELT 194
Spc7 smart00787
Spc7 kinetochore protein; This domain is found in cell division proteins which are required ...
 690-842 3.05e-05

Spc7 kinetochore protein; This domain is found in cell division proteins which are required for kinetochore-spindle association.


Pssm-ID: 197874 [Multi-domain]  Cd Length: 312  Bit Score: 48.48  E-value: 3.05e-05
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159648420   690 SVETYSEEKAKK------------IKSEYEKKLQTMNKELQRL----QTAQKEHARLLKNQSQYEKQLKKLQQEVTEMKK 753
Cdd:smart00787  121 LVKTFARLEAKKmwyewrmkllegLKEGLDENLEGLKEDYKLLmkelELLNSIKPKLRDRKDALEEELRQLKQLEDELED 200

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159648420   754 TKVRLMKQMKEEQEKARMTESRRNREIAQLkkEQRKREHQLKLleAQKRNQEVILRRKTEEVTALRRQVRPLSDKVAGKV 833
Cdd:smart00787  201 CDPTELDRAKEKLKKLLQEIMIKVKKLEEL--EEELQELESKI--EDLTNKKSELNTEIAEAEKKLEQCRGFTFKEIEKL 276


                    ....*....
gi 1159648420   834 SRKLSLPEH 842
Cdd:smart00787  277 KEQLKLLQS 285
WD40 smart00320
WD40 repeats; Note that these repeats are permuted with respect to the structural repeats ...
 1592-1629 3.43e-05

WD40 repeats; Note that these repeats are permuted with respect to the structural repeats (blades) of the beta propeller domain.


Pssm-ID: 197651 [Multi-domain]  Cd Length: 40  Bit Score: 43.07  E-value: 3.43e-05
                            10        20        30        40
                    ....*....|....*....|....*....|....*....|
gi 1159648420  1592 TFAPIGEMKGHDSPINAIC--TNSSQIFTAADDRTVRIWK 1629
Cdd:smart00320    1 SGELLKTLKGHTGPVTSVAfsPDGKYLASGSDDGTIKLWD 40
TPH pfam13868
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ...
 661-814 3.47e-05

Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of eukaryotic proteins. Trichoplein or mitostatin, was first defined as a meiosis-specific nuclear structural protein. It has since been linked with mitochondrial movement. It is associated with the mitochondrial outer membrane, and over-expression leads to reduction in mitochondrial motility whereas lack of it enhances mitochondrial movement. The activity appears to be mediated through binding the mitochondria to the actin intermediate filaments (IFs). The family is in the trichohyalin-plectin-homology domain.


Pssm-ID: 464007 [Multi-domain]  Cd Length: 341  Bit Score: 48.38  E-value: 3.47e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159648420  661 RQYEEKLMMLQ-HKIRDTQLERdqvlqnlgsvetysEEKAKKIKSEYEKKLQTMnkelqrlqtAQKEHARLLKnqsQYEK 739
Cdd:pfam13868    9 RELNSKLLAAKcNKERDAQIAE--------------KKRIKAEEKEEERRLDEM---------MEEERERALE---EEEE 62

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159648420  740 QLKKLQQEVTEMKKTkvrLMKQMKE------EQEKARMTESRRNREIAQ------LKKEQRKREHQLKLLEAQKRNQEVI 807
Cdd:pfam13868   63 KEEERKEERKRYRQE---LEEQIEEreqkrqEEYEEKLQEREQMDEIVEriqeedQAEAEEKLEKQRQLREEIDEFNEEQ 139


                   ....*..
gi 1159648420  808 LRRKTEE 814
Cdd:pfam13868  140 AEWKELE 146
flagell_FliJ TIGR02473
flagellar export protein FliJ; Members of this family are the FliJ protein found, in nearly ...
 688-810 3.57e-05

flagellar export protein FliJ; Members of this family are the FliJ protein found, in nearly every case, in the midst of other flagellar biosynthesis genes in bacgterial genomes. Typically the fliJ gene is found adjacent to the gene for the flagellum-specific ATPase FliI. Sequence scoring in the gray zone between trusted and noise cutoffs include both probable FliJ proteins and components of bacterial type III secretion systems.


Pssm-ID: 131526 [Multi-domain]  Cd Length: 141  Bit Score: 45.77  E-value: 3.57e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159648420  688 LGSVETYSEEKAKKIKSEYEKKLQTMNKELQRLQ--TAQKEHARLLKN-----------QSQYEKQLKKLQQEVTEMKKT 754
Cdd:TIGR02473    4 LQKLLDLREKEEEQAKLELAKAQAEFERLETQLQqlIKYREEYEQQALekvgagtsaleLSNYQRFIRQLDQRIQQQQQE 83

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 1159648420  755 KVRLMKQMkeEQEKARMTESRRNREIAQLKKEQRKREHQL-KLLEAQKRNQEVILRR 810
Cdd:TIGR02473   84 LALLQQEV--EAKRERLLEARRELKALEKLKEKKQKEYRAeEAKREQKEMDELATQR 138
iSH2_PI3K_IA_R cd12923
Inter-Src homology 2 (iSH2) helical domain of Class IA Phosphoinositide 3-kinase Regulatory ...
 696-810 4.65e-05

Inter-Src homology 2 (iSH2) helical domain of Class IA Phosphoinositide 3-kinase Regulatory subunits; PI3Ks catalyze the transfer of the gamma-phosphoryl group from ATP to the 3-hydroxyl of the inositol ring of D-myo-phosphatidylinositol (PtdIns) or its derivatives. They play an important role in a variety of fundamental cellular processes, including cell motility, the Ras pathway, vesicle trafficking and secretion, immune cell activation, and apoptosis. They are classified according to their substrate specificity, regulation, and domain structure. Class IA PI3Ks are heterodimers of a p110 catalytic (C) subunit and a p85-related regulatory (R) subunit. The R subunit down-regulates PI3K basal activity, stabilizes the C subunit, and plays a role in the activation downstream of tyrosine kinases. All R subunits contain two SH2 domains that flank an intervening helical domain (iSH2), which binds to the N-terminal adaptor-binding domain (ABD) of the catalytic subunit. In vertebrates, there are three genes (PIK3R1, PIK3R2, and PIK3R3) that encode for different Class IA PI3K R subunits.


Pssm-ID: 214016 [Multi-domain]  Cd Length: 152  Bit Score: 45.68  E-value: 4.65e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159648420  696 EEKAKKIKsEYEKKLQTMNKELQRLQ--------------TAQ----------KEHARLL-----KNQSQYEKQL----K 742
Cdd:cd12923      4 EKLAKKLK-EINKEYLDKSREYDELYekynklsqeiqlkrQALeafeeavkmfEEQLRTQekfqkEAQPHEKQRLmennE 82

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1159648420  743 KLQQEVTEMKKTKVRLMKQMKEEQEKARMTESRRN---REIAQLKKEqrkREHQLKLLEAQKRNQEVILRR 810
Cdd:cd12923     83 LLKSRLKELEESKEQLEEDLRKQVAYNRELEREMNslkPELMQLRKQ---KDQYLRWLKRKGVSQEEINQL 150
Uso1_p115_C pfam04871
Uso1 / p115 like vesicle tethering protein, C terminal region; Also known as General vesicular ...
 697-791 4.94e-05

Uso1 / p115 like vesicle tethering protein, C terminal region; Also known as General vesicular transport factor, Transcytosis associate protein (TAP) and Vesicle docking protein, this myosin-shaped molecule consists of an N-terminal globular head region, a coiled-coil tail which mediates dimerization, and a short C-terminal acidic region. p115 tethers COP1 vesicles to the Golgi by binding the coiled coil proteins giantin (on the vesicles) and GM130 (on the Golgi), via its C-terminal acidic region. It is required for intercisternal transport in the golgi stack. This family consists of the acidic C-terminus, which binds to the golgins giantin and GM130. p115 is thought to juxtapose two membranes by binding giantin with one acidic region, and GM130 with another.


Pssm-ID: 461461 [Multi-domain]  Cd Length: 121  Bit Score: 45.08  E-value: 4.94e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159648420  697 EKAKKIKSE---YEKKLQTMNKELQRLQTAQKEHARLLKNQSQYEKQLKKLQQEVTEMKKtkvrlmkQMKEEQEKARMTE 773
Cdd:pfam04871    1 AKKSELESEassLKNENTELKAELQELSKQYNSLEQKESQAKELEAEVKKLEEALKKLKA-------ELSEEKQKEKEKQ 73

                           90
                   ....*....|....*...
gi 1159648420  774 SRRNREIAQLKKEQRKRE 791
Cdd:pfam04871   74 SELDDLLLLLGDLEEKVE 91
GBP_C pfam02841
Guanylate-binding protein, C-terminal domain; Transcription of the anti-viral ...
 682-825 5.15e-05

Guanylate-binding protein, C-terminal domain; Transcription of the anti-viral guanylate-binding protein (GBP) is induced by interferon-gamma during macrophage induction. This family contains GBP1 and GPB2, both GTPases capable of binding GTP, GDP and GMP.


Pssm-ID: 460721 [Multi-domain]  Cd Length: 297  Bit Score: 47.67  E-value: 5.15e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159648420  682 DQVLQN-LGSVETYSE----------EKAKKIKSEYEKKlQTMNKELQRLQTAQKEHARLLKNQ-SQYEKQLKKLQQEvt 749
Cdd:pfam02841  175 EEVLQEfLQSKEAVEEailqtdqaltAKEKAIEAERAKA-EAAEAEQELLREKQKEEEQMMEAQeRSYQEHVKQLIEK-- 251

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1159648420  750 eMKKTKvrlmKQMKEEQEkaRMTESRRNREIAQLKKEQRkrehqlklleaqkrnqevilrrktEEVTALRRQVRPL 825
Cdd:pfam02841  252 -MEAER----EQLLAEQE--RMLEHKLQEQEELLKEGFK------------------------TEAESLQKEIQDL 296
PTZ00121 PTZ00121
MAEBL; Provisional
 638-815 5.96e-05

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 48.98  E-value: 5.96e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159648420  638 EIAIKQKLIDELENSQRRLQTLKRQYEEKLMMLQHKIRDTQLERDQVLQNLGSVEtySEEKAKKIKSEYEKKlqtmnKEL 717
Cdd:PTZ00121  1221 EDAKKAEAVKKAEEAKKDAEEAKKAEEERNNEEIRKFEEARMAHFARRQAAIKAE--EARKADELKKAEEKK-----KAD 1293

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159648420  718 QRLQTAQKEHARLLKNQSQYEKQLKKLQQEVTEMKKTKVRLMKQMKEEQEKARMTESRRNREIAQLKKEQRKRE-HQLKL 796
Cdd:PTZ00121  1294 EAKKAEEKKKADEAKKKAEEAKKADEAKKKAEEAKKKADAAKKKAEEAKKAAEAAKAEAEAAADEAEAAEEKAEaAEKKK 1373

                          170
                   ....*....|....*....
gi 1159648420  797 LEAQKRNQEviLRRKTEEV 815
Cdd:PTZ00121  1374 EEAKKKADA--AKKKAEEK 1390
FliJ pfam02050
Flagellar FliJ protein;
647-782 6.11e-05

Flagellar FliJ protein;


Pssm-ID: 426581 [Multi-domain]  Cd Length: 123  Bit Score: 44.58  E-value: 6.11e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159648420  647 DELENSQRRLQTLKRQYEEKLMMLQHKIRDTQLERDQVLQNLGSvetyseekakkikSEYEKKLQTMNKELQRLQTAQKE 726
Cdd:pfam02050    1 DEAARELAEAQRELQQAEEKLEELQQYRAEYQQQLSGAGQGISA-------------AELRNYQAFISQLDEAIAQQQQE 67

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 1159648420  727 HARLLKNQSQYEKQLKKLQQEVTEMKKTKVRlmkQMKEEQEKARMTESRRNREIAQ 782
Cdd:pfam02050   68 LAQAEAQVEKAREEWQEARQERKSLEKLRER---EKKEERKEQNRREQKQLDELAA 120
GumC COG3206
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
643-955 6.66e-05

Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 442439 [Multi-domain]  Cd Length: 687  Bit Score: 48.47  E-value: 6.66e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159648420  643 QKLIDELENSQRRLQTlKRQYEEKLMMLQHKIRDTQLERDQVLQnLgSVETYSEEKAKKIKSEYEKKLQTMNKELQRLQT 722
Cdd:COG3206     97 ERVVDKLNLDEDPLGE-EASREAAIERLRKNLTVEPVKGSNVIE-I-SYTSPDPELAAAVANALAEAYLEQNLELRREEA 173

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159648420  723 AQKehARLLKNQ-SQYEKQLKKLQQEVTEMKKTKVRLMKQMKEEQEKARMTESrrNREIAQLKKEQRKREHQLKLLEAQK 801
Cdd:COG3206    174 RKA--LEFLEEQlPELRKELEEAEAALEEFRQKNGLVDLSEEAKLLLQQLSEL--ESQLAEARAELAEAEARLAALRAQL 249

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159648420  802 RNQEVILRRKTE--EVTALRRQVRPLSDKVAGKVSRklSLPEHPiqepsssssvehdgSRIAAQQKMRIPVARVQALSVT 879
Cdd:COG3206    250 GSGPDALPELLQspVIQQLRAQLAELEAELAELSAR--YTPNHP--------------DVIALRAQIAALRAQLQQEAQR 313

                          250       260       270       280       290       300       310
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1159648420  880 ATNGTGRKYQrkavtsrvyssrAARMKWQLLERRVTDIIMQRMTISNMEADMNRLLTQREELTKRREKLSKRREKL 955
Cdd:COG3206    314 ILASLEAELE------------ALQAREASLQAQLAQLEARLAELPELEAELRRLEREVEVARELYESLLQRLEEA 377
CAF-1_p150 pfam11600
Chromatin assembly factor 1 complex p150 subunit, N-terminal; CAF-1_p150 is a polypeptide ...
 723-843 6.70e-05

Chromatin assembly factor 1 complex p150 subunit, N-terminal; CAF-1_p150 is a polypeptide subunit of CAF-1, which functions in depositing newly synthesized and acetylated histones H3/H4 into chromatin during DNA replication and repair. CAF-1_p150 includes the HP1 interaction site, the PEST, KER and ED interacting sites. CAF-1_p150 interacts directly with newly synthesized and acetylated histones through the acidic KER and ED domains. The PEST domain is associated with proteins that undergo rapid proteolysis.


Pssm-ID: 402959 [Multi-domain]  Cd Length: 164  Bit Score: 45.83  E-value: 6.70e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159648420  723 AQKEHARLLKNQSQYEKQlKKLQQEvtemKKTKVRLMKQMKEEQEKARmTESRRNREIAQLKKEQRKRE----------H 792
Cdd:pfam11600   11 EEKEKQRLEKDKERLRRQ-LKLEAE----KEEKERLKEEAKAEKERAK-EEARRKKEEEKELKEKERREkkekdekekaE 84

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 1159648420  793 QLKLLEAQKRNQEVIL------RRKTEEVTALRRQVRPLSDKVAGkVSRKLSLPEHP 843
Cdd:pfam11600   85 KLRLKEEKRKEKQEALeakleeKRKKEEEKRLKEEEKRIKAEKAE-ITRFLQKPKTQ 140
BBP1_C pfam15272
Spindle pole body component BBP1, C-terminal; This C-terminal domain of BBP1, a spindle pole ...
 643-805 7.70e-05

Spindle pole body component BBP1, C-terminal; This C-terminal domain of BBP1, a spindle pole body component, carries coiled-coils that are necessary for the localization of BBP1 to the spindle pole body (SPB). Although not a membrane protein itself, BBP1 binds to Mps2 as well as to Spc29 and the half-bridge protein Kar1, thus providing a model for how the SPB core is tethered within the nuclear envelope and to the half-bridge


Pssm-ID: 405864 [Multi-domain]  Cd Length: 183  Bit Score: 45.85  E-value: 7.70e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159648420  643 QKLIDELENSQRRLQTLKRQYEEKlmmlqhkirdtqlerdqvlqnlgsvetysEEKAKKIKSEYEKK-LQTMNKELQRLQ 721
Cdd:pfam15272    7 LELLDKLDKNNRALHLLNKDVRER-----------------------------DEHYQLQETSYKKKyLQTRNELINELK 57

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159648420  722 TAQKEHARLLKNQSQYeKQLKKLQQEVTEMKKTKVRLMKQ-----MKEEQEKARMTESR-----RNREI-AQLKKEQRKR 790
Cdd:pfam15272   58 QSKKLYDNYYKLYSKY-QQLKKISNESLDLQSTITNLESQlvdqaIDKDREIHNLNEKIlslelRNQELeTKREIDKMKY 136

                          170
                   ....*....|....*
gi 1159648420  791 EHQLKLLEAQKRNQE 805
Cdd:pfam15272  137 ESRIDELERQLKEQE 151
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
638-823 8.06e-05

Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 48.37  E-value: 8.06e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159648420  638 EIAIKQKLIDELENSQRRLQTLKRQYEE----------KLMMLQHKIRDTQLERDQVLQNLGSVETYSEEKAKKIKSEYE 707
Cdd:COG4913    669 EIAELEAELERLDASSDDLAALEEQLEEleaeleeleeELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLELR 748

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159648420  708 KKLQTMNKELQRLQTAQKEHARLLKNQSQYEKQLKKLQQEVtemkktkVRLMKQMKEEQEKAR---MTESRRNREIAQLK 784
Cdd:COG4913    749 ALLEERFAAALGDAVERELRENLEERIDALRARLNRAEEEL-------ERAMRAFNREWPAETadlDADLESLPEYLALL 821

                          170       180       190
                   ....*....|....*....|....*....|....*....
gi 1159648420  785 KEQRKREhqlkLLEAQKRNQEVILRRKTEEVTALRRQVR 823
Cdd:COG4913    822 DRLEEDG----LPEYEERFKELLNENSIEFVADLLSKLR 856
DUF5401 pfam17380
Family of unknown function (DUF5401); This is a family of unknown function found in ...
 647-794 8.92e-05

Family of unknown function (DUF5401); This is a family of unknown function found in Chromadorea.


Pssm-ID: 375164 [Multi-domain]  Cd Length: 722  Bit Score: 47.81  E-value: 8.92e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159648420  647 DELENsQRRLQTLKRQYEEKLmmlQHKIRDTQLERDQVL---QNLGSVETYSEEKAKKIKSEyEKKLQTMNKELQRLQTA 723
Cdd:pfam17380  454 EEQER-QQQVERLRQQEEERK---RKKLELEKEKRDRKRaeeQRRKILEKELEERKQAMIEE-ERKRKLLEKEMEERQKA 528

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1159648420  724 QKEHARLLKNQSQYEKqlkklQQEVTEMKktkvRLMKQM-KEEQEKARMTESRRNREIAQLKKEQRKREHQL 794
Cdd:pfam17380  529 IYEEERRREAEEERRK-----QQEMEERR----RIQEQMrKATEERSRLEAMEREREMMRQIVESEKARAEY 591
sbcc TIGR00618
exonuclease SbcC; All proteins in this family for which functions are known are part of an ...
 649-1177 9.13e-05

exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]


Pssm-ID: 129705 [Multi-domain]  Cd Length: 1042  Bit Score: 48.04  E-value: 9.13e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159648420  649 LENSQRRLQTLK-----RQYEEKLMMLQHKIRDTQLERDQVLQNLGSVETYSEEKAKkiksEYEKKLQTMNKELQRLQTA 723
Cdd:TIGR00618  159 KAKSKEKKELLMnlfplDQYTQLALMEFAKKKSLHGKAELLTLRSQLLTLCTPCMPD----TYHERKQVLEKELKHLREA 234

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159648420  724 QKE----HARLLKNQSQYEKQLKK---LQQEVTEMKKTKVRLmKQMKEEQEK--------------ARMTESRRNREI-- 780
Cdd:TIGR00618  235 LQQtqqsHAYLTQKREAQEEQLKKqqlLKQLRARIEELRAQE-AVLEETQERinrarkaaplaahiKAVTQIEQQAQRih 313

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159648420  781 AQLKKEQRKRE----------------HQLKLLEAQKRNQEVILRRKTEEVTALRRQvrplSDKVAGKVSRKLSLP---E 841
Cdd:TIGR00618  314 TELQSKMRSRAkllmkraahvkqqssiEEQRRLLQTLHSQEIHIRDAHEVATSIREI----SCQQHTLTQHIHTLQqqkT 389

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159648420  842 HPIQEPSSSSSVEHDGSRIAAQQKMRIPVARVQALSVTATNGTGRKYQRKAVTSRVYSSRAA-----------RMKWQLL 910
Cdd:TIGR00618  390 TLTQKLQSLCKELDILQREQATIDTRTSAFRDLQGQLAHAKKQQELQQRYAELCAAAITCTAqceklekihlqESAQSLK 469

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159648420  911 ERrvTDIIMQRMTISNMEADMNRLLTQREELTKRREKLSKRR------EKLMKDGGGSETDRNVQNINE--EMESLTANI 982
Cdd:TIGR00618  470 ER--EQQLQTKEQIHLQETRKKAVVLARLLELQEEPCPLCGScihpnpARQDIDNPGPLTRRMQRGEQTyaQLETSEEDV 547

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159648420  983 DYINDSISDcQANIMQMEEAKEEGETLDVTAVINA--CTLTEARYLLDHfltmgINKGLQAAQKEAQIKVLEGRLKQTEI 1060
Cdd:TIGR00618  548 YHQLTSERK-QRASLKEQMQEIQQSFSILTQCDNRskEDIPNLQNITVR-----LQDLTEKLSEAEDMLACEQHALLRKL 621

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159648420 1061 TSATQNQLLFHMLKEKA-ELNPELDALlgHALQDNLedsTDEDAPLHSPGTEGSSLSSDLLKLCGEVKPKSKARRRTTTQ 1139
Cdd:TIGR00618  622 QPEQDLQDVRLHLQQCSqELALKLTAL--HALQLTL---TQERVREHALSIRVLPKELLASRQLALQKMQSEKEQLTYWK 696

                          570       580       590       600       610
                   ....*....|....*....|....*....|....*....|....*....|....
gi 1159648420 1140 MELLYADS------------SDLVSEI----SAADSTLAGPLASVAETQASGMA 1177
Cdd:TIGR00618  697 EMLAQCQTllrelethieeyDREFNEIenasSSLGSDLAAREDALNQSLKELMH 750
COG1340 COG1340
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
713-825 1.05e-04

Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];


Pssm-ID: 440951 [Multi-domain]  Cd Length: 297  Bit Score: 46.83  E-value: 1.05e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159648420  713 MNKELQRLQtaqKEHARLLKNQSQYEKQLKKLQQEVTEMKKTKVRLMKQMKEEQEKARMTESRR---NREIAQLKKEQRK 789
Cdd:COG1340      6 LSSSLEELE---EKIEELREEIEELKEKRDELNEELKELAEKRDELNAQVKELREEAQELREKRdelNEKVKELKEERDE 82

                           90       100       110
                   ....*....|....*....|....*....|....*....
gi 1159648420  790 REHQLKLLEAQ---KRNQEVILRRKTEEVTALRRQVRPL 825
Cdd:COG1340     83 LNEKLNELREEldeLRKELAELNKAGGSIDKLRKEIERL 121
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 362-1057 1.08e-04

Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 47.62  E-value: 1.08e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159648420  362 LKYANRARNIKNKVMVNQDR-ASQQINALRSEIARLQMELMEYKTGKRIIDEEGVEsindmfhenamLQTENNNLRVRIK 440
Cdd:COG1196    216 RELKEELKELEAELLLLKLReLEAELEELEAELEELEAELEELEAELAELEAELEE-----------LRLELEELELELE 284

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159648420  441 AMQETVDALRARITQLMSDQANQVLARAGEGNEEISNmihnyIKEIEDLRAKLLESEAVNENLRRNLSRASTRStyfggp 520
Cdd:COG1196    285 EAQAEEYELLAELARLEQDIARLEERRRELEERLEEL-----EEELAELEEELEELEEELEELEEELEEAEEEL------ 353

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159648420  521 safsASMLSSEKETLEILDiakkdleklkkkerkkkksvkedntdNEQEKRDEKGSSERENNELEAEEIQEAsdredeee 600
Cdd:COG1196    354 ----EEAEAELAEAEEALL--------------------------EAEAELAEAEEELEELAEELLEALRAA-------- 395

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159648420  601 eddededdmevvessdesdsdsdekENYQADLANITCEIAIKQKLIDELENSQRRLQTLKRQYEEKLMMLQHKIRDTQLE 680
Cdd:COG1196    396 -------------------------AELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEE 450

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159648420  681 RDQvlqnlgsvetyseekakkikseyekklqtmnkELQRLQTAQKEHARLLKNQSQYEKQLKKLQQEVTEmKKTKVRLMK 760
Cdd:COG1196    451 EAE--------------------------------LEEEEEALLELLAELLEEAALLEAALAELLEELAE-AAARLLLLL 497

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159648420  761 QMKEEQE-----KARMTESRRNREIAQLKKEQRKREHQLKLLEAQkRNQEVILRRKTEEVTALRRQVRPLSDKVAGKVSR 835
Cdd:COG1196    498 EAEADYEgflegVKAALLLAGLRGLAGAVAVLIGVEAAYEAALEA-ALAAALQNIVVEDDEVAAAAIEYLKAAKAGRATF 576

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159648420  836 klsLPEHPIQEPSSSSSVEHDGSRIAAqqkmripVARVQALSVTAtngtGRKYQRKAVTSRVYSSRAARMkWQLLERRVT 915
Cdd:COG1196    577 ---LPLDKIRARAALAAALARGAIGAA-------VDLVASDLREA----DARYYVLGDTLLGRTLVAARL-EAALRRAVT 641

                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159648420  916 DIIMQRMTISNMEADMNRLLTQREELTKRREKLSKRREKLMKdgggsETDRNVQNINEEMESLTANIDYINDSISDCQAN 995
Cdd:COG1196    642 LAGRLREVTLEGEGGSAGGSLTGGSRRELLAALLEAEAELEE-----LAERLAEEELELEEALLAEEEEERELAEAEEER 716

                          650       660       670       680       690       700
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1159648420  996 IMQMEEAKEEGETLDVTAVINACTLTEARYLLDHFLTMGINKGLQAAQKEAQIKVLEGRLKQ 1057
Cdd:COG1196    717 LEEELEEEALEEQLEAEREELLEELLEEEELLEEEALEELPEPPDLEELERELERLEREIEA 778
mS26_PET12 cd23703
Saccharomyces cerevisiae mitochondrial small ribosomal subunit protein mS26 and similar ...
 695-796 1.28e-04

Saccharomyces cerevisiae mitochondrial small ribosomal subunit protein mS26 and similar proteins; mS26, also known as mitochondrial 37S ribosomal protein PET12, is a component of the mitochondrial small ribosomal subunit (mt-SSU) of Saccharomyces cerevisiae mitochondrial ribosome (mitoribosome), a dedicated translation machinery responsible for the synthesis of mitochondrial genome-encoded proteins, including at least some of the essential transmembrane subunits of the mitochondrial respiratory chain. The mitoribosomes are attached to the mitochondrial inner membrane and translation products are cotranslationally integrated into the membrane. The family also includes a group of uncharacterized proteins from pezizomycotina, which show high sequence similarity with mS26.


Pssm-ID: 467916 [Multi-domain]  Cd Length: 179  Bit Score: 45.24  E-value: 1.28e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159648420  695 SEEKAKKIKSEYEKKLQTMNkELQR--LQTA-QKEHARLLKNQSQYEKQLKKLQQE----VTEMKKTKVRL--------- 758
Cdd:cd23703     37 KEPKPKSPLSEYQEWKRKMA-ELRRqnLREGlRELEERKLKTEELRAKRSERKQAEreraLNAPEREDERLtlptiesal 115

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|..
gi 1159648420  759 ----MKQMKEEQEKARMTESRRNREIAQLKKEQRKREHQLKL 796
Cdd:cd23703    116 lgplMRVRTDPEREERAAKRRANREAKELAKKEARADALHEL 157
Cast pfam10174
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ...
 364-807 1.28e-04

RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part of the CAZ (cytomatrix at the active zone) complex which is involved in determining the site of synaptic vesicle fusion. The C-terminus is a PDZ-binding motif that binds directly to RIM (a small G protein Rab-3A effector). The family also contains four coiled-coil domains.


Pssm-ID: 431111 [Multi-domain]  Cd Length: 766  Bit Score: 47.51  E-value: 1.28e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159648420  364 YANRARNIKNKVmvnqDRASQQINALRSEIARLQMEL----MEYKTGKRIIDeegV--ESINDMFHENAMLQTENNNLRV 437
Cdd:pfam10174  280 YKSHSKFMKNKI----DQLKQELSKKESELLALQTKLetltNQNSDCKQHIE---VlkESLTAKEQRAAILQTEVDALRL 352

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159648420  438 RIKAMQETVDALRARITQLMSDQANQvlaragegNEEISNM----------IHNYIKEIEDLRAKLLESEAVNENLRRNL 507
Cdd:pfam10174  353 RLEEKESFLNKKTKQLQDLTEEKSTL--------AGEIRDLkdmldvkerkINVLQKKIENLQEQLRDKDKQLAGLKERV 424

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159648420  508 SRASTRSTYFGGPSAFSASMLSSEKETLEILdiakkdleklkkkerkkkksvKEDNTDNEQEKRDEKGSSERENNELEae 587
Cdd:pfam10174  425 KSLQTDSSNTDTALTTLEEALSEKERIIERL---------------------KEQREREDRERLEELESLKKENKDLK-- 481

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159648420  588 eiQEASDREDEEEEDDEDEDDMEVVESSDESDSDSdeKENYQADLanitcEIAIKQKlIDELEnsqrRLQTlkrqyeekl 667
Cdd:pfam10174  482 --EKVSALQPELTEKESSLIDLKEHASSLASSGLK--KDSKLKSL-----EIAVEQK-KEECS----KLEN--------- 538

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159648420  668 mmlQHKirdtqlerdqvlqnlgsvETYSEEKAKKIKSEYEKKLQTMNKELQRLQ----TAQKEHARLLK--NQSQYEKQL 741
Cdd:pfam10174  539 ---QLK------------------KAHNAEEAVRTNPEINDRIRLLEQEVARYKeesgKAQAEVERLLGilREVENEKND 597

                          410       420       430       440       450       460
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1159648420  742 KklQQEVTEMKKTKVRLMKQMKEEQEKARMTESRRNREIAQLKKEQRKREHQLKLLEAQKRNQEVI 807
Cdd:pfam10174  598 K--DKKIAELESLTLRQMKEQNKKVANIKHGQQEMKKKGAQLLEEARRREDNLADNSQQLQLEELM 661
OmpH smart00935
Outer membrane protein (OmpH-like); This family includes outer membrane proteins such as OmpH ...
 713-830 1.35e-04

Outer membrane protein (OmpH-like); This family includes outer membrane proteins such as OmpH among others. Skp (OmpH) has been characterized as a molecular chaperone that interacts with unfolded proteins as they emerge in the periplasm from the Sec translocation machinery.


Pssm-ID: 214922 [Multi-domain]  Cd Length: 140  Bit Score: 44.11  E-value: 1.35e-04
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159648420   713 MNKELQRLQTAQKEHARLLKNQSQYEKQLKKLQQEVTEMKKtkvrlmkqmKEEQEKARMTESRRNREIAQLkkEQRKREH 792
Cdd:smart00935    6 VQKILQESPAGKAAQKQLEKEFKKRQAELEKLEKELQKLKE---------KLQKDAATLSEAAREKKEKEL--QKKVQEF 74

                            90       100       110
                    ....*....|....*....|....*....|....*...
gi 1159648420   793 QLKLLEAQKRNQevilRRKTEEVTALRRQVRPLSDKVA 830
Cdd:smart00935   75 QRKQQKLQQDLQ----KRQQEELQKILDKINKAIKEVA 108
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 761-1079 1.35e-04

chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]


Pssm-ID: 274009 [Multi-domain]  Cd Length: 1164  Bit Score: 47.37  E-value: 1.35e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159648420  761 QMKEEQEKAR--MTESRRNREIA---------QLKKEQRKREHQLKLLEAQKRNQEVILRRKTEEVTALRRQVRplsdkv 829
Cdd:TIGR02169  167 EFDRKKEKALeeLEEVEENIERLdliidekrqQLERLRREREKAERYQALLKEKREYEGYELLKEKEALERQKE------ 240

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159648420  830 agKVSRKLSLPEHPIQEpsSSSSVEHDGSRIAA-QQKMRIPVARVQALsvtatnGTGRKYQRKAVTSRVYSSRA-ARMKW 907
Cdd:TIGR02169  241 --AIERQLASLEEELEK--LTEEISELEKRLEEiEQLLEELNKKIKDL------GEEEQLRVKEKIGELEAEIAsLERSI 310

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159648420  908 QLLERRVTDiiMQRmTISNMEADMNRLLTQREELTKRREKLSKRREKLMKDgggsetdrnVQNINEEMESLTANIDYIND 987
Cdd:TIGR02169  311 AEKERELED--AEE-RLAKLEAEIDKLLAEIEELEREIEEERKRRDKLTEE---------YAELKEELEDLRAELEEVDK 378

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159648420  988 SISDCQANIMQMEEAKEegetlDVTAVINactltEARYLLDHFLTMGINKGLQAAQKEAQIKVLEGRL---------KQT 1058
Cdd:TIGR02169  379 EFAETRDELKDYREKLE-----KLKREIN-----ELKRELDRLQEELQRLSEELADLNAAIAGIEAKIneleeekedKAL 448

                          330       340
                   ....*....|....*....|...
gi 1159648420 1059 EITSATQN--QLLFHMLKEKAEL 1079
Cdd:TIGR02169  449 EIKKQEWKleQLAADLSKYEQEL 471
TPR_MLP1_2 pfam07926
TPR/MLP1/MLP2-like protein; The sequences featured in this family are similar to a region of ...
 697-797 1.49e-04

TPR/MLP1/MLP2-like protein; The sequences featured in this family are similar to a region of human TPR protein and to yeast myosin-like proteins 1 (MLP1) and 2 (MLP2). These proteins share a number of features; for example, they all have coiled-coil regions and all three are associated with nuclear pores. TPR is thought to be a component of nuclear pore complex- attached intra-nuclear filaments, and is implicated in nuclear protein import. Moreover, its N-terminal region is involved in the activation of oncogenic kinases, possibly by mediating the dimerization of kinase domains or by targeting these kinases to the nuclear pore complex. MLP1 and MLP2 are involved in the process of telomere length regulation, where they are thought to interact with proteins such as Tel1p and modulate their activity.


Pssm-ID: 462316 [Multi-domain]  Cd Length: 129  Bit Score: 43.78  E-value: 1.49e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159648420  697 EKAKKIKSEYEKKLQTMNKELQ----RLQTAQK-------EHARLLKNQSQYEKQLKKLQQEVTEMKKTKVRLMKQMKEE 765
Cdd:pfam07926   11 KRLKEEAADAEAQLQKLQEDLEkqaeIAREAQQnyerelvLHAEDIKALQALREELNELKAEIAELKAEAESAKAELEES 90

                           90       100       110
                   ....*....|....*....|....*....|....*
gi 1159648420  766 QEKARMTESRRNREIAQLKkeqRKRE---HQLKLL 797
Cdd:pfam07926   91 EESWEEQKKELEKELSELE---KRIEdlnEQNKLL 122
Myosin_tail_1 pfam01576
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ...
 645-821 1.62e-04

Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.


Pssm-ID: 460256 [Multi-domain]  Cd Length: 1081  Bit Score: 47.09  E-value: 1.62e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159648420  645 LIDELENSQRRLQTL---KRQYEEKLMMLQHKIR-------DTQLER---DQVLQNLGSVETYSEekakKIKSEYEKKLQ 711
Cdd:pfam01576  361 LTEQLEQAKRNKANLekaKQALESENAELQAELRtlqqakqDSEHKRkklEGQLQELQARLSESE----RQRAELAEKLS 436

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159648420  712 TMNKELQRLQT----AQKEHARLLKNQSQYEKQLKKLQ---QEVTEMK---KTKVR--------LMKQMKEEQEKARMTE 773
Cdd:pfam01576  437 KLQSELESVSSllneAEGKNIKLSKDVSSLESQLQDTQellQEETRQKlnlSTRLRqledernsLQEQLEEEEEAKRNVE 516

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*...
gi 1159648420  774 SRRNREIAQLKKEQRKREHQLKLLEAQKRNQevilRRKTEEVTALRRQ 821
Cdd:pfam01576  517 RQLSTLQAQLSDMKKKLEEDAGTLEALEEGK----KRLQRELEALTQQ 560
HlpA COG2825
Periplasmic chaperone for outer membrane proteins, Skp family [Cell wall/membrane/envelope ...
 713-830 1.65e-04

Periplasmic chaperone for outer membrane proteins, Skp family [Cell wall/membrane/envelope biogenesis, Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 442073 [Multi-domain]  Cd Length: 171  Bit Score: 44.44  E-value: 1.65e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159648420  713 MNKELQRLQTAQKEHARLLKNQSQYEKQLKKLQQEVTEMKKTKVRLMKQMKEEQEKARMtesrrnREIAQLKKE-QRKRe 791
Cdd:COG2825     31 VQRILQESPEGKAAQKKLEKEFKKRQAELQKLEKELQALQEKLQKEAATLSEEERQKKE------RELQKKQQElQRKQ- 103

                           90       100       110
                   ....*....|....*....|....*....|....*....
gi 1159648420  792 hqlklleaQKRNQEvILRRKTEEVTALRRQVRPLSDKVA 830
Cdd:COG2825    104 --------QEAQQD-LQKRQQELLQPILEKIQKAIKEVA 133
HOOK pfam05622
HOOK protein coiled-coil region; This family consists of several HOOK1, 2 and 3 proteins from ...
 365-896 1.67e-04

HOOK protein coiled-coil region; This family consists of several HOOK1, 2 and 3 proteins from different eukaryotic organizms. The different members of the human gene family are HOOK1, HOOK2 and HOOK3. Different domains have been identified in the three human HOOK proteins, and it was demonstrated that the highly conserved NH2-domain mediates attachment to microtubules, whereas this central coiled-coil motif mediates homodimerization and the more divergent C-terminal domains are involved in binding to specific organelles (organelle-binding domains). It has been demonstrated that endogenous HOOK3 binds to Golgi membranes, whereas both HOOK1 and HOOK2 are localized to discrete but unidentified cellular structures. In mice the Hook1 gene is predominantly expressed in the testis. Hook1 function is necessary for the correct positioning of microtubular structures within the haploid germ cell. Disruption of Hook1 function in mice causes abnormal sperm head shape and fragile attachment of the flagellum to the sperm head. This entry includes the central coiled-coiled domain and the divergent C-terminal domain.


Pssm-ID: 461694 [Multi-domain]  Cd Length: 528  Bit Score: 46.99  E-value: 1.67e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159648420  365 ANRARNIKNKVMVNQDrasqQINALRSEIARLQMELMEYK--------TGKRIID-EEGVESINDmfhENAMLQTENNNL 435
Cdd:pfam05622   13 AQRCHELDQQVSLLQE----EKNSLQQENKKLQERLDQLEsgddsgtpGGKKYLLlQKQLEQLQE---ENFRLETARDDY 85

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159648420  436 RVRIKAMQETVDALRARITQLMS--DQANQ------VLARAGEGNEEISNMIHNYIKEIEDLR-----AKLLEsEAVNEN 502
Cdd:pfam05622   86 RIKCEELEKEVLELQHRNEELTSlaEEAQAlkdemdILRESSDKVKKLEATVETYKKKLEDLGdlrrqVKLLE-ERNAEY 164

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159648420  503 LRRNLSRAStrstyfggpSAFSASMLSSEKETL--EILDIakkdleklkkKERKKKKSVKEDNTDNEQEKRDEKGSS--- 577
Cdd:pfam05622  165 MQRTLQLEE---------ELKKANALRGQLETYkrQVQEL----------HGKLSEESKKADKLEFEYKKLEEKLEAlqk 225

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159648420  578 ERE------------NNELEAEEIQEASDREDEEEEDDEDEDDmevvessdesdsdsdekENYQADLAnitcEIAIKQKL 645
Cdd:pfam05622  226 EKErliierdtlretNEELRCAQLQQAELSQADALLSPSSDPG-----------------DNLAAEIM----PAEIREKL 284

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159648420  646 ID-ELENSQRRLQTlKRQYEEKLMMLQHKIRDTQLERDQvlqnlgsVETYSEEKAKKIKSeyekkLQTMNKELQRLQTAQ 724
Cdd:pfam05622  285 IRlQHENKMLRLGQ-EGSYRERLTELQQLLEDANRRKNE-------LETQNRLANQRILE-----LQQQVEELQKALQEQ 351

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159648420  725 KEHArllKNQSQYEKQLKKLQQEVTEMKKTKVRLMKQMKEEQEKARMTESRRnreIAQLKKEQRKREHQLKLLEAQ-KRN 803
Cdd:pfam05622  352 GSKA---EDSSLLKQKLEEHLEKLHEAQSELQKKKEQIEELEPKQDSNLAQK---IDELQEALRKKDEDMKAMEERyKKY 425

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159648420  804 QEvilrrKTEEVtalrrqVRPLSDKVAGKVSRKLSLPEHPIQEPS-SSSSVEHDGSRIAAQQKMRipvarvQALSVTATN 882
Cdd:pfam05622  426 VE-----KAKSV------IKTLDPKQNPASPPEIQALKNQLLEKDkKIEHLERDFEKSKLQREQE------EKLIVTAWY 488

                          570
                   ....*....|....
gi 1159648420  883 GTGRKYQRKAVTSR 896
Cdd:pfam05622  489 NMGMALHRKAIEER 502
DUF4200 pfam13863
Domain of unknown function (DUF4200); This family is found in eukaryotes. It is a coiled-coil ...
 648-764 1.70e-04

Domain of unknown function (DUF4200); This family is found in eukaryotes. It is a coiled-coil domain of unknwon function.


Pssm-ID: 464003 [Multi-domain]  Cd Length: 119  Bit Score: 43.33  E-value: 1.70e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159648420  648 ELENSQRRLQTLKRQYEEKLMMLQHKIRdtQLERdqvlqnlgsvetySEEKAKKIKSEYEKKLQTMNKELQR-LQTAQKE 726
Cdd:pfam13863    7 EMFLVQLALDAKREEIERLEELLKQREE--ELEK-------------KEQELKEDLIKFDKFLKENDAKRRRaLKKAEEE 71

                           90       100       110
                   ....*....|....*....|....*....|....*...
gi 1159648420  727 HarllKNQSQYEKQLKKLQQEVTEMKKTKVRLMKQMKE 764
Cdd:pfam13863   72 T----KLKKEKEKEIKKLTAQIEELKSEISKLEEKLEE 105
Filament pfam00038
Intermediate filament protein;
644-823 1.76e-04

Intermediate filament protein;


Pssm-ID: 459643 [Multi-domain]  Cd Length: 313  Bit Score: 46.07  E-value: 1.76e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159648420  644 KLIDELENSQRRLQTLKRQYEEKLMMLQHKIRDTQLERDQVlqnlgsvetyseEKAKKIKSEYEKKLQTMNKELQRLQTA 723
Cdd:pfam00038   72 RLQLELDNLRLAAEDFRQKYEDELNLRTSAENDLVGLRKDL------------DEATLARVDLEAKIESLKEELAFLKKN 139

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159648420  724 QKEHARLLKNQ--------------------------SQYEKQLKKLQQEVTEMKKTKVR-----------LMKQMKEEQ 766
Cdd:pfam00038  140 HEEEVRELQAQvsdtqvnvemdaarkldltsalaeirAQYEEIAAKNREEAEEWYQSKLEelqqaaarngdALRSAKEEI 219

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 1159648420  767 EKARMTESRRNREIAQLKKEQRKREHQLKLLEAQKRNQEVILRRKTEEVTALRRQVR 823
Cdd:pfam00038  220 TELRRTIQSLEIELQSLKKQKASLERQLAETEERYELQLADYQELISELEAELQETR 276
PRK00409 PRK00409
recombination and DNA strand exchange inhibitor protein; Reviewed
 697-811 1.77e-04

recombination and DNA strand exchange inhibitor protein; Reviewed


Pssm-ID: 234750 [Multi-domain]  Cd Length: 782  Bit Score: 47.13  E-value: 1.77e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159648420  697 EKAKKIKSEYEKKLQTMNKELQRLQTAQKEHAR----LLKnqsQYEKQLKKLQQEVTEMKKTKVRLMKQMKEEQEKArmt 772
Cdd:PRK00409   505 EEAKKLIGEDKEKLNELIASLEELERELEQKAEeaeaLLK---EAEKLKEELEEKKEKLQEEEDKLLEEAEKEAQQA--- 578

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....
gi 1159648420  773 esrrnreIAQLKKE-----QRKREHQLKLLEAQKRnQEVILRRK 811
Cdd:PRK00409   579 -------IKEAKKEadeiiKELRQLQKGGYASVKA-HELIEARK 614
MscS_porin pfam12795
Mechanosensitive ion channel porin domain; The small mechanosensitive channel, MscS, is a part ...
 630-821 1.87e-04

Mechanosensitive ion channel porin domain; The small mechanosensitive channel, MscS, is a part of the turgor-driven solute efflux system that protects bacteria from lysis in the event of osmotic shock. The MscS protein alone is sufficient to form a functional mechanosensitive channel gated directly by tension in the lipid bilayer. The MscS proteins are heptamers of three transmembrane subunits with seven converging M3 domains, and this MscS_porin is towards the N-terminal of the molecules. The high concentration of negative charges at the extracellular entrance of the pore helps select the cations for efflux.


Pssm-ID: 432790 [Multi-domain]  Cd Length: 238  Bit Score: 45.37  E-value: 1.87e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159648420  630 ADLANITCEIAIKQKLIDELENSQRRLQTLKRqYEEKLMMLQHKIRDTQLERDQVLQNLGSVETYSEEKAKKI-----KS 704
Cdd:pfam12795    3 DELEKAKLDEAAKKKLLQDLQQALSLLDKIDA-SKQRAAAYQKALDDAPAELRELRQELAALQAKAEAAPKEIlaslsLE 81

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159648420  705 EYEKKLqtmNKELQRLQTAQKEHARLLKNQSQYEKQLKKLQQEVTEMKK--TKVR-LMKQMKEEQEkaRMTESRRNreia 781
Cdd:pfam12795   82 ELEQRL---LQTSAQLQELQNQLAQLNSQLIELQTRPERAQQQLSEARQrlQQIRnRLNGPAPPGE--PLSEAQRW---- 152

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|..
gi 1159648420  782 QLKKEQRKREHQLKLL--EAQKRNQEVILRRKTEEVTALRRQ 821
Cdd:pfam12795  153 ALQAELAALKAQIDMLeqELLSNNNRQDLLKARRDLLTLRIQ 194
DUF3584 pfam12128
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ...
 648-987 1.93e-04

Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. Proteins in this family are typically between 943 to 1234 amino acids in length. This family contains a P-loop motif suggesting it is a nucleotide binding protein. It may be involved in replication.


Pssm-ID: 432349 [Multi-domain]  Cd Length: 1191  Bit Score: 47.14  E-value: 1.93e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159648420  648 ELENSQRRLQTLKRQYEEKLMMLQHKIRDTQLERDQVLQNLGSVETYSEEKAKKIkseyEKKLQTMNKELQRLQTAQKEH 727
Cdd:pfam12128  633 ELEKASREETFARTALKNARLDLRRLFDEKQSEKDKKNKALAERKDSANERLNSL----EAQLKQLDKKHQAWLEEQKEQ 708

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159648420  728 ARLLKNQSQyekqlkKLQQEVTEMKKTKVRLMKQMKEEQEkarmteSRRNREIAQLKkEQRKREhqlklLEAQKRNQEVI 807
Cdd:pfam12128  709 KREARTEKQ------AYWQVVEGALDAQLALLKAAIAARR------SGAKAELKALE-TWYKRD-----LASLGVDPDVI 770

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159648420  808 LRRKTEEVTALRRQVRPLSDKVAGKVSRKLSLPEHPIQEPSSSSSVEHDGSriaAQQKMRIPVARVQALSvtatngtgrK 887
Cdd:pfam12128  771 AKLKREIRTLERKIERIAVRRQEVLRYFDWYQETWLQRRPRLATQLSNIER---AISELQQQLARLIADT---------K 838

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159648420  888 YQRKAVTSRVYSSRAARMKWQLLERRVtDIIMQRMTISNMEADMNRL-------LTQREELTKRREKLSKRREKLMKDGG 960
Cdd:pfam12128  839 LRRAKLEMERKASEKQQVRLSENLRGL-RCEMSKLATLKEDANSEQAqgsigerLAQLEDLKLKRDYLSESVKKYVEHFK 917

                          330       340
                   ....*....|....*....|....*..
gi 1159648420  961 GSETDRNVQNINEEMESLTANIDYIND 987
Cdd:pfam12128  918 NVIADHSGSGLAETWESLREEDHYQND 944
HlpA COG2825
Periplasmic chaperone for outer membrane proteins, Skp family [Cell wall/membrane/envelope ...
 696-770 1.99e-04

Periplasmic chaperone for outer membrane proteins, Skp family [Cell wall/membrane/envelope biogenesis, Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 442073 [Multi-domain]  Cd Length: 171  Bit Score: 44.44  E-value: 1.99e-04
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1159648420  696 EEKAKKIKSEYEKKLQTMNKELQRLQTA-QKEhaRLLKNQSQYEKQLKKLQQEVTEMKKTKVRLMKQMKEEQEKAR 770
Cdd:COG2825     45 QKKLEKEFKKRQAELQKLEKELQALQEKlQKE--AATLSEEERQKKERELQKKQQELQRKQQEAQQDLQKRQQELL 118
OmpH pfam03938
Outer membrane protein (OmpH-like); This family includes outer membrane proteins such as OmpH ...
 715-830 2.02e-04

Outer membrane protein (OmpH-like); This family includes outer membrane proteins such as OmpH among others. Skp (OmpH) has been characterized as a molecular chaperone that interacts with unfolded proteins as they emerge in the periplasm from the Sec translocation machinery.


Pssm-ID: 461098 [Multi-domain]  Cd Length: 140  Bit Score: 43.72  E-value: 2.02e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159648420  715 KELQRLQTAQKEharLLKNQSQYEKQLKKLQQEVTEMKKTKVRLMKQMKEEQEKarmtesrRNREIAQLKKEqrkrehql 794
Cdd:pfam03938   12 EESPEGKAAQAQ---LEKKFKKRQAELEAKQKELQKLYEELQKDGALLEEEREE-------KEQELQKKEQE-------- 73

                           90       100       110
                   ....*....|....*....|....*....|....*.
gi 1159648420  795 kLLEAQKRNQEVILRRKTEEVTALRRQVRPLSDKVA 830
Cdd:pfam03938   74 -LQQLQQKAQQELQKKQQELLQPIQDKINKAIKEVA 108
DUF3584 pfam12128
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ...
 627-1059 2.29e-04

Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. Proteins in this family are typically between 943 to 1234 amino acids in length. This family contains a P-loop motif suggesting it is a nucleotide binding protein. It may be involved in replication.


Pssm-ID: 432349 [Multi-domain]  Cd Length: 1191  Bit Score: 46.76  E-value: 2.29e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159648420  627 NYQADLANITCEI-AIKQKLIDELENSQRRLQTLKRQYEEKLMMLqHKIRDTQleRDQVLQNLGSVETYSEEKAKKIKSE 705
Cdd:pfam12128  351 SWQSELENLEERLkALTGKHQDVTAKYNRRRSKIKEQNNRDIAGI-KDKLAKI--REARDRQLAVAEDDLQALESELREQ 427

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159648420  706 YEKKLQTMNKELQRLQTAQKEhARLLKNQSQYEKQLKkLQQEVtemkktKVRLMKQMKEEQEKARMTESRRNREIAQLKK 785
Cdd:pfam12128  428 LEAGKLEFNEEEYRLKSRLGE-LKLRLNQATATPELL-LQLEN------FDERIERAREEQEAANAEVERLQSELRQARK 499

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159648420  786 --EQRKREHQ---LKLLEAQKRNQEVILRRKTEEVTA---LRRQVRPLSDKVAGKVSRKLSLPE--HPIQEPSSSSSVEH 855
Cdd:pfam12128  500 rrDQASEALRqasRRLEERQSALDELELQLFPQAGTLlhfLRKEAPDWEQSIGKVISPELLHRTdlDPEVWDGSVGGELN 579

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159648420  856 DGSriaaqqkMRIPVARVQALSVTATNGTGRKyqRKAVTSRVY---SSRAARMKWQL------LERRVTDIIMQRMTISN 926
Cdd:pfam12128  580 LYG-------VKLDLKRIDVPEWAASEEELRE--RLDKAEEALqsaREKQAAAEEQLvqangeLEKASREETFARTALKN 650

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159648420  927 MEADMNRLLTQREELTKRREKLSKRREKLMK------DGGGSETDRNVQNINEE-----MESLTANIDYINDSISDCQAN 995
Cdd:pfam12128  651 ARLDLRRLFDEKQSEKDKKNKALAERKDSANerlnslEAQLKQLDKKHQAWLEEqkeqkREARTEKQAYWQVVEGALDAQ 730

                          410       420       430       440       450       460
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1159648420  996 IMQMEEAKEEGETlDVTAVINACTLTEARYLldhfLTMGINkGLQAAQKEAQIKVLEGRLKQTE 1059
Cdd:pfam12128  731 LALLKAAIAARRS-GAKAELKALETWYKRDL----ASLGVD-PDVIAKLKREIRTLERKIERIA 788
Cep57_CLD pfam14073
Centrosome localization domain of Cep57; The CLD or centrosome localization domain of Cep57 is ...
 670-804 2.43e-04

Centrosome localization domain of Cep57; The CLD or centrosome localization domain of Cep57 is found at the N-terminus, and lies approximately between residues 58 and 239. This region lies within the first alpha-helical coiled-coil segment of Cep57, and localizes to the centrosome internally to gamma-tubulin, suggesting that it is either on both centrioles or on a centromatrix component. This N-terminal region can also multimerize with the N-terminus of other Cep57 molecules. The C-terminal part, Family Cep57_MT_bd, pfam06657, is the microtubule-binding region of Cep57.


Pssm-ID: 464080 [Multi-domain]  Cd Length: 178  Bit Score: 44.16  E-value: 2.43e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159648420  670 LQHKIRDTQLERDQ-----------------VLQNLGSVETYSEEKAKKIKSEYEKKLQT-------MNKELQR----LQ 721
Cdd:pfam14073    9 LQEKIRRLELERKQaednlkqlsretshykeVLQKENDARDPSRGEVSKQNQELISQLAAaesrcslLEKQLEYmrkmVE 88

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159648420  722 TAQKEHARLLKNQSQYEKQLKKLQQEVtemkktKVRLMKQMKEEQEKARMTESRRNRE--IAQLKKEQRKREHQLKLLEa 799
Cdd:pfam14073   89 NAEKERTAVLEKQASLERERSQDSSEL------QAQLEKLEKLEQEYLRLTRTQSLAEtkIKELEEKLQEEEHQRKLVQ- 161


                   ....*
gi 1159648420  800 QKRNQ 804
Cdd:pfam14073  162 EKAAQ 166
ATP-synt_Fo_b cd06503
F-type ATP synthase, membrane subunit b; Membrane subunit b is a component of the Fo complex ...
 681-783 2.44e-04

F-type ATP synthase, membrane subunit b; Membrane subunit b is a component of the Fo complex of FoF1-ATP synthase. The F-type ATP synthases (FoF1-ATPase) consist of two structural domains: the F1 (assembly factor one) complex containing the soluble catalytic core, and the Fo (oligomycin sensitive factor) complex containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. F1 is composed of alpha (or A), beta (B), gamma (C), delta (D) and epsilon (E) subunits with a stoichiometry of 3:3:1:1:1, while Fo consists of the three subunits a, b, and c (1:2:10-14). An oligomeric ring of 10-14 c subunits (c-ring) make up the Fo rotor. The flux of protons through the ATPase channel (Fo) drives the rotation of the c-ring, which in turn is coupled to the rotation of the F1 complex gamma subunit rotor due to the permanent binding between the gamma and epsilon subunits of F1 and the c-ring of Fo. The F-ATP synthases are primarily found in the inner membranes of eukaryotic mitochondria, in the thylakoid membranes of chloroplasts or in the plasma membranes of bacteria. The F-ATP synthases are the primary producers of ATP, using the proton gradient generated by oxidative phosphorylation (mitochondria) or photosynthesis (chloroplasts). Alternatively, under conditions of low driving force, ATP synthases function as ATPases, thus generating a transmembrane proton or Na(+) gradient at the expense of energy derived from ATP hydrolysis. This group also includes F-ATP synthase that has also been found in the archaea Candidatus Methanoperedens.


Pssm-ID: 349951 [Multi-domain]  Cd Length: 132  Bit Score: 43.20  E-value: 2.44e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159648420  681 RDQVLQNLGSVETySEEKAKKIKSEYEKKLQTMNKELQR-LQTAQKEHarllknQSQYEKQLKKLQQEVTEMKKTKvrlM 759
Cdd:cd06503     32 EEKIAESLEEAEK-AKEEAEELLAEYEEKLAEARAEAQEiIEEARKEA------EKIKEEILAEAKEEAERILEQA---K 101

                           90       100
                   ....*....|....*....|....
gi 1159648420  760 KQMKEEQEKArMTESRrnREIAQL 783
Cdd:cd06503    102 AEIEQEKEKA-LAELR--KEVADL 122
WD40 pfam00400
WD domain, G-beta repeat;
1595-1628 2.51e-04

WD domain, G-beta repeat;


Pssm-ID: 459801 [Multi-domain]  Cd Length: 39  Bit Score: 40.41  E-value: 2.51e-04
                           10        20        30
                   ....*....|....*....|....*....|....*.
gi 1159648420 1595 PIGEMKGHDSPINAIC--TNSSQIFTAADDRTVRIW 1628
Cdd:pfam00400    3 LLKTLEGHTGSVTSLAfsPDGKLLASGSDDGTVKVW 38
OmpH pfam03938
Outer membrane protein (OmpH-like); This family includes outer membrane proteins such as OmpH ...
 696-770 2.83e-04

Outer membrane protein (OmpH-like); This family includes outer membrane proteins such as OmpH among others. Skp (OmpH) has been characterized as a molecular chaperone that interacts with unfolded proteins as they emerge in the periplasm from the Sec translocation machinery.


Pssm-ID: 461098 [Multi-domain]  Cd Length: 140  Bit Score: 43.33  E-value: 2.83e-04
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1159648420  696 EEKAKKIKSEYEKKLQTMNKELQRLQTAQKEHARLLKNQSQyeKQLKKLQQEVTEMKKTKVRLMKQMKEEQEKAR 770
Cdd:pfam03938   21 QAQLEKKFKKRQAELEAKQKELQKLYEELQKDGALLEEERE--EKEQELQKKEQELQQLQQKAQQELQKKQQELL 93
PRK10929 PRK10929
putative mechanosensitive channel protein; Provisional
 640-843 2.83e-04

putative mechanosensitive channel protein; Provisional


Pssm-ID: 236798 [Multi-domain]  Cd Length: 1109  Bit Score: 46.59  E-value: 2.83e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159648420  640 AIKQKLID------ELENSQRRLQTLKRQYEEKLMML---QHKIRDTQLERDQVLQNLGSVET----------YSEEKAK 700
Cdd:PRK10929   106 ALEQEILQvssqllEKSRQAQQEQDRAREISDSLSQLpqqQTEARRQLNEIERRLQTLGTPNTplaqaqltalQAESAAL 185

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159648420  701 KIK-SEYE-KKLQTMNK-ELQRLQT--AQKEHARLLKNQSQYEKQLKKLQQEVTEMKKTKVRLMKQMKEEQEKARMTESR 775
Cdd:PRK10929   186 KALvDELElAQLSANNRqELARLRSelAKKRSQQLDAYLQALRNQLNSQRQREAERALESTELLAEQSGDLPKSIVAQFK 265

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1159648420  776 RNREIAQLKKEQRKRehqLKLLEAQKR--NQEVILRRKTeeVTALRRQVRPLSDKVA------GKVSRklsLPEHP 843
Cdd:PRK10929   266 INRELSQALNQQAQR---MDLIASQQRqaASQTLQVRQA--LNTLREQSQWLGVSNAlgealrAQVAR---LPEMP 333
GBP_C cd16269
Guanylate-binding protein, C-terminal domain; Guanylate-binding protein (GBP), C-terminal ...
 643-806 3.23e-04

Guanylate-binding protein, C-terminal domain; Guanylate-binding protein (GBP), C-terminal domain. Guanylate-binding proteins (GBPs) are synthesized after activation of the cell by interferons. The biochemical properties of GBPs are clearly different from those of Ras-like and heterotrimeric GTP-binding proteins. They bind guanine nucleotides with low affinity (micromolar range), are stable in their absence, and have a high turnover GTPase. In addition to binding GDP/GTP, they have the unique ability to bind GMP with equal affinity and hydrolyze GTP not only to GDP, but also to GMP. This C-terminal domain has been shown to mediate inhibition of endothelial cell proliferation by inflammatory cytokines.


Pssm-ID: 293879 [Multi-domain]  Cd Length: 291  Bit Score: 45.26  E-value: 3.23e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159648420  643 QKLIDELENSQRRLQTLK----RQYEEKLMMLQHKIRdtQLER-----DQVLQN-LGSVETYSE----------EKAKKI 702
Cdd:cd16269    123 QELSAPLEEKISQGSYSVpggyQLYLEDREKLVEKYR--QVPRkgvkaEEVLQEfLQSKEAEAEailqadqaltEKEKEI 200

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159648420  703 KSEYEKKlQTMNKELQRLQTAQKEHARLLKNQsqyekqlKKLQQEvtEMKKtkvrLMKQMKEEQEKarmTESRRNREIAQ 782
Cdd:cd16269    201 EAERAKA-EAAEQERKLLEEQQRELEQKLEDQ-------ERSYEE--HLRQ----LKEKMEEEREN---LLKEQERALES 263

                          170       180
                   ....*....|....*....|....
gi 1159648420  783 LKKEQRKREHQLKLLEAQKRNQEV 806
Cdd:cd16269    264 KLKEQEALLEEGFKEQAELLQEEI 287
COG5022 COG5022
Myosin heavy chain [General function prediction only];
647-819 3.28e-04

Myosin heavy chain [General function prediction only];


Pssm-ID: 227355 [Multi-domain]  Cd Length: 1463  Bit Score: 46.22  E-value: 3.28e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159648420  647 DELENSQRRLQTLKRqYEEKLMMLQHKI-RDTQLERDQVLQNLGSVETYSEEKAKKIKSEYEKK------LQTMNKELQR 719
Cdd:COG5022    918 DLIENLEFKTELIAR-LKKLLNNIDLEEgPSIEYVKLPELNKLHEVESKLKETSEEYEDLLKKStilvreGNKANSELKN 996

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159648420  720 LQTAQKEHARLLKNQSQYEKQLKKLQQEVTEMKKTKVRLMKQMKEEQEKARMTESRRNREIA--QLKKE------QRKRE 791
Cdd:COG5022    997 FKKELAELSKQYGALQESTKQLKELPVEVAELQSASKIISSESTELSILKPLQKLKGLLLLEnnQLQARykalklRRENS 1076

                          170       180       190
                   ....*....|....*....|....*....|.
gi 1159648420  792 HQLKLLEAQKRNQEVILRR---KTEEVTALR 819
Cdd:COG5022   1077 LLDDKQLYQLESTENLLKTinvKDLEVTNRN 1107
MukB COG3096
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ...
 638-824 3.46e-04

Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 442330 [Multi-domain]  Cd Length: 1470  Bit Score: 46.10  E-value: 3.46e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159648420  638 EIAIKQKLIDELENSQRRLQTLKRQYEE-KLMMLQHKIRDTQLER-----DQVLQNLGSVeTYSEEKAKKIKSeyekklQ 711
Cdd:COG3096    911 FIQQHGKALAQLEPLVAVLQSDPEQFEQlQADYLQAKEQQRRLKQqifalSEVVQRRPHF-SYEDAVGLLGEN------S 983

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159648420  712 TMNKEL-QRLQTAQKEHARLLKNQSQYEKQLKKLQQEVTEMK---KTKVRLMKQMKEE------------QEKARMTESR 775
Cdd:COG3096    984 DLNEKLrARLEQAEEARREAREQLRQAQAQYSQYNQVLASLKssrDAKQQTLQELEQEleelgvqadaeaEERARIRRDE 1063

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*....
gi 1159648420  776 RNREIAQLKKEQRKREHQLKLLEAQKRNQEVILRRKTEEVTALRRQVRP 824
Cdd:COG3096   1064 LHEELSQNRSRRSQLEKQLTRCEAEMDSLQKRLRKAERDYKQEREQVVQ 1112
PRK11637 PRK11637
AmiB activator; Provisional
 703-795 4.30e-04

AmiB activator; Provisional


Pssm-ID: 236942 [Multi-domain]  Cd Length: 428  Bit Score: 45.45  E-value: 4.30e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159648420  703 KSEYEKKlQTMNKEL---QRLQTAQKEHARLL--KNQSQYEKQLKKLQQEVTEMKKTKVRLMKQMKEEQEKARMTESRRN 777
Cdd:PRK11637   186 KAELEEK-QSQQKTLlyeQQAQQQKLEQARNErkKTLTGLESSLQKDQQQLSELRANESRLRDSIARAEREAKARAEREA 264

                           90
                   ....*....|....*...
gi 1159648420  778 REIAQLkkeqRKREHQLK 795
Cdd:PRK11637   265 REAARV----RDKQKQAK 278
ADIP pfam11559
Afadin- and alpha -actinin-Binding; This family is found in mammals where it is localized at ...
 678-785 4.86e-04

Afadin- and alpha -actinin-Binding; This family is found in mammals where it is localized at cell-cell adherens junctions, and in Sch. pombe and other fungi where it anchors spindle-pole bodies to spindle microtubules. It is a coiled-coil structure, and in pombe, it is required for anchoring the minus end of spindle microtubules to the centrosome equivalent, the spindle-pole body. The name ADIP derives from the family being composed of Afadin- and alpha -Actinin-Binding Proteins localized at Cell-Cell Adherens Junctions.


Pssm-ID: 463295 [Multi-domain]  Cd Length: 151  Bit Score: 42.69  E-value: 4.86e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159648420  678 QLERDQ-VLQNLgsvetysEEKAKKIKSEYE------KKLQTMNKELQR-LQTAQKEHARLLKNQSQYEKQLKKLQQEVT 749
Cdd:pfam11559   46 QRDRDLeFRESL-------NETIRTLEAEIErlqskiERLKTQLEDLEReLALLQAKERQLEKKLKTLEQKLKNEKEELQ 118

                           90       100       110
                   ....*....|....*....|....*....|....*.
gi 1159648420  750 EMKKTKVRLMKQMKEEQEKarmtesrRNREIAQLKK 785
Cdd:pfam11559  119 RLKNALQQIKTQFAHEVKK-------RDREIEKLKE 147
KASH_CCD pfam14662
Coiled-coil region of CCDC155 or KASH; This coiled-coil region is found in the central part of ...
 708-822 5.00e-04

Coiled-coil region of CCDC155 or KASH; This coiled-coil region is found in the central part of KASH or Klarsicht/ANC-1/Syne/homology proteins. KASH are a meiosis-specific proteins that localize at telomeres and interact with SUN1, thus being implicated in meiotic chromosome dynamics and homolog pairing.


Pssm-ID: 405365 [Multi-domain]  Cd Length: 191  Bit Score: 43.63  E-value: 5.00e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159648420  708 KKLQTMNKELQR-LQTAQKEHARLLKNQSQYEKQLKKLQQEVTEmkktkvrlMKQMKEEQEKARMTESR--RNREIAQLK 784
Cdd:pfam14662   18 QKLLQENSKLKAtVETREETNAKLLEENLNLRKQAKSQQQAVQK--------EKLLEEELEDLKLIVNSleEARRSLLAQ 89

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|
gi 1159648420  785 KEQRKREHQ------LKLLEAQKRNQEVI--LRRKTEEVTA----LRRQV 822
Cdd:pfam14662   90 NKQLEKENQsllqeiESLQEENKKNQAERdkLQKKKKELLKskacLKEQL 139
WD40 pfam00400
WD domain, G-beta repeat;
1459-1500 5.24e-04

WD domain, G-beta repeat;


Pssm-ID: 459801 [Multi-domain]  Cd Length: 39  Bit Score: 39.64  E-value: 5.24e-04
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|..
gi 1159648420 1459 FQSTGKLTGHQGPVMCLtvdRISNGQDLIVTGSKDHYIKMFD 1500
Cdd:pfam00400    1 GKLLKTLEGHTGSVTSL---AFSPDGKLLASGSDDGTVKVWD 39
PRK15335 PRK15335
type III secretion system protein SpaM; Provisional
 653-801 5.34e-04

type III secretion system protein SpaM; Provisional


Pssm-ID: 185235  Cd Length: 147  Bit Score: 42.74  E-value: 5.34e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159648420  653 QRRLQTLKRQYEEKLMMLQHKIRDTQLERDQVLQNLGSVETYSEekakkikseyekKLQTMNKELQRlqtaqKEHARLLK 732
Cdd:PRK15335    11 QRRCTVFHSQCESILLRYQDEDRGLQAEEEAILEQIAGLKLLLD------------TLRAENRQLSR-----EEIYTLLR 73

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1159648420  733 NQSQYEKQLKKLQQEVTEMKKTKVRLMKQMKEEQEKARM---TESRRNREIAQLKKEQRKREHQLKLLEAQK 801
Cdd:PRK15335    74 KQSIVRRQIKDLELQIIQIQEKRSELEKKREEFQKKSKYwlrKEGNYQRWIIRQKRFYIQREIQQEEAESEE 145
OmpH smart00935
Outer membrane protein (OmpH-like); This family includes outer membrane proteins such as OmpH ...
 696-770 5.94e-04

Outer membrane protein (OmpH-like); This family includes outer membrane proteins such as OmpH among others. Skp (OmpH) has been characterized as a molecular chaperone that interacts with unfolded proteins as they emerge in the periplasm from the Sec translocation machinery.


Pssm-ID: 214922 [Multi-domain]  Cd Length: 140  Bit Score: 42.19  E-value: 5.94e-04
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1159648420   696 EEKAKKIKSEYEKKLQTMNKELQRLQTAQKEHARLLkNQSQYEKQLKKLQQEVTEMKKTKVRLMKQMKEEQEKAR 770
Cdd:smart00935   20 QKQLEKEFKKRQAELEKLEKELQKLKEKLQKDAATL-SEAAREKKEKELQKKVQEFQRKQQKLQQDLQKRQQEEL 93
PKK pfam12474
Polo kinase kinase; This domain family is found in eukaryotes, and is approximately 140 amino ...
 625-747 5.97e-04

Polo kinase kinase; This domain family is found in eukaryotes, and is approximately 140 amino acids in length. The family is found in association with pfam00069. Polo-like kinase 1 (Plx1) is essential during mitosis for the activation of Cdc25C, for spindle assembly, and for cyclin B degradation. This family is Polo kinase kinase (PKK) which phosphorylates Polo kinase and Polo-like kinase to activate them. PKK is a serine/threonine kinase.


Pssm-ID: 463600 [Multi-domain]  Cd Length: 139  Bit Score: 42.16  E-value: 5.97e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159648420  625 KENYQADLANITCeiaiKQK-LIDELENSQ--RRLQTLKRQ-YEEK--LMMLQHKIRDTQLERDQvlqnlgsvetySEEK 698
Cdd:pfam12474   20 KKRYEKELEQLER----QQKqQIEKLEQRQtqELRRLPKRIrAEQKkrLKMFRESLKQEKKELKQ-----------EVEK 84

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*....
gi 1159648420  699 AKKIKSEYEKKlqtMNKELQRLQTAQKEHARLLKNQSQYEKQLKKLQQE 747
Cdd:pfam12474   85 LPKFQRKEAKR---QRKEELELEQKHEELEFLQAQSEALERELQQLQNE 130
GBP_C pfam02841
Guanylate-binding protein, C-terminal domain; Transcription of the anti-viral ...
 697-830 6.30e-04

Guanylate-binding protein, C-terminal domain; Transcription of the anti-viral guanylate-binding protein (GBP) is induced by interferon-gamma during macrophage induction. This family contains GBP1 and GPB2, both GTPases capable of binding GTP, GDP and GMP.


Pssm-ID: 460721 [Multi-domain]  Cd Length: 297  Bit Score: 44.20  E-value: 6.30e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159648420  697 EKAKKIKSEYEkklQTMNKELQRLQTAQKeharLLKNQSQYEKQLKKLQQEVTEMKKtkvrlmkQMKEEQEKARMTESRR 776
Cdd:pfam02841  155 EERDKLEAKYN---QVPRKGVKAEEVLQE----FLQSKEAVEEAILQTDQALTAKEK-------AIEAERAKAEAAEAEQ 220

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....
gi 1159648420  777 NREIAQLKKEQRKrehqlklLEAQKRNQEVILRRKTEEVTALRRQVRPLSDKVA 830
Cdd:pfam02841  221 ELLREKQKEEEQM-------MEAQERSYQEHVKQLIEKMEAEREQLLAEQERML 267
MAP7 pfam05672
MAP7 (E-MAP-115) family; The organization of microtubules varies with the cell type and is ...
 654-791 6.42e-04

MAP7 (E-MAP-115) family; The organization of microtubules varies with the cell type and is presumably controlled by tissue-specific microtubule-associated proteins (MAPs). The 115-kDa epithelial MAP (E-MAP-115/MAP7) has been identified as a microtubule-stabilising protein predominantly expressed in cell lines of epithelial origin. The binding of this microtubule associated protein is nucleotide independent.


Pssm-ID: 461709 [Multi-domain]  Cd Length: 153  Bit Score: 42.34  E-value: 6.42e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159648420  654 RRLQTLKRQYEEKLMMLQHKIRdtQLERDQVLQNLGSVETYSEEKAKKI-----KSEYEKKLQTMNKELQRLQTAQKEHA 728
Cdd:pfam05672   20 RRQAREQREREEQERLEKEEEE--RLRKEELRRRAEEERARREEEARRLeeerrREEEERQRKAEEEAEEREQREQEEQE 97

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1159648420  729 RLlknQSQYEKQLKKLQQEVTEMKKTKVRLMKQmkEEQEKarmtESRRNReIAQLKKEQRKRE 791
Cdd:pfam05672   98 RL---QKQKEEAEAKAREEAERQRQEREKIMQQ--EEQER----LERKKR-IEEIMKRTRKSD 150
MAP7 pfam05672
MAP7 (E-MAP-115) family; The organization of microtubules varies with the cell type and is ...
 726-821 7.19e-04

MAP7 (E-MAP-115) family; The organization of microtubules varies with the cell type and is presumably controlled by tissue-specific microtubule-associated proteins (MAPs). The 115-kDa epithelial MAP (E-MAP-115/MAP7) has been identified as a microtubule-stabilising protein predominantly expressed in cell lines of epithelial origin. The binding of this microtubule associated protein is nucleotide independent.


Pssm-ID: 461709 [Multi-domain]  Cd Length: 153  Bit Score: 42.34  E-value: 7.19e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159648420  726 EHARLLKNQSQYEKQlKKLQQEVTEmkktkvrlmKQMKEEQEKARMTESRRNREIAQLKKEQRKREHQLKLLEAQKRNQE 805
Cdd:pfam05672   18 EKRRQAREQREREEQ-ERLEKEEEE---------RLRKEELRRRAEEERARREEEARRLEEERRREEEERQRKAEEEAEE 87

                           90
                   ....*....|....*.
gi 1159648420  806 VILRRKtEEVTALRRQ 821
Cdd:pfam05672   88 REQREQ-EEQERLQKQ 102
PRK01156 PRK01156
chromosome segregation protein; Provisional
 386-959 7.89e-04

chromosome segregation protein; Provisional


Pssm-ID: 100796 [Multi-domain]  Cd Length: 895  Bit Score: 44.89  E-value: 7.89e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159648420  386 INALRSEIARLQMELMEYKtgKRIIDEEGVESIndmfhenamLQTENNNLRVRIKAMQETVDALRARITQLMS--DQANQ 463
Cdd:PRK01156   185 IDYLEEKLKSSNLELENIK--KQIADDEKSHSI---------TLKEIERLSIEYNNAMDDYNNLKSALNELSSleDMKNR 253

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159648420  464 VLA--RAGEGNEEISNMIHNYIKEIEDlRAKLLESEAVNENlrRNLSRAstrstYFGgpsafSASMLSSEKETLEILDia 541
Cdd:PRK01156   254 YESeiKTAESDLSMELEKNNYYKELEE-RHMKIINDPVYKN--RNYIND-----YFK-----YKNDIENKKQILSNID-- 318

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159648420  542 kkDLEKLKKKERKKKKSVKEDNTDNEQEKRdEKGSSERENNELEAEEiqeasdredeeeeddededdMEVVESSDESDSD 621
Cdd:PRK01156   319 --AEINKYHAIIKKLSVLQKDYNDYIKKKS-RYDDLNNQILELEGYE--------------------MDYNSYLKSIESL 375

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159648420  622 SDEKENYQADLANITCEIA--IKQKLID------ELENSQRRLQtlkrQYEEKLMMLQHKIRDTQLERDQVLQNLGSVE- 692
Cdd:PRK01156   376 KKKIEEYSKNIERMSAFISeiLKIQEIDpdaikkELNEINVKLQ----DISSKVSSLNQRIRALRENLDELSRNMEMLNg 451

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159648420  693 ---------TYSEEKAKKIKSEYEKKLQTMNKELQRLQTAQK---EHARLLKNQSQY------------EKQLKKLQQEV 748
Cdd:PRK01156   452 qsvcpvcgtTLGEEKSNHIINHYNEKKSRLEEKIREIEIEVKdidEKIVDLKKRKEYleseeinksineYNKIESARADL 531

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159648420  749 TEMKKTKVRLM-KQMKEEQEKARMT-------ESRR---NREIAQLKK------EQRKREHQLKLLEAQKRNQEVI---- 807
Cdd:PRK01156   532 EDIKIKINELKdKHDKYEEIKNRYKslkledlDSKRtswLNALAVISLidietnRSRSNEIKKQLNDLESRLQEIEigfp 611

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159648420  808 ---------LRRKTEEVTALRRQVRPLSDKvagkvsrklslpehPIQEPSSSSSVEHDGSRIAaQQKMRIPvaRVQALSV 878
Cdd:PRK01156   612 ddksyidksIREIENEANNLNNKYNEIQEN--------------KILIEKLRGKIDNYKKQIA-EIDSIIP--DLKEITS 674

                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159648420  879 TATNGTGRkyqRKAVTSRVYSSRAARMKWqlleRRVTDIIMQRMT-ISNMEADMNRLLTQREELTKRREKLSKRREKLMK 957
Cdd:PRK01156   675 RINDIEDN---LKKSRKALDDAKANRARL----ESTIEILRTRINeLSDRINDINETLESMKKIKKAIGDLKRLREAFDK 747


                   ..
gi 1159648420  958 DG 959
Cdd:PRK01156   748 SG 749
WD40 smart00320
WD40 repeats; Note that these repeats are permuted with respect to the structural repeats ...
 1459-1500 8.29e-04

WD40 repeats; Note that these repeats are permuted with respect to the structural repeats (blades) of the beta propeller domain.


Pssm-ID: 197651 [Multi-domain]  Cd Length: 40  Bit Score: 38.83  E-value: 8.29e-04
                            10        20        30        40
                    ....*....|....*....|....*....|....*....|..
gi 1159648420  1459 FQSTGKLTGHQGPVMCLtvdRISNGQDLIVTGSKDHYIKMFD 1500
Cdd:smart00320    2 GELLKTLKGHTGPVTSV---AFSPDGKYLASGSDDGTIKLWD 40
OmpH pfam03938
Outer membrane protein (OmpH-like); This family includes outer membrane proteins such as OmpH ...
 699-786 8.50e-04

Outer membrane protein (OmpH-like); This family includes outer membrane proteins such as OmpH among others. Skp (OmpH) has been characterized as a molecular chaperone that interacts with unfolded proteins as they emerge in the periplasm from the Sec translocation machinery.


Pssm-ID: 461098 [Multi-domain]  Cd Length: 140  Bit Score: 41.79  E-value: 8.50e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159648420  699 AKKIKSEYEKKLQTMNKELQRLQTA-QKEHARLLKNQSQYEKQLKKLQQEVtemkktkVRLMKQMKEEQEKARMT-ESRR 776
Cdd:pfam03938   17 GKAAQAQLEKKFKKRQAELEAKQKElQKLYEELQKDGALLEEEREEKEQEL-------QKKEQELQQLQQKAQQElQKKQ 89

                           90
                   ....*....|
gi 1159648420  777 NREIAQLKKE 786
Cdd:pfam03938   90 QELLQPIQDK 99
Cast pfam10174
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ...
 642-771 9.16e-04

RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part of the CAZ (cytomatrix at the active zone) complex which is involved in determining the site of synaptic vesicle fusion. The C-terminus is a PDZ-binding motif that binds directly to RIM (a small G protein Rab-3A effector). The family also contains four coiled-coil domains.


Pssm-ID: 431111 [Multi-domain]  Cd Length: 766  Bit Score: 44.81  E-value: 9.16e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159648420  642 KQKLIDELENSQRRLQTLKR-----QYEEkLMMLQHKirdTQLERDQVLQNLGSVETYSEEKAK---KIKSEYEKKLQT- 712
Cdd:pfam10174  631 KKKGAQLLEEARRREDNLADnsqqlQLEE-LMGALEK---TRQELDATKARLSSTQQSLAEKDGhltNLRAERRKQLEEi 706

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1159648420  713 --MNKELQRLQTAQKEHARLLKNQSQYEKqlKKLQQEVTEMKKTKVRLMKQMKeEQEKARM 771
Cdd:pfam10174  707 leMKQEALLAAISEKDANIALLELSSSKK--KKTQEEVMALKREKDRLVHQLK-QQTQNRM 764
PTZ00121 PTZ00121
MAEBL; Provisional
 567-1004 9.86e-04

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 44.75  E-value: 9.86e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159648420  567 EQEKRDEKGSSERENNELEAEEIQEASDREDEEEEDDEDEDDMEVVESSDESDSdsDEKENYQADLANITCEIAIKQKLI 646
Cdd:PTZ00121  1398 KKAEEDKKKADELKKAAAAKKKADEAKKKAEEKKKADEAKKKAEEAKKADEAKK--KAEEAKKAEEAKKKAEEAKKADEA 1475

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159648420  647 DELENSQRRLQTLKRQYEEKLMMLQhKIRDTQLERDQVLQNLGSVETYSEEKAKKI----KSEYEKKLQTMNK--ELQRL 720
Cdd:PTZ00121  1476 KKKAEEAKKADEAKKKAEEAKKKAD-EAKKAAEAKKKADEAKKAEEAKKADEAKKAeeakKADEAKKAEEKKKadELKKA 1554

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159648420  721 QTAQK-EHARLLKNQSQYEKQLKKLQQEVTEMKKT-KVRLMKQMKEEQEKARM-TESRRNREIAQLKKEQRKREHQLKLL 797
Cdd:PTZ00121  1555 EELKKaEEKKKAEEAKKAEEDKNMALRKAEEAKKAeEARIEEVMKLYEEEKKMkAEEAKKAEEAKIKAEELKKAEEEKKK 1634

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159648420  798 EAQKRNQEVILRRKTEEVTALRRQVRPLSDKVAGKVSRKLSLPEHPIQEPSSSSSVEHDGSRIAAQQKMRIPVARVQALS 877
Cdd:PTZ00121  1635 VEQLKKKEAEEKKKAEELKKAEEENKIKAAEEAKKAEEDKKKAEEAKKAEEDEKKAAEALKKEAEEAKKAEELKKKEAEE 1714

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159648420  878 VtatngtgRKYQ--RKAVTSRVYSSRAARMKWQLLERRVTDIIMQrmtisnmEADMNRLLTQREELTKRREKLSKRREKL 955
Cdd:PTZ00121  1715 K-------KKAEelKKAEEENKIKAEEAKKEAEEDKKKAEEAKKD-------EEEKKKIAHLKKEEEKKAEEIRKEKEAV 1780

                          410       420       430       440       450       460
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1159648420  956 MKDG-------GGSETDRNVQNINEEMESL----TANIDYINDSISDCQANI--------MQMEEAKE 1004
Cdd:PTZ00121  1781 IEEEldeedekRRMEVDKKIKDIFDNFANIieggKEGNLVINDSKEMEDSAIkevadsknMQLEEADA 1848
CCDC66 pfam15236
Coiled-coil domain-containing protein 66; This protein family, named Coiled-coil ...
 696-791 1.11e-03

Coiled-coil domain-containing protein 66; This protein family, named Coiled-coil domain-containing protein 66 (CCDC) refers to a protein domain found in eukaryotes, and is approximately 160 amino acids in length. CCDC66 protein is detected mainly in the inner segments of photoreceptors in many vertebrates including mice and humans. It has been found in dogs, that a mutation in the CCDC66 gene causes generalized progressive retinal atrophy (gPRA). This shows that the protein encoded for by this gene is vital for healthy vision and guards against photoreceptor cell degeneration. The structure of CCDC66 proteins includes a heptad repeat pattern which contains at least one coiled-coil domain. There are at least two or more alpha-helices which form a cable-like structure.


Pssm-ID: 434558 [Multi-domain]  Cd Length: 154  Bit Score: 41.70  E-value: 1.11e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159648420  696 EEKAKKIKSEYEKKLQTMNKELQRLQTaQKEharllKNQSQYEKQLKKlQQEVTEMKKTKVRLMKQ-MKEEQEKARMtes 774
Cdd:pfam15236   66 EEKERQKKLEEERRRQEEQEEEERLRR-ERE-----EEQKQFEEERRK-QKEKEEAMTRKTQALLQaMQKAQELAQR--- 135

                           90
                   ....*....|....*..
gi 1159648420  775 rrnreiaqLKKEQRKRE 791
Cdd:pfam15236  136 --------LKQEQRIRE 144
HEC1 COG5185
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell ...
 625-1069 1.19e-03

Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 444066 [Multi-domain]  Cd Length: 594  Bit Score: 44.18  E-value: 1.19e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159648420  625 KENYQADLANITCEIAIKQKLIDELENSQRRLQtLKRQYEEKlmmlqhKIRDTQLerdqvlQNLGSVETYSEEKAKKIKS 704
Cdd:COG5185    156 VETGIIKDIFGKLTQELNQNLKKLEIFGLTLGL-LKGISELK------KAEPSGT------VNSIKESETGNLGSESTLL 222

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159648420  705 EYEKKLQTMNKELQRLQTAQKEHARLlknqSQYEKQLKKLQQEVTEMKKTKVR----LMKQMKEEQEKARMTESRRNREI 780
Cdd:COG5185    223 EKAKEIINIEEALKGFQDPESELEDL----AQTSDKLEKLVEQNTDLRLEKLGenaeSSKRLNENANNLIKQFENTKEKI 298

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159648420  781 AQLKKEQRKREHQLKL------------LEAQKRNQEVILRRKTEEVTALRRQvrpLSDKVAGKVSRKLSLPEHPIQEPS 848
Cdd:COG5185    299 AEYTKSIDIKKATESLeeqlaaaeaeqeLEESKRETETGIQNLTAEIEQGQES---LTENLEAIKEEIENIVGEVELSKS 375

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159648420  849 S----SSSVEHDGSRIAAQQKMRipvarvqalsvtatngTGRKYQRKAVTSrvySSRAARMKWQLLERRVTDIimqRMTI 924
Cdd:COG5185    376 SeeldSFKDTIESTKESLDEIPQ----------------NQRGYAQEILAT---LEDTLKAADRQIEELQRQI---EQAT 433

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159648420  925 SNMEADMNRLLTQREELTKRReKLSKRREKLMKDGGGSETDRNVQ----NINEEMESLTANIDYINDSISDCQANIMQME 1000
Cdd:COG5185    434 SSNEEVSKLLNELISELNKVM-READEESQSRLEEAYDEINRSVRskkeDLNEELTQIESRVSTLKATLEKLRAKLERQL 512

                          410       420       430       440       450       460
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1159648420 1001 EAKeeGETLDVTAVINACTLTEARYLLDHFLTMGINKGLQAAQKEAQIKVLEGRLKQTEITSATQNQLL 1069
Cdd:COG5185    513 EGV--RSKLDQVAESLKDFMRARGYAHILALENLIPASELIQASNAKTDGQAANLRTAVIDELTQYLST 579
GBP_C cd16269
Guanylate-binding protein, C-terminal domain; Guanylate-binding protein (GBP), C-terminal ...
 653-823 1.27e-03

Guanylate-binding protein, C-terminal domain; Guanylate-binding protein (GBP), C-terminal domain. Guanylate-binding proteins (GBPs) are synthesized after activation of the cell by interferons. The biochemical properties of GBPs are clearly different from those of Ras-like and heterotrimeric GTP-binding proteins. They bind guanine nucleotides with low affinity (micromolar range), are stable in their absence, and have a high turnover GTPase. In addition to binding GDP/GTP, they have the unique ability to bind GMP with equal affinity and hydrolyze GTP not only to GDP, but also to GMP. This C-terminal domain has been shown to mediate inhibition of endothelial cell proliferation by inflammatory cytokines.


Pssm-ID: 293879 [Multi-domain]  Cd Length: 291  Bit Score: 43.33  E-value: 1.27e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159648420  653 QRRLQTLKRQYEEKLMMLQHKIRDTQLER-DQVLQNL----------------GSVETYSEEKaKKIKSEYEkklQTMNK 715
Cdd:cd16269     89 QKFQKKLMEQLEEKKEEFCKQNEEASSKRcQALLQELsapleekisqgsysvpGGYQLYLEDR-EKLVEKYR---QVPRK 164

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159648420  716 ELQrlqtAQKEHARLLKNQSQYEKQLKKLQQEVTEMKKtkvrlmkQMKEEQEKARMTESRRnreiaQLKKEQRKREHQlk 795
Cdd:cd16269    165 GVK----AEEVLQEFLQSKEAEAEAILQADQALTEKEK-------EIEAERAKAEAAEQER-----KLLEEQQRELEQ-- 226

                          170       180
                   ....*....|....*....|....*...
gi 1159648420  796 LLEAQKRNQEVILRRKTEEVTALRRQVR 823
Cdd:cd16269    227 KLEDQERSYEEHLRQLKEKMEEERENLL 254
ATP-synt_Fo_b cd06503
F-type ATP synthase, membrane subunit b; Membrane subunit b is a component of the Fo complex ...
 711-833 1.28e-03

F-type ATP synthase, membrane subunit b; Membrane subunit b is a component of the Fo complex of FoF1-ATP synthase. The F-type ATP synthases (FoF1-ATPase) consist of two structural domains: the F1 (assembly factor one) complex containing the soluble catalytic core, and the Fo (oligomycin sensitive factor) complex containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. F1 is composed of alpha (or A), beta (B), gamma (C), delta (D) and epsilon (E) subunits with a stoichiometry of 3:3:1:1:1, while Fo consists of the three subunits a, b, and c (1:2:10-14). An oligomeric ring of 10-14 c subunits (c-ring) make up the Fo rotor. The flux of protons through the ATPase channel (Fo) drives the rotation of the c-ring, which in turn is coupled to the rotation of the F1 complex gamma subunit rotor due to the permanent binding between the gamma and epsilon subunits of F1 and the c-ring of Fo. The F-ATP synthases are primarily found in the inner membranes of eukaryotic mitochondria, in the thylakoid membranes of chloroplasts or in the plasma membranes of bacteria. The F-ATP synthases are the primary producers of ATP, using the proton gradient generated by oxidative phosphorylation (mitochondria) or photosynthesis (chloroplasts). Alternatively, under conditions of low driving force, ATP synthases function as ATPases, thus generating a transmembrane proton or Na(+) gradient at the expense of energy derived from ATP hydrolysis. This group also includes F-ATP synthase that has also been found in the archaea Candidatus Methanoperedens.


Pssm-ID: 349951 [Multi-domain]  Cd Length: 132  Bit Score: 41.27  E-value: 1.28e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159648420  711 QTMNKELQRLQTAQKEHARLLKnqsQYEKQLKKLQQEVTEMkktkvrlMKQMKEEQEKarmtesRRNREIAQLKKE-QRK 789
Cdd:cd06503     33 EKIAESLEEAEKAKEEAEELLA---EYEEKLAEARAEAQEI-------IEEARKEAEK------IKEEILAEAKEEaERI 96

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....
gi 1159648420  790 REHQLKLLEAQKrnQEVIlrrkteevTALRRQVRPLSDKVAGKV 833
Cdd:cd06503     97 LEQAKAEIEQEK--EKAL--------AELRKEVADLAVEAAEKI 130
cc_LAMB4_C cd22301
C-terminal coiled-coil domain found in laminin subunit beta-4 (LAMB4); LAMB4, also called ...
 697-753 1.40e-03

C-terminal coiled-coil domain found in laminin subunit beta-4 (LAMB4); LAMB4, also called laminin beta-1-related protein, is a component of laminin, a complex glycoprotein consisting of three different polypeptide chains (alpha, beta, gamma). Binding to cells via a high affinity receptor, laminin is thought to mediate the attachment, migration, and organization of cells into tissues during embryonic development by interacting with other extracellular matrix components. Mutations or loss of LAMB4 may be features of gastric and colorectal cancers. Reduced LAMB4 levels may contribute to colonic dysmotility associated with diverticulitis. This model corresponds to the C-terminal coiled-coil domain of LAMB4, which may be involved in the integrin binding activity.


Pssm-ID: 411972 [Multi-domain]  Cd Length: 70  Bit Score: 39.26  E-value: 1.40e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 1159648420  697 EKAKKIKSEYEKKLQTMNKELQRLQTAQKEHARLLKNQSQYEKQLKKLQQEVTEMKK 753
Cdd:cd22301      2 ERLKNIKKEAENLAKEIEDKMKRIEDLEKRIQDLNKRKEDKANQLARLEKQVISLRK 58
PRK01156 PRK01156
chromosome segregation protein; Provisional
 625-1080 1.47e-03

chromosome segregation protein; Provisional


Pssm-ID: 100796 [Multi-domain]  Cd Length: 895  Bit Score: 44.12  E-value: 1.47e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159648420  625 KENYQADLANITCEIAIKQKLIDELENSQRRLQTLKRQY------EEKLMML--------QHKIRD-----TQLE-RDQV 684
Cdd:PRK01156   234 YNNLKSALNELSSLEDMKNRYESEIKTAESDLSMELEKNnyykelEERHMKIindpvyknRNYINDyfkykNDIEnKKQI 313

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159648420  685 LQNL-GSVETYSE-----EKAKKIKSEYEKKLQTM---NKELQRLQTAQKEHARLLKNQSQ-------YEKQLKKLQQEV 748
Cdd:PRK01156   314 LSNIdAEINKYHAiikklSVLQKDYNDYIKKKSRYddlNNQILELEGYEMDYNSYLKSIESlkkkieeYSKNIERMSAFI 393

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159648420  749 TEMKKTKVRLMKQMKEEQEKARMTESRRNREIAQLkkEQRKREHQLKLLEAqKRNQEVI--------------------- 807
Cdd:PRK01156   394 SEILKIQEIDPDAIKKELNEINVKLQDISSKVSSL--NQRIRALRENLDEL-SRNMEMLngqsvcpvcgttlgeeksnhi 470

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159648420  808 -------LRRKTEEVTALRRQVRPLSDKVAGKVSRKLSLPEHPIQEPSSS----SSVEHDgsriaaQQKMRIPVARVQAL 876
Cdd:PRK01156   471 inhynekKSRLEEKIREIEIEVKDIDEKIVDLKKRKEYLESEEINKSINEynkiESARAD------LEDIKIKINELKDK 544

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159648420  877 SVtatngtgrKYQrkAVTSRVYSsraarMKWQLLERRVTDIIMQRMTISNMEADMNRllTQREELTKRREKLSKRREKLM 956
Cdd:PRK01156   545 HD--------KYE--EIKNRYKS-----LKLEDLDSKRTSWLNALAVISLIDIETNR--SRSNEIKKQLNDLESRLQEIE 607

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159648420  957 KD------------GGGSETDRNVQNINEEMESLTANIDYINDSISDCQANIMQMEEAKEEGETLDVTAVINACTLTEAR 1024
Cdd:PRK01156   608 IGfpddksyidksiREIENEANNLNNKYNEIQENKILIEKLRGKIDNYKKQIAEIDSIIPDLKEITSRINDIEDNLKKSR 687

                          490       500       510       520       530
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 1159648420 1025 YLLDHFLTmginkglQAAQKEAQIKVLEGRLKQTEITSATQNQLLFHMLKEKAELN 1080
Cdd:PRK01156   688 KALDDAKA-------NRARLESTIEILRTRINELSDRINDINETLESMKKIKKAIG 736
ATAD3_N pfam12037
ATPase family AAA domain-containing protein 3, N-terminal; This is the conserved N-terminal ...
 699-830 1.66e-03

ATPase family AAA domain-containing protein 3, N-terminal; This is the conserved N-terminal domain of ATPase family AAA domain-containing protein 3 (ATAD3) which is involved in dimerization and interacts with the inner surface of the outer mitochondrial membrane. This domain is found associated with the AAA ATPase domain (pfam00004). ATAD3 is essential for mitochondrial network organization, mitochondrial metabolism and cell growth at organizm and cellular level. It may also play an important role in mitochondrial protein synthesis.


Pssm-ID: 463442 [Multi-domain]  Cd Length: 264  Bit Score: 42.66  E-value: 1.66e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159648420  699 AKKI-KSEYEKKLQtmnkELQRLQ--TAQKEHARLLKnqsQYEKQLKKLQQEvtemkKTKVrlmkqMKEEQEKARMTESR 775
Cdd:pfam12037   35 ARELeSSPHAKKAL----ELMKKQeqTRQAELQAKIK---EYEAAQEQLKIE-----RQRV-----EYEERRKTLQEETK 97

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 1159648420  776 RNREIAQLKKE-QRKReHQLKLLEAQKRNQEviLRRKTEEVTALRRQVRPLSDKVA 830
Cdd:pfam12037   98 QKQQRAQYQDElARKR-YQDQLEAQRRRNEE--LLRKQEESVAKQEAMRIQAQRRQ 150
ClassIIa_HDAC5_Gln-rich-N cd10164
Glutamine-rich N-terminal helical domain of HDAC5, a Class IIa histone deacetylase; This ...
 707-806 1.70e-03

Glutamine-rich N-terminal helical domain of HDAC5, a Class IIa histone deacetylase; This family consists of the glutamine-rich domain of histone deacetylase 5 (HDAC5). It belongs to a superfamily that consists of the glutamine-rich N-terminal helical extension to certain Class IIa histone deacetylases (HDACs), including HDAC4, HDAC5 and HDCA9; it is missing from HDAC7. This domain confers responsiveness to calcium signals and mediates interactions with transcription factors and cofactors, and it is able to repress transcription independently of the HDAC C-terminal, zinc-dependent catalytic domain. It has many intra- and inter-helical interactions which are possibly involved in reversible assembly and disassembly of proteins. HDACs regulate diverse cellular processes through enzymatic deacetylation of histone as well as non-histone proteins, in particular deacetylating N(6)-acetyl-lysine residues.


Pssm-ID: 197400 [Multi-domain]  Cd Length: 97  Bit Score: 39.81  E-value: 1.70e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159648420  707 EKKLQtmnKELQRLQTAQKEHARLLKNQSQYEKQLKKLQQEVTEMKKTKVRlmKQMKEEQEKARMTESRRNREIAQLKKE 786
Cdd:cd10164      6 EQQLQ---QELLLLKQQQQLQKQLLFAEFQKQHEHLTRQHEVQLQKHLKVR--AELFSEQQQQEILAAKRQQELEQQRKR 80

                           90       100
                   ....*....|....*....|
gi 1159648420  787 QRKREHQlklLEAQKRNQEV 806
Cdd:cd10164     81 EQQRQEE---LEKQRLEQQL 97
Snf7 pfam03357
Snf7; This family of proteins are involved in protein sorting and transport from the endosome ...
 643-773 2.04e-03

Snf7; This family of proteins are involved in protein sorting and transport from the endosome to the vacuole/lysosome in eukaryotic cells. Vacuoles/lysosomes play an important role in the degradation of both lipids and cellular proteins. In order to perform this degradative function, vacuoles/lysosomes contain numerous hydrolases which have been transported in the form of inactive precursors via the biosynthetic pathway and are proteolytically activated upon delivery to the vacuole/lysosome. The delivery of transmembrane proteins, such as activated cell surface receptors to the lumen of the vacuole/lysosome, either for degradation/downregulation, or in the case of hydrolases, for proper localization, requires the formation of multivesicular bodies (MVBs). These late endosomal structures are formed by invaginating and budding of the limiting membrane into the lumen of the compartment. During this process, a subset of the endosomal membrane proteins is sorted into the forming vesicles. Mature MVBs fuse with the vacuole/lysosome, thereby releasing cargo containing vesicles into its hydrolytic lumen for degradation. Endosomal proteins that are not sorted into the intralumenal MVB vesicles are either recycled back to the plasma membrane or Golgi complex, or remain in the limiting membrane of the MVB and are thereby transported to the limiting membrane of the vacuole/lysosome as a consequence of fusion. Therefore, the MVB sorting pathway plays a critical role in the decision between recycling and degradation of membrane proteins. A few archaeal sequences are also present within this family.


Pssm-ID: 460896 [Multi-domain]  Cd Length: 168  Bit Score: 41.45  E-value: 2.04e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159648420  643 QKLIDELENSQRRLQTLKRQYEEKLMMLQHKIRdtqleRDQVLQNLGSVETYSEEKAKKIKSeyekkLQTMNKELQRLQT 722
Cdd:pfam03357    7 RKAIRKLDKKQESLEKKIEKLELEIKKLAKKGN-----KDAALLLLKQKKRYEKQLDQLDGQ-----LSNLEQQRMAIEN 76

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|..
gi 1159648420  723 AqKEHARLLKNQSQYEKQLKKLQQEvteMKKTKV-RLMKQMKEEQEKARMTE 773
Cdd:pfam03357   77 A-KSNQEVLNAMKQGAKAMKAMNKL---MDIDKIdKLMDEIEDQMEKADEIS 124
Tropomyosin pfam00261
Tropomyosin; Tropomyosin is an alpha-helical protein that forms a coiled-coil structure of 2 ...
 742-818 2.27e-03

Tropomyosin; Tropomyosin is an alpha-helical protein that forms a coiled-coil structure of 2 parallel helices containing 2 sets of 7 alternating actin binding sites. The protein is best known for its role in regulating the interaction between actin and myosin in muscle contraction, but is also involved in the organization and dynamics of the cytoskeleton in non-muscle cells. There are multiple cell-specific isoforms, expressed by alternative promoters and alternative RNA processing of at least four genes. Muscle isoforms of tropomyosin are characterized by having 284 amino acid residues and a highly conserved N-terminal region, whereas non-muscle forms are generally smaller and are heterogeneous in their N-terminal region.


Pssm-ID: 459736 [Multi-domain]  Cd Length: 235  Bit Score: 41.94  E-value: 2.27e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159648420  742 KKLQQEVTEMKKTKVRL---MKQMKEEQEKARMTESRR---NREIAQLKKEQRKREHQL-----KLLEAQKRNQEVILRR 810
Cdd:pfam00261    1 KKMQQIKEELDEAEERLkeaMKKLEEAEKRAEKAEAEVaalNRRIQLLEEELERTEERLaealeKLEEAEKAADESERGR 80


                   ....*...
gi 1159648420  811 KTEEVTAL 818
Cdd:pfam00261   81 KVLENRAL 88
Myosin_tail_1 pfam01576
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ...
 696-859 2.38e-03

Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.


Pssm-ID: 460256 [Multi-domain]  Cd Length: 1081  Bit Score: 43.24  E-value: 2.38e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159648420  696 EEKAKKIKsEYEKKLQTMNKELQrlqtaqKEHARLLKNQSQYEKQLKKLQQEVTEMKKTKVRLMKQMKEEQEKARMTESR 775
Cdd:pfam01576   11 EEELQKVK-ERQQKAESELKELE------KKHQQLCEEKNALQEQLQAETELCAEAEEMRARLAARKQELEEILHELESR 83

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159648420  776 RNRE---IAQLKKEQRKREHQLKLLEAQKRNQEVIlRRK--TEEVTA------LRRQVRPLSDKvAGKVSRKLSLPEHPI 844
Cdd:pfam01576   84 LEEEeerSQQLQNEKKKMQQHIQDLEEQLDEEEAA-RQKlqLEKVTTeakikkLEEDILLLEDQ-NSKLSKERKLLEERI 161

                          170
                   ....*....|....*
gi 1159648420  845 QEPSSSSSVEHDGSR 859
Cdd:pfam01576  162 SEFTSNLAEEEEKAK 176
ClpA COG0542
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein ...
 705-817 2.42e-03

ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 440308 [Multi-domain]  Cd Length: 836  Bit Score: 43.15  E-value: 2.42e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159648420  705 EYEKKLQTMNKELQRLQTAQKE--HARLlknqSQYEKQLKKLQQEVTEMKKtkvrlmkqmKEEQEKARMTESRRNRE-IA 781
Cdd:COG0542    415 ELERRLEQLEIEKEALKKEQDEasFERL----AELRDELAELEEELEALKA---------RWEAEKELIEEIQELKEeLE 481

                           90       100       110
                   ....*....|....*....|....*....|....*.
gi 1159648420  782 QLKKEQRKREHQLKLLEAQKRNQEVILRrktEEVTA 817
Cdd:COG0542    482 QRYGKIPELEKELAELEEELAELAPLLR---EEVTE 514
DASH_Spc19 pfam08287
Spc19; Spc19 is a component of the DASH complex. The DASH complex associates with the spindle ...
 626-730 2.49e-03

Spc19; Spc19 is a component of the DASH complex. The DASH complex associates with the spindle pole body and is important for spindle and kinetochore integrity during cell division.


Pssm-ID: 429900 [Multi-domain]  Cd Length: 148  Bit Score: 40.69  E-value: 2.49e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159648420  626 ENYQADLAN-ITCEIaikQKLIDELENS----QRRLQTLKRQYEeklmmlqhkirdtqlERDQVLQNLGSVETYSEEKAK 700
Cdd:pfam08287   50 EAAKASLREeIEPQI---DELLDKAEKSleklERREETLKAKLE---------------LNEGRLSNAESSARDEEGSQE 111

                           90       100       110
                   ....*....|....*....|....*....|
gi 1159648420  701 KIKSEYEKKLQTMNKELQRLQTAQKEHARL 730
Cdd:pfam08287  112 SDEEVNSSEGDATNEELERLRALRQKKERL 141
BRE1 pfam08647
BRE1 E3 ubiquitin ligase; BRE1 is an E3 ubiquitin ligase that has been shown to act as a ...
 714-800 2.63e-03

BRE1 E3 ubiquitin ligase; BRE1 is an E3 ubiquitin ligase that has been shown to act as a transcriptional activator through direct activator interactions.


Pssm-ID: 462547 [Multi-domain]  Cd Length: 95  Bit Score: 39.10  E-value: 2.63e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159648420  714 NKELQRLQTAQKE-HARLLKNQSQY---EKQLKKLQQEVTEMKKTKVRLMKQMKE---EQEKARMTESRRNREIAQLKKE 786
Cdd:pfam08647    2 QTELVKLEQAFEElSEQLDKKVKDLtilEEKKLRLEAEKAKADQKYFAAMRSKDAlenENKKLNTLLSKSSELIEQLKET 81

                           90
                   ....*....|....
gi 1159648420  787 QRKREHQLKLLEAQ 800
Cdd:pfam08647   82 EKEFVRKLKNLEKE 95
Nup88 pfam10168
Nuclear pore component; Nup88 can be divided into two structural domains; the N-terminal ...
 643-763 2.66e-03

Nuclear pore component; Nup88 can be divided into two structural domains; the N-terminal two-thirds of the protein has no obvious structural motifs but is the region for binding to Nup98, one of the components of the nuclear pore. the C-terminal end is a predicted coiled-coil domain. Nup88 is overexpressed in tumour cells.


Pssm-ID: 462975 [Multi-domain]  Cd Length: 713  Bit Score: 43.11  E-value: 2.66e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159648420  643 QKLIDELENSQRRLQTLKRQYEEklmmlqhkIRDTQ---LER-DQVLQNLGSVETYSEEKAKKIKSE---YEKKLQTMNK 715
Cdd:pfam10168  578 QSLEEERKSLSERAEKLAEKYEE--------IKDKQeklMRRcKKVLQRLNSQLPVLSDAEREMKKEletINEQLKHLAN 649

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 1159648420  716 EL---------QRLQTAQKEHARLLKNQSQYEKQLKKLQQEVTEMKKTKVRLMKQMK 763
Cdd:pfam10168  650 AIkqakkkmnyQRYQIAKSQSIRKKSSLSLSEKQRKTIKEILKQLGSEIDELIKQVK 706
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
724-955 2.78e-03

Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 42.83  E-value: 2.78e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159648420  724 QKEHARLLKNQSQ----YEKQLKKLQQEVTEMKKTKVRLmKQMKEEQEKARmtesrrnREIAQLKKEQRKREHQLKLLEA 799
Cdd:COG4717     52 EKEADELFKPQGRkpelNLKELKELEEELKEAEEKEEEY-AELQEELEELE-------EELEELEAELEELREELEKLEK 123

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159648420  800 QKRNQEVILRRKteevtALRRQVRPLSDKVagkvsRKLSLPEHPIQEpsssssVEHDGSRIAAQQkmripvarvqalsvt 879
Cdd:COG4717    124 LLQLLPLYQELE-----ALEAELAELPERL-----EELEERLEELRE------LEEELEELEAEL--------------- 172

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1159648420  880 atngtgRKYQRKAVTSRVYSSRAARMKWQLLERRVTDIIMQRMTIsnmEADMNRLLTQREELTKRREKLSKRREKL 955
Cdd:COG4717    173 ------AELQEELEELLEQLSLATEEELQDLAEELEELQQRLAEL---EEELEEAQEELEELEEELEQLENELEAA 239
XRCC4 pfam06632
DNA double-strand break repair and V(D)J recombination protein XRCC4; This family consists of ...
 688-776 2.92e-03

DNA double-strand break repair and V(D)J recombination protein XRCC4; This family consists of several eukaryotic DNA double-strand break repair and V(D)J recombination protein XRCC4 sequences. In the non-homologous end joining pathway of DNA double-strand break repair, the ligation step is catalyzed by a complex of XRCC4 and DNA ligase IV. It is thought that XRCC4 and ligase IV are essential for alignment-based gap filling, as well as for final ligation of the breaks.


Pssm-ID: 369011 [Multi-domain]  Cd Length: 336  Bit Score: 42.40  E-value: 2.92e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159648420  688 LGSVE-TYSEEKAKKIKSEYEKKLQTMNKELQRLQTAQKEHARLLKNQSQYEKQLKK-------LQQE-------VTEMK 752
Cdd:pfam06632  112 LGSVKlQKVPEPAEVIRELISYCLDCIAELQAKNEHLQKENERLQRDWNDVTGRLEKcvkakeeLEADlykrfilVLNEK 191

                           90       100
                   ....*....|....*....|....*
gi 1159648420  753 KTKVR-LMKQMKEEQEKARMTESRR 776
Cdd:pfam06632  192 KAKIRsLQKLLNELQESEESTEQKR 216
Lipase_chap pfam03280
Proteobacterial lipase chaperone protein;
627-786 2.92e-03

Proteobacterial lipase chaperone protein;


Pssm-ID: 427230 [Multi-domain]  Cd Length: 185  Bit Score: 41.14  E-value: 2.92e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159648420  627 NYQADLANITCEIAIKQKLIDELENSQRRLQTLKRQY-----EEKLMMLQHKIRDTQLERDQVLQNLGsveTYSEEKAKK 701
Cdd:pfam03280    7 AYKEALAELDAPAPALGDSLAALRARLEQLQALRRRYfspeeADALFGEEEAYDRYALERLAIAQDSA---LSAEEKQQR 83

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159648420  702 IKsEYEKKL----QTMNKELQRLQTAQKEHARLLKN----QSQYEKQ-----------LKKLQQEVTEMkKTKVRLMKQM 762
Cdd:pfam03280   84 LA-ALRAQLpedlRAAREAQQRLQELAARTAQLQKAgaspQQLRQARaqlvgpeaaqrLAALDQQRAAW-QQRLDDYLAE 161

                          170       180
                   ....*....|....*....|....
gi 1159648420  763 KEEQEKARMTESRRNREIAQLKKE 786
Cdd:pfam03280  162 RQQINAAGLSEQERQAAIAQLRQQ 185
Spc7 smart00787
Spc7 kinetochore protein; This domain is found in cell division proteins which are required ...
 939-1033 3.28e-03

Spc7 kinetochore protein; This domain is found in cell division proteins which are required for kinetochore-spindle association.


Pssm-ID: 197874 [Multi-domain]  Cd Length: 312  Bit Score: 42.31  E-value: 3.28e-03
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159648420   939 EELTKRREKLSKRREKLMkdgggsETDRNVQNINEEMESLTANIDYINDSISDCQANIMQMEEAKEEgetldvtavINAC 1018
Cdd:smart00787  204 TELDRAKEKLKKLLQEIM------IKVKKLEELEEELQELESKIEDLTNKKSELNTEIAEAEKKLEQ---------CRGF 268

                            90
                    ....*....|....*
gi 1159648420  1019 TLTEARYLLDHFLTM 1033
Cdd:smart00787  269 TFKEIEKLKEQLKLL 283
CHASE3 COG5278
Extracytoplasmic sensor domain CHASE3 (specificity unknown) [Signal transduction mechanisms];
626-1071 3.50e-03

Extracytoplasmic sensor domain CHASE3 (specificity unknown) [Signal transduction mechanisms];


Pssm-ID: 444089 [Multi-domain]  Cd Length: 530  Bit Score: 42.59  E-value: 3.50e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159648420  626 ENYQADLANITCEIAIKQKLIDELENSQRRLQTLKRQYEEKLMMLQHKI---RDTQLERDQVLQNLGSVETYSEEkAKKI 702
Cdd:COG5278     79 EPYEEARAEIDELLAELRSLTADNPEQQARLDELEALIDQWLAELEQVIalrRAGGLEAALALVRSGEGKALMDE-IRAR 157

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159648420  703 KSEYEKKLQTMNKELQRLQTAQKEHARLLKNQSQYEKQLKKLQQEVTEMKKTKVRLMKQMKEEQEKARMTESRRNREIAQ 782
Cdd:COG5278    158 LLLLALALAALLLAAAALLLLLLALAALLALAELLLLALARALAALLLLLLLEAELAAAAALLAAAAALAALAALELLAA 237

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159648420  783 LKKEQRKREHQLKLLEAQKRNQEVILRRKTEEVTALRRQVRPLSDKVAGKVSRKLSLPEHPIQEpsSSSSVEHDGSRIAA 862
Cdd:COG5278    238 LALALALLLAALLLALLAALALAALLAAALLALAALLLALAAAAALAAAAALELAAAEALALAE--LELELLLAAAAAAA 315

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159648420  863 QQKMRIPVARVQALSVTATNGTGRKYQRKAVTSRVYSSRAARMKWQLLERRVTDIIMQRMTISNMEADMNRLLTQREELT 942
Cdd:COG5278    316 AAAAAAAAALAALLALALATALAAAAAALALLAALLAEAAAAAAEEAEAAAEAAAAALAGLAEVEAEGAAEAVELEVLAI 395

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159648420  943 KRREKLSKRREKLMKDGGGSETDRNVQNINEEMESLTANIDYINDSISDCQANIMQMEEAKEEGETLDVTAVINActlte 1022
Cdd:COG5278    396 AAAAAAAAAEAAAAAAAAAAASAAEALELAEALAEALALAEEEALALAAASSELAEAGAALALAAAEALAEELAA----- 470

                          410       420       430       440
                   ....*....|....*....|....*....|....*....|....*....
gi 1159648420 1023 ARYLLDHFLTMGINKGLQAAQKEAQIKVLEGRLKQTEITSATQNQLLFH 1071
Cdd:COG5278    471 VAALAALAAAAAALAEAEAAAALAAAAALSLALALAALLLAAAEAALAA 519
KASH_CCD pfam14662
Coiled-coil region of CCDC155 or KASH; This coiled-coil region is found in the central part of ...
 646-822 3.63e-03

Coiled-coil region of CCDC155 or KASH; This coiled-coil region is found in the central part of KASH or Klarsicht/ANC-1/Syne/homology proteins. KASH are a meiosis-specific proteins that localize at telomeres and interact with SUN1, thus being implicated in meiotic chromosome dynamics and homolog pairing.


Pssm-ID: 405365 [Multi-domain]  Cd Length: 191  Bit Score: 40.93  E-value: 3.63e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159648420  646 IDELENSQRRLQ----TLKRQYEEKLMMLQHKIRDTQLERDQVLQNLGSVEtyseeKAKKIKSEYEKKLQTMNkELQRLQ 721
Cdd:pfam14662   10 VEDLQANNQKLLqensKLKATVETREETNAKLLEENLNLRKQAKSQQQAVQ-----KEKLLEEELEDLKLIVN-SLEEAR 83

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159648420  722 TAQKEHARLLK--NQSQYEKQLkKLQQEVTEMKKTKVRLMKQMKEeqekarmtesrrnreiaqLKKEQRKREHQLKLLEA 799
Cdd:pfam14662   84 RSLLAQNKQLEkeNQSLLQEIE-SLQEENKKNQAERDKLQKKKKE------------------LLKSKACLKEQLHSCED 144

                          170       180
                   ....*....|....*....|...
gi 1159648420  800 QKRNQEVILRRKTEEVTALRRQV 822
Cdd:pfam14662  145 LACNRETILIEKTTQIEELKSTV 167
PspA COG1842
Phage shock protein A [Transcription, Signal transduction mechanisms];
644-770 3.97e-03

Phage shock protein A [Transcription, Signal transduction mechanisms];


Pssm-ID: 441447 [Multi-domain]  Cd Length: 217  Bit Score: 41.35  E-value: 3.97e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159648420  644 KLIDELENSQRRLQTLKRQYEEKL---------MMLQHKirdtQLERdQVLQNLGSVETYsEEKAKKIKS--------EY 706
Cdd:COG1842     16 ALLDKAEDPEKMLDQAIRDMEEDLvearqalaqVIANQK----RLER-QLEELEAEAEKW-EEKARLALEkgredlarEA 89

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1159648420  707 EKKLQTMNKELQRLQTaqkEHARLLKNQSQYEKQLKKLQQEVTEMkKTKVRLMKqMKEEQEKAR 770
Cdd:COG1842     90 LERKAELEAQAEALEA---QLAQLEEQVEKLKEALRQLESKLEEL-KAKKDTLK-ARAKAAKAQ 148
Gal_mutarotas_2 pfam13802
Galactose mutarotase-like; This family is found N-terminal to glycosyl-hydrolase domains, and ...
 1833-1892 4.15e-03

Galactose mutarotase-like; This family is found N-terminal to glycosyl-hydrolase domains, and appears to be similar to the galactose mutarotase superfamily.


Pssm-ID: 463987 [Multi-domain]  Cd Length: 67  Bit Score: 37.83  E-value: 4.15e-03
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1159648420 1833 VYGFGEqehesfkHSMDFV----TYGMFSRDQAPTPL--VNLYGVHPFYMCVEaDSNAHGVLLLNS 1892
Cdd:pfam13802    4 VYGLGE-------RAGPLNkrgtRYRLWNTDAFGYELdtDPLYKSIPFYISHN-GGRGYGVFWDNP 61
UDM1_RNF168_RNF169-like cd22249
UDM1 (ubiquitin-dependent DSB recruitment module 1) found in RING finger proteins RNF168, ...
 737-806 4.24e-03

UDM1 (ubiquitin-dependent DSB recruitment module 1) found in RING finger proteins RNF168, RNF169 and similar proteins; This model represents the UDM1 (ubiquitin-dependent double-strand break [DSB] recruitment module 1) found in RING finger proteins, RNF168 and RNF169. RNF168 is an E3 ubiquitin-protein ligase that promotes non-canonical K27 ubiquitination to signal DNA damage. It functions, together with RNF8, as a DNA damage response (DDR) factor that promotes a series of ubiquitylation events on substrates such as H2A and H2AX. With H2AK13/15 ubiquitylation, it facilitates recruitment of repair factors p53-binding protein 1 (53BP1) or the RAP80-BRCA1 complex to sites of double-strand breaks (DSBs), and inhibits homologous recombination (HR) in cells deficient in the tumor suppressor BRCA1. RNF168 also promotes H2A neddylation, which antagonizes ubiquitylation of H2A and regulates DNA damage repair. In addition, RNF168 forms a functional complex with RAD6A or RAD6B during the DNA damage response. RNF169 is an uncharacterized E3 ubiquitin-protein ligase paralogous to RNF168. It functions as a negative regulator of the DNA damage signaling cascade. RNF169 recognizes polyubiquitin structures but does not itself contribute to double-strand break (DSB)-induced chromatin ubiquitylation. It contributes to the regulation of DSB repair pathway utilization via functionally competing with recruiting repair factors, 53BP1 and RAP80-BRCA1, for association with RNF168-modified chromatin, independent of its catalytic activity, limiting the magnitude of the RNF8/RNF168-dependent signaling response to DSBs. The UDM1 domain comprises LRM1 (LR motif 1), UMI (ubiquitin-interacting motif [UIM]- and MIU-related UBD) and MIU1 (motif interacting with ubiquitin 1). Mutations of Ub-interacting residues in UDM1 have little effect on the accumulation of RNF168 to DSB sites, suggesting that it may not be the main site of binding ubiquitylated and polyubiquitylated targets.


Pssm-ID: 409016 [Multi-domain]  Cd Length: 66  Bit Score: 37.63  E-value: 4.24e-03
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159648420  737 YEKQLKKLQQEvtemkktkvrlMKQMKEEQEKARMtesrrnrEIAQLKKEQRKREHQLKLLEAQKRNQEV 806
Cdd:cd22249     11 YEAQLKKLEEE-----------RRKEREEEEKASE-------ELIRKLQEEEERQRKREREEQLKQDEEL 62
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
629-837 4.57e-03

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 41.81  E-value: 4.57e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159648420  629 QADLANITCEIAIKQKLIDELENSQRRLQTLKRQYEEKLMMLQHKI--RDTQLE--RDQVLQNLGSVETYSEEKAKKIKS 704
Cdd:COG4372    100 QEELESLQEEAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIaeREEELKelEEQLESLQEELAALEQELQALSEA 179

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159648420  705 EYEKKLQTMNKELQRLQTAQKEHARLLKNQ-SQYEKQLKKLQQEVTEMKKTKVRLMKQMKEEQEKARMTESRRNREIAQL 783
Cdd:COG4372    180 EAEQALDELLKEANRNAEKEEELAEAEKLIeSLPRELAEELLEAKDSLEAKLGLALSALLDALELEEDKEELLEEVILKE 259

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....
gi 1159648420  784 KKEQRKREHQLKLLEAQKRNQEVILRRKTEEVTALRRQVRPLSDKVAGKVSRKL 837
Cdd:COG4372    260 IEELELAILVEKDTEEEELEIAALELEALEEAALELKLLALLLNLAALSLIGAL 313
PRK02224 PRK02224
DNA double-strand break repair Rad50 ATPase;
385-1009 4.72e-03

DNA double-strand break repair Rad50 ATPase;


Pssm-ID: 179385 [Multi-domain]  Cd Length: 880  Bit Score: 42.33  E-value: 4.72e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159648420  385 QINALRSEIARLQMELMEYKTgKRIIDEEGVESINDMFHENAMLQTENNNLRVRIKAMQETV-------DALRARITQL- 456
Cdd:PRK02224   207 RLNGLESELAELDEEIERYEE-QREQARETRDEADEVLEEHEERREELETLEAEIEDLRETIaetererEELAEEVRDLr 285

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159648420  457 -----MSDQANQVLARAGEGNeeisnmihnyiKEIEDLRAKLLESEAVNENLRRNLSRASTrstyfggpsafSASMLSSE 531
Cdd:PRK02224   286 erleeLEEERDDLLAEAGLDD-----------ADAEAVEARREELEDRDEELRDRLEECRV-----------AAQAHNEE 343

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159648420  532 KETLeildiakkdleklkkkerkkkksvkEDNTDNEQEKRDEKgsseREnnelEAEEIqeasdredeeeeddededdmev 611
Cdd:PRK02224   344 AESL-------------------------REDADDLEERAEEL----RE----EAAEL---------------------- 368

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159648420  612 vessdesdsdsdekenyQADLANITCEIAIKQKLIDELENsqrRLQTLKRQYE---EKLMMLQHKIRDTQLERDQVLQNL 688
Cdd:PRK02224   369 -----------------ESELEEAREAVEDRREEIEELEE---EIEELRERFGdapVDLGNAEDFLEELREERDELRERE 428

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159648420  689 GSVETYSEEKAKKIkseyekklqtmnKELQRLQTAQK-----------EHARLLknqSQYEKQLKKLQQEVTEMKKTKVR 757
Cdd:PRK02224   429 AELEATLRTARERV------------EEAEALLEAGKcpecgqpvegsPHVETI---EEDRERVEELEAELEDLEEEVEE 493

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159648420  758 LMKQMkEEQEKARMTESRRNReiaqlKKEQRKREHQLKlleAQKRNqevILRRKTEEVTALRRQVRPLSDkvagkvsrkl 837
Cdd:PRK02224   494 VEERL-ERAEDLVEAEDRIER-----LEERREDLEELI---AERRE---TIEEKRERAEELRERAAELEA---------- 551

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159648420  838 slpehpiqepsssssvEHDGSRIAAQQKM-RIPVARVQalsVTATNGtgrkyQRKAVTSRVYSsraarmkwqlLERRVTD 916
Cdd:PRK02224   552 ----------------EAEEKREAAAEAEeEAEEAREE---VAELNS-----KLAELKERIES----------LERIRTL 597

                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159648420  917 IimqrMTISNMEADMNRLLTQREEL----TKRREKLSKRREKLMK-----DGGGSETDRN--------VQNINEEMESLT 979
Cdd:PRK02224   598 L----AAIADAEDEIERLREKREALaelnDERRERLAEKRERKREleaefDEARIEEAREdkeraeeyLEQVEEKLDELR 673

                          650       660       670
                   ....*....|....*....|....*....|
gi 1159648420  980 ANIDYINDSISDCQANIMQMEEAKEEGETL 1009
Cdd:PRK02224   674 EERDDLQAEIGAVENELEELEELRERREAL 703
PspA_IM30 pfam04012
PspA/IM30 family; This family includes PspA a protein that suppresses sigma54-dependent ...
 645-830 4.76e-03

PspA/IM30 family; This family includes PspA a protein that suppresses sigma54-dependent transcription. The PspA protein, a negative regulator of the Escherichia coli phage shock psp operon, is produced when virulence factors are exported through secretins in many Gram-negative pathogenic bacteria and its homolog in plants, VIPP1, plays a critical role in thylakoid biogenesis, essential for photosynthesis. Activation of transcription by the enhancer-dependent bacterial sigma(54) containing RNA polymerase occurs through ATP hydrolysis-driven protein conformational changes enabled by activator proteins that belong to the large AAA(+) mechanochemical protein family. It has been shown that PspA directly and specifically acts upon and binds to the AAA(+) domain of the PspF transcription activator.


Pssm-ID: 461130 [Multi-domain]  Cd Length: 215  Bit Score: 40.82  E-value: 4.76e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159648420  645 LIDELENSQRrlqtlkrqyeeklmMLQHKIRDTQLERDQVLQNLgsvetyseEKAKKIKSEYEKKLQTMNKELQRLQtaQ 724
Cdd:pfam04012   16 GLDKAEDPEK--------------MLEQAIRDMQSELVKARQAL--------AQTIARQKQLERRLEQQTEQAKKLE--E 71

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159648420  725 KEHARLLKNQSQYEK----QLKKLQQEVTEMKKtkvrLMKQMKEEQEKARMTESRRNREIAQLKKEQRKrehqLKL-LEA 799
Cdd:pfam04012   72 KAQAALTKGNEELARealaEKKSLEKQAEALET----QLAQQRSAVEQLRKQLAALETKIQQLKAKKNL----LKArLKA 143

                          170       180       190
                   ....*....|....*....|....*....|.
gi 1159648420  800 QKRNQEVILRRKTEEVTALRRQVRPLSDKVA 830
Cdd:pfam04012  144 AKAQEAVQTSLGSLSTSSATDSFERIEEKIE 174
atpG CHL00118
ATP synthase CF0 B' subunit; Validated
 680-787 4.87e-03

ATP synthase CF0 B' subunit; Validated


Pssm-ID: 214369 [Multi-domain]  Cd Length: 156  Bit Score: 39.97  E-value: 4.87e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159648420  680 ERDQVLQNlgSVETYSE--EKAKKIKSEYEKKLQTMNKELQ-RLQTAQKEHARLLknqsqyEKQLKKLQQEVTEMKKTkv 756
Cdd:CHL00118    53 ERKEYIRK--NLTKASEilAKANELTKQYEQELSKARKEAQlEITQSQKEAKEIV------ENELKQAQKYIDSLLNE-- 122

                           90       100       110
                   ....*....|....*....|....*....|.
gi 1159648420  757 rLMKQMKEEQEKARMTESRRNREIAQLKKEQ 787
Cdd:CHL00118   123 -ATKQLEAQKEKALKSLEEQVDTLSDQIEEK 152
flagell_FliJ TIGR02473
flagellar export protein FliJ; Members of this family are the FliJ protein found, in nearly ...
 655-784 4.96e-03

flagellar export protein FliJ; Members of this family are the FliJ protein found, in nearly every case, in the midst of other flagellar biosynthesis genes in bacgterial genomes. Typically the fliJ gene is found adjacent to the gene for the flagellum-specific ATPase FliI. Sequence scoring in the gray zone between trusted and noise cutoffs include both probable FliJ proteins and components of bacterial type III secretion systems.


Pssm-ID: 131526 [Multi-domain]  Cd Length: 141  Bit Score: 39.61  E-value: 4.96e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159648420  655 RLQTLKRQYEEKLMM-LQHKIRDTQLERDQVLQNLGSVETYSEEKAKKIKSEYE-KKLQTMNKELQRLQTAQKEHARLL- 731
Cdd:TIGR02473    6 KLLDLREKEEEQAKLeLAKAQAEFERLETQLQQLIKYREEYEQQALEKVGAGTSaLELSNYQRFIRQLDQRIQQQQQELa 85

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|...
gi 1159648420  732 KNQSQYEKQLKKLQQEVTEMKKTKVRLMKQMKEEQEKARMTESRRNREIAQLK 784
Cdd:TIGR02473   86 LLQQEVEAKRERLLEARRELKALEKLKEKKQKEYRAEEAKREQKEMDELATQR 138
HOOK pfam05622
HOOK protein coiled-coil region; This family consists of several HOOK1, 2 and 3 proteins from ...
 643-841 5.06e-03

HOOK protein coiled-coil region; This family consists of several HOOK1, 2 and 3 proteins from different eukaryotic organizms. The different members of the human gene family are HOOK1, HOOK2 and HOOK3. Different domains have been identified in the three human HOOK proteins, and it was demonstrated that the highly conserved NH2-domain mediates attachment to microtubules, whereas this central coiled-coil motif mediates homodimerization and the more divergent C-terminal domains are involved in binding to specific organelles (organelle-binding domains). It has been demonstrated that endogenous HOOK3 binds to Golgi membranes, whereas both HOOK1 and HOOK2 are localized to discrete but unidentified cellular structures. In mice the Hook1 gene is predominantly expressed in the testis. Hook1 function is necessary for the correct positioning of microtubular structures within the haploid germ cell. Disruption of Hook1 function in mice causes abnormal sperm head shape and fragile attachment of the flagellum to the sperm head. This entry includes the central coiled-coiled domain and the divergent C-terminal domain.


Pssm-ID: 461694 [Multi-domain]  Cd Length: 528  Bit Score: 41.98  E-value: 5.06e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159648420  643 QKLIDELENSQRRLQTLKRQY----EEKLMMLQ--HKIRDtQLERDQVLQNLGSVetyseeKAKKIkSEYEKKLQTMNKE 716
Cdd:pfam05622    3 SEAQEEKDELAQRCHELDQQVsllqEEKNSLQQenKKLQE-RLDQLESGDDSGTP------GGKKY-LLLQKQLEQLQEE 74

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159648420  717 LQRLQTAqKEHARLlKNQSQyEKQLKKLQQEVTEMKKtkvrlmkqmkeeqekarMTEsrrnrEIAQLKKEQ---RKREHQ 793
Cdd:pfam05622   75 NFRLETA-RDDYRI-KCEEL-EKEVLELQHRNEELTS-----------------LAE-----EAQALKDEMdilRESSDK 129

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*...
gi 1159648420  794 LKLLEAQKRnqevILRRKTEEVTALRRQVRPLSDKVAGKVSRKLSLPE 841
Cdd:pfam05622  130 VKKLEATVE----TYKKKLEDLGDLRRQVKLLEERNAEYMQRTLQLEE 173
V_HD-PTP_like cd09234
Protein-interacting V-domain of mammalian His-Domain type N23 protein tyrosine phosphatase and ...
 642-813 5.18e-03

Protein-interacting V-domain of mammalian His-Domain type N23 protein tyrosine phosphatase and related domains; This family contains the V-shaped (V) domain of mammalian His-Domain type N23 protein tyrosine phosphatase (HD-PTP, also known as PTPN23) and related domains. It belongs to the V_Alix_like superfamily which includes the V domains of Bro1 and Rim20 (also known as PalA) from Saccharomyces cerevisiae, mammalian Alix (apoptosis-linked gene-2 interacting protein X/ also known as apoptosis-linked gene-2 interacting protein 1, AIP1), and related domains. HD_PTP interacts with the ESCRT (Endosomal Sorting Complexes Required for Transport) system, and participates in cell migration and endosomal trafficking. The related Alix V-domain (belonging to a different family in this superfamily) contains a binding site, partially conserved in the superfamily, for the retroviral late assembly (L) domain YPXnL motif. The Alix V-domain is also a dimerization domain. In addition to the V-domain, HD_PTP also has an N-terminal Bro1-like domain, a proline-rich region (PRR), a catalytically inactive tyrosine phosphatase domain, and a region containing a PEST motif. Bro1-like domains bind components of the ESCRT-III complex, specifically to CHMP4 in the case of HD-PTP. The Bro1-like domain of HD-PTP can also bind human immunodeficiency virus type 1 (HIV-1) nucleocapsid. HD-PTP is encoded by the PTPN23 gene, a tumor suppressor gene candidate frequently absent in human kidney, breast, lung, and cervical tumors. This family also contains Drosophila Myopic, which promotes epidermal growth factor receptor (EGFR) signaling, and Caenorhabditis elegans (enhancer of glp-1) EGO-2 which promotes Notch signaling.


Pssm-ID: 185747 [Multi-domain]  Cd Length: 337  Bit Score: 41.51  E-value: 5.18e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159648420  642 KQKLIDELENSQRRLQTLKRQYEEKLMMLQHKIRDTQLERDQVLQNLGSVETySEEKAKKIKSEYEK------KLQTMNK 715
Cdd:cd09234     70 RPDTIKNLVEAMGELSDVYQDVEAMLNEIESLLEEEELQEKEFQEAVGKRGS-SIAHVTELKRELKKykeaheKASQSNT 148

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159648420  716 ELQRLQTAQKEHARLLK-------------------NQSQYEKQLKKLQQEVTEMKKTKVRLMKQMKEEQEKARMTES-- 774
Cdd:cd09234    149 ELHKAMNLHIANLKLLAgpldelqkklpspslldrpEDEAIEKELKRILNKVNEMRKQRRSLEQQLRDAIHEDDITSKlv 228

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|.
gi 1159648420  775 -RRNREIAQLKKEQRKREHQLK-LLEAQKRNQEVILRRKTE 813
Cdd:cd09234    229 tTTGGDMEDLFKEELKKHDQLVnLIEQNLAAQENILKALTE 269
AtpF COG0711
FoF1-type ATP synthase, membrane subunit b or b' [Energy production and conversion]; FoF1-type ...
 696-836 5.36e-03

FoF1-type ATP synthase, membrane subunit b or b' [Energy production and conversion]; FoF1-type ATP synthase, membrane subunit b or b' is part of the Pathway/BioSystem: FoF1-type ATP synthase


Pssm-ID: 440475 [Multi-domain]  Cd Length: 152  Bit Score: 39.77  E-value: 5.36e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159648420  696 EEKAKKIKSEyekklqtmnkeLQRLQTAQKEHARLLKnqsQYEKQLKKLQQEVTEMKKTKVRLMKQMKEE-QEKARmtes 774
Cdd:COG0711     30 DERQEKIADG-----------LAEAERAKEEAEAALA---EYEEKLAEARAEAAEIIAEARKEAEAIAEEaKAEAE---- 91

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1159648420  775 rrnREIAQLKKeqrkrehqlkllEAQKRnqevILRRKTEEVTALRRQVRPLSDKVAGKVSRK 836
Cdd:COG0711     92 ---AEAERIIA------------QAEAE----IEQERAKALAELRAEVADLAVAIAEKILGK 134
sbcc TIGR00618
exonuclease SbcC; All proteins in this family for which functions are known are part of an ...
 567-838 6.36e-03

exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]


Pssm-ID: 129705 [Multi-domain]  Cd Length: 1042  Bit Score: 41.88  E-value: 6.36e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159648420  567 EQEKRDEKGSSERENNELEAEEIQEASDREDEEEEDDEDEDDMEVVESSDESDSDSDEKEnyqadlanitcEIAIKQKLI 646
Cdd:TIGR00618  638 SQELALKLTALHALQLTLTQERVREHALSIRVLPKELLASRQLALQKMQSEKEQLTYWKE-----------MLAQCQTLL 706

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159648420  647 DELENSqrrLQTLKRQYEEKLMMLQHKIRDTQLERDQVLQNLGSVETYSEEKAKKIKSEYEKKLQTMNKELQRLQtaqkE 726
Cdd:TIGR00618  707 RELETH---IEEYDREFNEIENASSSLGSDLAAREDALNQSLKELMHQARTVLKARTEAHFNNNEEVTAALQTGA----E 779

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159648420  727 HARLLKNQSQYEKQLKKLQQEvtemkktkvrlMKQMKEE-QEKARMTESRRNREIAQLKKEQRKREHQL----KLLEAQK 801
Cdd:TIGR00618  780 LSHLAAEIQFFNRLREEDTHL-----------LKTLEAEiGQEIPSDEDILNLQCETLVQEEEQFLSRLeeksATLGEIT 848

                          250       260       270
                   ....*....|....*....|....*....|....*....
gi 1159648420  802 RNQEVILRRKTEEVTALRRQVR--PLSDKVAGKVSRKLS 838
Cdd:TIGR00618  849 HQLLKYEECSKQLAQLTQEQAKiiQLSDKLNGINQIKIQ 887
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
374-707 6.46e-03

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 41.43  E-value: 6.46e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159648420  374 KVMVNQDRASQQINALRSEIARLQMEL------MEYKTGKRIIDEEGVESINDMFHEnamLQTENNNLRVRIKAMQETVD 447
Cdd:COG4372     35 KALFELDKLQEELEQLREELEQAREELeqleeeLEQARSELEQLEEELEELNEQLQA---AQAELAQAQEELESLQEEAE 111

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159648420  448 ALRARITQLMSDQAN--QVLARAGEGNEEISNMIHNYIKEIEDLRAKLLESEAVNENLRRNLSRASTRSTYfggpSAFSA 525
Cdd:COG4372    112 ELQEELEELQKERQDleQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAALEQELQALSEAEAE----QALDE 187

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159648420  526 SMLSSEKETLEILDIAKKDLEKLKKKERKKKKSVKEDNTDNEQEKRDEKGSSERENNELEAEEIQEASDREDEEEEDDED 605
Cdd:COG4372    188 LLKEANRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLGLALSALLDALELEEDKEELLEEVILKEIEELELAI 267

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159648420  606 EDDMEVVESSDESDSDSDEKENYQADlanitCEIAIKQKLIDELENSQRRLQT-LKRQYEEKLMMLQHKIRDTQLERDQV 684
Cdd:COG4372    268 LVEKDTEEEELEIAALELEALEEAAL-----ELKLLALLLNLAALSLIGALEDaLLAALLELAKKLELALAILLAELADL 342

                          330       340
                   ....*....|....*....|...
gi 1159648420  685 LQNLGSVETYSEEKAKKIKSEYE 707
Cdd:COG4372    343 LQLLLVGLLDNDVLELLSKGAEA 365
ALIX_LYPXL_bnd pfam13949
ALIX V-shaped domain binding to HIV; The binding of the LYPxL motif of late HIV p6Gag and EIAV ...
 641-822 6.54e-03

ALIX V-shaped domain binding to HIV; The binding of the LYPxL motif of late HIV p6Gag and EIAV p9Gag to this domain is necessary for viral budding.This domain is generally central between an N-terminal Bro1 domain, pfam03097 and a C-terminal proline-rich domain. The retroviruses thus used this domain to hijack the ESCRT system of the cell.


Pssm-ID: 464053 [Multi-domain]  Cd Length: 294  Bit Score: 41.07  E-value: 6.54e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159648420  641 IKQKLIDELENSQRRLQtlKRQYEEKLMMLQHKIRDTQLERDQVLQNL-GSVETYSE--EKAKK----IKSEY---EKKL 710
Cdd:pfam13949   32 LKQRNREILDEAEKLLD--EEESEDEQLRAKYGTRWTRPPSSELTATLrAEIRKYREilEQASEsdsqVRSKFrehEEDL 109

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159648420  711 QTMNKELQRLQTA---QKEHARLLKNQSQYEKqLKKLQQEVTEMKKTKVRLMKQMKEEQEK-----ARMTESRRNREIAQ 782
Cdd:pfam13949  110 ELLSGPDEDLEAFlpsSRRAKNSPSVEEQVAK-LRELLNKLNELKREREQLLKDLKEKARNddispKLLLEKARLIAPNQ 188

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 1159648420  783 ----LKKEQRKREHQLKLLEAQKRNQEVIL-------------RRKTEEVTALRRQV 822
Cdd:pfam13949  189 eeqlFEEELEKYDPLQNRLEQNLHKQEELLkeiteanneflqdKRVDSEKQRQREEA 245
UDM1_RNF168_RNF169-like cd22249
UDM1 (ubiquitin-dependent DSB recruitment module 1) found in RING finger proteins RNF168, ...
 698-765 6.80e-03

UDM1 (ubiquitin-dependent DSB recruitment module 1) found in RING finger proteins RNF168, RNF169 and similar proteins; This model represents the UDM1 (ubiquitin-dependent double-strand break [DSB] recruitment module 1) found in RING finger proteins, RNF168 and RNF169. RNF168 is an E3 ubiquitin-protein ligase that promotes non-canonical K27 ubiquitination to signal DNA damage. It functions, together with RNF8, as a DNA damage response (DDR) factor that promotes a series of ubiquitylation events on substrates such as H2A and H2AX. With H2AK13/15 ubiquitylation, it facilitates recruitment of repair factors p53-binding protein 1 (53BP1) or the RAP80-BRCA1 complex to sites of double-strand breaks (DSBs), and inhibits homologous recombination (HR) in cells deficient in the tumor suppressor BRCA1. RNF168 also promotes H2A neddylation, which antagonizes ubiquitylation of H2A and regulates DNA damage repair. In addition, RNF168 forms a functional complex with RAD6A or RAD6B during the DNA damage response. RNF169 is an uncharacterized E3 ubiquitin-protein ligase paralogous to RNF168. It functions as a negative regulator of the DNA damage signaling cascade. RNF169 recognizes polyubiquitin structures but does not itself contribute to double-strand break (DSB)-induced chromatin ubiquitylation. It contributes to the regulation of DSB repair pathway utilization via functionally competing with recruiting repair factors, 53BP1 and RAP80-BRCA1, for association with RNF168-modified chromatin, independent of its catalytic activity, limiting the magnitude of the RNF8/RNF168-dependent signaling response to DSBs. The UDM1 domain comprises LRM1 (LR motif 1), UMI (ubiquitin-interacting motif [UIM]- and MIU-related UBD) and MIU1 (motif interacting with ubiquitin 1). Mutations of Ub-interacting residues in UDM1 have little effect on the accumulation of RNF168 to DSB sites, suggesting that it may not be the main site of binding ubiquitylated and polyubiquitylated targets.


Pssm-ID: 409016 [Multi-domain]  Cd Length: 66  Bit Score: 37.25  E-value: 6.80e-03
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1159648420  698 KAKKIKSEYEKKLQTMNKELQRLQTAQkEHARllknqsqyEKQLKKLQQEVTEMKKTKVRLMKQMKEE 765
Cdd:cd22249      3 KPGEIREEYEAQLKKLEEERRKEREEE-EKAS--------EELIRKLQEEEERQRKREREEQLKQDEE 61
ATP-synt_Fo_b cd06503
F-type ATP synthase, membrane subunit b; Membrane subunit b is a component of the Fo complex ...
 646-751 6.83e-03

F-type ATP synthase, membrane subunit b; Membrane subunit b is a component of the Fo complex of FoF1-ATP synthase. The F-type ATP synthases (FoF1-ATPase) consist of two structural domains: the F1 (assembly factor one) complex containing the soluble catalytic core, and the Fo (oligomycin sensitive factor) complex containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. F1 is composed of alpha (or A), beta (B), gamma (C), delta (D) and epsilon (E) subunits with a stoichiometry of 3:3:1:1:1, while Fo consists of the three subunits a, b, and c (1:2:10-14). An oligomeric ring of 10-14 c subunits (c-ring) make up the Fo rotor. The flux of protons through the ATPase channel (Fo) drives the rotation of the c-ring, which in turn is coupled to the rotation of the F1 complex gamma subunit rotor due to the permanent binding between the gamma and epsilon subunits of F1 and the c-ring of Fo. The F-ATP synthases are primarily found in the inner membranes of eukaryotic mitochondria, in the thylakoid membranes of chloroplasts or in the plasma membranes of bacteria. The F-ATP synthases are the primary producers of ATP, using the proton gradient generated by oxidative phosphorylation (mitochondria) or photosynthesis (chloroplasts). Alternatively, under conditions of low driving force, ATP synthases function as ATPases, thus generating a transmembrane proton or Na(+) gradient at the expense of energy derived from ATP hydrolysis. This group also includes F-ATP synthase that has also been found in the archaea Candidatus Methanoperedens.


Pssm-ID: 349951 [Multi-domain]  Cd Length: 132  Bit Score: 38.96  E-value: 6.83e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159648420  646 IDELENSQRRLQTLKRQYEEKLmmlqhkiRDTQLERDQVLQNlgsvetySEEKAKKIKSEYekklqtmnkelqrLQTAQK 725
Cdd:cd06503     39 LEEAEKAKEEAEELLAEYEEKL-------AEARAEAQEIIEE-------ARKEAEKIKEEI-------------LAEAKE 91

                           90       100       110
                   ....*....|....*....|....*....|.
gi 1159648420  726 EHARLLKN-----QSQYEKQLKKLQQEVTEM 751
Cdd:cd06503     92 EAERILEQakaeiEQEKEKALAELRKEVADL 122
Cgr1 pfam03879
Cgr1 family; Members of this family are coiled-coil proteins that are involved in pre-rRNA ...
 742-823 7.24e-03

Cgr1 family; Members of this family are coiled-coil proteins that are involved in pre-rRNA processing.


Pssm-ID: 427562 [Multi-domain]  Cd Length: 107  Bit Score: 38.37  E-value: 7.24e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159648420  742 KKLQQEVTEMKKTKVRL--MKQMKEEQEKARMTESRRNREiaqlKKEQRKREHQLklleAQKRNQEVILRRKteevtalR 819
Cdd:pfam03879   33 EKRQEKRLELKAIKAKEkeLKDEKEAERQRRIQAIKERRE----AKEEKERYEEL----AAKMHAKKVERLK-------R 97


                   ....
gi 1159648420  820 RQVR 823
Cdd:pfam03879   98 KEKR 101
ClassIIa_HDAC9_Gln-rich-N cd10163
Glutamine-rich N-terminal helical domain of HDAC9, a Class IIa histone deacetylase; This ...
 708-779 7.28e-03

Glutamine-rich N-terminal helical domain of HDAC9, a Class IIa histone deacetylase; This family consists of the glutamine-rich domain of histone deacetylase 9 (HDAC9). It belongs to a superfamily that consists of the glutamine-rich N-terminal helical extension to certain Class IIa histone deacetylases (HDACs), including HDAC4, HDAC5 and HDCA9; it is missing from HDAC7. This domain confers responsiveness to calcium signals and mediates interactions with transcription factors and cofactors, and it is able to repress transcription independently of the HDAC C-terminal, zinc-dependent catalytic domain. It has many intra- and inter-helical interactions which are possibly involved in reversible assembly and disassembly of proteins. HDACs regulate diverse cellular processes through enzymatic deacetylation of histone as well as non-histone proteins, in particular deacetylating N(6)-acetyl-lysine residues.


Pssm-ID: 197399 [Multi-domain]  Cd Length: 90  Bit Score: 37.81  E-value: 7.28e-03
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1159648420  708 KKLQTMNKELQrLQTAQKEHARLLK-NQSQYEKQLKkLQQEVTEMKKTKVRLMKQMKEEQEKARMTESRRNRE 779
Cdd:cd10163     17 QQQQQIQKQLL-IAEFQKQHENLTRqHQAQLQEHLK-LQQELLAMKQQQELLEKEQKLEQQRQEQELERHRRE 87
CENP-F_leu_zip pfam10473
Leucine-rich repeats of kinetochore protein Cenp-F/LEK1; Cenp-F, a centromeric kinetochore, ...
 696-802 7.30e-03

Leucine-rich repeats of kinetochore protein Cenp-F/LEK1; Cenp-F, a centromeric kinetochore, microtubule-binding protein consisting of two 1,600-amino acid-long coils, is essential for the full functioning of the mitotic checkpoint pathway. There are several leucine-rich repeats along the sequence of LEK1 that are considered to be zippers, though they do not appear to be binding DNA directly in this instance.


Pssm-ID: 463102 [Multi-domain]  Cd Length: 140  Bit Score: 39.20  E-value: 7.30e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159648420  696 EEKAKKIKSE---YEKKLQTMNKELQRLQTAQkEHARLLKNQSQYE------------KQLKKLQQEVTEMKKTKVRLMK 760
Cdd:pfam10473    9 LEKLKESERKadsLKDKVENLERELEMSEENQ-ELAILEAENSKAEvetlkaeieemaQNLRDLELDLVTLRSEKENLTK 87

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*....
gi 1159648420  761 QMKEEQEKARMTESR----RNR-EIAQLKKEQRKREHQ--LKLLEAQKR 802
Cdd:pfam10473   88 ELQKKQERVSELESLnsslENLlEEKEQEKVQMKEESKtaVEMLQTQLK 136
ATG16 pfam08614
Autophagy protein 16 (ATG16); Autophagy is a ubiquitous intracellular degradation system for ...
 691-827 8.11e-03

Autophagy protein 16 (ATG16); Autophagy is a ubiquitous intracellular degradation system for eukaryotic cells. During autophagy, cytoplasmic components are enclosed in autophagosomes and delivered to lysosomes/vacuoles. ATG16 (also known as Apg16) has been shown to be bind to Apg5 and is required for the function of the Apg12p-Apg5p conjugate in the yeast autophagy pathway.


Pssm-ID: 462536 [Multi-domain]  Cd Length: 176  Bit Score: 39.53  E-value: 8.11e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159648420  691 VETYSE--EKAKKIKSEYEKKLQTMNKELQRLQ--TAQKEHARLLKNQSQyEKQLKKLQQEVTEMKKTKVRLMKQMKEeq 766
Cdd:pfam08614    6 IDAYNRllDRTALLEAENAKLQSEPESVLPSTSssKLSKASPQSASIQSL-EQLLAQLREELAELYRSRGELAQRLVD-- 82

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1159648420  767 ekarMTEsrrnrEIAQLKKEQRKREHQLKLLEAQKRNQEVILRRKTEEVTALRRQVRPLSD 827
Cdd:pfam08614   83 ----LNE-----ELQELEKKLREDERRLAALEAERAQLEEKLKDREEELREKRKLNQDLQD 134
235kDa-fam TIGR01612
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in ...
 354-806 8.31e-03

reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in plasmodium species alternately annotated as reticulocyte binding protein, 235-kDa family protein and rhoptry protein. Rhoptry protein is localized on the cell surface and is extremely large (although apparently lacking in repeat structure) and is important for the process of invasion of the RBCs by the parasite. These proteins are found in P. falciparum, P. vivax and P. yoelii.


Pssm-ID: 130673 [Multi-domain]  Cd Length: 2757  Bit Score: 41.96  E-value: 8.31e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159648420  354 DFMETLNtlKYANRARNIKNKVMVNQDRASQQINALRSEIARLQMELMEYKT--GKRIIDEEGvESINDMFHENAMLQTE 431
Cdd:TIGR01612  843 DFLNKVD--KFINFENNCKEKIDSEHEQFAELTNKIKAEISDDKLNDYEKKFndSKSLINEIN-KSIEEEYQNINTLKKV 919

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159648420  432 NNNLRVrIKAMQETVDALRARITQLmSDQANQVLARAGEGN-------EEISNMIHNYIKEIEDL--RAKLLESEAVN-- 500
Cdd:TIGR01612  920 DEYIKI-CENTKESIEKFHNKQNIL-KEILNKNIDTIKESNlieksykDKFDNTLIDKINELDKAfkDASLNDYEAKNne 997

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159648420  501 -----ENLRRNLSRASTRSTYfggpSAFSasmlSSEKETLEIldIAKKDLEKLKKKERKKKKSVKEDNTDNEQEKRDEKG 575
Cdd:TIGR01612  998 likyfNDLKANLGKNKENMLY----HQFD----EKEKATNDI--EQKIEDANKNIPNIEIAIHTSIYNIIDEIEKEIGKN 1067

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159648420  576 SSERENNELEAEEIQEASDREDEEEEDDEDEDDMEVVESSDESDSDSDEKE-----NYQADlANITCEIAIKQK---LID 647
Cdd:TIGR01612 1068 IELLNKEILEEAEINITNFNEIKEKLKHYNFDDFGKEENIKYADEINKIKDdiknlDQKID-HHIKALEEIKKKsenYID 1146

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159648420  648 ELENSQRRLQ--TLKRQYEEKLMMLQHKIRD--TQLER--------DQVLQNLGSVET--YSEEKAKKIKSEYEKKLQTM 713
Cdd:TIGR01612 1147 EIKAQINDLEdvADKAISNDDPEEIEKKIENivTKIDKkkniydeiKKLLNEIAEIEKdkTSLEEVKGINLSYGKNLGKL 1226

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159648420  714 NkeLQRLQTAQKEHARLLKNQSQYEKQL---KKLQQEVTEMKKTKVRLMKQMK------EEQEKARMTESRRNREIAQLK 784
Cdd:TIGR01612 1227 F--LEKIDEEKKKSEHMIKAMEAYIEDLdeiKEKSPEIENEMGIEMDIKAEMEtfnishDDDKDHHIISKKHDENISDIR 1304

                          490       500       510
                   ....*....|....*....|....*....|....*..
gi 1159648420  785 KEQR---------------KREHQLKLLEAQKRNQEV 806
Cdd:TIGR01612 1305 EKSLkiiedfseesdindiKKELQKNLLDAQKHNSDI 1341
HMMR_N pfam15905
Hyaluronan mediated motility receptor N-terminal; HMMR_N is the N-terminal region of ...
 643-747 9.40e-03

Hyaluronan mediated motility receptor N-terminal; HMMR_N is the N-terminal region of eukaryotic hyaluronan-mediated motility receptor proteins. The protein is functionally associated with BRCA1 and thus predicted to be a common, low-penetrance breast cancer candidate.


Pssm-ID: 464932 [Multi-domain]  Cd Length: 329  Bit Score: 40.95  E-value: 9.40e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159648420  643 QKLIDELENSQRRLQTLKRQYEEKLMMLQHKIRDtQLERDQVLQnlgsvetysEEKAKKIkSEYEKKLQTMNKELQRLqt 722
Cdd:pfam15905  246 AQLEELLKEKNDEIESLKQSLEEKEQELSKQIKD-LNEKCKLLE---------SEKEELL-REYEEKEQTLNAELEEL-- 312

                           90       100
                   ....*....|....*....|....*
gi 1159648420  723 aqKEHARLLKNQSQyekqlkKLQQE 747
Cdd:pfam15905  313 --KEKLTLEEQEHQ------KLQQK 329
LRRFIP pfam09738
LRRFIP family; LRRFIP1 is a transcriptional repressor which preferentially binds to the ...
 628-795 9.42e-03

LRRFIP family; LRRFIP1 is a transcriptional repressor which preferentially binds to the GC-rich consensus sequence (5'- AGCCCCCGGCG-3') and may regulate expression of TNF, EGFR and PDGFA. LRRFIP2 may function as activator of the canonical Wnt signalling pathway, in association with DVL3, upstream of CTNNB1/beta-catenin.


Pssm-ID: 462869 [Multi-domain]  Cd Length: 303  Bit Score: 40.84  E-value: 9.42e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159648420  628 YQADLanitceiaikqkLIDELENSQRRLQTLKRQYEEK----------LMMLQHK---IRDTQLERDQVLQN----LGS 690
Cdd:pfam09738  121 YQVDL------------LKDKLEEMEESLAELQRELREKnkelerlkrnLRRLQFQlaeLKEQLKQRDELIEKhglvIVP 188

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159648420  691 VETyseekakkIKSEYEKKLQTMNKelqrlQTAQKEHARLLK--NQSQYEKQLKKLQQEVTEMKKTKVRLMKQMKEEQEK 768
Cdd:pfam09738  189 DEN--------TNGEEENSPADAKR-----ALVSVEAAEVLEsaGEGSLDVRLKKLADEKEELLDEVRKLKLQLEEEKSK 255

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*..
gi 1159648420  769 ARMTESRR--------------------NREIAQLKKEQRKREHQLK 795
Cdd:pfam09738  256 RNSTRSSQspdgfglengshvievqreaNKQISDYKFKLQKAEQEIT 302
MAT1 pfam06391
CDK-activating kinase assembly factor MAT1; MAT1 is an assembly/targeting factor for ...
 718-804 9.80e-03

CDK-activating kinase assembly factor MAT1; MAT1 is an assembly/targeting factor for cyclin-dependent kinase-activating kinase (CAK), which interacts with the transcription factor TFIIH. The domain found to the N-terminal side of this domain is a C3HC4 RING finger.


Pssm-ID: 461894 [Multi-domain]  Cd Length: 202  Bit Score: 39.92  E-value: 9.80e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159648420  718 QRLQTAQKEHARL-LKN---QSQYEKQLKKLQQEVTEMKKTKVRLMKQMKEEQEKARmtesRRNRE-------------- 779
Cdd:pfam06391   68 KKIEQYEKENKDLiLKNkmkLSQEEEELEELLELEKREKEERRKEEKQEEEEEKEKK----EKAKQelidelmtsnkdae 143

                           90       100
                   ....*....|....*....|....*..
gi 1159648420  780 --IAQLKKEQRKREHQLKLLEAQKRNQ 804
Cdd:pfam06391  144 eiIAQHKKTAKKRKSERRRKLEELNRV 170
 
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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