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Conserved domains on  [gi|71143119|ref|NP_055888|]
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signal-induced proliferation-associated 1-like protein 3 [Homo sapiens]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
SPAR_C pfam11881
C-terminal domain of SPAR protein; This domain is found st the C-terminus of many ...
 1477-1726 7.02e-102

C-terminal domain of SPAR protein; This domain is found st the C-terminus of many spine-associated Rap GTPase-activating - SPAR - proteins in eukaryotes. This domain is found associated with pfam02145, pfam00595. The exact function is not known.


:

Pssm-ID: 463383  Cd Length: 242  Bit Score: 326.76  E-value: 7.02e-102
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71143119   1477 KQVDtNTKNVFGQPRLRASLRDLRSPRKNYKSTIEDDLKKLIIMDNLGPE-QERDTG----QSPQKGLQRTLSDESLCSG 1551
Cdd:pfam11881    1 KRHQ-SDGNVSGQPRLRASLRDLRSPQKNYKSTIEEDLKKLIIMDSPPPEeQERKPSfpgnPSPRRSLQRTLSDESICSG 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71143119   1552 RREPSFASPAG-LEPGLPSDVLFTSTcafpsSTLPARRQHQHPHPPvgpgaTPAAGSGFPEKKSTISASELSLADGRDR- 1629
Cdd:pfam11881   80 QREPSFSSRDSvLDQALPSDVLFSCT-----STLPRSPTTRSAPLR-----RASYALGMKSLHGDLSASDLSLTDLRDRr 149

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71143119   1630 PLRRLDPGLMPLPDTAAGLEWSSLVNAAKAYEVQRAVSLFSLNDPALSPDippaHSPVHSHLSLERGPPTPRTTPTMSEE 1709
Cdd:pfam11881  150 PLRRLDPGLMPLPDTAAGLDWSHLVDAAKAFEVQRAASFFSLDDNHRSPD----AASSPQQLSLQVAPQTPRTTSTSSEE 225

                          250
                   ....*....|....*..
gi 71143119   1710 PPLDLTGKVYQLEVMLK 1726
Cdd:pfam11881  226 SPADLTGKVYQLEAMLK 242
Rap_GAP pfam02145
Rap/ran-GAP;
641-821 2.80e-88

Rap/ran-GAP;


:

Pssm-ID: 460463  Cd Length: 179  Bit Score: 284.79  E-value: 2.80e-88
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71143119    641 YNNEEAGPAFEEFLSLIGEKVCLKGFTKYAAQLDVKTDSTGTHSLYTMYQDYEIMFHVSTLLPYTPNNRQQLLRKRHIGN 720
Cdd:pfam02145    1 LSNEEGSPAYEEFLNLLGWLVELKGFKGYRGGLDTKNNTTGEYSYYWADRGTEIMFHVSTLMPTTENDPQQLEKKRHIGN 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71143119    721 DIVTIIFQEPGaLPFTPKNIRSHFQHVFIIVRVHNPCTDNVCYSMAVTRSKDAPPFGPPIPSGTTFRKSDV--FRDFLLa 798
Cdd:pfam02145   81 DIVNIVFNESG-GPFDPSTIKSQFNHVFIVVQPNLPDTDNTLYRVSVVRKDDVPPFGPLLPDPKIFSKDNLpeFVRFLA- 158

                          170       180
                   ....*....|....*....|...
gi 71143119    799 kvINAENAAHKSDKFHTMATRTR 821
Cdd:pfam02145  159 --INAERAALKSSSFAERLRRIR 179
PDZ_SIPA1-like cd06745
PDZ domain of signal-induced proliferation-associated protein 1 (SIPA1), and related domains; ...
 966-1038 1.31e-42

PDZ domain of signal-induced proliferation-associated protein 1 (SIPA1), and related domains; PDZ (PSD-95 (Postsynaptic density protein 95), Dlg (Discs large protein), and ZO-1 (Zonula occludens-1)) domain of SIPA1, and related domains. The Rap-GTPase activating protein SIPA1 (also known as GTPase-activating protein Spa-1, p130 SPA1) is a metastasis promoter; a polymorphism in a region of the Sipa1 gene encoding the PDZ domain is associated with metastasis. The SIPA1 PDZ domain binds ribosomal RNA processing 1 homolog B (Rrp1b). SIPA1 also forms a complex with water channel aquaporin-2 (AQP2) and plays a role in trafficking of AQP2, targeted positioning of which strictly regulates body water homeostasis; the SIPA1 PDZ domain binds AQP2. Rrp1b or AQP2 binding inhibits the RapGAP activity of SIPA1. PDZ domains usually bind in a sequence-specific manner to short peptide sequences located at the C-terminal end of their partner proteins (known as PDZ binding motifs). The PDZ superfamily includes canonical PDZ domains as well as those with circular permutations and domain swapping mediated by beta-strands. This SIPA1-like family domain is a canonical PDZ domain containing six beta-strands A-F and two alpha-helices (alpha-helix 1 and 2), arranged as beta-strands A, B, C, alpha-helix 1, beta-strands D, E, alpha-helix 2 and beta- strand F.


:

Pssm-ID: 467227 [Multi-domain]  Cd Length: 73  Bit Score: 150.12  E-value: 1.31e-42
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 71143119  966 DMTLRRNGLGQLGFHVKYDGTVAEVEDYGFAWQAGLRQGSRLVEICKVAVVTLTHDQMIDLLRTSVTVKVVII 1038
Cdd:cd06745    1 ELTLRRNGLGQLGFHVNYEGFVTEVERFGFAWQAGLRQGSRLVEICKVPVATLTHEQMIDLLRTSVKVKVTVI 73
PHA03247 super family cl33720
large tegument protein UL36; Provisional
 1064-1490 1.18e-04

large tegument protein UL36; Provisional


The actual alignment was detected with superfamily member PHA03247:

Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 47.24  E-value: 1.18e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71143119  1064 EQESITPGGRPPYRSNAPwqwSGPASHNSLPASKWAT-PTTPGHAQSLSRPlkQTPIVPFRESQPLHSKRPVSFPETPYT 1142
Cdd:PHA03247 2542 ELASDDAGDPPPPLPPAA---PPAAPDRSVPPPRPAPrPSEPAVTSRARRP--DAPPQSARPRAPVDDRGDPRGPAPPSP 2616

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71143119  1143 VSPAGADRVPPYRQPSGSFSTPGSATYVRyKPSPERYTAAPHPllsldphfSHDGTSSGDSSSGGLTSQESTMERQKPEP 1222
Cdd:PHA03247 2617 LPPDTHAPDPPPPSPSPAANEPDPHPPPT-VPPPERPRDDPAP--------GRVSRPRRARRLGRAAQASSPPQRPRRRA 2687

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71143119  1223 LwhVPAQARLSAIAgssgnkHPSRQDAAGKDSPNRHSKGEPqysshsssntlssnASSSHSDDRWFDPLDPLEPEQDPLS 1302
Cdd:PHA03247 2688 A--RPTVGSLTSLA------DPPPPPPTPEPAPHALVSATP--------------LPPGPAAARQASPALPAAPAPPAVP 2745

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71143119  1303 KGGSSDSGIDTTLYTSSPSCMSLAKAPRPAKPHKPPGSMGLCGGGREAAGRSHHADRRREVSPAPAVAGQSKGYRPKLYS 1382
Cdd:PHA03247 2746 AGPATPGGPARPARPPTTAGPPAPAPPAAPAAGPPRRLTRPAVASLSESRESLPSPWDPADPPAAVLAPAAALPPAASPA 2825

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71143119  1383 SGSSTPTGLAGGSRDPPRQPS--------------DMGSRVGYPAQVYKTASAETPRPSQLAQPSPFQLSASVPKSFFSK 1448
Cdd:PHA03247 2826 GPLPPPTSAQPTAPPPPPGPPppslplggsvapggDVRRRPPSRSPAAKPAAPARPPVRRLARPAVSRSTESFALPPDQP 2905

                         410       420       430       440       450
                  ....*....|....*....|....*....|....*....|....*....|.
gi 71143119  1449 QPVRNKHPTGWKRT---------EEPPPRPLPFSDPKKQVDTNTKNVfGQP 1490
Cdd:PHA03247 2906 ERPPQPQAPPPPQPqpqpppppqPQPPPPPPPRPQPPLAPTTDPAGA-GEP 2955
 
Name Accession Description Interval E-value
SPAR_C pfam11881
C-terminal domain of SPAR protein; This domain is found st the C-terminus of many ...
 1477-1726 7.02e-102

C-terminal domain of SPAR protein; This domain is found st the C-terminus of many spine-associated Rap GTPase-activating - SPAR - proteins in eukaryotes. This domain is found associated with pfam02145, pfam00595. The exact function is not known.


Pssm-ID: 463383  Cd Length: 242  Bit Score: 326.76  E-value: 7.02e-102
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71143119   1477 KQVDtNTKNVFGQPRLRASLRDLRSPRKNYKSTIEDDLKKLIIMDNLGPE-QERDTG----QSPQKGLQRTLSDESLCSG 1551
Cdd:pfam11881    1 KRHQ-SDGNVSGQPRLRASLRDLRSPQKNYKSTIEEDLKKLIIMDSPPPEeQERKPSfpgnPSPRRSLQRTLSDESICSG 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71143119   1552 RREPSFASPAG-LEPGLPSDVLFTSTcafpsSTLPARRQHQHPHPPvgpgaTPAAGSGFPEKKSTISASELSLADGRDR- 1629
Cdd:pfam11881   80 QREPSFSSRDSvLDQALPSDVLFSCT-----STLPRSPTTRSAPLR-----RASYALGMKSLHGDLSASDLSLTDLRDRr 149

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71143119   1630 PLRRLDPGLMPLPDTAAGLEWSSLVNAAKAYEVQRAVSLFSLNDPALSPDippaHSPVHSHLSLERGPPTPRTTPTMSEE 1709
Cdd:pfam11881  150 PLRRLDPGLMPLPDTAAGLDWSHLVDAAKAFEVQRAASFFSLDDNHRSPD----AASSPQQLSLQVAPQTPRTTSTSSEE 225

                          250
                   ....*....|....*..
gi 71143119   1710 PPLDLTGKVYQLEVMLK 1726
Cdd:pfam11881  226 SPADLTGKVYQLEAMLK 242
Rap_GAP pfam02145
Rap/ran-GAP;
641-821 2.80e-88

Rap/ran-GAP;


Pssm-ID: 460463  Cd Length: 179  Bit Score: 284.79  E-value: 2.80e-88
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71143119    641 YNNEEAGPAFEEFLSLIGEKVCLKGFTKYAAQLDVKTDSTGTHSLYTMYQDYEIMFHVSTLLPYTPNNRQQLLRKRHIGN 720
Cdd:pfam02145    1 LSNEEGSPAYEEFLNLLGWLVELKGFKGYRGGLDTKNNTTGEYSYYWADRGTEIMFHVSTLMPTTENDPQQLEKKRHIGN 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71143119    721 DIVTIIFQEPGaLPFTPKNIRSHFQHVFIIVRVHNPCTDNVCYSMAVTRSKDAPPFGPPIPSGTTFRKSDV--FRDFLLa 798
Cdd:pfam02145   81 DIVNIVFNESG-GPFDPSTIKSQFNHVFIVVQPNLPDTDNTLYRVSVVRKDDVPPFGPLLPDPKIFSKDNLpeFVRFLA- 158

                          170       180
                   ....*....|....*....|...
gi 71143119    799 kvINAENAAHKSDKFHTMATRTR 821
Cdd:pfam02145  159 --INAERAALKSSSFAERLRRIR 179
PDZ_SIPA1-like cd06745
PDZ domain of signal-induced proliferation-associated protein 1 (SIPA1), and related domains; ...
 966-1038 1.31e-42

PDZ domain of signal-induced proliferation-associated protein 1 (SIPA1), and related domains; PDZ (PSD-95 (Postsynaptic density protein 95), Dlg (Discs large protein), and ZO-1 (Zonula occludens-1)) domain of SIPA1, and related domains. The Rap-GTPase activating protein SIPA1 (also known as GTPase-activating protein Spa-1, p130 SPA1) is a metastasis promoter; a polymorphism in a region of the Sipa1 gene encoding the PDZ domain is associated with metastasis. The SIPA1 PDZ domain binds ribosomal RNA processing 1 homolog B (Rrp1b). SIPA1 also forms a complex with water channel aquaporin-2 (AQP2) and plays a role in trafficking of AQP2, targeted positioning of which strictly regulates body water homeostasis; the SIPA1 PDZ domain binds AQP2. Rrp1b or AQP2 binding inhibits the RapGAP activity of SIPA1. PDZ domains usually bind in a sequence-specific manner to short peptide sequences located at the C-terminal end of their partner proteins (known as PDZ binding motifs). The PDZ superfamily includes canonical PDZ domains as well as those with circular permutations and domain swapping mediated by beta-strands. This SIPA1-like family domain is a canonical PDZ domain containing six beta-strands A-F and two alpha-helices (alpha-helix 1 and 2), arranged as beta-strands A, B, C, alpha-helix 1, beta-strands D, E, alpha-helix 2 and beta- strand F.


Pssm-ID: 467227 [Multi-domain]  Cd Length: 73  Bit Score: 150.12  E-value: 1.31e-42
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 71143119  966 DMTLRRNGLGQLGFHVKYDGTVAEVEDYGFAWQAGLRQGSRLVEICKVAVVTLTHDQMIDLLRTSVTVKVVII 1038
Cdd:cd06745    1 ELTLRRNGLGQLGFHVNYEGFVTEVERFGFAWQAGLRQGSRLVEICKVPVATLTHEQMIDLLRTSVKVKVTVI 73
PDZ smart00228
Domain present in PSD-95, Dlg, and ZO-1/2; Also called DHR (Dlg homologous region) or GLGF ...
 963-1040 1.54e-09

Domain present in PSD-95, Dlg, and ZO-1/2; Also called DHR (Dlg homologous region) or GLGF (relatively well conserved tetrapeptide in these domains). Some PDZs have been shown to bind C-terminal polypeptides; others appear to bind internal (non-C-terminal) polypeptides. Different PDZs possess different binding specificities.


Pssm-ID: 214570 [Multi-domain]  Cd Length: 85  Bit Score: 56.23  E-value: 1.54e-09
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71143119     963 ETVDMTLRRNGlGQLGFHVKYDG------TVAEVEDYGFAWQAGLRQGSRLVEICKVAVVTLTHDQMIDLLR-TSVTVKV 1035
Cdd:smart00228    1 EPRLVELEKGG-GGLGFSLVGGKdegggvVVSSVVPGSPAAKAGLRVGDVILEVNGTSVEGLTHLEAVDLLKkAGGKVTL 79


                    ....*
gi 71143119    1036 VIIPP 1040
Cdd:smart00228   80 TVLRG 84
PHA03247 PHA03247
large tegument protein UL36; Provisional
 1064-1490 1.18e-04

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 47.24  E-value: 1.18e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71143119  1064 EQESITPGGRPPYRSNAPwqwSGPASHNSLPASKWAT-PTTPGHAQSLSRPlkQTPIVPFRESQPLHSKRPVSFPETPYT 1142
Cdd:PHA03247 2542 ELASDDAGDPPPPLPPAA---PPAAPDRSVPPPRPAPrPSEPAVTSRARRP--DAPPQSARPRAPVDDRGDPRGPAPPSP 2616

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71143119  1143 VSPAGADRVPPYRQPSGSFSTPGSATYVRyKPSPERYTAAPHPllsldphfSHDGTSSGDSSSGGLTSQESTMERQKPEP 1222
Cdd:PHA03247 2617 LPPDTHAPDPPPPSPSPAANEPDPHPPPT-VPPPERPRDDPAP--------GRVSRPRRARRLGRAAQASSPPQRPRRRA 2687

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71143119  1223 LwhVPAQARLSAIAgssgnkHPSRQDAAGKDSPNRHSKGEPqysshsssntlssnASSSHSDDRWFDPLDPLEPEQDPLS 1302
Cdd:PHA03247 2688 A--RPTVGSLTSLA------DPPPPPPTPEPAPHALVSATP--------------LPPGPAAARQASPALPAAPAPPAVP 2745

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71143119  1303 KGGSSDSGIDTTLYTSSPSCMSLAKAPRPAKPHKPPGSMGLCGGGREAAGRSHHADRRREVSPAPAVAGQSKGYRPKLYS 1382
Cdd:PHA03247 2746 AGPATPGGPARPARPPTTAGPPAPAPPAAPAAGPPRRLTRPAVASLSESRESLPSPWDPADPPAAVLAPAAALPPAASPA 2825

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71143119  1383 SGSSTPTGLAGGSRDPPRQPS--------------DMGSRVGYPAQVYKTASAETPRPSQLAQPSPFQLSASVPKSFFSK 1448
Cdd:PHA03247 2826 GPLPPPTSAQPTAPPPPPGPPppslplggsvapggDVRRRPPSRSPAAKPAAPARPPVRRLARPAVSRSTESFALPPDQP 2905

                         410       420       430       440       450
                  ....*....|....*....|....*....|....*....|....*....|.
gi 71143119  1449 QPVRNKHPTGWKRT---------EEPPPRPLPFSDPKKQVDTNTKNVfGQP 1490
Cdd:PHA03247 2906 ERPPQPQAPPPPQPqpqpppppqPQPPPPPPPRPQPPLAPTTDPAGA-GEP 2955
PDZ pfam00595
PDZ domain; PDZ domains are found in diverse signaling proteins.
 966-1038 3.01e-04

PDZ domain; PDZ domains are found in diverse signaling proteins.


Pssm-ID: 395476 [Multi-domain]  Cd Length: 81  Bit Score: 41.11  E-value: 3.01e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71143119    966 DMTLRRNGLGQLGFHVKYDG-------TVAEVEDYGFAWQAGLRQGSRLVEICKVAVVTLTHDQMIDLLRTSV-TVKVVI 1037
Cdd:pfam00595    1 QVTLEKDGRGGLGFSLKGGSdqgdpgiFVSEVLPGGAAEAGGLKVGDRILSINGQDVENMTHEEAVLALKGSGgKVTLTI 80


                   .
gi 71143119   1038 I 1038
Cdd:pfam00595   81 L 81
PHA03247 PHA03247
large tegument protein UL36; Provisional
 1292-1686 1.57e-03

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 43.77  E-value: 1.57e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71143119  1292 DPLEPEQDPLSKGGSSDSGIDTTLYTSSPSCMSLAKAPRPAKPHKPPGSMGLCGGGREAAGRSHHADRRREVSPAPAVAG 1371
Cdd:PHA03247 2700 DPPPPPPTPEPAPHALVSATPLPPGPAAARQASPALPAAPAPPAVPAGPATPGGPARPARPPTTAGPPAPAPPAAPAAGP 2779

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71143119  1372 QSKGYRPKLYSSGSSTPtglaggSRDPPRQPSDMGSRVGYPAQVYKTAS--------------AETPRPSQLAQPSPFQL 1437
Cdd:PHA03247 2780 PRRLTRPAVASLSESRE------SLPSPWDPADPPAAVLAPAAALPPAAspagplppptsaqpTAPPPPPGPPPPSLPLG 2853

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71143119  1438 SASVPKSFFSKQPVRNKHPTGWKRTEEPPPRPLPFSDPKKQVDTntknvFGQPRLraSLRDLRSPRKNYKSTIEDDLkkl 1517
Cdd:PHA03247 2854 GSVAPGGDVRRRPPSRSPAAKPAAPARPPVRRLARPAVSRSTES-----FALPPD--QPERPPQPQAPPPPQPQPQP--- 2923

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71143119  1518 iimdnlgPEQERDTGQSPQKGL-QRTLSDESLCSGRREPSFASPAglePGLPSDVlftstcafPSSTLPARRQHQHPHPP 1596
Cdd:PHA03247 2924 -------PPPPQPQPPPPPPPRpQPPLAPTTDPAGAGEPSGAVPQ---PWLGALV--------PGRVAVPRFRVPQPAPS 2985

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71143119  1597 V-GPGATPAAGSGFPEKKSTISASELSLADGRDRPLRRLDPGLMPLPDTAAGLEWSSLVNAAKAYEVQravslfslndpA 1675
Cdd:PHA03247 2986 ReAPASSTPPLTGHSLSRVSSWASSLALHEETDPPPVSLKQTLWPPDDTEDSDADSLFDSDSERSDLE-----------A 3054

                         410
                  ....*....|.
gi 71143119  1676 LSPDIPPAHSP 1686
Cdd:PHA03247 3055 LDPLPPEPHDP 3065
 
Name Accession Description Interval E-value
SPAR_C pfam11881
C-terminal domain of SPAR protein; This domain is found st the C-terminus of many ...
 1477-1726 7.02e-102

C-terminal domain of SPAR protein; This domain is found st the C-terminus of many spine-associated Rap GTPase-activating - SPAR - proteins in eukaryotes. This domain is found associated with pfam02145, pfam00595. The exact function is not known.


Pssm-ID: 463383  Cd Length: 242  Bit Score: 326.76  E-value: 7.02e-102
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71143119   1477 KQVDtNTKNVFGQPRLRASLRDLRSPRKNYKSTIEDDLKKLIIMDNLGPE-QERDTG----QSPQKGLQRTLSDESLCSG 1551
Cdd:pfam11881    1 KRHQ-SDGNVSGQPRLRASLRDLRSPQKNYKSTIEEDLKKLIIMDSPPPEeQERKPSfpgnPSPRRSLQRTLSDESICSG 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71143119   1552 RREPSFASPAG-LEPGLPSDVLFTSTcafpsSTLPARRQHQHPHPPvgpgaTPAAGSGFPEKKSTISASELSLADGRDR- 1629
Cdd:pfam11881   80 QREPSFSSRDSvLDQALPSDVLFSCT-----STLPRSPTTRSAPLR-----RASYALGMKSLHGDLSASDLSLTDLRDRr 149

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71143119   1630 PLRRLDPGLMPLPDTAAGLEWSSLVNAAKAYEVQRAVSLFSLNDPALSPDippaHSPVHSHLSLERGPPTPRTTPTMSEE 1709
Cdd:pfam11881  150 PLRRLDPGLMPLPDTAAGLDWSHLVDAAKAFEVQRAASFFSLDDNHRSPD----AASSPQQLSLQVAPQTPRTTSTSSEE 225

                          250
                   ....*....|....*..
gi 71143119   1710 PPLDLTGKVYQLEVMLK 1726
Cdd:pfam11881  226 SPADLTGKVYQLEAMLK 242
Rap_GAP pfam02145
Rap/ran-GAP;
641-821 2.80e-88

Rap/ran-GAP;


Pssm-ID: 460463  Cd Length: 179  Bit Score: 284.79  E-value: 2.80e-88
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71143119    641 YNNEEAGPAFEEFLSLIGEKVCLKGFTKYAAQLDVKTDSTGTHSLYTMYQDYEIMFHVSTLLPYTPNNRQQLLRKRHIGN 720
Cdd:pfam02145    1 LSNEEGSPAYEEFLNLLGWLVELKGFKGYRGGLDTKNNTTGEYSYYWADRGTEIMFHVSTLMPTTENDPQQLEKKRHIGN 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71143119    721 DIVTIIFQEPGaLPFTPKNIRSHFQHVFIIVRVHNPCTDNVCYSMAVTRSKDAPPFGPPIPSGTTFRKSDV--FRDFLLa 798
Cdd:pfam02145   81 DIVNIVFNESG-GPFDPSTIKSQFNHVFIVVQPNLPDTDNTLYRVSVVRKDDVPPFGPLLPDPKIFSKDNLpeFVRFLA- 158

                          170       180
                   ....*....|....*....|...
gi 71143119    799 kvINAENAAHKSDKFHTMATRTR 821
Cdd:pfam02145  159 --INAERAALKSSSFAERLRRIR 179
PDZ_SIPA1-like cd06745
PDZ domain of signal-induced proliferation-associated protein 1 (SIPA1), and related domains; ...
 966-1038 1.31e-42

PDZ domain of signal-induced proliferation-associated protein 1 (SIPA1), and related domains; PDZ (PSD-95 (Postsynaptic density protein 95), Dlg (Discs large protein), and ZO-1 (Zonula occludens-1)) domain of SIPA1, and related domains. The Rap-GTPase activating protein SIPA1 (also known as GTPase-activating protein Spa-1, p130 SPA1) is a metastasis promoter; a polymorphism in a region of the Sipa1 gene encoding the PDZ domain is associated with metastasis. The SIPA1 PDZ domain binds ribosomal RNA processing 1 homolog B (Rrp1b). SIPA1 also forms a complex with water channel aquaporin-2 (AQP2) and plays a role in trafficking of AQP2, targeted positioning of which strictly regulates body water homeostasis; the SIPA1 PDZ domain binds AQP2. Rrp1b or AQP2 binding inhibits the RapGAP activity of SIPA1. PDZ domains usually bind in a sequence-specific manner to short peptide sequences located at the C-terminal end of their partner proteins (known as PDZ binding motifs). The PDZ superfamily includes canonical PDZ domains as well as those with circular permutations and domain swapping mediated by beta-strands. This SIPA1-like family domain is a canonical PDZ domain containing six beta-strands A-F and two alpha-helices (alpha-helix 1 and 2), arranged as beta-strands A, B, C, alpha-helix 1, beta-strands D, E, alpha-helix 2 and beta- strand F.


Pssm-ID: 467227 [Multi-domain]  Cd Length: 73  Bit Score: 150.12  E-value: 1.31e-42
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 71143119  966 DMTLRRNGLGQLGFHVKYDGTVAEVEDYGFAWQAGLRQGSRLVEICKVAVVTLTHDQMIDLLRTSVTVKVVII 1038
Cdd:cd06745    1 ELTLRRNGLGQLGFHVNYEGFVTEVERFGFAWQAGLRQGSRLVEICKVPVATLTHEQMIDLLRTSVKVKVTVI 73
PDZ_canonical cd00136
canonical PDZ domain; Canonical PDZ (PSD-95 (Postsynaptic density protein 95), Dlg (Discs ...
 966-1036 3.30e-10

canonical PDZ domain; Canonical PDZ (PSD-95 (Postsynaptic density protein 95), Dlg (Discs large protein), and ZO-1 (Zonula occludens-1)) domain. PDZ domains usually bind to short specific peptide sequences located at the C-terminal end of their partner proteins known as PDZ binding motifs. These domains can also interact with internal peptide motifs and certain lipids, and can take part in a head-to-tail oligomerization with other PDZ domains. The PDZ superfamily includes canonical PDZ domains as well as those with circular permutations and domain swapping mediated by beta-strands. The canonical PDZ domain contains six beta-strands A-F and two alpha-helices (alpha-helix 1 and 2), arranged in the order: beta-strands A, B, C, alpha-helix 1, beta-strands D, E, alpha-helix 2 and beta-strand F.


Pssm-ID: 467153 [Multi-domain]  Cd Length: 81  Bit Score: 57.94  E-value: 3.30e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71143119  966 DMTLRRNGLGQLGFHVKYDG------TVAEVEDYGFAWQAG-LRQGSRLVEICKVAVVTLTHDQMIDLLRTS---VTVKV 1035
Cdd:cd00136    1 TVTLEKDPGGGLGFSIRGGKdggggiFVSRVEPGGPAARDGrLRVGDRILEVNGVSLEGLTHEEAVELLKSAggeVTLTV 80


                 .
gi 71143119 1036 V 1036
Cdd:cd00136   81 R 81
PDZ smart00228
Domain present in PSD-95, Dlg, and ZO-1/2; Also called DHR (Dlg homologous region) or GLGF ...
 963-1040 1.54e-09

Domain present in PSD-95, Dlg, and ZO-1/2; Also called DHR (Dlg homologous region) or GLGF (relatively well conserved tetrapeptide in these domains). Some PDZs have been shown to bind C-terminal polypeptides; others appear to bind internal (non-C-terminal) polypeptides. Different PDZs possess different binding specificities.


Pssm-ID: 214570 [Multi-domain]  Cd Length: 85  Bit Score: 56.23  E-value: 1.54e-09
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71143119     963 ETVDMTLRRNGlGQLGFHVKYDG------TVAEVEDYGFAWQAGLRQGSRLVEICKVAVVTLTHDQMIDLLR-TSVTVKV 1035
Cdd:smart00228    1 EPRLVELEKGG-GGLGFSLVGGKdegggvVVSSVVPGSPAAKAGLRVGDVILEVNGTSVEGLTHLEAVDLLKkAGGKVTL 79


                    ....*
gi 71143119    1036 VIIPP 1040
Cdd:smart00228   80 TVLRG 84
PDZ2_APBA1_3-like cd06793
PDZ domain 2 of amyloid-beta A4 precursor protein-binding family A member 1 (APBA1), APBA2, ...
 965-1031 3.56e-07

PDZ domain 2 of amyloid-beta A4 precursor protein-binding family A member 1 (APBA1), APBA2, APBA3, and related domains; PDZ (PSD-95 (Postsynaptic density protein 95), Dlg (Discs large protein), and ZO-1 (Zonula occludens-1)) domain 2 of APBA1, APBA2, APBA3, and related domains. The APBA/X11/Mint protein family includes three members: neuron specific APBA1 (also known as X11alpha and Mint1) and APBA2 (also known as X11beta and Mint2), and the ubiquitously expressed APBA3 (also known as X12gamma and Mint3). They are involved in regulating neuronal signaling, trafficking, and plasticity. They contain two PDZ domains (PDZ1 and PDZ2) which bind a variety of proteins: Arf GTPases (APBA1 and APBA2 PDZ2) and neurexin (APBA1 and APBA2 PDZ1 and 2) which are involved in vesicle docking and exocytosis; alpha1B subunit of N-type Ca2+ channel (APBA1 PDZ1) that is involved in ion channels; KIF17 (APBA1 PDZ1) that is involved in transport and traffic; and Alzheimer's disease related proteins, APP (APBA3 PDZ2), CCS (APBA1 PDZ2), NF-kappa-B/p65 (APBA2 PDZ2), presenilin-1 (APBA1 and APBA2 PDZ1 and PDZ2). PDZ domains usually bind in a sequence-specific manner to short peptide sequences located at the C-terminal end of their partner proteins (known as PDZ binding motifs). The PDZ superfamily includes canonical PDZ domains as well as those with circular permutations and domain swapping mediated by beta-strands. This APBA1,3-like family domain is a canonical PDZ domain containing six beta-strands A-F and two alpha-helices (alpha-helix 1 and 2), arranged as beta-strands A, B, C, alpha-helix 1, beta-strands D, E, alpha-helix 2 and beta-strand F.


Pssm-ID: 467255 [Multi-domain]  Cd Length: 78  Bit Score: 49.32  E-value: 3.56e-07
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 71143119  965 VDMTLRRNGLG-QLGFHVKyDGTVAEVEDYGFAWQAGLRQGSRLVEICKVAVVTLTHDQMIDLLRTSV 1031
Cdd:cd06793    3 TTVLIRRPDLKyQLGFSVQ-NGIICSLLRGGIAERGGVRVGHRIIEINGQSVVATPHEKIVQLLSNSV 69
PDZ_SHANK1_3-like cd06746
PDZ domain of SH3 and multiple ankyrin repeat domains protein 1 (SHANK1), SHANK2, SHANK3, and ...
 989-1036 4.64e-05

PDZ domain of SH3 and multiple ankyrin repeat domains protein 1 (SHANK1), SHANK2, SHANK3, and related domains; PDZ (PSD-95 (Postsynaptic density protein 95), Dlg (Discs large protein), and ZO-1 (Zonula occludens-1)) domain of SHANK1, SHANK2, SHANK3, and related domains. SHANK family proteins, SHANK1 (also known as somatostatin receptor-interacting protein, SSTR-interacting protein, SSTRIP), SHANK2 (also known as cortactin-binding protein 1, proline-rich synapse-associated protein 1), and SHANK3 (proline-rich synapse-associated protein 2) are synaptic scaffolding proteins which are highly enriched in the post-synaptic densities of excitatory synapses. They have been implicated in synaptic transmission, synapse formation, synaptic plasticity, and cytoskeletal remodeling, and are regulators of Cav1 calcium current and CREB target expression. Many protein ligands have been identified for the Shank PDZ domain, such as GKAP (also known as SAPAP), betaPIX (a guanine nucleotide exchange factor used by Rho GTPase family members Rac1 and Cdc42), alpha-latrotoxin, neuroligin, group I metabotropic glutamate receptors (mGluRs), and L-type calcium channels. PDZ domains usually bind in a sequence-specific manner to short peptide sequences located at the C-terminal end of their partner proteins (known as PDZ binding motifs). The PDZ superfamily includes canonical PDZ domains as well as those with circular permutations and domain swapping mediated by beta-strands. This SHANK-like family domain is a canonical PDZ domain containing six beta-strands A-F and two alpha-helices (alpha-helix 1 and 2), arranged as beta-strands A, B, C, alpha-helix 1, beta-strands D, E, alpha-helix 2 and beta- strand F.


Pssm-ID: 467228 [Multi-domain]  Cd Length: 101  Bit Score: 44.12  E-value: 4.64e-05
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|.
gi 71143119  989 EVEDYGFAWQAGLRQGSRLVEICKVAVVTLTHDQMIDLLRTS---VTVKVV 1036
Cdd:cd06746   48 SVDPGGVADKAGLKKGDFLLEINGEDVVKASHEQVVNLIRQSgntLVLKVV 98
PHA03247 PHA03247
large tegument protein UL36; Provisional
 1064-1490 1.18e-04

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 47.24  E-value: 1.18e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71143119  1064 EQESITPGGRPPYRSNAPwqwSGPASHNSLPASKWAT-PTTPGHAQSLSRPlkQTPIVPFRESQPLHSKRPVSFPETPYT 1142
Cdd:PHA03247 2542 ELASDDAGDPPPPLPPAA---PPAAPDRSVPPPRPAPrPSEPAVTSRARRP--DAPPQSARPRAPVDDRGDPRGPAPPSP 2616

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71143119  1143 VSPAGADRVPPYRQPSGSFSTPGSATYVRyKPSPERYTAAPHPllsldphfSHDGTSSGDSSSGGLTSQESTMERQKPEP 1222
Cdd:PHA03247 2617 LPPDTHAPDPPPPSPSPAANEPDPHPPPT-VPPPERPRDDPAP--------GRVSRPRRARRLGRAAQASSPPQRPRRRA 2687

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71143119  1223 LwhVPAQARLSAIAgssgnkHPSRQDAAGKDSPNRHSKGEPqysshsssntlssnASSSHSDDRWFDPLDPLEPEQDPLS 1302
Cdd:PHA03247 2688 A--RPTVGSLTSLA------DPPPPPPTPEPAPHALVSATP--------------LPPGPAAARQASPALPAAPAPPAVP 2745

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71143119  1303 KGGSSDSGIDTTLYTSSPSCMSLAKAPRPAKPHKPPGSMGLCGGGREAAGRSHHADRRREVSPAPAVAGQSKGYRPKLYS 1382
Cdd:PHA03247 2746 AGPATPGGPARPARPPTTAGPPAPAPPAAPAAGPPRRLTRPAVASLSESRESLPSPWDPADPPAAVLAPAAALPPAASPA 2825

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71143119  1383 SGSSTPTGLAGGSRDPPRQPS--------------DMGSRVGYPAQVYKTASAETPRPSQLAQPSPFQLSASVPKSFFSK 1448
Cdd:PHA03247 2826 GPLPPPTSAQPTAPPPPPGPPppslplggsvapggDVRRRPPSRSPAAKPAAPARPPVRRLARPAVSRSTESFALPPDQP 2905

                         410       420       430       440       450
                  ....*....|....*....|....*....|....*....|....*....|.
gi 71143119  1449 QPVRNKHPTGWKRT---------EEPPPRPLPFSDPKKQVDTNTKNVfGQP 1490
Cdd:PHA03247 2906 ERPPQPQAPPPPQPqpqpppppqPQPPPPPPPRPQPPLAPTTDPAGA-GEP 2955
PDZ_NHERF-like cd06768
PDZ domains of the Na+/H+ exchange regulatory cofactor (NHERF) family (NHERF1-4), and related ...
 978-1036 1.24e-04

PDZ domains of the Na+/H+ exchange regulatory cofactor (NHERF) family (NHERF1-4), and related domains; PDZ (PSD-95 (Postsynaptic density protein 95), Dlg (Discs large protein), and ZO-1 (Zonula occludens-1)) domain of the Na+/H+ exchange regulatory cofactor (NHERF) family of multi-PDZ-domain-containing scaffolding proteins (NHERF1-4), and related domains. The NHERF family includes NHERF1 (also known as EBP50), NHERF2 (also known as E3KARP; TKA-1; SIP-1), NHERF3 (also known as CAP70; CLAMP; Napi-Cap-1; PDZD1) and NHERF4 (also known as IKEPP; PDZK2; Napi-Cap-2). NHERF1 and NHERF2 have tandem PDZ domains (PDZ1-2); NHERF3 and NHERF4 have four PDZ domains (PDZ1-4). NHERFs are involved in the regulation of multiple receptors or transporters, such as type II sodium-phosphate cotransporter (Npt2a), purinergic P2Y1 receptor P2Y1R, the beta2-adrenergic receptor (beta2-AR), parathyroid hormone receptor type 1 (PTHR), the lysophosphatidic acid receptors (LPARs), sodium-hydrogen exchanger 3 (NHE3), and cystic fibrosis transmembrane conductance regulator (CFTR). NHERF-PDZ1 domain interaction partners include Npt2a, purinergic P2Y1 receptor, beta2-AR, CFTR, PTHR, NH3, G-protein-coupled receptor kinase 6 (GRK6A), platelet-derived growth factor receptor (PDGFR), B1 subunit of the H+ATPase, cholesterol, receptor for activated C-kinase RACK1, aquaporin 9, among others. The NHERF PDZ2 domain interacts with fewer proteins: NHERF1 PDZ2 binds Npt2a, PTHR, beta-catenin, aquaporin 9, and RACK1; NHERF2 PDZ2 binds LPA2, P2Y1R, and NHE3, cGMP-dependent protein kinase type II (cGKII). NHERF4 PDZ1 and PDZ4 bind the epithelial Ca(2+) channels TRPV5 and TRPV6. NHERF2/NHERF3 heterodimerization is mediated by PDZ domains of NHERF2 and the C-terminal PDZ domain recognition motif of NHERF3. NHERF4 regulates several transporters mediating influx of xenobiotics and nutrients in the small intestine. PDZ domains usually bind in a sequence-specific manner to short peptide sequences located at the C-terminal end of their partner proteins (known as PDZ binding motifs). The PDZ superfamily includes canonical PDZ domains as well as those with circular permutations and domain swapping mediated by beta-strands. This NHERF-like family domain is a canonical PDZ domain containing six beta-strands A-F and two alpha-helices (alpha-helix 1 and 2), arranged in the order: beta-strands A, B, C, alpha-helix 1, beta-strands D, E, alpha-helix 2 and beta-strand F.


Pssm-ID: 467249 [Multi-domain]  Cd Length: 80  Bit Score: 42.04  E-value: 1.24e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 71143119  978 GFHVKYD----GT-VAEVEDYGFAWQAGLRQGSRLVEICKVAVVTLTHDQMIDLLRTS---VTVKVV 1036
Cdd:cd06768   13 GFNLHAEkgrpGHfIREVDPGSPAERAGLKDGDRLVEVNGENVEGESHEQVVEKIKASgnqVTLLVV 79
PDZ pfam00595
PDZ domain; PDZ domains are found in diverse signaling proteins.
 966-1038 3.01e-04

PDZ domain; PDZ domains are found in diverse signaling proteins.


Pssm-ID: 395476 [Multi-domain]  Cd Length: 81  Bit Score: 41.11  E-value: 3.01e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71143119    966 DMTLRRNGLGQLGFHVKYDG-------TVAEVEDYGFAWQAGLRQGSRLVEICKVAVVTLTHDQMIDLLRTSV-TVKVVI 1037
Cdd:pfam00595    1 QVTLEKDGRGGLGFSLKGGSdqgdpgiFVSEVLPGGAAEAGGLKVGDRILSINGQDVENMTHEEAVLALKGSGgKVTLTI 80


                   .
gi 71143119   1038 I 1038
Cdd:pfam00595   81 L 81
PDZ_rhophilin-like cd06712
PDZ domain of rhophilin-1, rhophilin-2, and related domains; PDZ (PSD-95 (Postsynaptic density ...
 964-1036 4.68e-04

PDZ domain of rhophilin-1, rhophilin-2, and related domains; PDZ (PSD-95 (Postsynaptic density protein 95), Dlg (Discs large protein), and ZO-1 (Zonula occludens-1)) domain of rhophilin-1, rhophilin-2, and related domains. Rhophilin-1 (RHPN1, also known as GTP-Rho-binding protein 1) and rhophilin-2 (RHPN2, also known as GTP-Rho-binding protein 2) are Rho-GTP binding proteins involved in cytoskeletal dynamics. Rhophilin-2 inhibits RhoA's activity to induce F-actin stress fibers. PDZ domains usually bind in a sequence-specific manner to short peptide sequences located at the C-terminal end of their partner proteins (known as PDZ binding motifs). The PDZ superfamily includes canonical PDZ domains as well as those with circular permutations and domain swapping mediated by beta-strands. This rhophilin-like family domain is a canonical PDZ domain containing six beta-strands A-F and two alpha-helices (alpha-helix 1 and 2), arranged in the order: beta-strands A, B, C, alpha-helix 1, beta-strands D, E, alpha-helix 2 and beta-strand F.


Pssm-ID: 467196 [Multi-domain]  Cd Length: 78  Bit Score: 40.65  E-value: 4.68e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 71143119  964 TVDMTLRRNGLGqlgFHVKYDG--TVAEVEDYGFAWQAGLRQGSRLVEICKVAVVTLTHDQMIDLLRT----SVTVKVV 1036
Cdd:cd06712    3 TVHLTKEEGGFG---FTLRGDSpvQVASVDPGSCAAEAGLKEGDYIVSVGGVDCKWSKHSEVVKLLKSageeGLELQVV 78
PHA03247 PHA03247
large tegument protein UL36; Provisional
 1292-1686 1.57e-03

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 43.77  E-value: 1.57e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71143119  1292 DPLEPEQDPLSKGGSSDSGIDTTLYTSSPSCMSLAKAPRPAKPHKPPGSMGLCGGGREAAGRSHHADRRREVSPAPAVAG 1371
Cdd:PHA03247 2700 DPPPPPPTPEPAPHALVSATPLPPGPAAARQASPALPAAPAPPAVPAGPATPGGPARPARPPTTAGPPAPAPPAAPAAGP 2779

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71143119  1372 QSKGYRPKLYSSGSSTPtglaggSRDPPRQPSDMGSRVGYPAQVYKTAS--------------AETPRPSQLAQPSPFQL 1437
Cdd:PHA03247 2780 PRRLTRPAVASLSESRE------SLPSPWDPADPPAAVLAPAAALPPAAspagplppptsaqpTAPPPPPGPPPPSLPLG 2853

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71143119  1438 SASVPKSFFSKQPVRNKHPTGWKRTEEPPPRPLPFSDPKKQVDTntknvFGQPRLraSLRDLRSPRKNYKSTIEDDLkkl 1517
Cdd:PHA03247 2854 GSVAPGGDVRRRPPSRSPAAKPAAPARPPVRRLARPAVSRSTES-----FALPPD--QPERPPQPQAPPPPQPQPQP--- 2923

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71143119  1518 iimdnlgPEQERDTGQSPQKGL-QRTLSDESLCSGRREPSFASPAglePGLPSDVlftstcafPSSTLPARRQHQHPHPP 1596
Cdd:PHA03247 2924 -------PPPPQPQPPPPPPPRpQPPLAPTTDPAGAGEPSGAVPQ---PWLGALV--------PGRVAVPRFRVPQPAPS 2985

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71143119  1597 V-GPGATPAAGSGFPEKKSTISASELSLADGRDRPLRRLDPGLMPLPDTAAGLEWSSLVNAAKAYEVQravslfslndpA 1675
Cdd:PHA03247 2986 ReAPASSTPPLTGHSLSRVSSWASSLALHEETDPPPVSLKQTLWPPDDTEDSDADSLFDSDSERSDLE-----------A 3054

                         410
                  ....*....|.
gi 71143119  1676 LSPDIPPAHSP 1686
Cdd:PHA03247 3055 LDPLPPEPHDP 3065
PDZ_SNX27-like cd23070
PDZ domain of sorting nexin-27 (SNX27), and related domains; PDZ (PSD-95 (Postsynaptic density ...
 987-1031 3.71e-03

PDZ domain of sorting nexin-27 (SNX27), and related domains; PDZ (PSD-95 (Postsynaptic density protein 95), Dlg (Discs large protein), and ZO-1 (Zonula occludens-1)) domain of SNX27, and related domains. SNX27 is involved in retrograde transport from endosome to plasma membrane. The PDZ domain of SNX27 links cargo identification to retromer-mediated transport. SNX27 binds to the retromer complex (vacuolar protein sorting 26(VPS26)-VPS29-VPS35), via its PDZ domain binding to VPS26. The SNX27 PDZ domain also binds to cargo including the G-protein-coupled receptors (GPCRs): beta2-adrenergic receptor (beta2AR), beta1AR, parathyroid hormone receptor (PTHR), alpha-amino-3-hydroxy-5-methyl-4-isoxazolepropionic acid receptors (AMPARs), NMDA receptors, 5-hydroxytryptamine 4a receptors, frizzled receptors, and somatostatin receptor subtype 5 (SSTR5). Additional binding partners of the SNX27 PDZ domain include G protein-gated inwardly rectifying potassium (Kir3) channels, angiotensin-converting enzyme 2 (ACE2), and PTEN (phosphatase and tensin homolog deleted on chromosome 10); PTEN binding to SNX27 prevents SNX27's association with the retromer complex. SNX27 has been reported to be a host factor needed for efficient entry of an engineered SARS-CoV-2 variant, the spike protein of which contains a deletion at the S1/S2 subunit cleavage site; the PDZ domain of SNX27 binds angiotensin-converting enzyme 2 (ACE2), and may be involved in recycling ACE2 to the plasma membrane, thereby promoting viral entry. PDZ domains usually bind in a sequence-specific manner to short peptide sequences located at the C-terminal end of their partner proteins (known as PDZ binding motifs). The PDZ superfamily includes canonical PDZ domains as well as those with circular permutations and domain swapping mediated by beta-strands. This SNX27-like family domain is a canonical PDZ domain containing six beta-strands A-F and two alpha-helices (alpha-helix 1 and 2), arranged in the order: beta-strands A, B, C, alpha-helix 1, beta-strands D, E, alpha-helix 2 and beta-strand F.


Pssm-ID: 467283 [Multi-domain]  Cd Length: 93  Bit Score: 38.54  E-value: 3.71e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*
gi 71143119  987 VAEVEDYGFAWQAGLRQGSRLVEICKVAVVTLTHDQMIDLLRTSV 1031
Cdd:cd23070   40 VSAVLEGGAADKAGVRKGDRILEVNGVNVEGATHKQVVDLIKSGG 84
PHA03247 PHA03247
large tegument protein UL36; Provisional
 1040-1245 6.44e-03

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 41.46  E-value: 6.44e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71143119  1040 PFEDGTPRR-GWPETydmnTSEPKTEQESITPGGRPPYRSNAPWQWSGPASHNSLPA-SKWATPTTPGHAQSLSRPLKQT 1117
Cdd:PHA03247 2748 PATPGGPARpARPPT----TAGPPAPAPPAAPAAGPPRRLTRPAVASLSESRESLPSpWDPADPPAAVLAPAAALPPAAS 2823

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71143119  1118 P---IVPFRESQPLHSKRPVSFPETPYT----VSPAG-ADRVPPYRQPSGSFSTPGSATYVRY-KPSPERYTAA-PHPLL 1187
Cdd:PHA03247 2824 PagpLPPPTSAQPTAPPPPPGPPPPSLPlggsVAPGGdVRRRPPSRSPAAKPAAPARPPVRRLaRPAVSRSTESfALPPD 2903

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 71143119  1188 SLDPhfshdGTSSGDSSSGGLTSQESTMERQKPEPLWHVPAQARLSAIAGSSGNKHPS 1245
Cdd:PHA03247 2904 QPER-----PPQPQAPPPPQPQPQPPPPPQPQPPPPPPPRPQPPLAPTTDPAGAGEPS 2956
PHA03307 PHA03307
transcriptional regulator ICP4; Provisional
 1058-1467 8.15e-03

transcriptional regulator ICP4; Provisional


Pssm-ID: 223039 [Multi-domain]  Cd Length: 1352  Bit Score: 41.31  E-value: 8.15e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71143119  1058 TSEPKTEQESITPGGRPPYRSNAPWQWSGPASHNSLPASKWATPTTPGHAQSLSRPLKQTPIV-PFRESQPLHSKRPVSF 1136
Cdd:PHA03307   72 PPGPGTEAPANESRSTPTWSLSTLAPASPAREGSPTPPGPSSPDPPPPTPPPASPPPSPAPDLsEMLRPVGSPGPPPAAS 151

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71143119  1137 PETPYTVSPAGADRVPPYRQPSGSFSTPGSATYVRYKPSPERYTAAPHPLLSLDPHFSHDGTSSGDSSSGGLTSQESTME 1216
Cdd:PHA03307  152 PPAAGASPAAVASDAASSRQAALPLSSPEETARAPSSPPAEPPPSTPPAAASPRPPRRSSPISASASSPAPAPGRSAADD 231

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71143119  1217 R-QKPEPLWHVPAQARLSAIAGSSGNKHPSRQDAagkdsPNRHSKGEPQYSSHSSSNTLSSNASSSHSDDRWfdpldple 1295
Cdd:PHA03307  232 AgASSSDSSSSESSGCGWGPENECPLPRPAPITL-----PTRIWEASGWNGPSSRPGPASSSSSPRERSPSP-------- 298

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71143119  1296 peQDPLSKGGSSDSGIDTTLYTSSPSCMSLAK-APRPAKPHKPPGSmglcgggreaAGRSHHADRRREvSPAPAVAGQSK 1374
Cdd:PHA03307  299 --SPSSPGSGPAPSSPRASSSSSSSRESSSSStSSSSESSRGAAVS----------PGPSPSRSPSPS-RPPPPADPSSP 365

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71143119  1375 GYRPKLYSSGSSTPTglAGGSRDPPRQPSDMGSRvgypaqvYKTASAETPRPSQLAQPSPfqLSASVPKSFFSkQPVRNK 1454
Cdd:PHA03307  366 RKRPRPSRAPSSPAA--SAGRPTRRRARAAVAGR-------ARRRDATGRFPAGRPRPSP--LDAGAASGAFY-ARYPLL 433

                         410
                  ....*....|....*
gi 71143119  1455 HPTG--WKRTEEPPP 1467
Cdd:PHA03307  434 TPSGepWPGSPPPPP 448
cpPDZ_CPP-like cd06782
circularly permuted PDZ domain of C-terminal processing peptidase (CPP), a serine protease, ...
 996-1035 9.57e-03

circularly permuted PDZ domain of C-terminal processing peptidase (CPP), a serine protease, and related domains; PDZ (PSD-95 (Postsynaptic density protein 95), Dlg (Discs large protein), and ZO-1 (Zonula occludens-1)) domain of CPP (also known as tail-specific protease, PRC protein, Protease Re, and Photosystem II D1 protein processing peptidase), and related domains. CPP belongs to the peptidase S41A family. It cleaves a C-terminal 11 residue peptide from the precursor form of penicillin-binding protein 3, and may have a role in protecting bacterium from thermal and osmotic stresses. In the plant chloroplast, the enzyme removes the C-terminal extension of the D1 polypeptide of photosystem II. PDZ domains usually bind in a sequence-specific manner to short peptide sequences located at the C-terminal of their partner proteins (known as PDZ binding motifs). The PDZ superfamily includes canonical PDZ domains and as well as those with circular permutations and domain swapping of beta-strands. The canonical PDZ domain contains six beta-strands A-F and two alpha-helices (alpha-helix 1 and 2); arranged as A, B, C, alpha-helix 1, beta-strands D, E, alpha-helix 2 and beta-strand F. This CPP-like PDZ domain is a circularly permuted PDZ domain which places beta-strand A on the C-terminus. Another permutation exists in the PDZ superfamily which places both beta-strands A and B on the C-terminus.


Pssm-ID: 467623 [Multi-domain]  Cd Length: 88  Bit Score: 37.08  E-value: 9.57e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....
gi 71143119  996 AWQAGLRQGSRLVEICKVAVVTLTHDQMIDLLR----TSVTVKV 1035
Cdd:cd06782   27 AEKAGIKPGDVIVAVDGESVRGMSLDEVVKLLRgpkgTKVKLTI 70
 
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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