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Conserved domains on  [gi|1694460682|ref|NP_001358027|]
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signal-induced proliferation-associated 1-like protein 3 [Rattus norvegicus]

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 ...
 1471-1721 4.10e-107

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: 341.40  E-value: 4.10e-107
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1694460682 1471 KQVDtNAKNVFGQPRLRASLRDLRSPRKNYKSTIEDDLKKLIIMDNLGPE-QDRDTG----QSPQKSLQRTLSDESLCSG 1545
Cdd:pfam11881    1 KRHQ-SDGNVSGQPRLRASLRDLRSPQKNYKSTIEEDLKKLIIMDSPPPEeQERKPSfpgnPSPRRSLQRTLSDESICSG 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1694460682 1546 RREPSYASPTS-LEPGLPSDVLFTSTctfpsSTLPARRQHQHSHPPSGAPNTipatgnGFPEKKSAISASELSLADGRDR 1624
Cdd:pfam11881   80 QREPSFSSRDSvLDQALPSDVLFSCT-----STLPRSPTTRSAPLRRASYAL------GMKSLHGDLSASDLSLTDLRDR 148

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1694460682 1625 -PLRRLDPGMMPLPDTAAGLEWSSLVNAAKAYEVQRAVSLFSLNDPALSPDippaHSPVHSHLSLERGPQTPRTTPTMSE 1703
Cdd:pfam11881  149 rPLRRLDPGLMPLPDTAAGLDWSHLVDAAKAFEVQRAASFFSLDDNHRSPD----AASSPQQLSLQVAPQTPRTTSTSSE 224

                          250
                   ....*....|....*...
gi 1694460682 1704 ESPLDLTGKVYQLEVMLK 1721
Cdd:pfam11881  225 ESPADLTGKVYQLEAMLK 242
Rap_GAP pfam02145
Rap/ran-GAP;
635-815 5.81e-89

Rap/ran-GAP;


:

Pssm-ID: 460463  Cd Length: 179  Bit Score: 286.72  E-value: 5.81e-89
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1694460682  635 YNNEEAGPAFEEFLDLLGDKVCLKGFTKYAAQLDVKTDSTGTHSLYTTYQDYEIMFHVSTLLPYTPNNRQQLLRKRHIGN 714
Cdd:pfam02145    1 LSNEEGSPAYEEFLNLLGWLVELKGFKGYRGGLDTKNNTTGEYSYYWADRGTEIMFHVSTLMPTTENDPQQLEKKRHIGN 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1694460682  715 DIVTIIFQEPGaLPFTPKNIRSHFQHVFIIVRVHNPCTENVCYSMAVTRSKDAPPFGPPIPNGTTFRKSDV--FRDFLLa 792
Cdd:pfam02145   81 DIVNIVFNESG-GPFDPSTIKSQFNHVFIVVQPNLPDTDNTLYRVSVVRKDDVPPFGPLLPDPKIFSKDNLpeFVRFLA- 158

                          170       180
                   ....*....|....*....|...
gi 1694460682  793 kvINAENAAHKSDKFHTMATRTR 815
Cdd:pfam02145  159 --INAERAALKSSSFAERLRRIR 179
PDZ_SIPA1-like cd06745
PDZ domain of signal-induced proliferation-associated protein 1 (SIPA1), and related domains; ...
 960-1032 1.60e-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: 149.74  E-value: 1.60e-42
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1694460682  960 DMTLRRNGLGQLGFHVKYDGTVAEVEDYGFAWQAGLRQGSRLVEICKVAVVTLSHDQMIDLLRTSVTVKVVII 1032
Cdd:cd06745      1 ELTLRRNGLGQLGFHVNYEGFVTEVERFGFAWQAGLRQGSRLVEICKVPVATLTHEQMIDLLRTSVKVKVTVI 73
PHA03247 super family cl33720
large tegument protein UL36; Provisional
 1065-1706 1.30e-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: 1.30e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1694460682 1065 GGRPPYRSNAPwqwSGPASHNSLPATKWTtPATPGHAQSlSRlpKHTPGVPFRESQPLHSKRPVSFPETPFAASPAGADR 1144
Cdd:PHA03247  2549 GDPPPPLPPAA---PPAAPDRSVPPPRPA-PRPSEPAVT-SR--ARRPDAPPQSARPRAPVDDRGDPRGPAPPSPLPPDT 2621

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1694460682 1145 VPPYRQPsgsfstPGSATYARYKPSPERYAAAPHPLLSFDPHFIHDGMSSGDSSSGGLTSQESTMERPKPEPLwhVPAQA 1224
Cdd:PHA03247  2622 HAPDPPP------PSPSPAANEPDPHPPPTVPPPERPRDDPAPGRVSRPRRARRLGRAAQASSPPQRPRRRAA--RPTVG 2693

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1694460682 1225 RLSAMTgsmgskHPSRQDAAGKDSPNRHSKGEPqysshsssntlssnASSSHSDDRWFDPLDPLEPEPDPFSKGGSSDSG 1304
Cdd:PHA03247  2694 SLTSLA------DPPPPPPTPEPAPHALVSATP--------------LPPGPAAARQASPALPAAPAPPAVPAGPATPGG 2753

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1694460682 1305 IDTTLYTSSPscmslAKTPRPTKPHKPPGsiglcgggresagrphpADRRREVSPAPAVAAQNKGYRPKMYSSGSSTPPG 1384
Cdd:PHA03247  2754 PARPARPPTT-----AGPPAPAPPAAPAA-----------------GPPRRLTRPAVASLSESRESLPSPWDPADPPAAV 2811

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1694460682 1385 LVGGSRDPPRQASDMGSRTgyPTQVYKTTSAETPRPSQlsqcSPFQLSTSV-PKSFFSKQPAHNKHSTGWKRADEPPPRP 1463
Cdd:PHA03247  2812 LAPAAALPPAASPAGPLPP--PTSAQPTAPPPPPGPPP----PSLPLGGSVaPGGDVRRRPPSRSPAAKPAAPARPPVRR 2885

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1694460682 1464 LPFTESKKQVDTNAKNVFGQPRlraslrdLRSPRKNYKSTIEDDLkkliimdnlgPEQDRDTGQSPQKSL-QRTLSDESL 1542
Cdd:PHA03247  2886 LARPAVSRSTESFALPPDQPER-------PPQPQAPPPPQPQPQP----------PPPPQPQPPPPPPPRpQPPLAPTTD 2948

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1694460682 1543 CSGRREPSYASPtslEPGLPSDVlftstctfPSSTLPARRQHQHSHPPSGAPNTIPATGNGFPEKKSAISASELSLADGR 1622
Cdd:PHA03247  2949 PAGAGEPSGAVP---QPWLGALV--------PGRVAVPRFRVPQPAPSREAPASSTPPLTGHSLSRVSSWASSLALHEET 3017

                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1694460682 1623 DRPLRRLDPGMMPLPDTAAGLEWSSLVNAAKAYEVQravslfslndpALSPDIPPAHSPVHShlslergPQTPRTTPTMS 1702
Cdd:PHA03247  3018 DPPPVSLKQTLWPPDDTEDSDADSLFDSDSERSDLE-----------ALDPLPPEPHDPFAH-------EPDPATPEAGA 3079


                   ....
gi 1694460682 1703 EESP 1706
Cdd:PHA03247  3080 RESP 3083
 
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 ...
 1471-1721 4.10e-107

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: 341.40  E-value: 4.10e-107
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1694460682 1471 KQVDtNAKNVFGQPRLRASLRDLRSPRKNYKSTIEDDLKKLIIMDNLGPE-QDRDTG----QSPQKSLQRTLSDESLCSG 1545
Cdd:pfam11881    1 KRHQ-SDGNVSGQPRLRASLRDLRSPQKNYKSTIEEDLKKLIIMDSPPPEeQERKPSfpgnPSPRRSLQRTLSDESICSG 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1694460682 1546 RREPSYASPTS-LEPGLPSDVLFTSTctfpsSTLPARRQHQHSHPPSGAPNTipatgnGFPEKKSAISASELSLADGRDR 1624
Cdd:pfam11881   80 QREPSFSSRDSvLDQALPSDVLFSCT-----STLPRSPTTRSAPLRRASYAL------GMKSLHGDLSASDLSLTDLRDR 148

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1694460682 1625 -PLRRLDPGMMPLPDTAAGLEWSSLVNAAKAYEVQRAVSLFSLNDPALSPDippaHSPVHSHLSLERGPQTPRTTPTMSE 1703
Cdd:pfam11881  149 rPLRRLDPGLMPLPDTAAGLDWSHLVDAAKAFEVQRAASFFSLDDNHRSPD----AASSPQQLSLQVAPQTPRTTSTSSE 224

                          250
                   ....*....|....*...
gi 1694460682 1704 ESPLDLTGKVYQLEVMLK 1721
Cdd:pfam11881  225 ESPADLTGKVYQLEAMLK 242
Rap_GAP pfam02145
Rap/ran-GAP;
635-815 5.81e-89

Rap/ran-GAP;


Pssm-ID: 460463  Cd Length: 179  Bit Score: 286.72  E-value: 5.81e-89
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1694460682  635 YNNEEAGPAFEEFLDLLGDKVCLKGFTKYAAQLDVKTDSTGTHSLYTTYQDYEIMFHVSTLLPYTPNNRQQLLRKRHIGN 714
Cdd:pfam02145    1 LSNEEGSPAYEEFLNLLGWLVELKGFKGYRGGLDTKNNTTGEYSYYWADRGTEIMFHVSTLMPTTENDPQQLEKKRHIGN 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1694460682  715 DIVTIIFQEPGaLPFTPKNIRSHFQHVFIIVRVHNPCTENVCYSMAVTRSKDAPPFGPPIPNGTTFRKSDV--FRDFLLa 792
Cdd:pfam02145   81 DIVNIVFNESG-GPFDPSTIKSQFNHVFIVVQPNLPDTDNTLYRVSVVRKDDVPPFGPLLPDPKIFSKDNLpeFVRFLA- 158

                          170       180
                   ....*....|....*....|...
gi 1694460682  793 kvINAENAAHKSDKFHTMATRTR 815
Cdd:pfam02145  159 --INAERAALKSSSFAERLRRIR 179
PDZ_SIPA1-like cd06745
PDZ domain of signal-induced proliferation-associated protein 1 (SIPA1), and related domains; ...
 960-1032 1.60e-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: 149.74  E-value: 1.60e-42
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1694460682  960 DMTLRRNGLGQLGFHVKYDGTVAEVEDYGFAWQAGLRQGSRLVEICKVAVVTLSHDQMIDLLRTSVTVKVVII 1032
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 ...
 957-1034 2.24e-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: 55.85  E-value: 2.24e-09
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1694460682   957 ETVDMTLRRNGlGQLGFHVKYDG------TVAEVEDYGFAWQAGLRQGSRLVEICKVAVVTLSHDQMIDLLR-TSVTVKV 1029
Cdd:smart00228    1 EPRLVELEKGG-GGLGFSLVGGKdegggvVVSSVVPGSPAAKAGLRVGDVILEVNGTSVEGLTHLEAVDLLKkAGGKVTL 79


                    ....*
gi 1694460682  1030 VIIPP 1034
Cdd:smart00228   80 TVLRG 84
PHA03247 PHA03247
large tegument protein UL36; Provisional
 1065-1706 1.30e-04

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 47.24  E-value: 1.30e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1694460682 1065 GGRPPYRSNAPwqwSGPASHNSLPATKWTtPATPGHAQSlSRlpKHTPGVPFRESQPLHSKRPVSFPETPFAASPAGADR 1144
Cdd:PHA03247  2549 GDPPPPLPPAA---PPAAPDRSVPPPRPA-PRPSEPAVT-SR--ARRPDAPPQSARPRAPVDDRGDPRGPAPPSPLPPDT 2621

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1694460682 1145 VPPYRQPsgsfstPGSATYARYKPSPERYAAAPHPLLSFDPHFIHDGMSSGDSSSGGLTSQESTMERPKPEPLwhVPAQA 1224
Cdd:PHA03247  2622 HAPDPPP------PSPSPAANEPDPHPPPTVPPPERPRDDPAPGRVSRPRRARRLGRAAQASSPPQRPRRRAA--RPTVG 2693

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1694460682 1225 RLSAMTgsmgskHPSRQDAAGKDSPNRHSKGEPqysshsssntlssnASSSHSDDRWFDPLDPLEPEPDPFSKGGSSDSG 1304
Cdd:PHA03247  2694 SLTSLA------DPPPPPPTPEPAPHALVSATP--------------LPPGPAAARQASPALPAAPAPPAVPAGPATPGG 2753

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1694460682 1305 IDTTLYTSSPscmslAKTPRPTKPHKPPGsiglcgggresagrphpADRRREVSPAPAVAAQNKGYRPKMYSSGSSTPPG 1384
Cdd:PHA03247  2754 PARPARPPTT-----AGPPAPAPPAAPAA-----------------GPPRRLTRPAVASLSESRESLPSPWDPADPPAAV 2811

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1694460682 1385 LVGGSRDPPRQASDMGSRTgyPTQVYKTTSAETPRPSQlsqcSPFQLSTSV-PKSFFSKQPAHNKHSTGWKRADEPPPRP 1463
Cdd:PHA03247  2812 LAPAAALPPAASPAGPLPP--PTSAQPTAPPPPPGPPP----PSLPLGGSVaPGGDVRRRPPSRSPAAKPAAPARPPVRR 2885

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1694460682 1464 LPFTESKKQVDTNAKNVFGQPRlraslrdLRSPRKNYKSTIEDDLkkliimdnlgPEQDRDTGQSPQKSL-QRTLSDESL 1542
Cdd:PHA03247  2886 LARPAVSRSTESFALPPDQPER-------PPQPQAPPPPQPQPQP----------PPPPQPQPPPPPPPRpQPPLAPTTD 2948

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1694460682 1543 CSGRREPSYASPtslEPGLPSDVlftstctfPSSTLPARRQHQHSHPPSGAPNTIPATGNGFPEKKSAISASELSLADGR 1622
Cdd:PHA03247  2949 PAGAGEPSGAVP---QPWLGALV--------PGRVAVPRFRVPQPAPSREAPASSTPPLTGHSLSRVSSWASSLALHEET 3017

                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1694460682 1623 DRPLRRLDPGMMPLPDTAAGLEWSSLVNAAKAYEVQravslfslndpALSPDIPPAHSPVHShlslergPQTPRTTPTMS 1702
Cdd:PHA03247  3018 DPPPVSLKQTLWPPDDTEDSDADSLFDSDSERSDLE-----------ALDPLPPEPHDPFAH-------EPDPATPEAGA 3079


                   ....
gi 1694460682 1703 EESP 1706
Cdd:PHA03247  3080 RESP 3083
PDZ pfam00595
PDZ domain; PDZ domains are found in diverse signaling proteins.
 960-1032 3.58e-04

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


Pssm-ID: 395476 [Multi-domain]  Cd Length: 81  Bit Score: 40.73  E-value: 3.58e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1694460682  960 DMTLRRNGLGQLGFHVKYDG-------TVAEVEDYGFAWQAGLRQGSRLVEICKVAVVTLSHDQMIDLLRTSV-TVKVVI 1031
Cdd:pfam00595    1 QVTLEKDGRGGLGFSLKGGSdqgdpgiFVSEVLPGGAAEAGGLKVGDRILSINGQDVENMTHEEAVLALKGSGgKVTLTI 80


                   .
gi 1694460682 1032 I 1032
Cdd:pfam00595   81 L 81
 
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 ...
 1471-1721 4.10e-107

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: 341.40  E-value: 4.10e-107
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1694460682 1471 KQVDtNAKNVFGQPRLRASLRDLRSPRKNYKSTIEDDLKKLIIMDNLGPE-QDRDTG----QSPQKSLQRTLSDESLCSG 1545
Cdd:pfam11881    1 KRHQ-SDGNVSGQPRLRASLRDLRSPQKNYKSTIEEDLKKLIIMDSPPPEeQERKPSfpgnPSPRRSLQRTLSDESICSG 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1694460682 1546 RREPSYASPTS-LEPGLPSDVLFTSTctfpsSTLPARRQHQHSHPPSGAPNTipatgnGFPEKKSAISASELSLADGRDR 1624
Cdd:pfam11881   80 QREPSFSSRDSvLDQALPSDVLFSCT-----STLPRSPTTRSAPLRRASYAL------GMKSLHGDLSASDLSLTDLRDR 148

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1694460682 1625 -PLRRLDPGMMPLPDTAAGLEWSSLVNAAKAYEVQRAVSLFSLNDPALSPDippaHSPVHSHLSLERGPQTPRTTPTMSE 1703
Cdd:pfam11881  149 rPLRRLDPGLMPLPDTAAGLDWSHLVDAAKAFEVQRAASFFSLDDNHRSPD----AASSPQQLSLQVAPQTPRTTSTSSE 224

                          250
                   ....*....|....*...
gi 1694460682 1704 ESPLDLTGKVYQLEVMLK 1721
Cdd:pfam11881  225 ESPADLTGKVYQLEAMLK 242
Rap_GAP pfam02145
Rap/ran-GAP;
635-815 5.81e-89

Rap/ran-GAP;


Pssm-ID: 460463  Cd Length: 179  Bit Score: 286.72  E-value: 5.81e-89
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1694460682  635 YNNEEAGPAFEEFLDLLGDKVCLKGFTKYAAQLDVKTDSTGTHSLYTTYQDYEIMFHVSTLLPYTPNNRQQLLRKRHIGN 714
Cdd:pfam02145    1 LSNEEGSPAYEEFLNLLGWLVELKGFKGYRGGLDTKNNTTGEYSYYWADRGTEIMFHVSTLMPTTENDPQQLEKKRHIGN 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1694460682  715 DIVTIIFQEPGaLPFTPKNIRSHFQHVFIIVRVHNPCTENVCYSMAVTRSKDAPPFGPPIPNGTTFRKSDV--FRDFLLa 792
Cdd:pfam02145   81 DIVNIVFNESG-GPFDPSTIKSQFNHVFIVVQPNLPDTDNTLYRVSVVRKDDVPPFGPLLPDPKIFSKDNLpeFVRFLA- 158

                          170       180
                   ....*....|....*....|...
gi 1694460682  793 kvINAENAAHKSDKFHTMATRTR 815
Cdd:pfam02145  159 --INAERAALKSSSFAERLRRIR 179
PDZ_SIPA1-like cd06745
PDZ domain of signal-induced proliferation-associated protein 1 (SIPA1), and related domains; ...
 960-1032 1.60e-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: 149.74  E-value: 1.60e-42
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1694460682  960 DMTLRRNGLGQLGFHVKYDGTVAEVEDYGFAWQAGLRQGSRLVEICKVAVVTLSHDQMIDLLRTSVTVKVVII 1032
Cdd:cd06745      1 ELTLRRNGLGQLGFHVNYEGFVTEVERFGFAWQAGLRQGSRLVEICKVPVATLTHEQMIDLLRTSVKVKVTVI 73
PDZ_canonical cd00136
canonical PDZ domain; Canonical PDZ (PSD-95 (Postsynaptic density protein 95), Dlg (Discs ...
 960-1030 6.21e-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: 57.17  E-value: 6.21e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1694460682  960 DMTLRRNGLGQLGFHVKYDG------TVAEVEDYGFAWQAG-LRQGSRLVEICKVAVVTLSHDQMIDLLRTS---VTVKV 1029
Cdd:cd00136      1 TVTLEKDPGGGLGFSIRGGKdggggiFVSRVEPGGPAARDGrLRVGDRILEVNGVSLEGLTHEEAVELLKSAggeVTLTV 80


                   .
gi 1694460682 1030 V 1030
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 ...
 957-1034 2.24e-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: 55.85  E-value: 2.24e-09
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1694460682   957 ETVDMTLRRNGlGQLGFHVKYDG------TVAEVEDYGFAWQAGLRQGSRLVEICKVAVVTLSHDQMIDLLR-TSVTVKV 1029
Cdd:smart00228    1 EPRLVELEKGG-GGLGFSLVGGKdegggvVVSSVVPGSPAAKAGLRVGDVILEVNGTSVEGLTHLEAVDLLKkAGGKVTL 79


                    ....*
gi 1694460682  1030 VIIPP 1034
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, ...
 959-1025 5.19e-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: 48.94  E-value: 5.19e-07
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1694460682  959 VDMTLRRNGLG-QLGFHVKyDGTVAEVEDYGFAWQAGLRQGSRLVEICKVAVVTLSHDQMIDLLRTSV 1025
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 ...
 983-1030 4.58e-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: 4.58e-05
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|.
gi 1694460682  983 EVEDYGFAWQAGLRQGSRLVEICKVAVVTLSHDQMIDLLRTS---VTVKVV 1030
Cdd:cd06746     48 SVDPGGVADKAGLKKGDFLLEINGEDVVKASHEQVVNLIRQSgntLVLKVV 98
PHA03247 PHA03247
large tegument protein UL36; Provisional
 1065-1706 1.30e-04

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 47.24  E-value: 1.30e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1694460682 1065 GGRPPYRSNAPwqwSGPASHNSLPATKWTtPATPGHAQSlSRlpKHTPGVPFRESQPLHSKRPVSFPETPFAASPAGADR 1144
Cdd:PHA03247  2549 GDPPPPLPPAA---PPAAPDRSVPPPRPA-PRPSEPAVT-SR--ARRPDAPPQSARPRAPVDDRGDPRGPAPPSPLPPDT 2621

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1694460682 1145 VPPYRQPsgsfstPGSATYARYKPSPERYAAAPHPLLSFDPHFIHDGMSSGDSSSGGLTSQESTMERPKPEPLwhVPAQA 1224
Cdd:PHA03247  2622 HAPDPPP------PSPSPAANEPDPHPPPTVPPPERPRDDPAPGRVSRPRRARRLGRAAQASSPPQRPRRRAA--RPTVG 2693

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1694460682 1225 RLSAMTgsmgskHPSRQDAAGKDSPNRHSKGEPqysshsssntlssnASSSHSDDRWFDPLDPLEPEPDPFSKGGSSDSG 1304
Cdd:PHA03247  2694 SLTSLA------DPPPPPPTPEPAPHALVSATP--------------LPPGPAAARQASPALPAAPAPPAVPAGPATPGG 2753

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1694460682 1305 IDTTLYTSSPscmslAKTPRPTKPHKPPGsiglcgggresagrphpADRRREVSPAPAVAAQNKGYRPKMYSSGSSTPPG 1384
Cdd:PHA03247  2754 PARPARPPTT-----AGPPAPAPPAAPAA-----------------GPPRRLTRPAVASLSESRESLPSPWDPADPPAAV 2811

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1694460682 1385 LVGGSRDPPRQASDMGSRTgyPTQVYKTTSAETPRPSQlsqcSPFQLSTSV-PKSFFSKQPAHNKHSTGWKRADEPPPRP 1463
Cdd:PHA03247  2812 LAPAAALPPAASPAGPLPP--PTSAQPTAPPPPPGPPP----PSLPLGGSVaPGGDVRRRPPSRSPAAKPAAPARPPVRR 2885

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1694460682 1464 LPFTESKKQVDTNAKNVFGQPRlraslrdLRSPRKNYKSTIEDDLkkliimdnlgPEQDRDTGQSPQKSL-QRTLSDESL 1542
Cdd:PHA03247  2886 LARPAVSRSTESFALPPDQPER-------PPQPQAPPPPQPQPQP----------PPPPQPQPPPPPPPRpQPPLAPTTD 2948

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1694460682 1543 CSGRREPSYASPtslEPGLPSDVlftstctfPSSTLPARRQHQHSHPPSGAPNTIPATGNGFPEKKSAISASELSLADGR 1622
Cdd:PHA03247  2949 PAGAGEPSGAVP---QPWLGALV--------PGRVAVPRFRVPQPAPSREAPASSTPPLTGHSLSRVSSWASSLALHEET 3017

                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1694460682 1623 DRPLRRLDPGMMPLPDTAAGLEWSSLVNAAKAYEVQravslfslndpALSPDIPPAHSPVHShlslergPQTPRTTPTMS 1702
Cdd:PHA03247  3018 DPPPVSLKQTLWPPDDTEDSDADSLFDSDSERSDLE-----------ALDPLPPEPHDPFAH-------EPDPATPEAGA 3079


                   ....
gi 1694460682 1703 EESP 1706
Cdd:PHA03247  3080 RESP 3083
PDZ_NHERF-like cd06768
PDZ domains of the Na+/H+ exchange regulatory cofactor (NHERF) family (NHERF1-4), and related ...
 972-1030 1.38e-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: 1.38e-04
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1694460682  972 GFHVKYD----GT-VAEVEDYGFAWQAGLRQGSRLVEICKVAVVTLSHDQMIDLLRTS---VTVKVV 1030
Cdd:cd06768     13 GFNLHAEkgrpGHfIREVDPGSPAERAGLKDGDRLVEVNGENVEGESHEQVVEKIKASgnqVTLLVV 79
PDZ pfam00595
PDZ domain; PDZ domains are found in diverse signaling proteins.
 960-1032 3.58e-04

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


Pssm-ID: 395476 [Multi-domain]  Cd Length: 81  Bit Score: 40.73  E-value: 3.58e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1694460682  960 DMTLRRNGLGQLGFHVKYDG-------TVAEVEDYGFAWQAGLRQGSRLVEICKVAVVTLSHDQMIDLLRTSV-TVKVVI 1031
Cdd:pfam00595    1 QVTLEKDGRGGLGFSLKGGSdqgdpgiFVSEVLPGGAAEAGGLKVGDRILSINGQDVENMTHEEAVLALKGSGgKVTLTI 80


                   .
gi 1694460682 1032 I 1032
Cdd:pfam00595   81 L 81
PHA03307 PHA03307
transcriptional regulator ICP4; Provisional
 1052-1464 9.39e-04

transcriptional regulator ICP4; Provisional


Pssm-ID: 223039 [Multi-domain]  Cd Length: 1352  Bit Score: 44.39  E-value: 9.39e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1694460682 1052 TSEPKMESEAATPGGRPPYRSNAPWQWSGPASHNSLPATKWTTPATPGHAQSLSRLPKHTPGVP--FRESQPLHSKRPVS 1129
Cdd:PHA03307    72 PPGPGTEAPANESRSTPTWSLSTLAPASPAREGSPTPPGPSSPDPPPPTPPPASPPPSPAPDLSemLRPVGSPGPPPAAS 151

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1694460682 1130 FPETPfAASPAGADRVPPYRQPSGSFSTPGSATYARYKPSPERYAAAPHPLLSFDPHfihdgmssgdsssggltsqestm 1209
Cdd:PHA03307   152 PPAAG-ASPAAVASDAASSRQAALPLSSPEETARAPSSPPAEPPPSTPPAAASPRPP----------------------- 207

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1694460682 1210 ERPKPEPLWHVPAQARLSAMTGSmgSKHPSRQDAAGKDSPNRHSKGEPQYSSHSSSNTLSSNassshsddRWFDPLDPLE 1289
Cdd:PHA03307   208 RRSSPISASASSPAPAPGRSAAD--DAGASSSDSSSSESSGCGWGPENECPLPRPAPITLPT--------RIWEASGWNG 277

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1694460682 1290 PEPDPFSkgGSSDSGIDTtlytSSPScmslaktPRPTKPHKPPGSIGLCGGGRESAGRPHPADRRREVSPAPAVAAQNKG 1369
Cdd:PHA03307   278 PSSRPGP--ASSSSSPRE----RSPS-------PSPSSPGSGPAPSSPRASSSSSSSRESSSSSTSSSSESSRGAAVSPG 344

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1694460682 1370 YRPKMYSSGSSTPPGLVGgsrDPPRQASDMGSRTGYPTQvyktTSAETPRPSQLSQCSPFQLSTSVPKSFFSKQPAHNKH 1449
Cdd:PHA03307   345 PSPSRSPSPSRPPPPADP---SSPRKRPRPSRAPSSPAA----SAGRPTRRRARAAVAGRARRRDATGRFPAGRPRPSPL 417

                          410
                   ....*....|....*
gi 1694460682 1450 STGWKRADEPPPRPL 1464
Cdd:PHA03307   418 DAGAASGAFYARYPL 432
PDZ_rhophilin-like cd06712
PDZ domain of rhophilin-1, rhophilin-2, and related domains; PDZ (PSD-95 (Postsynaptic density ...
 958-1030 1.28e-03

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: 39.10  E-value: 1.28e-03
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1694460682  958 TVDMTLRRNGLGqlgFHVKYDG--TVAEVEDYGFAWQAGLRQGSRLVEICKVAVVTLSHDQMIDLLRT----SVTVKVV 1030
Cdd:cd06712      3 TVHLTKEEGGFG---FTLRGDSpvQVASVDPGSCAAEAGLKEGDYIVSVGGVDCKWSKHSEVVKLLKSageeGLELQVV 78
PHA03247 PHA03247
large tegument protein UL36; Provisional
 1041-1383 3.20e-03

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 42.62  E-value: 3.20e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1694460682 1041 RRGWPETYDMSTSEPKMESEAATPGGRPPYRSNAPWQWSGPASHNSLPATKWTTPATPGHAQSLSrlpkhTPGVPfresq 1120
Cdd:PHA03247  2685 RRAARPTVGSLTSLADPPPPPPTPEPAPHALVSATPLPPGPAAARQASPALPAAPAPPAVPAGPA-----TPGGP----- 2754

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1694460682 1121 plhskRPVSFPETPFAASPAGADRVPPYRQPSGSFSTPGSATYARYKPSPERYAAAPHPLLSFDPHFIHDGMSSGDSSSG 1200
Cdd:PHA03247  2755 -----ARPARPPTTAGPPAPAPPAAPAAGPPRRLTRPAVASLSESRESLPSPWDPADPPAAVLAPAAALPPAASPAGPLP 2829

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1694460682 1201 GLTSQESTMERPKPEPLWHVPAQARLSAMTGSMGSKHPSRQDAAGKDSPNR---HSKGEPQYSSHSSSNtlssnassshs 1277
Cdd:PHA03247  2830 PPTSAQPTAPPPPPGPPPPSLPLGGSVAPGGDVRRRPPSRSPAAKPAAPARppvRRLARPAVSRSTESF----------- 2898

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1694460682 1278 ddrwfdPLDPLEPEPDPFSKGGSSDSGIDTTLYTSSPScMSLAKTPRPTKPhkPPGSIGLCGGGRESAGRPHPADRRREV 1357
Cdd:PHA03247  2899 ------ALPPDQPERPPQPQAPPPPQPQPQPPPPPQPQ-PPPPPPPRPQPP--LAPTTDPAGAGEPSGAVPQPWLGALVP 2969

                          330       340
                   ....*....|....*....|....*.
gi 1694460682 1358 SPAPAVAAQNKGYRPKMYSSGSSTPP 1383
Cdd:PHA03247  2970 GRVAVPRFRVPQPAPSREAPASSTPP 2995
PDZ1_L-delphilin-like cd06743
PDZ domain 1 of delphilin (L-delphilin isoform), and related domains; PDZ (PSD-95 ...
 961-1034 7.36e-03

PDZ domain 1 of delphilin (L-delphilin isoform), and related domains; PDZ (PSD-95 (Postsynaptic density protein 95), Dlg (Discs large protein), and ZO-1 (Zonula occludens-1)) domain 1 of delphilin (also known as glutamate receptor, ionotropic, delta 2-interacting protein 1, L-delphilin). Delphilin, a postsynaptic protein which is selectively expressed at cerebellar Purkinje cells, links the glutamate receptor delta 2 subunit (GluRdelta2) with the actin cytoskeleton and various signaling molecules. Two alternatively spliced isoforms of delphilin have been characterized: L-delphilin has two PDZ domains, PDZ1 and PDZ2, and S-delphilin has a single PDZ domain (PDZ2). These two isoforms are differently palmitoylated and may be involved in controlling GluRdelta2 signaling in Purkinje cells. 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 delphilin-like family PDZ1 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: 467225 [Multi-domain]  Cd Length: 76  Bit Score: 36.87  E-value: 7.36e-03
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1694460682  961 MTLRRNGLGQLGFHVKYDGT--VAEVEDYGFAWQAGLRQGSRLVEICKVAVVTLSHDQMIDLLRTSVTVkvviiPP 1034
Cdd:cd06743      1 PATNQGWPEAFGFSIGGSGPcyILSVEEGSSAHAAGLQPGDQILELDGQDVSSLSCEAIIALARRCPSV-----PP 71
cpPDZ_CPP-like cd06782
circularly permuted PDZ domain of C-terminal processing peptidase (CPP), a serine protease, ...
 990-1029 8.24e-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: 8.24e-03
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....
gi 1694460682  990 AWQAGLRQGSRLVEICKVAVVTLSHDQMIDLLR----TSVTVKV 1029
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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