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Conserved domains on  [gi|1720360873|ref|XP_030100839|]
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PDZ domain-containing protein GIPC3 isoform X3 [Mus musculus]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
PDZ_GIPC3 cd23079
PDZ domain of PDZ domain-containing protein GIPC3, and related domains; PDZ (PSD-95 ...
 179-267 8.88e-58

PDZ domain of PDZ domain-containing protein GIPC3, and related domains; PDZ (PSD-95 (Postsynaptic density protein 95), Dlg (Discs large protein), and ZO-1 (Zonula occludens-1)) domain of GIPC3, and related domains. GIPC3 (also known as C19orf64) belongs to the GIPC family, members of which contain an N-terminal GIPC-homology 1 (GH1) domain, a central PDZ domain, and a C-terminal GH2 domain. GIPC proteins function as adaptor molecules that assemble RTKs, GPCRs, integrins, transmembrane proteins and cytoplasmic signaling regulators as cargoes of MYO6-dependent endocytic transport. Mutations in the Gipc3 gene cause nonsyndromic hearing loss. 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 GIPC3 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: 467292 [Multi-domain]  Cd Length: 89  Bit Score: 193.60  E-value: 8.88e-58
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720360873  179 RGETKEVEVTKTEDALGLTITDNGAGYAFIKRIKEGSIINRIEAVCVGDSIEAINDHSIVGCRHYEVAKMLRELPKSQPF 258
Cdd:cd23079      1 RGETKEVEVTKTEDALGLTITDNGAGYAFIKRIKEGSIIDRIKAVCVGDHIEAINDQSIVGCRHYEVAKMLRELPKSQPF 80


                   ....*....
gi 1720360873  259 TLRLVQPRR 267
Cdd:cd23079     81 TLRLVEPKR 89
PHA03247 super family cl33720
large tegument protein UL36; Provisional
 311-715 2.57e-06

large tegument protein UL36; Provisional


The actual alignment was detected with superfamily member PHA03247:

Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 52.25  E-value: 2.57e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720360873  311 PGFRTRPGRRSGRVRLSRRVRGGGVGSYRRGPRRLWLACVGVSSPGPSPLPQRHSRSQDSPETRPaTRTQPSSETQVHPE 390
Cdd:PHA03247  2648 PPERPRDDPAPGRVSRPRRARRLGRAAQASSPPQRPRRRAARPTVGSLTSLADPPPPPPTPEPAP-HALVSATPLPPGPA 2726

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720360873  391 AQPGSSTQFSSKSQPEPHPcSGTQVSSEGQTSSRTNTEVQPSSRTRPSSLTQAHPETQLGSSTQSefqAGSGTQVSPKAS 470
Cdd:PHA03247  2727 AARQASPALPAAPAPPAVP-AGPATPGGPARPARPPTTAGPPAPAPPAAPAAGPPRRLTRPAVAS---LSESRESLPSPW 2802

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720360873  471 SCSRTKVDVLPSSRTRASSVTQAHPKAQPDSSTQLSSETQLESLvgPEFQSCSKTKIEAQDNSRTQPSS------VTQAH 544
Cdd:PHA03247  2803 DPADPPAAVLAPAAALPPAASPAGPLPPPTSAQPTAPPPPPGPP--PPSLPLGGSVAPGGDVRRRPPSRspaakpAAPAR 2880

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720360873  545 PKAQLGSVTLVSEVQPAFrSQPSPGVQSDSRTQVSSEAQAGFGTQSSPRPEPCSKTHLEPDCQPIPRTQPGSEVQP-GFE 623
Cdd:PHA03247  2881 PPVRRLARPAVSRSTESF-ALPPDQPERPPQPQAPPPPQPQPQPPPPPQPQPPPPPPPRPQPPLAPTTDPAGAGEPsGAV 2959

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720360873  624 ATPHSGAQGNSDTHARLRTQASPQVNFCLETKSTSRTQSGSESGLGS-----RTQIHPDRKPCSRAQ----PDIGTNPDA 694
Cdd:PHA03247  2960 PQPWLGALVPGRVAVPRFRVPQPAPSREAPASSTPPLTGHSLSRVSSwasslALHEETDPPPVSLKQtlwpPDDTEDSDA 3039

                          410       420
                   ....*....|....*....|..
gi 1720360873  695 AAQVMADPQPSRMQ-PSPVPQP 715
Cdd:PHA03247  3040 DSLFDSDSERSDLEaLDPLPPE 3061
PHA03247 super family cl33720
large tegument protein UL36; Provisional
 779-1161 5.18e-06

large tegument protein UL36; Provisional


The actual alignment was detected with superfamily member PHA03247:

Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 51.09  E-value: 5.18e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720360873  779 EPLTDETQVGSSSQPSSTPLPSAGTQSHTAtqskLKPQPCSPAQLPTSASQsPEPQASPSDESDSEAQPRGRSR------ 852
Cdd:PHA03247  2594 QSARPRAPVDDRGDPRGPAPPSPLPPDTHA----PDPPPPSPSPAANEPDP-HPPPTVPPPERPRDDPAPGRVSrprrar 2668

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720360873  853 ---KALTAEPHPQMPCTPKSRPSLG-LSQSADPTPPRRWHAGSRTQSDSGTQTDFQAWPSSGAYvgwarhrrsqlqslte 928
Cdd:PHA03247  2669 rlgRAAQASSPPQRPRRRAARPTVGsLTSLADPPPPPPTPEPAPHALVSATPLPPGPAAARQAS---------------- 2732

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720360873  929 kePSSRSLSSSGGRKQHSVTTGASCVPQQNTgqwLGSAAHSASRTQVSLQVPSRTGAQPSAGKDSSSRTRLDSSPSPSPS 1008
Cdd:PHA03247  2733 --PALPAAPAPPAVPAGPATPGGPARPARPP---TTAGPPAPAPPAAPAAGPPRRLTRPAVASLSESRESLPSPWDPADP 2807

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720360873 1009 PSPSPSPSPSPSPSPSPspspspspdTSGSQPSTVARPLSFRDSRRPQTPGLQP---IKEPKPLTR--PQSPSPLTPRAP 1083
Cdd:PHA03247  2808 PAAVLAPAAALPPAASP---------AGPLPPPTSAQPTAPPPPPGPPPPSLPLggsVAPGGDVRRrpPSRSPAAKPAAP 2878

                          330       340       350       360       370       380       390
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1720360873 1084 T-PAPSKVAGPWPQDGTQATAGPRPGPSLSLLGPGSPGPDTPQKPALLPKPQLGCQKPNPPTICITPSPSPGSGSLPHP 1161
Cdd:PHA03247  2879 ArPPVRRLARPAVSRSTESFALPPDQPERPPQPQAPPPPQPQPQPPPPPQPQPPPPPPPRPQPPLAPTTDPAGAGEPSG 2957
 
Name Accession Description Interval E-value
PDZ_GIPC3 cd23079
PDZ domain of PDZ domain-containing protein GIPC3, and related domains; PDZ (PSD-95 ...
 179-267 8.88e-58

PDZ domain of PDZ domain-containing protein GIPC3, and related domains; PDZ (PSD-95 (Postsynaptic density protein 95), Dlg (Discs large protein), and ZO-1 (Zonula occludens-1)) domain of GIPC3, and related domains. GIPC3 (also known as C19orf64) belongs to the GIPC family, members of which contain an N-terminal GIPC-homology 1 (GH1) domain, a central PDZ domain, and a C-terminal GH2 domain. GIPC proteins function as adaptor molecules that assemble RTKs, GPCRs, integrins, transmembrane proteins and cytoplasmic signaling regulators as cargoes of MYO6-dependent endocytic transport. Mutations in the Gipc3 gene cause nonsyndromic hearing loss. 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 GIPC3 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: 467292 [Multi-domain]  Cd Length: 89  Bit Score: 193.60  E-value: 8.88e-58
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720360873  179 RGETKEVEVTKTEDALGLTITDNGAGYAFIKRIKEGSIINRIEAVCVGDSIEAINDHSIVGCRHYEVAKMLRELPKSQPF 258
Cdd:cd23079      1 RGETKEVEVTKTEDALGLTITDNGAGYAFIKRIKEGSIIDRIKAVCVGDHIEAINDQSIVGCRHYEVAKMLRELPKSQPF 80


                   ....*....
gi 1720360873  259 TLRLVQPRR 267
Cdd:cd23079     81 TLRLVEPKR 89
PDZ smart00228
Domain present in PSD-95, Dlg, and ZO-1/2; Also called DHR (Dlg homologous region) or GLGF ...
 181-265 1.80e-08

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: 52.77  E-value: 1.80e-08
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720360873   181 ETKEVEVTKTEDALGLTITDNGA--GYAFIKRIKEGSIINRiEAVCVGDSIEAINDHSIVGCRHYEVAKMLRElpKSQPF 258
Cdd:smart00228    1 EPRLVELEKGGGGLGFSLVGGKDegGGVVVSSVVPGSPAAK-AGLRVGDVILEVNGTSVEGLTHLEAVDLLKK--AGGKV 77


                    ....*..
gi 1720360873   259 TLRLVQP 265
Cdd:smart00228   78 TLTVLRG 84
PHA03247 PHA03247
large tegument protein UL36; Provisional
 311-715 2.57e-06

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 52.25  E-value: 2.57e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720360873  311 PGFRTRPGRRSGRVRLSRRVRGGGVGSYRRGPRRLWLACVGVSSPGPSPLPQRHSRSQDSPETRPaTRTQPSSETQVHPE 390
Cdd:PHA03247  2648 PPERPRDDPAPGRVSRPRRARRLGRAAQASSPPQRPRRRAARPTVGSLTSLADPPPPPPTPEPAP-HALVSATPLPPGPA 2726

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720360873  391 AQPGSSTQFSSKSQPEPHPcSGTQVSSEGQTSSRTNTEVQPSSRTRPSSLTQAHPETQLGSSTQSefqAGSGTQVSPKAS 470
Cdd:PHA03247  2727 AARQASPALPAAPAPPAVP-AGPATPGGPARPARPPTTAGPPAPAPPAAPAAGPPRRLTRPAVAS---LSESRESLPSPW 2802

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720360873  471 SCSRTKVDVLPSSRTRASSVTQAHPKAQPDSSTQLSSETQLESLvgPEFQSCSKTKIEAQDNSRTQPSS------VTQAH 544
Cdd:PHA03247  2803 DPADPPAAVLAPAAALPPAASPAGPLPPPTSAQPTAPPPPPGPP--PPSLPLGGSVAPGGDVRRRPPSRspaakpAAPAR 2880

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720360873  545 PKAQLGSVTLVSEVQPAFrSQPSPGVQSDSRTQVSSEAQAGFGTQSSPRPEPCSKTHLEPDCQPIPRTQPGSEVQP-GFE 623
Cdd:PHA03247  2881 PPVRRLARPAVSRSTESF-ALPPDQPERPPQPQAPPPPQPQPQPPPPPQPQPPPPPPPRPQPPLAPTTDPAGAGEPsGAV 2959

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720360873  624 ATPHSGAQGNSDTHARLRTQASPQVNFCLETKSTSRTQSGSESGLGS-----RTQIHPDRKPCSRAQ----PDIGTNPDA 694
Cdd:PHA03247  2960 PQPWLGALVPGRVAVPRFRVPQPAPSREAPASSTPPLTGHSLSRVSSwasslALHEETDPPPVSLKQtlwpPDDTEDSDA 3039

                          410       420
                   ....*....|....*....|..
gi 1720360873  695 AAQVMADPQPSRMQ-PSPVPQP 715
Cdd:PHA03247  3040 DSLFDSDSERSDLEaLDPLPPE 3061
PHA03247 PHA03247
large tegument protein UL36; Provisional
 779-1161 5.18e-06

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 51.09  E-value: 5.18e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720360873  779 EPLTDETQVGSSSQPSSTPLPSAGTQSHTAtqskLKPQPCSPAQLPTSASQsPEPQASPSDESDSEAQPRGRSR------ 852
Cdd:PHA03247  2594 QSARPRAPVDDRGDPRGPAPPSPLPPDTHA----PDPPPPSPSPAANEPDP-HPPPTVPPPERPRDDPAPGRVSrprrar 2668

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720360873  853 ---KALTAEPHPQMPCTPKSRPSLG-LSQSADPTPPRRWHAGSRTQSDSGTQTDFQAWPSSGAYvgwarhrrsqlqslte 928
Cdd:PHA03247  2669 rlgRAAQASSPPQRPRRRAARPTVGsLTSLADPPPPPPTPEPAPHALVSATPLPPGPAAARQAS---------------- 2732

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720360873  929 kePSSRSLSSSGGRKQHSVTTGASCVPQQNTgqwLGSAAHSASRTQVSLQVPSRTGAQPSAGKDSSSRTRLDSSPSPSPS 1008
Cdd:PHA03247  2733 --PALPAAPAPPAVPAGPATPGGPARPARPP---TTAGPPAPAPPAAPAAGPPRRLTRPAVASLSESRESLPSPWDPADP 2807

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720360873 1009 PSPSPSPSPSPSPSPSPspspspspdTSGSQPSTVARPLSFRDSRRPQTPGLQP---IKEPKPLTR--PQSPSPLTPRAP 1083
Cdd:PHA03247  2808 PAAVLAPAAALPPAASP---------AGPLPPPTSAQPTAPPPPPGPPPPSLPLggsVAPGGDVRRrpPSRSPAAKPAAP 2878

                          330       340       350       360       370       380       390
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1720360873 1084 T-PAPSKVAGPWPQDGTQATAGPRPGPSLSLLGPGSPGPDTPQKPALLPKPQLGCQKPNPPTICITPSPSPGSGSLPHP 1161
Cdd:PHA03247  2879 ArPPVRRLARPAVSRSTESFALPPDQPERPPQPQAPPPPQPQPQPPPPPQPQPPPPPPPRPQPPLAPTTDPAGAGEPSG 2957
PHA03307 PHA03307
transcriptional regulator ICP4; Provisional
 545-886 9.76e-05

transcriptional regulator ICP4; Provisional


Pssm-ID: 223039 [Multi-domain]  Cd Length: 1352  Bit Score: 46.70  E-value: 9.76e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720360873  545 PKAQLGSVTLVSEVQPAFRSQPSPGVQSDSRTQV-SSEAQAGFGTQSSPRPEPCSKTHLEPdcqpiprTQPGSEVQPGFE 623
Cdd:PHA03307    46 DSAELAAVTVVAGAAACDRFEPPTGPPPGPGTEApANESRSTPTWSLSTLAPASPAREGSP-------TPPGPSSPDPPP 118

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720360873  624 ATPHSGAQG---NSDTHARLRTQASPQVNFCLETKSTSRTQSGSESGLGSRTQ------IHPDRKPC-SRAQPDIGTNPD 693
Cdd:PHA03307   119 PTPPPASPPpspAPDLSEMLRPVGSPGPPPAASPPAAGASPAAVASDAASSRQaalplsSPEETARApSSPPAEPPPSTP 198

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720360873  694 AAAQVMADPQPSRMQPSPVPQPHSGIQTNVRRQLGSEHHPSSQSQKPGSESQPRYETATTMAWPF--------PETWSGL 765
Cdd:PHA03307   199 PAAASPRPPRRSSPISASASSPAPAPGRSAADDAGASSSDSSSSESSGCGWGPENECPLPRPAPItlptriweASGWNGP 278

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720360873  766 GRRACLGPQARSSEPLTDETQVGSSSQPSSTPLPSA-GTQSHTATQSKLKPQPCSPAQLPTSASQSPEPQASPSDESDSE 844
Cdd:PHA03307   279 SSRPGPASSSSSPRERSPSPSPSSPGSGPAPSSPRAsSSSSSSRESSSSSTSSSSESSRGAAVSPGPSPSRSPSPSRPPP 358

                          330       340       350       360
                   ....*....|....*....|....*....|....*....|..
gi 1720360873  845 AQPRGRSRKALTAEPHPQMPCTPKSRpslglsqsadpTPPRR 886
Cdd:PHA03307   359 PADPSSPRKRPRPSRAPSSPAASAGR-----------PTRRR 389
PDZ pfam00595
PDZ domain; PDZ domains are found in diverse signaling proteins.
 194-261 6.75e-04

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


Pssm-ID: 395476 [Multi-domain]  Cd Length: 81  Bit Score: 39.57  E-value: 6.75e-04
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1720360873  194 LGLTI---TDNGAGYAFIKRIKEGSIINRiEAVCVGDSIEAINDHSIVGCRHYEVAKMLRELPKSQPFTLR 261
Cdd:pfam00595   12 LGFSLkggSDQGDPGIFVSEVLPGGAAEA-GGLKVGDRILSINGQDVENMTHEEAVLALKGSGGKVTLTIL 81
 
Name Accession Description Interval E-value
PDZ_GIPC3 cd23079
PDZ domain of PDZ domain-containing protein GIPC3, and related domains; PDZ (PSD-95 ...
 179-267 8.88e-58

PDZ domain of PDZ domain-containing protein GIPC3, and related domains; PDZ (PSD-95 (Postsynaptic density protein 95), Dlg (Discs large protein), and ZO-1 (Zonula occludens-1)) domain of GIPC3, and related domains. GIPC3 (also known as C19orf64) belongs to the GIPC family, members of which contain an N-terminal GIPC-homology 1 (GH1) domain, a central PDZ domain, and a C-terminal GH2 domain. GIPC proteins function as adaptor molecules that assemble RTKs, GPCRs, integrins, transmembrane proteins and cytoplasmic signaling regulators as cargoes of MYO6-dependent endocytic transport. Mutations in the Gipc3 gene cause nonsyndromic hearing loss. 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 GIPC3 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: 467292 [Multi-domain]  Cd Length: 89  Bit Score: 193.60  E-value: 8.88e-58
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720360873  179 RGETKEVEVTKTEDALGLTITDNGAGYAFIKRIKEGSIINRIEAVCVGDSIEAINDHSIVGCRHYEVAKMLRELPKSQPF 258
Cdd:cd23079      1 RGETKEVEVTKTEDALGLTITDNGAGYAFIKRIKEGSIIDRIKAVCVGDHIEAINDQSIVGCRHYEVAKMLRELPKSQPF 80


                   ....*....
gi 1720360873  259 TLRLVQPRR 267
Cdd:cd23079     81 TLRLVEPKR 89
PDZ_GIPC cd06707
PDZ domain of GIPC family proteins; GIPC1/GIPC (GAIP/RGS19-interacting protein), GIPC2, and ...
 179-267 1.98e-54

PDZ domain of GIPC family proteins; GIPC1/GIPC (GAIP/RGS19-interacting protein), GIPC2, and GIPC3 (also known as C19orf64) constitute the GIPC family. These proteins contain an N-terminal GIPC-homology 1 (GH1) domain, a central PDZ domain, and a C-terminal GH2 domain. GIPC proteins function as adaptor molecules that assemble RTKs, GPCRs, integrins, transmembrane proteins and cytoplasmic signaling regulators as cargoes of MYO6-dependent endocytic transport. Mutations in the Gipc1 and Gipc2 genes have been linked to cancer, while mutations in the Gipc3 gene cause nonsyndromic hearing loss. 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 GIPC 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: 467191 [Multi-domain]  Cd Length: 89  Bit Score: 183.97  E-value: 1.98e-54
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720360873  179 RGETKEVEVTKTEDALGLTITDNGAGYAFIKRIKEGSIINRIEAVCVGDSIEAINDHSIVGCRHYEVAKMLRELPKSQPF 258
Cdd:cd06707      1 KGQPKEIEVTKSEDALGLTITDNGAGYAFIKRIKEGSIMDKVPAICVGDHIEKINGESLVGCRHYEVARMLKEIPIGETF 80


                   ....*....
gi 1720360873  259 TLRLVQPRR 267
Cdd:cd06707     81 TLRLVEPKK 89
PDZ_GIPC1 cd23077
PDZ domain of PDZ domain-containing protein GIPC1; PDZ (PSD-95 (Postsynaptic density protein ...
 177-269 3.28e-45

PDZ domain of PDZ domain-containing protein GIPC1; PDZ (PSD-95 (Postsynaptic density protein 95), Dlg (Discs large protein), and ZO-1 (Zonula occludens-1)) domain of GIPC1, and related domains. GIPC1 (also known as GIPC, GAIP/RGS19-interacting protein or Tax-interacting protein 2) belongs to the GIPC family, members of which contain an N-terminal GIPC-homology 1 (GH1) domain, a central PDZ domain, and a C-terminal GH2 domain. GIPC1 functions as an adaptor molecule for loading PDZ-target cargoes on the MYO6 motor protein. The GIPC1 PDZ domain interacts with a variety of ligands, such as RGS19, NRP1, GLUT1, SEMA4C, SDC4 and IGF1R. 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 GIPC1 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: 467290 [Multi-domain]  Cd Length: 94  Bit Score: 157.66  E-value: 3.28e-45
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720360873  177 HVRGETKEVEVTKTEDALGLTITDNGAGYAFIKRIKEGSIINRIEAVCVGDSIEAINDHSIVGCRHYEVAKMLRELPKSQ 256
Cdd:cd23077      1 HVKGQRKEVEVFKSEDALGLTITDNGAGYAFIKRIKEGSVIDRIQLISVGDMIEAINGQSLLGCRHYEVARLLKELPRGR 80

                           90
                   ....*....|...
gi 1720360873  257 PFTLRLVQPRRAF 269
Cdd:cd23077     81 TFTLKLTEPRKAF 93
PDZ_GIPC2 cd23078
PDZ domain of PDZ domain-containing protein GIPC2, and related domains; PDZ (PSD-95 ...
 177-269 2.36e-44

PDZ domain of PDZ domain-containing protein GIPC2, and related domains; PDZ (PSD-95 (Postsynaptic density protein 95), Dlg (Discs large protein), and ZO-1 (Zonula occludens-1)) domain of GIPC2, and related domains. GIPC2 belongs to the GIPC family, members of which contain an N-terminal GIPC-homology 1 (GH1) domain, a central PDZ domain, and a C-terminal GH2 domain. GIPC proteins function as adaptor molecules that assemble RTKs, GPCRs, integrins, transmembrane proteins and cytoplasmic signaling regulators as cargoes of MYO6-dependent endocytic transport. Mutations in the Gipc2 gene have been linked to cancer. 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 GIPC2 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: 467291  Cd Length: 93  Bit Score: 155.46  E-value: 2.36e-44
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720360873  177 HVRGETKEVEVTKTEDALGLTITDNGAGYAFIKRIKEGSIINRIEAVCVGDSIEAINDHSIVGCRHYEVAKMLRELPKSQ 256
Cdd:cd23078      1 HVKGIKKEVNVYKSEDSLGLTITDNGVGYAFIKRIKDGSVIDSVKTICVGDHIECINGENIVGWRHYEVAKKLKELKKEE 80

                           90
                   ....*....|...
gi 1720360873  257 PFTLRLVQPRRAF 269
Cdd:cd23078     81 LFTLKLIEPKKAF 93
PDZ_canonical cd00136
canonical PDZ domain; Canonical PDZ (PSD-95 (Postsynaptic density protein 95), Dlg (Discs ...
 184-263 4.08e-09

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: 54.47  E-value: 4.08e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720360873  184 EVEVTKTEDA-LGLTIT--DNGAGYAFIKRIKEGSIINRIEAVCVGDSIEAINDHSIVGCRHYEVAKMLRELPKsqpfTL 260
Cdd:cd00136      1 TVTLEKDPGGgLGFSIRggKDGGGGIFVSRVEPGGPAARDGRLRVGDRILEVNGVSLEGLTHEEAVELLKSAGG----EV 76


                   ...
gi 1720360873  261 RLV 263
Cdd:cd00136     77 TLT 79
PDZ smart00228
Domain present in PSD-95, Dlg, and ZO-1/2; Also called DHR (Dlg homologous region) or GLGF ...
 181-265 1.80e-08

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: 52.77  E-value: 1.80e-08
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720360873   181 ETKEVEVTKTEDALGLTITDNGA--GYAFIKRIKEGSIINRiEAVCVGDSIEAINDHSIVGCRHYEVAKMLRElpKSQPF 258
Cdd:smart00228    1 EPRLVELEKGGGGLGFSLVGGKDegGGVVVSSVVPGSPAAK-AGLRVGDVILEVNGTSVEGLTHLEAVDLLKK--AGGKV 77


                    ....*..
gi 1720360873   259 TLRLVQP 265
Cdd:smart00228   78 TLTVLRG 84
PHA03247 PHA03247
large tegument protein UL36; Provisional
 311-715 2.57e-06

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 52.25  E-value: 2.57e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720360873  311 PGFRTRPGRRSGRVRLSRRVRGGGVGSYRRGPRRLWLACVGVSSPGPSPLPQRHSRSQDSPETRPaTRTQPSSETQVHPE 390
Cdd:PHA03247  2648 PPERPRDDPAPGRVSRPRRARRLGRAAQASSPPQRPRRRAARPTVGSLTSLADPPPPPPTPEPAP-HALVSATPLPPGPA 2726

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720360873  391 AQPGSSTQFSSKSQPEPHPcSGTQVSSEGQTSSRTNTEVQPSSRTRPSSLTQAHPETQLGSSTQSefqAGSGTQVSPKAS 470
Cdd:PHA03247  2727 AARQASPALPAAPAPPAVP-AGPATPGGPARPARPPTTAGPPAPAPPAAPAAGPPRRLTRPAVAS---LSESRESLPSPW 2802

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720360873  471 SCSRTKVDVLPSSRTRASSVTQAHPKAQPDSSTQLSSETQLESLvgPEFQSCSKTKIEAQDNSRTQPSS------VTQAH 544
Cdd:PHA03247  2803 DPADPPAAVLAPAAALPPAASPAGPLPPPTSAQPTAPPPPPGPP--PPSLPLGGSVAPGGDVRRRPPSRspaakpAAPAR 2880

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720360873  545 PKAQLGSVTLVSEVQPAFrSQPSPGVQSDSRTQVSSEAQAGFGTQSSPRPEPCSKTHLEPDCQPIPRTQPGSEVQP-GFE 623
Cdd:PHA03247  2881 PPVRRLARPAVSRSTESF-ALPPDQPERPPQPQAPPPPQPQPQPPPPPQPQPPPPPPPRPQPPLAPTTDPAGAGEPsGAV 2959

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720360873  624 ATPHSGAQGNSDTHARLRTQASPQVNFCLETKSTSRTQSGSESGLGS-----RTQIHPDRKPCSRAQ----PDIGTNPDA 694
Cdd:PHA03247  2960 PQPWLGALVPGRVAVPRFRVPQPAPSREAPASSTPPLTGHSLSRVSSwasslALHEETDPPPVSLKQtlwpPDDTEDSDA 3039

                          410       420
                   ....*....|....*....|..
gi 1720360873  695 AAQVMADPQPSRMQ-PSPVPQP 715
Cdd:PHA03247  3040 DSLFDSDSERSDLEaLDPLPPE 3061
PDZ3_GRIP1-2-like cd06684
PDZ domain 3 of glutamate receptor-interacting protein 1 (GRIP1) and GRIP2, and related ...
 185-250 2.62e-06

PDZ domain 3 of glutamate receptor-interacting protein 1 (GRIP1) and GRIP2, and related domains; PDZ (PSD-95 (Postsynaptic density protein 95), Dlg (Discs large protein), and ZO-1 (Zonula occludens-1)) domain of alpha-amino-3-hydroxy-5-methyl-4-isoxazolepropionic acid receptor (AMPAR) binding proteins GRIP1 (ABP/GRIP2) and GRIP2, and related domains. GRIP1 and GRIP2 each have 7 PDZ domains. The interaction of GRIP1 and GRIP2 with GluA2/3 (AMPAR subunit) regulates AMPAR trafficking and synaptic targeting. GRIP1 has an essential role in regulating AMPAR trafficking during synaptic plasticity and learning and memory. GRIP1 and GRIP2 interact with a variety of other proteins associated with protein trafficking and internalization, for example GRIP1 also interacts with KIF5 (also known as kinesin 1), EphB receptors, scaffold protein liprin-alpha, and the rasGEF GRASP-1. 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 GRIP family PDZ3 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: 467172 [Multi-domain]  Cd Length: 87  Bit Score: 46.48  E-value: 2.62e-06
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720360873  185 VEVTKTE-DALGLTITD---NGAGYAFIKRIKEGSIINRIEAVCVGDSIEAINDHSIVGCRHYEVAKMLR 250
Cdd:cd06684      5 VEIEKTPgSSLGITLSTsthRNKQVIVIDSIKPASIADRCGALHVGDHILSIDGTSVEHCSLAEATQLLA 74
PHA03247 PHA03247
large tegument protein UL36; Provisional
 779-1161 5.18e-06

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 51.09  E-value: 5.18e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720360873  779 EPLTDETQVGSSSQPSSTPLPSAGTQSHTAtqskLKPQPCSPAQLPTSASQsPEPQASPSDESDSEAQPRGRSR------ 852
Cdd:PHA03247  2594 QSARPRAPVDDRGDPRGPAPPSPLPPDTHA----PDPPPPSPSPAANEPDP-HPPPTVPPPERPRDDPAPGRVSrprrar 2668

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720360873  853 ---KALTAEPHPQMPCTPKSRPSLG-LSQSADPTPPRRWHAGSRTQSDSGTQTDFQAWPSSGAYvgwarhrrsqlqslte 928
Cdd:PHA03247  2669 rlgRAAQASSPPQRPRRRAARPTVGsLTSLADPPPPPPTPEPAPHALVSATPLPPGPAAARQAS---------------- 2732

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720360873  929 kePSSRSLSSSGGRKQHSVTTGASCVPQQNTgqwLGSAAHSASRTQVSLQVPSRTGAQPSAGKDSSSRTRLDSSPSPSPS 1008
Cdd:PHA03247  2733 --PALPAAPAPPAVPAGPATPGGPARPARPP---TTAGPPAPAPPAAPAAGPPRRLTRPAVASLSESRESLPSPWDPADP 2807

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720360873 1009 PSPSPSPSPSPSPSPSPspspspspdTSGSQPSTVARPLSFRDSRRPQTPGLQP---IKEPKPLTR--PQSPSPLTPRAP 1083
Cdd:PHA03247  2808 PAAVLAPAAALPPAASP---------AGPLPPPTSAQPTAPPPPPGPPPPSLPLggsVAPGGDVRRrpPSRSPAAKPAAP 2878

                          330       340       350       360       370       380       390
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1720360873 1084 T-PAPSKVAGPWPQDGTQATAGPRPGPSLSLLGPGSPGPDTPQKPALLPKPQLGCQKPNPPTICITPSPSPGSGSLPHP 1161
Cdd:PHA03247  2879 ArPPVRRLARPAVSRSTESFALPPDQPERPPQPQAPPPPQPQPQPPPPPQPQPPPPPPPRPQPPLAPTTDPAGAGEPSG 2957
PDZ7_PDZD2-PDZ4_hPro-IL-16-like cd06763
PDZ domain 7 of PDZ domain containing 2 (PDZD2), PDZ domain 4 of human pro-interleukin-16 ...
 184-260 5.40e-06

PDZ domain 7 of PDZ domain containing 2 (PDZD2), PDZ domain 4 of human pro-interleukin-16 (isoform 1, 1332 AA), and related domains; PDZ (PSD-95 (Postsynaptic density protein 95), Dlg (Discs large protein), and ZO-1 (Zonula occludens-1)) domain 7 of PDZD2, also known as KIAA0300, PIN-1, PAPIN, activated in prostate cancer (AIPC) and PDZ domain-containing protein 3 (PDZK3). PDZD2 has seven PDZ domains. PDZD2 is expressed at exceptionally high levels in the pancreas and certain cancer tissues, such as prostate cancer. It promotes the proliferation of insulinoma cells and is upregulated during prostate tumorigenesis. In osteosarcoma (OS), the microRNA miR-363 acts as a tumor suppressor by inhibiting PDZD2. This family include the PDZ domain of the secreted mature form of human interleukin-16 (IL-16); this is the fourth PDZ domain (PDZ4) of human pro-interleukin-16 (isoform 1, also known as nPro-Il-16). Precursor IL-16 is cleaved to produce pro-IL-16 and C-terminal mature IL-16. Pro-IL-16 functions as a regulator of T cell growth; mature IL-16 is a CD4 ligand that induces chemotaxis and CD25 expression in CD4+ T cells. IL-16 bioactivity has been closely associated with the progression of several different cancers 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 PDZD2-like family PDZ7 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: 467244 [Multi-domain]  Cd Length: 86  Bit Score: 45.68  E-value: 5.40e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720360873  184 EVEVTKTEDALGLTItDNGAGYA------FIKRIKEGSIINRIEAVCVGDSIEAINDHSIVGCRHYEVAKMLRELPkSQP 257
Cdd:cd06763      3 TVELEKGSAGLGFSL-EGGKGSPlgdrplTIKRIFKGGAAEQSGVLQVGDEILQINGTSLQGLTRFEAWNIIKSLP-EGP 80


                   ...
gi 1720360873  258 FTL 260
Cdd:cd06763     81 VTL 83
PDZ_CASK-like cd10831
PDZ domain of peripheral plasma membrane protein CASK, Caenorhabditis Lin-2, and related ...
 190-263 2.60e-05

PDZ domain of peripheral plasma membrane protein CASK, Caenorhabditis Lin-2, and related domains; PDZ (PSD-95 (Postsynaptic density protein 95), Dlg (Discs large protein), and ZO-1 (Zonula occludens-1)) domain of CASK, Caenorhabditis elegans Lin-2, and related domains. CASK and Lin-2 are membrane-associated guanylate kinase (MAGUK)-like proteins. CASK (also known as Calcium/calmodulin-dependent protein kinase, CAKI, and Camguk) has a role in synaptic transmembrane protein anchoring and ion channel trafficking. CASK may regulate transmembrane proteins that bind calcium, calmodulin, or nucleotides; it regulates the Drosophila ether a go-go (eag) potassium channel, and also regulates autophosphorylation of CaMKII. CASK binding partners include the transcription factor TBR1, and cell-surface proteins, including amyloid precursor protein, neurexins, and syndecans. Lin-2, as a component of the CLin-10-Lin-2-Lin-7 complex, plays a role in controlling the basolateral localization of the EGF receptor Let-23; this complex also associates with the neuron-specific motor protein KIF17 to transport vesicles containing N-methyl-D-aspartate (NMDA) receptor 2B along microtubules. CASK may also function in targeting or scaffolding of the protein parkin which is selectively truncated by a Parkinson's disease-causing mutation; the C-terminus of parkin functions as a class II PDZ-binding motif that binds CASK. 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 MPP6-MPP2-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: 467267 [Multi-domain]  Cd Length: 81  Bit Score: 43.63  E-value: 2.60e-05
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1720360873  190 TEDALGLTITDNGAGYAFIKRIKEGSIINRIEAVCVGDSIEAINDHSIVGCRHYEVAKMLRELPKSqpFTLRLV 263
Cdd:cd10831      9 TDEPMGITLKMNEDGRCIVARIMHGGMIHRQGTLHVGDEIREINGISVANQTVEQLQKMLREARGS--ITFKIV 80
PDZ4_MAGI-1_3-like cd06734
PDZ domain 4 of membrane-associated guanylate kinase inverted 1 (MAGI-1), MAGI-2, and MAGI-3, ...
 184-251 4.28e-05

PDZ domain 4 of membrane-associated guanylate kinase inverted 1 (MAGI-1), MAGI-2, and MAGI-3, and related domains; PDZ (PSD-95 (Postsynaptic density protein 95), Dlg (Discs large protein), and ZO-1 (Zonula occludens-1)) domain 4 of MAGI1, 2, 3 (MAGI is also known as Membrane-associated guanylate kinase, WW and PDZ domain-containing protein) and related domains. MAGI proteins have been implicated in the control of cell migration and invasion through altering the activity of phosphatase and tensin homolog (PTEN) and modulating Akt signaling. Four MAGI proteins have been identified (MAGI1-3 and MAGIX). MAGI1-3 have 6 PDZ domains and bind to the C-terminus of PTEN via their PDZ2 domain. MAGIX has a single PDZ domain that is related to MAGI1-3 PDZ domain 5. Other binding partners for MAGI1 include JAM4, C-terminal tail of high risk HPV-18 E6, megalin, TRAF6, Kir4.1 (basolateral K+ channel subunit), and cadherin 23; for MAGI2, include DASM1, dendrin, axin, beta- and delta-catenin, neuroligin, hyperpolarization-activated cation channels, beta1-adrenergic receptors, NMDA receptor, and TARPs; and for MAGI3 includes LPA2. 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 MAGI family PDZ4 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: 467216 [Multi-domain]  Cd Length: 84  Bit Score: 42.99  E-value: 4.28e-05
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1720360873  184 EVEVTKTED-ALGLTI--TDNGAGYAFIKRIKEGSIINRIEAVCVGDSIEAINDHSIVGCRHYEVAKMLRE 251
Cdd:cd06734      3 DVTLTRRENeGFGFVIisSVNKKSGSKIGRIIPGSPADRCGQLKVGDRILAVNGISILNLSHGDIVNLIKD 73
PHA03307 PHA03307
transcriptional regulator ICP4; Provisional
 545-886 9.76e-05

transcriptional regulator ICP4; Provisional


Pssm-ID: 223039 [Multi-domain]  Cd Length: 1352  Bit Score: 46.70  E-value: 9.76e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720360873  545 PKAQLGSVTLVSEVQPAFRSQPSPGVQSDSRTQV-SSEAQAGFGTQSSPRPEPCSKTHLEPdcqpiprTQPGSEVQPGFE 623
Cdd:PHA03307    46 DSAELAAVTVVAGAAACDRFEPPTGPPPGPGTEApANESRSTPTWSLSTLAPASPAREGSP-------TPPGPSSPDPPP 118

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720360873  624 ATPHSGAQG---NSDTHARLRTQASPQVNFCLETKSTSRTQSGSESGLGSRTQ------IHPDRKPC-SRAQPDIGTNPD 693
Cdd:PHA03307   119 PTPPPASPPpspAPDLSEMLRPVGSPGPPPAASPPAAGASPAAVASDAASSRQaalplsSPEETARApSSPPAEPPPSTP 198

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720360873  694 AAAQVMADPQPSRMQPSPVPQPHSGIQTNVRRQLGSEHHPSSQSQKPGSESQPRYETATTMAWPF--------PETWSGL 765
Cdd:PHA03307   199 PAAASPRPPRRSSPISASASSPAPAPGRSAADDAGASSSDSSSSESSGCGWGPENECPLPRPAPItlptriweASGWNGP 278

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720360873  766 GRRACLGPQARSSEPLTDETQVGSSSQPSSTPLPSA-GTQSHTATQSKLKPQPCSPAQLPTSASQSPEPQASPSDESDSE 844
Cdd:PHA03307   279 SSRPGPASSSSSPRERSPSPSPSSPGSGPAPSSPRAsSSSSSSRESSSSSTSSSSESSRGAAVSPGPSPSRSPSPSRPPP 358

                          330       340       350       360
                   ....*....|....*....|....*....|....*....|..
gi 1720360873  845 AQPRGRSRKALTAEPHPQMPCTPKSRpslglsqsadpTPPRR 886
Cdd:PHA03307   359 PADPSSPRKRPRPSRAPSSPAASAGR-----------PTRRR 389
PRK07764 PRK07764
DNA polymerase III subunits gamma and tau; Validated
 765-1162 1.12e-04

DNA polymerase III subunits gamma and tau; Validated


Pssm-ID: 236090 [Multi-domain]  Cd Length: 824  Bit Score: 46.52  E-value: 1.12e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720360873  765 LGRRACLGPQARSSEPltdetqvGSSSQPSSTPLPSAGtQSHTATQSKLKPQPcSPAQLPTSASQSPEPQASPSDESDSE 844
Cdd:PRK07764   381 LERRLGVAGGAGAPAA-------AAPSAAAAAPAAAPA-PAAAAPAAAAAPAP-AAAPQPAPAPAPAPAPPSPAGNAPAG 451

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720360873  845 AQPRGRSRKALTAEPHP---QMPCTPKSRPSLGLSQSADPTPPRRWHAGSRTQSDSGTQTDFQAWPSSGAYVGwaRHRRS 921
Cdd:PRK07764   452 GAPSPPPAAAPSAQPAPapaAAPEPTAAPAPAPPAAPAPAAAPAAPAAPAAPAGADDAATLRERWPEILAAVP--KRSRK 529

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720360873  922 qlqSLTEKEPSSRSLSSSGGRKQHSVTTGAScvpqqntGQWLGSAAHSASRTQVSLQV------------PSRTGAQPSA 989
Cdd:PRK07764   530 ---TWAILLPEATVLGVRGDTLVLGFSTGGL-------ARRFASPGNAEVLVTALAEElggdwqveavvgPAPGAAGGEG 599

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720360873  990 GKDSSSRTRLDSSPSPSPSPSPSPSPSPSPSPSPSPSPSPSPSPDTSGSQPSTVARPLSFRDSRRPQTPGLQPIKEPKPL 1069
Cdd:PRK07764   600 PPAPASSGPPEEAARPAAPAAPAAPAAPAPAGAAAAPAEASAAPAPGVAAPEHHPKHVAVPDASDGGDGWPAKAGGAAPA 679

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720360873 1070 TRPQSPSPLTPRAPTPAPSK--VAGPWPQDGTQATAGPRPGPSLSLLGPGSPGPDTPQKPALLPKPqlgcqkPNPPTICI 1147
Cdd:PRK07764   680 APPPAPAPAAPAAPAGAAPAqpAPAPAATPPAGQADDPAAQPPQAAQGASAPSPAADDPVPLPPEP------DDPPDPAG 753

                          410
                   ....*....|....*
gi 1720360873 1148 TPSPSPGSGSLPHPS 1162
Cdd:PRK07764   754 APAQPPPPPAPAPAA 768
PDZ_CNK1_2_3-like cd06748
PDZ domain of connector enhancer of kinase suppressor of ras 1 (CNK1), CNK2, CNK3, and related ...
 189-261 1.30e-04

PDZ domain of connector enhancer of kinase suppressor of ras 1 (CNK1), CNK2, CNK3, and related domains; PDZ (PSD-95 (Postsynaptic density protein 95), Dlg (Discs large protein), and ZO-1 (Zonula occludens-1)) domain of CNK1 (also known as connector enhancer of KSR 1 (CNKSR1), CNK homolog protein 1, connector enhancer of KSR-like), CNK2 (also known as CNKSR2, CNK homolog protein 2), and CNK3 (also known as CNKSR3, CNK homolog protein 3, CNKSR family member 3, maguin-like). CNK proteins modulate Ras-mediated signaling, acting downstream of Ras as a scaffold for the Raf/MEK/ERK kinase cascade. They also modulate signaling mediated via Rho family small GTPases, through interactions with various guanine nucleotide exchange factors (GEFs) and GTPase activating proteins (GAPs), and modulate the insulin signaling pathway through interactions with the Arf guanine nucleotide exchange factors. CNK proteins also regulate cell proliferation and migration by acting as scaffolds for the PI3K/Akt and JNK signaling cascades. CNK2 plays a role in the molecular processes that govern morphology of the postsynaptic density (PSD), and influences subcellular localization of the regulatory NCK-interacting kinase TNIK. TNIK binds a region of CNK2 including the PDZ and the DUF domain; this region also binds the kinase MINK1. CNK2 may also influence the membrane localization of MINK1. CNK3 plays a part in transepithelial sodium transport; it coordinates assembly of an epithelial sodium channel (ENaC)-regulatory complex. 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 CNK1-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: 467230 [Multi-domain]  Cd Length: 81  Bit Score: 41.44  E-value: 1.30e-04
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1720360873  189 KTEDALGLTITDNGAGYAFIKRIKEGSIINRIEAVCVGDSIEAINDHSIVGCRHYEVAKMLRELPKSQPFTLR 261
Cdd:cd06748      9 KPEEGLGLEIKSTYNGLHVITGTKENSPADRCGKIHAGDEVIQVNYQTVVGWQLKNLVRALREDPHGVTLTLK 81
PRK07764 PRK07764
DNA polymerase III subunits gamma and tau; Validated
 559-872 1.92e-04

DNA polymerase III subunits gamma and tau; Validated


Pssm-ID: 236090 [Multi-domain]  Cd Length: 824  Bit Score: 45.75  E-value: 1.92e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720360873  559 QPAFRSQPSPGVQSDSRTQVSSEAQAGfgtQSSPRPEPCSKTHLEPDCQPIPRTQPGSEVQPGFEATPHSGAQGNSDTHA 638
Cdd:PRK07764   434 APAPAPAPPSPAGNAPAGGAPSPPPAA---APSAQPAPAPAAAPEPTAAPAPAPPAAPAPAAAPAAPAAPAAPAGADDAA 510

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720360873  639 RLRtQASPQVNFCLETKSTSRTQsgsesGLGSRTQIHPDRKPC------------SRAQPD------------------- 687
Cdd:PRK07764   511 TLR-ERWPEILAAVPKRSRKTWA-----ILLPEATVLGVRGDTlvlgfstgglarRFASPGnaevlvtalaeelggdwqv 584

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720360873  688 ---IGTNPDAAAQVMADPQPSRMQPSPVPQPHSGIQTNVR---RQLGSEHHPSSQSQKPGSESQPRYETATTMA-WPFPE 760
Cdd:PRK07764   585 eavVGPAPGAAGGEGPPAPASSGPPEEAARPAAPAAPAAPaapAPAGAAAAPAEASAAPAPGVAAPEHHPKHVAvPDASD 664

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720360873  761 TWSGLGRRACLGPQARSSEPLTDETQVGSSSQPSSTPLPSAGTQSHTATQSKLKPQPCSPAQLPTSASQSPEPQASPSDE 840
Cdd:PRK07764   665 GGDGWPAKAGGAAPAAPPPAPAPAAPAAPAGAAPAQPAPAPAATPPAGQADDPAAQPPQAAQGASAPSPAADDPVPLPPE 744

                          330       340       350
                   ....*....|....*....|....*....|..
gi 1720360873  841 SDSEAQPRGRSRKAlTAEPHPQMPCTPKSRPS 872
Cdd:PRK07764   745 PDDPPDPAGAPAQP-PPPPAPAPAAAPAAAPP 775
PHA03247 PHA03247
large tegument protein UL36; Provisional
 353-895 1.99e-04

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 46.08  E-value: 1.99e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720360873  353 SSPGPSPLPQRHSRSQDSPETRPATRTQPSSetqvhPEAQPGSSTQFSSKSQPEPHPCSGTQVSSEGqtssrtntevqPS 432
Cdd:PHA03247  2567 SVPPPRPAPRPSEPAVTSRARRPDAPPQSAR-----PRAPVDDRGDPRGPAPPSPLPPDTHAPDPPP-----------PS 2630

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720360873  433 SRTRPSSLTQAHPETQLGSSTQSEFQAGSGTQVSPKASSCSRTKVDVLPSSRTRassvtqahPKAQPDSstqlssetqle 512
Cdd:PHA03247  2631 PSPAANEPDPHPPPTVPPPERPRDDPAPGRVSRPRRARRLGRAAQASSPPQRPR--------RRAARPT----------- 2691

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720360873  513 slvgpefqscsktkieaqdnsrtqpssvtqahpkaqLGSVTlvsevqpAFRSQPSPGVQSDSRTQVSSEAqagfgTQSSP 592
Cdd:PHA03247  2692 ------------------------------------VGSLT-------SLADPPPPPPTPEPAPHALVSA-----TPLPP 2723

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720360873  593 RPEPCSKTHLEPDCQPIPRTQPGSEVQPGFEATPhsgaqgnsdtharlrtqASPQvnfcletkstsrTQSGSESGLGSRT 672
Cdd:PHA03247  2724 GPAAARQASPALPAAPAPPAVPAGPATPGGPARP-----------------ARPP------------TTAGPPAPAPPAA 2774

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720360873  673 qihPDRKPCSRAQPDIGTNPDAAAQVMADPQPSRMQPSPVPQPHSGIQTNVRRQLGSEHHPSSQSQKPGSESQPRYETAT 752
Cdd:PHA03247  2775 ---PAAGPPRRLTRPAVASLSESRESLPSPWDPADPPAAVLAPAAALPPAASPAGPLPPPTSAQPTAPPPPPGPPPPSLP 2851

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720360873  753 TMAWPFPE---TWSGLGRRACLGPQARSSEPLTDETQVGSSSQPSSTPLPSAGTQSHTATQSKLKPQPCSPAQLPTSASQ 829
Cdd:PHA03247  2852 LGGSVAPGgdvRRRPPSRSPAAKPAAPARPPVRRLARPAVSRSTESFALPPDQPERPPQPQAPPPPQPQPQPPPPPQPQP 2931

                          490       500       510       520       530       540       550
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1720360873  830 SPEPQASPSDESDSEAQPRGRSrKALTAEPHPQMPC------------TPKSRPSlgLSQSADPTPPRRWHAGSRTQS 895
Cdd:PHA03247  2932 PPPPPPRPQPPLAPTTDPAGAG-EPSGAVPQPWLGAlvpgrvavprfrVPQPAPS--REAPASSTPPLTGHSLSRVSS 3006
PDZ3_MUPP1-like cd06791
PDZ domain 3 of multi-PDZ-domain protein 1 (MUPP1) and PATJ (protein-associated tight junction) ...
 181-263 2.50e-04

PDZ domain 3 of multi-PDZ-domain protein 1 (MUPP1) and PATJ (protein-associated tight junction) and related domains; PDZ (PSD-95 (Postsynaptic density protein 95), Dlg (Discs large protein), and ZO-1 (Zonula occludens-1)) domain 3 of MUPP1 and PATJ, and related domains. MUPP1 and PATJ serve as scaffolding proteins linking different proteins and protein complexes involved in the organization of tight junctions and epithelial polarity. MUPP1 contains an L27 (Lin-2 and Lin-7 binding) domain and 13 PDZ domains. PATJ (also known as INAD-like) contains an L27 domain and ten PDZ domains. MUPP1 and PATJ share several binding partners, including junctional adhesion molecules (JAM), zonula occludens (ZO)-3, Pals1 (protein associated with Lin-7), Par (partitioning defective)-6 proteins, and nectins (adherence junction adhesion molecules). PATJ lacks 3 PDZ domains seen in MUPP1: PDZ6, 9, and 13; consequently, MUPP1 PDZ7 and 8 align with PATJ PDZ6 and 7; and MUPP1 PDZ domains 10-12 align with PATJ PDZ domains 8-10. 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 MUPP1-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: 467253 [Multi-domain]  Cd Length: 89  Bit Score: 41.06  E-value: 2.50e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720360873  181 ETKEVEVTKTEDALGLTItdngAGYA-----------FIKRIKEGSIIN---RIEavcVGDSIEAINDHSIVGCRHYEVA 246
Cdd:cd06791      1 ETFEVELVKDEQGLGITI----AGYVgekasgelsgiFVKSIIPGSAADqdgRIQ---VNDQIIAVDGVNLQGFTNQEAV 73

                           90
                   ....*....|....*..
gi 1720360873  247 KMLRElpKSQPFTLRLV 263
Cdd:cd06791     74 EVLRN--TGQVVHLTLA 88
PDZ2_MAGI-1_3-like cd06732
PDZ domain 2 of membrane-associated guanylate kinase inverted 1 (MAGI-1), MAGI-2, and MAGI-3, ...
 180-264 2.81e-04

PDZ domain 2 of membrane-associated guanylate kinase inverted 1 (MAGI-1), MAGI-2, and MAGI-3, and related domains; PDZ (PSD-95 (Postsynaptic density protein 95), Dlg (Discs large protein), and ZO-1 (Zonula occludens-1)) domain 2 of MAGI1, 2, 3 (MAGI is also known as Membrane-associated guanylate kinase, WW and PDZ domain-containing protein) and related domains. MAGI proteins have been implicated in the control of cell migration and invasion through altering the activity of phosphatase and tensin homolog (PTEN) and modulating Akt signaling. Four MAGI proteins have been identified (MAGI1-3 and MAGIX). MAGI1-3 have 6 PDZ domains and bind to the C-terminus of PTEN via their PDZ2 domain. MAGIX has a single PDZ domain that is related to MAGI1-3 PDZ domain 5. Other binding partners for MAGI1 include JAM4, C-terminal tail of high risk HPV-18 E6, megalin, TRAF6, Kir4.1 (basolateral K+ channel subunit), and cadherin 23; for MAGI2, include DASM1, dendrin, axin, beta- and delta-catenin, neuroligin, hyperpolarization-activated cation channels, beta1-adrenergic receptors, NMDA receptor, and TARPs; and for MAGI3 includes LPA2. 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 MAGI family PDZ2 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: 467214 [Multi-domain]  Cd Length: 82  Bit Score: 40.62  E-value: 2.81e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720360873  180 GETKEVEVTKTEDALGLTITDNGAGyAFIKRIKEgsiINRIEAVCVGDSIEAINDHSIVGCRHYEVAKMLRELPKSQPFT 259
Cdd:cd06732      1 PELVTVPIVKGPMGFGFTIADSPQG-QRVKQILD---PQRCRGLQEGDLIVEINGQNVQNLSHAQVVDVLKECPKGSEVT 76


                   ....*
gi 1720360873  260 LrLVQ 264
Cdd:cd06732     77 L-LVQ 80
PDZ2_Par3-like cd23058
PDZ domain 2 of partitioning defective 3 (Par3), and related domains; PDZ (PSD-95 ...
 180-260 4.86e-04

PDZ domain 2 of partitioning defective 3 (Par3), and related domains; PDZ (PSD-95 (Postsynaptic density protein 95), Dlg (Discs large protein), and ZO-1 (Zonula occludens-1)) domain 2 of Par3 (or PAR3 or Par-3, also known as Atypical PKC isotype-specific-interacting protein, ASIP, Drosophila Bazooka) and related domains. Par3 is a scaffold protein involved in organizing cell polarity across animals. Par3 binds numerous molecules both for its recruitment to one pole of the cell and for downstream contributions to polarized cell function. It regulates cell polarity by targeting the Par complex proteins Par6 and atypical protein kinase C (aPKC) to specific cortical sites. Physical interactions between Par3 and the Par complex include Par3 PDZ domain 1 binding to the Par6 PDZ domain, Par3 PDZ domain 1 and PDZ domain 3 binding the Par6's PDZ-binding motif, and an interaction with an undefined region of aPKC that requires both Par3 PDZ2 and PDZ3. The PDZ domains of Par3 have also been implicated as potential phosphoinositide signaling integrators, since its second PDZ domain binds to phosphoinositides, and the third PDZ interacts with phosphoinositide phosphatase PTEN. 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 Par3 family PDZ2 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: 467271 [Multi-domain]  Cd Length: 93  Bit Score: 40.32  E-value: 4.86e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720360873  180 GETKEVEVTKTEDALGLTIT--DN---GAGYAFIKRI-KEGSIIN--RIEAvcvGDSIEAINDHSIVGCRHYEVAKMLRE 251
Cdd:cd23058      3 GKKLHIQLKKGPEGLGFSITsrDNptgGSGPIYIKNIlPKGAAIQdgRLKA---GDRLLEVNGVDVTGKTQEEVVSLLRS 79


                   ....*....
gi 1720360873  252 LPKSQPFTL 260
Cdd:cd23058     80 TKLGGTVSL 88
PDZ_MPP-like cd06726
PDZ domain of membrane palmitoylated proteins (MPPs), and related domains; PDZ (PSD-95 ...
 185-260 5.53e-04

PDZ domain of membrane palmitoylated proteins (MPPs), and related domains; PDZ (PSD-95 (Postsynaptic density protein 95), Dlg (Discs large protein), and ZO-1 (Zonula occludens-1)) domain of MPP1-7 (also known as MAGUK p55 subfamily members 1-7), and related domains. MPPs comprise a subfamily of a larger group of multidomain proteins, namely, membrane-associated guanylate kinases (MAGUKs). MPPs form diverse protein complexes at the cell membranes, which are involved in a wide range of cellular processes, including establishing proper cell structure, polarity and cell adhesion. MPPs have only one PDZ domain. 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 MPP1-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: 467208 [Multi-domain]  Cd Length: 80  Bit Score: 39.94  E-value: 5.53e-04
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1720360873  185 VEVTKTED-ALGLTITDNGaGYAFIKRIKEGSIINRIEAVCVGDSIEAINDHSIVGCRHYEVAKMLRELPKSQPFTL 260
Cdd:cd06726      3 VEFEKARDePLGATIKMEE-DSVIVARILHGGMAHRSGLLHVGDEILEINGIPVSGKTVDELQKLLSSLSGSVTFKL 78
PDZ pfam00595
PDZ domain; PDZ domains are found in diverse signaling proteins.
 194-261 6.75e-04

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


Pssm-ID: 395476 [Multi-domain]  Cd Length: 81  Bit Score: 39.57  E-value: 6.75e-04
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1720360873  194 LGLTI---TDNGAGYAFIKRIKEGSIINRiEAVCVGDSIEAINDHSIVGCRHYEVAKMLRELPKSQPFTLR 261
Cdd:pfam00595   12 LGFSLkggSDQGDPGIFVSEVLPGGAAEA-GGLKVGDRILSINGQDVENMTHEEAVLALKGSGGKVTLTIL 81
PDZ2_PDZD2-like cd06758
PDZ domain 2 of PDZ domain containing 2 (PDZD2), and related domains; PDZ (PSD-95 ...
 183-254 9.10e-04

PDZ domain 2 of PDZ domain containing 2 (PDZD2), and related domains; PDZ (PSD-95 (Postsynaptic density protein 95), Dlg (Discs large protein), and ZO-1 (Zonula occludens-1)) domain 2 of PDZD2, also known as KIAA0300, PIN-1, activated in prostate cancer (AIPC) and PDZ domain-containing protein 3 (PDZK3). PDZD2 has seven PDZ domains, and is expressed at exceptionally high levels in the pancreas and certain cancer tissues such as prostate cancer. It promotes the proliferation of insulinoma cells and is upregulated during prostate tumorigenesis. In osteosarcoma (OS), the microRNA miR-363 acts as a tumor suppressor by inhibiting PDZD2. 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 PDZD2-like family PDZ2 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: 467239 [Multi-domain]  Cd Length: 88  Bit Score: 39.26  E-value: 9.10e-04
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1720360873  183 KEVEVTKTEDALGLTITdNGAGYA------FIKRIKEGSIINRIEAVCVGDSIEAINDHSIVGCRHYEVAKMLRELPK 254
Cdd:cd06758      3 WKMHLLKEKGGLGIQIT-GGKGSKrgdigiFVAGVEEGGSADRDGRLKKGDELLMINGQSLIGLSHQEAVAILRSSAS 79
PDZ_neurabin-like cd06790
PDZ domain of neurabin-1 and neurabin-2, and related domains; PDZ (PSD-95 (Postsynaptic ...
 184-250 1.43e-03

PDZ domain of neurabin-1 and neurabin-2, and related domains; PDZ (PSD-95 (Postsynaptic density protein 95), Dlg (Discs large protein), and ZO-1 (Zonula occludens-1)) domain of neurabin-1 (also known as protein phosphatase 1 regulatory subunit 9A) and neurabin-2 (also known as spinophilin, and protein phosphatase 1 regulatory subunit 9B), and related domains. Neurabin-1 and neurabin-2 are neuronal scaffolding proteins that play important roles in the regulation of synaptic transmission through their ability to interact with and target protein phosphatase 1 (PP1) to dendritic spines where PP1 dephosphorylates and inactivates glutamate receptors. Neurabin-2 interacts with multiple other synaptic proteins, including synaptic signaling and scaffolding proteins (e.g., GluN1 and SAPAP3) and cytoskeletal proteins (e.g., neurofilament medium polypeptide, NF-M). Neurabin-1 and neurabin-2 also binds F-actin. Other binding partners of neurabin-1 include adenosine A1 receptor (A1R), SAD-1 kinase and 70 kDa ribosomal protein S6 kinase (p70-S6K). This PDZ domain is immediately C-terminal to the PP1 binding domain. 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 neurabin-like PDZ 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: 467252 [Multi-domain]  Cd Length: 90  Bit Score: 38.94  E-value: 1.43e-03
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1720360873  184 EVEVTKTEDALGLTITDNGAGYA--------FIKRIKEGSIINRIEAVCVGDSIEAINDHSIVGCRHYEVAKMLR 250
Cdd:cd06790      4 PVELEKGSEGLGISIIGMGVGADagleklgiFVKTVTEGGAAQRDGRIQVNDQIVEVDGISLVGVTQAFAASVLR 78
PDZ4_MUPP1-like cd06668
PDZ domain 4 of multi-PDZ-domain protein 1 (MUPP1) and PATJ (protein-associated tight junction) ...
 184-260 1.58e-03

PDZ domain 4 of multi-PDZ-domain protein 1 (MUPP1) and PATJ (protein-associated tight junction) and related domains; PDZ (PSD-95 (Postsynaptic density protein 95), Dlg (Discs large protein), and ZO-1 (Zonula occludens-1)) domain 4 of MUPP1 and PATJ, and related domains. MUPP1 and PATJ serve as scaffolding proteins linking different proteins and protein complexes involved in the organization of tight junctions and epithelial polarity. MUPP1 contains an L27 (Lin-2 and Lin-7 binding) domain and 13 PDZ domains. PATJ (also known as INAD-like) contains an L27 domain and ten PDZ domains. MUPP1 and PATJ share several binding partners, including junctional adhesion molecules (JAM), zonula occludens (ZO)-3, Pals1 (protein associated with Lin-7), Par (partitioning defective)-6 proteins, and nectins (adherence junction adhesion molecules). PATJ lacks 3 PDZ domains seen in MUPP1: PDZ6, 9, and 13; consequently, MUPP1 PDZ7 and 8 align with PATJ PDZ6 and 7; and MUPP1 PDZ domains 10-12 align with PATJ PDZ domains 8-10. 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 MUPP1-like family PDZ4 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: 467156 [Multi-domain]  Cd Length: 88  Bit Score: 38.82  E-value: 1.58e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720360873  184 EVEVTKTED-----ALGL----TITDNGAGYAFIKRIKEGSIINRIEAVCVGDSIEAINDHSIVGCRHYEVAKMLRELPk 254
Cdd:cd06668      1 EIVVAQLSKfsessGLGIslegTVDVEVRGHHYIRSILPEGPVGRNGKLFSGDELLEVNGIQLLGLSHKEVVSILKELP- 79


                   ....*.
gi 1720360873  255 sQPFTL 260
Cdd:cd06668     80 -PPVRL 84
PDZ9_MUPP1-like cd10817
PDZ domain 9 of multi-PDZ-domain protein 1 (MUPP1) and related domains; PDZ (PSD-95 ...
 185-246 1.78e-03

PDZ domain 9 of multi-PDZ-domain protein 1 (MUPP1) and related domains; PDZ (PSD-95 (Postsynaptic density protein 95), Dlg (Discs large protein), and ZO-1 (Zonula occludens-1)) domain 9 of MUPP1. MUPP1 and PATJ serve as scaffolding proteins linking different proteins and protein complexes involved in the organization of tight junctions and epithelial polarity. MUPP1 contains an L27 (Lin-2 and Lin-7 binding) domain and 13 PDZ domains. PATJ (also known as INAD-like) contains an L27 domain and ten PDZ domains. PATJ lacks 3 PDZ domains seen in MUPP1: PDZ6, PDZ9, and PDZ13. This MuPP1-like PDZ9 domain is therefore absent from PATJ. MUPP1 and PATJ share several binding partners, including junctional adhesion molecules (JAM), zonula occludens (ZO)-3, Pals1 (protein associated with Lin-7), Par (partitioning defective)-6 proteins, and nectins (adherence junction adhesion molecules). 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 MUPP1-like family PDZ9 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: 467263 [Multi-domain]  Cd Length: 79  Bit Score: 38.48  E-value: 1.78e-03
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1720360873  185 VEVTKTEDALGLTI----TDNGAgyaFIKRIKEGSIINRIEAVCVGDSIEAINDHSIVGCrHYEVA 246
Cdd:cd10817      2 VELPKDQGGLGIAIseedTENGI---VIKSLTEGGPAAKDGRLKVGDQILAVDDESVVGC-PYEKA 63
PDZ_MPP1-like cd10830
PDZ domain of membrane palmitoylated protein1 (MPP1), and related domains; PDZ (PSD-95 ...
 190-251 2.01e-03

PDZ domain of membrane palmitoylated protein1 (MPP1), and related domains; PDZ (PSD-95 (Postsynaptic density protein 95), Dlg (Discs large protein), and ZO-1 (Zonula occludens-1)) domain of MPP1, and related domains. MPP1 (also known as MAGUK p55 subfamily member 1, erythrocyte membrane protein p55, EMP55) is a membrane-associated guanylate kinase (MAGUK)-like protein which forms a complex with protein 4.1 and glycophorin C (GPC) at the cytoplasmic face of the plasma membrane; this complex is essential for cytoskeleton-membrane linkage in erythrocytes and many non-erythroid cells, and participates in the determination of membrane stability and cell shape. MPP1, by interacting with various scaffold proteins and cytoskeletal proteins in the postsynaptic density, also plays an important role in organizing synaptic and non-synaptic structures. MPP1 is also a component of the Crumbs protein complex in the mammalian retina and may link the Usher protein network and the Crumbs protein complex. The MPP1 PDZ domain binding partners include GPC, ABCC4, and CADM1/Necl-2/SynCAM1. 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 MPP1-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: 467266 [Multi-domain]  Cd Length: 81  Bit Score: 38.31  E-value: 2.01e-03
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1720360873  190 TEDALGLTITDNGAGYAFIKRIKEGSIINRIEAVCVGDSIEAINDHSIVGCRHYEVAKMLRE 251
Cdd:cd10830      9 TEEPMGITLKLNEKQSCIVARILHGGMIHRQGSLHVGDEILEINGKSVTNHSVDQLQKMLKE 70
PDZ4_Scribble-like cd06701
PDZ domain 4 of Drosophila Scribble, human Scribble homolog, and related domains; PDZ (PSD-95 ...
 183-251 2.10e-03

PDZ domain 4 of Drosophila Scribble, human Scribble homolog, and related domains; PDZ (PSD-95 (Postsynaptic density protein 95), Dlg (Discs large protein), and ZO-1 (Zonula occludens-1)) domain 4 of Drosophila Scribble (also known as LAP4), human Scribble homolog (also known as hScrib, LAP4, CriB1, ScrB1 and Vartul), and related domains. They belong to the LAP family, which describes proteins that contain either one or four PDZ domains and 16 LRRs (leucine-rich repeats) and function in controlling cell shape, size and subcellular protein localization. In Drosophila, the Scribble complex, comprising Scribble, discs large, and lethal giant larvae, plays a role in apico-basal cell polarity, in other forms of polarity, including regulation of the actin cytoskeleton, cell signaling and vesicular trafficking, and in tumor development. Mammalian Scribble is important in many aspects of cancer development. Scribble and its homologs can be downregulated or overexpressed in cancer; they have a role in cancer beyond their function in loss of cell polarity. 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 Scribble-like family PDZ4 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: 467185 [Multi-domain]  Cd Length: 98  Bit Score: 38.75  E-value: 2.10e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720360873  183 KEVEVTKTED-ALGLTITDNGAGYA-----------FIKRIKEGSIINRIEAVCVGDSIEAINDHSIVGCRHYEVAKMLR 250
Cdd:cd06701      5 QELTIVKEPGeKLGISIRGGAKGHAgnpldptdegiFISKINPDGAAARDGRLKVGQRILEVNGQSLLGATHQEAVRILR 84


                   .
gi 1720360873  251 E 251
Cdd:cd06701     85 S 85
PHA03378 PHA03378
EBNA-3B; Provisional
 1040-1160 3.18e-03

EBNA-3B; Provisional


Pssm-ID: 223065 [Multi-domain]  Cd Length: 991  Bit Score: 41.59  E-value: 3.18e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720360873 1040 PSTVARPLSFRDSRRPQTPGLQPIKEPKPLTRPQSPSPLTPRAPTPAPSKVAGPWPQDGTQATAGPRPGP-----SLSLL 1114
Cdd:PHA03378   731 PGRARPPAAAPGRARPPAAAPGRARPPAAAPGRARPPAAAPGAPTPQPPPQAPPAPQQRPRGAPTPQPPPqagptSMQLM 810

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1720360873 1115 GPGSPGPDTPQKPALLPKPQLGCQKPNPPT---------ICITPSPSPGSGSLPH 1160
Cdd:PHA03378   811 PRAAPGQQGPTKQILRQLLTGGVKRGRPSLkkpaalerqAAAGPTPSPGSGTSDK 865
PHA03269 PHA03269
envelope glycoprotein C; Provisional
 1038-1163 5.97e-03

envelope glycoprotein C; Provisional


Pssm-ID: 165527 [Multi-domain]  Cd Length: 566  Bit Score: 40.87  E-value: 5.97e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720360873 1038 SQPSTVARP-LSFRDSRRPQTPGLQPIKE----PKPLTRPQSPSPLTPR---APTPAPSKVAGPWPQDGTQATAGPRPGP 1109
Cdd:PHA03269    21 NLNTNIPIPeLHTSAATQKPDPAPAPHQAasraPDPAVAPTSAASRKPDlaqAPTPAASEKFDPAPAPHQAASRAPDPAV 100

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....
gi 1720360873 1110 SLSLlgPGSPGPDTPQKPALLPKPQLGCQKPNPPTICITPSPSPGSGSLPHPSL 1163
Cdd:PHA03269   101 APQL--AAAPKPDAAEAFTSAAQAHEAPADAGTSAASKKPDPAAHTQHSPPPFA 152
PDZ12_MUPP1-like cd06675
PDZ domain 12 of multi-PDZ-domain protein 1 (MUPP1), PDZ domain 10 of protein-associated tight ...
 185-250 6.77e-03

PDZ domain 12 of multi-PDZ-domain protein 1 (MUPP1), PDZ domain 10 of protein-associated tight junction (PATJ, and related domains; PDZ (PSD-95 (Postsynaptic density protein 95), Dlg (Discs large protein), and ZO-1 (Zonula occludens-1)) domain 12 of MUPP1, PDZ domain 10 of PATJ, and related domains. MUPP1 and PATJ serve as scaffolding proteins linking different proteins and protein complexes involved in the organization of tight junctions and epithelial polarity. MUPP1 contains an L27 (Lin-2 and Lin-7 binding) domain and 13 PDZ domains. PATJ (also known as INAD-like) contains an L27 domain and ten PDZ domains. MUPP1 and PATJ share several binding partners, including junctional adhesion molecules (JAM), zonula occludens (ZO)-3, Pals1 (protein associated with Lin-7), Par (partitioning defective)-6 proteins, and nectins (adherence junction adhesion molecules). PATJ lacks 3 PDZ domains seen in MUPP1: PDZ6, 9, and 13; consequently, MUPP1 PDZ7 and 8 align with PATJ PDZ6 and 7; and MUPP1 PDZ domains 10-12 align with PATJ PDZ domains 8-10. 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 MUPP1-like PDZ12 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: 467163 [Multi-domain]  Cd Length: 86  Bit Score: 36.96  E-value: 6.77e-03
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1720360873  185 VEVTKTE-DALGLTITdNGAGY------AFIKRIKEGSIINRIEAVCVGDSIEAINDHSIVGCRHYEVAKMLR 250
Cdd:cd06675      3 VEIKRGPqDSLGISIA-GGVGSplgdvpVFIAMIQPNGVAAQTGKLKVGDRIVSINGQSTDGLTHSEAVNLLK 74
PDZ4_LNX1_2-like cd06680
PDZ domain 4 of human Ligand of Numb protein X 1 (LNX1) and LNX2, and related domains; PDZ ...
 207-259 6.93e-03

PDZ domain 4 of human Ligand of Numb protein X 1 (LNX1) and LNX2, and related domains; PDZ (PSD-95 (Postsynaptic density protein 95), Dlg (Discs large protein), and ZO-1 (Zonula occludens-1)) domain 4 of LNX1 (also known as PDZ domain-containing RING finger protein 2, PDZRN2)and LNX2 (also known as PDZ domain-containing RING finger protein 1, PDZRN1), and related domains. LNX1 and LNX2 are Ring (Really Interesting New Gene) finger and PDZ domain-containing E3 ubiquitin ligases that bind to the cell fate determinant protein NUMB and mediate its ubiquitination. LNX1 can ubiquitinate a number of other ligands including PPFIA1, KLHL11, KIF7 and ERC2. LNX1 and LNX2 each have four PDZ domains. 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 LNX family PDZ4 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: 467168 [Multi-domain]  Cd Length: 89  Bit Score: 36.94  E-value: 6.93e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|...
gi 1720360873  207 FIKRIKEGSIINRIEAVCVGDSIEAINDHSIVGCRHYEVAKMLRELPKSQPFT 259
Cdd:cd06680     31 FVKSIVPGTPAYNDGRLKCGDIILAVNGVSTVGMSHAALVPLLKEQRGRVTLT 83
PHA03307 PHA03307
transcriptional regulator ICP4; Provisional
 773-1159 7.03e-03

transcriptional regulator ICP4; Provisional


Pssm-ID: 223039 [Multi-domain]  Cd Length: 1352  Bit Score: 40.54  E-value: 7.03e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720360873  773 PQARSSEPLTDETQVGSSSQPSSTPLPSAGTQSHTATQSKLKPQPCSPAQlPTSASQSPEPQASPSDESDSEAQPRGRSR 852
Cdd:PHA03307    73 PGPGTEAPANESRSTPTWSLSTLAPASPAREGSPTPPGPSSPDPPPPTPP-PASPPPSPAPDLSEMLRPVGSPGPPPAAS 151

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720360873  853 KALTAEPHPQMPCTPKSRPSLGLsqsADPTPPRRWHAGSRTQSDSGTQTDFQAWPSSGayvgwarHRRSQLQSLTEKEPS 932
Cdd:PHA03307   152 PPAAGASPAAVASDAASSRQAAL---PLSSPEETARAPSSPPAEPPPSTPPAAASPRP-------PRRSSPISASASSPA 221

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720360873  933 SRSLSSSGGRKQHSVTTGASCVPQqntgqwlGSAAHSASRTQVSLQVPSRTGAQPSAGKDSSSRTRlDSSPSPSPSPSPS 1012
Cdd:PHA03307   222 PAPGRSAADDAGASSSDSSSSESS-------GCGWGPENECPLPRPAPITLPTRIWEASGWNGPSS-RPGPASSSSSPRE 293

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720360873 1013 PSPSPSPSPSPSPSPSPSPSPDTSGSQPSTVARPLSFRDSRRPQTPGLQPikePKPLTRPQSPSPLTPRAPTPAPSKVAG 1092
Cdd:PHA03307   294 RSPSPSPSSPGSGPAPSSPRASSSSSSSRESSSSSTSSSSESSRGAAVSP---GPSPSRSPSPSRPPPPADPSSPRKRPR 370

                          330       340       350       360       370       380       390
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1720360873 1093 PWPQDGTQATAGPRPGP---SLSLLGPGSPGPDTPQKPALLPKPQLGCQKPNPPTICITP-------SPSPGSGSLP 1159
Cdd:PHA03307   371 PSRAPSSPAASAGRPTRrraRAAVAGRARRRDATGRFPAGRPRPSPLDAGAASGAFYARYplltpsgEPWPGSPPPP 447
PDZ_MPP3-MPP4-MPP7-like cd06799
PDZ domain of membrane palmitoylated proteins 3 (MPP3), MPP4, and MPP7, and related domains; ...
 183-264 7.36e-03

PDZ domain of membrane palmitoylated proteins 3 (MPP3), MPP4, and MPP7, and related domains; PDZ (PSD-95 (Postsynaptic density protein 95), Dlg (Discs large protein), and ZO-1 (Zonula occludens-1)) domain of MPP3, MPP4, and MPP7, and related domains. MPP3 (also known as MAGUK p55 subfamily member 3, erythrocyte membrane protein p55, or EMP55), MPP4 (also known as MAGUK p55 subfamily member 4 or Discs large homolog 6), and MPP7 (also known as MAGUK p55 subfamily member 7) are membrane-associated guanylate kinase (MAGUK)-like proteins. MPP3 is part of a cell adhesion protein complex including tumor suppressor CADM1 and actin-binding protein 4.1B. Participation in the Crumbs cell polarity complex has also been demonstrated for MPP7 in epithelial cells, and for MPP3 and MPP4 in the retina. MPP4 is needed for proper localization of plasma membrane calcium ATPases and maintenance of calcium homeostasis at the rod photoreceptor synaptic terminals. Binding partners of the MPP3 PDZ domain include nectin-3, serotonin 5-hydroxytryptamine, 5-HT(2C) receptor, and a cell adhesion protein, TSLC1 (tumor suppressor in lung cancer 1); fragments of MPP4 having the PDZ domain bind CRB (PDZ-SH3-GUK) and GABA transporter GAT1 (PDZ-SH3). 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 MPP1-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: 467260 [Multi-domain]  Cd Length: 81  Bit Score: 36.45  E-value: 7.36e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720360873  183 KEVEVTKTEDALGLTI-TDNGAGYAFIKRIKEGSIINRIEAVCVGDSIEAINDHSIVGCRHYEVAKMLRELpkSQPFTLR 261
Cdd:cd06799      1 KIVRLVKNNEPLGATIkRDEKTGAIVVARIMRGGAADRSGLIHVGDELREVNGISVEGKDPEEVIQILANS--QGPITFK 78


                   ...
gi 1720360873  262 LVQ 264
Cdd:cd06799     79 LIP 81
PRK10263 PRK10263
DNA translocase FtsK; Provisional
 559-1145 8.29e-03

DNA translocase FtsK; Provisional


Pssm-ID: 236669 [Multi-domain]  Cd Length: 1355  Bit Score: 40.45  E-value: 8.29e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720360873  559 QPAFRSQPSPGVQsdsrTQVSSEAQAGFGTQSSPRPEPCSKTHLEPDCQPIPRTQPGSevQPGFEATPHSGAQGNSDTHA 638
Cdd:PRK10263   355 QPTVAWQPVPGPQ----TGEPVIAPAPEGYPQQSQYAQPAVQYNEPLQQPVQPQQPYY--APAAEQPAQQPYYAPAPEQP 428

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720360873  639 RLRTQASPQVnfcletkstsrtqsgsesglgsrtqihpdrkpcsraqpdigTNPDAAAQVMADPQPSRMQPSPVPQPHSG 718
Cdd:PRK10263   429 AQQPYYAPAP-----------------------------------------EQPVAGNAWQAEEQQSTFAPQSTYQTEQT 467

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720360873  719 IQTNVrRQLGSEHHPSSQSQKPGSESQPRYETATTMAWPFPETWSGLGRRACLGPQ-ARSSEPLTDETQVGSSSQPsSTP 797
Cdd:PRK10263   468 YQQPA-AQEPLYQQPQPVEQQPVVEPEPVVEETKPARPPLYYFEEVEEKRAREREQlAAWYQPIPEPVKEPEPIKS-SLK 545

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720360873  798 LPSAGTQSHTATQSKLKPQPCSPAQlPTSASQSPEPQASPSDESDSEAQPRGRSRKALTAE-PHPQMPCTPKSR--PSLG 874
Cdd:PRK10263   546 APSVAAVPPVEAAAAVSPLASGVKK-ATLATGAAATVAAPVFSLANSGGPRPQVKEGIGPQlPRPKRIRVPTRRelASYG 624

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720360873  875 LSQSADPTPPRRWHAGSRTQSDSGTQ-TDFQAwpssgayvgwarhrRSQLQSLTEKEPSSRSLSSSGGRKQHSVttgasc 953
Cdd:PRK10263   625 IKLPSQRAAEEKAREAQRNQYDSGDQyNDDEI--------------DAMQQDELARQFAQTQQQRYGEQYQHDV------ 684

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720360873  954 vpQQNTGQWLGSAAHSASRTQVSLQVPSRTGAQPsAGKDSSSRTRLDSSPSPSPSPSPSPSPSPSPSPSPSPSPSPSPSP 1033
Cdd:PRK10263   685 --PVNAEDADAAAEAELARQFAQTQQQRYSGEQP-AGANPFSLDDFEFSPMKALLDDGPHEPLFTPIVEPVQQPQQPVAP 761

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720360873 1034 DTSGSQPST-VARPLSFRDSRRPQTPGLQPIKEPKPLT-RPQSPSPLTPRAPTP---APSKVAGPWPQdGTQATAGPRPG 1108
Cdd:PRK10263   762 QQQYQQPQQpVAPQPQYQQPQQPVAPQPQYQQPQQPVApQPQYQQPQQPVAPQPqyqQPQQPVAPQPQ-YQQPQQPVAPQ 840

                          570       580       590
                   ....*....|....*....|....*....|....*....
gi 1720360873 1109 PSLSLLGP--GSPGPDTPQKPALLPKPQLGCQKPNPPTI 1145
Cdd:PRK10263   841 PQDTLLHPllMRNGDSRPLHKPTTPLPSLDLLTPPPSEV 879
PRK07764 PRK07764
DNA polymerase III subunits gamma and tau; Validated
 772-1124 9.16e-03

DNA polymerase III subunits gamma and tau; Validated


Pssm-ID: 236090 [Multi-domain]  Cd Length: 824  Bit Score: 40.35  E-value: 9.16e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720360873  772 GPQARSSEPLTDETQVGSSSQPSSTPLPSAGTQSHTATQSKLKPQP---CSPAQLPTSASQSPEPQASPSDESDSEAQPR 848
Cdd:PRK07764   398 APSAAAAAPAAAPAPAAAAPAAAAAPAPAAAPQPAPAPAPAPAPPSpagNAPAGGAPSPPPAAAPSAQPAPAPAAAPEPT 477

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720360873  849 GRSRKALTAEPHPQMPCTPKSRPSLGLSQSADPTPPRRW-------HAGSR------------TQSDSGTQTDFQAWPSS 909
Cdd:PRK07764   478 AAPAPAPPAAPAPAAAPAAPAAPAAPAGADDAATLRERWpeilaavPKRSRktwaillpeatvLGVRGDTLVLGFSTGGL 557

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720360873  910 GAYVGWARHRRSQLQSLTEK------------EPSSRSLSSSGGRKQHSVTTGASCVPQQnTGQWLGSAAHSASRTQVSL 977
Cdd:PRK07764   558 ARRFASPGNAEVLVTALAEElggdwqveavvgPAPGAAGGEGPPAPASSGPPEEAARPAA-PAAPAAPAAPAPAGAAAAP 636

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720360873  978 QVPSRTGAQPSAGKDSSSRTRLDSSPSPSPSPSPSPSPSPSPSPSPSPSPSPSPSPDTSGSQPSTVARPLSFRDSRRPQT 1057
Cdd:PRK07764   637 AEASAAPAPGVAAPEHHPKHVAVPDASDGGDGWPAKAGGAAPAAPPPAPAPAAPAAPAGAAPAQPAPAPAATPPAGQADD 716

                          330       340       350       360       370       380
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1720360873 1058 PGLQPIKEPKPLTRPQ-SPSPLTPRAPTPAPSKVAGPWPQDGTQATAGPRPGPSLSLLGPGSPGPDTP 1124
Cdd:PRK07764   717 PAAQPPQAAQGASAPSpAADDPVPLPPEPDDPPDPAGAPAQPPPPPAPAPAAAPAAAPPPSPPSEEEE 784
PDZ6_GRIP1-2-like cd06683
PDZ domain 6 of glutamate receptor-interacting protein 1 (GRIP1) and GRIP2, and related ...
 185-239 9.72e-03

PDZ domain 6 of glutamate receptor-interacting protein 1 (GRIP1) and GRIP2, and related domains; PDZ (PSD-95 (Postsynaptic density protein 95), Dlg (Discs large protein), and ZO-1 (Zonula occludens-1)) domain of alpha-amino-3-hydroxy-5-methyl-4-isoxazolepropionic acid receptor (AMPAR) binding proteins GRIP1 (ABP/GRIP2) and GRIP2, and related domains. GRIP1 and GRIP2 each have 7 PDZ domains. The interaction of GRIP1 and GRIP2 with GluA2/3 (AMPAR subunit) regulates AMPAR trafficking and synaptic targeting. GRIP1 has an essential role in regulating AMPAR trafficking during synaptic plasticity and learning and memory. GRIP1 and GRIP2 interact with a variety of other proteins associated with protein trafficking and internalization, for example GRIP1 also interacts with KIF5 (also known as kinesin 1), EphB receptors, scaffold protein liprin-alpha, and the rasGEF GRASP-1. 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 GRIP family PDZ6 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: 467171 [Multi-domain]  Cd Length: 85  Bit Score: 36.51  E-value: 9.72e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 1720360873  185 VEVTKTEDALGLTITdnGAGYAF----IKRIKEGSIINRIEAVCVGDSIEAINDHSIVG 239
Cdd:cd06683      6 VELKRYGGPLGITIS--GTEEPFdpivISGLTEGGLAERTGAIHVGDRILAINGESLRG 62
 
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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