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Conserved domains on  [gi|557948073|ref|NP_001273683|]
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synaptopodin-2 isoform d [Homo sapiens]

Protein Classification

PDZ domain-containing protein( domain architecture ID 10097540)

PDZ (PSD-95, Dlg, and ZO-1/2) domain-containing protein is involved in protein-protein interactions and may play a role in scaffolding supramolecular complexes

CATH:  2.30.42.10
Gene Ontology:  GO:0005515
SCOP:  4001790

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
PDZ_canonical super family cl49608
canonical PDZ domain; Canonical PDZ (PSD-95 (Postsynaptic density protein 95), Dlg (Discs ...
2-54 7.92e-22

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.


The actual alignment was detected with superfamily member cd10820:

Pssm-ID: 483948 [Multi-domain]  Cd Length: 78  Bit Score: 90.45  E-value: 7.92e-22
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 557948073    2 VTQIRNQSKASGSGLCEGDEVVSINGNPCADLTYPEVIKLMESITDSLQMLIK 54
Cdd:cd10820    26 VAKIRKKSKAALAGLCEGDELLSINGKPCADLSHSEAMDLIDSSGDTLQLLIK 78
PHA03247 super family cl33720
large tegument protein UL36; Provisional
562-1039 1.40e-09

large tegument protein UL36; Provisional


The actual alignment was detected with superfamily member PHA03247:

Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 63.03  E-value: 1.40e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557948073  562 PGSVNQPATPFSPTRNMTSPIADF-PAPPPYSAVTPPPDAFSRgvsSPIAGPAQPPPWPQPAPWSQPAFYDSSERIA--S 638
Cdd:PHA03247 2589 PDAPPQSARPRAPVDDRGDPRGPApPSPLPPDTHAPDPPPPSP---SPAANEPDPHPPPTVPPPERPRDDPAPGRVSrpR 2665
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557948073  639 RDERISVPAKRTGILQEAKRRS---TTKPMFTFKEP---KVSPNPELLSLLQNSEGKRGTGAGGDSGPeedylslgaeac 712
Cdd:PHA03247 2666 RARRLGRAAQASSPPQRPRRRAarpTVGSLTSLADPpppPPTPEPAPHALVSATPLPPGPAAARQASP------------ 2733
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557948073  713 nfmqsSSAKQKTPPPVAPKPAVKSSSSQPVTPVSPVWSPGVAPTQPPAFPTSNPSKGTVVSSIKIAQPSYPPARPAS--T 790
Cdd:PHA03247 2734 -----ALPAAPAPPAVPAGPATPGGPARPARPPTTAGPPAPAPPAAPAAGPPRRLTRPAVASLSESRESLPSPWDPAdpP 2808
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557948073  791 LNVAGPFKGPQAAVASQNYTPKPTVSTPTVNAVQPGAVGPSNELPGMSGRGAQlFAKRQSrmekyvvdsdtvqahaARAQ 870
Cdd:PHA03247 2809 AAVLAPAAALPPAASPAGPLPPPTSAQPTAPPPPPGPPPPSLPLGGSVAPGGD-VRRRPP----------------SRSP 2871
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557948073  871 SPTPSLPASWKYSSNVRAPPPVAYNPIHSPSYPLAALKsQPSAAQPSKMGKKKGKKPLNAldvmkHQPYQLNASLFTFQP 950
Cdd:PHA03247 2872 AAKPAAPARPPVRRLARPAVSRSTESFALPPDQPERPP-QPQAPPPPQPQPQPPPPPQPQ-----PPPPPPPRPQPPLAP 2945
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557948073  951 PDAKDGLPQKSSVKVNSALA-------------MKQALPPRPVNAASPTNVQASSVYSVPAYTSPPSFFAEASSPVSASP 1017
Cdd:PHA03247 2946 TTDPAGAGEPSGAVPQPWLGalvpgrvavprfrVPQPAPSREAPASSTPPLTGHSLSRVSSWASSLALHEETDPPPVSLK 3025
                         490       500
                  ....*....|....*....|..
gi 557948073 1018 VPVGIPTSPKQESASSSYFVAP 1039
Cdd:PHA03247 3026 QTLWPPDDTEDSDADSLFDSDS 3047
 
Name Accession Description Interval E-value
PDZ_SYNPO2-like cd10820
PDZ domain of synaptopodin 2 (SYNPO2), synaptopodin 2-like protein (SYNPO2L), and related ...
2-54 7.92e-22

PDZ domain of synaptopodin 2 (SYNPO2), synaptopodin 2-like protein (SYNPO2L), and related domains; PDZ (PSD-95 (Postsynaptic density protein 95), Dlg (Discs large protein), and ZO-1 (Zonula occludens-1)) domain of SYNPO2, SYNPO2L, and related domains. SYNPO2 (also known as genethonin-2, myopodin) is a cytoskeleton adaptor protein. It participates in chaperone-assisted selective autophagy (CASA), a mechanism for the disposal of misfolded and damaged proteins and provides a link between the CASA chaperone complex and a membrane-tethering and fusion machinery that generates autophagosome membranes. The SYNPO2 PPxY motif binds CASA cochaperone BCL2-associated athanogene 3 (BAG3) and the SYNPO2 PDZ domain binds vacuolar protein sorting 18 homolog (VPS18). There are three isoforms of SYNPO2, which possess an amino-terminal PDZ domain (SYNPO2a, b, c); the short isoform SYNPO2d, lacks the 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 SYNPO2-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: 467264 [Multi-domain]  Cd Length: 78  Bit Score: 90.45  E-value: 7.92e-22
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 557948073    2 VTQIRNQSKASGSGLCEGDEVVSINGNPCADLTYPEVIKLMESITDSLQMLIK 54
Cdd:cd10820    26 VAKIRKKSKAALAGLCEGDELLSINGKPCADLSHSEAMDLIDSSGDTLQLLIK 78
PHA03247 PHA03247
large tegument protein UL36; Provisional
562-1039 1.40e-09

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 63.03  E-value: 1.40e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557948073  562 PGSVNQPATPFSPTRNMTSPIADF-PAPPPYSAVTPPPDAFSRgvsSPIAGPAQPPPWPQPAPWSQPAFYDSSERIA--S 638
Cdd:PHA03247 2589 PDAPPQSARPRAPVDDRGDPRGPApPSPLPPDTHAPDPPPPSP---SPAANEPDPHPPPTVPPPERPRDDPAPGRVSrpR 2665
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557948073  639 RDERISVPAKRTGILQEAKRRS---TTKPMFTFKEP---KVSPNPELLSLLQNSEGKRGTGAGGDSGPeedylslgaeac 712
Cdd:PHA03247 2666 RARRLGRAAQASSPPQRPRRRAarpTVGSLTSLADPpppPPTPEPAPHALVSATPLPPGPAAARQASP------------ 2733
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557948073  713 nfmqsSSAKQKTPPPVAPKPAVKSSSSQPVTPVSPVWSPGVAPTQPPAFPTSNPSKGTVVSSIKIAQPSYPPARPAS--T 790
Cdd:PHA03247 2734 -----ALPAAPAPPAVPAGPATPGGPARPARPPTTAGPPAPAPPAAPAAGPPRRLTRPAVASLSESRESLPSPWDPAdpP 2808
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557948073  791 LNVAGPFKGPQAAVASQNYTPKPTVSTPTVNAVQPGAVGPSNELPGMSGRGAQlFAKRQSrmekyvvdsdtvqahaARAQ 870
Cdd:PHA03247 2809 AAVLAPAAALPPAASPAGPLPPPTSAQPTAPPPPPGPPPPSLPLGGSVAPGGD-VRRRPP----------------SRSP 2871
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557948073  871 SPTPSLPASWKYSSNVRAPPPVAYNPIHSPSYPLAALKsQPSAAQPSKMGKKKGKKPLNAldvmkHQPYQLNASLFTFQP 950
Cdd:PHA03247 2872 AAKPAAPARPPVRRLARPAVSRSTESFALPPDQPERPP-QPQAPPPPQPQPQPPPPPQPQ-----PPPPPPPRPQPPLAP 2945
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557948073  951 PDAKDGLPQKSSVKVNSALA-------------MKQALPPRPVNAASPTNVQASSVYSVPAYTSPPSFFAEASSPVSASP 1017
Cdd:PHA03247 2946 TTDPAGAGEPSGAVPQPWLGalvpgrvavprfrVPQPAPSREAPASSTPPLTGHSLSRVSSWASSLALHEETDPPPVSLK 3025
                         490       500
                  ....*....|....*....|..
gi 557948073 1018 VPVGIPTSPKQESASSSYFVAP 1039
Cdd:PHA03247 3026 QTLWPPDDTEDSDADSLFDSDS 3047
PDZ smart00228
Domain present in PSD-95, Dlg, and ZO-1/2; Also called DHR (Dlg homologous region) or GLGF ...
2-57 1.32e-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: 53.15  E-value: 1.32e-08
                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|....*.
gi 557948073      2 VTQIRNQSKASGSGLCEGDEVVSINGNPCADLTYPEVIKLMESITDSLQMLIKRPS 57
Cdd:smart00228   30 VSSVVPGSPAAKAGLRVGDVILEVNGTSVEGLTHLEAVDLLKKAGGKVTLTVLRGG 85
PDZ pfam00595
PDZ domain; PDZ domains are found in diverse signaling proteins.
11-54 2.51e-03

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


Pssm-ID: 395476 [Multi-domain]  Cd Length: 81  Bit Score: 38.03  E-value: 2.51e-03
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....
gi 557948073    11 ASGSGLCEGDEVVSINGNPCADLTYPEVIKLMESITDSLQMLIK 54
Cdd:pfam00595   38 AEAGGLKVGDRILSINGQDVENMTHEEAVLALKGSGGKVTLTIL 81
Herpes_BLLF1 pfam05109
Herpes virus major outer envelope glycoprotein (BLLF1); This family consists of the BLLF1 ...
736-1024 7.48e-03

Herpes virus major outer envelope glycoprotein (BLLF1); This family consists of the BLLF1 viral late glycoprotein, also termed gp350/220. It is the most abundantly expressed glycoprotein in the viral envelope of the Herpesviruses and is the major antigen responsible for stimulating the production of neutralising antibodies in vivo.


Pssm-ID: 282904 [Multi-domain]  Cd Length: 886  Bit Score: 40.67  E-value: 7.48e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557948073   736 SSSSQPVTPvSPvwSPGVAPTQPPAFPTSNPSKGTVVSSIKIAQPSypPARPASTLNVAGPFKG---PQAAVASQN---Y 809
Cdd:pfam05109  482 TSGASPVTP-SP--SPRDNGTESKAPDMTSPTSAVTTPTPNATSPT--PAVTTPTPNATSPTLGktsPTSAVTTPTpnaT 556
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557948073   810 TPKPTVSTPTVNAVQP--GAVGPSNELPGMSGRGAqlfakrqsrmekyvvdSDTVQAHAARAQSPTPSLPASwKYSSNVR 887
Cdd:pfam05109  557 SPTPAVTTPTPNATIPtlGKTSPTSAVTTPTPNAT----------------SPTVGETSPQANTTNHTLGGT-SSTPVVT 619
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557948073   888 APPPVAYNPIHSPSYPLAALKSQPSAAQPSkmGKKKGKKPLNALDVMKHQPyqlnasLFTFQPPDAKDGLPQKSSVKVNS 967
Cdd:pfam05109  620 SPPKNATSAVTTGQHNITSSSTSSMSLRPS--SISETLSPSTSDNSTSHMP------LLTSAHPTGGENITQVTPASTST 691
                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 557948073   968 ALAMKQALPPRPVNAASPTNVQASSVYSVPAYT-----SPPSffaEASSPVSASPVPVGIPT 1024
Cdd:pfam05109  692 HHVSTSSPAPRPGTTSQASGPGNSSTSTKPGEVnvtkgTPPK---NATSPQAPSGQKTAVPT 750
 
Name Accession Description Interval E-value
PDZ_SYNPO2-like cd10820
PDZ domain of synaptopodin 2 (SYNPO2), synaptopodin 2-like protein (SYNPO2L), and related ...
2-54 7.92e-22

PDZ domain of synaptopodin 2 (SYNPO2), synaptopodin 2-like protein (SYNPO2L), and related domains; PDZ (PSD-95 (Postsynaptic density protein 95), Dlg (Discs large protein), and ZO-1 (Zonula occludens-1)) domain of SYNPO2, SYNPO2L, and related domains. SYNPO2 (also known as genethonin-2, myopodin) is a cytoskeleton adaptor protein. It participates in chaperone-assisted selective autophagy (CASA), a mechanism for the disposal of misfolded and damaged proteins and provides a link between the CASA chaperone complex and a membrane-tethering and fusion machinery that generates autophagosome membranes. The SYNPO2 PPxY motif binds CASA cochaperone BCL2-associated athanogene 3 (BAG3) and the SYNPO2 PDZ domain binds vacuolar protein sorting 18 homolog (VPS18). There are three isoforms of SYNPO2, which possess an amino-terminal PDZ domain (SYNPO2a, b, c); the short isoform SYNPO2d, lacks the 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 SYNPO2-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: 467264 [Multi-domain]  Cd Length: 78  Bit Score: 90.45  E-value: 7.92e-22
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 557948073    2 VTQIRNQSKASGSGLCEGDEVVSINGNPCADLTYPEVIKLMESITDSLQMLIK 54
Cdd:cd10820    26 VAKIRKKSKAALAGLCEGDELLSINGKPCADLSHSEAMDLIDSSGDTLQLLIK 78
PHA03247 PHA03247
large tegument protein UL36; Provisional
562-1039 1.40e-09

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 63.03  E-value: 1.40e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557948073  562 PGSVNQPATPFSPTRNMTSPIADF-PAPPPYSAVTPPPDAFSRgvsSPIAGPAQPPPWPQPAPWSQPAFYDSSERIA--S 638
Cdd:PHA03247 2589 PDAPPQSARPRAPVDDRGDPRGPApPSPLPPDTHAPDPPPPSP---SPAANEPDPHPPPTVPPPERPRDDPAPGRVSrpR 2665
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557948073  639 RDERISVPAKRTGILQEAKRRS---TTKPMFTFKEP---KVSPNPELLSLLQNSEGKRGTGAGGDSGPeedylslgaeac 712
Cdd:PHA03247 2666 RARRLGRAAQASSPPQRPRRRAarpTVGSLTSLADPpppPPTPEPAPHALVSATPLPPGPAAARQASP------------ 2733
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557948073  713 nfmqsSSAKQKTPPPVAPKPAVKSSSSQPVTPVSPVWSPGVAPTQPPAFPTSNPSKGTVVSSIKIAQPSYPPARPAS--T 790
Cdd:PHA03247 2734 -----ALPAAPAPPAVPAGPATPGGPARPARPPTTAGPPAPAPPAAPAAGPPRRLTRPAVASLSESRESLPSPWDPAdpP 2808
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557948073  791 LNVAGPFKGPQAAVASQNYTPKPTVSTPTVNAVQPGAVGPSNELPGMSGRGAQlFAKRQSrmekyvvdsdtvqahaARAQ 870
Cdd:PHA03247 2809 AAVLAPAAALPPAASPAGPLPPPTSAQPTAPPPPPGPPPPSLPLGGSVAPGGD-VRRRPP----------------SRSP 2871
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557948073  871 SPTPSLPASWKYSSNVRAPPPVAYNPIHSPSYPLAALKsQPSAAQPSKMGKKKGKKPLNAldvmkHQPYQLNASLFTFQP 950
Cdd:PHA03247 2872 AAKPAAPARPPVRRLARPAVSRSTESFALPPDQPERPP-QPQAPPPPQPQPQPPPPPQPQ-----PPPPPPPRPQPPLAP 2945
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557948073  951 PDAKDGLPQKSSVKVNSALA-------------MKQALPPRPVNAASPTNVQASSVYSVPAYTSPPSFFAEASSPVSASP 1017
Cdd:PHA03247 2946 TTDPAGAGEPSGAVPQPWLGalvpgrvavprfrVPQPAPSREAPASSTPPLTGHSLSRVSSWASSLALHEETDPPPVSLK 3025
                         490       500
                  ....*....|....*....|..
gi 557948073 1018 VPVGIPTSPKQESASSSYFVAP 1039
Cdd:PHA03247 3026 QTLWPPDDTEDSDADSLFDSDS 3047
PDZ smart00228
Domain present in PSD-95, Dlg, and ZO-1/2; Also called DHR (Dlg homologous region) or GLGF ...
2-57 1.32e-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: 53.15  E-value: 1.32e-08
                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|....*.
gi 557948073      2 VTQIRNQSKASGSGLCEGDEVVSINGNPCADLTYPEVIKLMESITDSLQMLIKRPS 57
Cdd:smart00228   30 VSSVVPGSPAAKAGLRVGDVILEVNGTSVEGLTHLEAVDLLKKAGGKVTLTVLRGG 85
PHA03247 PHA03247
large tegument protein UL36; Provisional
553-1124 3.60e-08

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 58.41  E-value: 3.60e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557948073  553 PMNRTAKPFPGSVNQPATPFSPTRNMTSPiADFPAPPPYSAVTPPPDAFSRGVSS-----------PIAGPAQPPPWPQP 621
Cdd:PHA03247 2489 PFAAGAAPDPGGGGPPDPDAPPAPSRLAP-AILPDEPVGEPVHPRMLTWIRGLEElasddagdpppPLPPAAPPAAPDRS 2567
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557948073  622 APWSQPAFYDSSERIASRDERISVPAkrtgilQEAKRRSTTKPMFTFKEPkVSPNPellsllqnsegkrgtgAGGDSGPE 701
Cdd:PHA03247 2568 VPPPRPAPRPSEPAVTSRARRPDAPP------QSARPRAPVDDRGDPRGP-APPSP----------------LPPDTHAP 2624
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557948073  702 EDYLSLGAEACNFMQSSSAKQKTPPPVAPKPAVKSSSSQPVTPVSPVWSPGV-APTQPPAFPTSNPSKGTVVSSIKIAQP 780
Cdd:PHA03247 2625 DPPPPSPSPAANEPDPHPPPTVPPPERPRDDPAPGRVSRPRRARRLGRAAQAsSPPQRPRRRAARPTVGSLTSLADPPPP 2704
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557948073  781 SYPPARPASTLNVAGPFK-GPQAAVASQNYTPKPTVSTPTVNA-VQPGAVGPSNELPGMSGRGAQLF-AKRQSRMEKYVV 857
Cdd:PHA03247 2705 PPTPEPAPHALVSATPLPpGPAAARQASPALPAAPAPPAVPAGpATPGGPARPARPPTTAGPPAPAPpAAPAAGPPRRLT 2784
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557948073  858 DSDTVQAHAARAQSPTPSLPASwkySSNVRAPPPVAYNPIHSPSYPLAALKSQPSAAQPSKMGKKKGKKPLNAL-----D 932
Cdd:PHA03247 2785 RPAVASLSESRESLPSPWDPAD---PPAAVLAPAAALPPAASPAGPLPPPTSAQPTAPPPPPGPPPPSLPLGGSvapggD 2861
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557948073  933 VMKHQPYQLNASLFTFQPPDAKDGLPQKSSVKVNSALAMKQALPPRPVNAASPTNVQASSVYSVPAYTSPPsffaeassp 1012
Cdd:PHA03247 2862 VRRRPPSRSPAAKPAAPARPPVRRLARPAVSRSTESFALPPDQPERPPQPQAPPPPQPQPQPPPPPQPQPP--------- 2932
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557948073 1013 vsasPVPVGIPTSPKQESASSSYFVAPRPKFSAKKSGVTIqeSGRsLSLPGRSVPPPISTSPWVYQPTYSYSSKPTDGLE 1092
Cdd:PHA03247 2933 ----PPPPPRPQPPLAPTTDPAGAGEPSGAVPQPWLGALV--PGR-VAVPRFRVPQPAPSREAPASSTPPLTGHSLSRVS 3005
                         570       580       590
                  ....*....|....*....|....*....|..
gi 557948073 1093 KANKRPTPWEAAAKSPLGLVDDAFQPRNIQES 1124
Cdd:PHA03247 3006 SWASSLALHEETDPPPVSLKQTLWPPDDTEDS 3037
PDZ2_ZO1-like_ds cd06728
PDZ domain 2 of Zonula Occludens-1 (ZO-1), ZO-2 and ZO-3, and related domains; form ...
2-56 6.72e-08

PDZ domain 2 of Zonula Occludens-1 (ZO-1), ZO-2 and ZO-3, and related domains; form domain-swapping dimers; PDZ (PSD-95 (Postsynaptic density protein 95), Dlg (Discs large protein), and ZO-1 (Zonula occludens-1)) domain 2 of ZO-1, -2, -3 and related domains. Zonula occludens proteins (ZO-1, ZO-2, ZO-3) are multi-PDZ domain proteins involved in the maintenance and biogenesis of multi-protein networks at the cytoplasmic surface of intercellular contacts in epithelial and endothelial cells. They have three N-terminal PDZ domains, PDZ1-3, followed by a Src homology-3 (SH3) domain and a guanylate kinase (GuK)-like domain. Among protein-protein interactions for all ZO proteins is the binding of the first PDZ domain (PDZ1) to the C-termini of claudins , and the homo- and hetero-dimerization of ZO-proteins via their second PDZ domain (PDZ2), which takes place by symmetrical domain swapping of the first two beta-strands of PDZ2. At the cell level, ZO-1 and ZO-2 are involved in polarity maintenance, gene transcription, cell proliferation, and tumor cell metastasis. 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 ZO 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: 467210 [Multi-domain]  Cd Length: 79  Bit Score: 51.07  E-value: 6.72e-08
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 557948073    2 VTQIRNQSKASGSG-LCEGDEVVSINGNPCADLTYPEVIKLMESITDSLQMLIKRP 56
Cdd:cd06728    24 VKEITPDSLAAKDGnLQEGDIILKINGTPVENLSLSEAKKLIEKSKDKLQLVVLRD 79
PDZ_canonical cd00136
canonical PDZ domain; Canonical PDZ (PSD-95 (Postsynaptic density protein 95), Dlg (Discs ...
2-54 3.91e-07

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: 48.69  E-value: 3.91e-07
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 557948073    2 VTQIRNQSKASGSG-LCEGDEVVSINGNPCADLTYPEVIKLMESITDSLQMLIK 54
Cdd:cd00136    28 VSRVEPGGPAARDGrLRVGDRILEVNGVSLEGLTHEEAVELLKSAGGEVTLTVR 81
PDZ_PDLIM-like cd06753
PDZ domain of PDZ-LIM family proteins, and related domains; PDZ (PSD-95 (Postsynaptic density ...
9-55 1.32e-05

PDZ domain of PDZ-LIM family proteins, and related domains; PDZ (PSD-95 (Postsynaptic density protein 95), Dlg (Discs large protein), and ZO-1 (Zonula occludens-1)) domain of PDZ-LIM family proteins including PDLIM1-7, and related domains. PDZ-LIM family proteins (also known as Zasp PDZ domain proteins) are involved in the rearrangement of the actin cytoskeleton; they mediate association with the cytoskeleton through alpha-actinin as well as with other proteins involved in signal transduction pathways. Members of this family include PDLIM1 (also known as C-terminal LIM domain protein 1, elfin, LIM domain protein CLP-36), PDLIM2 (also known as PDZ-LIM protein mystique), PDLIM3 (also known as actinin-associated LIM protein, alpha-actinin-2-associated LIM protein, ALP), PDLIM4 (also known as LIM protein RIL, Reversion-induced LIM protein), PDLIM5 (also known as enigma homolog, ENH, enigma-like PDZ and LIM domains protein), PDLIM6 (also known as LIM domain-binding protein 3, ZASP, Cypher, Oracle), and PDLIM7 (also known as PDZ and LIM domain protein 7, LIM mineralization protein, LMP; protein enigma). PDLIM1 has been shown to negatively regulate NF-kappaB-mediated signaling in the cytoplasm. PDLIM7 negatively regulates p53 through binding murine double minute 2 (MDM2). The PDZ domains of PDZ-LIM family proteins PDLIM1, 2, 3, 5, 6, 7 have been shown to bind actin. Other PDZ-LIM family PDZ domain binding partners include thyroid receptor interacting protein-6 (PDLIM4-PDZ), the LIM domain of PDLIM4 (PDLIM4-PDZ), tropomyosin (PDLIM7-PDZ), myotilin and calsarcin 1 (PDLIM6-PDZ), and proteins from the myotilin and FATZ (calsarcin/myozenin) families (PDLIM1, 3, 4, 6 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 PDLIM-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: 467235 [Multi-domain]  Cd Length: 79  Bit Score: 44.44  E-value: 1.32e-05
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*..
gi 557948073    9 SKASGSGLCEGDEVVSINGNPCADLTYPEVIKLMESITDSLQMLIKR 55
Cdd:cd06753    33 GKAAQANLRPGDVILAINGESTEGMTHLEAQNKIKAATGSLSLTLER 79
PDZ1_harmonin cd06737
PDZ domain 1 of harmonin isoforms a, b, and c, and related domains; PDZ (PSD-95 (Postsynaptic ...
2-55 1.90e-04

PDZ domain 1 of harmonin isoforms a, b, and c, and related domains; PDZ (PSD-95 (Postsynaptic density protein 95), Dlg (Discs large protein), and ZO-1 (Zonula occludens-1)) domain 1 of harmonin isoforms a, b, and c, and related domains. Harmonin (also known as Usher Type 1C, PDZ-73 and AIE-75) is a key organizer of the Usher (USH) protein interactome. USH syndrome is the leading cause of hereditary sensory deaf-blindness in humans; three clinically distinct types of USH have been identified, type 1 to 3. The gene encoding harmonin (USH1C) is the causative gene for the USH type 1C phenotype. There are at least 10 alternatively spliced isoforms of harmonin, which are divided into three subclasses (a, b, and c). All isoforms contain the first two PDZ domains and the first coiled-coil domain. The a and b isoforms all have a third PDZ domain. The different PDZ domains are responsible for interactions with all known Usher syndrome type 1 proteins, and most Usher syndrome type 2 proteins. 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 harmonin family PDZ1 domain is a canonical PDZ domain containing six beta-strands A-F and two alpha-helices (alpha-helix 1 and 2), arranged in the order: beta-strands A, B, C, alpha-helix 1, beta-strands D, E, alpha-helix 2 and beta-strand F.


Pssm-ID: 467219 [Multi-domain]  Cd Length: 85  Bit Score: 41.47  E-value: 1.90e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 557948073    2 VTQIRNQSKASGSGLCEGDEVVSINGNPCADLTYPEVIKLMESiTDSLQMLIKR 55
Cdd:cd06737    31 VSHVSPGSQADNKGLRVGDEIVRINGYSISQCTHEEVINLIKT-KKTVSLKVRH 83
PDZ_rhophilin-like cd06712
PDZ domain of rhophilin-1, rhophilin-2, and related domains; PDZ (PSD-95 (Postsynaptic density ...
2-51 7.52e-04

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


Pssm-ID: 467196 [Multi-domain]  Cd Length: 78  Bit Score: 39.49  E-value: 7.52e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 557948073    2 VTQIRNQSKASGSGLCEGDEVVSINGNPCADLTYPEVIKLMESI-TDSLQM 51
Cdd:cd06712    25 VASVDPGSCAAEAGLKEGDYIVSVGGVDCKWSKHSEVVKLLKSAgEEGLEL 75
PDZ_ZASP52-like cd23068
PDZ domain of Drosophila melanogaster PDZ and LIM domain protein Zasp52 (also known as Zasp), ...
1-55 1.18e-03

PDZ domain of Drosophila melanogaster PDZ and LIM domain protein Zasp52 (also known as Zasp), and related domains; PDZ (PSD-95 (Postsynaptic density protein 95), Dlg (Discs large protein), and ZO-1 (Zonula occludens-1)) domain of Drosophila melanogaster Zasp52 and related domains. Drosophila melanogaster Zasp52 (also known as Z band alternatively spliced PDZ-motif protein or Zasp) colocalizes with integrins at myotendinous junctions and with alpha-actinin at Z-disks and is required for muscle attachment as well as Z-disk assembly and maintenance. The Zasp52 actin-binding site includes the extended PDZ domain and the ZM region. The Zasp52-PDZ domain is required for myofibril assembly. 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 Zasp52-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: 467281 [Multi-domain]  Cd Length: 82  Bit Score: 39.05  E-value: 1.18e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 557948073    1 MVTQIRNQSKASGSGLCEGDEVVSINGNPCADLTYPEVIKLMESITDSLQMLIKR 55
Cdd:cd23068    28 SIQKVNPGSPADKAGLRRGDVILRINGTDTSNLTHKQAQDLIKRAGNDLQLTVQR 82
PDZ5_PDZD2-like cd06761
PDZ domain 5 of PDZ domain containing 2 (PDZD2), and related domains; PDZ (PSD-95 ...
10-55 2.04e-03

PDZ domain 5 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 5 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. 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. 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 PDZ5 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: 467242 [Multi-domain]  Cd Length: 85  Bit Score: 38.63  E-value: 2.04e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*.
gi 557948073   10 KASGSGLCEGDEVVSINGNPCADLTYPEVIKLMESITDSLQMLIKR 55
Cdd:cd06761    40 RESMGKLTAGDEIVSINGTPVSAMSYQETCHLMQNLPKSLTLEVQK 85
PDZ pfam00595
PDZ domain; PDZ domains are found in diverse signaling proteins.
11-54 2.51e-03

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


Pssm-ID: 395476 [Multi-domain]  Cd Length: 81  Bit Score: 38.03  E-value: 2.51e-03
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....
gi 557948073    11 ASGSGLCEGDEVVSINGNPCADLTYPEVIKLMESITDSLQMLIK 54
Cdd:pfam00595   38 AEAGGLKVGDRILSINGQDVENMTHEEAVLALKGSGGKVTLTIL 81
PDZ_shroom2_3_4-like cd06750
PDZ domain of shroom2, shroom3, shroom4, and related domains; PDZ (PSD-95 (Postsynaptic ...
2-55 2.70e-03

PDZ domain of shroom2, shroom3, shroom4, and related domains; PDZ (PSD-95 (Postsynaptic density protein 95), Dlg (Discs large protein), and ZO-1 (Zonula occludens-1)) domain of shroom2, shroom3, shroom4, and related domains. Shroom family proteins shroom2 (also known as apical-like protein; protein APXL), shroom3 (also known as shroom-related protein), and shroom4 (also known as second homolog of apical protein) are essential regulators of cell morphology during animal development; they regulate cell architecture by directing the subcellular distribution and activation of Rho kinase (ROCK), which results in the localized activation of non-muscle myosin. The interaction between shroom and ROCK is mediated by the shroom domain 2 (SD2). 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 shroom2,3,4-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: 467232 [Multi-domain]  Cd Length: 82  Bit Score: 38.09  E-value: 2.70e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 557948073    2 VTQIRNQSKASGSG-LCEGDEVVSINGNPCADlTYPEVIKLMESITDSLQMLIKR 55
Cdd:cd06750    29 ISKIEEGGKAASVGkLQVGDEVVNINGVPLSG-SRQEAIQLVKGSHKTLKLVVRR 82
PDZ_MPP-like cd06726
PDZ domain of membrane palmitoylated proteins (MPPs), and related domains; PDZ (PSD-95 ...
2-53 3.42e-03

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: 37.63  E-value: 3.42e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 557948073    2 VTQIRNQSKASGSGLC-EGDEVVSINGNPCADLTYPEVIKLMESITDSLQMLI 53
Cdd:cd06726    26 VARILHGGMAHRSGLLhVGDEILEINGIPVSGKTVDELQKLLSSLSGSVTFKL 78
PDZ3_PTPN13_FRMPD2-like cd06695
PDZ domain 3 of protein tyrosine phosphatase non-receptor type 13 (PTPN13), FERM and PDZ ...
11-56 4.40e-03

PDZ domain 3 of protein tyrosine phosphatase non-receptor type 13 (PTPN13), FERM and PDZ domain-containing protein 2 (FRMPD2), and related domains; PDZ (PSD-95 (Postsynaptic density protein 95), Dlg (Discs large protein), and ZO-1 (Zonula occludens-1)) domain 3 of PTPN13 [also known as Fas-associated protein-tyrosine phosphatase 1 (FAP-1), protein-tyrosine phosphatase 1E (PTP-E1), and protein-tyrosine phosphatase (PTPL1)], FRMPD2 (also known as PDZ domain-containing protein 4; PDZ domain-containing protein 5C), and related domains. PTPN13 regulates negative apoptotic signaling and mediates phosphoinositide 3-kinase (PI3K) signaling. PTPN13 has five PDZ domains. Proteins known to interact with PTPN13 PDZ domains include: PLEKHA1 and PLEKHA2 via PTPN13-PDZ domain 1, Fas receptor and thyroid receptor-interacting protein 6 via PTPN13-PDZ domain 2, nerve growth factor receptor and protein kinase N2 via PTPN13-PDZ domain 3, PDZ and LIM domain 4 (PDLIM4) via PTPN13-PDZ domains 2 and 4, and brain calpain-2 via PTPN13-PDZ domains 3, 4 and 5. Calpain-2-mediated PTPN13 fragments may be involved in abnormal tau aggregation and increased risk for Alzheimer's disease. 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). FRMPD2 is localized in the basolateral membranes of polarized epithelial cells and is associated with tight junction formation and immune response; it contains 3 PDZ domains). The PDZ superfamily includes canonical PDZ domains as well as those with circular permutations and domain swapping mediated by beta-strands. This PTPN13 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: 467181 [Multi-domain]  Cd Length: 90  Bit Score: 37.62  E-value: 4.40e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*..
gi 557948073   11 ASGSGLC-EGDEVVSINGNPCADLTYPEVIKLMESITDSLQMLIKRP 56
Cdd:cd06695    44 AAESGLIqEGDVILAVNGEPLKGLSYQEVLSLLRGAPPEVTLLLCRP 90
PDZ3_PDZD2-PDZ1_hPro-IL-16-like cd06759
PDZ domain 3 of PDZ domain containing 2 (PDZD2), PDZ domain 1 of human pro-interleukin-16 ...
16-45 6.56e-03

PDZ domain 3 of PDZ domain containing 2 (PDZD2), PDZ domain 1 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 3 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. 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 also includes the first PDZ domain (PDZ1) of human pro-interleukin-16 (isoform 1, also known as nPro-Il-16; 1332 amino-acid protein). Precursor IL-16 is cleaved to produce pro-IL-16 and mature IL-16 (derived from the C-terminal 121 AA). 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 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: 467240 [Multi-domain]  Cd Length: 87  Bit Score: 36.87  E-value: 6.56e-03
                          10        20        30
                  ....*....|....*....|....*....|
gi 557948073   16 LCEGDEVVSINGNPCADLTYPEVIKLMESI 45
Cdd:cd06759    48 LKEGDEILEVNGESLQGLTHQEAIQKFKQI 77
PRK12323 PRK12323
DNA polymerase III subunit gamma/tau;
799-1003 6.94e-03

DNA polymerase III subunit gamma/tau;


Pssm-ID: 237057 [Multi-domain]  Cd Length: 700  Bit Score: 40.63  E-value: 6.94e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557948073  799 GPQAAVASQNYTPKPTVSTPTVNAVQPGAVGPSNELPGMSGRGAQLFAKRQSRMEkyvvdSDTVQAHAARAQSPTPSLPA 878
Cdd:PRK12323  373 GPATAAAAPVAQPAPAAAAPAAAAPAPAAPPAAPAAAPAAAAAARAVAAAPARRS-----PAPEALAAARQASARGPGGA 447
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557948073  879 SWKYSSNVRAPPPVAYNPIHSPSYPLAALKSQPSAAQPSKMGKKKGKKPlnaldvmkhQPYQLNASLFTFQPPDAKDGLP 958
Cdd:PRK12323  448 PAPAPAPAAAPAAAARPAAAGPRPVAAAAAAAPARAAPAAAPAPADDDP---------PPWEELPPEFASPAPAQPDAAP 518
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*
gi 557948073  959 QKSSVKVNSALAMKQALPPRPVNAASPTNVQASSVYSVPAYTSPP 1003
Cdd:PRK12323  519 AGWVAESIPDPATADPDDAFETLAPAPAAAPAPRAAAATEPVVAP 563
PDZ_6 pfam17820
PDZ domain; This entry represents the PDZ domain from a wide variety of proteins.
2-55 7.30e-03

PDZ domain; This entry represents the PDZ domain from a wide variety of proteins.


Pssm-ID: 436067 [Multi-domain]  Cd Length: 54  Bit Score: 35.97  E-value: 7.30e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 557948073     2 VTQIRNQSKASGSGLCEGDEVVSINGNPCADLTypEVIKLMESITDS-LQMLIKR 55
Cdd:pfam17820    2 VTAVVPGSPAERAGLRVGDVILAVNGKPVRSLE--DVARLLQGSAGEsVTLTVRR 54
Herpes_BLLF1 pfam05109
Herpes virus major outer envelope glycoprotein (BLLF1); This family consists of the BLLF1 ...
736-1024 7.48e-03

Herpes virus major outer envelope glycoprotein (BLLF1); This family consists of the BLLF1 viral late glycoprotein, also termed gp350/220. It is the most abundantly expressed glycoprotein in the viral envelope of the Herpesviruses and is the major antigen responsible for stimulating the production of neutralising antibodies in vivo.


Pssm-ID: 282904 [Multi-domain]  Cd Length: 886  Bit Score: 40.67  E-value: 7.48e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557948073   736 SSSSQPVTPvSPvwSPGVAPTQPPAFPTSNPSKGTVVSSIKIAQPSypPARPASTLNVAGPFKG---PQAAVASQN---Y 809
Cdd:pfam05109  482 TSGASPVTP-SP--SPRDNGTESKAPDMTSPTSAVTTPTPNATSPT--PAVTTPTPNATSPTLGktsPTSAVTTPTpnaT 556
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557948073   810 TPKPTVSTPTVNAVQP--GAVGPSNELPGMSGRGAqlfakrqsrmekyvvdSDTVQAHAARAQSPTPSLPASwKYSSNVR 887
Cdd:pfam05109  557 SPTPAVTTPTPNATIPtlGKTSPTSAVTTPTPNAT----------------SPTVGETSPQANTTNHTLGGT-SSTPVVT 619
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557948073   888 APPPVAYNPIHSPSYPLAALKSQPSAAQPSkmGKKKGKKPLNALDVMKHQPyqlnasLFTFQPPDAKDGLPQKSSVKVNS 967
Cdd:pfam05109  620 SPPKNATSAVTTGQHNITSSSTSSMSLRPS--SISETLSPSTSDNSTSHMP------LLTSAHPTGGENITQVTPASTST 691
                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 557948073   968 ALAMKQALPPRPVNAASPTNVQASSVYSVPAYT-----SPPSffaEASSPVSASPVPVGIPT 1024
Cdd:pfam05109  692 HHVSTSSPAPRPGTTSQASGPGNSSTSTKPGEVnvtkgTPPK---NATSPQAPSGQKTAVPT 750
PDZ_ARHGAP21_23-like cd06756
PDZ domain of ARHGAP21 and ARHGAP23, and related domains; PDZ (PSD-95 (Postsynaptic density ...
2-53 8.75e-03

PDZ domain of ARHGAP21 and ARHGAP23, and related domains; PDZ (PSD-95 (Postsynaptic density protein 95), Dlg (Discs large protein), and ZO-1 (Zonula occludens-1)) domain of ARHGAP21, ARHGAP23, and related domains. This subfamily includes the GAPs (GTPase activating proteins): ARHGAP21 (Rho GTPase-activating protein 21; also known as Rho GTPase-activating protein 10, Rho-type GTPase-activating protein 21) and ARHGAP23 (Rho GTPase-activating protein 23; also known as Rho-type GTPase-activating protein 23). GAPs deactivate Rho GTPases by accelerating GTP hydrolysis. ARHGAP21/23 interact with a planar cell polarity (PCP) protein Pk1 to regulate a lateral signaling pathway in migrating cells. The ARHGAP21 PDZ domain binds claudin-2. 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 ARHGAP21-23-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: 467238 [Multi-domain]  Cd Length: 109  Bit Score: 37.44  E-value: 8.75e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 557948073    2 VTQIRNQSKASGSGLCEGDEVVSINGNPCADLTYPEVIKLMESITDSLQMLI 53
Cdd:cd06756    57 VKQVKEGGPAHQAGLCTGDRIVKVNGESVIGKTYSQVIALIQNSDSTLELSV 108
PDZ2_DLG5-like cd06765
PDZ domain 2 of Discs Large 5 (Dlg5) and related domains; PDZ (PSD-95 (Postsynaptic density ...
11-55 8.76e-03

PDZ domain 2 of Discs Large 5 (Dlg5) and related domains; PDZ (PSD-95 (Postsynaptic density protein 95), Dlg (Discs large protein), and ZO-1 (Zonula occludens-1)) domain 2 of Drosophila and mammalian Dlg5, and related domains. Dlg5 is a scaffold protein with multiple conserved functions that are independent of each other in regulating growth, cell polarity, and cell adhesion. It has a coiled-coil domain, 4 PDZ domains and a MAGUK domain (an SH3 domain next to a non-catalytically active guanylate kinase domain). Deregulation of Dlg5 has been implicated in the malignancy of several cancer types. 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 Dlg5-like family PSZ2 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: 467246 [Multi-domain]  Cd Length: 77  Bit Score: 36.55  E-value: 8.76e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*
gi 557948073   11 ASGSGLCEGDEVVSINGNPCADLTYPEVIKLMESITDSLQMLIKR 55
Cdd:cd06765    30 AKEGSLTVGDRIIAINGIALDNKSLSECEALLRSCRDSLSLSLMK 74
PRK14951 PRK14951
DNA polymerase III subunits gamma and tau; Provisional
945-1074 9.41e-03

DNA polymerase III subunits gamma and tau; Provisional


Pssm-ID: 237865 [Multi-domain]  Cd Length: 618  Bit Score: 40.08  E-value: 9.41e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557948073  945 LFTFQPPDAKDGLPQKSSvkvnSALAMKQALPPRPVNAASPTNVQASSVySVPAYTSPPSFFAEASSPVSASPVPVGIPT 1024
Cdd:PRK14951  361 LLAFKPAAAAEAAAPAEK----KTPARPEAAAPAAAPVAQAAAAPAPAA-APAAAASAPAAPPAAAPPAPVAAPAAAAPA 435
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 557948073 1025 SPKQESASSsyfVAPRPKFSAKKSGVTIQESGRSLSLPGRSVPPPISTSP 1074
Cdd:PRK14951  436 AAPAAAPAA---VALAPAPPAQAAPETVAIPVRVAPEPAVASAAPAPAAA 482
Atrophin-1 pfam03154
Atrophin-1 family; Atrophin-1 is the protein product of the dentatorubral-pallidoluysian ...
736-1108 9.95e-03

Atrophin-1 family; Atrophin-1 is the protein product of the dentatorubral-pallidoluysian atrophy (DRPLA) gene. DRPLA OMIM:125370 is a progressive neurodegenerative disorder. It is caused by the expansion of a CAG repeat in the DRPLA gene on chromosome 12p. This results in an extended polyglutamine region in atrophin-1, that is thought to confer toxicity to the protein, possibly through altering its interactions with other proteins. The expansion of a CAG repeat is also the underlying defect in six other neurodegenerative disorders, including Huntington's disease. One interaction of expanded polyglutamine repeats that is thought to be pathogenic is that with the short glutamine repeat in the transcriptional coactivator CREB binding protein, CBP. This interaction draws CBP away from its usual nuclear location to the expanded polyglutamine repeat protein aggregates that are characteriztic of the polyglutamine neurodegenerative disorders. This interferes with CBP-mediated transcription and causes cytotoxicity.


Pssm-ID: 460830 [Multi-domain]  Cd Length: 991  Bit Score: 40.14  E-value: 9.95e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557948073   736 SSSSQPVTPVSPVWSPGVAP--TQPPAFPTSNPSKGTVVSSIKIAQPSYPPArPASTLNVAgPFKGPQAAVASQNyTPKP 813
Cdd:pfam03154  193 QAATAGPTPSAPSVPPQGSPatSQPPNQTQSTAAPHTLIQQTPTLHPQRLPS-PHPPLQPM-TQPPPPSQVSPQP-LPQP 269
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557948073   814 TVSTPTVNAVQPGAVGPSN-ELPGMSGRGAQLFAKRQSRMEKYVVDSDTVQAHAARAQSPTPSLPASwkyssnvraPPPV 892
Cdd:pfam03154  270 SLHGQMPPMPHSLQTGPSHmQHPVPPQPFPLTPQSSQSQVPPGPSPAAPGQSQQRIHTPPSQSQLQS---------QQPP 340
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557948073   893 AYNPIHSPSYPLAALKSQPSAAQPSKMGKKKGKKPLNaldVMKHQPYQLNASLftfQPPDAKDGLPQKSSVKVNSA---- 968
Cdd:pfam03154  341 REQPLPPAPLSMPHIKPPPTTPIPQLPNPQSHKHPPH---LSGPSPFQMNSNL---PPPPALKPLSSLSTHHPPSAhppp 414
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557948073   969 ---LAMKQALPPRPvnaASPTNVQASSVYSVPAYTSPPSFFAEASSPVSASPVPVGIPTSPKQESASSSyfvaprPKFSA 1045
Cdd:pfam03154  415 lqlMPQSQQLPPPP---AQPPVLTQSQSLPPPAASHPPTSGLHQVPSQSPFPQHPFVPGGPPPITPPSG------PPTST 485
                          330       340       350       360       370       380
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 557948073  1046 KKSGVTIQESGRSLSLPGRSVPPPISTSpwvyQPTYSYSSKPTDGLEKANKRPTPWEAAAKSP 1108
Cdd:pfam03154  486 SSAMPGIQPPSSASVSSSGPVPAAVSCP----LPPVQIKEEALDEAEEPESPPPPPRSPSPEP 544
 
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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