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Conserved domains on  [gi|25151513|ref|NP_741112|]
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Tyrosine-protein phosphatase 1 [Caenorhabditis elegans]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
PTPc-N3_4 cd14541
catalytic domain of tyrosine-protein phosphatase non-receptor type 21 and type 14; ...
 366-577 3.67e-160

catalytic domain of tyrosine-protein phosphatase non-receptor type 21 and type 14; Tyrosine-protein phosphatase non-receptor type 3 (PTPN3) and type 4 (PTPN4) belong to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. PTPN3 and PTPN4 are large modular proteins containing an N-terminal FERM domain, a PDZ domain and a C-terminal catalytic PTP domain. PTPN3 interacts with mitogen-activated protein kinase p38gamma and serves as its specific phosphatase. PTPN4 functions in TCR cell signaling, apoptosis, cerebellar synaptic plasticity, and innate immune responses.


:

Pssm-ID: 350389 [Multi-domain]  Cd Length: 212  Bit Score: 456.02  E-value: 3.67e-160
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25151513 366 DYINANYVNMEIPSSGIVNRYIACQGPLAHTSSDFWVMVWEQHCTTIVMLTTITERGRVKCHQYWPRVFETQEYGRLMIK 445
Cdd:cd14541   1 DYINANYVNMEIPGSGIVNRYIAAQGPLPNTCADFWQMVWEQKSTLIVMLTTLVERGRVKCHQYWPDLGETMQFGNLQIT 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25151513 446 CIKDKQTTNCCYREFSIRDRNSSEERRVTQMQYIAWPDHGVPDDPKHFIQFVDEVRKARQGSVDPIVVHCSAGIGRTGVL 525
Cdd:cd14541  81 CVSEEVTPSFAFREFILTNTNTGEERHITQMQYLAWPDHGVPDDSSDFLDFVKRVRQNRVGMVEPTVVHCSAGIGRTGVL 160

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|..
gi 25151513 526 ILMETAACLVESNEPVYPLDIVRTMRDQRAMLIQTPGQYTFVCESILRAYHD 577
Cdd:cd14541 161 ITMETAMCLIEANEPVYPLDIVRTMRDQRAMLIQTPSQYRFVCEAILRVYEE 212
PDZ_PTPN3-4-like cd06706
PDZ domain of tyrosine-protein phosphatase non-receptor type 3 (PTPN3), tyrosine-protein ...
 176-266 1.48e-53

PDZ domain of tyrosine-protein phosphatase non-receptor type 3 (PTPN3), tyrosine-protein phosphatase non-receptor type 4 (PTNP4), and related domains; PDZ (PSD-95 (Postsynaptic density protein 95), Dlg (Discs large protein), and ZO-1 (Zonula occludens-1)) domain of PTPN3, PTPN4 and related domains. PTPN3 (also known as protein-tyrosine phosphatase H1, PTP-H1) has a tumor-suppressive or a tumor-promoting role in many cancers. It serves as a specific phosphatase for the MAP kinase p38gamma; the two interact via their PDZ domains and cooperate to promote Ras-induced oncogenesis. Interaction partners of the PTPN3 PDZ domain include p38gamma and human papillomavirus E6 oncoprotein. PTPN4 (also known as protein-tyrosine phosphatase MEG1) plays a role in immunity, learning, synaptic plasticity or cell homeostasis. p38gamma is also an interaction partner of the PTPN4 PDZ domain: PTPN4 regulates neuronal cell homeostasis by protecting neurons against apoptosis; binding of the C terminus of p38gamma to the PDZ domain of PTPN4, antagonizes the catalytic autoinhibition of PTPN4, leading to cell apoptosis. Other interaction partners of the PTPN4 PDZ domain include glutamate receptor subunit GluN2A, and RABV strain G protein, among others. 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 PTPN3-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: 467190 [Multi-domain]  Cd Length: 90  Bit Score: 177.12  E-value: 1.48e-53
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25151513 176 DQVVTIKMRPDRHGRFGFNVKGGADQNYPVIVSRVAPGSSADKCQPRLNEGDQVLFIDGRDVSTMSHDHVVQFIRSARSg 255
Cdd:cd06706   1 DGLVLIRMKPDENGRFGFNVKGGVDQKMPVIVSRVAPGTPADLCIPRLNEGDQVLLINGRDISEHTHDQVVMFIKASRE- 79

                        90
                ....*....|.
gi 25151513 256 LNGGELHLTIR 266
Cdd:cd06706  80 RHSGELVLLVR 90
 
Name Accession Description Interval E-value
PTPc-N3_4 cd14541
catalytic domain of tyrosine-protein phosphatase non-receptor type 21 and type 14; ...
 366-577 3.67e-160

catalytic domain of tyrosine-protein phosphatase non-receptor type 21 and type 14; Tyrosine-protein phosphatase non-receptor type 3 (PTPN3) and type 4 (PTPN4) belong to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. PTPN3 and PTPN4 are large modular proteins containing an N-terminal FERM domain, a PDZ domain and a C-terminal catalytic PTP domain. PTPN3 interacts with mitogen-activated protein kinase p38gamma and serves as its specific phosphatase. PTPN4 functions in TCR cell signaling, apoptosis, cerebellar synaptic plasticity, and innate immune responses.


Pssm-ID: 350389 [Multi-domain]  Cd Length: 212  Bit Score: 456.02  E-value: 3.67e-160
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25151513 366 DYINANYVNMEIPSSGIVNRYIACQGPLAHTSSDFWVMVWEQHCTTIVMLTTITERGRVKCHQYWPRVFETQEYGRLMIK 445
Cdd:cd14541   1 DYINANYVNMEIPGSGIVNRYIAAQGPLPNTCADFWQMVWEQKSTLIVMLTTLVERGRVKCHQYWPDLGETMQFGNLQIT 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25151513 446 CIKDKQTTNCCYREFSIRDRNSSEERRVTQMQYIAWPDHGVPDDPKHFIQFVDEVRKARQGSVDPIVVHCSAGIGRTGVL 525
Cdd:cd14541  81 CVSEEVTPSFAFREFILTNTNTGEERHITQMQYLAWPDHGVPDDSSDFLDFVKRVRQNRVGMVEPTVVHCSAGIGRTGVL 160

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|..
gi 25151513 526 ILMETAACLVESNEPVYPLDIVRTMRDQRAMLIQTPGQYTFVCESILRAYHD 577
Cdd:cd14541 161 ITMETAMCLIEANEPVYPLDIVRTMRDQRAMLIQTPSQYRFVCEAILRVYEE 212
PTPc smart00194
Protein tyrosine phosphatase, catalytic domain;
315-573 5.46e-113

Protein tyrosine phosphatase, catalytic domain;


Pssm-ID: 214550 [Multi-domain]  Cd Length: 259  Bit Score: 337.32  E-value: 5.46e-113
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25151513    315 KVVDHFEMLYRKKPGM-SMNICRLTANLAKNRYRDVCPYDDTRVTLQASP--SGDYINANYVNMEIPSsgivNRYIACQG 391
Cdd:smart00194   1 GLEEEFEKLDRLKPDDeSCTVAAFPENRDKNRYKDVLPYDHTRVKLKPPPgeGSDYINASYIDGPNGP----KAYIATQG 76

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25151513    392 PLAHTSSDFWVMVWEQHCTTIVMLTTITERGRVKCHQYWPR-VFETQEYGRLMIKCIKDKQTTNCCYREFSIRDRNSSEE 470
Cdd:smart00194  77 PLPSTVEDFWRMVWEQKVTVIVMLTELVEKGREKCAQYWPDeEGEPLTYGDITVTLKSVEKVDDYTIRTLEVTNTGCSET 156

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25151513    471 RRVTQMQYIAWPDHGVPDDPKHFIQFVDEVRKARQGSVDPIVVHCSAGIGRTGVLILMETAACLVESNEPVYPLDIVRTM 550
Cdd:smart00194 157 RTVTHYHYTNWPDHGVPESPESILDLIRAVRKSQSTSTGPIVVHCSAGVGRTGTFIAIDILLQQLEAGKEVDIFEIVKEL 236

                          250       260
                   ....*....|....*....|...
gi 25151513    551 RDQRAMLIQTPGQYTFVCESILR 573
Cdd:smart00194 237 RSQRPGMVQTEEQYIFLYRAILE 259
Y_phosphatase pfam00102
Protein-tyrosine phosphatase;
340-572 1.07e-107

Protein-tyrosine phosphatase;


Pssm-ID: 459674 [Multi-domain]  Cd Length: 234  Bit Score: 323.04  E-value: 1.07e-107
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25151513   340 NLAKNRYRDVCPYDDTRVTLQASP-SGDYINANYvnmeIPSSGIVNRYIACQGPLAHTSSDFWVMVWEQHCTTIVMLTTI 418
Cdd:pfam00102   1 NLEKNRYKDVLPYDHTRVKLTGDPgPSDYINASY----IDGYKKPKKYIATQGPLPNTVEDFWRMVWEEKVTIIVMLTEL 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25151513   419 TERGRVKCHQYWPR-VFETQEYGRLMIKCIKDKQTTNCCY-REFSIRDRNSSEERRVTQMQYIAWPDHGVPDDPKHFIQF 496
Cdd:pfam00102  77 EEKGREKCAQYWPEeEGESLEYGDFTVTLKKEKEDEKDYTvRTLEVSNGGSEETRTVKHFHYTGWPDHGVPESPNSLLDL 156

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 25151513   497 VDEVRKARQGSVD-PIVVHCSAGIGRTGVLILMETAACLVESNEPVYPLDIVRTMRDQRAMLIQTPGQYTFVCESIL 572
Cdd:pfam00102 157 LRKVRKSSLDGRSgPIVVHCSAGIGRTGTFIAIDIALQQLEAEGEVDIFQIVKELRSQRPGMVQTLEQYIFLYDAIL 233
PDZ_PTPN3-4-like cd06706
PDZ domain of tyrosine-protein phosphatase non-receptor type 3 (PTPN3), tyrosine-protein ...
 176-266 1.48e-53

PDZ domain of tyrosine-protein phosphatase non-receptor type 3 (PTPN3), tyrosine-protein phosphatase non-receptor type 4 (PTNP4), and related domains; PDZ (PSD-95 (Postsynaptic density protein 95), Dlg (Discs large protein), and ZO-1 (Zonula occludens-1)) domain of PTPN3, PTPN4 and related domains. PTPN3 (also known as protein-tyrosine phosphatase H1, PTP-H1) has a tumor-suppressive or a tumor-promoting role in many cancers. It serves as a specific phosphatase for the MAP kinase p38gamma; the two interact via their PDZ domains and cooperate to promote Ras-induced oncogenesis. Interaction partners of the PTPN3 PDZ domain include p38gamma and human papillomavirus E6 oncoprotein. PTPN4 (also known as protein-tyrosine phosphatase MEG1) plays a role in immunity, learning, synaptic plasticity or cell homeostasis. p38gamma is also an interaction partner of the PTPN4 PDZ domain: PTPN4 regulates neuronal cell homeostasis by protecting neurons against apoptosis; binding of the C terminus of p38gamma to the PDZ domain of PTPN4, antagonizes the catalytic autoinhibition of PTPN4, leading to cell apoptosis. Other interaction partners of the PTPN4 PDZ domain include glutamate receptor subunit GluN2A, and RABV strain G protein, among others. 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 PTPN3-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: 467190 [Multi-domain]  Cd Length: 90  Bit Score: 177.12  E-value: 1.48e-53
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25151513 176 DQVVTIKMRPDRHGRFGFNVKGGADQNYPVIVSRVAPGSSADKCQPRLNEGDQVLFIDGRDVSTMSHDHVVQFIRSARSg 255
Cdd:cd06706   1 DGLVLIRMKPDENGRFGFNVKGGVDQKMPVIVSRVAPGTPADLCIPRLNEGDQVLLINGRDISEHTHDQVVMFIKASRE- 79

                        90
                ....*....|.
gi 25151513 256 LNGGELHLTIR 266
Cdd:cd06706  80 RHSGELVLLVR 90
PHA02742 PHA02742
protein tyrosine phosphatase; Provisional
 331-566 1.72e-41

protein tyrosine phosphatase; Provisional


Pssm-ID: 165109 [Multi-domain]  Cd Length: 303  Bit Score: 152.08  E-value: 1.72e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25151513  331 SMNICRLTANLAKNRYRDVCPYDDTRVTLQASPSG-DYINANYVNmeipSSGIVNRYIACQGPLAHTSSDFWVMVWEQHC 409
Cdd:PHA02742  43 SCNESLELKNMKKCRYPDAPCFDRNRVILKIEDGGdDFINASYVD----GHNAKGRFICTQAPLEETALDFWQAIFQDQV 118

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25151513  410 TTIVMLTTITERGRVKCHQYW-PRVFETQEYGRLMIKCIKDKQTTNCCYREFSIRDRNSSEERRVTQMQYIAWPDHGVPD 488
Cdd:PHA02742 119 RVIVMITKIMEDGKEACYPYWmPHERGKATHGEFKIKTKKIKSFRNYAVTNLCLTDTNTGASLDIKHFAYEDWPHGGLPR 198

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25151513  489 DPKHFIQFVDEVRKAR-QGSVD----------PIVVHCSAGIGRTGVLILMETAACLVESNEPVYPLDIVRTMRDQRAML 557
Cdd:PHA02742 199 DPNKFLDFVLAVREADlKADVDikgenivkepPILVHCSAGLDRAGAFCAIDICISKYNERAIIPLLSIVRDLRKQRHNC 278


                 ....*....
gi 25151513  558 IQTPGQYTF 566
Cdd:PHA02742 279 LSLPQQYIF 287
COG5599 COG5599
Protein tyrosine phosphatase [Signal transduction mechanisms];
340-574 1.23e-38

Protein tyrosine phosphatase [Signal transduction mechanisms];


Pssm-ID: 444335 [Multi-domain]  Cd Length: 282  Bit Score: 143.31  E-value: 1.23e-38
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25151513 340 NLAKNRYRDVCPYDDTRVTlqasPSGDYINANYVnmeipSSGIVNRYIACQGPLAHTSSDFWVMVWEQHCTTIVMLTTIT 419
Cdd:COG5599  42 GSPLNRFRDIQPYKETALR----ANLGYLNANYI-----QVIGNHRYIATQYPLEEQLEDFFQMLFDNNTPVLVVLASDD 112

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25151513 420 E--RGRVKCHQYWPrvfETQEYGRLMIKcIKDKQTTNC----CYREFSIRDRNSSEE-RRVTQMQYIAWPDHGVPDDP-- 490
Cdd:COG5599 113 EisKPKVKMPVYFR---QDGEYGKYEVS-SELTESIQLrdgiEARTYVLTIKGTGQKkIEIPVLHVKNWPDHGAISAEal 188

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25151513 491 KHFIQFVDEVRKARQGSVDPIVVHCSAGIGRTGVLILM-------ETAACLVESNEPvypldIVRTMRDQRAM-LIQTPG 562
Cdd:COG5599 189 KNLADLIDKKEKIKDPDKLLPVVHCRAGVGRTGTLIAClalsksiNALVQITLSVEE-----IVIDMRTSRNGgMVQTSE 263

                       250
                ....*....|....*
gi 25151513 563 QYTF---VCESILRA 574
Cdd:COG5599 264 QLDVlvkLAEQQIRP 278
PDZ pfam00595
PDZ domain; PDZ domains are found in diverse signaling proteins.
 180-266 2.74e-20

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


Pssm-ID: 395476 [Multi-domain]  Cd Length: 81  Bit Score: 85.41  E-value: 2.74e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25151513   180 TIKMRPDRHGRFGFNVKGGADQ-NYPVIVSRVAPGSSAdKCQPrLNEGDQVLFIDGRDVSTMSHDHVVQFIRSArsglnG 258
Cdd:pfam00595   1 QVTLEKDGRGGLGFSLKGGSDQgDPGIFVSEVLPGGAA-EAGG-LKVGDRILSINGQDVENMTHEEAVLALKGS-----G 73


                  ....*...
gi 25151513   259 GELHLTIR 266
Cdd:pfam00595  74 GKVTLTIL 81
PDZ smart00228
Domain present in PSD-95, Dlg, and ZO-1/2; Also called DHR (Dlg homologous region) or GLGF ...
 188-268 3.33e-16

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: 73.95  E-value: 3.33e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25151513    188 HGRFGFNVKGGADQNYPVIVSRVAPGSSADKCQprLNEGDQVLFIDGRDVSTMSHDHVVQFIRSArsglnGGELHLTIRP 267
Cdd:smart00228  11 GGGLGFSLVGGKDEGGGVVVSSVVPGSPAAKAG--LRVGDVILEVNGTSVEGLTHLEAVDLLKKA-----GGKVTLTVLR 83


                   .
gi 25151513    268 N 268
Cdd:smart00228  84 G 84
CtpA COG0793
C-terminal processing protease CtpA/Prc, contains a PDZ domain [Posttranslational modification, ...
 205-268 2.77e-05

C-terminal processing protease CtpA/Prc, contains a PDZ domain [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 440556 [Multi-domain]  Cd Length: 341  Bit Score: 46.40  E-value: 2.77e-05
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 25151513 205 VIVSRVAPGSSADKcqPRLNEGDQVLFIDGRDVSTMSHDHVVQFIRsarsGLNGGELHLTIRPN 268
Cdd:COG0793  73 VVVVSVIPGSPAEK--AGIKPGDIILAIDGKSVAGLTLDDAVKLLR----GKAGTKVTLTIKRP 130
 
Name Accession Description Interval E-value
PTPc-N3_4 cd14541
catalytic domain of tyrosine-protein phosphatase non-receptor type 21 and type 14; ...
 366-577 3.67e-160

catalytic domain of tyrosine-protein phosphatase non-receptor type 21 and type 14; Tyrosine-protein phosphatase non-receptor type 3 (PTPN3) and type 4 (PTPN4) belong to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. PTPN3 and PTPN4 are large modular proteins containing an N-terminal FERM domain, a PDZ domain and a C-terminal catalytic PTP domain. PTPN3 interacts with mitogen-activated protein kinase p38gamma and serves as its specific phosphatase. PTPN4 functions in TCR cell signaling, apoptosis, cerebellar synaptic plasticity, and innate immune responses.


Pssm-ID: 350389 [Multi-domain]  Cd Length: 212  Bit Score: 456.02  E-value: 3.67e-160
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25151513 366 DYINANYVNMEIPSSGIVNRYIACQGPLAHTSSDFWVMVWEQHCTTIVMLTTITERGRVKCHQYWPRVFETQEYGRLMIK 445
Cdd:cd14541   1 DYINANYVNMEIPGSGIVNRYIAAQGPLPNTCADFWQMVWEQKSTLIVMLTTLVERGRVKCHQYWPDLGETMQFGNLQIT 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25151513 446 CIKDKQTTNCCYREFSIRDRNSSEERRVTQMQYIAWPDHGVPDDPKHFIQFVDEVRKARQGSVDPIVVHCSAGIGRTGVL 525
Cdd:cd14541  81 CVSEEVTPSFAFREFILTNTNTGEERHITQMQYLAWPDHGVPDDSSDFLDFVKRVRQNRVGMVEPTVVHCSAGIGRTGVL 160

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|..
gi 25151513 526 ILMETAACLVESNEPVYPLDIVRTMRDQRAMLIQTPGQYTFVCESILRAYHD 577
Cdd:cd14541 161 ITMETAMCLIEANEPVYPLDIVRTMRDQRAMLIQTPSQYRFVCEAILRVYEE 212
PTPc-N3 cd14600
catalytic domain of tyrosine-protein phosphatase non-receptor type 3; Tyrosine-protein ...
 303-577 1.50e-138

catalytic domain of tyrosine-protein phosphatase non-receptor type 3; Tyrosine-protein phosphatase non-receptor type 3 (PTPN3), also called protein-tyrosine phosphatase H1 (PTP-H1), belongs to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. PTPN3 interacts with mitogen-activated protein kinase p38gamma and serves as its specific phosphatase. PTPN3 and p38gamma cooperate to promote Ras-induced oncogenesis. PTPN3 is a large modular protein containing an N-terminal FERM domain, a PDZ domain and a C-terminal catalytic PTP domain. Its PDZ domain binds with the PDZ-binding motif of p38gamma and enables efficient tyrosine dephosphorylation.


Pssm-ID: 350448 [Multi-domain]  Cd Length: 274  Bit Score: 403.46  E-value: 1.50e-138
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25151513 303 SLQLLADSLNSGKVVDHFEMLYRKKPGMSMNICRLTANLAKNRYRDVCPYDDTRVTLQASPsgDYINANYVNMEIPSSGI 382
Cdd:cd14600   3 SMAQLKKGLESGTVLIQFEQLYRKKPGLAITCAKLPQNMDKNRYKDVLPYDATRVVLQGNE--DYINASYVNMEIPSANI 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25151513 383 VNRYIACQGPLAHTSSDFWVMVWEQHCTTIVMLTTITERGRVKCHQYWPRVFETQEYGRLMIKCIKDKQTTNCCYREFSI 462
Cdd:cd14600  81 VNKYIATQGPLPHTCAQFWQVVWEQKLSLIVMLTTLTERGRTKCHQYWPDPPDVMEYGGFRVQCHSEDCTIAYVFREMLL 160

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25151513 463 RDRNSSEERRVTQMQYIAWPDHGVPDDPKHFIQFVDEVRKARQGSVdPIVVHCSAGIGRTGVLILMETAACLVESNEPVY 542
Cdd:cd14600 161 TNTQTGEERTVTHLQYVAWPDHGVPDDSSDFLEFVNYVRSKRVENE-PVLVHCSAGIGRTGVLVTMETAMCLTERNQPVY 239

                       250       260       270
                ....*....|....*....|....*....|....*
gi 25151513 543 PLDIVRTMRDQRAMLIQTPGQYTFVCESILRAYHD 577
Cdd:cd14600 240 PLDIVRKMRDQRAMMVQTSSQYKFVCEAILRVYEE 274
PTPc-N4 cd14601
catalytic domain of tyrosine-protein phosphatase non-receptor type 4; Tyrosine-protein ...
 366-577 1.12e-113

catalytic domain of tyrosine-protein phosphatase non-receptor type 4; Tyrosine-protein phosphatase non-receptor type 4 (PTPN4), also called protein-tyrosine phosphatase MEG1, belongs to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. PTPN4 functions in TCR cell signaling, apoptosis, cerebellar synaptic plasticity, and innate immune responses. It specifically inhibits the TRIF-dependent TLR4 pathway by suppressing tyrosine phosphorylation of TRAM. It is a large modular protein containing an N-terminal FERM domain, a PDZ domain and a C-terminal catalytic PTP domain; the PDZ domain regulates the catalytic activity of PTPN4.


Pssm-ID: 350449 [Multi-domain]  Cd Length: 212  Bit Score: 337.69  E-value: 1.12e-113
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25151513 366 DYINANYVNMEIPSSGIVNRYIACQGPLAHTSSDFWVMVWEQHCTTIVMLTTITERGRVKCHQYWPRVFETQEYGRLMIK 445
Cdd:cd14601   1 DYINANYINMEIPSSSIINRYIACQGPLPNTCSDFWQMTWEQGSSMVVMLTTQVERGRVKCHQYWPEPSGSSSYGGFQVT 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25151513 446 CIKDKQTTNCCYREFSIRDRNSSEERRVTQMQYIAWPDHGVPDDPKHFIQFVDEVRKARQGSVDPIVVHCSAGIGRTGVL 525
Cdd:cd14601  81 CHSEEGNPAYVFREMTLTNLEKNESRPLTQIQYIAWPDHGVPDDSSDFLDFVCLVRNKRAGKDEPVVVHCSAGIGRTGVL 160

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|..
gi 25151513 526 ILMETAACLVESNEPVYPLDIVRTMRDQRAMLIQTPGQYTFVCESILRAYHD 577
Cdd:cd14601 161 ITMETAMCLIECNQPVYPLDIVRTMRDQRAMMIQTPSQYRFVCEAILKVYEE 212
PTPc smart00194
Protein tyrosine phosphatase, catalytic domain;
315-573 5.46e-113

Protein tyrosine phosphatase, catalytic domain;


Pssm-ID: 214550 [Multi-domain]  Cd Length: 259  Bit Score: 337.32  E-value: 5.46e-113
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25151513    315 KVVDHFEMLYRKKPGM-SMNICRLTANLAKNRYRDVCPYDDTRVTLQASP--SGDYINANYVNMEIPSsgivNRYIACQG 391
Cdd:smart00194   1 GLEEEFEKLDRLKPDDeSCTVAAFPENRDKNRYKDVLPYDHTRVKLKPPPgeGSDYINASYIDGPNGP----KAYIATQG 76

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25151513    392 PLAHTSSDFWVMVWEQHCTTIVMLTTITERGRVKCHQYWPR-VFETQEYGRLMIKCIKDKQTTNCCYREFSIRDRNSSEE 470
Cdd:smart00194  77 PLPSTVEDFWRMVWEQKVTVIVMLTELVEKGREKCAQYWPDeEGEPLTYGDITVTLKSVEKVDDYTIRTLEVTNTGCSET 156

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25151513    471 RRVTQMQYIAWPDHGVPDDPKHFIQFVDEVRKARQGSVDPIVVHCSAGIGRTGVLILMETAACLVESNEPVYPLDIVRTM 550
Cdd:smart00194 157 RTVTHYHYTNWPDHGVPESPESILDLIRAVRKSQSTSTGPIVVHCSAGVGRTGTFIAIDILLQQLEAGKEVDIFEIVKEL 236

                          250       260
                   ....*....|....*....|...
gi 25151513    551 RDQRAMLIQTPGQYTFVCESILR 573
Cdd:smart00194 237 RSQRPGMVQTEEQYIFLYRAILE 259
Y_phosphatase pfam00102
Protein-tyrosine phosphatase;
340-572 1.07e-107

Protein-tyrosine phosphatase;


Pssm-ID: 459674 [Multi-domain]  Cd Length: 234  Bit Score: 323.04  E-value: 1.07e-107
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25151513   340 NLAKNRYRDVCPYDDTRVTLQASP-SGDYINANYvnmeIPSSGIVNRYIACQGPLAHTSSDFWVMVWEQHCTTIVMLTTI 418
Cdd:pfam00102   1 NLEKNRYKDVLPYDHTRVKLTGDPgPSDYINASY----IDGYKKPKKYIATQGPLPNTVEDFWRMVWEEKVTIIVMLTEL 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25151513   419 TERGRVKCHQYWPR-VFETQEYGRLMIKCIKDKQTTNCCY-REFSIRDRNSSEERRVTQMQYIAWPDHGVPDDPKHFIQF 496
Cdd:pfam00102  77 EEKGREKCAQYWPEeEGESLEYGDFTVTLKKEKEDEKDYTvRTLEVSNGGSEETRTVKHFHYTGWPDHGVPESPNSLLDL 156

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 25151513   497 VDEVRKARQGSVD-PIVVHCSAGIGRTGVLILMETAACLVESNEPVYPLDIVRTMRDQRAMLIQTPGQYTFVCESIL 572
Cdd:pfam00102 157 LRKVRKSSLDGRSgPIVVHCSAGIGRTGTFIAIDIALQQLEAEGEVDIFQIVKELRSQRPGMVQTLEQYIFLYDAIL 233
PTPc cd00047
catalytic domain of protein tyrosine phosphatases; Protein tyrosine phosphatases (PTP, EC 3.1. ...
 367-569 1.41e-86

catalytic domain of protein tyrosine phosphatases; Protein tyrosine phosphatases (PTP, EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides; they regulate phosphotyrosine levels in signal transduction pathways. The depth of the active site cleft renders the enzyme specific for phosphorylated Tyr (pTyr) residues, instead of pSer or pThr. This family has a distinctive active site signature motif, HCSAGxGRxG, and are characterized as either transmembrane, receptor-like or non-transmembrane (soluble) PTPs. Receptor-like PTP domains tend to occur in two copies in the cytoplasmic region of the transmembrane proteins, only one copy may be active.


Pssm-ID: 350343 [Multi-domain]  Cd Length: 200  Bit Score: 267.23  E-value: 1.41e-86
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25151513 367 YINANYvnmeIPSSGIVNRYIACQGPLAHTSSDFWVMVWEQHCTTIVMLTTITERGRVKCHQYWP-RVFETQEYGRLMIK 445
Cdd:cd00047   1 YINASY----IDGYRGPKEYIATQGPLPNTVEDFWRMVWEQKVSVIVMLTNLVEKGREKCERYWPeEGGKPLEYGDITVT 76

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25151513 446 CIKDKQTTNCCYREFSIRDRNSSEERRVTQMQYIAWPDHGVPDDPKHFIQFVDEVRKARQGSVDPIVVHCSAGIGRTGVL 525
Cdd:cd00047  77 LVSEEELSDYTIRTLELSPKGCSESREVTHLHYTGWPDHGVPSSPEDLLALVRRVRKEARKPNGPIVVHCSAGVGRTGTF 156

                       170       180       190       200
                ....*....|....*....|....*....|....*....|....
gi 25151513 526 ILMETAACLVESNEPVYPLDIVRTMRDQRAMLIQTPGQYTFVCE 569
Cdd:cd00047 157 IAIDILLERLEAEGEVDVFEIVKALRKQRPGMVQTLEQYEFIYE 200
R-PTPc-LAR-1 cd14553
catalytic domain of LAR family receptor-type tyrosine-protein phosphatases, repeat 1; The LAR ...
 339-574 3.93e-74

catalytic domain of LAR family receptor-type tyrosine-protein phosphatases, repeat 1; The LAR (leukocyte common antigen-related) family of receptor-type tyrosine-protein phosphatases (RPTPs) include three vertebrate members: LAR (or PTPRF), R-PTP-delta (or PTPRD), and R-PTP-sigma (or PTPRS). They belong to the larger family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. LAR-RPTPs are synaptic adhesion molecules; they bind to distinct synaptic membrane proteins and are physiologically responsible for mediating presynaptic development by shaping various synaptic adhesion pathways. They play roles in various aspects of neuronal development, including axon guidance, neurite extension, and synapse formation and function. LAR-RPTPs contain an extracellular region with three immunoglobulin-like (Ig) domains and four to eight fibronectin type III (FN3) repeats (determined by alternative splicing), a single transmembrane domain, followed by an intracellular region with a membrane-proximal catalytic PTP domain (repeat 1, also called D1) and a membrane-distal non-catalytic PTP-like domain (repeat 2, also called D2). This model represents the catalytic PTP domain (repeat 1).


Pssm-ID: 350401 [Multi-domain]  Cd Length: 238  Bit Score: 236.52  E-value: 3.93e-74
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25151513 339 ANLAKNRYRDVCPYDDTRVTLQA---SPSGDYINANYVNMEIPSsgivNRYIACQGPLAHTSSDFWVMVWEQHCTTIVML 415
Cdd:cd14553   2 VNKPKNRYANVIAYDHSRVILQPiegVPGSDYINANYCDGYRKQ----NAYIATQGPLPETFGDFWRMVWEQRSATIVMM 77

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25151513 416 TTITERGRVKCHQYWP-RVFETqeYGRLMIKCIKDKQTTNCCYREFSIRDRNSSEERRVTQMQYIAWPDHGVPDDPKHFI 494
Cdd:cd14553  78 TKLEERSRVKCDQYWPtRGTET--YGLIQVTLLDTVELATYTVRTFALHKNGSSEKREVRQFQFTAWPDHGVPEHPTPFL 155

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25151513 495 QFVDEVRKARQGSVDPIVVHCSAGIGRTGVLILMEtaaCLVESNEPVYPLDI---VRTMRDQRAMLIQTPGQYTFVCESI 571
Cdd:cd14553 156 AFLRRVKACNPPDAGPIVVHCSAGVGRTGCFIVID---SMLERIKHEKTVDIyghVTCLRAQRNYMVQTEDQYIFIHDAL 232


                ...
gi 25151513 572 LRA 574
Cdd:cd14553 233 LEA 235
PTPc-N20_13 cd14538
catalytic domain of tyrosine-protein phosphatase non-receptor type 20 and type 13; ...
 367-574 6.58e-72

catalytic domain of tyrosine-protein phosphatase non-receptor type 20 and type 13; Tyrosine-protein phosphatase non-receptor type 20 (PTPN20) and type 13 (PTPN13, also known as PTPL1) belong to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. Human PTPN20 is a widely expressed phosphatase with a dynamic subcellular distribution that is targeted to sites of actin polymerization. Human PTPN13 is an important regulator of tumor aggressiveness.


Pssm-ID: 350386 [Multi-domain]  Cd Length: 207  Bit Score: 229.57  E-value: 6.58e-72
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25151513 367 YINANYVNmeIPSSGIVNRYIACQGPLAHTSSDFWVMVWEQHCTTIVMLTTITERGRVKCHQYWPRVFETQ--EYGRLMI 444
Cdd:cd14538   1 YINASHIR--IPVGGDTYHYIACQGPLPNTTGDFWQMVWEQKSEVIAMVTQDVEGGKVKCHRYWPDSLNKPliCGGRLEV 78

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25151513 445 KCIKDKQTTNCCYREFSIRDRNSSEERRVTQMQYIAWPDHGVPDDPKHFIQFVDEVRKARQGSvdPIVVHCSAGIGRTGV 524
Cdd:cd14538  79 SLEKYQSLQDFVIRRISLRDKETGEVHHITHLNFTTWPDHGTPQSADPLLRFIRYMRRIHNSG--PIVVHCSAGIGRTGV 156

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|
gi 25151513 525 LILMETAACLVESNEPVYPLDIVRTMRDQRAMLIQTPGQYTFVCESILRA 574
Cdd:cd14538 157 LITIDVALGLIERDLPFDIQDIVKDLREQRQGMIQTKDQYIFCYKACLEV 206
R3-PTPc cd14548
catalytic domain of R3 subfamily receptor-type tyrosine-protein phosphatases and similar ...
 345-567 3.16e-70

catalytic domain of R3 subfamily receptor-type tyrosine-protein phosphatases and similar proteins; R3 subfamily receptor-type phosphotyrosine phosphatases (RPTP) are characterized by a unique modular composition consisting of multiple extracellular fibronectin type III (FN3) repeats and a single (most RPTP subtypes have two) cytoplasmic catalytic PTP domain. Vertebrate members include receptor-type tyrosine-protein phosphatase-like O (PTPRO), J (PTPRJ), Q (PTPRQ), B (PTPRB), V (PTPRV) and H (PTPRH). They belong to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. Most members are PTPs, except for PTPRQ, which dephosphorylates phosphatidylinositide substrates. PTPRV is characterized only in rodents; its function has been lost in humans. Both vertebrate and invertebrate R3 subfamily RPTPs are involved in the control of a variety of cellular processes, including cell growth, differentiation, mitotic cycle and oncogenic transformation.


Pssm-ID: 350396 [Multi-domain]  Cd Length: 222  Bit Score: 225.70  E-value: 3.16e-70
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25151513 345 RYRDVCPYDDTRVTLQASPS---GDYINANYvnmeIPSSGIVNRYIACQGPLAHTSSDFWVMVWEQHCTTIVMLTTITER 421
Cdd:cd14548   1 RYTNILPYDHSRVKLIPINEeegSDYINANY----IPGYNSPREFIATQGPLPGTKDDFWRMVWEQNSHTIVMLTQCMEK 76

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25151513 422 GRVKCHQYWPRVFETQEYGRLMIKCIKDKQTTNCCYREFSIRdrNSSEERRVTQMQYIAWPDHGVPDDPKHFIQFVDEVR 501
Cdd:cd14548  77 GRVKCDHYWPFDQDPVYYGDITVTMLSESVLPDWTIREFKLE--RGDEVRSVRQFHFTAWPDHGVPEAPDSLLRFVRLVR 154

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 25151513 502 KARQGSVDPIVVHCSAGIGRTGVLILMETAACLVESNEPVYPLDIVRTMRDQRAMLIQTPGQYTFV 567
Cdd:cd14548 155 DYIKQEKGPTIVHCSAGVGRTGTFIALDRLLQQIESEDYVDIFGIVYDLRKHRPLMVQTEAQYIFL 220
PTPc-N9 cd14543
catalytic domain of tyrosine-protein phosphatase non-receptor type 9; Tyrosine-protein ...
 320-566 4.36e-69

catalytic domain of tyrosine-protein phosphatase non-receptor type 9; Tyrosine-protein phosphatase non-receptor type 9 (PTPN9), also called protein-tyrosine phosphatase MEG2, belongs to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. PTPN9 plays an important role in promoting intracellular secretary vesicle fusion in hematopoietic cells and promotes the dephosphorylation of ErbB2 and EGFR in breast cancer cells, leading to impaired activation of STAT5 and STAT3. It also directly dephosphorylates STAT3 at the Tyr705 residue, resulting in its inactivation. PTPN9 has been found to be dysregulated in various human cancers, including breast, colorectal, and gastric cancer.


Pssm-ID: 350391 [Multi-domain]  Cd Length: 271  Bit Score: 224.55  E-value: 4.36e-69
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25151513 320 FEMLYRKKPGMSMNICRLTANLAKNRYRDVCPYDDTRVTLQA---SPSGDYINANYVNmeipssGIVNR--YIACQGPLA 394
Cdd:cd14543   9 YEDIRREPPAGTFLCSLAPANQEKNRYGDVLCLDQSRVKLPKrngDERTDYINANFMD------GYKQKnaYIATQGPLP 82

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25151513 395 HTSSDFWVMVWEQHCTTIVMLTTITERGRVKCHQYWPRVFETQE-YGRL-----MIKCIKD-KQTTnccyreFSIRDRNS 467
Cdd:cd14543  83 KTYSDFWRMVWEQKVLVIVMTTRVVERGRVKCGQYWPLEEGSSLrYGDLtvtnlSVENKEHyKKTT------LEIHNTET 156

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25151513 468 SEERRVTQMQYIAWPDHGVPDDPKHFIQFVDEVRKARQGSVD-------------PIVVHCSAGIGRTGVLILMETaaCL 534
Cdd:cd14543 157 DESRQVTHFQFTSWPDFGVPSSAAALLDFLGEVRQQQALAVKamgdrwkghppgpPIVVHCSAGIGRTGTFCTLDI--CL 234

                       250       260       270
                ....*....|....*....|....*....|....*
gi 25151513 535 VESNEpVYPLDI---VRTMRDQRAMLIQTPGQYTF 566
Cdd:cd14543 235 SQLED-VGTLNVmqtVRRMRTQRAFSIQTPDQYYF 268
PTPc-N13 cd14597
catalytic domain of tyrosine-protein phosphatase non-receptor type 13; Tyrosine-protein ...
 340-572 2.52e-67

catalytic domain of tyrosine-protein phosphatase non-receptor type 13; Tyrosine-protein phosphatase non-receptor type 13 (PTPN13, also known as PTPL1) belongs to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. Human PTPN13 is an important regulator of tumor aggressiveness. It regulates breast cancer cell aggressiveness through direct inactivation of Src kinase. In hepatocellular carcinoma, PTPN13 is a tumor suppressor. PTPN13 contains a FERM domain, five PDZ domains, and a C-terminal catalytic PTP domain. With its PDZ domains, PTPN13 has numerous interacting partners that can actively participate in the regulation of its phosphatase activity or can permit direct or indirect recruitment of tyrosine phosphorylated substrates. Its FERM domain is necessary for localization to the membrane.


Pssm-ID: 350445 [Multi-domain]  Cd Length: 234  Bit Score: 218.55  E-value: 2.52e-67
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25151513 340 NLAKNRYRDVCPYDDTRVTLQASpsGDYINANYVNMEIPSSGIVnrYIACQGPLAHTSSDFWVMVWEQHCTTIVMLTTIT 419
Cdd:cd14597   3 NRKKNRYKNILPYDTTRVPLGDE--GGYINASFIKMPVGDEEFV--YIACQGPLPTTVADFWQMVWEQKSTVIAMMTQEV 78

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25151513 420 ERGRVKCHQYWPRVF--ETQEYGRLMIKCIKDKQTTNCCYREFSIRDRNSSEERRVTQMQYIAWPDHGVPDDPKHFIQFV 497
Cdd:cd14597  79 EGGKIKCQRYWPEILgkTTMVDNRLQLTLVRMQQLKNFVIRVLELEDIQTREVRHITHLNFTAWPDHDTPSQPEQLLTFI 158

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 25151513 498 DEVRKARQGSvdPIVVHCSAGIGRTGVLILMETAACLVESNEPVYPLDIVRTMRDQRAMLIQTPGQYTFVCESIL 572
Cdd:cd14597 159 SYMRHIHKSG--PIITHCSAGIGRSGTLICIDVVLGLISKDLDFDISDIVRTMRLQRHGMVQTEDQYIFCYQVIL 231
PTPc-N11_6 cd14544
catalytic domain of tyrosine-protein phosphatase non-receptor type 11 and type 6; ...
 340-567 6.54e-66

catalytic domain of tyrosine-protein phosphatase non-receptor type 11 and type 6; Tyrosine-protein phosphatase non-receptor type 11 (PTPN11) and type 6 (PTPN6) belong to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. PTPN11 and PTPN6, are also called SH2 domain-containing tyrosine phosphatase 2 (SHP2) and 1 (SHP1), respectively. They contain two tandem SH2 domains: a catalytic PTP domain, and a C-terminal tail with regulatory properties. Although structurally similar, they have different localization and different roles in signal transduction. PTPN11/SHP2 is expressed ubiquitously and plays a positive role in cell signaling, leading to cell activation, while PTPN6/SHP1 expression is restricted mainly to hematopoietic and epithelial cells and functions as a negative regulator of signaling events.


Pssm-ID: 350392 [Multi-domain]  Cd Length: 251  Bit Score: 215.40  E-value: 6.54e-66
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25151513 340 NLAKNRYRDVCPYDDTRVTLQ----ASPSGDYINANYV---NMEIPSSGIVNRYIACQGPLAHTSSDFWVMVWEQHCTTI 412
Cdd:cd14544   1 NKGKNRYKNILPFDHTRVILKdrdpNVPGSDYINANYIrneNEGPTTDENAKTYIATQGCLENTVSDFWSMVWQENSRVI 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25151513 413 VMLTTITERGRVKCHQYWPRVFETQEYGRLMIKCIKDKQTTNCCYREFSI-RDRNSSEERRVTQMQYIAWPDHGVPDDPK 491
Cdd:cd14544  81 VMTTKEVERGKNKCVRYWPDEGMQKQYGPYRVQNVSEHDTTDYTLRELQVsKLDQGDPIREIWHYQYLSWPDHGVPSDPG 160

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25151513 492 HFIQFVDEVRKaRQGSVD---PIVVHCSAGIGRTGVLILMETAACLVESNEPVYPLDIVRTM---RDQRAMLIQTPGQYT 565
Cdd:cd14544 161 GVLNFLEDVNQ-RQESLPhagPIVVHCSAGIGRTGTFIVIDMLLDQIKRKGLDCDIDIQKTIqmvRSQRSGMVQTEAQYK 239


                ..
gi 25151513 566 FV 567
Cdd:cd14544 240 FI 241
R-PTPc-H cd14619
catalytic domain of receptor-type tyrosine-protein phosphatase H; Receptor-type ...
 344-573 4.41e-65

catalytic domain of receptor-type tyrosine-protein phosphatase H; Receptor-type tyrosine-protein phosphatase H (PTPRH or R-PTP-H), also known as stomach cancer-associated protein tyrosine phosphatase 1 (SAP-1), belongs to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. PTPRH is a member of the R3 subfamily of receptor-type phosphotyrosine phosphatases (RPTP), characterized by a unique modular composition consisting of multiple extracellular fibronectin type III (FN3) repeats and a single (most RPTP subtypes have two) cytoplasmic catalytic PTP domain. It is localized specifically at microvilli of the brush border in gastrointestinal epithelial cells. It plays a role in intestinal immunity by regulating CEACAM20 through tyrosine dephosphorylation. It is also a negative regulator of integrin-mediated signaling and may contribute to contact inhibition of cell growth and motility.


Pssm-ID: 350467 [Multi-domain]  Cd Length: 233  Bit Score: 212.83  E-value: 4.41e-65
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25151513 344 NRYRDVCPYDDTRVTL---QASPSGDYINANYvnmeIPSSGIVNRYIACQGPLAHTSSDFWVMVWEQHCTTIVMLTTITE 420
Cdd:cd14619   1 NRFRNVLPYDWSRVPLkpiHEEPGSDYINANY----MPGYWSSQEFIATQGPLPQTVGDFWRMIWEQQSSTIVMLTNCME 76

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25151513 421 RGRVKCHQYWPRVFETQEYGRLMIKCIKDKQTTNCCYREFSIRDRNSSEERRVTQMQYIAWPDHGVPDDPKHFIQFVDEV 500
Cdd:cd14619  77 AGRVKCEHYWPLDYTPCTYGHLRVTVVSEEVMENWTVREFLLKQVEEQKTLSVRHFHFTAWPDHGVPSSTDTLLAFRRLL 156

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 25151513 501 RK--ARQGSVDPIVVHCSAGIGRTGVLILMETAACLVESNEPVYPLDIVRTMRDQRAMLIQTPGQYTFVCESILR 573
Cdd:cd14619 157 RQwlDQTMSGGPTVVHCSAGVGRTGTLIALDVLLQQLQSEGLLGPFSFVQKMRENRPLMVQTESQYVFLHQCILD 231
PTPc-N18 cd14603
catalytic domain of tyrosine-protein phosphatase non-receptor type 18; Tyrosine-protein ...
 324-567 6.86e-65

catalytic domain of tyrosine-protein phosphatase non-receptor type 18; Tyrosine-protein phosphatase non-receptor type 18 (PTPN18), also called brain-derived phosphatase, belongs to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. PTPN18 regulates HER2-mediated cellular functions through defining both its phosphorylation and ubiquitination states. The N-terminal catalytic PTP domain of PTPN18 blocks lysosomal routing and delays the degradation of HER2 by dephosphorylation, and its C-terminal PEST domain promotes K48-linked HER2 ubiquitination and its destruction via the proteasome pathway.


Pssm-ID: 350451 [Multi-domain]  Cd Length: 266  Bit Score: 213.53  E-value: 6.86e-65
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25151513 324 YRKKPGMSMNICRLTANLAKNRYRDVCPYDDTRVTL---QASPSGDYINANYVNmeipssGIVN--RYIACQGPLAHTSS 398
Cdd:cd14603  14 FKADYVCSTVAGGRKENVKKNRYKDILPYDQTRVILsllQEEGHSDYINANFIK------GVDGsrAYIATQGPLSHTVL 87

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25151513 399 DFWVMVWEQHCTTIVMLTTITERGRVKCHQYWPRVFETQEYGRLMIKCIKDKQTT-NCCYREFSIRDRNssEERRVTQMQ 477
Cdd:cd14603  88 DFWRMIWQYGVKVILMACREIEMGKKKCERYWAQEQEPLQTGPFTITLVKEKRLNeEVILRTLKVTFQK--ESRSVSHFQ 165

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25151513 478 YIAWPDHGVPDDPKHFIQFVDEVRKARQGSVDPIVVHCSAGIGRTGVLILMETAACLVESnEPVYP----LDIVRTMRDQ 553
Cdd:cd14603 166 YMAWPDHGIPDSPDCMLAMIELARRLQGSGPEPLCVHCSAGCGRTGVICTVDYVRQLLLT-QRIPPdfsiFDVVLEMRKQ 244

                       250
                ....*....|....
gi 25151513 554 RAMLIQTPGQYTFV 567
Cdd:cd14603 245 RPAAVQTEEQYEFL 258
PTP_fungal cd18533
fungal protein tyrosine phosphatases; This subfamily contains Saccharomyces cerevisiae ...
 367-567 1.15e-64

fungal protein tyrosine phosphatases; This subfamily contains Saccharomyces cerevisiae protein-tyrosine phosphatases 1 (PTP1) and 2 (PTP2), Schizosaccharomyces pombe PTP1, PTP2, and PTP3, and similar fungal proteins. PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides; they regulate phosphotyrosine levels in signal transduction pathways. PTP2, together with PTP3, is the major phosphatase that dephosphorylates and inactivates the MAP kinase HOG1 and also modulates its subcellular localization.


Pssm-ID: 350509 [Multi-domain]  Cd Length: 212  Bit Score: 210.95  E-value: 1.15e-64
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25151513 367 YINANYVNMEIPSSgivNRYIACQGPLAHTSSDFWVMVWEQHCTTIVMLTTITERGRVKCHQYWPRVFETQEYGRLMIKC 446
Cdd:cd18533   1 YINASYITLPGTSS---KRYIATQGPLPATIGDFWKMIWQNNVGVIVMLTPLVENGREKCDQYWPSGEYEGEYGDLTVEL 77

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25151513 447 IKDKQTTNCCY--REFSIRdRNSSEERRVTQMQYIAWPDHGVPDDPKHFIQFVDEVRKARQG--SVDPIVVHCSAGIGRT 522
Cdd:cd18533  78 VSEEENDDGGFivREFELS-KEDGKVKKVYHIQYKSWPDFGVPDSPEDLLTLIKLKRELNDSasLDPPIIVHCSAGVGRT 156

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*.
gi 25151513 523 GVLILMET-----------AACLVESNEPVYplDIVRTMRDQRAMLIQTPGQYTFV 567
Cdd:cd18533 157 GTFIALDSlldelkrglsdSQDLEDSEDPVY--EIVNQLRKQRMSMVQTLRQYIFL 210
PTPc-N21_14 cd14540
catalytic domain of tyrosine-protein phosphatase non-receptor type 21 and type 14; ...
 367-573 3.53e-64

catalytic domain of tyrosine-protein phosphatase non-receptor type 21 and type 14; Tyrosine-protein phosphatase non-receptor type 21 (PTPN21) and type 14 (PTPN14) belong to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. Both PTPN21 and PTPN14 contain an N-terminal FERM domain and a C-terminal catalytic PTP domain, separated by a long intervening sequence.


Pssm-ID: 350388 [Multi-domain]  Cd Length: 219  Bit Score: 209.62  E-value: 3.53e-64
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25151513 367 YINANYVNMEIpsSGIVNRYIACQGPLAHTSSDFWVMVWEQHCTTIVMLTTITERGRVKCHQYWPRV---FETQEYGRLM 443
Cdd:cd14540   1 YINASHITATV--GGKQRFYIAAQGPLQNTVGDFWQMVWEQGVYLVVMVTAEEEGGREKCFRYWPTLggeHDALTFGEYK 78

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25151513 444 IKCIKDKQTTNCCYREFSIRDRNSSEERRVTQMQYIAWPDHGVPDDPKHFIQFVDEVRKARQGSVD---------PIVVH 514
Cdd:cd14540  79 VSTKFSVSSGCYTTTGLRVKHTLSGQSRTVWHLQYTDWPDHGCPEDVSGFLDFLEEINSVRRHTNQdvaghnrnpPTLVH 158

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*....
gi 25151513 515 CSAGIGRTGVLILMETAACLVESNEPVYPLDIVRTMRDQRAMLIQTPGQYTFVCESILR 573
Cdd:cd14540 159 CSAGVGRTGVVILADLMLYCLDHNEELDIPRVLALLRHQRMLLVQTLAQYKFVYNVLIQ 217
PTPc-N14 cd14599
catalytic domain of tyrosine-protein phosphatase non-receptor type 14; Tyrosine-protein ...
 305-567 3.60e-64

catalytic domain of tyrosine-protein phosphatase non-receptor type 14; Tyrosine-protein phosphatase non-receptor type 14 (PTPN14), also called protein-tyrosine phosphatase pez, belongs to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. PTPN14 is a potential tumor suppressor and plays a regulatory role in the Hippo and Wnt/beta-catenin signaling pathways. It contains an N-terminal FERM domain and a C-terminal catalytic PTP domain, separated by a long intervening sequence.


Pssm-ID: 350447 [Multi-domain]  Cd Length: 287  Bit Score: 212.16  E-value: 3.60e-64
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25151513 305 QLLADSLNSGKVVDHFEMLYRKKPGMSMNICRLTANLAKNRYRDVCPYDDTRVTL---QASPSGdYINANYVNMEIpsSG 381
Cdd:cd14599   3 KTLERKLEEGMVFTEYEQIPKKKADGVFTTATLPENAERNRIREVVPYEENRVELvptKENNTG-YINASHIKVTV--GG 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25151513 382 IVNRYIACQGPLAHTSSDFWVMVWEQHCTTIVMLTTITERGRVKCHQYWPRV---FETQEYGRLmiKCIKDKQTTNCCYR 458
Cdd:cd14599  80 EEWHYIATQGPLPHTCHDFWQMVWEQGVNVIAMVTAEEEGGRSKSHRYWPKLgskHSSATYGKF--KVTTKFRTDSGCYA 157

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25151513 459 EFSIRDRN--SSEERRVTQMQYIAWPDHGVPDDPKHFIQFVDEVRKARQ---GSVD-------PIVVHCSAGIGRTGVLI 526
Cdd:cd14599 158 TTGLKVKHllSGQERTVWHLQYTDWPDHGCPEEVQGFLSYLEEIQSVRRhtnSMLDstkncnpPIVVHCSAGVGRTGVVI 237

                       250       260       270       280
                ....*....|....*....|....*....|....*....|.
gi 25151513 527 LMETAACLVESNEPVYPLDIVRTMRDQRAMLIQTPGQYTFV 567
Cdd:cd14599 238 LTELMIGCLEHNEKVEVPVMLRHLREQRMFMIQTIAQYKFV 278
R5-PTPc-1 cd14549
catalytic domain of R5 subfamily receptor-type tyrosine-protein phosphatases, repeat 1; The R5 ...
 367-567 2.58e-63

catalytic domain of R5 subfamily receptor-type tyrosine-protein phosphatases, repeat 1; The R5 subfamily of receptor-type phosphotyrosine phosphatases (RPTP) is composed of receptor-type tyrosine-protein phosphatase Z (PTPRZ) and G (PTPRG). They belong to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. They are type 1 integral membrane proteins consisting of an extracellular region with a carbonic anhydrase-like (CAH) and a fibronectin type III (FN3) domains, and an intracellular region with a catalytic PTP domain (repeat 1) proximal to the membrane, and a catalytically inactive PTP-fold domain (repeat 2) distal to the membrane. This model represents the catalytic PTP domain (repeat 1).


Pssm-ID: 350397 [Multi-domain]  Cd Length: 204  Bit Score: 206.82  E-value: 2.58e-63
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25151513 367 YINANYVnmeiPSSGIVNRYIACQGPLAHTSSDFWVMVWEQHCTTIVMLTTITERGRVKCHQYWPRVfETQEYGRLMIKC 446
Cdd:cd14549   1 YINANYV----DGYNKARAYIATQGPLPSTFDDFWRMVWEQNSAIIVMITNLVERGRRKCDQYWPKE-GTETYGNIQVTL 75

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25151513 447 IKDKQTTNCCYREFSIRDRN------SSEERRVTQMQYIAWPDHGVPDDPKHFIQFVDEVRKARQGSVDPIVVHCSAGIG 520
Cdd:cd14549  76 LSTEVLATYTVRTFSLKNLKlkkvkgRSSERVVYQYHYTQWPDHGVPDYTLPVLSFVRKSSAANPPGAGPIVVHCSAGVG 155

                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*..
gi 25151513 521 RTGVLILMETAACLVESNEPVYPLDIVRTMRDQRAMLIQTPGQYTFV 567
Cdd:cd14549 156 RTGTYIVIDSMLQQIQDKGTVNVFGFLKHIRTQRNYLVQTEEQYIFI 202
PTPc-N1_2 cd14545
catalytic domain of tyrosine-protein phosphatase non-receptor type 1 and type 2; ...
 343-566 1.13e-62

catalytic domain of tyrosine-protein phosphatase non-receptor type 1 and type 2; Tyrosine-protein phosphatase non-receptor type 1 (PTPN1) type 2 (PTPN2) belong to the family of classical tyrosine-specific protein tyrosine phosphatases, (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. PTPN1 (or PTP-1B) is the first PTP to be purified and characterized and is the prototypical intracellular PTP found in a wide variety of human tissues. It dephosphorylates and regulates the activity of a number of receptor tyrosine kinases, including the insulin receptor, the EGF receptor, and the PDGF receptor. PTPN2 (or TCPTP), a tumor suppressor, dephosphorylates and inactivates EGFRs, Src family kinases, Janus-activated kinases (JAKs)-1 and -3, and signal transducer and activators of transcription (STATs)-1, -3 and -5, in a cell type and context-dependent manner.


Pssm-ID: 350393 [Multi-domain]  Cd Length: 231  Bit Score: 206.09  E-value: 1.13e-62
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25151513 343 KNRYRDVCPYDDTRVTLQ-ASPSGDYINANYVnmEIPSSGivNRYIACQGPLAHTSSDFWVMVWEQHCTTIVMLTTITER 421
Cdd:cd14545   1 LNRYRDRDPYDHDRSRVKlKQGDNDYINASLV--EVEEAK--RSYILTQGPLPNTSGHFWQMVWEQNSKAVIMLNKLMEK 76

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25151513 422 GRVKCHQYWPRVfETQEYGR----LMIKCIKDKQTTNCCYREFSIRDRNSSEERRVTQMQYIAWPDHGVPDDPKHFIQFV 497
Cdd:cd14545  77 GQIKCAQYWPQG-EGNAMIFedtgLKVTLLSEEDKSYYTVRTLELENLKTQETREVLHFHYTTWPDFGVPESPAAFLNFL 155

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 25151513 498 DEVRKArqGS----VDPIVVHCSAGIGRTGVLILMETaaCLVE-SNEPVYPLDI---VRTMRDQRAMLIQTPGQYTF 566
Cdd:cd14545 156 QKVRES--GSlssdVGPPVVHCSAGIGRSGTFCLVDT--CLVLiEKGNPSSVDVkkvLLEMRKYRMGLIQTPDQLRF 228
R-PTPc-F-1 cd14626
catalytic domain of receptor-type tyrosine-protein phosphatase F, repeat 1; Receptor-type ...
 337-574 4.80e-62

catalytic domain of receptor-type tyrosine-protein phosphatase F, repeat 1; Receptor-type tyrosine-protein phosphatase F (PTPRF), also known as leukocyte common antigen related (LAR), is the prototypical member of the LAR family of receptor-type tyrosine-protein phosphatases (RPTPs), which belong to the larger family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. PTPRF/LAR plays a role for LAR in cadherin complexes where it associates with and dephosphorylates beta-catenin, a pathway which may be critical for cadherin complex stability and cell-cell association. It also regulates focal adhesions through cyclin-dependent kinase-1 and is involved in axon guidance in the developing nervous system. It also functions in regulating insulin signaling. PTPRF contains an extracellular region with three immunoglobulin-like (Ig) domains and four to eight fibronectin type III (FN3) repeats (determined by alternative splicing), a single transmembrane domain, followed by an intracellular region with a membrane-proximal catalytic PTP domain (repeat 1, also called D1) and a membrane-distal non-catalytic PTP-like domain (repeat 2, also called D2). This model represents the catalytic PTP domain (repeat 1).


Pssm-ID: 350474 [Multi-domain]  Cd Length: 276  Bit Score: 206.43  E-value: 4.80e-62
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25151513 337 LTANLAKNRYRDVCPYDDTRVTL---QASPSGDYINANYVNMEIPSsgivNRYIACQGPLAHTSSDFWVMVWEQHCTTIV 413
Cdd:cd14626  38 LEVNKPKNRYANVIAYDHSRVILtsvDGVPGSDYINANYIDGYRKQ----NAYIATQGPLPETLSDFWRMVWEQRTATIV 113

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25151513 414 MLTTITERGRVKCHQYWPrVFETQEYGRLMIKCIKDKQTTNCCYREFSIRDRNSSEERRVTQMQYIAWPDHGVPDDPKHF 493
Cdd:cd14626 114 MMTRLEEKSRVKCDQYWP-IRGTETYGMIQVTLLDTVELATYSVRTFALYKNGSSEKREVRQFQFMAWPDHGVPEYPTPI 192

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25151513 494 IQFVDEVRKARQGSVDPIVVHCSAGIGRTGVLILMETAACLVESNEPVYPLDIVRTMRDQRAMLIQTPGQYTFVCESILR 573
Cdd:cd14626 193 LAFLRRVKACNPPDAGPMVVHCSAGVGRTGCFIVIDAMLERMKHEKTVDIYGHVTCMRSQRNYMVQTEDQYIFIHEALLE 272


                .
gi 25151513 574 A 574
Cdd:cd14626 273 A 273
R-PTPc-S-1 cd14625
catalytic domain of receptor-type tyrosine-protein phosphatase S, repeat 1; Receptor-type ...
 337-574 7.71e-61

catalytic domain of receptor-type tyrosine-protein phosphatase S, repeat 1; Receptor-type tyrosine-protein phosphatase S (PTPRS), also known as receptor-type tyrosine-protein phosphatase sigma (R-PTP-sigma), belongs to the LAR (leukocyte common antigen-related) family of receptor-type tyrosine-protein phosphatases (RPTPs), which belong to the larger family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. PTPRS is a receptor for glycosaminoglycans, including heparan sulfate proteoglycan and neural chondroitin sulfate proteoglycans (CSPGs), which present a barrier to axon regeneration. It also plays a role in stimulating neurite outgrowth in response to the heparan sulfate proteoglycan GPC2. PTPRS contains an extracellular region with three immunoglobulin-like (Ig) domains and four to eight fibronectin type III (FN3) repeats (determined by alternative splicing), a single transmembrane domain, followed by an intracellular region with a membrane-proximal catalytic PTP domain (repeat 1, also called D1) and a membrane-distal non-catalytic PTP-like domain (repeat 2, also called D2). This model represents the catalytic PTP domain (repeat 1).


Pssm-ID: 350473 [Multi-domain]  Cd Length: 282  Bit Score: 203.40  E-value: 7.71e-61
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25151513 337 LTANLAKNRYRDVCPYDDTRVTLQASPS---GDYINANYVNmeipSSGIVNRYIACQGPLAHTSSDFWVMVWEQHCTTIV 413
Cdd:cd14625  44 LEVNKPKNRYANVIAYDHSRVILQPIEGimgSDYINANYID----GYRKQNAYIATQGPLPETFGDFWRMVWEQRSATVV 119

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25151513 414 MLTTITERGRVKCHQYWPRVfETQEYGRLMIKCIKDKQTTNCCYREFSIRDRNSSEERRVTQMQYIAWPDHGVPDDPKHF 493
Cdd:cd14625 120 MMTKLEEKSRIKCDQYWPSR-GTETYGMIQVTLLDTIELATFCVRTFSLHKNGSSEKREVRQFQFTAWPDHGVPEYPTPF 198

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25151513 494 IQFVDEVRKARQGSVDPIVVHCSAGIGRTGVLILMETaacLVESNEPVYPLDI---VRTMRDQRAMLIQTPGQYTFVCES 570
Cdd:cd14625 199 LAFLRRVKTCNPPDAGPIVVHCSAGVGRTGCFIVIDA---MLERIKHEKTVDIyghVTLMRSQRNYMVQTEDQYSFIHDA 275


                ....
gi 25151513 571 ILRA 574
Cdd:cd14625 276 LLEA 279
PTPc-N6 cd14606
catalytic domain of tyrosine-protein phosphatase non-receptor type 6; Tyrosine-protein ...
 340-573 1.65e-60

catalytic domain of tyrosine-protein phosphatase non-receptor type 6; Tyrosine-protein phosphatase non-receptor type 6 (PTPN6), also called SH2 domain-containing protein-tyrosine phosphatase 1 (SHP1 or SHP-1), belongs to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. PTPN6 expression is restricted mainly to hematopoietic and epithelial cells. It is an important regulator of hematopoietic cells, downregulating pathways that promote cell growth, survival, adhesion, and activation. It regulates glucose homeostasis by modulating insulin signalling in the liver and muscle, and it also negatively regulates bone resorption, affecting both the formation and the function of osteoclasts. PTPN6 contains two tandem SH2 domains, a catalytic PTP domain, and a C-terminal tail with regulatory properties.


Pssm-ID: 350454 [Multi-domain]  Cd Length: 266  Bit Score: 201.65  E-value: 1.65e-60
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25151513 340 NLAKNRYRDVCPYDDTRVTLQAS----PSGDYINANYVNMEIPSSG-IVNRYIACQGPLAHTSSDFWVMVWEQHCTTIVM 414
Cdd:cd14606  18 NKSKNRYKNILPFDHSRVILQGRdsniPGSDYINANYVKNQLLGPDeNAKTYIASQGCLEATVNDFWQMAWQENSRVIVM 97

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25151513 415 LTTITERGRVKCHQYWPRVFETQEYGRLMIKCIKDKQTTNCCYREFSIRDRNSSEE-RRVTQMQYIAWPDHGVPDDPKHF 493
Cdd:cd14606  98 TTREVEKGRNKCVPYWPEVGMQRAYGPYSVTNCGEHDTTEYKLRTLQVSPLDNGELiREIWHYQYLSWPDHGVPSEPGGV 177

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25151513 494 IQFVDEVRKARQG--SVDPIVVHCSAGIGRTGVLILMETAACLVESNEPVYPLDIVRTM---RDQRAMLIQTPGQYTFVC 568
Cdd:cd14606 178 LSFLDQINQRQESlpHAGPIIVHCSAGIGRTGTIIVIDMLMENISTKGLDCDIDIQKTIqmvRAQRSGMVQTEAQYKFIY 257


                ....*
gi 25151513 569 ESILR 573
Cdd:cd14606 258 VAIAQ 262
R-PTPc-V cd14618
catalytic domain of receptor-type tyrosine-protein phosphatase V; Receptor-type ...
 344-572 1.22e-59

catalytic domain of receptor-type tyrosine-protein phosphatase V; Receptor-type tyrosine-protein phosphatase V (PTPRV or R-PTP-V), also known as embryonic stem cell protein-tyrosine phosphatase (ES cell phosphatase) or osteotesticular protein-tyrosine phosphatase (OST-PTP), belongs to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. PTPRV is a member of the R3 subfamily of receptor-type phosphotyrosine phosphatases (RPTP), characterized by a unique modular composition consisting of multiple extracellular fibronectin type III (FN3) repeats and a single (most RPTP subtypes have two) cytoplasmic catalytic PTP domain. In rodents, it may play a role in the maintenance of pluripotency and may function in signaling pathways during bone remodeling. It is the only PTP whose function has been lost between rodent and human. The human OST-PTP gene is a pseudogene.


Pssm-ID: 350466 [Multi-domain]  Cd Length: 230  Bit Score: 198.24  E-value: 1.22e-59
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25151513 344 NRYRDVCPYDDTRVTLQ---ASPSGDYINANYvnmeIPSSGIVNRYIACQGPLAHTSSDFWVMVWEQHCTTIVMLTTITE 420
Cdd:cd14618   1 NRYPHVLPYDHSRVRLSqlgGEPHSDYINANF----IPGYTSPQEFIATQGPLKKTIEDFWRLVWEQQVCNIIMLTVGME 76

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25151513 421 RGRVKCHQYWPRVFETQEYGRLMIKCIKDKQTTNCCYREFSIRDRNSSEERRVTQMQYIAWPDHGVPDDPKHFIQFVDEV 500
Cdd:cd14618  77 NGRVLCDHYWPSESTPVSYGHITVHLLAQSSEDEWTRREFKLWHEDLRKERRVKHLHYTAWPDHGIPESTSSLMAFRELV 156

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 25151513 501 R---KARQGSvDPIVVHCSAGIGRTGVLILMETAACLVESNEPVYPLDIVRTMRDQRAMLIQTPGQYTFVCESIL 572
Cdd:cd14618 157 RehvQATKGK-GPTLVHCSAGVGRSGTFIALDRLLRQLKEEKVVDVFNTVYILRMHRYLMIQTLSQYIFLHSCIL 230
R-PTPc-B cd14617
catalytic domain of receptor-type tyrosine-protein phosphatase B; Receptor-type ...
 344-567 1.93e-59

catalytic domain of receptor-type tyrosine-protein phosphatase B; Receptor-type tyrosine-protein phosphatase B (PTPRB), also known as receptor-type tyrosine-protein phosphatase beta (R-PTP-beta) or vascular endothelial protein tyrosine phosphatase(VE-PTP), belongs to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. PTPRB/VE-PTP is a member of the R3 subfamily of receptor-type phosphotyrosine phosphatases (RPTP), characterized by a unique modular composition consisting of multiple extracellular fibronectin type III (FN3) repeats and a single (most RPTP subtypes have two) cytoplasmic catalytic PTP domain. It is expressed specifically in vascular endothelial cells and it plays an important role in blood vessel remodeling and angiogenesis.


Pssm-ID: 350465 [Multi-domain]  Cd Length: 228  Bit Score: 197.83  E-value: 1.93e-59
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25151513 344 NRYRDVCPYDDTRVTL---QASPSGDYINANYvnmeIPSSGIVNRYIACQGPLAHTSSDFWVMVWEQHCTTIVMLTTITE 420
Cdd:cd14617   1 NRYNNILPYDSTRVKLsnvDDDPCSDYINASY----IPGNNFRREYIATQGPLPGTKDDFWKMVWEQNVHNIVMVTQCVE 76

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25151513 421 RGRVKCHQYWPRVFETQEYGRLMIKCIKDKQTTNCCYREFSIrdrnSSEE-----RRVTQMQYIAWPDHGVPDDPKHFIQ 495
Cdd:cd14617  77 KGRVKCDHYWPADQDSLYYGDLIVQMLSESVLPEWTIREFKI----CSEEqldapRLVRHFHYTVWPDHGVPETTQSLIQ 152

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 25151513 496 FVDEVRK--ARQGSVDPIVVHCSAGIGRTGVLILMETAACLVESNEPVYPLDIVRTMRDQRAMLIQTPGQYTFV 567
Cdd:cd14617 153 FVRTVRDyiNRTPGSGPTVVHCSAGVGRTGTFIALDRILQQLDSKDSVDIYGAVHDLRLHRVHMVQTECQYVYL 226
R-PTP-LAR-2 cd14554
PTP-like domain of the LAR family receptor-type tyrosine-protein phosphatases, repeat 2; The ...
 337-566 2.57e-59

PTP-like domain of the LAR family receptor-type tyrosine-protein phosphatases, repeat 2; The LAR (leukocyte common antigen-related) family of receptor-type tyrosine-protein phosphatases (RPTPs) include three vertebrate members: LAR (or PTPRF), R-PTP-delta (or PTPRD), and R-PTP-sigma (or PTPRS). They belong to the larger family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. LAR-RPTPs are synaptic adhesion molecules; they bind to distinct synaptic membrane proteins and are physiologically responsible for mediating presynaptic development by shaping various synaptic adhesion pathways. They play roles in various aspects of neuronal development, including axon guidance, neurite extension, and synapse formation and function. LAR-RPTPs contain an extracellular region with three immunoglobulin-like (Ig) domains and four to eight fibronectin type III (FN3) repeats (determined by alternative splicing), a single transmembrane domain, followed by an intracellular region with a membrane-proximal catalytic PTP domain (repeat 1, also called D1) and a membrane-distal non-catalytic PTP-like domain (repeat 2, also called D2). This model represents the non-catalytic PTP-like domain (repeat 2).


Pssm-ID: 350402 [Multi-domain]  Cd Length: 238  Bit Score: 197.75  E-value: 2.57e-59
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25151513 337 LTANLAKNRYRDVCPYDDTRVTLQASPS---GDYINANYVNmeipssGIVNR--YIACQGPLAHTSSDFWVMVWEQHCTT 411
Cdd:cd14554   3 LPCNKFKNRLVNILPYESTRVCLQPIRGvegSDYINASFID------GYRQRgaYIATQGPLAETTEDFWRMLWEHNSTI 76

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25151513 412 IVMLTTITERGRVKCHQYWPrVFETQEYGRLMIKCIKDKQTTNCCYREFSIRDRNSSEERRVTQMQYIAWPDHGVPDDPK 491
Cdd:cd14554  77 IVMLTKLREMGREKCHQYWP-AERSARYQYFVVDPMAEYNMPQYILREFKVTDARDGQSRTVRQFQFTDWPEQGVPKSGE 155

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 25151513 492 HFIQFVDEVRKAR--QGSVDPIVVHCSAGIGRTGVLILMETAACLVESNEPVYPLDIVRTMRDQRAMLIQTPGQYTF 566
Cdd:cd14554 156 GFIDFIGQVHKTKeqFGQEGPITVHCSAGVGRTGVFITLSIVLERMRYEGVVDVFQTVKLLRTQRPAMVQTEDQYQF 232
PTPc-KIM cd14547
catalytic domain of the kinase interaction motif (KIM) family of protein-tyrosine phosphatases; ...
 344-567 3.20e-59

catalytic domain of the kinase interaction motif (KIM) family of protein-tyrosine phosphatases; The kinase interaction motif (KIM) family of protein-tyrosine phosphatases (PTPs) includes tyrosine-protein phosphatases non-receptor type 7 (PTPN7) and non-receptor type 5 (PTPN5), and protein-tyrosine phosphatase receptor type R (PTPRR). PTPN7 is also called hematopoietic protein-tyrosine phosphatase (HePTP) while PTPN5 is also called striatal-enriched protein-tyrosine phosphatase (STEP). They belong to the family of classical tyrosine-specific PTPs (EC 3.1.3.48) that catalyze the dephosphorylation of phosphotyrosine peptides. KIM-PTPs are characterized by the presence of a 16-amino-acid KIM that binds specifically to members of the MAPK (mitogen-activated protein kinase) family. They are highly specific to the MAPKs ERK1/2 (extracellular-signal-regulated kinase 1/2) and p38, over JNK (c-Jun N-terminal kinase); they dephosphorylate these kinases and thereby critically modulate cell proliferation and differentiation.


Pssm-ID: 350395 [Multi-domain]  Cd Length: 224  Bit Score: 196.85  E-value: 3.20e-59
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25151513 344 NRYRDVCPYDDTRVTL---QASPSGDYINANYVNmeiPSSGIVNRYIACQGPLAHTSSDFWVMVWEQHCTTIVMLTTITE 420
Cdd:cd14547   1 NRYKTILPNEHSRVCLpsvDDDPLSSYINANYIR---GYDGEEKAYIATQGPLPNTVADFWRMVWQEKTPIIVMITNLTE 77

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25151513 421 RgRVKCHQYWPrVFETQEYGRLMIKCIKDKQTTNCCYREFSIrdRNSSEERRVTQMQYIAWPDHGVPDDPKHFIQFVDEV 500
Cdd:cd14547  78 A-KEKCAQYWP-EEENETYGDFEVTVQSVKETDGYTVRKLTL--KYGGEKRYLKHYWYTSWPDHKTPEAAQPLLSLVQEV 153

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 25151513 501 RKARQGSVD--PIVVHCSAGIGRTGVLILMETAACLVESNEPVYPLDIVRTMRDQRAMLIQTPGQYTFV 567
Cdd:cd14547 154 EEARQTEPHrgPIVVHCSAGIGRTGCFIATSIGCQQLREEGVVDVLGIVCQLRLDRGGMVQTAEQYEFV 222
R-PTPc-O cd14614
catalytic domain of receptor-type tyrosine-protein phosphatase O; Receptor-type ...
 337-567 8.55e-59

catalytic domain of receptor-type tyrosine-protein phosphatase O; Receptor-type tyrosine-protein phosphatase O (PTPRO or R-PTP-O), also known as glomerular epithelial protein 1 or protein tyrosine phosphatase U2 (PTP-U2), belongs to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. PTPRO is a member of the R3 subfamily of receptor-type phosphotyrosine phosphatases (RPTP), characterized by a unique modular composition consisting of multiple extracellular fibronectin type III (FN3) repeats and a single (most RPTP subtypes have two) cytoplasmic catalytic PTP domain. It is essential for sustaining the structure and function of foot processes by regulating tyrosine phosphorylation of podocyte proteins. It has been identified as a synaptic cell adhesion molecule (CAM) that serves as a potent initiator of synapse formation. It is also a tumor suppressor in several types of cancer, such as hepatocellular carcinoma, lung cancer, and breast cancer.


Pssm-ID: 350462 [Multi-domain]  Cd Length: 245  Bit Score: 196.65  E-value: 8.55e-59
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25151513 337 LTANLAKNRYRDVCPYDDTRV---TLQASPSGDYINANYvnmeIPSSGIVNRYIACQGPLAHTSSDFWVMVWEQHCTTIV 413
Cdd:cd14614   9 LPVNRCKNRYTNILPYDFSRVklvSMHEEEGSDYINANY----IPGYNSPQEYIATQGPLPETRNDFWKMVLQQKSQIIV 84

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25151513 414 MLTTITERGRVKCHQYWPRVFETQEYGRLMIKCIKDKQTTNCCYREFSIrdRNSSEERRVTQMQYIAWPDHGVP--DDPK 491
Cdd:cd14614  85 MLTQCNEKRRVKCDHYWPFTEEPVAYGDITVEMLSEEEQPDWAIREFRV--SYADEVQDVMHFNYTAWPDHGVPtaNAAE 162

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 25151513 492 HFIQFVDEVRKARQGSVDPIVVHCSAGIGRTGVLILMETAACLVESNEPVYPLDIVRTMRDQRAMLIQTPGQYTFV 567
Cdd:cd14614 163 SILQFVQMVRQQAVKSKGPMIIHCSAGVGRTGTFIALDRLLQHIRDHEFVDILGLVSEMRSYRMSMVQTEEQYIFI 238
R-PTPc-D-1 cd14624
catalytic domain of receptor-type tyrosine-protein phosphatase D, repeat 1; Receptor-type ...
 337-574 2.53e-58

catalytic domain of receptor-type tyrosine-protein phosphatase D, repeat 1; Receptor-type tyrosine-protein phosphatase D (PTPRD), also known as receptor-type tyrosine-protein phosphatase delta (R-PTP-delta), belongs to the LAR (leukocyte common antigen-related) family of receptor-type tyrosine-protein phosphatases (RPTPs), which belong to the larger family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. LAR-RPTPs are synaptic adhesion molecules that play roles in various aspects of neuronal development, including axon guidance, neurite extension, and synapse formation and function. PTPRD is involved in pre-synaptic differentiation through interaction with SLITRK2. It contains an extracellular region with three immunoglobulin-like (Ig) domains and four to eight fibronectin type III (FN3) repeats (determined by alternative splicing), a single transmembrane domain, followed by an intracellular region with a membrane-proximal catalytic PTP domain (repeat 1, also called D1) and a membrane-distal non-catalytic PTP-like domain (repeat 2, also called D2). This model represents the catalytic PTP domain (repeat 1).


Pssm-ID: 350472 [Multi-domain]  Cd Length: 284  Bit Score: 196.88  E-value: 2.53e-58
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25151513 337 LTANLAKNRYRDVCPYDDTRVTLQAS---PSGDYINANYVNMEIPSsgivNRYIACQGPLAHTSSDFWVMVWEQHCTTIV 413
Cdd:cd14624  44 LEVNKPKNRYANVIAYDHSRVLLSAIegiPGSDYINANYIDGYRKQ----NAYIATQGALPETFGDFWRMIWEQRSATVV 119

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25151513 414 MLTTITERGRVKCHQYWPRVfETQEYGRLMIKCIKDKQTTNCCYREFSIRDRNSSEERRVTQMQYIAWPDHGVPDDPKHF 493
Cdd:cd14624 120 MMTKLEERSRVKCDQYWPSR-GTETYGLIQVTLLDTVELATYCVRTFALYKNGSSEKREVRQFQFTAWPDHGVPEHPTPF 198

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25151513 494 IQFVDEVRKARQGSVDPIVVHCSAGIGRTGVLILMETAACLVESNEPVYPLDIVRTMRDQRAMLIQTPGQYTFVCESILR 573
Cdd:cd14624 199 LAFLRRVKTCNPPDAGPMVVHCSAGVGRTGCFIVIDAMLERIKHEKTVDIYGHVTLMRAQRNYMVQTEDQYIFIHDALLE 278


                .
gi 25151513 574 A 574
Cdd:cd14624 279 A 279
R-PTPc-J cd14615
catalytic domain of receptor-type tyrosine-protein phosphatase J; Receptor-type ...
 344-567 3.44e-58

catalytic domain of receptor-type tyrosine-protein phosphatase J; Receptor-type tyrosine-protein phosphatase J (PTPRJ or R-PTP-J), also known as receptor-type tyrosine-protein phosphatase eta (R-PTP-eta) or density-enhanced phosphatase 1 (DEP-1) OR CD148, belongs to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. PTPRJ is a member of the R3 subfamily of receptor-type phosphotyrosine phosphatases (RPTP), characterized by a unique modular composition consisting of multiple extracellular fibronectin type III (FN3) repeats (eight in PTPRJ) and a single (most RPTP subtypes have two) cytoplasmic catalytic PTP domain. It is expressed in various cell types including epithelial, hematopoietic, and endothelial cells. It plays a role in cell adhesion, migration, proliferation and differentiation. It dephosphorylates or contributes to the dephosphorylation of various substrates including protein kinases such as FLT3, PDGFRB, MET, RET (variant MEN2A), VEGFR-2, LYN, SRC, MAPK1, MAPK3, and EGFR, as well as PIK3R1 and PIK3R2.


Pssm-ID: 350463 [Multi-domain]  Cd Length: 229  Bit Score: 194.26  E-value: 3.44e-58
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25151513 344 NRYRDVCPYDDTRVTL--QASPSGDYINANYvnmeIPSSGIVNRYIACQGPLAHTSSDFWVMVWEQHCTTIVMLTTITER 421
Cdd:cd14615   1 NRYNNVLPYDISRVKLsvQSHSTDDYINANY----MPGYNSKKEFIAAQGPLPNTVKDFWRMVWEKNVYAIVMLTKCVEQ 76

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25151513 422 GRVKCHQYWPRVfETQEYGRLMIKCIKDKQTTNCCYREFSIRDRNSSEERRVTQMQYIAWPDHGVPDDPKHFIQFVDEVR 501
Cdd:cd14615  77 GRTKCEEYWPSK-QKKDYGDITVTMTSEIVLPEWTIRDFTVKNAQTNESRTVRHFHFTSWPDHGVPETTDLLINFRHLVR 155

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 25151513 502 K-ARQGSVD-PIVVHCSAGIGRTGVLILMETAACLVESNEPVYPLDIVRTMRDQRAMLIQTPGQYTFV 567
Cdd:cd14615 156 EyMKQNPPNsPILVHCSAGVGRTGTFIAIDRLIYQIENENVVDVYGIVYDLRMHRPLMVQTEDQYVFL 223
PTPc-N20 cd14596
catalytic domain of tyrosine-protein phosphatase non-receptor type 20; Tyrosine-protein ...
 367-574 3.56e-57

catalytic domain of tyrosine-protein phosphatase non-receptor type 20; Tyrosine-protein phosphatase non-receptor type 20 (PTPN20) belongs to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. Human PTPN20 is a widely expressed phosphatase with a dynamic subcellular distribution that is targeted to sites of actin polymerization.


Pssm-ID: 350444 [Multi-domain]  Cd Length: 207  Bit Score: 190.73  E-value: 3.56e-57
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25151513 367 YINANYVNMeiPSSGIVNRYIACQGPLAHTSSDFWVMVWEQHCTTIVMLTTITERGRVKCHQYWP-RVFETQEYGRLMIK 445
Cdd:cd14596   1 YINASYITM--PVGEEELFYIATQGPLPSTIDDFWQMVWENRSDVIAMMTREVERGKVKCHRYWPeTLQEPMELENYQLR 78

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25151513 446 CIKDKQTTNCCYREFSIRDRNSSEERRVTQMQYIAWPDHGVPDDPKHFIQFVDEVRKARQGSvdPIVVHCSAGIGRTGVL 525
Cdd:cd14596  79 LENYQALQYFIIRIIKLVEKETGENRLIKHLQFTTWPDHGTPQSSDQLVKFICYMRKVHNTG--PIVVHCSAGIGRAGVL 156

                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*....
gi 25151513 526 ILMETAACLVESNEPVYPLDIVRTMRDQRAMLIQTPGQYTFVCESILRA 574
Cdd:cd14596 157 ICVDVLLSLIEKDLSFNIKDIVREMRQQRYGMIQTKDQYLFCYKVVLEV 205
PTPc-N2 cd14607
catalytic domain of tyrosine-protein phosphatase non-receptor type 2; Tyrosine-protein ...
 326-566 6.36e-57

catalytic domain of tyrosine-protein phosphatase non-receptor type 2; Tyrosine-protein phosphatase non-receptor type 2 (PTPN2), also called T-cell protein-tyrosine phosphatase (TCPTP), belongs to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. PTPN2, a tumor suppressor, dephosphorylates and inactivates EGFRs, Src family kinases, Janus-activated kinases (JAKs)-1 and -3, and signal transducer and activators of transcription (STATs)-1, -3 and -5, in a cell type and context-dependent manner. It is deleted in 6% of all T-cell acute lymphoblastic leukemias and is associated with constitutive JAK1/STAT5 signaling and tumorigenesis.


Pssm-ID: 350455 [Multi-domain]  Cd Length: 257  Bit Score: 192.10  E-value: 6.36e-57
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25151513 326 KKPGMSMNICRLTANLAKNRYRDVCPYDDTRVTLQaSPSGDYINANYVNMEIPSsgivNRYIACQGPLAHTSSDFWVMVW 405
Cdd:cd14607  10 ESHDYPHRVAKYPENRNRNRYRDVSPYDHSRVKLQ-NTENDYINASLVVIEEAQ----RSYILTQGPLPNTCCHFWLMVW 84

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25151513 406 EQHCTTIVMLTTITERGRVKCHQYWP----RVFETQEYG---RLMIKCIKDKQTTnccyREFSIRDRNSSEERRVTQMQY 478
Cdd:cd14607  85 QQKTKAVVMLNRIVEKDSVKCAQYWPtdeeEVLSFKETGfsvKLLSEDVKSYYTV----HLLQLENINSGETRTISHFHY 160

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25151513 479 IAWPDHGVPDDPKHFIQFVDEVRKARQGSVD--PIVVHCSAGIGRTGVLILMETAACLVESNEP--VYPLDIVRTMRDQR 554
Cdd:cd14607 161 TTWPDFGVPESPASFLNFLFKVRESGSLSPEhgPAVVHCSAGIGRSGTFSLVDTCLVLMEKKDPdsVDIKQVLLDMRKYR 240

                       250
                ....*....|..
gi 25151513 555 AMLIQTPGQYTF 566
Cdd:cd14607 241 MGLIQTPDQLRF 252
PTPc-N11 cd14605
catalytic domain of tyrosine-protein phosphatase non-receptor type 11; Tyrosine-protein ...
 340-567 1.61e-56

catalytic domain of tyrosine-protein phosphatase non-receptor type 11; Tyrosine-protein phosphatase non-receptor type 11 (PTPN11), also called SH2 domain-containing tyrosine phosphatase 2 (SHP-2 or SHP2), belongs to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. PTPN11 promotes the activation of the RAS/Mitogen-Activated Protein Kinases (MAPK) Extracellular-Regulated Kinases 1/2 (ERK1/2) pathway, a canonical signaling cascade that plays key roles in various cellular processes, including proliferation, survival, differentiation, migration, or metabolism. It also regulates the phosphoinositide 3-kinase (PI3K)/AKT pathway, a fundamental cascade that functions in cell survival, proliferation, migration, morphogenesis, and metabolism. PTPN11 dysregulation is associated with several developmental diseases and malignancies, such as Noonan syndrome and juvenile myelomonocytic leukemia. It contains two tandem SH2 domains, a catalytic PTP domain, and a C-terminal tail with regulatory properties.


Pssm-ID: 350453 [Multi-domain]  Cd Length: 253  Bit Score: 191.00  E-value: 1.61e-56
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25151513 340 NLAKNRYRDVCPYDDTRVTLQ----ASPSGDYINANYV----NMEIPSSGIVNRYIACQGPLAHTSSDFWVMVWEQHCTT 411
Cdd:cd14605   2 NKNKNRYKNILPFDHTRVVLHdgdpNEPVSDYINANIImpefETKCNNSKPKKSYIATQGCLQNTVNDFWRMVFQENSRV 81

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25151513 412 IVMLTTITERGRVKCHQYWPRVFETQEYGRLMIKCIKDKQTTNCCYREFSI-RDRNSSEERRVTQMQYIAWPDHGVPDDP 490
Cdd:cd14605  82 IVMTTKEVERGKSKCVKYWPDEYALKEYGVMRVRNVKESAAHDYILRELKLsKVGQGNTERTVWQYHFRTWPDHGVPSDP 161

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25151513 491 KHFIQFVDEVRKARQGSVD--PIVVHCSAGIGRTGVLILMETAACLVESNEPVYPLDIVRTM---RDQRAMLIQTPGQYT 565
Cdd:cd14605 162 GGVLDFLEEVHHKQESIMDagPVVVHCSAGIGRTGTFIVIDILIDIIREKGVDCDIDVPKTIqmvRSQRSGMVQTEAQYR 241


                ..
gi 25151513 566 FV 567
Cdd:cd14605 242 FI 243
R-PTPc-G-1 cd17667
catalytic domain of receptor-type tyrosine-protein phosphatase G, repeat 1; Receptor-type ...
 340-576 2.97e-56

catalytic domain of receptor-type tyrosine-protein phosphatase G, repeat 1; Receptor-type tyrosine-protein phosphatase G (PTPRG), also called protein-tyrosine phosphatase gamma (R-PTP-gamma), belongs to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. PTPRG is an important tumor suppressor gene in multiple human cancers such as lung, ovarian, and breast cancers. It is widely expressed in many tissues, including the central nervous system, where it plays a role during neuroinflammation processes. It can dephosphorylate platelet-derived growth factor receptor beta (PDGFRB) and may play a role in PDGFRB-related infantile myofibromatosis. PTPRG has four splicing isoforms: three transmembrane isoforms, PTPRG-A, B, and C, and one secretory isoform, PTPRG-S, which are expressed in many tissues including the brain. PTPRG is a type 1 integral membrane protein consisting of an extracellular region with a carbonic anhydrase-like (CAH) and a fibronectin type III (FN3) domains, and an intracellular region with a catalytic PTP domain (repeat 1) proximal to the membrane, and a catalytically inactive PTP-fold domain (repeat 2) distal to the membrane. This model represents the catalytic PTP domain (repeat 1).


Pssm-ID: 350505 [Multi-domain]  Cd Length: 274  Bit Score: 191.02  E-value: 2.97e-56
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25151513 340 NLAKNRYRDVCPYDDTRVTLQASPS-----GDYINANYVNmeipSSGIVNRYIACQGPLAHTSSDFWVMVWEQHCTTIVM 414
Cdd:cd17667  27 NKHKNRYINILAYDHSRVKLRPLPGkdskhSDYINANYVD----GYNKAKAYIATQGPLKSTFEDFWRMIWEQNTGIIVM 102

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25151513 415 LTTITERGRVKCHQYWPRVfETQEYGRLMIKCIKDKQTTNCCYREFSIRD-----------RNSSEERRVTQMQYIAWPD 483
Cdd:cd17667 103 ITNLVEKGRRKCDQYWPTE-NSEEYGNIIVTLKSTKIHACYTVRRFSIRNtkvkkgqkgnpKGRQNERTVIQYHYTQWPD 181

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25151513 484 HGVPDDPKHFIQFVDEVRKARQGSVDPIVVHCSAGIGRTGVLILMETAACLVESNEPVYPLDIVRTMRDQRAMLIQTPGQ 563
Cdd:cd17667 182 MGVPEYALPVLTFVRRSSAARTPEMGPVLVHCSAGVGRTGTYIVIDSMLQQIKDKSTVNVLGFLKHIRTQRNYLVQTEEQ 261

                       250
                ....*....|...
gi 25151513 564 YTFVCESILRAYH 576
Cdd:cd17667 262 YIFIHDALLEAIL 274
R-PTPc-T-1 cd14630
catalytic domain of receptor-type tyrosine-protein phosphatase T, repeat 1; Receptor-type ...
 340-574 1.67e-54

catalytic domain of receptor-type tyrosine-protein phosphatase T, repeat 1; Receptor-type tyrosine-protein phosphatase T (PTPRT), also known as receptor-type tyrosine-protein phosphatase rho (RPTP-rho or PTPrho), belongs to the type IIb subfamily of receptor protein tyrosine phosphatases (RPTPs), which belong to the larger family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. PTPRT is highly expressed in the nervous system and it plays a critical role in regulation of synaptic formation and neuronal development. It dephosphorylates a specific tyrosine residue in syntaxin-binding protein 1, a key component of synaptic vesicle fusion machinery, and regulates its binding to syntaxin 1. PTPRT has been identified as a potential candidate gene for autism spectrum disorder (ASD) susceptibility. It contains an extracellular region with an Meprin-A5 (neuropilin)-mu (MAM) domain, an immunoglobulin (Ig) domain, and four fibronectin type III (FN3) repeats, a transmembrane domain, and an intracellular segment with a juxtamembrane domain similar to the cytoplasmic domain of classical cadherins and two tandem PTP domains. This model represents the first (repeat 1) PTP domain.


Pssm-ID: 350478 [Multi-domain]  Cd Length: 237  Bit Score: 184.84  E-value: 1.67e-54
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25151513 340 NLAKNRYRDVCPYDDTRVTLQ---ASPSGDYINANYVN-MEIPssgivNRYIACQGPLAHTSSDFWVMVWEQHCTTIVML 415
Cdd:cd14630   3 NRNKNRYGNIISYDHSRVRLQlldGDPHSDYINANYIDgYHRP-----RHYIATQGPMQETVKDFWRMIWQENSASVVMV 77

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25151513 416 TTITERGRVKCHQYWPRvfETQEYGRLMIKCIKDKQTTNCCYREFSIRDRNSSEERRVTQMQYIAWPDHGVPDDPKHFIQ 495
Cdd:cd14630  78 TNLVEVGRVKCVRYWPD--DTEVYGDIKVTLIETEPLAEYVIRTFTVQKKGYHEIREIRQFHFTSWPDHGVPCYATGLLG 155

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 25151513 496 FVDEVRKARQGSVDPIVVHCSAGIGRTGVLILMETAACLVESNEPVYPLDIVRTMRDQRAMLIQTPGQYTFVCESILRA 574
Cdd:cd14630 156 FVRQVKFLNPPDAGPIVVHCSAGAGRTGCFIAIDIMLDMAENEGVVDIFNCVRELRAQRVNMVQTEEQYVFVHDAILEA 234
PDZ_PTPN3-4-like cd06706
PDZ domain of tyrosine-protein phosphatase non-receptor type 3 (PTPN3), tyrosine-protein ...
 176-266 1.48e-53

PDZ domain of tyrosine-protein phosphatase non-receptor type 3 (PTPN3), tyrosine-protein phosphatase non-receptor type 4 (PTNP4), and related domains; PDZ (PSD-95 (Postsynaptic density protein 95), Dlg (Discs large protein), and ZO-1 (Zonula occludens-1)) domain of PTPN3, PTPN4 and related domains. PTPN3 (also known as protein-tyrosine phosphatase H1, PTP-H1) has a tumor-suppressive or a tumor-promoting role in many cancers. It serves as a specific phosphatase for the MAP kinase p38gamma; the two interact via their PDZ domains and cooperate to promote Ras-induced oncogenesis. Interaction partners of the PTPN3 PDZ domain include p38gamma and human papillomavirus E6 oncoprotein. PTPN4 (also known as protein-tyrosine phosphatase MEG1) plays a role in immunity, learning, synaptic plasticity or cell homeostasis. p38gamma is also an interaction partner of the PTPN4 PDZ domain: PTPN4 regulates neuronal cell homeostasis by protecting neurons against apoptosis; binding of the C terminus of p38gamma to the PDZ domain of PTPN4, antagonizes the catalytic autoinhibition of PTPN4, leading to cell apoptosis. Other interaction partners of the PTPN4 PDZ domain include glutamate receptor subunit GluN2A, and RABV strain G protein, among others. 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 PTPN3-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: 467190 [Multi-domain]  Cd Length: 90  Bit Score: 177.12  E-value: 1.48e-53
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25151513 176 DQVVTIKMRPDRHGRFGFNVKGGADQNYPVIVSRVAPGSSADKCQPRLNEGDQVLFIDGRDVSTMSHDHVVQFIRSARSg 255
Cdd:cd06706   1 DGLVLIRMKPDENGRFGFNVKGGVDQKMPVIVSRVAPGTPADLCIPRLNEGDQVLLINGRDISEHTHDQVVMFIKASRE- 79

                        90
                ....*....|.
gi 25151513 256 LNGGELHLTIR 266
Cdd:cd06706  80 RHSGELVLLVR 90
PTPc-N1 cd14608
catalytic domain of tyrosine-protein phosphatase non-receptor type 1; Tyrosine-protein ...
 334-566 4.62e-53

catalytic domain of tyrosine-protein phosphatase non-receptor type 1; Tyrosine-protein phosphatase non-receptor type 1 (PTPN1), also called protein-tyrosine phosphatase 1B (PTP-1B), belongs to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. PTPN1/PTP-1B is the first PTP to be purified and characterized and is the prototypical intracellular PTP found in a wide variety of human tissues. It contains an N-terminal catalytic PTP domain, followed by two tandem proline-rich motifs that mediate interaction with SH3-domain-containing proteins, and a small hydrophobic stretch that localizes the enzyme to the endoplasmic reticulum (ER). It dephosphorylates and regulates the activity of a number of receptor tyrosine kinases, including the insulin receptor, the EGF receptor, and the PDGF receptor.


Pssm-ID: 350456 [Multi-domain]  Cd Length: 277  Bit Score: 182.53  E-value: 4.62e-53
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25151513 334 ICRLTANLAKNRYRDVCPYDDTRVTLQASpSGDYINANYVNMEIPSsgivNRYIACQGPLAHTSSDFWVMVWEQHCTTIV 413
Cdd:cd14608  19 VAKLPKNKNRNRYRDVSPFDHSRIKLHQE-DNDYINASLIKMEEAQ----RSYILTQGPLPNTCGHFWEMVWEQKSRGVV 93

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25151513 414 MLTTITERGRVKCHQYWPRVFETQ---EYGRLMIKCIKDKQTTNCCYREFSIRDRNSSEERRVTQMQYIAWPDHGVPDDP 490
Cdd:cd14608  94 MLNRVMEKGSLKCAQYWPQKEEKEmifEDTNLKLTLISEDIKSYYTVRQLELENLTTQETREILHFHYTTWPDFGVPESP 173

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25151513 491 KHFIQFVDEVRKArqGSVD----PIVVHCSAGIGRTGVLILMETAACLVESNEPVYPLDIVRT---MRDQRAMLIQTPGQ 563
Cdd:cd14608 174 ASFLNFLFKVRES--GSLSpehgPVVVHCSAGIGRSGTFCLADTCLLLMDKRKDPSSVDIKKVlleMRKFRMGLIQTADQ 251


                ...
gi 25151513 564 YTF 566
Cdd:cd14608 252 LRF 254
R-PTPc-typeIIb-1 cd14555
catalytic domain of type IIb (or R2B) subfamily receptor-type tyrosine-protein phosphatases, ...
 367-574 4.90e-53

catalytic domain of type IIb (or R2B) subfamily receptor-type tyrosine-protein phosphatases, repeat 1; The type II (or R2B) subfamily of receptor protein tyrosine phosphatases (RPTPs) include the prototypical member PTPmu (or PTPRM), PCP-2 (or PTPRU), PTPrho (or PTPRT), and PTPkappa (or PTPRK). They belong to the larger family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. Type IIb RPTPs mediate cell-cell adhesion though homophilic interactions; their ligand is an identical molecule on an adjacent cell. No heterophilic interactions between the subfamily members have been observed. They also commonly function as tumor suppressors. They contain an extracellular region with an Meprin-A5 (neuropilin)-mu (MAM) domain, an immunoglobulin (Ig) domain, and four fibronectin type III (FN3) repeats, a transmembrane domain, and an intracellular segment with a juxtamembrane domain similar to the cytoplasmic domain of classical cadherins and two tandem PTP domains. This model represents the first (repeat 1) PTP domain.


Pssm-ID: 350403 [Multi-domain]  Cd Length: 204  Bit Score: 179.73  E-value: 4.90e-53
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25151513 367 YINANYVNMEIPSsgivNRYIACQGPLAHTSSDFWVMVWEQHCTTIVMLTTITERGRVKCHQYWPRvfETQEYGRLMIKC 446
Cdd:cd14555   1 YINANYIDGYHRP----NHYIATQGPMQETVYDFWRMVWQENSASIVMVTNLVEVGRVKCSRYWPD--DTEVYGDIKVTL 74

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25151513 447 IKDKQTTNCCYREFSIRDRNSSEERRVTQMQYIAWPDHGVPDDPKHFIQFVDEVRKARQGSVDPIVVHCSAGIGRTGVLI 526
Cdd:cd14555  75 VETEPLAEYVVRTFALERRGYHEIREVRQFHFTGWPDHGVPYHATGLLGFIRRVKASNPPSAGPIVVHCSAGAGRTGCYI 154

                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*...
gi 25151513 527 LMETAACLVESNEPVYPLDIVRTMRDQRAMLIQTPGQYTFVCESILRA 574
Cdd:cd14555 155 VIDIMLDMAEREGVVDIYNCVKELRSRRVNMVQTEEQYIFIHDAILEA 202
PTPc-N21 cd14598
catalytic domain of tyrosine-protein phosphatase non-receptor type 21; Tyrosine-protein ...
 367-567 7.66e-52

catalytic domain of tyrosine-protein phosphatase non-receptor type 21; Tyrosine-protein phosphatase non-receptor type 21 (PTPN21), also called protein-tyrosine phosphatase D1, belongs to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. PTPN21 is a component of a multivalent scaffold complex nucleated by focal adhesion kinase (FAK) at specific intracellular sites. It promotes cytoskeleton events that induce cell adhesion and migration by modulating Src-FAK signaling. It can also selectively associate with and stimulate Tec family kinases and modulate Stat3 activation. Human PTPN21 may also play a pathologic role in gastrointestinal tract tumorigenesis. PTPN21 contains an N-terminal FERM domain and a C-terminal catalytic PTP domain, separated by a long intervening sequence.


Pssm-ID: 350446 [Multi-domain]  Cd Length: 220  Bit Score: 177.09  E-value: 7.66e-52
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25151513 367 YINANYVNMEIpsSGIVNRYIACQGPLAHTSSDFWVMVWEQHCTTIVMLTTITERGRVKCHQYWPRV---FETQEYGRLm 443
Cdd:cd14598   1 YINASHIKVTV--GGKEWDYIATQGPLQNTCQDFWQMVWEQGVAIIAMVTAEEEGGREKSFRYWPRLgsrHNTVTYGRF- 77

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25151513 444 iKCIKDKQTTNCCYREFSIRDRN--SSEERRVTQMQYIAWPDHGVPDDPKHFIQFVDEVRKAR---------QGSVDPIV 512
Cdd:cd14598  78 -KITTRFRTDSGCYATTGLKIKHllTGQERTVWHLQYTDWPEHGCPEDLKGFLSYLEEIQSVRrhtnstidpKSPNPPVL 156

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*...
gi 25151513 513 VHCSAGIGRTGVLILMETAACLVESNEpvyPLDIVRT---MRDQRAMLIQTPGQYTFV 567
Cdd:cd14598 157 VHCSAGVGRTGVVILSEIMIACLEHNE---MLDIPRVldmLRQQRMMMVQTLSQYTFV 211
PTPc-N7 cd14612
catalytic domain of tyrosine-protein phosphatase non-receptor type 7; Tyrosine-protein ...
 342-567 2.55e-51

catalytic domain of tyrosine-protein phosphatase non-receptor type 7; Tyrosine-protein phosphatase non-receptor type 7 (PTPN7), also called hematopoietic protein-tyrosine phosphatase (HePTP) or LC-PTP. belongs to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. PTPN7/HePTP is a kinase interaction motif (KIM)-PTP, characterized by the presence of a 16-amino-acid KIM that binds specifically to members of the MAPK (mitogen-activated protein kinase) family. PTPN7/HePTP is found exclusively in the white blood cells in bone marrow, thymus, spleen, lymph nodes and all myeloid and lymphoid cell lines. It negatively regulates T-cell activation and proliferation, and is often dysregulated in the preleukemic disorder myelodysplastic syndrome, as well as in acute myelogenous leukemia.


Pssm-ID: 350460 [Multi-domain]  Cd Length: 247  Bit Score: 176.95  E-value: 2.55e-51
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25151513 342 AKNRYRDVCPYDDTRVTLQASPS----GDYINANYVNmeiPSSGIVNRYIACQGPLAHTSSDFWVMVWEQHCTTIVMLTT 417
Cdd:cd14612  17 SKDRYKTILPNPQSRVCLRRAGSqeeeGSYINANYIR---GYDGKEKAYIATQGPMLNTVSDFWEMVWQEECPIIVMITK 93

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25151513 418 ITERgRVKCHQYWPRVFETqeYGRLMIKCIKDKQttnccYREFSIRD---RNSSEERRVTQMQYIAWPDHGVPDDPKHFI 494
Cdd:cd14612  94 LKEK-KEKCVHYWPEKEGT--YGRFEIRVQDMKE-----CDGYTIRDltiQLEEESRSVKHYWFSSWPDHQTPESAGPLL 165

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 25151513 495 QFVDEVRKARQ--GSVDPIVVHCSAGIGRTGVLILMETAACLVESNEPVYPLDIVRTMRDQRAMLIQTPGQYTFV 567
Cdd:cd14612 166 RLVAEVEESRQtaASPGPIVVHCSAGIGRTGCFIATSIGCQQLKDTGKVDILGIVCQLRLDRGGMIQTSEQYQFL 240
R-PTPc-E-1 cd14620
catalytic domain of receptor-type tyrosine-protein phosphatase E, repeat 1; Receptor-type ...
 346-572 3.29e-51

catalytic domain of receptor-type tyrosine-protein phosphatase E, repeat 1; Receptor-type tyrosine-protein phosphatase E (PTPRE), also known as receptor-type tyrosine-protein phosphatase epsilon (R-PTP-epsilon), belongs to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. The PTPRE gene contains two distinct promoters that generate the two major isoforms: transmembrane (receptor type RPTPe or PTPeM) and cytoplasmic (cyt-PTPe or PTPeC). Receptor type RPTPe plays a critical role in signaling transduction pathways and phosphoprotein network topology in red blood cells, and may also play a role in osteoclast formation and function. It also negatively regulates PDGFRbeta-mediated signaling pathways that are crucial for the pathogenesis of atherosclerosis. cyt-PTPe acts as a negative regulator of insulin receptor signaling in skeletal muscle. It regulates insulin-induced phosphorylation of proteins downstream of the insulin receptor. Receptor type RPTPe contains a small extracellular region, a single transmembrane segment, and an intracellular region two tandem catalytic PTP domains. This model represents the first PTP domain (repeat 1).


Pssm-ID: 350468 [Multi-domain]  Cd Length: 229  Bit Score: 175.90  E-value: 3.29e-51
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25151513 346 YRDVCPYDDTRVTL---QASPSGDYINANYVNMEIPSsgivNRYIACQGPLAHTSSDFWVMVWEQHCTTIVMLTTITERG 422
Cdd:cd14620   1 YPNILPYDHSRVILsqlDGIPCSDYINASYIDGYKEK----NKFIAAQGPKQETVNDFWRMVWEQKSATIVMLTNLKERK 76

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25151513 423 RVKCHQYWPRVfETQEYGRLMIkCIKDKQT-TNCCYREFSIR---DRNSSEERRVTQMQYIAWPDHGVPDDPKHFIQFVD 498
Cdd:cd14620  77 EEKCYQYWPDQ-GCWTYGNIRV-AVEDCVVlVDYTIRKFCIQpqlPDGCKAPRLVTQLHFTSWPDFGVPFTPIGMLKFLK 154

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 25151513 499 EVRKARQGSVDPIVVHCSAGIGRTGVLILMETAACLVESNEPVYPLDIVRTMRDQRAMLIQTPGQYTFVCESIL 572
Cdd:cd14620 155 KVKSVNPVHAGPIVVHCSAGVGRTGTFIVIDAMIDMMHAEQKVDVFEFVSRIRNQRPQMVQTDMQYSFIYQALL 228
R-PTP-N cd14609
PTP-like domain of receptor-type tyrosine-protein phosphatase N; Receptor-type ...
 288-571 4.76e-51

PTP-like domain of receptor-type tyrosine-protein phosphatase N; Receptor-type tyrosine-protein phosphatase-like N (PTPRN or R-PTP-N), also called islet cell antigen 512 (ICA512) or PTP IA-2, belongs to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). It consists of a large ectodomain that contains a RESP18HD (regulated endocrine-specific protein 18 homology domain), followed by a transmembrane segment, and a single, catalytically-impaired, PTP domain. PTPRN is located in secretory granules of neuroendocrine cells and is involved in the generation, cargo storage, traffic, exocytosis and recycling of insulin secretory granules, as well as in beta-cell proliferation. It is a major autoantigen in type 1 diabetes and is involved in the regulation of insulin secretion.


Pssm-ID: 350457 [Multi-domain]  Cd Length: 281  Bit Score: 177.15  E-value: 4.76e-51
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25151513 288 ARVADSVPNSDKLSKSLQLLADslnsgkvvdhfemlYRKKPGmSMNICRLTANLAKNRYRDVCPYDDTRVTLQA--SPS- 364
Cdd:cd14609   5 AYMEDHLRNRDRLAKEWQALCA--------------YQAEPN-TCSTAQGEANVKKNRNPDFVPYDHARIKLKAesNPSr 69

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25151513 365 GDYINANYVNMEIPSsgiVNRYIACQGPLAHTSSDFWVMVWEQHCTTIVMLTTITERGRVKCHQYWP-------RVFETQ 437
Cdd:cd14609  70 SDYINASPIIEHDPR---MPAYIATQGPLSHTIADFWQMVWENGCTVIVMLTPLVEDGVKQCDRYWPdegsslyHIYEVN 146

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25151513 438 EYGRlMIKCikdkqtTNCCYREFSIRDRNSSEERRVTQMQYIAWPDHGVPDDPKHFIQFVDEVRKARQGSVDPIVVHCSA 517
Cdd:cd14609 147 LVSE-HIWC------EDFLVRSFYLKNVQTQETRTLTQFHFLSWPAEGIPSSTRPLLDFRRKVNKCYRGRSCPIIVHCSD 219

                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|....*..
gi 25151513 518 GIGRTGVLILMETAacLVESNEPVYPLDIVRTM---RDQRAMLIQTPGQYTFVCESI 571
Cdd:cd14609 220 GAGRTGTYILIDMV--LNRMAKGVKEIDIAATLehvRDQRPGMVRTKDQFEFALTAV 274
R-PTP-D-2 cd14628
PTP-like domain of receptor-type tyrosine-protein phosphatase D, repeat 2; Receptor-type ...
 311-566 4.98e-51

PTP-like domain of receptor-type tyrosine-protein phosphatase D, repeat 2; Receptor-type tyrosine-protein phosphatase-like D (PTPRD), also known as receptor-type tyrosine-protein phosphatase delta (R-PTP-delta), belongs to the LAR (leukocyte common antigen-related) family of receptor-type tyrosine-protein phosphatases (RPTPs), which belong to the larger family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. LAR-RPTPs are synaptic adhesion molecules that play roles in various aspects of neuronal development, including axon guidance, neurite extension, and synapse formation and function. PTPRD is involved in pre-synaptic differentiation through interaction with SLITRK2. It contains an extracellular region with three immunoglobulin-like (Ig) domains and four to eight fibronectin type III (FN3) repeats (determined by alternative splicing), a single transmembrane domain, followed by an intracellular region with a membrane-proximal catalytic PTP domain (repeat 1, also called D1) and a membrane-distal non-catalytic PTP-like domain (repeat 2, also called D2). This model represents the non-catalytic PTP-like domain (repeat 2). Although described as non-catalytic, this domain contains the catalytic cysteine and the active site signature motif, HCSAGxGRxG.


Pssm-ID: 350476 [Multi-domain]  Cd Length: 292  Bit Score: 177.62  E-value: 4.98e-51
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25151513 311 LNSGKVVDHFEMLYRKKPGMSMNICR-LTANLA----KNRYRDVCPYDDTRVTLQ---ASPSGDYINANYVNMEIPSSGi 382
Cdd:cd14628  18 IETGENVTGMELEFKRLASSKAHTSRfISANLPcnkfKNRLVNIMPYESTRVCLQpirGVEGSDYINASFIDGYRQQKA- 96

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25151513 383 vnrYIACQGPLAHTSSDFWVMVWEQHCTTIVMLTTITERGRVKCHQYWPrVFETQEYGRLMIKCIKDKQTTNCCYREFSI 462
Cdd:cd14628  97 ---YIATQGPLAETTEDFWRMLWEHNSTIVVMLTKLREMGREKCHQYWP-AERSARYQYFVVDPMAEYNMPQYILREFKV 172

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25151513 463 RDRNSSEERRVTQMQYIAWPDHGVPDDPKHFIQFVDEVRKARQ--GSVDPIVVHCSAGIGRTGVLILMETAACLVESNEP 540
Cdd:cd14628 173 TDARDGQSRTVRQFQFTDWPEQGVPKSGEGFIDFIGQVHKTKEqfGQDGPISVHCSAGVGRTGVFITLSIVLERMRYEGV 252

                       250       260
                ....*....|....*....|....*.
gi 25151513 541 VYPLDIVRTMRDQRAMLIQTPGQYTF 566
Cdd:cd14628 253 VDIFQTVKMLRTQRPAMVQTEDQYQF 278
PTPc-N22_18_12 cd14542
catalytic domain of tyrosine-protein phosphatase non-receptor type 22, type 18 and type 12; ...
 367-567 1.84e-50

catalytic domain of tyrosine-protein phosphatase non-receptor type 22, type 18 and type 12; Tyrosine-protein phosphatase non-receptor type 22 (PTPN22), type 18 (PTPN18) and type 12 (PTPN12) belong to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. PTPN22 is expressed in hematopoietic cells and it functions as a key regulator of immune homeostasis by inhibiting T-cell receptor signaling through the direct dephosphorylation of Src family kinases (Lck and Fyn), ITAMs of the TCRz/CD3 complex, and other signaling molecules. TPN18 regulates HER2-mediated cellular functions through defining both its phosphorylation and ubiquitination states. PTPN12 is characterized as a tumor suppressor and a pivotal regulator of EGFR/HER2 signaling.


Pssm-ID: 350390 [Multi-domain]  Cd Length: 202  Bit Score: 172.99  E-value: 1.84e-50
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25151513 367 YINANYVNmeipssGIVNR--YIACQGPLAHTSSDFWVMVWEQHCTTIVMLTTITERGRVKCHQYWPRVFE-TQEYGRLM 443
Cdd:cd14542   1 YINANFIK------GVSGSkaYIATQGPLPNTVLDFWRMIWEYNVQVIVMACREFEMGKKKCERYWPEEGEeQLQFGPFK 74

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25151513 444 IKCIKDKQTTNccyrEFSIRD---RNSSEERRVTQMQYIAWPDHGVPDDPKHFIQFVDEVRKArQGSVD-PIVVHCSAGI 519
Cdd:cd14542  75 ISLEKEKRVGP----DFLIRTlkvTFQKESRTVYQFHYTAWPDHGVPSSVDPILDLVRLVRDY-QGSEDvPICVHCSAGC 149

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|.
gi 25151513 520 GRTGVLILMETAACLVES---NEPVYPLDIVRTMRDQRAMLIQTPGQYTFV 567
Cdd:cd14542 150 GRTGTICAIDYVWNLLKTgkiPEEFSLFDLVREMRKQRPAMVQTKEQYELV 200
R-PTP-S-2 cd14627
PTP-like domain of receptor-type tyrosine-protein phosphatase S, repeat 2; Receptor-type ...
 304-572 1.86e-50

PTP-like domain of receptor-type tyrosine-protein phosphatase S, repeat 2; Receptor-type tyrosine-protein phosphatase S (PTPRS), also known as receptor-type tyrosine-protein phosphatase sigma (R-PTP-sigma), belongs to the LAR (leukocyte common antigen-related) family of receptor-type tyrosine-protein phosphatases (RPTPs), which belong to the larger family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. PTPRS is a receptor for glycosaminoglycans, including heparan sulfate proteoglycan and neural chondroitin sulfate proteoglycans (CSPGs), which present a barrier to axon regeneration. It also plays a role in stimulating neurite outgrowth in response to the heparan sulfate proteoglycan GPC2. PTPRS contains an extracellular region with three immunoglobulin-like (Ig) domains and four to eight fibronectin type III (FN3) repeats (determined by alternative splicing), a single transmembrane domain, followed by an intracellular region with a membrane-proximal catalytic PTP domain (repeat 1, also called D1) and a membrane-distal non-catalytic PTP-like domain (repeat 2, also called D2). This model represents the non-catalytic PTP-like domain (repeat 2). Although described as non-catalytic, this domain contains the catalytic cysteine and the active site signature motif, HCSAGxGRxG.


Pssm-ID: 350475 [Multi-domain]  Cd Length: 290  Bit Score: 176.08  E-value: 1.86e-50
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25151513 304 LQLLAdSLNSGKVVDHFEMLYRKKPGMSMNICR-LTANLA----KNRYRDVCPYDDTRVTLQ---ASPSGDYINANYVNM 375
Cdd:cd14627  13 IQKLA-QVEVGEHVTGMELEFKRLANSKAHTSRfISANLPcnkfKNRLVNIMPYETTRVCLQpirGVEGSDYINASFIDG 91

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25151513 376 EIPSSGivnrYIACQGPLAHTSSDFWVMVWEQHCTTIVMLTTITERGRVKCHQYWPrVFETQEYGRLMIKCIKDKQTTNC 455
Cdd:cd14627  92 YRQQKA----YIATQGPLAETTEDFWRMLWENNSTIVVMLTKLREMGREKCHQYWP-AERSARYQYFVVDPMAEYNMPQY 166

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25151513 456 CYREFSIRDRNSSEERRVTQMQYIAWPDHGVPDDPKHFIQFVDEVRKARQ--GSVDPIVVHCSAGIGRTGVLILMETAAC 533
Cdd:cd14627 167 ILREFKVTDARDGQSRTVRQFQFTDWPEQGVPKSGEGFIDFIGQVHKTKEqfGQDGPISVHCSAGVGRTGVFITLSIVLE 246

                       250       260       270
                ....*....|....*....|....*....|....*....
gi 25151513 534 LVESNEPVYPLDIVRTMRDQRAMLIQTPGQYTFVCESIL 572
Cdd:cd14627 247 RMRYEGVVDIFQTVKMLRTQRPAMVQTEDEYQFCYQAAL 285
R-PTPc-M-1 cd14633
catalytic domain of receptor-type tyrosine-protein phosphatase M, repeat 1; Receptor-type ...
 340-574 3.60e-50

catalytic domain of receptor-type tyrosine-protein phosphatase M, repeat 1; Receptor-type tyrosine-protein phosphatase M (PTPRM), also known as protein-tyrosine phosphatase mu (R-PTP-mu or PTPmu), belongs to the type IIb subfamily of receptor protein tyrosine phosphatases (RPTPs), which belong to the larger family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. PTPRM/PTPmu is a homophilic cell adhesion molecule expressed in CNS neurons and glia. It is required for E-, N-, and R-cadherin-dependent neurite outgrowth. Loss of PTPmu contributes to tumor cell migration and dispersal of human glioblastomas. PTPRM contains an extracellular region with an Meprin-A5 (neuropilin)-mu (MAM) domain, an immunoglobulin (Ig) domain, and four fibronectin type III (FN3) repeats, a transmembrane domain, and an intracellular segment with a juxtamembrane domain similar to the cytoplasmic domain of classical cadherins and two tandem PTP domains. This model represents the first (repeat 1) PTP domain.


Pssm-ID: 350481 [Multi-domain]  Cd Length: 273  Bit Score: 174.46  E-value: 3.60e-50
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25151513 340 NLAKNRYRDVCPYDDTRVTLQ---ASPSGDYINANYVN-MEIPssgivNRYIACQGPLAHTSSDFWVMVWEQHCTTIVML 415
Cdd:cd14633  40 NRMKNRYGNIIAYDHSRVRLQpieGETSSDYINGNYIDgYHRP-----NHYIATQGPMQETIYDFWRMVWHENTASIIMV 114

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25151513 416 TTITERGRVKCHQYWPRvfETQEYGRLMIKCIKDKQTTNCCYREFSIRDRNSSEERRVTQMQYIAWPDHGVPDDPKHFIQ 495
Cdd:cd14633 115 TNLVEVGRVKCCKYWPD--DTEIYKDIKVTLIETELLAEYVIRTFAVEKRGVHEIREIRQFHFTGWPDHGVPYHATGLLG 192

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 25151513 496 FVDEVRKARQGSVDPIVVHCSAGIGRTGVLILMETAACLVESNEPVYPLDIVRTMRDQRAMLIQTPGQYTFVCESILRA 574
Cdd:cd14633 193 FVRQVKSKSPPNAGPLVVHCSAGAGRTGCFIVIDIMLDMAEREGVVDIYNCVRELRSRRVNMVQTEEQYVFIHDAILEA 271
PTP-N23 cd14539
PTP-like domain of tyrosine-protein phosphatase non-receptor type 23; Tyrosine-protein ...
 367-566 5.23e-50

PTP-like domain of tyrosine-protein phosphatase non-receptor type 23; Tyrosine-protein phosphatase non-receptor type 23 (PTPN23), also called His domain-containing protein tyrosine phosphatase (HD-PTP) or protein tyrosine phosphatase TD14 (PTP-TD14), is a catalytically inactive member of the tyrosine-specific protein tyrosine phosphatase (PTP) family. Human PTPN23 may be involved in the regulation of small nuclear ribonucleoprotein assembly and pre-mRNA splicing by modifying the survival motor neuron (SMN) complex. It plays a role in ciliogenesis and is part of endosomal sorting complex required for transport (ESCRT) pathways. PTPN23 contains five domains: a BRO1-like domain that plays a role in endosomal sorting; a V-domain that interacts with Lys63-linked polyubiquitinated substrates; a central proline-rich region that might recruit SH3-containing proteins; a PTP-like domain; and a proteolytic degradation-targeting motif, also known as a PEST sequence.


Pssm-ID: 350387 [Multi-domain]  Cd Length: 205  Bit Score: 171.80  E-value: 5.23e-50
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25151513 367 YINANYVNMEIPSSgivNRYIACQGPLAHTSSDFWVMVWEQHCTTIVMLTTITERGRVKCHQYWP-RVFETQEYGRLMIK 445
Cdd:cd14539   1 YINASLIEDLTPYC---PRFIATQAPLPGTAADFWLMVYEQQVSVIVMLVSEQENEKQKVHRYWPtERGQALVYGAITVS 77

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25151513 446 CIKDKQTTNCCYREFSIRDRNSSEERRVTQMQYIAWPDHGVPDDPKHFIQFVDEVR---KARQGSVDPIVVHCSAGIGRT 522
Cdd:cd14539  78 LQSVRTTPTHVERIISIQHKDTRLSRSVVHLQFTTWPELGLPDSPNPLLRFIEEVHshyLQQRSLQTPIVVHCSSGVGRT 157

                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*
gi 25151513 523 GVLILMETAACLVESNEPVYPL-DIVRTMRDQRAMLIQTPGQYTF 566
Cdd:cd14539 158 GAFCLLYAAVQEIEAGNGIPDLpQLVRKMRQQRKYMLQEKEHLKF 202
R-PTPc-K-1 cd14631
catalytic domain of receptor-type tyrosine-protein phosphatase K, repeat 1; Receptor-type ...
 356-574 8.51e-50

catalytic domain of receptor-type tyrosine-protein phosphatase K, repeat 1; Receptor-type tyrosine-protein phosphatase K (PTPRK), also known as receptor-type tyrosine-protein phosphatase kappa (RPTP-kappa or PTPkappa), belongs to the type IIb subfamily of receptor protein tyrosine phosphatases (RPTPs), which belong to the larger family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. PTPRK is widely expressed and has been shown to stimulate cell motility and neurite outgrowth. It is required for anti-proliferative and pro-migratory effects of TGF-beta, suggesting a role in regulation, maintenance, and restoration of cell adhesion. It is a potential tumour suppressor in primary central nervous system lymphomas, colorectal cancer, and breast cancer. It contains an extracellular region with an Meprin-A5 (neuropilin)-mu (MAM) domain, an immunoglobulin (Ig) domain, and four fibronectin type III (FN3) repeats, a transmembrane domain, and an intracellular segment with a juxtamembrane domain similar to the cytoplasmic domain of classical cadherins and two tandem PTP domains. This model represents the first (repeat 1) PTP domain.


Pssm-ID: 350479 [Multi-domain]  Cd Length: 218  Bit Score: 171.74  E-value: 8.51e-50
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25151513 356 RVTLQA---SPSGDYINANYVN-MEIPSsgivnRYIACQGPLAHTSSDFWVMVWEQHCTTIVMLTTITERGRVKCHQYWP 431
Cdd:cd14631   1 RVILQPvedDPSSDYINANYIDgYQRPS-----HYIATQGPVHETVYDFWRMIWQEQSACIVMVTNLVEVGRVKCYKYWP 75

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25151513 432 RvfETQEYGRLMIKCIKDKQTTNCCYREFSIRDRNSSEERRVTQMQYIAWPDHGVPDDPKHFIQFVDEVRKARQGSVDPI 511
Cdd:cd14631  76 D--DTEVYGDFKVTCVEMEPLAEYVVRTFTLERRGYNEIREVKQFHFTGWPDHGVPYHATGLLSFIRRVKLSNPPSAGPI 153

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 25151513 512 VVHCSAGIGRTGVLILMETAACLVESNEPVYPLDIVRTMRDQRAMLIQTPGQYTFVCESILRA 574
Cdd:cd14631 154 VVHCSAGAGRTGCYIVIDIMLDMAEREGVVDIYNCVKALRSRRINMVQTEEQYIFIHDAILEA 216
R-PTP-F-2 cd14629
PTP-like domain of receptor-type tyrosine-protein phosphatase F, repeat 2; Receptor-type ...
 320-572 9.13e-50

PTP-like domain of receptor-type tyrosine-protein phosphatase F, repeat 2; Receptor-type tyrosine-protein phosphatase F (PTPRF), also known as leukocyte common antigen related (LAR), is the prototypical member of the LAR family of receptor-type tyrosine-protein phosphatases (RPTPs), which belong to the larger family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. PTPRF/LAR plays a role for LAR in cadherin complexes where it associates with and dephosphorylates beta-catenin, a pathway which may be critical for cadherin complex stability and cell-cell association. It also regulates focal adhesions through cyclin-dependent kinase-1 and is involved in axon guidance in the developing nervous system. It also functions in regulating insulin signaling. PTPRF contains an extracellular region with three immunoglobulin-like (Ig) domains and four to eight fibronectin type III (FN3) repeats (determined by alternative splicing), a single transmembrane domain, followed by an intracellular region with a membrane-proximal catalytic PTP domain (repeat 1, also called D1) and a membrane-distal non-catalytic PTP-like domain (repeat 2, also called D2). This model represents the non-catalytic PTP-like domain (repeat 2). Although described as non-catalytic, this domain contains the catalytic cysteine and the active site signature motif, HCSAGxGRxG.


Pssm-ID: 350477 [Multi-domain]  Cd Length: 291  Bit Score: 174.14  E-value: 9.13e-50
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25151513 320 FEMLYRKKPGMSMNI-CRLTANLAKNRYRDVCPYDDTRVTLQ---ASPSGDYINANYVNMEIPSSGivnrYIACQGPLAH 395
Cdd:cd14629  32 FKLLANSKAHTSRFIsANLPCNKFKNRLVNIMPYELTRVCLQpirGVEGSDYINASFIDGYRQQKA----YIATQGPLAE 107

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25151513 396 TSSDFWVMVWEQHCTTIVMLTTITERGRVKCHQYWPrVFETQEYGRLMIKCIKDKQTTNCCYREFSIRDRNSSEERRVTQ 475
Cdd:cd14629 108 TTEDFWRMLWEHNSTIVVMLTKLREMGREKCHQYWP-AERSARYQYFVVDPMAEYNMPQYILREFKVTDARDGQSRTIRQ 186

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25151513 476 MQYIAWPDHGVPDDPKHFIQFVDEVRKARQ--GSVDPIVVHCSAGIGRTGVLILMETAACLVESNEPVYPLDIVRTMRDQ 553
Cdd:cd14629 187 FQFTDWPEQGVPKTGEGFIDFIGQVHKTKEqfGQDGPITVHCSAGVGRTGVFITLSIVLERMRYEGVVDMFQTVKTLRTQ 266

                       250
                ....*....|....*....
gi 25151513 554 RAMLIQTPGQYTFVCESIL 572
Cdd:cd14629 267 RPAMVQTEDQYQLCYRAAL 285
R-PTPc-U-1 cd14632
catalytic domain of receptor-type tyrosine-protein phosphatase U, repeat 1; Receptor-type ...
 367-574 2.25e-49

catalytic domain of receptor-type tyrosine-protein phosphatase U, repeat 1; Receptor-type tyrosine-protein phosphatase U (PTPRU), also known as pancreatic carcinoma phosphatase 2 (PCP-2), belongs to the type IIb subfamily of receptor protein tyrosine phosphatases (RPTPs), which belong to the larger family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. PTPRU/PCP-2 is the most distant member of the type IIb subfamily and may have a distinct biological function other than cell-cell aggregation. It localizes to the adherens junctions and directly binds and dephosphorylates beta-catenin, and regulates the balance between signaling and adhesive beta-catenin. It plays an important role in the maintenance of epithelial integrity. PTPRU contains an extracellular region with an Meprin-A5 (neuropilin)-mu (MAM) domain, an immunoglobulin (Ig) domain, and four fibronectin type III (FN3) repeats, a transmembrane domain, and an intracellular segment with a juxtamembrane domain similar to the cytoplasmic domain of classical cadherins and two tandem PTP domains. This model represents the first (repeat 1) PTP domain.


Pssm-ID: 350480 [Multi-domain]  Cd Length: 205  Bit Score: 170.23  E-value: 2.25e-49
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25151513 367 YINANYVNMEIPSsgivNRYIACQGPLAHTSSDFWVMVWEQHCTTIVMLTTITERGRVKCHQYWPRvfETQEYGRLMIKC 446
Cdd:cd14632   1 YINANYIDGYHRS----NHFIATQGPKQEMVYDFWRMVWQEHCSSIVMITKLVEVGRVKCSKYWPD--DSDTYGDIKITL 74

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25151513 447 IKDKQTTNCCYREFSIRDRNSSEERRVTQMQYIAWPDHGVPDDPKHFIQFVDEVRKARQGSVDPIVVHCSAGIGRTGVLI 526
Cdd:cd14632  75 LKTETLAEYSVRTFALERRGYSARHEVKQFHFTSWPEHGVPYHATGLLAFIRRVKASTPPDAGPVVVHCSAGAGRTGCYI 154

                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*...
gi 25151513 527 LMETAACLVESNEPVYPLDIVRTMRDQRAMLIQTPGQYTFVCESILRA 574
Cdd:cd14632 155 VLDVMLDMAECEGVVDIYNCVKTLCSRRINMIQTEEQYIFIHDAILEA 202
R-PTPc-Q cd14616
catalytic domain of receptor-type tyrosine-protein phosphatase Q; Receptor-type ...
 344-569 3.48e-49

catalytic domain of receptor-type tyrosine-protein phosphatase Q; Receptor-type tyrosine-protein phosphatase Q (PTPRQ or R-PTP-Q), also called phosphatidylinositol phosphatase PTPRQ, belongs to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. PTPRQ is a member of the R3 subfamily of receptor-type phosphotyrosine phosphatases (RPTP), characterized by a unique modular composition consisting of multiple extracellular fibronectin type III (FN3) repeats (18 in PTPRQ) and a single (most RPTP subtypes have two) cytoplasmic catalytic PTP domain. It displays low tyrosine-protein phosphatase activity; rather, it functions as a phosphatidylinositol phosphatase required for auditory processes. It regulates the levels of phosphatidylinositol 4,5-bisphosphate (PIP2) in the basal region of hair bundles. It can dephosphorylate a broad range of phosphatidylinositol phosphates, including phosphatidylinositol 3,4,5-trisphosphate and most phosphatidylinositol monophosphates and diphosphates.


Pssm-ID: 350464 [Multi-domain]  Cd Length: 224  Bit Score: 170.09  E-value: 3.48e-49
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25151513 344 NRYRDVCPYDDTRVTLQA---SPSGDYINANYVnmeipsSGIV--NRYIACQGPLAHTSSDFWVMVWEQHCTTIVMLTTI 418
Cdd:cd14616   1 NRFPNIKPYNNNRVKLIAdagVPGSDYINASYI------SGYLcpNEFIATQGPLPGTVGDFWRMVWETRAKTIVMLTQC 74

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25151513 419 TERGRVKCHQYWPRVFE-TQEYGRLMIKCIKDKQTTNCCYREFSIrdRNSSEERRVTQMQYIAWPDHGVPDDPKHFIQFV 497
Cdd:cd14616  75 FEKGRIRCHQYWPEDNKpVTVFGDIVITKLMEDVQIDWTIRDLKI--ERHGDYMMVRQCNFTSWPEHGVPESSAPLIHFV 152

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 25151513 498 DEVRKARQGSVDPIVVHCSAGIGRTGVLILMETAACLVESNEPVYPLDIVRTMRDQRAMLIQTPGQYTFVCE 569
Cdd:cd14616 153 KLVRASRAHDNTPMIVHCSAGVGRTGVFIALDHLTQHINDHDFVDIYGLVAELRSERMCMVQNLAQYIFLHQ 224
R-PTPc-A-1 cd14621
catalytic domain of receptor-type tyrosine-protein phosphatase A, repeat 1; Receptor-type ...
 340-575 8.81e-49

catalytic domain of receptor-type tyrosine-protein phosphatase A, repeat 1; Receptor-type tyrosine-protein phosphatase A (PTPRA), also known as receptor-type tyrosine-protein phosphatase alpha (R-PTP-alpha), belongs to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. PTPRA is a positive regulator of Src and Src family kinases via dephosphorylation of the Src-inhibitory tyrosine 527. Thus, it affects transformation and tumorigenesis, inhibition of proliferation, cell cycle arrest, integrin signaling, neuronal differentiation and outgrowth, and ion channel activity. It is also involved in interleukin-1 signaling in fibroblasts through its interaction with the focal adhesion targeting domain of focal adhesion kinase. PTPRA comprises a small extracellular domain, a transmembrane segment, and an intracellular region containing two tandem catalytic PTP domains. This model represents the first catalytic PTP domain (repeat 1).


Pssm-ID: 350469 [Multi-domain]  Cd Length: 296  Bit Score: 171.75  E-value: 8.81e-49
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25151513 340 NLAKNRYRDVCPYDDTRVTL---QASPSGDYINANYVNMEIPSsgivNRYIACQGPLAHTSSDFWVMVWEQHCTTIVMLT 416
Cdd:cd14621  52 NKEKNRYVNILPYDHSRVHLtpvEGVPDSDYINASFINGYQEK----NKFIAAQGPKEETVNDFWRMIWEQNTATIVMVT 127

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25151513 417 TITERGRVKCHQYWPRVfETQEYGRLMIKCIKDKQTTNCCYREFSIRD----RNSSEERRVTQMQYIAWPDHGVPDDPKH 492
Cdd:cd14621 128 NLKERKECKCAQYWPDQ-GCWTYGNIRVSVEDVTVLVDYTVRKFCIQQvgdvTNKKPQRLITQFHFTSWPDFGVPFTPIG 206

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25151513 493 FIQFVDEVRKARQGSVDPIVVHCSAGIGRTGVLILMETAACLVESNEPVYPLDIVRTMRDQRAMLIQTPGQYTFVCESIL 572
Cdd:cd14621 207 MLKFLKKVKNCNPQYAGAIVVHCSAGVGRTGTFIVIDAMLDMMHAERKVDVYGFVSRIRAQRCQMVQTDMQYVFIYQALL 286


                ...
gi 25151513 573 RAY 575
Cdd:cd14621 287 EHY 289
R-PTPc-A-E-1 cd14551
catalytic domain of receptor-type tyrosine-protein phosphatase A and E, repeat 1; ...
 367-567 3.13e-48

catalytic domain of receptor-type tyrosine-protein phosphatase A and E, repeat 1; Receptor-type tyrosine-protein phosphatase A (PTPRA) and E (PTPRE) belong to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. PTPRA and PTPRE share several functions including regulation of Src family kinases and voltage-gated potassium (Kv) channels. They both contain a small extracellular domain, a transmembrane segment, and an intracellular region containing two tandem catalytic PTP domains. This model represents the first catalytic PTP domain (repeat 1).


Pssm-ID: 350399 [Multi-domain]  Cd Length: 202  Bit Score: 167.01  E-value: 3.13e-48
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25151513 367 YINANYVNMEIPSsgivNRYIACQGPLAHTSSDFWVMVWEQHCTTIVMLTTITERGRVKCHQYWPRVFEtQEYGRLMIK- 445
Cdd:cd14551   1 YINASYIDGYQEK----NKFIAAQGPKDETVNDFWRMIWEQGSATIVMVTNLKERKEKKCSQYWPDQGC-WTYGNLRVRv 75

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25151513 446 --CIK--DKQTTNCCYREFSiRDRNSSEERRVTQMQYIAWPDHGVPDDPKHFIQFVDEVRKARQGSVDPIVVHCSAGIGR 521
Cdd:cd14551  76 edTVVlvDYTTRKFCIQKVN-RGIGEKRVRLVTQFHFTSWPDFGVPFTPIGMLKFLKKVKSANPPRAGPIVVHCSAGVGR 154

                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*.
gi 25151513 522 TGVLILMETAACLVESNEPVYPLDIVRTMRDQRAMLIQTPGQYTFV 567
Cdd:cd14551 155 TGTFIVIDAMLDMMHAEGKVDVFGFVSRIRQQRSQMVQTDMQYVFI 200
R-PTPc-Z-1 cd17668
catalytic domain of receptor-type tyrosine-protein phosphatase Z, repeat 1; Receptor-type ...
 367-572 8.27e-48

catalytic domain of receptor-type tyrosine-protein phosphatase Z, repeat 1; Receptor-type tyrosine-protein phosphatase Z (PTPRZ), also called receptor-type tyrosine-protein phosphatase zeta (R-PTP-zeta), belongs to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. Three isoforms are generated by alternative splicing from a single PTPRZ gene: two transmembrane isoforms, PTPRZ-A and PTPRZ-B, and one secretory isoform, PTPRZ-S (also known as phosphacan); all are preferentially expressed in the central nervous system (CNS) as chondroitin sulfate (CS) proteoglycans. PTPRZ isoforms play important roles in maintaining oligodendrocyte precursor cells in an undifferentiated state. PTPRZ is a type 1 integral membrane protein consisting of an extracellular region with a carbonic anhydrase-like (CAH) and a fibronectin type III (FN3) domains, and an intracellular region with a catalytic PTP domain (repeat 1) proximal to the membrane, and a catalytically inactive PTP-fold domain (repeat 2) distal to the membrane. This model represents the catalytic PTP domain (repeat 1).


Pssm-ID: 350506 [Multi-domain]  Cd Length: 209  Bit Score: 165.92  E-value: 8.27e-48
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25151513 367 YINANYVN-MEIPSSgivnrYIACQGPLAHTSSDFWVMVWEQHCTTIVMLTTITERGRVKCHQYWPrVFETQEYGRLMIK 445
Cdd:cd17668   1 YINANYVDgYNKPKA-----YIAAQGPLKSTAEDFWRMIWEHNVEVIVMITNLVEKGRRKCDQYWP-ADGSEEYGNFLVT 74

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25151513 446 CIKDKQTTNCCYREFSIRD--------RNSSEERRVTQMQYIAWPDHGVPDDPKHFIQFVDEVRKARQGSVDPIVVHCSA 517
Cdd:cd17668  75 QKSVQVLAYYTVRNFTLRNtkikkgsqKGRPSGRVVTQYHYTQWPDMGVPEYTLPVLTFVRKASYAKRHAVGPVVVHCSA 154

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*
gi 25151513 518 GIGRTGVLILMETAACLVESNEPVYPLDIVRTMRDQRAMLIQTPGQYTFVCESIL 572
Cdd:cd17668 155 GVGRTGTYIVLDSMLQQIQHEGTVNIFGFLKHIRSQRNYLVQTEEQYVFIHDALV 209
PTPc-N12 cd14604
catalytic domain of tyrosine-protein phosphatase non-receptor type 12; Tyrosine-protein ...
 340-571 1.59e-47

catalytic domain of tyrosine-protein phosphatase non-receptor type 12; Tyrosine-protein phosphatase non-receptor type 12 (PTPN12), also called PTP-PEST or protein-tyrosine phosphatase G1 (PTPG1), belongs to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. PTPN12 is characterized as a tumor suppressor and a pivotal regulator of EGFR/HER2 signaling. It regulates various physiological processes, including cell migration, immune response, and neuronal activity, by dephosphorylating multiple substrates including HER2, FAK, PYK2, PSTPIP, WASP, p130Cas, paxillin, Shc, catenin, c-Abl, ArgBP2, p190RhoGAP, RhoGDI, cell adhesion kinase beta, and Rho GTPase.


Pssm-ID: 350452 [Multi-domain]  Cd Length: 297  Bit Score: 168.19  E-value: 1.59e-47
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25151513 340 NLAKNRYRDVCPYDDTRV--TLQASP-SGDYINANYVN-MEIPSSgivnrYIACQGPLAHTSSDFWVMVWEQHCTTIVML 415
Cdd:cd14604  57 NVKKNRYKDILPFDHSRVklTLKTSSqDSDYINANFIKgVYGPKA-----YIATQGPLANTVIDFWRMIWEYNVAIIVMA 131

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25151513 416 TTITERGRVKCHQYWPRVFETQ-EYGRLMIKCIKDKQTTNCCYREFSIRDRNssEERRVTQMQYIAWPDHGVPDDPKHFI 494
Cdd:cd14604 132 CREFEMGRKKCERYWPLYGEEPmTFGPFRISCEAEQARTDYFIRTLLLEFQN--ETRRLYQFHYVNWPDHDVPSSFDSIL 209

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25151513 495 QFVDEVRKARQGSVDPIVVHCSAGIGRTGVLILMETAACLVESN---EPVYPLDIVRTMRDQRAMLIQTPGQYTFVCESI 571
Cdd:cd14604 210 DMISLMRKYQEHEDVPICIHCSAGCGRTGAICAIDYTWNLLKAGkipEEFNVFNLIQEMRTQRHSAVQTKEQYELVHRAI 289
R-PTP-N2 cd14610
PTP-like domain of receptor-type tyrosine-protein phosphatase N2; Receptor-type ...
 304-571 2.08e-47

PTP-like domain of receptor-type tyrosine-protein phosphatase N2; Receptor-type tyrosine-protein phosphatase N2 (PTPRN2 or R-PTP-N2), also called islet cell autoantigen-related protein (IAR), ICAAR, phogrin, or IA-2beta, belongs to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). It consists of a large ectodomain that contains a RESP18HD (regulated endocrine-specific protein 18 homology domain), followed by a transmembrane segment, and a single, catalytically-impaired, PTP domain. It is mainly expressed in neuropeptidergic neurons and peptide-secreting endocrine cells, including insulin-producing pancreatic beta-cells. It may function as a phosphatidylinositol phosphatase to regulate insulin secretion. It is also required for normal accumulation of the neurotransmitters norepinephrine, dopamine and serotonin in the brain.


Pssm-ID: 350458 [Multi-domain]  Cd Length: 283  Bit Score: 167.54  E-value: 2.08e-47
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25151513 304 LQLLADSL-NSGKVVDHFEML--YRKKPGMSmNICRLTANLAKNRYRDVCPYDDTRVTLQASPS---GDYINANYVNMEI 377
Cdd:cd14610   6 LSYMEDHLkNKNRLEKEWEALcaYQAEPNAT-NVAQREENVQKNRSLAVLPYDHSRIILKAENShshSDYINASPIMDHD 84

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25151513 378 PSSgivNRYIACQGPLAHTSSDFWVMVWEQHCTTIVMLTTITERGRVKCHQYWP-------RVFETQEYGRlMIKCikdk 450
Cdd:cd14610  85 PRN---PAYIATQGPLPATVADFWQMVWESGCVVIVMLTPLAENGVKQCYHYWPdegsnlyHIYEVNLVSE-HIWC---- 156

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25151513 451 qtTNCCYREFSIRDRNSSEERRVTQMQYIAWPDHGVPDDPKHFIQFVDEVRKARQGSVDPIVVHCSAGIGRTGVLILMET 530
Cdd:cd14610 157 --EDFLVRSFYLKNLQTNETRTVTQFHFLSWNDQGVPASTRSLLDFRRKVNKCYRGRSCPIIVHCSDGAGRSGTYILIDM 234

                       250       260       270       280
                ....*....|....*....|....*....|....*....|....
gi 25151513 531 AacLVESNEPVYPLDIVRT---MRDQRAMLIQTPGQYTFVCESI 571
Cdd:cd14610 235 V--LNKMAKGAKEIDIAATlehLRDQRPGMVQTKEQFEFALTAV 276
PTPc-N22 cd14602
catalytic domain of tyrosine-protein phosphatase non-receptor type 22; Tyrosine-protein ...
 343-575 6.38e-47

catalytic domain of tyrosine-protein phosphatase non-receptor type 22; Tyrosine-protein phosphatase non-receptor type 22 (PTPN22), also called lymphoid phosphatase (LyP), PEST-domain phosphatase (PEP), or hematopoietic cell protein-tyrosine phosphatase 70Z-PEP, belongs to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. PTPN22 is expressed in hematopoietic cells and it functions as a key regulator of immune homeostasis by inhibiting T-cell receptor signaling through the direct dephosphorylation of Src family kinases (Lck and Fyn), ITAMs of the TCRz/CD3 complex, and other signaling molecules. Mutations in the PTPN22 gene are associated with multiple connective tissue and autoimmune diseases including type 1 diabetes mellitus, rheumatoid arthritis, and systemic lupus erythematosus. PTPN22 contains an N-terminal catalytic PTP domain and four proline-rich regions at the C-terminus.


Pssm-ID: 350450 [Multi-domain]  Cd Length: 234  Bit Score: 164.63  E-value: 6.38e-47
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25151513 343 KNRYRDVCPYDDTRVTLQASPS---GDYINANYVNmeipssGIV--NRYIACQGPLAHTSSDFWVMVWEQHCTTIVMLTT 417
Cdd:cd14602   1 KNRYKDILPYDHSRVELSLITSdedSDYINANFIK------GVYgpRAYIATQGPLSTTLLDFWRMIWEYSVLIIVMACM 74

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25151513 418 ITERGRVKCHQYWPRVFETQ-EYGRLMIKCIKDKQTTNCCYRefSIRDRNSSEERRVTQMQYIAWPDHGVPDDPKHFIQF 496
Cdd:cd14602  75 EFEMGKKKCERYWAEPGEMQlEFGPFSVTCEAEKRKSDYIIR--TLKVKFNSETRTIYQFHYKNWPDHDVPSSIDPILEL 152

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25151513 497 VDEVRKARQGSVDPIVVHCSAGIGRTGVLILMETAACL-----VESNEPVYplDIVRTMRDQRAMLIQTPGQYTFVCESI 571
Cdd:cd14602 153 IWDVRCYQEDDSVPICIHCSAGCGRTGVICAIDYTWMLlkdgiIPENFSVF--SLIQEMRTQRPSLVQTKEQYELVYNAV 230


                ....
gi 25151513 572 LRAY 575
Cdd:cd14602 231 IELF 234
R-PTP-N-N2 cd14546
PTP-like domain of receptor-type tyrosine-protein phosphatase-like N and N2; Receptor-type ...
 367-571 7.09e-47

PTP-like domain of receptor-type tyrosine-protein phosphatase-like N and N2; Receptor-type tyrosine-protein phosphatase-like N (PTPRN) and N2 (PTPRN2) belong to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). They consist of a large ectodomain that contains a RESP18HD (regulated endocrine-specific protein 18 homology domain), followed by a transmembrane segment, and a single, catalytically-impaired, PTP domain. They are mainly expressed in neuropeptidergic neurons and peptide-secreting endocrine cells, including insulin-producing pancreatic beta-cells, and are involved in involved in the generation, cargo storage, traffic, exocytosis and recycling of insulin secretory granules, as well as in beta-cell proliferation. They also are major autoantigens in type 1 diabetes and are involved in the regulation of insulin secretion.


Pssm-ID: 350394 [Multi-domain]  Cd Length: 208  Bit Score: 163.38  E-value: 7.09e-47
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25151513 367 YINANYVNMEIPSSGIvnrYIACQGPLAHTSSDFWVMVWEQHCTTIVMLTTITERGRVKCHQYWPRVfETQEYGRLMIKC 446
Cdd:cd14546   1 YINASTIYDHDPRNPA---YIATQGPLPHTIADFWQMIWEQGCVVIVMLTRLQENGVKQCARYWPEE-GSEVYHIYEVHL 76

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25151513 447 IKDKqttNCC----YREFSIRDRNSSEERRVTQMQYIAWPDHGVPDDPKHFIQFVDEVRKARQGSVDPIVVHCSAGIGRT 522
Cdd:cd14546  77 VSEH---IWCddylVRSFYLKNLQTSETRTVTQFHFLSWPDEGIPASAKPLLEFRRKVNKSYRGRSCPIVVHCSDGAGRT 153

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|..
gi 25151513 523 GVLILMETAacLVESNEPVYPLDIVRT---MRDQRAMLIQTPGQYTFVCESI 571
Cdd:cd14546 154 GTYILIDMV--LNRMAKGAKEIDIAATlehLRDQRPGMVKTKDQFEFVLTAV 203
PTPc-N5 cd14613
catalytic domain of tyrosine-protein phosphatase non-receptor type 5; Tyrosine-protein ...
 343-567 9.75e-47

catalytic domain of tyrosine-protein phosphatase non-receptor type 5; Tyrosine-protein phosphatase non-receptor type 5 (PTPN5), also called striatum-enriched protein-tyrosine phosphatase (STEP) or neural-specific PTP, belongs to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. PTPN5/STEP is a kinase interaction motif (KIM)-PTP, characterized by the presence of a 16-amino-acid KIM that binds specifically to members of the MAPK (mitogen-activated protein kinase) family. It is a CNS-enriched protein that regulates key signaling proteins required for synaptic strengthening, as well as NMDA and AMPA receptor trafficking. PTPN5 is implicated in multiple neurologic and neuropsychiatric disorders, such as Alzheimer's disease, Parkinson's disease, schizophrenia, and fragile X syndrome.


Pssm-ID: 350461 [Multi-domain]  Cd Length: 258  Bit Score: 164.65  E-value: 9.75e-47
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25151513 343 KNRYRDVCPYDDTRVTLQASPSGD----YINANYVNmeiPSSGIVNRYIACQGPLAHTSSDFWVMVWEQHCTTIVMLTTI 418
Cdd:cd14613  28 KNRYKTILPNPHSRVCLTSPDQDDplssYINANYIR---GYGGEEKVYIATQGPTVNTVGDFWRMVWQERSPIIVMITNI 104

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25151513 419 TERGRvKCHQYWPRvfETQEYGRLMIKCIKDKQTTNCCYREFSIrdRNSSEERRVTQMQYIAWPDHGVPDDPKHFIQFVD 498
Cdd:cd14613 105 EEMNE-KCTEYWPE--EQVTYEGIEITVKQVIHADDYRLRLITL--KSGGEERGLKHYWYTSWPDQKTPDNAPPLLQLVQ 179

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 25151513 499 EVRKARQG---SVDPIVVHCSAGIGRTGVLIlMETAACLVESNEPVypLDIVRT---MRDQRAMLIQTPGQYTFV 567
Cdd:cd14613 180 EVEEARQQaepNCGPVIVHCSAGIGRTGCFI-ATSICCKQLRNEGV--VDILRTtcqLRLDRGGMIQTCEQYQFV 251
R-PTPc-C-1 cd14557
catalytic domain of receptor-type tyrosine-protein phosphatase C, repeat 1; Receptor-type ...
 367-567 6.07e-46

catalytic domain of receptor-type tyrosine-protein phosphatase C, repeat 1; Receptor-type tyrosine-protein phosphatase C (PTPRC), also known as CD45, leukocyte common antigen (LCA) or GP180, belongs to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. PTPRC/CD45 is found in all nucleated hematopoietic cells and is an essential regulator of T- and B-cell antigen receptor signaling. It controls immune response, both positively and negatively, by dephosphorylating a number of signaling molecules such as the Src family kinases, the CD3zeta chain of TCY, and ZAP-70 kinase. Mutations in the human PTPRC/CD45 gene are associated with severe combined immunodeficiency (SCID) and multiple sclerosis. PTPRC/CD45 contains an extracellular receptor-like region with fibronectin type III (FN3) repeats, a short transmembrane segment, and a cytoplasmic region comprising of a membrane proximal catalytically active PTP domain (repeat 1 or D1) and a membrane distal catalytically impaired PTP-like domain (repeat 2, or D2). This model represents repeat 1.


Pssm-ID: 350405 [Multi-domain]  Cd Length: 201  Bit Score: 160.76  E-value: 6.07e-46
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25151513 367 YINANYVN-MEIPssgivNRYIACQGPLAHTSSDFWVMVWEQHCTTIVMLTTITERGRVKCHQYWPRVFETQE-YGRLMI 444
Cdd:cd14557   1 YINASYIDgFKEP-----RKYIAAQGPKDETVDDFWRMIWEQKSTVIVMVTRCEEGNRNKCAQYWPSMEEGSRaFGDVVV 75

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25151513 445 KCIKDKQTTNCCYREFSIRD-RNSSEERRVTQMQYIAWPDHGVPDDPKHFIQFVDEVRKARQGSVDPIVVHCSAGIGRTG 523
Cdd:cd14557  76 KINEEKICPDYIIRKLNINNkKEKGSGREVTHIQFTSWPDHGVPEDPHLLLKLRRRVNAFNNFFSGPIVVHCSAGVGRTG 155

                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*..
gi 25151513 524 VLILMEtaaCLVESNEPVYPLDI---VRTMRDQRAMLIQTPGQYTFV 567
Cdd:cd14557 156 TYIGID---AMLEGLEAEGRVDVygyVVKLRRQRCLMVQVEAQYILI 199
R-PTPc-R cd14611
catalytic domain of receptor-type tyrosine-protein phosphatase R; Receptor-type ...
 343-567 1.28e-44

catalytic domain of receptor-type tyrosine-protein phosphatase R; Receptor-type tyrosine-protein phosphatase-like R (PTPRR or R-PTP-R), also called protein-tyrosine phosphatase PCPTP1, belongs to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. PTPRR is a kinase interaction motif (KIM)-PTP, characterized by the presence of a 16-amino-acid KIM that binds specifically to members of the MAPK (mitogen-activated protein kinase) family. The human and mouse PTPRR gene produces multiple neuronal protein isoforms of varying sizes (in human, PTPPBS-alpha, beta, gamma and delta). All isoforms contain the KIM motif and the catalytic PTP domain. PTPRR-deficient mice show significant defects in fine motor coordination and balance skills that are reminiscent of a mild ataxia.


Pssm-ID: 350459 [Multi-domain]  Cd Length: 226  Bit Score: 158.16  E-value: 1.28e-44
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25151513 343 KNRYRDVCPYDDTRVTLQASPSGD----YINANYVNmeiPSSGIVNRYIACQGPLAHTSSDFWVMVWEQHCTTIVMLTTI 418
Cdd:cd14611   2 KNRYKTILPNPHSRVCLKPKNSNDslstYINANYIR---GYGGKEKAFIATQGPMINTVNDFWQMVWQEDSPVIVMITKL 78

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25151513 419 TERGRvKCHQYWPRvfETQEYGRLMIKCIKDKQTTNCCYREFSIRdrNSSEERRVTQMQYIAWPDHGVPDDPKHFIQFVD 498
Cdd:cd14611  79 KEKNE-KCVLYWPE--KRGIYGKVEVLVNSVKECDNYTIRNLTLK--QGSQSRSVKHYWYTSWPDHKTPDSAQPLLQLML 153

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 25151513 499 EVRKARQGSVD--PIVVHCSAGIGRTGVLILMETAACLVESNEPVYPLDIVRTMRDQRAMLIQTPGQYTFV 567
Cdd:cd14611 154 DVEEDRLASPGrgPVVVHCSAGIGRTGCFIATTIGCQQLKEEGVVDVLSIVCQLRVDRGGMVQTSEQYEFV 224
R-PTPc-A-E-2 cd14552
catalytic domain of receptor-type tyrosine-protein phosphatase A and E, repeat 2; ...
 367-566 3.01e-43

catalytic domain of receptor-type tyrosine-protein phosphatase A and E, repeat 2; Receptor-type tyrosine-protein phosphatase A (PTPRA) and E (PTPRE) belong to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. PTPRA and PTPRE share several functions including regulation of Src family kinases and voltage-gated potassium (Kv) channels. They both contain a small extracellular domain, a transmembrane segment, and an intracellular region containing two tandem catalytic PTP domains. This model represents the second PTP domain (repeat 2).


Pssm-ID: 350400 [Multi-domain]  Cd Length: 202  Bit Score: 153.58  E-value: 3.01e-43
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25151513 367 YINANYV---NMEipssgivNRYIACQGPLAHTSSDFWVMVWEQHCTTIVMLTTITERGRVKCHQYWPRVfETQEYGRLM 443
Cdd:cd14552   1 YINASFIdgyRQK-------DAYIATQGPLDHTVEDFWRMIWEWKSCSIVMLTEIKERSQNKCAQYWPED-GSVSSGDIT 72

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25151513 444 IKCIKDKQTTNCCYREFSIRDRNSSEERRVTQMQYIAWPDHGVPDDPKHFIQFVDEVRKARQGSVD-PIVVHCSAGIGRT 522
Cdd:cd14552  73 VELKDQTDYEDYTLRDFLVTKGKGGSTRTVRQFHFHGWPEVGIPDNGKGMIDLIAAVQKQQQQSGNhPITVHCSAGAGRT 152

                       170       180       190       200
                ....*....|....*....|....*....|....*....|....
gi 25151513 523 GVLILMETAACLVESNEPVYPLDIVRTMRDQRAMLIQTPGQYTF 566
Cdd:cd14552 153 GTFCALSTVLERVKAEGVLDVFQVVKSLRLQRPHMVQTLEQYEF 196
PTPc_plant_PTP1 cd17658
protein tyrosine phosphatase 1 from Arabidopsis thaliana and similar plant PTPs; Arabidopsis ...
 367-566 6.50e-43

protein tyrosine phosphatase 1 from Arabidopsis thaliana and similar plant PTPs; Arabidopsis thaliana protein tyrosine phosphatase 1 (AtPTP1) belongs to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. AtPTP1 dephosphorylates and inhibits MAP kinase 6 (MPK6) in non-oxidative stress conditions. Together with MAP kinase phosphatase 1 (MKP1) it expresses salicylic acid (SA) and camalexin biosynthesis, and therefore, modulating defense response.


Pssm-ID: 350496 [Multi-domain]  Cd Length: 206  Bit Score: 152.62  E-value: 6.50e-43
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25151513 367 YINANYVnmEIPSSGIVNRYIACQGPLAHTSSDFWVMVWEQHCTTIVMLTTITERGR-VKCHQYWPRV-FETQEYGRLMI 444
Cdd:cd17658   1 YINASLV--ETPASESLPKFIATQGPLPHTFEDFWEMVIQQRCPVIIMLTRLVDNYStAKCADYFPAEeNESREFGRISV 78

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25151513 445 KCIKDKQT-TNCCYREFSIRDRNSSEE-RRVTQMQYIAWPDHGVPDDPKhfiqFVDEVRKARQG---SVDPIVVHCSAGI 519
Cdd:cd17658  79 TNKKLKHSqHSITLRVLEVQYIESEEPpLSVLHIQYPEWPDHGVPKDTR----SVRELLKRLYGippSAGPIVVHCSAGI 154

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|.
gi 25151513 520 GRTGVLILME-TAACLVESNepVYPLDI---VRTMRDQRAMLIQTPGQYTF 566
Cdd:cd17658 155 GRTGAYCTIHnTIRRILEGD--MSAVDLsktVRKFRSQRIGMVQTQDQYIF 203
R-PTPc-A-2 cd14623
catalytic domain of receptor-type tyrosine-protein phosphatase A, repeat 2; Receptor-type ...
 345-566 1.32e-42

catalytic domain of receptor-type tyrosine-protein phosphatase A, repeat 2; Receptor-type tyrosine-protein phosphatase A (PTPRA), also known as receptor-type tyrosine-protein phosphatase alpha (R-PTP-alpha), belongs to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. PTPRA is a positive regulator of Src and Src family kinases via dephosphorylation of the Src-inhibitory tyrosine 527. Thus, it affects transformation and tumorigenesis, inhibition of proliferation, cell cycle arrest, integrin signaling, neuronal differentiation and outgrowth, and ion channel activity. It is also involved in interleukin-1 signaling in fibroblasts through its interaction with the focal adhesion targeting domain of focal adhesion kinase. PTPRA comprises a small extracellular domain, a transmembrane segment, and an intracellular region containing two tandem catalytic PTP domains. This model represents the second PTP domain (repeat 2).


Pssm-ID: 350471 [Multi-domain]  Cd Length: 228  Bit Score: 152.51  E-value: 1.32e-42
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25151513 345 RYRDVCPYDDTRVTL---QASPSGDYINANYVNmeipSSGIVNRYIACQGPLAHTSSDFWVMVWEQHCTTIVMLTTITER 421
Cdd:cd14623   1 RVLQIIPYEFNRVIIpvkRGEENTDYVNASFID----GYRQKDSYIASQGPLQHTIEDFWRMIWEWKSCSIVMLTELEER 76

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25151513 422 GRVKCHQYWPRVfETQEYGRLMIKCIKDKQTTNCCYREFSIRDRNSSEERRVTQMQYIAWPDHGVPDDPKHFIQFVDEVR 501
Cdd:cd14623  77 GQEKCAQYWPSD-GSVSYGDITIELKKEEECESYTVRDLLVTNTRENKSRQIRQFHFHGWPEVGIPSDGKGMINIIAAVQ 155

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 25151513 502 KARQGSVD-PIVVHCSAGIGRTGVLILMETAACLVESNEPVYPLDIVRTMRDQRAMLIQTPGQYTF 566
Cdd:cd14623 156 KQQQQSGNhPITVHCSAGAGRTGTFCALSTVLERVKAEGILDVFQTVKSLRLQRPHMVQTLEQYEF 221
R-PTPc-E-2 cd14622
catalytic domain of receptor-type tyrosine-protein phosphatase E, repeat 2; Receptor-type ...
 366-575 9.84e-42

catalytic domain of receptor-type tyrosine-protein phosphatase E, repeat 2; Receptor-type tyrosine-protein phosphatase E (PTPRE), also known as receptor-type tyrosine-protein phosphatase epsilon (R-PTP-epsilon), belongs to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. The PTPRE gene contains two distinct promoters that generate the two major isoforms: transmembrane (receptor type RPTPe or PTPeM) and cytoplasmic (cyt-PTPe or PTPeC). Receptor type RPTPe plays a critical role in signaling transduction pathways and phosphoprotein network topology in red blood cells, and may also play a role in osteoclast formation and function. It also negatively regulates PDGFRbeta-mediated signaling pathways that are crucial for the pathogenesis of atherosclerosis. cyt-PTPe acts as a negative regulator of insulin receptor signaling in skeletal muscle. It regulates insulin-induced phosphorylation of proteins downstream of the insulin receptor. Receptor type RPTPe contains a small extracellular region, a single transmembrane segment, and an intracellular region two tandem catalytic PTP domains. This model represents the second PTP domain (repeat 2).


Pssm-ID: 350470 [Multi-domain]  Cd Length: 205  Bit Score: 149.39  E-value: 9.84e-42
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25151513 366 DYINANYVNmeipssGIVNR--YIACQGPLAHTSSDFWVMVWEQHCTTIVMLTTITERGRVKCHQYWPRVfETQEYGRLM 443
Cdd:cd14622   1 DYINASFID------GYRQKdyFIATQGPLAHTVEDFWRMVWEWKCHTIVMLTELQEREQEKCVQYWPSE-GSVTHGEIT 73

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25151513 444 IKCIKDKQTTNCCYREFSIRDRNSSEERRVTQMQYIAWPDHGVPDDPKHFIQFVDEVRKARQGSVD-PIVVHCSAGIGRT 522
Cdd:cd14622  74 IEIKNDTLLETISIRDFLVTYNQEKQTRLVRQFHFHGWPEIGIPAEGKGMIDLIAAVQKQQQQTGNhPIVVHCSAGAGRT 153

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|...
gi 25151513 523 GVLILMETAACLVESNEPVYPLDIVRTMRDQRAMLIQTPGQYTFvCESILRAY 575
Cdd:cd14622 154 GTFIALSNILERVKAEGLLDVFQTVKSLRLQRPHMVQTLEQYEF-CYRVVQDF 205
PHA02742 PHA02742
protein tyrosine phosphatase; Provisional
 331-566 1.72e-41

protein tyrosine phosphatase; Provisional


Pssm-ID: 165109 [Multi-domain]  Cd Length: 303  Bit Score: 152.08  E-value: 1.72e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25151513  331 SMNICRLTANLAKNRYRDVCPYDDTRVTLQASPSG-DYINANYVNmeipSSGIVNRYIACQGPLAHTSSDFWVMVWEQHC 409
Cdd:PHA02742  43 SCNESLELKNMKKCRYPDAPCFDRNRVILKIEDGGdDFINASYVD----GHNAKGRFICTQAPLEETALDFWQAIFQDQV 118

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25151513  410 TTIVMLTTITERGRVKCHQYW-PRVFETQEYGRLMIKCIKDKQTTNCCYREFSIRDRNSSEERRVTQMQYIAWPDHGVPD 488
Cdd:PHA02742 119 RVIVMITKIMEDGKEACYPYWmPHERGKATHGEFKIKTKKIKSFRNYAVTNLCLTDTNTGASLDIKHFAYEDWPHGGLPR 198

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25151513  489 DPKHFIQFVDEVRKAR-QGSVD----------PIVVHCSAGIGRTGVLILMETAACLVESNEPVYPLDIVRTMRDQRAML 557
Cdd:PHA02742 199 DPNKFLDFVLAVREADlKADVDikgenivkepPILVHCSAGLDRAGAFCAIDICISKYNERAIIPLLSIVRDLRKQRHNC 278


                 ....*....
gi 25151513  558 IQTPGQYTF 566
Cdd:PHA02742 279 LSLPQQYIF 287
PHA02738 PHA02738
hypothetical protein; Provisional
 339-579 1.17e-40

hypothetical protein; Provisional


Pssm-ID: 222923 [Multi-domain]  Cd Length: 320  Bit Score: 150.08  E-value: 1.17e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25151513  339 ANLAKNRYRDVCPYDDTRVTLQASPS-GDYINANYVNmeipSSGIVNRYIACQGPLAHTSSDFWVMVWEQHCTTIVMLTT 417
Cdd:PHA02738  48 KNRKLNRYLDAVCFDHSRVILPAERNrGDYINANYVD----GFEYKKKFICGQAPTRQTCYDFYRMLWMEHVQIIVMLCK 123

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25151513  418 ITERGRVKCHQYWPRVFETQ-EYGRLMIKCIkdKQTTNCCYREFSIRDRNSSEE-RRVTQMQYIAWPDHGVPDDPKHFIQ 495
Cdd:PHA02738 124 KKENGREKCFPYWSDVEQGSiRFGKFKITTT--QVETHPHYVKSTLLLTDGTSAtQTVTHFNFTAWPDHDVPKNTSEFLN 201

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25151513  496 FVDEVRKARQ-------------GSVDPIVVHCSAGIGRTGVLILMETAACLVESNEPVYPLDIVRTMRDQRAMLIQTPG 562
Cdd:PHA02738 202 FVLEVRQCQKelaqeslqighnrLQPPPIVVHCNAGLGRTPCYCVVDISISRFDACATVSIPSIVSSIRNQRYYSLFIPF 281

                        250
                 ....*....|....*..
gi 25151513  563 QYtFVCESILRAYHDGT 579
Cdd:PHA02738 282 QY-FFCYRAVKRYVNLT 297
PHA02746 PHA02746
protein tyrosine phosphatase; Provisional
 340-573 3.59e-40

protein tyrosine phosphatase; Provisional


Pssm-ID: 165113 [Multi-domain]  Cd Length: 323  Bit Score: 149.02  E-value: 3.59e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25151513  340 NLAKNRYRDVCPYDDTRVTLQASPS------GD----------------YINANYVNmeipssGI--VNRYIACQGPLAH 395
Cdd:PHA02746  51 NLKKNRFHDIPCWDHSRVVINAHESlkmfdvGDsdgkkievtsednaenYIHANFVD------GFkeANKFICAQGPKED 124

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25151513  396 TSSDFWVMVWEQHCTTIVMLTTiTERGRVKCHQYW--PRVFETQeYGRLMIKCIKDKQTTNCCYREFSIRDRNSSEERRV 473
Cdd:PHA02746 125 TSEDFFKLISEHESQVIVSLTD-IDDDDEKCFELWtkEEDSELA-FGRFVAKILDIIEELSFTKTRLMITDKISDTSREI 202

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25151513  474 TQMQYIAWPDHGVPDDPKHFIQFVDEVRKARQ----------GSVDPIVVHCSAGIGRTGVLILMETAACLVESNEPVYP 543
Cdd:PHA02746 203 HHFWFPDWPDNGIPTGMAEFLELINKVNEEQAelikqadndpQTLGPIVVHCSAGIGRAGTFCAIDNALEQLEKEKEVCL 282

                        250       260       270
                 ....*....|....*....|....*....|
gi 25151513  544 LDIVRTMRDQRAMLIQTPGQYTFvCESILR 573
Cdd:PHA02746 283 GEIVLKIRKQRHSSVFLPEQYAF-CYKALK 311
R-PTP-C-2 cd14558
PTP-like domain of receptor-type tyrosine-protein phosphatase C, repeat 2; Receptor-type ...
 367-566 4.24e-39

PTP-like domain of receptor-type tyrosine-protein phosphatase C, repeat 2; Receptor-type tyrosine-protein phosphatase C (PTPRC), also known as CD45, leukocyte common antigen (LCA) or GP180, belongs to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. PTPRC/CD45 is found in all nucleated hematopoietic cells and is an essential regulator of T- and B-cell antigen receptor signaling. It controls immune response, both positively and negatively, by dephosphorylating a number of signaling molecules such as the Src family kinases, the CD3zeta chain of TCY, and ZAP-70 kinase. Mutations in the human PTPRC/CD45 gene are associated with severe combined immunodeficiency (SCID) and multiple sclerosis. PTPRC/CD45 contains an extracellular receptor-like region with fibronectin type III (FN3) repeats, a short transmembrane segment, and a cytoplasmic region comprising of a membrane proximal catalytically active PTP domain (repeat 1 or D1) and a membrane distal catalytically impaired PTP-like domain (repeat 2, or D2). This model represents repeat 2.


Pssm-ID: 350406 [Multi-domain]  Cd Length: 203  Bit Score: 142.15  E-value: 4.24e-39
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25151513 367 YINANYVN-MEIPSSgivnrYIACQGPLAHTSSDFWVMVWEQHCTTIVMLTTITERGRVKCHQYWPRvfETQEYGRLMIK 445
Cdd:cd14558   1 YINASFIDgYWGPKS-----LIATQGPLPDTIADFWQMIFQKKVKVIVMLTELKEGDQEQCAQYWGD--EKKTYGDIEVE 73

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25151513 446 CIKDKQTTNCCYREFSIRDRNSSEERRVTQMQYIAWPDHGVPDDPKHFIQFVDEVRK------ARQGSVDPIVVHCSAGI 519
Cdd:cd14558  74 LKDTEKSPTYTVRVFEITHLKRKDSRTVYQYQYHKWKGEELPEKPKDLVDMIKSIKQklpyknSKHGRSVPIVVHCSDGS 153

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|.
gi 25151513 520 GRTGV----LILMETAaclvESNEPVYPLDIVRTMRDQRAMLIQTPGQYTF 566
Cdd:cd14558 154 SRTGIfcalWNLLESA----ETEKVVDVFQVVKALRKQRPGMVSTLEQYQF 200
COG5599 COG5599
Protein tyrosine phosphatase [Signal transduction mechanisms];
340-574 1.23e-38

Protein tyrosine phosphatase [Signal transduction mechanisms];


Pssm-ID: 444335 [Multi-domain]  Cd Length: 282  Bit Score: 143.31  E-value: 1.23e-38
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25151513 340 NLAKNRYRDVCPYDDTRVTlqasPSGDYINANYVnmeipSSGIVNRYIACQGPLAHTSSDFWVMVWEQHCTTIVMLTTIT 419
Cdd:COG5599  42 GSPLNRFRDIQPYKETALR----ANLGYLNANYI-----QVIGNHRYIATQYPLEEQLEDFFQMLFDNNTPVLVVLASDD 112

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25151513 420 E--RGRVKCHQYWPrvfETQEYGRLMIKcIKDKQTTNC----CYREFSIRDRNSSEE-RRVTQMQYIAWPDHGVPDDP-- 490
Cdd:COG5599 113 EisKPKVKMPVYFR---QDGEYGKYEVS-SELTESIQLrdgiEARTYVLTIKGTGQKkIEIPVLHVKNWPDHGAISAEal 188

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25151513 491 KHFIQFVDEVRKARQGSVDPIVVHCSAGIGRTGVLILM-------ETAACLVESNEPvypldIVRTMRDQRAM-LIQTPG 562
Cdd:COG5599 189 KNLADLIDKKEKIKDPDKLLPVVHCRAGVGRTGTLIAClalsksiNALVQITLSVEE-----IVIDMRTSRNGgMVQTSE 263

                       250
                ....*....|....*
gi 25151513 563 QYTF---VCESILRA 574
Cdd:COG5599 264 QLDVlvkLAEQQIRP 278
PHA02747 PHA02747
protein tyrosine phosphatase; Provisional
 340-567 3.02e-38

protein tyrosine phosphatase; Provisional


Pssm-ID: 165114 [Multi-domain]  Cd Length: 312  Bit Score: 143.22  E-value: 3.02e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25151513  340 NLAKNRYRDVCPYDDTRVTLQ--ASPSGDYINANYVN-MEIPssgivNRYIACQGPLAHTSSDFWVMVWEQHCTTIVMLT 416
Cdd:PHA02747  51 NQPKNRYWDIPCWDHNRVILDsgGGSTSDYIHANWIDgFEDD-----KKFIATQGPFAETCADFWKAVWQEHCSIIVMLT 125

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25151513  417 -TITERGRVKCHQYW-PRVFETQEYGRLMIKCIKDKQTTNCCYREFSIRDRNSSEERRVTQMQYIAWPDHGVPDDPKHFI 494
Cdd:PHA02747 126 pTKGTNGEEKCYQYWcLNEDGNIDMEDFRIETLKTSVRAKYILTLIEITDKILKDSRKISHFQCSEWFEDETPSDHPDFI 205

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25151513  495 QFVDEVRKARQGS----------VDPIVVHCSAGIGRTGVLILMETAACLVESNEPVYPLDIVRTMRDQRAMLIQTPGQY 564
Cdd:PHA02747 206 KFIKIIDINRKKSgklfnpkdalLCPIVVHCSDGVGKTGIFCAVDICLNQLVKRKAICLAKTAEKIREQRHAGIMNFDDY 285


                 ...
gi 25151513  565 TFV 567
Cdd:PHA02747 286 LFI 288
R-PTPc-typeIIb-2 cd14556
PTP domain of type IIb (or R2B) subfamily receptor-type tyrosine-protein phosphatases, repeat ...
 367-569 1.65e-33

PTP domain of type IIb (or R2B) subfamily receptor-type tyrosine-protein phosphatases, repeat 2; The type IIb (or R2B) subfamily of receptor protein tyrosine phosphatases (RPTPs) include the prototypical member PTPmu (or PTPRM), PCP-2 (or PTPRU), PTPrho (or PTPRT), and PTPkappa (or PTPRK). They belong to the larger family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. Type IIb RPTPs mediate cell-cell adhesion though homophilic interactions; their ligand is an identical molecule on an adjacent cell. No heterophilic interactions between the subfamily members have been observed. They also commonly function as tumor suppressors. They contain an extracellular region with an Meprin-A5 (neuropilin)-mu (MAM) domain, an immunoglobulin (Ig) domain, and four fibronectin type III (FN3) repeats, a transmembrane domain, and an intracellular segment with a juxtamembrane domain similar to the cytoplasmic domain of classical cadherins and two tandem PTP domains. This model represents the second (repeat 2) PTP domain.


Pssm-ID: 350404 [Multi-domain]  Cd Length: 201  Bit Score: 126.75  E-value: 1.65e-33
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25151513 367 YINANYVNmeipSSGIVNRYIACQGPLAHTSSDFWVMVWEQHCTTIVMLTTITERGRvKCHQYWPrVFETQEYGRLMIKC 446
Cdd:cd14556   1 YINAALLD----SYKQPAAFIVTQHPLPNTVTDFWRLVYDYGCTSIVMLNQLDPKDQ-SCPQYWP-DEGSGTYGPIQVEF 74

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25151513 447 IKDKQTTNCCYREFSIRD--RNSSEERRVTQMQYIAWPDHG-VPDDPKHFIQFVDEVRKARQGSVD-PIVVHCSAGIGRT 522
Cdd:cd14556  75 VSTTIDEDVISRIFRLQNttRPQEGYRMVQQFQFLGWPRDRdTPPSKRALLKLLSEVEKWQEQSGEgPIVVHCLNGVGRS 154

                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*..
gi 25151513 523 GVLILMETAACLVESNEPVYPLDIVRTMRDQRAMLIQTPGQYTFVCE 569
Cdd:cd14556 155 GVFCAISSVCERIKVENVVDVFQAVKTLRNHRPNMVETEEQYKFCYD 201
PTPc_motif smart00404
Protein tyrosine phosphatase, catalytic domain motif;
473-572 2.27e-32

Protein tyrosine phosphatase, catalytic domain motif;


Pssm-ID: 214649 [Multi-domain]  Cd Length: 105  Bit Score: 120.16  E-value: 2.27e-32
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25151513    473 VTQMQYIAWPDHGVPDDPKHFIQFVDEVRKARQGSVD--PIVVHCSAGIGRTGVLILMETAACLVESNEP-VYPLDIVRT 549
Cdd:smart00404   2 VKHYHYTGWPDHGVPESPDSILELLRAVKKNLNQSESsgPVVVHCSAGVGRTGTFVAIDILLQQLEAEAGeVDIFDTVKE 81

                           90       100
                   ....*....|....*....|...
gi 25151513    550 MRDQRAMLIQTPGQYTFVCESIL 572
Cdd:smart00404  82 LRSQRPGMVQTEEQYLFLYRALL 104
PTPc_DSPc smart00012
Protein tyrosine phosphatase, catalytic domain, undefined specificity; Protein tyrosine ...
 473-572 2.27e-32

Protein tyrosine phosphatase, catalytic domain, undefined specificity; Protein tyrosine phosphatases. Homologues detected by this profile and not by those of "PTPc" or "DSPc" are predicted to be protein phosphatases with a similar fold to DSPs and PTPs, yet with unpredicted specificities.


Pssm-ID: 214469 [Multi-domain]  Cd Length: 105  Bit Score: 120.16  E-value: 2.27e-32
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25151513    473 VTQMQYIAWPDHGVPDDPKHFIQFVDEVRKARQGSVD--PIVVHCSAGIGRTGVLILMETAACLVESNEP-VYPLDIVRT 549
Cdd:smart00012   2 VKHYHYTGWPDHGVPESPDSILELLRAVKKNLNQSESsgPVVVHCSAGVGRTGTFVAIDILLQQLEAEAGeVDIFDTVKE 81

                           90       100
                   ....*....|....*....|...
gi 25151513    550 MRDQRAMLIQTPGQYTFVCESIL 572
Cdd:smart00012  82 LRSQRPGMVQTEEQYLFLYRALL 104
R-PTPc-K-2 cd14636
PTP domain of receptor-type tyrosine-protein phosphatase K, repeat 2; Receptor-type ...
 367-566 5.67e-21

PTP domain of receptor-type tyrosine-protein phosphatase K, repeat 2; Receptor-type tyrosine-protein phosphatase K (PTPRK), also known as receptor-type tyrosine-protein phosphatase kappa (RPTP-kappa or PTPkappa), belongs to the type IIb subfamily of receptor protein tyrosine phosphatases (RPTPs), which belong to the larger family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. PTPRK is widely expressed and has been shown to stimulate cell motility and neurite outgrowth. It is required for anti-proliferative and pro-migratory effects of TGF-beta, suggesting a role in regulation, maintenance, and restoration of cell adhesion. It is a potential tumour suppressor in primary central nervous system lymphomas, colorectal cancer, and breast cancer. It contains an extracellular region with an Meprin-A5 (neuropilin)-mu (MAM) domain, an immunoglobulin (Ig) domain, and four fibronectin type III (FN3) repeats, a transmembrane domain, and an intracellular segment with a juxtamembrane domain similar to the cytoplasmic domain of classical cadherins and two tandem PTP domains. This model represents the second (repeat 2) PTP domain.


Pssm-ID: 350484 [Multi-domain]  Cd Length: 206  Bit Score: 91.24  E-value: 5.67e-21
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25151513 367 YINANYVN-MEIPSSgivnrYIACQGPLAHTSSDFWVMVWEQHCTTIVMLTTIT-ERGrvkCHQYWPRVfETQEYGRLMI 444
Cdd:cd14636   1 YINAALMDsYRQPAA-----FIVTQHPLPNTVKDFWRLVYDYGCTSIVMLNEVDlAQG---CPQYWPEE-GMLRYGPIQV 71

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25151513 445 KCIKDKQTTNCCYREFSIRDRNSSEE--RRVTQMQYIAWPDH-GVPDDPKHFIQFVDEVRKARQGSVD---PIVVHCSAG 518
Cdd:cd14636  72 ECMSCSMDCDVISRIFRICNLTRPQEgyLMVQQFQYLGWASHrEVPGSKRSFLKLILQVEKWQEECDEgegRTIIHCLNG 151

                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*...
gi 25151513 519 IGRTGVLILMETAACLVESNEPVYPLDIVRTMRDQRAMLIQTPGQYTF 566
Cdd:cd14636 152 GGRSGMFCAISIVCEMIKRQNVVDVFHAVKTLRNSKPNMVETPEQYRF 199
PDZ pfam00595
PDZ domain; PDZ domains are found in diverse signaling proteins.
 180-266 2.74e-20

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


Pssm-ID: 395476 [Multi-domain]  Cd Length: 81  Bit Score: 85.41  E-value: 2.74e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25151513   180 TIKMRPDRHGRFGFNVKGGADQ-NYPVIVSRVAPGSSAdKCQPrLNEGDQVLFIDGRDVSTMSHDHVVQFIRSArsglnG 258
Cdd:pfam00595   1 QVTLEKDGRGGLGFSLKGGSDQgDPGIFVSEVLPGGAA-EAGG-LKVGDRILSINGQDVENMTHEEAVLALKGS-----G 73


                  ....*...
gi 25151513   259 GELHLTIR 266
Cdd:pfam00595  74 GKVTLTIL 81
PDZ_canonical cd00136
canonical PDZ domain; Canonical PDZ (PSD-95 (Postsynaptic density protein 95), Dlg (Discs ...
 180-266 2.93e-20

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: 85.29  E-value: 2.93e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25151513 180 TIKMRPDRHGRFGFNVKGGADQNYPVIVSRVAPGSSADKCQpRLNEGDQVLFIDGRDVSTMSHDHVVQFIRSArsglnGG 259
Cdd:cd00136   1 TVTLEKDPGGGLGFSIRGGKDGGGGIFVSRVEPGGPAARDG-RLRVGDRILEVNGVSLEGLTHEEAVELLKSA-----GG 74


                ....*..
gi 25151513 260 ELHLTIR 266
Cdd:cd00136  75 EVTLTVR 81
R-PTPc-T-2 cd14634
PTP domain of receptor-type tyrosine-protein phosphatase T, repeat 2; Receptor-type ...
 367-572 9.20e-20

PTP domain of receptor-type tyrosine-protein phosphatase T, repeat 2; Receptor-type tyrosine-protein phosphatase T (PTPRT), also known as receptor-type tyrosine-protein phosphatase rho (RPTP-rho or PTPrho), belongs to the type IIb subfamily of receptor protein tyrosine phosphatases (RPTPs), which belong to the larger family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. PTPRT is highly expressed in the nervous system and it plays a critical role in regulation of synaptic formation and neuronal development. It dephosphorylates a specific tyrosine residue in syntaxin-binding protein 1, a key component of synaptic vesicle fusion machinery, and regulates its binding to syntaxin 1. PTPRT has been identified as a potential candidate gene for autism spectrum disorder (ASD) susceptibility. It contains an extracellular region with an Meprin-A5 (neuropilin)-mu (MAM) domain, an immunoglobulin (Ig) domain, and four fibronectin type III (FN3) repeats, a transmembrane domain, and an intracellular segment with a juxtamembrane domain similar to the cytoplasmic domain of classical cadherins and two tandem PTP domains. This model represents the second (repeat 2) PTP domain.


Pssm-ID: 350482 [Multi-domain]  Cd Length: 206  Bit Score: 87.77  E-value: 9.20e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25151513 367 YINANYVNM-EIPSSgivnrYIACQGPLAHTSSDFWVMVWEQHCTTIVMLTTITERGRvkCHQYWPRVfETQEYGRLMIK 445
Cdd:cd14634   1 YINAALMDShKQPAA-----FIVTQHPLPNTVADFWRLVFDYNCSSVVMLNEMDAAQL--CMQYWPEK-TSCCYGPIQVE 72

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25151513 446 CIKDKQTTNCCYREFSIRD--RNSSEERRVTQMQYIAWPDH-GVPDDPKHFIQFVDEVRKARQ---GSVDPIVVHCSAGI 519
Cdd:cd14634  73 FVSADIDEDIISRIFRICNmaRPQDGYRIVQHLQYIGWPAYrDTPPSKRSILKVVRRLEKWQEqydGREGRTVVHCLNGG 152

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|...
gi 25151513 520 GRTGVLILMETAACLVESNEPVYPLDIVRTMRDQRAMLIQTPGQYTFVCESIL 572
Cdd:cd14634 153 GRSGTFCAICSVCEMIQQQNIIDVFHTVKTLRNNKSNMVETLEQYKFVYEVAL 205
R-PTPc-U-2 cd14637
PTP domain of receptor-type tyrosine-protein phosphatase U, repeat 2; Receptor-type ...
 367-572 3.89e-19

PTP domain of receptor-type tyrosine-protein phosphatase U, repeat 2; Receptor-type tyrosine-protein phosphatase U (PTPRU), also known as pancreatic carcinoma phosphatase 2 (PCP-2), belongs to the type IIb subfamily of receptor protein tyrosine phosphatases (RPTPs), which belong to the larger family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. PTPRU/PCP-2 is the most distant member of the type IIb subfamily and may have a distinct biological function other than cell-cell aggregation. It localizes to the adherens junctions and directly binds and dephosphorylates beta-catenin, and regulates the balance between signaling and adhesive beta-catenin. It plays an important role in the maintenance of epithelial integrity. PTPRU contains an extracellular region with an Meprin-A5 (neuropilin)-mu (MAM) domain, an immunoglobulin (Ig) domain, and four fibronectin type III (FN3) repeats, a transmembrane domain, and an intracellular segment with a juxtamembrane domain similar to the cytoplasmic domain of classical cadherins and two tandem PTP domains. This model represents the second (repeat 2) PTP domain.


Pssm-ID: 350485 [Multi-domain]  Cd Length: 207  Bit Score: 86.12  E-value: 3.89e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25151513 367 YINANYVNMEIPSSGivnrYIACQGPLAHTSSDFWVMVWEQHCTTIVMLTTITERGRV-KCHQYWPRVfETQEYGRLMIK 445
Cdd:cd14637   1 YINAALTDSYTRSAA----FIVTLHPLQNTTTDFWRLVYDYGCTSVVMLNQLNQSNSAwPCLQYWPEP-GLQQYGPMEVE 75

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25151513 446 CIKDKQTTNCCYREFSIRD--RNSSEERRVTQMQYIAW-PDHGVPDDPKHFIQFVDEVRKARQGSVD-PIVVHCSAGIGR 521
Cdd:cd14637  76 FVSGSADEDIVTRLFRVQNitRLQEGHLMVRHFQFLRWsAYRDTPDSKKAFLHLLASVEKWQRESGEgRTVVHCLNGGGR 155

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|.
gi 25151513 522 TGVLILMETAACLVESNEPVYPLDIVRTMRDQRAMLIQTPGQYTFVCESIL 572
Cdd:cd14637 156 SGTYCASAMILEMIRCHNIVDVFYAVKTLRNYKPNMVETLEQYRFCYEIAL 206
R5-PTP-2 cd14550
PTP-like domain of R5 subfamily receptor-type tyrosine-protein phosphatases, repeat 2; The R5 ...
 367-518 9.41e-19

PTP-like domain of R5 subfamily receptor-type tyrosine-protein phosphatases, repeat 2; The R5 subfamily of receptor-type phosphotyrosine phosphatases (RPTP) is composed of receptor-type tyrosine-protein phosphatase Z (PTPRZ) and G (PTPRG). They belong to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. They are type 1 integral membrane proteins consisting of an extracellular region with a carbonic anhydrase-like (CAH) and a fibronectin type III (FN3) domains, and an intracellular region with a catalytic PTP domain (repeat 1) proximal to the membrane, and a catalytically inactive PTP-fold domain (repeat 2) distal to the membrane. This model represents the inactive PTP-like domain (repeat 2).


Pssm-ID: 350398 [Multi-domain]  Cd Length: 200  Bit Score: 84.68  E-value: 9.41e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25151513 367 YINANYVnMEIPSSgivNRYIACQGPLAHTSSDFWVMVWEQHCTTIVMLTTITERGrvKCHQYWPRVFETQEYG----RL 442
Cdd:cd14550   1 YINASYL-QGYRRS---NEFIITQHPLEHTIKDFWQMIWDHNSQTIVMLTDNELNE--DEPIYWPTKEKPLECEtfkvTL 74

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25151513 443 MIKCIK-DKQTTNCCYREFSIRDRNSSEERRVTQMQYIAWPDhgvPDDPKH-FIQFVDEVRKARQGSVDPIVVH-----C 515
Cdd:cd14550  75 SGEDHScLSNEIRLIVRDFILESTQDDYVLEVRQFQCPSWPN---PCSPIHtVFELINTVQEWAQQRDGPIVVHdryggV 151


                ...
gi 25151513 516 SAG 518
Cdd:cd14550 152 QAA 154
R-PTPc-M-2 cd14635
PTP domain of receptor-type tyrosine-protein phosphatase M, repeat 2; Receptor-type ...
 367-572 1.05e-18

PTP domain of receptor-type tyrosine-protein phosphatase M, repeat 2; Receptor-type tyrosine-protein phosphatase M (PTPRM), also known as protein-tyrosine phosphatase mu (R-PTP-mu or PTPmu), belongs to the type IIb subfamily of receptor protein tyrosine phosphatases (RPTPs), which belong to the larger family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. PTPRM/PTPmu is a homophilic cell adhesion molecule expressed in CNS neurons and glia. It is required for E-, N-, and R-cadherin-dependent neurite outgrowth. Loss of PTPmu contributes to tumor cell migration and dispersal of human glioblastomas. PTPRM contains an extracellular region with an Meprin-A5 (neuropilin)-mu (MAM) domain, an immunoglobulin (Ig) domain, and four fibronectin type III (FN3) repeats, a transmembrane domain, and an intracellular segment with a juxtamembrane domain similar to the cytoplasmic domain of classical cadherins and two tandem PTP domains. This model represents the second (repeat 2) PTP domain.


Pssm-ID: 350483 [Multi-domain]  Cd Length: 206  Bit Score: 84.74  E-value: 1.05e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25151513 367 YINANYVN-MEIPSSgivnrYIACQGPLAHTSSDFWVMVWEQHCTTIVMLTTITERGRvkCHQYWPRVfETQEYGRLMIK 445
Cdd:cd14635   1 YINAALMDsYKQPSA-----FIVTQHPLPNTVKDFWRLVLDYHCTSIVMLNDVDPAQL--CPQYWPEN-GVHRHGPIQVE 72

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25151513 446 CIKDKQTTNCCYREFSIRD--RNSSEERRVTQMQYIAWPDH-GVPDDPKHFIQFVDEVRKARQ---GSVDPIVVHCSAGI 519
Cdd:cd14635  73 FVSADLEEDIISRIFRIYNaaRPQDGYRMVQQFQFLGWPMYrDTPVSKRSFLKLIRQVDKWQEeynGGEGRTVVHCLNGG 152

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|...
gi 25151513 520 GRTGVLILMETAACLVESNEPVYPLDIVRTMRDQRAMLIQTPGQYTFVCESIL 572
Cdd:cd14635 153 GRSGTFCAISIVCEMLRHQRAVDVFHAVKTLRNNKPNMVDLLDQYKFCYEVAL 205
PDZ_ZASP52-like cd23068
PDZ domain of Drosophila melanogaster PDZ and LIM domain protein Zasp52 (also known as Zasp), ...
 184-266 1.81e-16

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: 74.49  E-value: 1.81e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25151513 184 RPDRHGRFGFNVKGGADQNYPVIVSRVAPGSSADKCqpRLNEGDQVLFIDGRDVSTMSHDHVVQFIRSArsglnGGELHL 263
Cdd:cd23068   6 RDDSNTPWGFRLQGGADFGQPLSIQKVNPGSPADKA--GLRRGDVILRINGTDTSNLTHKQAQDLIKRA-----GNDLQL 78


                ...
gi 25151513 264 TIR 266
Cdd:cd23068  79 TVQ 81
PDZ smart00228
Domain present in PSD-95, Dlg, and ZO-1/2; Also called DHR (Dlg homologous region) or GLGF ...
 188-268 3.33e-16

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: 73.95  E-value: 3.33e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25151513    188 HGRFGFNVKGGADQNYPVIVSRVAPGSSADKCQprLNEGDQVLFIDGRDVSTMSHDHVVQFIRSArsglnGGELHLTIRP 267
Cdd:smart00228  11 GGGLGFSLVGGKDEGGGVVVSSVVPGSPAAKAG--LRVGDVILEVNGTSVEGLTHLEAVDLLKKA-----GGKVTLTVLR 83


                   .
gi 25151513    268 N 268
Cdd:smart00228  84 G 84
PDZ_syntrophin-like cd06801
PDZ domain of syntrophins, and related domains; PDZ (PSD-95 (Postsynaptic density protein 95), ...
 180-266 1.86e-14

PDZ domain of syntrophins, and related domains; PDZ (PSD-95 (Postsynaptic density protein 95), Dlg (Discs large protein), and ZO-1 (Zonula occludens-1)) domain of syntrophins (including alpha-1-syntrophin, beta-1-syntrophin, beta-2-syntrophin, gamma-1-syntrophin, and gamma-2-syntrophin), and related domains. Syntrophins play a role in recruiting various signaling molecules into signaling complexes and help provide appropriate spatiotemporal regulation of signaling pathways. They function in cytoskeletal organization and maintenance; as components of the dystrophin-glycoprotein complex (DGC), they help maintain structural integrity of skeletal muscle fibers. They link voltage-gated sodium channels to the actin cytoskeleton and the extracellular matrix, and control the localization and activity of the actin reorganizing proteins such as PI3K, PI(3,4)P2 and TAPP1. Through association with various cytoskeletal proteins within the cells, they are involved in processes such as regulation of focal adhesions, myogenesis, calcium homeostasis, and cell migration. They also have roles in synapse formation and in the organization of utrophin, acetylcholine receptor, and acetylcholinesterase at the neuromuscular synapse. 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 syntrophin-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: 467262 [Multi-domain]  Cd Length: 83  Bit Score: 68.75  E-value: 1.86e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25151513 180 TIKMRPDRHGRFGFNVKGGADQNYPVIVSRVAPGSSADKCQpRLNEGDQVLFIDGRDVSTMSHDHVVQFIRSArsglnGG 259
Cdd:cd06801   2 TVRVVKQDVGGLGISIKGGAEHKMPILISKIFKGQAADQTG-QLFVGDAILSVNGENLEDATHDEAVQALKNA-----GD 75


                ....*..
gi 25151513 260 ELHLTIR 266
Cdd:cd06801  76 EVTLTVK 82
PTP_YopH-like cd14559
YopH and related bacterial protein tyrosine phosphatases; Yersinia outer protein H (YopH) ...
 344-564 3.05e-14

YopH and related bacterial protein tyrosine phosphatases; Yersinia outer protein H (YopH) belongs to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. YopH is an essential virulence determinant of the pathogenic bacterium by dephosphorylating several focal adhesion proteins including p130Cas in human epithelial cells, resulting in the disruption of focal adhesions and cell detachment from the extracellular matrix. It contains an N-terminal domain that contains signals required for TTSS-mediated delivery of YopH into host cells and a C-terminal catalytic PTP domain.


Pssm-ID: 350407 [Multi-domain]  Cd Length: 227  Bit Score: 72.43  E-value: 3.05e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25151513 344 NRYRDVCpyddTRVTLqasPSGDYINANYVNMeipssGIVNRYIACQGPLAHTSSDFWVMVWEQHCTTIVMLTTITERGR 423
Cdd:cd14559   1 NRFTNIQ----TRVST---PVGKNLNANRVQI-----GNKNVAIACQYPKNEQLEDHLKMLADNRTPCLVVLASNKDIQR 68

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25151513 424 VKCHQYWPRvfeTQEYGR-----LMIKCIKDKQTTNCCYREFSIRDRNSSEERRVtqMQYIAWPDHGvPDDPKHFIQFVD 498
Cdd:cd14559  69 KGLPPYFRQ---SGTYGSvtvksKKTGKDELVDGLKADMYNLKITDGNKTITIPV--VHVTNWPDHT-AISSEGLKELAD 142

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25151513 499 EVRKARQGSVDPI----------------VVHCSAGIGRTGVLIlmeTAACLVESNEPVYPLDIVRTMRDQR-AMLIQTP 561
Cdd:cd14559 143 LVNKSAEEKRNFYkskgssaindknkllpVIHCRAGVGRTGQLA---AAMELNKSPNNLSVEDIVSDMRTSRnGKMVQKD 219


                ...
gi 25151513 562 GQY 564
Cdd:cd14559 220 EQL 222
PDZ_PDLIM-like cd06753
PDZ domain of PDZ-LIM family proteins, and related domains; PDZ (PSD-95 (Postsynaptic density ...
 191-266 3.69e-14

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: 67.55  E-value: 3.69e-14
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 25151513 191 FGFNVKGGADQNYPVIVSRVAPGSSADKCQprLNEGDQVLFIDGRDVSTMSHDHVVQFIRSArsglnGGELHLTIR 266
Cdd:cd06753  10 WGFRLQGGKDFNQPLTISRVTPGGKAAQAN--LRPGDVILAINGESTEGMTHLEAQNKIKAA-----TGSLSLTLE 78
PDZ_PDZD11-like cd06752
PDZ domain of PDZ domain-containing protein 11, and related domains; PDZ (PSD-95 (Postsynaptic ...
 180-266 5.95e-14

PDZ domain of PDZ domain-containing protein 11, and related domains; PDZ (PSD-95 (Postsynaptic density protein 95), Dlg (Discs large protein), and ZO-1 (Zonula occludens-1)) domain of PDZD11, and related domains. PDZD11 (also known as ATPase-interacting PDZ protein, plasma membrane calcium ATPase-interacting single-PDZ protein, PMCA-interacting single-PDZ protein, PISP) is involved in the dynamic assembly of apical junctions (AJs). It is recruited by PLEKHA7 to AJs to promote the efficient junctional recruitment and stabilization of nectins, and the efficient early phases of assembly of AJs in epithelial cells. The PDZD11 PDZ domain binds nectin-1 and nectin-3. PDZD11 also binds to a PDZ binding motif located in the C-terminal tail of the human sodium-dependent multivitamin transporter, to the cytoplasmic tail of the Menkes copper ATPase ATP7A, and to the cytoplasmic tail of all plasma membrane Ca2+-ATPase b-splice variants. 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 PDZD11-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: 467234 [Multi-domain]  Cd Length: 83  Bit Score: 67.34  E-value: 5.95e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25151513 180 TIKMRPDRHGRFGFNVKGGADQNYPVIVSRVAPGSSADKCQprLNEGDQVLFIDGRDVSTMSHDHVVQFIRSARsglngg 259
Cdd:cd06752   2 TVVLKRPPGEQLGFNIRGGKASGLGIFISKVIPDSDAHRLG--LKEGDQILSVNGVDFEDIEHSEAVKVLKTAR------ 73


                ....*..
gi 25151513 260 ELHLTIR 266
Cdd:cd06752  74 EIQMRVR 80
PDZ_Lin-7-like cd06796
PDZ domain of protein Lin-7 and related domains; PDZ (PSD-95 (Postsynaptic density protein 95), ...
 191-266 6.98e-13

PDZ domain of protein Lin-7 and related domains; PDZ (PSD-95 (Postsynaptic density protein 95), Dlg (Discs large protein), and ZO-1 (Zonula occludens-1)) domain of Lin-7 (also known as LIN-7 or LIN7), and related domains. Lin-7 targets and organize protein complexes to epithelial and synaptic plasma membranes. There are three mammalian Lin-7 homologs: Lin-7A (protein lin-7 homolog A, also known as mammalian lin-seven protein 1 (MALS-1), vertebrate lin-7 homolog 1 (Veli-1), tax interaction protein 33); Lin-7B (also known as MALS-2, Veli-2); and Lin-7C (also known as MALS-3, Veli-3). Lin-7 is involved in localization of the Let-23 growth factor receptor to the basolateral membrane of epithelial cells, in tight junction localization of insulin receptor substrate p53 (IRSp53), in retaining gamma-aminobutyric (GABA) transporter (BGT-1) at the basolateral surface of epithelial cells, and in regulating recruitment of neurotransmitter receptors to the postsynaptic density (PSD). The Lin7 PDZ domain binds Let-23, BGT and beta-catenin, and NMDA (N-methyl-D-aspartate) receptor NR2B. Lin-7 also binds to the PDZ binding motif located in the C-terminal tail of Rhotekin, an effector protein for small GTPase Rho. 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 Lin-7-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: 467258 [Multi-domain]  Cd Length: 86  Bit Score: 64.38  E-value: 6.98e-13
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 25151513 191 FGFNVKGGADQNYPVIVSRVAPGSSADKcQPRLNEGDQVLFIDGRDVSTMSHDHVVQFIRSARsglngGELHLTIR 266
Cdd:cd06796  14 LGFNVMGGKEQNSPIYISRIIPGGVADR-HGGLKRGDQLLSVNGVSVEGEHHEKAVELLKAAQ-----GSVKLVVR 83
CDC14 COG2453
Protein-tyrosine phosphatase [Signal transduction mechanisms];
478-569 1.34e-12

Protein-tyrosine phosphatase [Signal transduction mechanisms];


Pssm-ID: 441989 [Multi-domain]  Cd Length: 140  Bit Score: 65.38  E-value: 1.34e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25151513 478 YIAWPDHGVPDDpKHFIQFVDEVRKARQGSvDPIVVHCSAGIGRTGVLIlmetAACLVESNEPvyPLDIVRTMRDQRAML 557
Cdd:COG2453  52 HLPIPDFGAPDD-EQLQEAVDFIDEALREG-KKVLVHCRGGIGRTGTVA----AAYLVLLGLS--AEEALARVRAARPGA 123

                        90
                ....*....|..
gi 25151513 558 IQTPGQYTFVCE 569
Cdd:COG2453 124 VETPAQRAFLER 135
R-PTP-G-2 cd17670
PTP-like domain of receptor-type tyrosine-protein phosphatase G, repeat 2; Receptor-type ...
 367-572 2.54e-12

PTP-like domain of receptor-type tyrosine-protein phosphatase G, repeat 2; Receptor-type tyrosine-protein phosphatase G (PTPRG), also called protein-tyrosine phosphatase gamma (R-PTP-gamma), belongs to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. PTPRG is an important tumor suppressor gene in multiple human cancers such as lung, ovarian, and breast cancers. It is widely expressed in many tissues, including the central nervous system, where it plays a role during neuroinflammation processes. It can dephosphorylate platelet-derived growth factor receptor beta (PDGFRB) and may play a role in PDGFRB-related infantile myofibromatosis. PTPRG is a type 1 integral membrane protein consisting of an extracellular region with a carbonic anhydrase-like (CAH) and a fibronectin type III (FN3) domains, and an intracellular region with a catalytic PTP domain (repeat 1) proximal to the membrane, and a catalytically inactive PTP-fold domain (repeat 2) distal to the membrane. This model represents the inactive PTP-like domain (repeat 2).


Pssm-ID: 350508 [Multi-domain]  Cd Length: 205  Bit Score: 66.24  E-value: 2.54e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25151513 367 YINANYVNMEIPSsgivNRYIACQGPLAHTSSDFWVMVWEQHCTTIVML---TTITERGRVkchqYWPRVFETQEYGRLM 443
Cdd:cd17670   1 YINASYIMGYYRS----NEFIITQHPLPHTTKDFWRMIWDHNAQIIVMLpdnQGLAEDEFV----YWPSREESMNCEAFT 72

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25151513 444 IKCIKDKQTTNCCYREFSIRD--RNSSEERRVTQMQYIAWPDHGVPDDPK----HFIQFVDEVRKARQGsvdPIVVHCSA 517
Cdd:cd17670  73 VTLISKDRLCLSNEEQIIIHDfiLEATQDDYVLEVRHFQCPKWPNPDAPIsstfELINVIKEEALTRDG---PTIVHDEF 149

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*
gi 25151513 518 GIGRTGVLILMETAACLVESNEPVYPLDIVRTMRDQRAMLIQTPGQYTFVCESIL 572
Cdd:cd17670 150 GAVSAGTLCALTTLSQQLENENAVDVYQVAKMINLMRPGVFTDIEQYQFLYKAML 204
R-PTP-Z-2 cd17669
catalytic domain of receptor-type tyrosine-protein phosphatase Z, repeat 2; Receptor-type ...
 367-572 3.52e-12

catalytic domain of receptor-type tyrosine-protein phosphatase Z, repeat 2; Receptor-type tyrosine-protein phosphatase Z (PTPRZ), also called receptor-type tyrosine-protein phosphatase zeta (R-PTP-zeta), belongs to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. Three isoforms are generated by alternative splicing from a single PTPRZ gene: two transmembrane isoforms, PTPRZ-A and PTPRZ-B, and one secretory isoform, PTPRZ-S (also known as phosphacan); all are preferentially expressed in the central nervous system (CNS) as chondroitin sulfate (CS) proteoglycans. PTPRZ isoforms play important roles in maintaining oligodendrocyte precursor cells in an undifferentiated state. PTPRZ is a type 1 integral membrane protein consisting of an extracellular region with a carbonic anhydrase-like (CAH) and a fibronectin type III (FN3) domains, and an intracellular region with a catalytic PTP domain (repeat 1) proximal to the membrane, and a catalytically inactive PTP-fold domain (repeat 2) distal to the membrane. This model represents the inactive PTP-like domain (repeat 2).


Pssm-ID: 350507 [Multi-domain]  Cd Length: 204  Bit Score: 65.79  E-value: 3.52e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25151513 367 YINANYVNMEIPSsgivNRYIACQGPLAHTSSDFWVMVWEQHCTTIVMLTTITERGRVKChQYWPRVFE---TQEYGRLM 443
Cdd:cd17669   1 YINASYIMGYYQS----NEFIITQHPLLHTIKDFWRMIWDHNAQLIVMLPDGQNMAEDEF-VYWPNKDEpinCETFKVTL 75

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25151513 444 I----KCIKDKQttNCCYREFSIRDRNSSEERRVTQMQYIAWPDhgvPDDP--KHF--IQFVDEVRKARQGsvdPIVVHC 515
Cdd:cd17669  76 IaeehKCLSNEE--KLIIQDFILEATQDDYVLEVRHFQCPKWPN---PDSPisKTFelISIIKEEAANRDG---PMIVHD 147

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*..
gi 25151513 516 SAGIGRTGVLILMETAACLVESNEPVYPLDIVRTMRDQRAMLIQTPGQYTFVCESIL 572
Cdd:cd17669 148 EHGGVTAGTFCALTTLMHQLEKENSVDVYQVAKMINLMRPGVFTDIEQYQFLYKAIL 204
PDZ3_MAGI-1_3-like cd06733
PDZ domain 3 of membrane-associated guanylate kinase inverted 1 (MAGI-1), MAGI-2, and MAGI-3, ...
 191-266 6.46e-12

PDZ domain 3 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 3 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 PDZ3 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: 467215 [Multi-domain]  Cd Length: 85  Bit Score: 61.47  E-value: 6.46e-12
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 25151513 191 FGFNVKGGADQNYPVIVSRVAPGSSADKCQpRLNEGDQVLFIDGRDVSTMSHDHVVQFIRSArsGLNgGELHLTIR 266
Cdd:cd06733  13 FGFRILGGTEEGSQVSIGAIVPGGAADLDG-RLRTGDELLSVDGVNVVGASHHKVVDLMGNA--ARN-GQVNLTVR 84
CDKN3-like cd14505
cyclin-dependent kinase inhibitor 3 and similar proteins; This family is composed of ...
 482-567 2.72e-11

cyclin-dependent kinase inhibitor 3 and similar proteins; This family is composed of eukaryotic cyclin-dependent kinase inhibitor 3 (CDKN3) and related archaeal and bacterial proteins. CDKN3 is also known as kinase-associated phosphatase (KAP), CDK2-associated dual-specificity phosphatase, cyclin-dependent kinase interactor 1 (CDI1), or cyclin-dependent kinase-interacting protein 2 (CIP2). It has been characterized as dual-specificity phosphatase, which function as a protein-serine/threonine phosphatase (EC 3.1.3.16) and protein-tyrosine-phosphatase (EC 3.1.3.48). It dephosphorylates CDK2 at a threonine residue in a cyclin-dependent manner, resulting in the inhibition of G1/S cell cycle progression. It also interacts with CDK1 and controls progression through mitosis by dephosphorylating CDC2. CDKN3 may also function as a tumor suppressor; its loss of function was found in a variety of cancers including glioblastoma and hepatocellular carcinoma. However, it has also been found over-expressed in many cancers such as breast, cervical, lung and prostate cancers, and may also have an oncogenic function.


Pssm-ID: 350355 [Multi-domain]  Cd Length: 163  Bit Score: 62.28  E-value: 2.72e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25151513 482 PDHGVPDDPKHFIQFVDEVRKA-RQGsvDPIVVHCSAGIGRTGVLilmetAACLV----ESNEPVYPLDIVRTMRDqRAm 556
Cdd:cd14505  81 PDGGVPSDIAQWQELLEELLSAlENG--KKVLIHCKGGLGRTGLI-----AACLLlelgDTLDPEQAIAAVRALRP-GA- 151

                        90
                ....*....|.
gi 25151513 557 lIQTPGQYTFV 567
Cdd:cd14505 152 -IQTPKQENFL 161
PDZ4_MAGI-1_3-like cd06734
PDZ domain 4 of membrane-associated guanylate kinase inverted 1 (MAGI-1), MAGI-2, and MAGI-3, ...
 179-267 8.67e-11

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: 58.39  E-value: 8.67e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25151513 179 VTIKmRPDRHGrFGFNVKGGADQNYPVIVSRVAPGSSADKCQpRLNEGDQVLFIDGRDVSTMSHDHVVQFIRSArsglnG 258
Cdd:cd06734   4 VTLT-RRENEG-FGFVIISSVNKKSGSKIGRIIPGSPADRCG-QLKVGDRILAVNGISILNLSHGDIVNLIKDS-----G 75


                ....*....
gi 25151513 259 GELHLTIRP 267
Cdd:cd06734  76 LSVTLTIVP 84
PDZ_SYNJ2BP-like cd06709
PDZ domain of synaptojanin-2-binding protein (SYNJ2BP), and related domains; PDZ (PSD-95 ...
 191-266 1.13e-10

PDZ domain of synaptojanin-2-binding protein (SYNJ2BP), and related domains; PDZ (PSD-95 (Postsynaptic density protein 95), Dlg (Discs large protein), and ZO-1 (Zonula occludens-1)) domain of SYNJ2BP, and related domains. SYNJ2BP (also known as mitochondrial outer membrane protein 25, OMP25) regulates endocytosis of activin type 2 receptor kinases through the Ral/RALBP1-dependent pathway and may be involved in suppression of activin-induced signal transduction. Binding partners of the SYNJ2BP PDZ domain include activin type II receptors (ActR-II), and SYNJ2. SYNJ2BP interacts with the PDZ binding motif of the Notch Delta-like ligand 1 (DLL1) and DLL4, promoting Delta-Notch signaling, and inhibiting sprouting angiogenesis. 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 SYNJ2BP-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: 467193 [Multi-domain]  Cd Length: 86  Bit Score: 58.07  E-value: 1.13e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25151513 191 FGFNVKGGADQNY-----PVIVSRVAPGSSADKcQPRLNEGDQVLFIDGRDVSTMSHDHVVQFIRSArsglnGGELHLTI 265
Cdd:cd06709  12 LGFNIVGGTDQPYipndsGIYVAKIKEDGAAAI-DGRLQEGDKILEINGQSLENLTHQDAVELFRNA-----GEDVKLKV 85


                .
gi 25151513 266 R 266
Cdd:cd06709  86 Q 86
PHA02740 PHA02740
protein tyrosine phosphatase; Provisional
 385-575 3.67e-10

protein tyrosine phosphatase; Provisional


Pssm-ID: 165107 [Multi-domain]  Cd Length: 298  Bit Score: 61.52  E-value: 3.67e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25151513  385 RYIACQGPLAHTSSDFWVMVWEQHCTTIVMLTTITERgrvKCH-QYWPRVFET-QEYGRLMIKCIKDKQTTNCCYREFSI 462
Cdd:PHA02740  92 KFICIINLCEDACDKFLQALSDNKVQIIVLISRHADK---KCFnQFWSLKEGCvITSDKFQIETLEIIIKPHFNLTLLSL 168

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25151513  463 RDRnSSEERRVTQMQYIAWPDHGVPDDPKHFIQF---VDEV-----RKARQGSVDPIVVHCSAGIGRTGVLILMETAACL 534
Cdd:PHA02740 169 TDK-FGQAQKISHFQYTAWPADGFSHDPDAFIDFfcnIDDLcadleKHKADGKIAPIIIDCIDGISSSAVFCVFDICATE 247

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|.
gi 25151513  535 VESNEPVYPLDIVRTMRDQRAMLIQTPGQYTFvCESILRAY 575
Cdd:PHA02740 248 FDKTGMLSIANALKKVRQKKYGCMNCLDDYVF-CYHLIAAY 287
PDZ_rhophilin-like cd06712
PDZ domain of rhophilin-1, rhophilin-2, and related domains; PDZ (PSD-95 (Postsynaptic density ...
 180-263 6.67e-10

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: 55.67  E-value: 6.67e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25151513 180 TIKMRPdRHGRFGFNVKGGAdqnyPVIVSRVAPGSSADKCQprLNEGDQVLFIDGRDVSTMSHDHVVQFIRSArsGLNGG 259
Cdd:cd06712   3 TVHLTK-EEGGFGFTLRGDS----PVQVASVDPGSCAAEAG--LKEGDYIVSVGGVDCKWSKHSEVVKLLKSA--GEEGL 73


                ....
gi 25151513 260 ELHL 263
Cdd:cd06712  74 ELQV 77
PDZ2_L-delphilin-like cd06744
PDZ domain 2 of delphilin (L-delphilin isoform), and related domains; PDZ (PSD-95 ...
 188-254 7.10e-10

PDZ domain 2 of delphilin (L-delphilin isoform), and related domains; PDZ (PSD-95 (Postsynaptic density protein 95), Dlg (Discs large protein), and ZO-1 (Zonula occludens-1)) domain 2 of delphilin (also known as glutamate receptor, ionotropic, delta 2-interacting protein 1, L-delphilin). Delphilin, a postsynaptic protein which it is selectively expressed at cerebellar Purkinje cells, links the glutamate receptor delta 2 subunit (GluRdelta2) with the actin cytoskeleton and various signaling molecules. Two alternatively spliced isoforms of delphilin have been characterized: L-delphilin has two PDZ domains, PDZ1 and PDZ2, and S-delphilin has a single PDZ domain (PDZ2). These two isoforms are differently palmitoylated and may be involved in controlling GluRdelta2 signaling in Purkinje cells. PDZ domains usually bind in a sequence-specific manner to short peptide sequences located at the C-terminal end of their partner proteins (known as PDZ binding motifs). The PDZ superfamily includes canonical PDZ domains as well as those with circular permutations and domain swapping mediated by beta-strands. This delphilin-like family 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: 467226 [Multi-domain]  Cd Length: 75  Bit Score: 55.36  E-value: 7.10e-10
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 25151513 188 HGRFGFNVKGgadqNYPVIVSRVAPGSSADKCQprLNEGDQVLFIDGRDVSTMSHDHVVQFIRSARS 254
Cdd:cd06744   8 NGSFGFTLRG----HAPVYIESVDPGSAAERAG--LKPGDRILFLNGLDVRNCSHDKVVSLLQGSGS 68
PTP_DSP_cys cd14494
cys-based protein tyrosine phosphatase and dual-specificity phosphatase superfamily; This ...
 384-569 1.01e-09

cys-based protein tyrosine phosphatase and dual-specificity phosphatase superfamily; This superfamily is composed of cys-based phosphatases, which includes classical protein tyrosine phosphatases (PTPs) as well as dual-specificity phosphatases (DUSPs or DSPs). They are characterized by a CxxxxxR conserved catalytic loop (where C is the catalytic cysteine, x is any amino acid, and R is an arginine). PTPs are part of the tyrosine phosphorylation/dephosphorylation regulatory mechanism, and are important in the response of the cells to physiologic and pathologic changes in their environment. DUSPs show more substrate diversity (including RNA and lipids) and include pTyr, pSer, and pThr phosphatases.


Pssm-ID: 350344 [Multi-domain]  Cd Length: 113  Bit Score: 56.20  E-value: 1.01e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25151513 384 NRYIACQGPLAHtSSDFWVMVWEQHCTTIVMLTtitergrvkchqywprvfetqeygrlmikcikdkqttnccyrefsir 463
Cdd:cd14494   7 LRLIAGALPLSP-LEADSRFLKQLGVTTIVDLT----------------------------------------------- 38

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25151513 464 drnsseerrvtqmqyiawpdhgvPDDPKHFIQFVDEVRKARQgsvdPIVVHCSAGIGRTGVLIlmeTAACLVESNEPVYp 543
Cdd:cd14494  39 -----------------------LAMVDRFLEVLDQAEKPGE----PVLVHCKAGVGRTGTLV---ACYLVLLGGMSAE- 87

                       170       180
                ....*....|....*....|....*..
gi 25151513 544 lDIVRTMRDQR-AMLIQTPGQYTFVCE 569
Cdd:cd14494  88 -EAVRIVRLIRpGGIPQTIEQLDFLIK 113
PDZ_SYNPO2-like cd10820
PDZ domain of synaptopodin 2 (SYNPO2), synaptopodin 2-like protein (SYNPO2L), and related ...
 191-265 1.02e-09

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: 55.01  E-value: 1.02e-09
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 25151513 191 FGFNVKGGADQNYPVIVSRVAPGSSAdkCQPRLNEGDQVLFIDGRDVSTMSHDHVVQFIRSArsglnGGELHLTI 265
Cdd:cd10820  10 WGFRLQGGSEQKKPLQVAKIRKKSKA--ALAGLCEGDELLSINGKPCADLSHSEAMDLIDSS-----GDTLQLLI 77
PDZ5_MAGI-1_3-like cd06735
PDZ domain 5 of membrane-associated guanylate kinase inverted 1 (MAGI-1), MAGI-2, and MAGI-3, ...
 191-267 1.18e-09

PDZ domain 5 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 5 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, and belongs to this MAGI1,2,3-like family. 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 PDZ5 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: 467217 [Multi-domain]  Cd Length: 84  Bit Score: 55.28  E-value: 1.18e-09
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 25151513 191 FGFNVKGGAD-QNYPVIVSRVAPGSSADKCQpRLNEGDQVLFIDGRDVSTMSHDHVVQFIRsarsglNGGE-LHLTIRP 267
Cdd:cd06735  13 FGFSIRGGREyNNMPLYVLRLAEDGPAQRDG-RLRVGDQILEINGESTQGMTHAQAIELIR------SGGSvVRLLLRR 84
PTP_PTPDC1 cd14506
protein tyrosine phosphatase domain of PTP domain-containing protein 1; protein tyrosine ...
 480-569 4.47e-09

protein tyrosine phosphatase domain of PTP domain-containing protein 1; protein tyrosine phosphatase domain-containing protein 1 (PTPDC1) is an uncharacterized non-receptor class protein-tyrosine phosphatase (PTP). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. Small interfering RNA (siRNA) knockdown of the ptpdc1 gene is associated with elongated cilia.


Pssm-ID: 350356 [Multi-domain]  Cd Length: 206  Bit Score: 56.59  E-value: 4.47e-09
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gi 25151513 480 AWPDHGVP------DDPKHFIQFVDEVRKarqgsvdpIVVHCSAGIGRTGVLIlmetAACLVESNEpVYPLDIVRTMRDQ 553
Cdd:cd14506  83 GWKDYGVPslttilDIVKVMAFALQEGGK--------VAVHCHAGLGRTGVLI----ACYLVYALR-MSADQAIRLVRSK 149

                        90
                ....*....|....*.
gi 25151513 554 RAMLIQTPGQYTFVCE 569
Cdd:cd14506 150 RPNSIQTRGQVLCVRE 165
PDZ_RGS12-like cd06710
PDZ domain of regulator of G-protein signaling 12 (RGS12), and related domains; PDZ (PSD-95 ...
 180-265 4.58e-09

PDZ domain of regulator of G-protein signaling 12 (RGS12), and related domains; PDZ (PSD-95 (Postsynaptic density protein 95), Dlg (Discs large protein), and ZO-1 (Zonula occludens-1)) domain of RGS12, and related domains. RGS12 downregulates GPCR signal transduction by increasing the GTPase activity of G-protein alpha subunits, thereby driving G-proteins into their inactive GDP-bound form. The RGS12 PDZ domain can bind selectively to C-terminal (A/S)-T-X-(L/V) motifs as found within both the CXCR2 IL-8 receptor, and the alternative 3' exon form of RGS12. 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 RGS12-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: 467194 [Multi-domain]  Cd Length: 76  Bit Score: 53.02  E-value: 4.58e-09
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                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25151513 180 TIKMRPDRHGrFGFNVKGGAdqnyPVIVSRVAPGSSADKCQprLNEGDQVLFIDGRDVSTMSHDHVVQFIrsarsGLNGG 259
Cdd:cd06710   2 TVEIARGRAG-YGFTISGQA----PCVLSCVVRGSPADVAG--LKAGDQILAVNGINVSKASHEDVVKLI-----GKCTG 69


                ....*.
gi 25151513 260 ELHLTI 265
Cdd:cd06710  70 VLRLVI 75
PDZ_FRMPD1_3_4-like cd06769
PDZ domain of FERM and PDZ domain-containing protein 1 (FRMPD1), FRMPD3, FRMPD4, and related ...
 180-257 7.95e-09

PDZ domain of FERM and PDZ domain-containing protein 1 (FRMPD1), FRMPD3, FRMPD4, and related domains; PDZ (PSD-95 (Postsynaptic density protein 95), Dlg (Discs large protein), and ZO-1 (Zonula occludens-1)) domain of FRMPD1, FRMPD3, FRMPD4, and related domains. FRMPD1 (also known as FERM domain-containing protein 2, FRMD2), inhibits the malignant phenotype of lung cancer by activating the Hippo pathway via interaction with WWC3; the FRMPD1 PDZ domain binds WWC3. FRMPD3 is a target gene of the neuron-specific transcription factor NPAS4 that is involved in synaptic plasticity. FRMPD4 (also known as PDZ domain-containing protein 10, PDZD10, PDZK10, PSD-95-interacting regulator of spine morphogenesis, and Preso) regulates dendritic spine morphogenesis, and mGluR1/5 signaling; the FRMPD4 PDZ domain binds PAK-interacting exchange factor-beta (betaPix). 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 FRMPD1,3,4-like family domain is a canonical PDZ domain containing six beta-strands A-F and two alpha-helices (alpha-helix 1 and 2), arranged in the order: beta-strands A, B, C, alpha-helix 1, beta-strands D, E, alpha-helix 2 and beta-strand F.


Pssm-ID: 467250 [Multi-domain]  Cd Length: 75  Bit Score: 52.63  E-value: 7.95e-09
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gi 25151513 180 TIKMRPDRHGRFGFNvkggADQNYPVIVSRVAPGSSAD-KCQPrlneGDQVLFIDGRDVSTMSHDHVVQFIRSARSGLN 257
Cdd:cd06769   1 TVEIQRDAVLGFGFV----AGSERPVVVRSVTPGGPSEgKLLP----GDQILKINNEPVEDLPRERVIDLIRECKDSIV 71
PDZ_TAX1BP3-like cd10822
PDZ domain of tax1-binding protein 3 (TAX1BP3), and related domains; PDZ (PSD-95 (Postsynaptic ...
 190-257 1.63e-08

PDZ domain of tax1-binding protein 3 (TAX1BP3), and related domains; PDZ (PSD-95 (Postsynaptic density protein 95), Dlg (Discs large protein), and ZO-1 (Zonula occludens-1)) domain of TAX1BP3, and related domains. TAX1BP3 (also known as glutaminase-interacting protein 3, tax interaction protein 1, TIP-1, tax-interacting protein 1) may regulate a number of protein-protein interactions by competing for PDZ domain binding sites. TAX1BP3 binds beta-catenin and may act as an inhibitor of the Wnt signaling pathway. It competes with LIN7A (also known as Lin-7A or LIN-7A) for inward rectifier potassium channel 4 (KCNJ4) binding, and thereby promotes KCNJ4 internalization. It may play a role in the Rho signaling pathway, and in the activation of CDC42 by the viral protein HPV16 E6. Binding partners of the TAX1BP3 PDZ domain include beta-catenin, KCNJ4, glutaminase liver isoform (GLS2), rho guanine nucleotide exchange factor 16 (ARHGEF16), rhotekin, and CDK5 regulatory subunit-associated protein 3 (also known as LAPZ). 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 TAX1BP3-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: 467265 [Multi-domain]  Cd Length: 94  Bit Score: 52.34  E-value: 1.63e-08
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gi 25151513 190 RFGFNVKGGADQ-------NYP---VIVSRVAPGSSADKCQPRLneGDQVLFIDGRDVSTMSHDHVVQFIRSARSGLN 257
Cdd:cd10822  14 ILGFSIGGGIDQdpsknpfSYTdkgIYVTRVSEGGPAEKAGLQV--GDKILQVNGWDMTMVTHKQAVKRLTKKKPVLR 89
PDZ_SHANK1_3-like cd06746
PDZ domain of SH3 and multiple ankyrin repeat domains protein 1 (SHANK1), SHANK2, SHANK3, and ...
 191-265 1.73e-08

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


Pssm-ID: 467228 [Multi-domain]  Cd Length: 101  Bit Score: 52.21  E-value: 1.73e-08
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gi 25151513 191 FGFNVKGG-ADQ---------NYPVI--VSRVAPGSSADKCQprLNEGDQVLFIDGRDVSTMSHDHVVQFIRSArsglnG 258
Cdd:cd06746  18 FGFVLRGAkAVGpileftptpAFPALqyLESVDPGGVADKAG--LKKGDFLLEINGEDVVKASHEQVVNLIRQS-----G 90


                ....*..
gi 25151513 259 GELHLTI 265
Cdd:cd06746  91 NTLVLKV 97
PDZ1_FL-whirlin cd06740
PDZ domain 1 of the full-length isoform of whirlin and related domains; PDZ (PSD-95 ...
 179-254 1.01e-07

PDZ domain 1 of the full-length isoform of whirlin and related domains; PDZ (PSD-95 (Postsynaptic density protein 95), Dlg (Discs large protein), and ZO-1 (Zonula occludens-1)) domain 1 of the full-length isoform of whirlin and related domains. Whirlin is an essential protein for developmental pathways in photoreceptor cells of the retina and hair cells of the inner ear. The full-length whirlin isoform has two harmonin N-like domains, three PDZ domains, a proline-rich region, and a PDZ-binding motif. Whirlin isoforms may form different complexes at the periciliary membrane complex (PMC) in photoreceptors, and the stereociliary tip and base in inner ear hair cells. It interacts with ADGRV1 and usherin at the PMC; with SANS and RpgrORF15 at the connecting cilium in photoreceptors; with EPS8, MYO15A, p55, and CASK proteins at the stereociliary tip of inner ear hair cells; and with ADGRV1, usherin, and PDZD7 at the stereociliary base in inner ear hair cells. Mutations in the gene encoding whirlin (WHRN; also known as USH2D and DFNB31), have been found to cause either USH2 subtype (USH2D) or autosomal recessive non-syndromic deafness type 31 (DFNB31). Whirlin is the key protein in the USH2 complex (whirlin, usherin and GPR98) which recruits other USH2 causative proteins at the periciliary membrane in photoreceptors and the ankle link of the stereocilia in hair cells. Whirlin's interaction with espin, another stereociliary protein, may be important for the architecture of the USH2 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 whirlin 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: 467222 [Multi-domain]  Cd Length: 82  Bit Score: 49.67  E-value: 1.01e-07
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gi 25151513 179 VTIKMRPDRHGrFGFNVKGGADQNYPVIVSRVAPGSSADKcqPRLNEGDQVLFIDGRDVSTMSHDHVVQFIRSARS 254
Cdd:cd06740   4 VTLKRSKSHEG-LGFSIRGGAEHGVGIYVSLVEPGSLAEK--EGLRVGDQILRVNDVSFEKVTHAEAVKILRVSKK 76
PDZ2_GRIP1-2-like cd06681
PDZ domain 2 of glutamate receptor-interacting protein 1 (GRIP1) and GRIP2, and related ...
 178-251 1.42e-07

PDZ domain 2 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 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: 467169 [Multi-domain]  Cd Length: 89  Bit Score: 49.54  E-value: 1.42e-07
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gi 25151513 178 VVTIKMRPDrHGRFGFNVKGGAD----QNYPVIVSRVAPGSSADkCQPRLNEGDQVLFIDGRDVSTMSHDHVVQFIRS 251
Cdd:cd06681   2 TVEVTLEKE-GNSFGFVIRGGAHedrnKSRPLTVTHVRPGGPAD-REGTIKPGDRLLSVDGISLHGATHAEAMSILKQ 77
PDZ1_harmonin cd06737
PDZ domain 1 of harmonin isoforms a, b, and c, and related domains; PDZ (PSD-95 (Postsynaptic ...
 183-254 1.44e-07

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: 49.18  E-value: 1.44e-07
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gi 25151513 183 MRPDRHGR--FGFNVKGGADQNYPVIVSRVAPGSSADkcQPRLNEGDQVLFIDGRDVSTMSHDHVVQFIRSARS 254
Cdd:cd06737   5 VRLDRRGPesLGFSVRGGLEHGCGLFVSHVSPGSQAD--NKGLRVGDEIVRINGYSISQCTHEEVINLIKTKKT 76
PDZ_SNX27-like cd23070
PDZ domain of sorting nexin-27 (SNX27), and related domains; PDZ (PSD-95 (Postsynaptic density ...
 177-265 1.53e-07

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


Pssm-ID: 467283 [Multi-domain]  Cd Length: 93  Bit Score: 49.33  E-value: 1.53e-07
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gi 25151513 177 QVVTIKmrPDRHGrFGFNVKGGAD----------QNYPVI--VSRVAPGSSADKCQPRlnEGDQVLFIDGRDVSTMSHDH 244
Cdd:cd23070   1 RVVTIV--KSETG-FGFNVRGQVSeggqlrsingELYAPLqhVSAVLEGGAADKAGVR--KGDRILEVNGVNVEGATHKQ 75

                        90       100
                ....*....|....*....|.
gi 25151513 245 VVQFIRSarsglNGGELHLTI 265
Cdd:cd23070  76 VVDLIKS-----GGDELTLTV 91
PDZ5_DrPTPN13-like cd23060
PDZ domain 5 of Danio rerio tyrosine-protein phosphatase non-receptor type 13 (Ptpn13) and ...
 189-265 3.43e-07

PDZ domain 5 of Danio rerio tyrosine-protein phosphatase non-receptor type 13 (Ptpn13) and related domains; PDZ (PSD-95 (Postsynaptic density protein 95), Dlg (Discs large protein), and ZO-1 (Zonula occludens-1)) domain 5 of Danio rerio Ptpn13, and related domains. Protein-tyrosine phosphatases (PTPs) dephosphorylate phosphotyrosyl residues in proteins that are phosphorylated by protein tyrosine kinases (PTKs). Danio rerio Ptpn13 is a classical non-receptor-like PTP. 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 PTPN13-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: 467273 [Multi-domain]  Cd Length: 80  Bit Score: 48.12  E-value: 3.43e-07
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gi 25151513 189 GRFGFNVKGGaDQNYPVIVSRVAPGSSADKcQPRLNEGDQVLFIDGRDVSTMSHDHVVQFIRSARsglngGELHLTI 265
Cdd:cd23060  10 GGLGFSLVGG-EGGSGIFVKSISPGGVADR-DGRLQVGDRLLQVNGESVIGLSHSKAVNILRKAK-----GTVQLTV 79
PDZ2-PTPN13_FRMPD2-like cd06792
PDZ domain 2 of tyrosine kinase PTPN13, FERM and PDZ domain-containing protein 2 (FRMPD2), and ...
 187-252 5.53e-07

PDZ domain 2 of tyrosine kinase PTPN13, FERM and PDZ domain-containing protein 2 (FRMPD2), and similar domains; PDZ (PSD-95 (Postsynaptic density protein 95), Dlg (Discs large protein), and ZO-1 (Zonula occludens-1)) domain 2 of human PTPN13, and related domains. PTPN13, also known as Fas-associated protein-tyrosine phosphatase 1 (FAP-1), protein-tyrosine phosphatase 1E (PTP-E1), and protein-tyrosine phosphatase (PTPL1), negatively regulates FAS-mediated apoptosis and NGFR-mediated pro-apoptotic signaling, and may also regulate phosphoinositide 3-kinase (PI3K) signaling. It contains 5 PDZ domains; interaction partners of its second PDZ domain (PDZ2) include the Fas receptor (TNFRSF6) and thyroid receptor-interacting protein 6 (TRIP6). The second PDZ (PDZ2) domain, but not PDZ1 or PDZ3, of FRMPD2 binds to GluN2A and GluN2B, two subunits of N-methyl-d-aspartic acid (NMDA) receptors. Other binding partners of the FRMPDZ2 PDZ2 domain include NOD2, and catenin family members, delta catenin (CTNND2), armadillo repeat gene deleted in velo-cardio-facial syndrome (ARVCF) and p0071 (also known as plakophilin 4; PKP4). 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 PTPN13-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: 467254 [Multi-domain]  Cd Length: 87  Bit Score: 47.59  E-value: 5.53e-07
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gi 25151513 187 RHGRFGFNVKGGADQNYP---VIVSRVAPGSSADkCQPRLNEGDQVLFIDGRDVSTMSHDHVVQFIRSA 252
Cdd:cd06792  10 KDGSLGISVTGGINTSVRhggIYVKSLVPGGAAE-QDGRIQKGDRLLEVNGVSLEGVTHKQAVECLKNA 77
PDZ_NHERF-like cd06768
PDZ domains of the Na+/H+ exchange regulatory cofactor (NHERF) family (NHERF1-4), and related ...
 191-264 6.80e-07

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


Pssm-ID: 467249 [Multi-domain]  Cd Length: 80  Bit Score: 47.05  E-value: 6.80e-07
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                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 25151513 191 FGFN---VKGGADQnypvIVSRVAPGSSADKCqpRLNEGDQVLFIDGRDVSTMSHDHVVQFIRSarsglNGGELHLT 264
Cdd:cd06768  12 YGFNlhaEKGRPGH----FIREVDPGSPAERA--GLKDGDRLVEVNGENVEGESHEQVVEKIKA-----SGNQVTLL 77
PDZ4_GRIP1-2-like cd06686
PDZ domain 4 of glutamate receptor-interacting protein 1 (GRIP1) and GRIP2, and related ...
 177-254 7.11e-07

PDZ domain 4 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 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: 467174 [Multi-domain]  Cd Length: 99  Bit Score: 47.73  E-value: 7.11e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25151513 177 QVVTIKMRPDRHGRFGFNVKGGA----DQNYPVIVSRVAPGSSADKCQPrLNEGDQVLFIDGRDVSTMSHDHVVQFIRSA 252
Cdd:cd06686   6 ETTEVILRGDPLKGFGIQLQGGVfateTLSSPPLISFIEPDSPAERCGV-LQVGDRVLSINGIPTEDRTLEEANQLLRDS 84


                ..
gi 25151513 253 RS 254
Cdd:cd06686  85 AS 86
PDZ2_PDZD7-like cd10834
PDZ domain 2 of the canonical isoform 1 of PDZ domain containing 7 (PDZD7), and related ...
 192-266 8.37e-07

PDZ domain 2 of the canonical isoform 1 of PDZ domain containing 7 (PDZD7), and related domains; PDZ (PSD-95 (Postsynaptic density protein 95), Dlg (Discs large protein), and ZO-1 (Zonula occludens-1)) domain 2 of the long isoform 1 of PDZD7, and related domains. PDZD7 is critical for the organization of Usher syndrome type 2 (USH2) complex. Usher syndrome is the leading cause of hereditary sensory deaf-blindness in humans; USH2 is the most common sub-type. Formation of the USH2 complex is based upon heterodimerization between PDZD7 and whirlin (another PDZ domain-containing protein) and a subsequent dynamic interplay between USH2 proteins via their multiple PDZ domains. The PDZD7 PDZ2 domain binds GPR98 (also known as VLGR1) and usherin (USH2A). PDZD7 and whirlin form heterodimers through their multiple PDZ domains; whirlin and PDZD7 interact with usherin and GPR98 to form an interdependent ankle link complex. PDZD7 also interacts with myosin VIIa. PDZD7 also forms homodimers through its PDZ2 domain. Various isoforms of PDZD7 produced by alternative splicing have been identified; this subgroup includes the second PDZ domain of the canonical isoform of PDZD7- isoform 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 PDZD7-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: 467270 [Multi-domain]  Cd Length: 85  Bit Score: 47.00  E-value: 8.37e-07
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 25151513 192 GFNVKGGADQNYPVIVSRVAPGSSADkcQPRLNEGDQVLFIDGRDVSTMSHDHVVQFIRSARsglnggELHLTIR 266
Cdd:cd10834  16 GFNIRGGSEYGLGIYVSKVDPGGLAE--QNGIKVGDQILAVNGVSFEDITHSKAVEVLKSQT------HLMLTIK 82
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 ...
 178-266 1.14e-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: 46.84  E-value: 1.14e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25151513 178 VVTIKMRPDRHGrFGFNVKGGADQ---NYPVIVSRVAPGSSADKCQpRLNEGDQVLFIDGRDVSTMSHDHVVQFIRSars 254
Cdd:cd06763   1 AVTVELEKGSAG-LGFSLEGGKGSplgDRPLTIKRIFKGGAAEQSG-VLQVGDEILQINGTSLQGLTRFEAWNIIKS--- 75

                        90
                ....*....|..
gi 25151513 255 gLNGGELHLTIR 266
Cdd:cd06763  76 -LPEGPVTLLIR 86
PDZ1_INAD-like cd23063
PDZ domain 1 of inactivation-no-after-potential D (INAD), and related domains; PDZ (PSD-95 ...
 191-257 1.19e-06

PDZ domain 1 of inactivation-no-after-potential D (INAD), and related domains; PDZ (PSD-95 (Postsynaptic density protein 95), Dlg (Discs large protein), and ZO-1 (Zonula occludens-1)) domain 1 of INAD, and related domains. INAD assembles key enzymes of the Drosophila compound eye photo-transduction pathway into a supramolecular complex, supporting efficient and fast light signaling. It contains 5 PDZ domains arranged in tandem (PDZ1-PDZ5) which independently bind various proteins. INAD PDZ2 binds eye-specific protein kinase C, INAD PDZ3 binds transient receptor potential (TRP) channel, and INAD PDZ4,5 tandem binds NORPA (phospholipase Cbeta, PLCbeta). Mutations of the inaD gene that lead to disruption of each of these interactions impair fly photo signal transduction. 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 INAD-like family PDZ1 domain is a canonical PDZ domain containing six beta-strands A-F and two alpha-helices (alpha-helix 1 and 2), arranged in the order: beta-strands A, B, C, alpha-helix 1, beta-strands D, E, alpha-helix 2 and beta-strand F.


Pssm-ID: 467276 [Multi-domain]  Cd Length: 87  Bit Score: 46.74  E-value: 1.19e-06
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 25151513 191 FGFNVKGGADQNYP------VIVSRVAPGSSADKCQpRLNEGDQVLFIDGRDVSTMSHDHVVQFIRSARSGLN 257
Cdd:cd23063  12 FGICIVRGEVKVSPntkttgIFIKGIIPDSPAHKCG-RLKVGDRILSVNGNDVRNSTEQAAIDLIKEADFKIV 83
PDZ4_PTPN13-like cd06696
PDZ domain 4 of protein tyrosine phosphatase non-receptor type 13 (PTPN13), and related ...
 175-252 1.55e-06

PDZ domain 4 of protein tyrosine phosphatase non-receptor type 13 (PTPN13), and related domains; PDZ (PSD-95 (Postsynaptic density protein 95), Dlg (Discs large protein), and ZO-1 (Zonula occludens-1)) domain 4 of PTPN13 [also known as Fas-associated protein-tyrosine phosphatase 1 (FAP-1), protein-tyrosine phosphatase 1E (PTP-E1), and protein-tyrosine phosphatase (PTPL1)] 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). The PDZ superfamily includes canonical PDZ domains as well as those with circular permutations and domain swapping mediated by beta-strands. This PTPN13 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: 467182 [Multi-domain]  Cd Length: 85  Bit Score: 46.15  E-value: 1.55e-06
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 25151513 175 EDQVVTIKMRPDRhGRFGFNVKGGADQNYPVIVSRVAPGSSADKcqpRLNEGDQVLFIDGRDVSTMSHDHVVQFIRSA 252
Cdd:cd06696   1 EVELEVTLTKSEK-GSLGFTVTKGKDDNGCYIHDIVQDPAKSDG---RLRPGDRLIMVNGVDVTNMSHTEAVSLLRAA 74
PDZ2_PDZD2-like cd06758
PDZ domain 2 of PDZ domain containing 2 (PDZD2), and related domains; PDZ (PSD-95 ...
 188-254 1.71e-06

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: 46.19  E-value: 1.71e-06
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25151513 188 HGRFGFNVKGGADQNYP---VIVSRVAPGSSADKCQpRLNEGDQVLFIDGRDVSTMSHDHVVQFIRSARS 254
Cdd:cd06758  11 KGGLGIQITGGKGSKRGdigIFVAGVEEGGSADRDG-RLKKGDELLMINGQSLIGLSHQEAVAILRSSAS 79
PDZ1_L-delphilin-like cd06743
PDZ domain 1 of delphilin (L-delphilin isoform), and related domains; PDZ (PSD-95 ...
 189-254 1.82e-06

PDZ domain 1 of delphilin (L-delphilin isoform), and related domains; PDZ (PSD-95 (Postsynaptic density protein 95), Dlg (Discs large protein), and ZO-1 (Zonula occludens-1)) domain 1 of delphilin (also known as glutamate receptor, ionotropic, delta 2-interacting protein 1, L-delphilin). Delphilin, a postsynaptic protein which is selectively expressed at cerebellar Purkinje cells, links the glutamate receptor delta 2 subunit (GluRdelta2) with the actin cytoskeleton and various signaling molecules. Two alternatively spliced isoforms of delphilin have been characterized: L-delphilin has two PDZ domains, PDZ1 and PDZ2, and S-delphilin has a single PDZ domain (PDZ2). These two isoforms are differently palmitoylated and may be involved in controlling GluRdelta2 signaling in Purkinje cells. PDZ domains usually bind in a sequence-specific manner to short peptide sequences located at the C-terminal end of their partner proteins (known as PDZ binding motifs). The PDZ superfamily includes canonical PDZ domains as well as those with circular permutations and domain swapping mediated by beta-strands. This delphilin-like family PDZ1 domain is a canonical PDZ domain containing six beta-strands A-F and two alpha-helices (alpha-helix 1 and 2), arranged in the order: beta-strands A, B, C, alpha-helix 1, beta-strands D, E, alpha-helix 2 and beta-strand F.


Pssm-ID: 467225 [Multi-domain]  Cd Length: 76  Bit Score: 45.73  E-value: 1.82e-06
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 25151513 189 GRFGFNVKGGAdqnyPVIVSRVAPGSSADkcQPRLNEGDQVLFIDGRDVSTMSHDHVVQFIRSARS 254
Cdd:cd06743   9 EAFGFSIGGSG----PCYILSVEEGSSAH--AAGLQPGDQILELDGQDVSSLSCEAIIALARRCPS 68
PDZ_RapGEF2_RapGEF6-like cd06755
PDZ domain of Rap guanine nucleotide exchange factor 2 and Rap guanine nucleotide exchange ...
 179-268 2.42e-06

PDZ domain of Rap guanine nucleotide exchange factor 2 and Rap guanine nucleotide exchange factor 6, and related domains; PDZ (PSD-95 (Postsynaptic density protein 95), Dlg (Discs large protein), and ZO-1 (Zonula occludens-1)) domain of Rap guanine nucleotide exchange factor 2 (RapGEF2, also named RA-GEF-1, PDZ-GEF1, CNrasGEF and nRapGEP) and Rap guanine nucleotide exchange factor 6 (RapGEF6, also named RA-GEF-2 and PDZ-GEF2). RapGEF2 and RapGEF6 constitute a subfamily of guanine nucleotide exchange factors (GEFs) for RAP small GTPases that is characterized by the possession of the PDZ and Ras/Rap-associating domains. They activate Rap small GTPases, by catalyzing the release of GDP from the inactive GDP-bound forms, thereby accelerating GTP loading to yield the active GTP-bound forms. The PDZ domain of RapGEF6 (also known as PDZ-GEF2) binds junctional adhesion molecule A (JAM-A). 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 RapGEF2 and RapGEF6 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: 467237 [Multi-domain]  Cd Length: 83  Bit Score: 45.72  E-value: 2.42e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25151513 179 VTIkMRPDRHGRFGFNVKGGADQNYPVIVSRVAPGSSADKCQprLNEGDQVLFIDGRDVSTMSHDHVVQFIRsarsglNG 258
Cdd:cd06755   3 VTL-TRPSRESPLHFSLLGGSEKGFGIFVSKVEKGSKAAEAG--LKRGDQILEVNGQNFENITLKKALEILR------NN 73

                        90
                ....*....|
gi 25151513 259 GELHLTIRPN 268
Cdd:cd06755  74 THLSITVKTN 83
PDZ1_MUPP1-like cd06689
PDZ domain 1 of multi-PDZ-domain protein 1 (MUPP1) and PATJ (protein-associated tight junction) ...
 177-265 2.82e-06

PDZ domain 1 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 1 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 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: 467176 [Multi-domain]  Cd Length: 102  Bit Score: 46.09  E-value: 2.82e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25151513 177 QVVTIKMRPDRHGRFGFNVKGGADQN---YPVIVSRVAPGSSADKCQpRLNEGDQVLFIDGRDV-STMSHDHVVQFIRSA 252
Cdd:cd06689  14 QVEYIELEKPESGGLGFSVVGLKSENrgeLGIFVQEIQPGSVAARDG-RLKENDQILAINGQPLdQSISHQQAIAILQQA 92

                        90
                ....*....|...
gi 25151513 253 RsglngGELHLTI 265
Cdd:cd06689  93 K-----GSVELVV 100
PDZ3_Scribble-like cd06702
PDZ domain 3 of Drosophila Scribble, human Scribble homolog, and related domains; PDZ (PSD-95 ...
 189-266 3.71e-06

PDZ domain 3 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 2 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 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: 467186 [Multi-domain]  Cd Length: 89  Bit Score: 45.33  E-value: 3.71e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25151513 189 GRFGFNVKGGADQ-NYP-------VIVSRVAPGSSADKCQPRLneGDQVLFIDGRDVSTMSHDHVVQFIRSarsglNGGE 260
Cdd:cd06702  10 GPLGLSIVGGSDHsSHPfgvdepgIFISKVIPDGAAAKSGLRI--GDRILSVNGKDLRHATHQEAVSALLS-----PGQE 82


                ....*.
gi 25151513 261 LHLTIR 266
Cdd:cd06702  83 IKLLVR 88
PDZ4_LNX1_2-like cd06680
PDZ domain 4 of human Ligand of Numb protein X 1 (LNX1) and LNX2, and related domains; PDZ ...
 180-268 4.58e-06

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: 45.03  E-value: 4.58e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25151513 180 TIKMRPDRHGRFGFNVKGGADQ---NYPVIVSRVAPGSSADKcQPRLNEGDQVLFIDGRDVSTMSHDHVVQFIRSARsgl 256
Cdd:cd06680   2 DITLRRSSSGSLGFSIVGGYEEshgNQPFFVKSIVPGTPAYN-DGRLKCGDIILAVNGVSTVGMSHAALVPLLKEQR--- 77

                        90
                ....*....|..
gi 25151513 257 ngGELHLTIRPN 268
Cdd:cd06680  78 --GRVTLTVVSW 87
PDZ6_PDZD2-PDZ3_hPro-IL-16-like cd06762
PDZ domain 6 of PDZ domain containing 2 (PDZD2), PDZ domain 3 of human pro-interleukin-16 ...
 192-253 5.72e-06

PDZ domain 6 of PDZ domain containing 2 (PDZD2), PDZ domain 3 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 6 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 third PDZ domain (PDZ3) 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 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: 467243 [Multi-domain]  Cd Length: 86  Bit Score: 44.56  E-value: 5.72e-06
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 25151513 192 GFNVKGGADQ-NYPVIVSRVAPGSSADKcQPRLNEGDQVLFIDGRDVSTMSHDHVVQFIRSAR 253
Cdd:cd06762  15 GFSLAGGSDLeNKSITVHRVFPSGLAAQ-EGTIQKGDRILSINGKSLKGVTHGDALSVLKQAR 76
PDZ3_Dlg1-2-4-like cd06795
PDZ domain 3 of human discs large homolog 1 (Dlg1), Dlg2, and Dlg4, Drosophila disc large (Dlg) ...
 192-252 1.19e-05

PDZ domain 3 of human discs large homolog 1 (Dlg1), Dlg2, and Dlg4, Drosophila disc large (Dlg), and related domains; PDZ (PSD-95 (Postsynaptic density protein 95), Dlg (Discs large protein), and ZO-1 (Zonula occludens-1)) domain 3 of Drosophila Dlg1, human Dlg1, 2, and 4 and related domains. Dlg1 (also known as synapse-associated protein Dlg197; SAP-97), Dlg2 (also known as channel-associated protein of synapse-110; postsynaptic density protein 93, PSD-93), Dlg4 (also known as postsynaptic density protein 95, PSD-95; synapse-associated protein 90, SAP-90) each have 3 PDZ domains and belong to the membrane-associated guanylate kinase family. Dlg1 regulates antigen receptor signaling and cell polarity in lymphocytes, B-cell proliferation and antibody production, and TGFalpha bioavailability; its PDZ3 domain binds pro-TGFalpha, and its PDZ2 domain binds the TACE metalloprotease responsible for cleaving pro-TGFalpha to a soluble form. Dlg2 is involved in N-methyl-D-aspartate (NMDA) receptor signaling, regulating surface expression of NMDA receptors in dorsal horn neurons of the spinal cord; it interacts with NMDA receptor subunits and with Shaker-type K+ channel subunits to cluster into a channel complex. The Dlg4 PDZ1 domain binds NMDA receptors, and its PDZ2 domain binds neuronal nitric oxide synthase (nNOS), forming a complex in neurons. The Drosophila Scribble complex (Scribble, Dlg, and lethal giant larvae) plays a role in apico-basal cell polarity, and in other forms of polarity, including regulation of the actin cytoskeleton, cell signaling and vesicular trafficking, and in tumor development; postsynaptic targeting of Drosophila DLG requires interactions mediated by the first two 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 Dlg-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: 467257 [Multi-domain]  Cd Length: 91  Bit Score: 43.88  E-value: 1.19e-05
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 25151513 192 GFNVKGGADqNYPVIVSRVAPGSSADKCQpRLNEGDQVLFIDGRDVSTMSHDHVVQFIRSA 252
Cdd:cd06795  15 GFNIVGGED-GEGIFISFILAGGPADLSG-ELRRGDQILSVNGVDLRNATHEQAAAALKNA 73
PDZ4_Scribble-like cd06701
PDZ domain 4 of Drosophila Scribble, human Scribble homolog, and related domains; PDZ (PSD-95 ...
 177-263 1.25e-05

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: 44.14  E-value: 1.25e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25151513 177 QVVTIKMRPDRhgRFGFNVKGGA--DQNYP-------VIVSRVAPGSSADKCQpRLNEGDQVLFIDGRDVSTMSHDHVVQ 247
Cdd:cd06701   5 QELTIVKEPGE--KLGISIRGGAkgHAGNPldptdegIFISKINPDGAAARDG-RLKVGQRILEVNGQSLLGATHQEAVR 81

                        90
                ....*....|....*.
gi 25151513 248 FIRSArsglnGGELHL 263
Cdd:cd06701  82 ILRSV-----GDTLTL 92
cpPDZ_CPP-like cd06782
circularly permuted PDZ domain of C-terminal processing peptidase (CPP), a serine protease, ...
 200-268 1.32e-05

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


Pssm-ID: 467623 [Multi-domain]  Cd Length: 88  Bit Score: 43.63  E-value: 1.32e-05
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 25151513 200 DQNYPVIVSrVAPGSSADKCqpRLNEGDQVLFIDGRDVSTMSHDHVVQFIRsarsGLNGGELHLTIRPN 268
Cdd:cd06782  12 DDGYLVVVS-PIPGGPAEKA--GIKPGDVIVAVDGESVRGMSLDEVVKLLR----GPKGTKVKLTIRRG 73
PDZ_ARHGEF11-12-like cd23069
PDZ domain of ARHGEF11, ARHGEF12, and related domains; PDZ (PSD-95 (Postsynaptic density ...
 179-251 1.48e-05

PDZ domain of ARHGEF11, ARHGEF12, and related domains; PDZ (PSD-95 (Postsynaptic density protein 95), Dlg (Discs large protein), and ZO-1 (Zonula occludens-1)) domain of ARHGEF11, ARHGEF12, and related domains. This subfamily includes the GEFs (guanine exchange factors) ARHGEF11 (Rho guanine nucleotide exchange factor 11, known as PDZ-RhoGEF) and ARHGEF12 (Rho guanine nucleotide exchange factor 12, also known as leukemia-associated RhoGEF). GEFs activate Rho GTPases by promoting GTP binding. ARHGEF11/12 are regulators of G protein signaling (RGS) domain-containing GEFs; the RGS domain mediates their binding to and activation of Galpha (and Gq also in the case of ARHGEF12), in response to G-protein coupled receptor activation. ARHGEF11 and 12 are involved in serum-signaling, and regulate Yes-Associated Protein (YAP1)-dependent transcription. The ARHGEF12 PDZ domain binds plexin-B1 and the receptor tyrosine kinase insulin-like growth factor receptor (IGF-R1) beta-subunit. ARHGEF12 also interacts with glutamate receptor delta-1(GluD1), a postsynaptic organizer of inhibitory synapses in cortical pyramidal neurons. The PDZ superfamily includes canonical PDZ domains as well as those with circular permutations and domain swapping mediated by beta-strands. This ARHGEF11-12-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: 467282 [Multi-domain]  Cd Length: 76  Bit Score: 43.15  E-value: 1.48e-05
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 25151513 179 VTIkmRPDRHGrFGFNVKGgadqNYPVIVSRVAPGSSADKCQprLNEGDQVLFIDGRDVSTMSHDHVVQFIRS 251
Cdd:cd23069   4 VVI--QRDENG-YGLTVSG----DNPVFVQSVKEGGAAYRAG--VQEGDRIIKVNGTLVTHSNHLEVVKLIKS 67
PDZ_GOPC-like cd06800
PDZ domain of Golgi-associated PDZ and coiled-coil motif-containing protein (GOPC), and ...
 180-255 2.15e-05

PDZ domain of Golgi-associated PDZ and coiled-coil motif-containing protein (GOPC), and related domains; PDZ (PSD-95 (Postsynaptic density protein 95), Dlg (Discs large protein), and ZO-1 (Zonula occludens-1)) domain of GOPC and related domains. GOPC, also known as PIST (PDZ domain protein interacting specifically with TC10), FIG (fused in glioblastoma), and CAL (CFTR-associated ligand), regulates the trafficking of a wide array of proteins, including small GTPases, receptors, and cell surface molecules such as cadherin 23 and CFTR. It may regulate CFTR chloride currents and acid-sensing ASIC3 currents by modulating cell surface expression of both channels, and may play a role in autophagy. Interaction partners of the GOPC PDZ domains include: FZD5, FZD8, ASIC3, CFTR, MUC3, ARFRP1, Ggamma13, neuroligin, and Stargazin. 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 GOPC-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: 467261 [Multi-domain]  Cd Length: 83  Bit Score: 43.13  E-value: 2.15e-05
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 25151513 180 TIKMRPDRHGRFGFNVKGGADQNYPVIVSRVAPGSSADKCQpRLNEGDQVLFIDGRDVSTMSHDHVVQfIRSARSG 255
Cdd:cd06800   2 KVLLSKEPHEGLGISITGGKEHGVPILISEIHEGQPADRCG-GLYVGDAILSVNGIDLRDAKHKEAVT-ILSQQRG 75
DUSP23 cd14504
dual specificity phosphatase 23; Dual specificity phosphatase 23 (DUSP23), also known as ...
 482-567 2.21e-05

dual specificity phosphatase 23; Dual specificity phosphatase 23 (DUSP23), also known as VH1-like phosphatase Z (VHZ) or low molecular mass dual specificity phosphatase 3 (LDP-3), functions as a protein-serine/threonine phosphatase (EC 3.1.3.16) and a protein-tyrosine-phosphatase (EC 3.1.3.48). It deactivates its MAPK substrates by dephosphorylating the threonine and tyrosine residues in the conserved Thr-Xaa-Tyr motif residing in their activation sites. DUSP23 is an atypical DUSP; it contains the catalytic dual specificity phosphatase domain but lacks the N-terminal Cdc25/rhodanese-like domain that is present in typical DUSPs or MKPs. It is able to enhance activation of JNK and p38 MAPK, and has been shown to dephosphorylate p44-ERK1 (MAPK3) in vitro. It has been associated with cell growth and human primary cancers. It has also been identified as a cell-cell adhesion regulatory protein; it promotes the dephosphorylation of beta-catenin at Tyr 142 and enhances the interaction between alpha- and beta-catenin.


Pssm-ID: 350354 [Multi-domain]  Cd Length: 142  Bit Score: 44.58  E-value: 2.21e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25151513 482 PDHGVP--DDPKHFIQFVDEVRKARQgsvdPIVVHCSAGIGRTGVLIlmetaACLVESNEPVYPLDIVRTMRDQRAMLIQ 559
Cdd:cd14504  58 EDYTPPtlEQIDEFLDIVEEANAKNE----AVLVHCLAGKGRTGTML-----ACYLVKTGKISAVDAINEIRRIRPGSIE 128


                ....*...
gi 25151513 560 TPGQYTFV 567
Cdd:cd14504 129 TSEQEKFV 136
PDZ_shroom2_3_4-like cd06750
PDZ domain of shroom2, shroom3, shroom4, and related domains; PDZ (PSD-95 (Postsynaptic ...
 192-252 2.35e-05

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: 42.71  E-value: 2.35e-05
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 25151513 192 GFNVKGGADQNYPVIVSRVAPGSSADKCQpRLNEGDQVLFIDGRDVSTmSHDHVVQFIRSA 252
Cdd:cd06750  14 GFTLKGGLEHGEPLVISKIEEGGKAASVG-KLQVGDEVVNINGVPLSG-SRQEAIQLVKGS 72
PDZ1_PDZD7-like cd10833
PDZ domain 1 of the canonical isoform 1 of PDZ domain containing 7 (PDZD7), and related ...
 178-234 2.50e-05

PDZ domain 1 of the canonical isoform 1 of PDZ domain containing 7 (PDZD7), and related domains; PDZ (PSD-95 (Postsynaptic density protein 95), Dlg (Discs large protein), and ZO-1 (Zonula occludens-1)) domain 1 of the long isoform 1 of PDZD7, and related domains. PDZD7 is critical for the organization of Usher syndrome type 2 (USH2) complex. Usher syndrome is the leading cause of hereditary sensory deaf-blindness in humans; USH2 is the most common sub-type. Formation of the USH2 complex is based upon heterodimerization between PDZD7 and whirlin (another PDZ domain-containing protein) and a subsequent dynamic interplay between USH2 proteins via their multiple PDZ domains. The PDZD7 PDZ2 domain binds GPR98 (also known as VLGR1) and usherin (USH2A). PDZD7 and whirlin form heterodimers through their multiple PDZ domains; whirlin and PDZD7 interact with usherin and GPR98 to form an interdependent ankle link complex. PDZD7 also interacts with myosin VIIa. PDZD7 also forms homodimers through its PDZ2 domain. Various isoforms of PDZD7 produced by alternative splicing have been identified; this subgroup includes the first PDZ domain of the canonical isoform of PDZD7- isoform 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 PDZD7-like family PDZ1 domain is a canonical PDZ domain containing six beta-strands A-F and two alpha-helices (alpha-helix 1 and 2), arranged in the order: beta-strands A, B, C, alpha-helix 1, beta-strands D, E, alpha-helix 2 and beta-strand F.


Pssm-ID: 467269 [Multi-domain]  Cd Length: 84  Bit Score: 42.81  E-value: 2.50e-05
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....*..
gi 25151513 178 VVTIKMRPDrhGRFGFNVKGGADQNYPVIVSRVAPGSSADKCQprLNEGDQVLFIDG 234
Cdd:cd10833   3 TVTVEKSPD--GSLGFSVRGGSEHGLGIFVSKVEEGSAAERAG--LCVGDKITEVNG 55
CtpA COG0793
C-terminal processing protease CtpA/Prc, contains a PDZ domain [Posttranslational modification, ...
 205-268 2.77e-05

C-terminal processing protease CtpA/Prc, contains a PDZ domain [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 440556 [Multi-domain]  Cd Length: 341  Bit Score: 46.40  E-value: 2.77e-05
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 25151513 205 VIVSRVAPGSSADKcqPRLNEGDQVLFIDGRDVSTMSHDHVVQFIRsarsGLNGGELHLTIRPN 268
Cdd:COG0793  73 VVVVSVIPGSPAEK--AGIKPGDIILAIDGKSVAGLTLDDAVKLLR----GKAGTKVTLTIKRP 130
PDZ3_GRIP1-2-like cd06684
PDZ domain 3 of glutamate receptor-interacting protein 1 (GRIP1) and GRIP2, and related ...
 202-267 3.14e-05

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: 42.62  E-value: 3.14e-05
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 25151513 202 NYPVIV-SRVAPGSSADKCQPrLNEGDQVLFIDGRDVSTMSHDHVVQFIRSArsglNGGELHLTIRP 267
Cdd:cd06684  26 NKQVIViDSIKPASIADRCGA-LHVGDHILSIDGTSVEHCSLAEATQLLASN----SGDQVKLEILP 87
PDZ_Par6-like cd06718
PDZ domain of partitioning defective 6 (Par6), Drosophila Rho GTPase-activating protein 100F ...
 177-267 3.91e-05

PDZ domain of partitioning defective 6 (Par6), Drosophila Rho GTPase-activating protein 100F (RhoGAP100F), and related domains; PDZ (PSD-95 (Postsynaptic density protein 95), Dlg (Discs large protein), and ZO-1 (Zonula occludens-1)) domain of Par6 (also known as PAR6 or Par-6), RhoGAP100F, and related domains. Par6 is part of a conserved machinery that directs metazoan cell polarity, a process necessary for the function of diverse cell types. Par6 forms a cell polarity-regulatory complex with atypical protein kinase C (aPKC) and Par3. Par6 can also directly associate with PALS1 (proteins associated with Lin7, also known as Stardust) providing a link between the Par3/aPKC/Par6 complex and the PALS1-PATJ (protein-associated TJ) complex. Binding partners of the Par6-PDZ domain include Par3, PALS1/Stardust; leucine-rich repeat-containing protein netrin-G ligand-2 (NGL-2), human crumbs (CRB3) involve in the morphogenesis of the tight junctions in mammalian epithelial cells, and PAR-6 co-operates with the Par6 semi-CRIB domain to bind CDC42. CDC42 regulates the Par6 PDZ domain through an allosteric CRIB-PDZ transition. Drosophila RhoGAP100F, also known as synapse defective protein 1 homolog (syd-1 homolog), is a GTPase activator for the Rho-type GTPases by converting them to an inactive GDP-bound form. The RhoGAP100F-PDZ domain binds the neurexin C terminus to control synapse formation at the Drosophila neuromuscular junction. 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 Par6-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: 467202 [Multi-domain]  Cd Length: 84  Bit Score: 42.17  E-value: 3.91e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25151513 177 QVVTIKMRPDrhGRFGFNVKGGADQNYP--VIVSRVAPGSSADKCQpRLNEGDQVLFIDGRDVSTMSHDHVVQFIRSARs 254
Cdd:cd06718   1 RRVELIKPPG--KPLGFYIRDGNGVERVpgIFISRLVLGSLADSTG-LLAVGDEILEVNGVEVTGKSLDDVTDMMVAPT- 76

                        90
                ....*....|...
gi 25151513 255 glnggELHLTIRP 267
Cdd:cd06718  77 -----RLIITVKP 84
PDZ2_FL-whirlin cd06741
PDZ domain 2 of the full-length isoform of whirlin and related domains; PDZ (PSD-95 ...
 188-266 3.96e-05

PDZ domain 2 of the full-length isoform of whirlin and related domains; PDZ (PSD-95 (Postsynaptic density protein 95), Dlg (Discs large protein), and ZO-1 (Zonula occludens-1)) domain 2 of the full-length isoform of whirlin and related domains. Whirlin is an essential protein for developmental pathways in photoreceptor cells of the retina and hair cells of the inner ear. The full-length whirlin isoform has two harmonin N-like domains, three PDZ domains, a proline-rich region, and a PDZ-binding motif. Whirlin isoforms may form different complexes at the periciliary membrane complex (PMC) in photoreceptors, and the stereociliary tip and base in inner ear hair cells. It interacts with ADGRV1 and usherin at the PMC; with SANS and RpgrORF15 at the connecting cilium in photoreceptors; with EPS8, MYO15A, p55, and CASK proteins at the stereociliary tip of inner ear hair cells; and with ADGRV1, usherin, and PDZD7 at the stereociliary base in inner ear hair cells. Mutations in the gene encoding whirlin (WHRN; also known as USH2D and DFNB31), have been found to cause either USH2 subtype (USH2D) or autosomal recessive non-syndromic deafness type 31 (DFNB31). Whirlin is the key protein in the USH2 complex (whirlin, usherin and GPR98) which recruits other USH2 causative proteins at the periciliary membrane in photoreceptors and the ankle link of the stereocilia in hair cells. Whirlin's interaction with espin, another stereociliary protein, may be important for the architecture of the USH2 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 whirlin 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: 467223 [Multi-domain]  Cd Length: 84  Bit Score: 42.25  E-value: 3.96e-05
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 25151513 188 HGRFGFNVKGGADQNYPVIVSRVAPGSSADKCQprLNEGDQVLFIDGRDVSTMSHDHVVQFIRSARsglnggELHLTIR 266
Cdd:cd06741  11 GQSLGLMIRGGAEYGLGIYVTGVDPGSVAENAG--LKVGDQILEVNGRSFLDITHDEAVKILKSSK------HLIMTVK 81
PDZ2_MUPP1-like cd06667
PDZ domain 2 of multi-PDZ-domain protein 1 (MUPP1) and PATJ (protein-associated tight junction) ...
 192-250 4.66e-05

PDZ domain 2 of multi-PDZ-domain protein 1 (MUPP1) and PATJ (protein-associated tight junction) and similar domains; PDZ (PSD-95 (Postsynaptic density protein 95), Dlg (Discs large protein), and ZO-1 (Zonula occludens-1)) domain 2 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 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: 467155 [Multi-domain]  Cd Length: 80  Bit Score: 41.88  E-value: 4.66e-05
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gi 25151513 192 GFNVKGGadQNYPVIVSRVAPGSSADKCQpRLNEGDQVLFIDGRDVSTMSHDHVVQFIR 250
Cdd:cd06667  13 GFGIVGG--KSTGVVVKTILPGGVADRDG-RLRSGDHILQIGDTNLRGMGSEQVAQVLR 68
PDZ_densin_erbin-like cd06749
PDZ domain of densin, erbin, and related domains; PDZ (PSD-95 (Postsynaptic density protein 95) ...
 179-252 5.10e-05

PDZ domain of densin, erbin, and related domains; PDZ (PSD-95 (Postsynaptic density protein 95), Dlg (Discs large protein), and ZO-1 (Zonula occludens-1)) domain of densin, erbin, and related domains. Densin (also known as leucine-rich repeat-containing protein 7, LRRC7, densin-180, protein LAP1) and erbin (also known as densin-180-like protein, Erbb2-interacting protein, protein LAP2) belong to the LAP (leucine-rich repeat and PDZ domain) family of scaffolding proteins that play roles in the maintenance of cell shape and apical-basal polarity. Densin and erbin are components of the excitatory postsynaptic compartment and are regulators of dendritic morphology and postsynaptic structure. The densin PDZ domain binds CaV1.3 alpha1 subunit, delta-catenin, and MAGUIN-1. Binding partners of the erbin PDZ domain include ErbB receptor tyrosine kinase ErbB2, HTLV-1 Tax1, Cav1.3 Ca2+channels, and constituents of the cadherin:catenin cell adhesion complex, in particular delta-catenin, p0071 and ARVCF. The erbin PDZ domain binds Smad3, a transductor of the TGFbeta pathway, possibly by a novel interface of binding. Erbin and two other LAP proteins (scribble and lano) redundantly regulate epithelial polarity and apical adhesion 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 densin and erbin-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: 467231 [Multi-domain]  Cd Length: 87  Bit Score: 41.93  E-value: 5.10e-05
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gi 25151513 179 VTIKMRPDrhgrFGFNVKGGAD-QNYP-------VIVSRVAPGSSADKC-QPrlneGDQVLFIDGRDVSTMSHDHVVQFI 249
Cdd:cd06749   3 VRIEKNPG----LGFSISGGIGsQGNPfrpdddgIFVTKVQPDGPASKLlQP----GDKILEVNGYDFVNIEHGQAVSLL 74


                ...
gi 25151513 250 RSA 252
Cdd:cd06749  75 KSF 77
CDC14_C cd14499
C-terminal dual-specificity phosphatase domain of CDC14 family proteins; The cell division ...
 482-528 5.35e-05

C-terminal dual-specificity phosphatase domain of CDC14 family proteins; The cell division control protein 14 (CDC14) family is highly conserved in all eukaryotes, although the roles of its members seem to have diverged during evolution. Yeast Cdc14, the best characterized member of this family, is a dual-specificity phosphatase that plays key roles in cell cycle control. It preferentially dephosphorylates cyclin-dependent kinase (CDK) targets, which makes it the main antagonist of CDK in the cell. Cdc14 functions at the end of mitosis and it triggers the events that completely eliminates the activity of CDK and other mitotic kinases. It is also involved in coordinating the nuclear division cycle with cytokinesis through the cytokinesis checkpoint, and in chromosome segregation. Cdc14 phosphatases also function in DNA replication, DNA damage checkpoint, and DNA repair. Vertebrates may contain more than one Cdc14 homolog; humans have three (CDC14A, CDC14B, and CDC14C). CDC14 family proteins contain a highly conserved N-terminal pseudophosphatase domain that contributes to substrate specificity and a C-terminal catalytic dual-specificity phosphatase domain with the PTP signature motif.


Pssm-ID: 350349 [Multi-domain]  Cd Length: 174  Bit Score: 43.98  E-value: 5.35e-05
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gi 25151513 482 PDHGVPDDP--KHFIQFVDEVRKArqgsvdpIVVHCSAGIGRTGVLI---LM 528
Cdd:cd14499  88 PDGSTPSDDivKKFLDICENEKGA-------IAVHCKAGLGRTGTLIacyLM 132
PDZ_RGS3-like cd06711
PDZ domain of regulator of G-protein signaling 3 (RGS3), and related domains; PDZ (PSD-95 ...
 191-254 5.50e-05

PDZ domain of regulator of G-protein signaling 3 (RGS3), and related domains; PDZ (PSD-95 (Postsynaptic density protein 95), Dlg (Discs large protein), and ZO-1 (Zonula occludens-1)) domain of RGS3, and related domains. RGS3 down-regulates GPCR signal transduction by increasing the GTPase activity of G-protein alpha subunits, thereby driving G-proteins into their inactive GDP-bound form. It downregulates G-protein-mediated release of inositol phosphates and activation of MAP kinases. In Eph/ephrin signaling, RGS3 binds via its PDZ domain to the cytoplasmic C terminus of Eph receptor tyrosine kinase EphB. 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 RGS3-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: 467195 [Multi-domain]  Cd Length: 77  Bit Score: 41.61  E-value: 5.50e-05
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gi 25151513 191 FGFNVKGgadqNYPVIVSRVAPGSSADKCQprLNEGDQVLFIDGRDVSTMSHDHVVQFIRSARS 254
Cdd:cd06711  12 FGFTICD----DSPVRVQAVDPGGPAEQAG--LQQGDTVLQINGQPVERSKCVELAHAIRNCPS 69
PDZ7_MUPP1-PD6_PATJ-like cd06671
PDZ domain 7 of multi-PDZ-domain protein 1 (MUPP1), PDZ domain 6 of PATJ (protein-associated ...
 205-252 8.91e-05

PDZ domain 7 of multi-PDZ-domain protein 1 (MUPP1), PDZ domain 6 of 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 7 of MUPP1 and PDZ domain 6 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 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: 467159 [Multi-domain]  Cd Length: 96  Bit Score: 41.54  E-value: 8.91e-05
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gi 25151513 205 VIVSRVAPGSSADKCQpRLNEGDQVLFIDGRDVSTMSHDHVVQFIRSA 252
Cdd:cd06671  38 IFIKHVLEDSPAGRNG-TLKTGDRILEVNGVDLRNATHEEAVEAIRNA 84
PDZ2_Scribble-like cd06703
PDZ domain 2 of Drosophila Scribble, human Scribble homolog, and related domains; PDZ (PSD-95 ...
 192-252 1.39e-04

PDZ domain 2 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 2 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 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: 467187 [Multi-domain]  Cd Length: 92  Bit Score: 41.09  E-value: 1.39e-04
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gi 25151513 192 GFNVKGGA------DQNYPVIVSRVAPGSSADKcQPRLNEGDQVLFIDGRDVSTMSHDHVVQFIRSA 252
Cdd:cd06703  15 GFSIAGGKgstpfrDGDEGIFISRITEGGAADR-DGKLQVGDRVLSINGVDVTEARHDQAVALLTSS 80
PDZ1_PTPN13-like cd23072
PDZ domain 1 of protein tyrosine phosphatase non-receptor type 13 (PTPN13), and related ...
 177-252 1.56e-04

PDZ domain 1 of protein tyrosine phosphatase non-receptor type 13 (PTPN13), and related domains; PDZ (PSD-95 (Postsynaptic density protein 95), Dlg (Discs large protein), and ZO-1 (Zonula occludens-1)) domain 1 of PTPN13 [also known as Fas-associated protein-tyrosine phosphatase 1 (FAP-1), protein-tyrosine phosphatase 1E (PTP-E1), and protein-tyrosine phosphatase (PTPL1)], 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). The PDZ superfamily includes canonical PDZ domains as well as those with circular permutations and domain swapping mediated by beta-strands. This PTPN13 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: 467285 [Multi-domain]  Cd Length: 92  Bit Score: 40.94  E-value: 1.56e-04
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gi 25151513 177 QVVTIKMRPDRHGRFGFNVKGGAD---QNYPVIVSRVAPGSSADkCQPRLNEGDQVLFIDGRDVSTMSHDHVVQFIRSA 252
Cdd:cd23072   1 EITLVNLKKDAKYGLGFQIVGGEKsgrLDLGIFISSITPGGPAD-LDGRLKPGDRLISVNDVSLEGLSHDAAVEILQNA 78
PDZ_6 pfam17820
PDZ domain; This entry represents the PDZ domain from a wide variety of proteins.
 206-266 1.59e-04

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


Pssm-ID: 436067 [Multi-domain]  Cd Length: 54  Bit Score: 39.82  E-value: 1.59e-04
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gi 25151513   206 IVSRVAPGSSADKC--QPrlneGDQVLFIDGRDVSTMshDHVVQFIRSArsglNGGELHLTIR 266
Cdd:pfam17820   1 VVTAVVPGSPAERAglRV----GDVILAVNGKPVRSL--EDVARLLQGS----AGESVTLTVR 53
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 ...
 192-266 1.89e-04

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: 40.34  E-value: 1.89e-04
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gi 25151513 192 GFNVKGGADQNYPVI---VSRVAPGSSADKcQPRLNEGDQVLFIDGRDVSTMSHDHVVQFIRSARSglngGELHLTIR 266
Cdd:cd06759  15 GFSIVGGRDSPRGPMgiyVKTIFPGGAAAE-DGRLKEGDEILEVNGESLQGLTHQEAIQKFKQIKK----GLVVLTVR 87
PDZ5_MUPP1-like cd06669
PDZ domain 5 of multi-PDZ-domain protein 1 (MUPP1), PATJ (protein-associated tight junction) ...
 175-256 2.21e-04

PDZ domain 5 of multi-PDZ-domain protein 1 (MUPP1), 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 5 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 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: 467157 [Multi-domain]  Cd Length: 98  Bit Score: 40.67  E-value: 2.21e-04
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gi 25151513 175 EDQVVTIKMRPDRHGrFGFNVKGGADQNYP---VIVSR-VAPGSSADKcQPRLNEGDQVLFIDGRDVSTMSHDHVVQFIR 250
Cdd:cd06669   5 SDEVTVIELEKGDRG-LGFSILDYQDPLDPsetVIVIRsLVPGGVAEQ-DGRLLPGDRLVFVNDVSLENASLDEAVQALK 82


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gi 25151513 251 SARSGL 256
Cdd:cd06669  83 SAPPGT 88
PDZ1_PTPN13_FRMPD2-like cd06694
PDZ domain 1 of protein tyrosine phosphatase non-receptor type 13 (PTPN13),FERM and PDZ ...
 178-252 2.30e-04

PDZ domain 1 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 1 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. 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. 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 PTPN13 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: 467180 [Multi-domain]  Cd Length: 92  Bit Score: 40.46  E-value: 2.30e-04
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gi 25151513 178 VVTIKmRPDRHGrFGFNVKGGADQNY---PVIVSRVAPGSSADKcQPRLNEGDQVLFIDGRDVSTMSHDHVVQFIRSA 252
Cdd:cd06694   4 IVTLK-KDPQKG-LGFTIVGGENSGSldlGIFVKSIIPGGPADK-DGRIKPGDRIIAINGQSLEGKTHHAAVEIIQNA 78
PDZ10_MUPP1-PDZ8_PATJ-like cd06673
PDZ domain 10 of multi-PDZ-domain protein 1 (MUPP1), domain 8 of PATJ (protein-associated ...
 179-252 2.30e-04

PDZ domain 10 of multi-PDZ-domain protein 1 (MUPP1), domain 8 of PATJ (protein-associated tight junction) and similar domains; PDZ (PSD-95 (Postsynaptic density protein 95), Dlg (Discs large protein), and ZO-1 (Zonula occludens-1)) domain 10 of MUPP1, PDZ domain 8 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 family PDZ10 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: 467161 [Multi-domain]  Cd Length: 86  Bit Score: 40.35  E-value: 2.30e-04
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gi 25151513 179 VTIKMRPDRHGrFGFNVKGGAD-QNYPVIVSRVAPGSSADKcQPRLNEGDQVLFIDGRDVSTMSHDHVVQFIRSA 252
Cdd:cd06673   4 TTIEINKGKKG-LGLSIVGGSDtLLGAIIIHEVYEDGAAAK-DGRLWAGDQILEVNGEDLRKATHDEAINVLRQT 76
PDZ1_MAGI-1_3-like cd06731
PDZ domain 1 of membrane-associated guanylate kinase inverted 1 (MAGI-1), MAGI-2, and MAGI-3, ...
 191-255 2.50e-04

PDZ domain 1 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 1 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 PDZ1 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: 467213 [Multi-domain]  Cd Length: 85  Bit Score: 39.89  E-value: 2.50e-04
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                ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 25151513 191 FGFNVKGGADQNYPVIVSRVAPGSSADKcQPRLNEGDQVLFIDGRDVSTMSHDHVVQFIRSARSG 255
Cdd:cd06731  13 FGFTIIGGDEPDEFLQIKSVVPDGPAAL-DGKLRTGDVLVSVNDTCVLGYTHADVVKLFQSIPIG 76
PDZ_tamalin_CYTIP-like cd06713
PDZ domain of tamalin, cytohesin-1-interacting protein (CYTIP), and related domains; PDZ ...
 207-252 2.85e-04

PDZ domain of tamalin, cytohesin-1-interacting protein (CYTIP), and related domains; PDZ (PSD-95 (Postsynaptic density protein 95), Dlg (Discs large protein), and ZO-1 (Zonula occludens-1)) domain of tamalin, cytohesin-1-interacting protein, and related domains. Tamalin (trafficking regulator and scaffold protein tamalin, also known as general receptor for phosphoinositides 1-associated scaffold protein, GRASP) functions to link receptors, including group 1 metabotropic glutamate receptors (mGluRs), to neuronal proteins. The tamalin PDZ domain binds the C-terminal domains of group I mGluRs; it also binds potassium/sodium hyperpolarization-activated cyclic nucleotide-gated channel 2 (HCN2), neurotrophin-3 (NT3) TrkCT1-truncated receptor, SAP90/PSD-95-associated protein, and tamalin itself. CYTIP (cytohesin-1-interacting protein, also known as Pleckstrin homology Sec7 and coiled-coil domain-binding protein) sequesters cytohesin-1 in the cytoplasm, limiting its interaction with beta2 integrins; cytohesin-1 binds the CYTIP coiled coil domain. The CYTIP PDZ domain can bind the C-terminal peptide of protocadherin alpha-1 (PCDHA1), indicating a possible interaction between the two. 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 tamalin-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: 467197 [Multi-domain]  Cd Length: 91  Bit Score: 39.91  E-value: 2.85e-04
                        10        20        30        40
                ....*....|....*....|....*....|....*....|....*.
gi 25151513 207 VSRVAPGSSADKCQprLNEGDQVLFIDGRDVSTMSHDHVVQFIRSA 252
Cdd:cd06713  39 VCRVHEDSPAYLAG--LTAGDVILSVNGVSVEGASHQEIVELIRSS 82
cpPDZ_Deg_HtrA-like cd06779
permuted PDZ domain of Deg/high-temperature requirement factor A (HtrA) family of housekeeping ...
 185-277 3.60e-04

permuted PDZ domain of Deg/high-temperature requirement factor A (HtrA) family of housekeeping serine proteases and related domains; PDZ (PSD-95 (Postsynaptic density protein 95), Dlg (Discs large protein), and ZO-1 (Zonula occludens-1)) domain of Deg/HtrA-type serine proteases that participate in folding and degradation of aberrant proteins, and in processing and maturation of native proteins. Typically, these proteases have an N-terminal serine protease domain and at least one C-terminal PDZ domain that recognizes substrates, and in some cases activates the protease function. An exception is yeast Nma11p which has two protease domains and four PDZ domains; its N-terminal half is comprised of a protease domain, followed by two PDZ domains, and its C-terminal half has a similar domain arrangement. HtrA-type proteases include the human HtrA1-4 and MBTPS2, tricorn protease, DegS, DegP and C-terminal processing peptidase, cyanobacterial serine proteases Hhoa, HhoB, and HtrA, and yeast Nma11p. PDZ domains usually bind in a sequence-specific manner to short peptide sequences located at the C-termini of their partner proteins (known as PDZ binding motifs). The PDZ superfamily includes canonical PDZ domains and as well as those with circular permutations and domain swapping of beta-strands. The canonical PDZ domain contains six beta-strands A-F and two alpha-helices (alpha-helix 1 and 2); arranged as A, B, C, alpha-helix 1, beta-strands D, E, alpha-helix 2 and beta-strand F. This Deg/HtrA family PDZ domain is a circularly permuted PDZ domain which places beta-strand A at the C-terminus. Another permutation exists in the PDZ superfamily which places both beta-strands A and B on the C-terminus.


Pssm-ID: 467621 [Multi-domain]  Cd Length: 91  Bit Score: 39.58  E-value: 3.60e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25151513 185 PDRHGRFGFNVKGGadqnypVIVSRVAPGSSADKcqPRLNEGDQVLFIDGRDVStmSHDHVVQFIRSARSGlnggelhLT 264
Cdd:cd06779  13 PLLAKELGLPVNRG------VLVAEVIPGSPAAK--AGLKEGDVILSVNGKPVT--SFNDLRAALDTKKPG-------DS 75

                        90
                ....*....|...
gi 25151513 265 IRPNVYRLGEEVD 277
Cdd:cd06779  76 LNLTILRDGKTLT 88
PDZ1-PDZRN4-like cd06715
PDZ domain 1 of PDZ domain-containing RING finger protein 4 (PDZRN4), PDZRN3-B, and related ...
 189-253 5.34e-04

PDZ domain 1 of PDZ domain-containing RING finger protein 4 (PDZRN4), PDZRN3-B, and related domains; PDZ (PSD-95 (Postsynaptic density protein 95), Dlg (Discs large protein), and ZO-1 (Zonula occludens-1)) domain 1 of PDZRN4, PDZRN3-B, and related domains. PDZRN4 (also known as ligand of numb protein X 4, and SEMACAP3-like protein) contains an N-terminal RING domain and two tandem repeat PDZ domains. It is involved in the progression of cancer, including human liver cancer and breast cancer, and may contribute to the tumorigenesis of rectal adenocarcinoma. Danio rerio PDZRN3-B may participate in neurogenesis: the first PDZ domain of Danio rerio Pdzrn3 interacts with Kidins220 (Kinase D-interacting substrate 220 kD, also named Ankyrin Repeat-Rich Membrane Spanning), a crucial mediator of signal transduction in neural tissues. 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 PDZRN4-like family PDZ1 domain is a canonical PDZ domain containing six beta-strands A-F and two alpha-helices (alpha-helix 1 and 2), arranged in the order: beta-strands A, B, C, alpha-helix 1, beta-strands D, E, alpha-helix 2 and beta-strand F.


Pssm-ID: 467199 [Multi-domain]  Cd Length: 92  Bit Score: 39.30  E-value: 5.34e-04
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 25151513 189 GRFGFNVKGG--------ADQNYPVIVSRVAPGSSADKcQPRLNEGDQVLFIDGRDVSTMSHDHVVQFIRSAR 253
Cdd:cd06715  12 GSLGFNIIGGrpcennqeGSSSEGIYVSKIVENGPAAD-EGGLQVHDRIIEVNGKDLSKATHEEAVEAFRTAK 83
PDZ_MPP-like cd06726
PDZ domain of membrane palmitoylated proteins (MPPs), and related domains; PDZ (PSD-95 ...
 179-267 5.41e-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: 38.79  E-value: 5.41e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25151513 179 VTIKMRPDRhgrfgfnvkggadqnypVIVSRVAPGSSADKcQPRLNEGDQVLFIDGRDVSTMSHDHVVQFIRSARsglng 258
Cdd:cd06726  15 ATIKMEEDS-----------------VIVARILHGGMAHR-SGLLHVGDEILEINGIPVSGKTVDELQKLLSSLS----- 71


                ....*....
gi 25151513 259 GELHLTIRP 267
Cdd:cd06726  72 GSVTFKLIP 80
PTP-IVa cd14500
protein tyrosine phosphatase type IVA family; Protein tyrosine phosphatases type IVA (PTP-IVa), ...
 472-554 5.98e-04

protein tyrosine phosphatase type IVA family; Protein tyrosine phosphatases type IVA (PTP-IVa), also known as protein-tyrosine phosphatases of regenerating liver (PRLs) constitute a family of small, prenylated phosphatases that are the most oncogenic of all PTPs. They stimulate progression from G1 into S phase during mitosis and enhances cell proliferation, cell motility and invasive activity, and promotes cancer metastasis. They associate with magnesium transporters of the cyclin M (CNNM) family, which results in increased intracellular magnesium levels that promote oncogenic transformation. Vertebrates contain three members: PRL-1, PRL-2, and PRL-3.


Pssm-ID: 350350 [Multi-domain]  Cd Length: 156  Bit Score: 40.67  E-value: 5.98e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25151513 472 RVTQMQYiawPDHGVPddPKH----FIQFVDEVRKARQGSVDPIVVHCSAGIGRTGVLIlmetAACLVESNEPvyPLDIV 547
Cdd:cd14500  60 KVHDWPF---DDGSPP--PDDvvddWLDLLKTRFKEEGKPGACIAVHCVAGLGRAPVLV----AIALIELGMK--PEDAV 128


                ....*..
gi 25151513 548 RTMRDQR 554
Cdd:cd14500 129 EFIRKKR 135
PDZ1_LNX1_2-like cd06677
PDZ domain 1 of human Ligand of Numb protein X 1 (LNX1) and LNX2, and related domains; PDZ ...
 177-265 7.12e-04

PDZ domain 1 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 1 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 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: 467165 [Multi-domain]  Cd Length: 89  Bit Score: 38.77  E-value: 7.12e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25151513 177 QVVTIKM-RPDRHGRFGFNVKGGADQnyP---VIVSRVAPGSSADKcQPRLNEGDQVLFIDGRDVSTMSHDHVVQFIRSA 252
Cdd:cd06677   2 EITTIEIhRSDPYEELGISIVGGNDT--PlinIVIQEVYRDGVIAR-DGRLLPGDQILEVNGVDISNVTHSQARSVLRQP 78

                        90
                ....*....|...
gi 25151513 253 RSglnggELHLTI 265
Cdd:cd06677  79 CP-----VLRLTV 86
PDZ1_ZO1-like cd06727
PDZ domain 1 of Zonula Occludens-1 (ZO-1), homologs ZO-2 and ZO-3, and related domains; PDZ ...
 191-266 7.35e-04

PDZ domain 1 of Zonula Occludens-1 (ZO-1), homologs ZO-2 and ZO-3, and related domains; PDZ (PSD-95 (Postsynaptic density protein 95), Dlg (Discs large protein), and ZO-1 (Zonula occludens-1)) domain 1 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 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: 467209 [Multi-domain]  Cd Length: 87  Bit Score: 38.79  E-value: 7.35e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25151513 191 FGFNVKGGADQNYP------VIVSRVAPGSSADKcqpRLNEGDQVLFIDGRDVSTMSHDHVVQFIRSArsglnGGELHLT 264
Cdd:cd06727  13 FGIAVSGGRDNPHFqsgdtsIVISDVLKGGPAEG---KLQENDRVVSVNGVSMENVEHSFAVQILRKC-----GKTANIT 84


                ..
gi 25151513 265 IR 266
Cdd:cd06727  85 VK 86
DSP_DUSP11 cd17665
dual-specificity phosphatase domain of dual specificity protein phosphatase 11 and similar ...
 475-526 8.61e-04

dual-specificity phosphatase domain of dual specificity protein phosphatase 11 and similar proteins; dual specificity protein phosphatase 11 (DUSP11), also known as RNA/RNP complex-1-interacting phosphatase or phosphatase that interacts with RNA/RNP complex 1 (PIR1), has RNA 5'-triphosphatase and diphosphatase activity, but only poor protein-tyrosine phosphatase activity. It has activity for short RNAs but is less active toward mononucleotide triphosphates, suggesting that its primary function in vivo is to dephosphorylate RNA 5'-ends. It may play a role in nuclear mRNA metabolism. Also included in this subfamily is baculovirus RNA 5'-triphosphatase for Autographa californica nuclear polyhedrosis virus.


Pssm-ID: 350503  Cd Length: 169  Bit Score: 40.34  E-value: 8.61e-04
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....
gi 25151513 475 QMQYIAWPDHGVPDDP--KHFIQFVDEVRKARQGSVDPIVVHCSAGIGRTGVLI 526
Cdd:cd17665  78 YYKKITCPGHQVPDDKtiQSFKDAVKDFLEKNKDNDKLIGVHCTHGLNRTGYLI 131
DUSP26 cd14578
dual specificity protein phosphatase 26; Dual specificity protein phosphatase 26 (DUSP26), ...
 428-557 1.01e-03

dual specificity protein phosphatase 26; Dual specificity protein phosphatase 26 (DUSP26), also called mitogen-activated protein kinase (MAPK) phosphatase 8 (MKP-8) or low-molecular-mass dual-specificity phosphatase 4 (LDP-4), functions as a protein-serine/threonine phosphatase (EC 3.1.3.16) and a protein-tyrosine-phosphatase (EC 3.1.3.48). It deactivates its MAPK substrates by dephosphorylating the threonine and tyrosine residues in the conserved Thr-Xaa-Tyr motif residing in their activation sites. DUSP26 is an atypical DUSP; it contains the catalytic dual specificity phosphatase domain but lacks the N-terminal Cdc25/rhodanese-like domain that is present in typical DUSPs or MKPs. It is a brain phosphatase highly overexpressed in neuroblastoma and has also been identified as a p53 phosphatase, dephosphorylating phospho-Ser20 and phospho-Ser37 in the p53 transactivation domain.


Pssm-ID: 350426 [Multi-domain]  Cd Length: 144  Bit Score: 39.82  E-value: 1.01e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25151513 428 QYWPRVF--------ETQEYGRLMIKCIkdkqtTNCCYREFsirdRNSSEERRVTQMQYIAWPDHGVP--DDPKHFIQFV 497
Cdd:cd14578   3 EVWPGLYlgdqdiaaNRRELRRLGITHI-----LNASHSKW----RGGAEYYEGLNIRYLGIEAHDSPafDMSIHFYPAA 73

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|
gi 25151513 498 DEVRKARQGSVDPIVVHCSAGIGRTGVLILmetAACLVESNEPVypLDIVRTMRDQRAML 557
Cdd:cd14578  74 DFIHRALSQPGGKILVHCAVGVSRSATLVL---AYLMIHHHMTL--VEAIKTVKDHRGII 128
PTP_VSP_TPTE cd14510
protein tyrosine phosphatase-like catalytic domain of voltage-sensitive phosphatase ...
 482-567 1.03e-03

protein tyrosine phosphatase-like catalytic domain of voltage-sensitive phosphatase/transmembrane phosphatase with tensin homology; Voltage-sensitive phosphatase (VSP) proteins comprise a family of phosphoinositide phosphatases with substrates that include phosphatidylinositol-4,5-diphosphate and phosphatidylinositol-3,4,5-trisphosphate. This family is conserved in deuterostomes; VSP was first identified as a sperm flagellar plasma membrane protein in Ciona intestinalis. Gene duplication events in primates resulted in the presence of paralogs, transmembrane phosphatase with tensin homology (TPTE) and TPTE2, that retain protein domain architecture but, in the case of TPTE, have lost catalytic activity. TPTE, also called cancer/testis antigen 44 (CT44), may play a role in the signal transduction pathways of the endocrine or spermatogenic function of the testis. TPTE2, also called TPTE and PTEN homologous inositol lipid phosphatase (TPIP), occurs in several differentially spliced forms; TPIP alpha displays phosphoinositide 3-phosphatase activity and is localized on the endoplasmic reticulum, while TPIP beta is cytosolic and lacks detectable phosphatase activity. VSP/TPTE proteins contain an N-terminal voltage sensor consisting of four transmembrane segments, a protein tyrosine phosphatase (PTP)-like phosphoinositide phosphatase catalytic domain, followed by a regulatory C2 domain.


Pssm-ID: 350360 [Multi-domain]  Cd Length: 177  Bit Score: 40.42  E-value: 1.03e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25151513 482 PDHGVPDDPKHFIqFVDEVRK-ARQGSVDPIVVHCSAGIGRTGVLI---LMETAAC--LVESnepvypLDIVRTMRDQRA 555
Cdd:cd14510  82 DDHNVPTLDEMLS-FTAEVREwMAADPKNVVAIHCKGGKGRTGTMVcawLIYSGQFesAKEA------LEYFGERRTDKS 154

                        90
                ....*....|....*..
gi 25151513 556 ML-----IQTPGQYTFV 567
Cdd:cd14510 155 VSskfqgVETPSQSRYV 171
PDZ9_MUPP1-like cd10817
PDZ domain 9 of multi-PDZ-domain protein 1 (MUPP1) and related domains; PDZ (PSD-95 ...
 189-266 1.20e-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: 38.10  E-value: 1.20e-03
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 25151513 189 GRFGFNVKGGADQNyPVIVSRVAPGSSADKCQpRLNEGDQVLFIDGRDVSTMSHDHVVQFIRSARsglngGELHLTIR 266
Cdd:cd10817   9 GGLGIAISEEDTEN-GIVIKSLTEGGPAAKDG-RLKVGDQILAVDDESVVGCPYEKAISLLKTAK-----GTVKLTVS 79
PDZ1_DLG5-like cd06764
PDZ domain 1 of Discs Large 5 (Dlg5) and related domains; PDZ (PSD-95 (Postsynaptic density ...
 191-266 1.25e-03

PDZ domain 1 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 1 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 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: 467245 [Multi-domain]  Cd Length: 95  Bit Score: 38.53  E-value: 1.25e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25151513 191 FGFNVKGGADQ-----NYPVIVSRVAPGSSADKcqpRLNEGDQVLFIDGRDVSTMSHDHVVQFIRSarsglNGGELHLTI 265
Cdd:cd06764  21 LGFDIAGGVNDpqfpgDCSIFVTKVDKGSIADG---RLRVNDCLLRINDVDLTNKDKKQAIQAVLN-----GGGVINMVV 92


                .
gi 25151513 266 R 266
Cdd:cd06764  93 R 93
TpbA-like cd14529
bacterial protein tyrosine and dual-specificity phosphatases related to Pseudomonas aeruginosa ...
 463-529 1.33e-03

bacterial protein tyrosine and dual-specificity phosphatases related to Pseudomonas aeruginosa TpbA; This subfamily contains bacterial protein tyrosine phosphatases (PTPs) and dual-specificity phosphatases (DUSPs) related to Pseudomonas aeruginosa TpbA, a DUSP that negatively regulates biofilm formation by converting extracellular quorum sensing signals and to Mycobacterium tuberculosis PtpB, a PTP virulence factor that attenuates host immune defenses by interfering with signal transduction pathways in macrophages. PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides, while DUSPs function as protein-serine/threonine phosphatases (EC 3.1.3.16) and PTPs.


Pssm-ID: 350378 [Multi-domain]  Cd Length: 158  Bit Score: 39.66  E-value: 1.33e-03
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 25151513 463 RDRNSSEERRVTQMQYIAWPDHGV---PDDPKHFIQFVDevRKARQGsvdPIVVHCSAGIGRTGV---LILME 529
Cdd:cd14529  46 RAASEEAAAKIDGVKYVNLPLSATrptESDVQSFLLIMD--LKLAPG---PVLIHCKHGKDRTGLvsaLYRIV 113
PTZ00242 PTZ00242
protein tyrosine phosphatase; Provisional
 481-554 1.42e-03

protein tyrosine phosphatase; Provisional


Pssm-ID: 185524 [Multi-domain]  Cd Length: 166  Bit Score: 39.62  E-value: 1.42e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25151513  481 WP--DHGVPddPKH----FIQFVDEVrKARQGSVDP-IVVHCSAGIGRTGVLIlmetAACLVESNEpVYPLDIVRTMRDQ 553
Cdd:PTZ00242  67 WPfdDGAPP--PKAvidnWLRLLDQE-FAKQSTPPEtIAVHCVAGLGRAPILV----ALALVEYGG-MEPLDAVGFVREK 138


                 .
gi 25151513  554 R 554
Cdd:PTZ00242 139 R 139
PDZ11_MUPP1-PDZ9_PATJ-like cd06674
PDZ domain 11 of MUPP1 of multi-PDZ-domain protein 1 (MUPP1), domain 9 of PATJ ...
 205-265 1.60e-03

PDZ domain 11 of MUPP1 of multi-PDZ-domain protein 1 (MUPP1), domain 9 of 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 11 of MUPP1, PDZ domain 9 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 family PDZ11 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: 467162 [Multi-domain]  Cd Length: 87  Bit Score: 37.65  E-value: 1.60e-03
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 25151513 205 VIVSRVAPGSSADKCQpRLNEGDQVLFIDGRDVSTMSHDHVVQFIRSARsglngGELHLTI 265
Cdd:cd06674  29 VFVSDIVKGGAADADG-RLMQGDQILSVNGEDVRNASQEAAAALLKCAQ-----GKVRLEV 83
PDZ1_syntenin-like cd06721
PDZ domain 1 of syntenin-1, syntenin-2, and related domains; PDZ (PSD-95 (Postsynaptic density ...
 186-266 1.65e-03

PDZ domain 1 of syntenin-1, syntenin-2, and related domains; PDZ (PSD-95 (Postsynaptic density protein 95), Dlg (Discs large protein), and ZO-1 (Zonula occludens-1)) domain 1 of syntenin-1, syntenin-2, and related domains. Syntenins are implicated in various cellular processes such as trafficking, signaling, and cancer metastasis. They bind to signaling and adhesion molecules, such as syndecans, neurexins, ephrin B, and phospholipid PIP2. Through its tandem PDZ domains (PDZ1 and PDZ2), syntenin links syndecans to other cell surface receptors and kinases, such as E-cadherin and ephrin-B, establishing signaling crosstalk. During syndecan binding, syntenin PDZ2 serves as a high-affinity domain, and PDZ1, also necessary for binding, acts as a complementary, low-affinity domain; this is also the case for syntenin binding to proto-oncogene c-Src. The syntenin PDZ domain-PIP2 interaction controls Arf6-mediated syndecan recycling through endosomal compartments; both PDZ1 and PDZ2 interact with PIP2. Different binding partners and downstream regulators of syntenin1 PDZ domains, such as to proto-oncogene c-Src, mitogen-activated protein kinase (MAPK), and focal adhesion kinase (FAK), have been identified that promote the progression and invasion of a variety of cancers, such as melanoma, glioblastoma multiforme and breast 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 syntenin-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: 467204 [Multi-domain]  Cd Length: 79  Bit Score: 37.60  E-value: 1.65e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25151513 186 DRHGRFGFNVKggaDQNYPVIVSRVAPGSSADKCQPRLneGDQVLFIDGRDVSTMSHDHVVQFIRSArsglNGGELHLTI 265
Cdd:cd06721   8 DQDGKIGLRVK---SIDKGVFVQLVQANSPAALAGLRF--GDQILQINGENVAGWSSDKAHKVLKKA----SPERITLAV 78


                .
gi 25151513 266 R 266
Cdd:cd06721  79 R 79
PDZ_nNOS-like cd06708
PDZ domain of neuronal nitric oxide synthase (nNOS), and related domains; PDZ (PSD-95 ...
 178-255 1.89e-03

PDZ domain of neuronal nitric oxide synthase (nNOS), and related domains; PDZ (PSD-95 (Postsynaptic density protein 95), Dlg (Discs large protein), and ZO-1 (Zonula occludens-1)) domain 1 of nNOS, and related domains. nNOS produces a key signaling molecule, nitric oxide (NO), which has diverse functions throughout the body and acts as a neurotransmitter and intracellular signaling molecule in the central and peripheral nervous system. nNOS is concentrated at synaptic junctions in the brain and motor endplates in skeletal muscle. The PDZ domain of neuronal nitric oxide synthase (nNOS) interacts with the PDZ domain of alpha1-syntrophin (in muscle cells) and with the second PDZ domain of Disks large homolog 4 (Dlg4, also known as PSD-95), and nitric oxide synthase 1 adaptor protein NOS1AP in neurons. Dlg4 binds NMDA receptors, and nNOS, forming a complex in neurons. NOS1AP competes with Dgl4 for the nNOS PDZ domain and prevents the coupling of nNos activation with NMDA receptor-mediated calcium influx. 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 nNOS-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: 467192 [Multi-domain]  Cd Length: 110  Bit Score: 38.13  E-value: 1.89e-03
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 25151513 178 VVTIKMRPDRHGRFGFNVKGGAdQNYPVIVSRVAPGSSADKCQpRLNEGDQVLFIDGRDVSTMSHDHVVQFIRSARSG 255
Cdd:cd06708   2 VISVRLFKRKVGGLGFLVKQRV-CKPPVIISDLIRGGAAEQSG-LVQVGDIILAVNGRPLVDVSYESALEVLRSIPSE 77
PDZ2-PDZRN4-like cd06716
PDZ domain 2 of PDZ domain-containing RING finger protein 4 (PDZRN4), PDZRN3-B, and related ...
 179-242 2.82e-03

PDZ domain 2 of PDZ domain-containing RING finger protein 4 (PDZRN4), PDZRN3-B, and related domains; PDZ (PSD-95 (Postsynaptic density protein 95), Dlg (Discs large protein), and ZO-1 (Zonula occludens-1)) domain 1 of PDZRN4, PDZRN3-B, and related domains. PDZRN4 (also known as ligand of numb protein X 4, and SEMACAP3-like protein) contains an N-terminal RING domain and two tandem repeat PDZ domains. It is involved in the progression of cancer, including human liver cancer and breast cancer, and may contribute to the tumorigenesis of rectal adenocarcinoma. Danio rerio PDZRN3-B may participate in neurogenesis: the first PDZ domain of Danio rerio Pdzrn3 interacts with Kidins220 (Kinase D-interacting substrate 220 kD, also named Ankyrin Repeat-Rich Membrane Spanning), a crucial mediator of signal transduction in neural tissues. 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 PDZRN4-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: 467200 [Multi-domain]  Cd Length: 88  Bit Score: 37.25  E-value: 2.82e-03
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 25151513 179 VTIKmRPDRHGRFGFNVKGGAD--QNYPVIVSRVAPGSSADKCQpRLNEGDQVLFIDGRDVSTMSH 242
Cdd:cd06716   6 VTLK-RSNSQEKLGLTLCYRTDdeEDTGIYVSEVDPNSIAAKDG-RIREGDQILQINGVDVQNREE 69
DegQ COG0265
Periplasmic serine protease, S1-C subfamily, contain C-terminal PDZ domain [Posttranslational ...
 198-277 2.89e-03

Periplasmic serine protease, S1-C subfamily, contain C-terminal PDZ domain [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 440035 [Multi-domain]  Cd Length: 274  Bit Score: 39.75  E-value: 2.89e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25151513 198 GADQNYPVIVSRVAPGSSADKCqpRLNEGDQVLFIDGRDVSTMshDHVVQFIRSARSglnGGELHLTirpnVYRLGEEVD 277
Cdd:COG0265 196 GLPEPEGVLVARVEPGSPAAKA--GLRPGDVILAVDGKPVTSA--RDLQRLLASLKP---GDTVTLT----VLRGGKELT 264
PDZ4_INAD-like cd23065
PDZ domain 4 of inactivation-no-after-potential D (INAD), and related domains; PDZ (PSD-95 ...
 180-247 4.64e-03

PDZ domain 4 of inactivation-no-after-potential D (INAD), and related domains; PDZ (PSD-95 (Postsynaptic density protein 95), Dlg (Discs large protein), and ZO-1 (Zonula occludens-1)) domain 4 of INAD, and related domains. INAD assembles key enzymes of the Drosophila compound eye photo-transduction pathway into a supramolecular complex, supporting efficient and fast light signaling. It contains 5 PDZ domains arranged in tandem (PDZ1-PDZ5) which independently bind various proteins. INAD PDZ2 binds eye-specific protein kinase C, INAD PDZ3 binds transient receptor potential (TRP) channel, and INAD PDZ4,5 tandem binds NORPA (phospholipase Cbeta, PLCbeta). Mutations of the inaD gene that lead to disruption of each of these interactions impair fly photo signal transduction. 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 INAD-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: 467278 [Multi-domain]  Cd Length: 82  Bit Score: 36.34  E-value: 4.64e-03
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 25151513 180 TIKMRPDRhGRFGFNVKGGADQ-NYPVIVSRVAPGSSADKcQPRLNEGDQVLFIDGRDVSTMSHDHVVQ 247
Cdd:cd23065   1 TIELKTDK-SPLGVSVVGGKNHvTTGCIITHIYPNSIVAA-DKRLKVFDQILDINGTKVHVMTTLKVHQ 67
PDZ2_APBA1_3-like cd06793
PDZ domain 2 of amyloid-beta A4 precursor protein-binding family A member 1 (APBA1), APBA2, ...
 178-267 4.71e-03

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


Pssm-ID: 467255 [Multi-domain]  Cd Length: 78  Bit Score: 36.22  E-value: 4.71e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25151513 178 VVTIK-MRPDRHGRFGFNVKGGadqnypVIVSrVAPGSSADKCQPRLneGDQVLFIDGRDVSTMSHDHVVQFIRSARsgl 256
Cdd:cd06793   2 VTTVLiRRPDLKYQLGFSVQNG------IICS-LLRGGIAERGGVRV--GHRIIEINGQSVVATPHEKIVQLLSNSV--- 69

                        90
                ....*....|.
gi 25151513 257 ngGELHLTIRP 267
Cdd:cd06793  70 --GEIHMKTMP 78
PDZ13_MUPP1-like cd06676
PDZ domain 13 of multi-PDZ-domain protein 1 (MUPP1) and related domains; PDZ (PSD-95 ...
 192-265 5.10e-03

PDZ domain 13 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 13 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 PDZ13 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 PDZ13 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: 467164 [Multi-domain]  Cd Length: 83  Bit Score: 36.16  E-value: 5.10e-03
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 25151513 192 GFNVKGGADQ---NYPVIVSRVAPGSSADKCQpRLNEGDQVLFIDGRDVSTMSHDHVVQFIRSARsglngGELHLTI 265
Cdd:cd06676  12 GFSIVGGFGSphgDLPIYVKTVFEKGAAAEDG-RLKRGDQILAVNGESLEGVTHEEAVNILKKTK-----GTVTLTV 82
PTP_PTEN-like cd14497
protein tyrosine phosphatase-like domain of phosphatase and tensin homolog and similar ...
 481-526 6.43e-03

protein tyrosine phosphatase-like domain of phosphatase and tensin homolog and similar proteins; Phosphatase and tensin homolog (PTEN) is a tumor suppressor that acts as a dual-specificity protein phosphatase and as a lipid phosphatase. It dephosphorylates phosphoinositide trisphosphate. In addition to PTEN, this family includes tensins, voltage-sensitive phosphatases (VSPs), and auxilins. They all contain a protein tyrosine phosphatase-like domain although not all are active phosphatases. Tensins are intracellular proteins that act as links between the extracellular matrix and the cytoskeleton, and thereby mediate signaling for cell shape and motility, and they may or may not have phosphatase activity. VSPs are phosphoinositide phosphatases with substrates that include phosphatidylinositol-4,5-diphosphate and phosphatidylinositol-3,4,5-trisphosphate. Auxilins are J domain-containing proteins that facilitate Hsc70-mediated dissociation of clathrin from clathrin-coated vesicles, and they do not exhibit phosphatase activity.


Pssm-ID: 350347 [Multi-domain]  Cd Length: 160  Bit Score: 37.56  E-value: 6.43e-03
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|
gi 25151513 481 WPDHGVPddPKHFIQ-FVDEVRKarQGSVDP---IVVHCSAGIGRTGVLI 526
Cdd:cd14497  68 FPDHHPP--PLGLLLeIVDDIDS--WLSEDPnnvAVVHCKAGKGRTGTVI 113
PDZ2_Par3-like cd23058
PDZ domain 2 of partitioning defective 3 (Par3), and related domains; PDZ (PSD-95 ...
 199-255 6.90e-03

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: 36.08  E-value: 6.90e-03
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....*..
gi 25151513 199 ADQNYPVIVSRVAPGSSADKcQPRLNEGDQVLFIDGRDVSTMSHDHVVQFIRSARSG 255
Cdd:cd23058  28 TGGSGPIYIKNILPKGAAIQ-DGRLKAGDRLLEVNGVDVTGKTQEEVVSLLRSTKLG 83
PDZ3_harmonin cd06739
PDZ domain 3 of harmonin isoforms a and b, and related domains; PDZ (PSD-95 (Postsynaptic ...
 177-265 7.71e-03

PDZ domain 3 of harmonin isoforms a and b, and related domains; PDZ (PSD-95 (Postsynaptic density protein 95), Dlg (Discs large protein), and ZO-1 (Zonula occludens-1)) domain 3 of harmonin isoforms a and b, 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 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: 467221 [Multi-domain]  Cd Length: 94  Bit Score: 36.13  E-value: 7.71e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25151513 177 QVVTIKmrpdRHGRFGFNVKGGADQnyP----VIVSRVAPGSSADKcQPRLNEGDQVLFIDGRDVSTMSHDHVVQFIRSA 252
Cdd:cd06739   4 RLLRIK----KNGPLDLALEGGIDS--PlggkIVVSAVYEGGAADK-HGGIVKGDQIMMVNGKSLTDVTLAEAEAALQRA 76

                        90
                ....*....|...
gi 25151513 253 rSGLNGGELHLTI 265
Cdd:cd06739  77 -MNSGGDWIDLVI 88
RseP COG0750
Membrane-associated protease RseP, regulator of RpoE activity [Posttranslational modification, ...
 198-317 7.73e-03

Membrane-associated protease RseP, regulator of RpoE activity [Posttranslational modification, protein turnover, chaperones, Transcription];


Pssm-ID: 440513 [Multi-domain]  Cd Length: 349  Bit Score: 38.91  E-value: 7.73e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25151513 198 GADQNYPVIVSRVAPGSSADKCQprLNEGDQVLFIDGRDVSTMshDHVVQFIRSA----------RsglNGGELHLTIRP 267
Cdd:COG0750 123 GVPVLTPPVVGEVVPGSPAAKAG--LQPGDRIVAINGQPVTSW--DDLVDIIRASpgkpltltveR---DGEELTLTVTP 195

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*..
gi 25151513 268 ------NVYRLGeeVdEPDSTMVPEPARVADSVPNSdkLSKSLQLLADSLNS-GKVV 317
Cdd:COG0750 196 rlveedGVGRIG--V-SPSGEVVTVRYGPLEALGAG--VKETWDMIVLTLKGlGKLI 247
PDZ1_GRIP1-2-like cd06687
PDZ domain 1 of glutamate receptor-interacting protein 1 (GRIP1) and GRIP2, and related ...
 191-252 8.92e-03

PDZ domain 1 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 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: 467175 [Multi-domain]  Cd Length: 83  Bit Score: 35.46  E-value: 8.92e-03
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 25151513 191 FGFNVKGGADQNYPVIVSRVAPGSSADKCQpRLNEGDQVLFIDGRDVSTMSHDHVVQFIRSA 252
Cdd:cd06687  13 LGLTVSGGIDKDGKPRVSNLRPGGIAARSD-QLNVGDYIKSVNGIRTTKLRHDEIISLLKNV 73
Oca4 COG2365
Protein tyrosine/serine phosphatase Oca4 [Signal transduction mechanisms];
462-528 9.91e-03

Protein tyrosine/serine phosphatase Oca4 [Signal transduction mechanisms];


Pssm-ID: 441932 [Multi-domain]  Cd Length: 248  Bit Score: 38.02  E-value: 9.91e-03
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 25151513 462 IRDRNSSEERRVTQMQ--YIAWPDhgvPDDPKHFIQFVDEVRKARQGsvdPIVVHCSAGIGRTGV---LILM 528
Cdd:COG2365  91 LRDGDLTPGDAEEFMLelYRAFVD---PDAADAYRAAFRALADAENG---PVLFHCTAGKDRTGVaaaLLLL 156
 
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.
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