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Conserved domains on  [gi|1720354236|ref|XP_030108159|]
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tyrosine-protein phosphatase non-receptor type 4 isoform X4 [Mus musculus]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
PTP_DSP_cys super family cl28904
cys-based protein tyrosine phosphatase and dual-specificity phosphatase superfamily; This ...
 405-678 4.35e-175

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.


The actual alignment was detected with superfamily member cd14600:

Pssm-ID: 475123 [Multi-domain]  Cd Length: 274  Bit Score: 500.15  E-value: 4.35e-175
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720354236 405 ESMIQLAEGLITGTVLAQFDQLYRKKPGMTMSCAKLPQNISKNRYRDISPYDATRVLLKGNEDYINANYINMEIPSSSII 484
Cdd:cd14600     2 ESMAQLKKGLESGTVLIQFEQLYRKKPGLAITCAKLPQNMDKNRYKDVLPYDATRVVLQGNEDYINASYVNMEIPSANIV 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720354236 485 NQYIACQGPLPHTCKDFWQMTWEQGSSMVVMLTTQVERGRVKCHQYWPEPSESSSYGCYQVTCHSEEGNPAYIFRKMTLF 564
Cdd:cd14600    82 NKYIATQGPLPHTCAQFWQVVWEQKLSLIVMLTTLTERGRTKCHQYWPDPPDVMEYGGFRVQCHSEDCTIAYVFREMLLT 161

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720354236 565 NQEKNESRQLTQIQYTAWPDHGVPDDSSDFLDFVCHVRDQRAgKEEPIIVHCSAGIGRTGVLITMETAMCLIECNQPVYP 644
Cdd:cd14600   162 NTQTGEERTVTHLQYVAWPDHGVPDDSSDFLEFVNYVRSKRV-ENEPVLVHCSAGIGRTGVLVTMETAMCLTERNQPVYP 240

                         250       260       270
                  ....*....|....*....|....*....|....
gi 1720354236 645 LDIVRTMRDQRAMMIQTPSQYRFVCEAILKVYEE 678
Cdd:cd14600   241 LDIVRKMRDQRAMMVQTSSQYKFVCEAILRVYEE 274
PDZ_PTPN3-4-like cd06706
PDZ domain of tyrosine-protein phosphatase non-receptor type 3 (PTPN3), tyrosine-protein ...
 277-366 4.38e-62

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: 201.39  E-value: 4.38e-62
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720354236 277 DNLVLIKMKPDENGRFGFNVKGGYDQKMPVIVSRVAPGTPADLCVPRLNEGDQVVLINGRDIAEHTHDQVVLFIKASCEK 356
Cdd:cd06706     1 DGLVLIRMKPDENGRFGFNVKGGVDQKMPVIVSRVAPGTPADLCIPRLNEGDQVLLINGRDISEHTHDQVVMFIKASRER 80

                          90
                  ....*....|
gi 1720354236 357 HSGELVLLVR 366
Cdd:cd06706    81 HSGELVLLVR 90
PH-like super family cl17171
Pleckstrin homology-like domain; The PH-like family includes the PH domain, both the Shc-like ...
 1-74 6.86e-46

Pleckstrin homology-like domain; The PH-like family includes the PH domain, both the Shc-like and IRS-like PTB domains, the ran-binding domain, the EVH1 domain, a domain in neurobeachin and the third domain of FERM. All of these domains have a PH fold, but lack significant sequence similarity. They are generally involved in targeting to protein to the appropriate cellular location or interacting with a binding partner. This domain family possesses multiple functions including the ability to bind inositol phosphates and to other proteins.


The actual alignment was detected with superfamily member cd13189:

Pssm-ID: 473070  Cd Length: 95  Bit Score: 157.86  E-value: 6.86e-46
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1720354236   1 MSGGILIYKNRVRMNTFLWLKIVKISFKCKQFFIQLRKELHESRETLLGFNMVNYRACKTLWKACVEHHTFFRL 74
Cdd:cd13189    22 SSAGILVFQNGIRINTFPWSKIVKISFKRKQFFIQLRREPNESRDTILGFNMLSYRACKNLWKSCVEHHTFFRL 95
FA pfam08736
FERM adjacent (FA); This region is found adjacent to Band 4.1 / FERM domains (pfam00373) in a ...
 88-129 1.91e-12

FERM adjacent (FA); This region is found adjacent to Band 4.1 / FERM domains (pfam00373) in a subset of FERM containing protein. The region has been hypothesized to play a role in regulatory adaptation, based on similarity to other protein kinase substrates.


:

Pssm-ID: 462582  Cd Length: 44  Bit Score: 61.80  E-value: 1.91e-12
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|..
gi 1720354236  88 YFTLGSKFRYCGRTEVQSVQYGKEKANKDRVFARSPSKPLAR 129
Cdd:pfam08736   2 FFSLGSKFRYSGRTQKQTVEDSSEILRPQPEFERSPSKRYPS 43
 
Name Accession Description Interval E-value
PTPc-N3 cd14600
catalytic domain of tyrosine-protein phosphatase non-receptor type 3; Tyrosine-protein ...
 405-678 4.35e-175

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: 500.15  E-value: 4.35e-175
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720354236 405 ESMIQLAEGLITGTVLAQFDQLYRKKPGMTMSCAKLPQNISKNRYRDISPYDATRVLLKGNEDYINANYINMEIPSSSII 484
Cdd:cd14600     2 ESMAQLKKGLESGTVLIQFEQLYRKKPGLAITCAKLPQNMDKNRYKDVLPYDATRVVLQGNEDYINASYVNMEIPSANIV 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720354236 485 NQYIACQGPLPHTCKDFWQMTWEQGSSMVVMLTTQVERGRVKCHQYWPEPSESSSYGCYQVTCHSEEGNPAYIFRKMTLF 564
Cdd:cd14600    82 NKYIATQGPLPHTCAQFWQVVWEQKLSLIVMLTTLTERGRTKCHQYWPDPPDVMEYGGFRVQCHSEDCTIAYVFREMLLT 161

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720354236 565 NQEKNESRQLTQIQYTAWPDHGVPDDSSDFLDFVCHVRDQRAgKEEPIIVHCSAGIGRTGVLITMETAMCLIECNQPVYP 644
Cdd:cd14600   162 NTQTGEERTVTHLQYVAWPDHGVPDDSSDFLEFVNYVRSKRV-ENEPVLVHCSAGIGRTGVLVTMETAMCLTERNQPVYP 240

                         250       260       270
                  ....*....|....*....|....*....|....
gi 1720354236 645 LDIVRTMRDQRAMMIQTPSQYRFVCEAILKVYEE 678
Cdd:cd14600   241 LDIVRKMRDQRAMMVQTSSQYKFVCEAILRVYEE 274
PTPc smart00194
Protein tyrosine phosphatase, catalytic domain;
421-674 8.28e-113

Protein tyrosine phosphatase, catalytic domain;


Pssm-ID: 214550 [Multi-domain]  Cd Length: 259  Bit Score: 340.41  E-value: 8.28e-113
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720354236  421 AQFDQLYRKKPGM-TMSCAKLPQNISKNRYRDISPYDATRVLLKGNE----DYINANYINMEIPSssiiNQYIACQGPLP 495
Cdd:smart00194   4 EEFEKLDRLKPDDeSCTVAAFPENRDKNRYKDVLPYDHTRVKLKPPPgegsDYINASYIDGPNGP----KAYIATQGPLP 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720354236  496 HTCKDFWQMTWEQGSSMVVMLTTQVERGRVKCHQYWP-EPSESSSYGCYQVTCHSEEGNPAYIFRKMTLFNQEKNESRQL 574
Cdd:smart00194  80 STVEDFWRMVWEQKVTVIVMLTELVEKGREKCAQYWPdEEGEPLTYGDITVTLKSVEKVDDYTIRTLEVTNTGCSETRTV 159

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720354236  575 TQIQYTAWPDHGVPDDSSDFLDFVCHVRDQRAGKEEPIIVHCSAGIGRTGVLITMETAMCLIECNQPVYPLDIVRTMRDQ 654
Cdd:smart00194 160 THYHYTNWPDHGVPESPESILDLIRAVRKSQSTSTGPIVVHCSAGVGRTGTFIAIDILLQQLEAGKEVDIFEIVKELRSQ 239

                          250       260
                   ....*....|....*....|
gi 1720354236  655 RAMMIQTPSQYRFVCEAILK 674
Cdd:smart00194 240 RPGMVQTEEQYIFLYRAILE 259
Y_phosphatase pfam00102
Protein-tyrosine phosphatase;
443-674 2.34e-107

Protein-tyrosine phosphatase;


Pssm-ID: 459674 [Multi-domain]  Cd Length: 234  Bit Score: 325.35  E-value: 2.34e-107
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720354236 443 NISKNRYRDISPYDATRVLLK---GNEDYINANYInmeiPSSSIINQYIACQGPLPHTCKDFWQMTWEQGSSMVVMLTTQ 519
Cdd:pfam00102   1 NLEKNRYKDVLPYDHTRVKLTgdpGPSDYINASYI----DGYKKPKKYIATQGPLPNTVEDFWRMVWEEKVTIIVMLTEL 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720354236 520 VERGRVKCHQYWPEPSESS-SYGCYQVTCHSEEGN-PAYIFRKMTLFNQEKNESRQLTQIQYTAWPDHGVPDDSSDFLDF 597
Cdd:pfam00102  77 EEKGREKCAQYWPEEEGESlEYGDFTVTLKKEKEDeKDYTVRTLEVSNGGSEETRTVKHFHYTGWPDHGVPESPNSLLDL 156

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1720354236 598 VCHVRD-QRAGKEEPIIVHCSAGIGRTGVLITMETAMCLIECNQPVYPLDIVRTMRDQRAMMIQTPSQYRFVCEAILK 674
Cdd:pfam00102 157 LRKVRKsSLDGRSGPIVVHCSAGIGRTGTFIAIDIALQQLEAEGEVDIFQIVKELRSQRPGMVQTLEQYIFLYDAILE 234
PDZ_PTPN3-4-like cd06706
PDZ domain of tyrosine-protein phosphatase non-receptor type 3 (PTPN3), tyrosine-protein ...
 277-366 4.38e-62

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: 201.39  E-value: 4.38e-62
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720354236 277 DNLVLIKMKPDENGRFGFNVKGGYDQKMPVIVSRVAPGTPADLCVPRLNEGDQVVLINGRDIAEHTHDQVVLFIKASCEK 356
Cdd:cd06706     1 DGLVLIRMKPDENGRFGFNVKGGVDQKMPVIVSRVAPGTPADLCIPRLNEGDQVLLINGRDISEHTHDQVVMFIKASRER 80

                          90
                  ....*....|
gi 1720354236 357 HSGELVLLVR 366
Cdd:cd06706    81 HSGELVLLVR 90
FERM_C_PTPN4_PTPN3_like cd13189
FERM domain C-lobe of Protein tyrosine phosphatase non-receptor proteins 3 and 4 (PTPN4 and ...
 1-74 6.86e-46

FERM domain C-lobe of Protein tyrosine phosphatase non-receptor proteins 3 and 4 (PTPN4 and PTPN3); PTPN4 (also called PTPMEG, protein tyrosine phosphatase, megakaryocyte) is a cytoplasmic protein-tyrosine phosphatase (PTP) thought to play a role in cerebellar function. PTPMEG-knockout mice have impaired memory formation and cerebellar long-term depression. PTPN3/PTPH1 is a membrane-associated PTP that is implicated in regulating tyrosine phosphorylation of growth factor receptors, p97 VCP (valosin-containing protein, or Cdc48 in Saccharomyces cerevisiae), and HBV (Hepatitis B Virus) gene expression; it is mutated in a subset of colon cancers. PTPMEG and PTPN3/PTPH1 contains a N-terminal FERM domain, a middle PDZ domain, and a C-terminal phosphatase domain. PTP1/Tyrosine-protein phosphatase 1 from nematodes and a FERM_C repeat 1 from Tetraodon nigroviridis are also included in this cd. The FERM domain has a cloverleaf tripart structure composed of: (1) FERM_N (A-lobe or F1); (2) FERM_M (B-lobe, or F2); and (3) FERM_C (C-lobe or F3). The C-lobe within the FERM domain is part of the PH domain family. The FERM domain is found in the cytoskeletal-associated proteins such as ezrin, moesin, radixin, 4.1R, and merlin. These proteins provide a link between the membrane and cytoskeleton and are involved in signal transduction pathways. The FERM domain is also found in protein tyrosine phosphatases (PTPs) , the tyrosine kinases FAK and JAK, in addition to other proteins involved in signaling. This domain is structurally similar to the PH and PTB domains and consequently is capable of binding to both peptides and phospholipids at different sites.


Pssm-ID: 270010  Cd Length: 95  Bit Score: 157.86  E-value: 6.86e-46
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1720354236   1 MSGGILIYKNRVRMNTFLWLKIVKISFKCKQFFIQLRKELHESRETLLGFNMVNYRACKTLWKACVEHHTFFRL 74
Cdd:cd13189    22 SSAGILVFQNGIRINTFPWSKIVKISFKRKQFFIQLRREPNESRDTILGFNMLSYRACKNLWKSCVEHHTFFRL 95
PHA02738 PHA02738
hypothetical protein; Provisional
 442-676 1.15e-43

hypothetical protein; Provisional


Pssm-ID: 222923 [Multi-domain]  Cd Length: 320  Bit Score: 159.71  E-value: 1.15e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720354236 442 QNISKNRYRDISPYDATRVLL---KGNEDYINANYINmeipSSSIINQYIACQGPLPHTCKDFWQMTWEQGSSMVVMLTT 518
Cdd:PHA02738   48 KNRKLNRYLDAVCFDHSRVILpaeRNRGDYINANYVD----GFEYKKKFICGQAPTRQTCYDFYRMLWMEHVQIIVMLCK 123

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720354236 519 QVERGRVKCHQYWPEPSESS-SYGCYQVTCHSEEGNPAYIfrKMTLFNQEKNESRQ-LTQIQYTAWPDHGVPDDSSDFLD 596
Cdd:PHA02738  124 KKENGREKCFPYWSDVEQGSiRFGKFKITTTQVETHPHYV--KSTLLLTDGTSATQtVTHFNFTAWPDHDVPKNTSEFLN 201

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720354236 597 FVCHVRD-QRAGKEE------------PIIVHCSAGIGRTGVLITMETAMCLIECNQPVYPLDIVRTMRDQRAMMIQTPS 663
Cdd:PHA02738  202 FVLEVRQcQKELAQEslqighnrlqppPIVVHCNAGLGRTPCYCVVDISISRFDACATVSIPSIVSSIRNQRYYSLFIPF 281

                         250
                  ....*....|...
gi 1720354236 664 QYrFVCEAILKVY 676
Cdd:PHA02738  282 QY-FFCYRAVKRY 293
COG5599 COG5599
Protein tyrosine phosphatase [Signal transduction mechanisms];
439-665 1.53e-37

Protein tyrosine phosphatase [Signal transduction mechanisms];


Pssm-ID: 444335 [Multi-domain]  Cd Length: 282  Bit Score: 141.38  E-value: 1.53e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720354236 439 KLPQNISKNRYRDISPYDATRVllKGNEDYINANYINMEIPsssiiNQYIACQGPLPHTCKDFWQMTWEQGSSMVVMLTT 518
Cdd:COG5599    38 QNINGSPLNRFRDIQPYKETAL--RANLGYLNANYIQVIGN-----HRYIATQYPLEEQLEDFFQMLFDNNTPVLVVLAS 110

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720354236 519 QVE--RGRVKCHQYWPEPSESSSYgcyqvTCHSEEGNPAYIFRKMTLFN------QEKNESRQLTQIQYTAWPDHGVPDD 590
Cdd:COG5599   111 DDEisKPKVKMPVYFRQDGEYGKY-----EVSSELTESIQLRDGIEARTyvltikGTGQKKIEIPVLHVKNWPDHGAISA 185

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720354236 591 S--SDFLDFVCHVRDQRAGKEEPIIVHCSAGIGRTGVLITMETAMCLIECNQPVYP--LDIVRTMRDQRAM-MIQTPSQY 665
Cdd:COG5599   186 EalKNLADLIDKKEKIKDPDKLLPVVHCRAGVGRTGTLIACLALSKSINALVQITLsvEEIVIDMRTSRNGgMVQTSEQL 265
FERM_C pfam09380
FERM C-terminal PH-like domain;
1-76 1.00e-28

FERM C-terminal PH-like domain;


Pssm-ID: 462779 [Multi-domain]  Cd Length: 85  Bit Score: 109.65  E-value: 1.00e-28
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1720354236   1 MSGGILIYKNRVRM-NTFLWLKIVKISFKCKQFFIQLRkelHESRETLLGFNMVNYRACKTLWKACVEHHTFFRLDR 76
Cdd:pfam09380  12 SAKGILVYEDNNKIlNLFPWREIRKISFKRKKFLIKLR---DKSSEETLGFYTESSRACKYLWKLCVEQHTFFRLRR 85
PDZ pfam00595
PDZ domain; PDZ domains are found in diverse signaling proteins.
 281-366 1.46e-18

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


Pssm-ID: 395476 [Multi-domain]  Cd Length: 81  Bit Score: 80.40  E-value: 1.46e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720354236 281 LIKMKPDENGRFGFNVKGGYDQK-MPVIVSRVAPGTPADlcVPRLNEGDQVVLINGRDIAEHTHDQVVLFIKAScekhSG 359
Cdd:pfam00595   1 QVTLEKDGRGGLGFSLKGGSDQGdPGIFVSEVLPGGAAE--AGGLKVGDRILSINGQDVENMTHEEAVLALKGS----GG 74


                  ....*..
gi 1720354236 360 ELVLLVR 366
Cdd:pfam00595  75 KVTLTIL 81
PDZ smart00228
Domain present in PSD-95, Dlg, and ZO-1/2; Also called DHR (Dlg homologous region) or GLGF ...
 288-368 2.08e-14

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: 68.94  E-value: 2.08e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720354236  288 ENGRFGFNVKGGYDQKMPVIVSRVAPGTPADLCvpRLNEGDQVVLINGRDIAEHTHDQVVLFIKASCEKhsgeLVLLVRP 367
Cdd:smart00228  10 GGGGLGFSLVGGKDEGGGVVVSSVVPGSPAAKA--GLRVGDVILEVNGTSVEGLTHLEAVDLLKKAGGK----VTLTVLR 83


                   .
gi 1720354236  368 N 368
Cdd:smart00228  84 G 84
FA pfam08736
FERM adjacent (FA); This region is found adjacent to Band 4.1 / FERM domains (pfam00373) in a ...
 88-129 1.91e-12

FERM adjacent (FA); This region is found adjacent to Band 4.1 / FERM domains (pfam00373) in a subset of FERM containing protein. The region has been hypothesized to play a role in regulatory adaptation, based on similarity to other protein kinase substrates.


Pssm-ID: 462582  Cd Length: 44  Bit Score: 61.80  E-value: 1.91e-12
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|..
gi 1720354236  88 YFTLGSKFRYCGRTEVQSVQYGKEKANKDRVFARSPSKPLAR 129
Cdd:pfam08736   2 FFSLGSKFRYSGRTQKQTVEDSSEILRPQPEFERSPSKRYPS 43
CtpA COG0793
C-terminal processing protease CtpA/Prc, contains a PDZ domain [Posttranslational modification, ...
 284-351 4.44e-03

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: 39.85  E-value: 4.44e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1720354236 284 MKPDENGRFG-----FNVKGGYdqkmpVIVSRVAPGTPADLcvPRLNEGDQVVLINGRDIAEHTHDQVVLFIK 351
Cdd:COG0793    51 FQESTSGEFGglgaeLGEEDGK-----VVVVSVIPGSPAEK--AGIKPGDIILAIDGKSVAGLTLDDAVKLLR 116
 
Name Accession Description Interval E-value
PTPc-N3 cd14600
catalytic domain of tyrosine-protein phosphatase non-receptor type 3; Tyrosine-protein ...
 405-678 4.35e-175

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: 500.15  E-value: 4.35e-175
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720354236 405 ESMIQLAEGLITGTVLAQFDQLYRKKPGMTMSCAKLPQNISKNRYRDISPYDATRVLLKGNEDYINANYINMEIPSSSII 484
Cdd:cd14600     2 ESMAQLKKGLESGTVLIQFEQLYRKKPGLAITCAKLPQNMDKNRYKDVLPYDATRVVLQGNEDYINASYVNMEIPSANIV 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720354236 485 NQYIACQGPLPHTCKDFWQMTWEQGSSMVVMLTTQVERGRVKCHQYWPEPSESSSYGCYQVTCHSEEGNPAYIFRKMTLF 564
Cdd:cd14600    82 NKYIATQGPLPHTCAQFWQVVWEQKLSLIVMLTTLTERGRTKCHQYWPDPPDVMEYGGFRVQCHSEDCTIAYVFREMLLT 161

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720354236 565 NQEKNESRQLTQIQYTAWPDHGVPDDSSDFLDFVCHVRDQRAgKEEPIIVHCSAGIGRTGVLITMETAMCLIECNQPVYP 644
Cdd:cd14600   162 NTQTGEERTVTHLQYVAWPDHGVPDDSSDFLEFVNYVRSKRV-ENEPVLVHCSAGIGRTGVLVTMETAMCLTERNQPVYP 240

                         250       260       270
                  ....*....|....*....|....*....|....
gi 1720354236 645 LDIVRTMRDQRAMMIQTPSQYRFVCEAILKVYEE 678
Cdd:cd14600   241 LDIVRKMRDQRAMMVQTSSQYKFVCEAILRVYEE 274
PTPc-N4 cd14601
catalytic domain of tyrosine-protein phosphatase non-receptor type 4; Tyrosine-protein ...
 467-678 1.61e-169

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: 483.68  E-value: 1.61e-169
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720354236 467 DYINANYINMEIPSSSIINQYIACQGPLPHTCKDFWQMTWEQGSSMVVMLTTQVERGRVKCHQYWPEPSESSSYGCYQVT 546
Cdd:cd14601     1 DYINANYINMEIPSSSIINRYIACQGPLPNTCSDFWQMTWEQGSSMVVMLTTQVERGRVKCHQYWPEPSGSSSYGGFQVT 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720354236 547 CHSEEGNPAYIFRKMTLFNQEKNESRQLTQIQYTAWPDHGVPDDSSDFLDFVCHVRDQRAGKEEPIIVHCSAGIGRTGVL 626
Cdd:cd14601    81 CHSEEGNPAYVFREMTLTNLEKNESRPLTQIQYIAWPDHGVPDDSSDFLDFVCLVRNKRAGKDEPVVVHCSAGIGRTGVL 160

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1720354236 627 ITMETAMCLIECNQPVYPLDIVRTMRDQRAMMIQTPSQYRFVCEAILKVYEE 678
Cdd:cd14601   161 ITMETAMCLIECNQPVYPLDIVRTMRDQRAMMIQTPSQYRFVCEAILKVYEE 212
PTPc-N3_4 cd14541
catalytic domain of tyrosine-protein phosphatase non-receptor type 21 and type 14; ...
 467-678 1.50e-161

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: 463.34  E-value: 1.50e-161
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720354236 467 DYINANYINMEIPSSSIINQYIACQGPLPHTCKDFWQMTWEQGSSMVVMLTTQVERGRVKCHQYWPEPSESSSYGCYQVT 546
Cdd:cd14541     1 DYINANYVNMEIPGSGIVNRYIAAQGPLPNTCADFWQMVWEQKSTLIVMLTTLVERGRVKCHQYWPDLGETMQFGNLQIT 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720354236 547 CHSEEGNPAYIFRKMTLFNQEKNESRQLTQIQYTAWPDHGVPDDSSDFLDFVCHVRDQRAGKEEPIIVHCSAGIGRTGVL 626
Cdd:cd14541    81 CVSEEVTPSFAFREFILTNTNTGEERHITQMQYLAWPDHGVPDDSSDFLDFVKRVRQNRVGMVEPTVVHCSAGIGRTGVL 160

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1720354236 627 ITMETAMCLIECNQPVYPLDIVRTMRDQRAMMIQTPSQYRFVCEAILKVYEE 678
Cdd:cd14541   161 ITMETAMCLIEANEPVYPLDIVRTMRDQRAMLIQTPSQYRFVCEAILRVYEE 212
PTPc smart00194
Protein tyrosine phosphatase, catalytic domain;
421-674 8.28e-113

Protein tyrosine phosphatase, catalytic domain;


Pssm-ID: 214550 [Multi-domain]  Cd Length: 259  Bit Score: 340.41  E-value: 8.28e-113
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720354236  421 AQFDQLYRKKPGM-TMSCAKLPQNISKNRYRDISPYDATRVLLKGNE----DYINANYINMEIPSssiiNQYIACQGPLP 495
Cdd:smart00194   4 EEFEKLDRLKPDDeSCTVAAFPENRDKNRYKDVLPYDHTRVKLKPPPgegsDYINASYIDGPNGP----KAYIATQGPLP 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720354236  496 HTCKDFWQMTWEQGSSMVVMLTTQVERGRVKCHQYWP-EPSESSSYGCYQVTCHSEEGNPAYIFRKMTLFNQEKNESRQL 574
Cdd:smart00194  80 STVEDFWRMVWEQKVTVIVMLTELVEKGREKCAQYWPdEEGEPLTYGDITVTLKSVEKVDDYTIRTLEVTNTGCSETRTV 159

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720354236  575 TQIQYTAWPDHGVPDDSSDFLDFVCHVRDQRAGKEEPIIVHCSAGIGRTGVLITMETAMCLIECNQPVYPLDIVRTMRDQ 654
Cdd:smart00194 160 THYHYTNWPDHGVPESPESILDLIRAVRKSQSTSTGPIVVHCSAGVGRTGTFIAIDILLQQLEAGKEVDIFEIVKELRSQ 239

                          250       260
                   ....*....|....*....|
gi 1720354236  655 RAMMIQTPSQYRFVCEAILK 674
Cdd:smart00194 240 RPGMVQTEEQYIFLYRAILE 259
Y_phosphatase pfam00102
Protein-tyrosine phosphatase;
443-674 2.34e-107

Protein-tyrosine phosphatase;


Pssm-ID: 459674 [Multi-domain]  Cd Length: 234  Bit Score: 325.35  E-value: 2.34e-107
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720354236 443 NISKNRYRDISPYDATRVLLK---GNEDYINANYInmeiPSSSIINQYIACQGPLPHTCKDFWQMTWEQGSSMVVMLTTQ 519
Cdd:pfam00102   1 NLEKNRYKDVLPYDHTRVKLTgdpGPSDYINASYI----DGYKKPKKYIATQGPLPNTVEDFWRMVWEEKVTIIVMLTEL 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720354236 520 VERGRVKCHQYWPEPSESS-SYGCYQVTCHSEEGN-PAYIFRKMTLFNQEKNESRQLTQIQYTAWPDHGVPDDSSDFLDF 597
Cdd:pfam00102  77 EEKGREKCAQYWPEEEGESlEYGDFTVTLKKEKEDeKDYTVRTLEVSNGGSEETRTVKHFHYTGWPDHGVPESPNSLLDL 156

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1720354236 598 VCHVRD-QRAGKEEPIIVHCSAGIGRTGVLITMETAMCLIECNQPVYPLDIVRTMRDQRAMMIQTPSQYRFVCEAILK 674
Cdd:pfam00102 157 LRKVRKsSLDGRSGPIVVHCSAGIGRTGTFIAIDIALQQLEAEGEVDIFQIVKELRSQRPGMVQTLEQYIFLYDAILE 234
PTPc cd00047
catalytic domain of protein tyrosine phosphatases; Protein tyrosine phosphatases (PTP, EC 3.1. ...
 468-670 1.38e-87

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: 272.62  E-value: 1.38e-87
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720354236 468 YINANYINMEipssSIINQYIACQGPLPHTCKDFWQMTWEQGSSMVVMLTTQVERGRVKCHQYWP-EPSESSSYGCYQVT 546
Cdd:cd00047     1 YINASYIDGY----RGPKEYIATQGPLPNTVEDFWRMVWEQKVSVIVMLTNLVEKGREKCERYWPeEGGKPLEYGDITVT 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720354236 547 CHSEEGNPAYIFRKMTLFNQEKNESRQLTQIQYTAWPDHGVPDDSSDFLDFVCHVRDQRAGKEEPIIVHCSAGIGRTGVL 626
Cdd:cd00047    77 LVSEEELSDYTIRTLELSPKGCSESREVTHLHYTGWPDHGVPSSPEDLLALVRRVRKEARKPNGPIVVHCSAGVGRTGTF 156

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....
gi 1720354236 627 ITMETAMCLIECNQPVYPLDIVRTMRDQRAMMIQTPSQYRFVCE 670
Cdd:cd00047   157 IAIDILLERLEAEGEVDVFEIVKALRKQRPGMVQTLEQYEFIYE 200
PTPc-N20_13 cd14538
catalytic domain of tyrosine-protein phosphatase non-receptor type 20 and type 13; ...
 468-675 2.34e-77

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: 246.13  E-value: 2.34e-77
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720354236 468 YINANYINMEIPSSSIinQYIACQGPLPHTCKDFWQMTWEQGSSMVVMLTTQVERGRVKCHQYWPEPSESSS--YGCYQV 545
Cdd:cd14538     1 YINASHIRIPVGGDTY--HYIACQGPLPNTTGDFWQMVWEQKSEVIAMVTQDVEGGKVKCHRYWPDSLNKPLicGGRLEV 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720354236 546 TCHSEEGNPAYIFRKMTLFNQEKNESRQLTQIQYTAWPDHGVPDDSSDFLDFVCHVRdqRAGKEEPIIVHCSAGIGRTGV 625
Cdd:cd14538    79 SLEKYQSLQDFVIRRISLRDKETGEVHHITHLNFTTWPDHGTPQSADPLLRFIRYMR--RIHNSGPIVVHCSAGIGRTGV 156

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|
gi 1720354236 626 LITMETAMCLIECNQPVYPLDIVRTMRDQRAMMIQTPSQYRFVCEAILKV 675
Cdd:cd14538   157 LITIDVALGLIERDLPFDIQDIVKDLREQRQGMIQTKDQYIFCYKACLEV 206
PTPc-N9 cd14543
catalytic domain of tyrosine-protein phosphatase non-receptor type 9; Tyrosine-protein ...
 422-667 2.84e-77

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: 248.43  E-value: 2.84e-77
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720354236 422 QFDQLYRKKPGMTMSCAKLPQNISKNRYRDISPYDATRVLLK---GNE--DYINANYINmeipSSSIINQYIACQGPLPH 496
Cdd:cd14543     8 EYEDIRREPPAGTFLCSLAPANQEKNRYGDVLCLDQSRVKLPkrnGDErtDYINANFMD----GYKQKNAYIATQGPLPK 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720354236 497 TCKDFWQMTWEQGSSMVVMLTTQVERGRVKCHQYWPEPSESS-SYGCYQVTCHSEEGNPAYIFRKMTLFNQEKNESRQLT 575
Cdd:cd14543    84 TYSDFWRMVWEQKVLVIVMTTRVVERGRVKCGQYWPLEEGSSlRYGDLTVTNLSVENKEHYKKTTLEIHNTETDESRQVT 163

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720354236 576 QIQYTAWPDHGVPDDSSDFLDFVCHVRDQRA------GKE-------EPIIVHCSAGIGRTGVLITMEtaMCLIECnQPV 642
Cdd:cd14543   164 HFQFTSWPDFGVPSSAAALLDFLGEVRQQQAlavkamGDRwkghppgPPIVVHCSAGIGRTGTFCTLD--ICLSQL-EDV 240

                         250       260
                  ....*....|....*....|....*...
gi 1720354236 643 YPLDI---VRTMRDQRAMMIQTPSQYRF 667
Cdd:cd14543   241 GTLNVmqtVRRMRTQRAFSIQTPDQYYF 268
PTPc-N13 cd14597
catalytic domain of tyrosine-protein phosphatase non-receptor type 13; Tyrosine-protein ...
 442-675 2.27e-74

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: 239.35  E-value: 2.27e-74
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720354236 442 QNISKNRYRDISPYDATRVLLKGNEDYINANYINMEIPSSSIInqYIACQGPLPHTCKDFWQMTWEQGSSMVVMLTTQVE 521
Cdd:cd14597     2 ENRKKNRYKNILPYDTTRVPLGDEGGYINASFIKMPVGDEEFV--YIACQGPLPTTVADFWQMVWEQKSTVIAMMTQEVE 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720354236 522 RGRVKCHQYWPEPSESSSY--GCYQVTCHSEEGNPAYIFRKMTLFNQEKNESRQLTQIQYTAWPDHGVPDDSSDFLDFVC 599
Cdd:cd14597    80 GGKIKCQRYWPEILGKTTMvdNRLQLTLVRMQQLKNFVIRVLELEDIQTREVRHITHLNFTAWPDHDTPSQPEQLLTFIS 159

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1720354236 600 HVRD-QRAGkeePIIVHCSAGIGRTGVLITMETAMCLIECNQPVYPLDIVRTMRDQRAMMIQTPSQYRFVCEAILKV 675
Cdd:cd14597   160 YMRHiHKSG---PIITHCSAGIGRSGTLICIDVVLGLISKDLDFDISDIVRTMRLQRHGMVQTEDQYIFCYQVILYV 233
R3-PTPc cd14548
catalytic domain of R3 subfamily receptor-type tyrosine-protein phosphatases and similar ...
 448-668 3.80e-74

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: 238.41  E-value: 3.80e-74
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720354236 448 RYRDISPYDATRVLLKG-----NEDYINANYInmeiPSSSIINQYIACQGPLPHTCKDFWQMTWEQGSSMVVMLTTQVER 522
Cdd:cd14548     1 RYTNILPYDHSRVKLIPineeeGSDYINANYI----PGYNSPREFIATQGPLPGTKDDFWRMVWEQNSHTIVMLTQCMEK 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720354236 523 GRVKCHQYWPEPSESSSYGCYQVTCHSEEGNPAYIFRKMTLfnQEKNESRQLTQIQYTAWPDHGVPDDSSDFLDFVCHVR 602
Cdd:cd14548    77 GRVKCDHYWPFDQDPVYYGDITVTMLSESVLPDWTIREFKL--ERGDEVRSVRQFHFTAWPDHGVPEAPDSLLRFVRLVR 154

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1720354236 603 DQRAGKEEPIIVHCSAGIGRTGVLITMETAMCLIECNQPVYPLDIVRTMRDQRAMMIQTPSQYRFV 668
Cdd:cd14548   155 DYIKQEKGPTIVHCSAGVGRTGTFIALDRLLQQIESEDYVDIFGIVYDLRKHRPLMVQTEAQYIFL 220
PTPc-N18 cd14603
catalytic domain of tyrosine-protein phosphatase non-receptor type 18; Tyrosine-protein ...
 427-676 8.17e-70

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: 228.56  E-value: 8.17e-70
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720354236 427 YRKKPGMTMSCAKLPQNISKNRYRDISPYDATRVLL-----KGNEDYINANYINmeipSSSIINQYIACQGPLPHTCKDF 501
Cdd:cd14603    14 FKADYVCSTVAGGRKENVKKNRYKDILPYDQTRVILsllqeEGHSDYINANFIK----GVDGSRAYIATQGPLSHTVLDF 89

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720354236 502 WQMTWEQGSSMVVMLTTQVERGRVKCHQYWPEPSESSSYGCYQVT-CHSEEGNPAYIFRKMTLFNQEknESRQLTQIQYT 580
Cdd:cd14603    90 WRMIWQYGVKVILMACREIEMGKKKCERYWAQEQEPLQTGPFTITlVKEKRLNEEVILRTLKVTFQK--ESRSVSHFQYM 167

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720354236 581 AWPDHGVPDDSSDFLDFVCHVRDQRAGKEEPIIVHCSAGIGRTGVLITME--TAMCLIECNQPVYPL-DIVRTMRDQRAM 657
Cdd:cd14603   168 AWPDHGIPDSPDCMLAMIELARRLQGSGPEPLCVHCSAGCGRTGVICTVDyvRQLLLTQRIPPDFSIfDVVLEMRKQRPA 247

                         250
                  ....*....|....*....
gi 1720354236 658 MIQTPSQYRFVCEAILKVY 676
Cdd:cd14603   248 AVQTEEQYEFLYHTVAQMF 266
R-PTPc-LAR-1 cd14553
catalytic domain of LAR family receptor-type tyrosine-protein phosphatases, repeat 1; The LAR ...
 443-673 2.01e-69

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: 226.51  E-value: 2.01e-69
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720354236 443 NISKNRYRDISPYDATRVLLKGNE-----DYINANYINMEIPSssiiNQYIACQGPLPHTCKDFWQMTWEQGSSMVVMLT 517
Cdd:cd14553     3 NKPKNRYANVIAYDHSRVILQPIEgvpgsDYINANYCDGYRKQ----NAYIATQGPLPETFGDFWRMVWEQRSATIVMMT 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720354236 518 TQVERGRVKCHQYWPEpSESSSYGCYQVTCHSEEGNPAYIFRKMTLFNQEKNESRQLTQIQYTAWPDHGVPDDSSDFLDF 597
Cdd:cd14553    79 KLEERSRVKCDQYWPT-RGTETYGLIQVTLLDTVELATYTVRTFALHKNGSSEKREVRQFQFTAWPDHGVPEHPTPFLAF 157

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1720354236 598 VCHVRDQRAGKEEPIIVHCSAGIGRTGVLITMEtamCLIECNQPVYPLDI---VRTMRDQRAMMIQTPSQYRFVCEAIL 673
Cdd:cd14553   158 LRRVKACNPPDAGPIVVHCSAGVGRTGCFIVID---SMLERIKHEKTVDIyghVTCLRAQRNYMVQTEDQYIFIHDALL 233
PTP_fungal cd18533
fungal protein tyrosine phosphatases; This subfamily contains Saccharomyces cerevisiae ...
 468-668 1.81e-67

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: 220.20  E-value: 1.81e-67
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720354236 468 YINANYINMEipsSSIINQYIACQGPLPHTCKDFWQMTWEQGSSMVVMLTTQVERGRVKCHQYWPEPSESSSYGCYQVTC 547
Cdd:cd18533     1 YINASYITLP---GTSSKRYIATQGPLPATIGDFWKMIWQNNVGVIVMLTPLVENGREKCDQYWPSGEYEGEYGDLTVEL 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720354236 548 --HSEEGNPAYIFRKMTLfNQEKNESRQLTQIQYTAWPDHGVPDDSSDFLDFVCHVRD--QRAGKEEPIIVHCSAGIGRT 623
Cdd:cd18533    78 vsEEENDDGGFIVREFEL-SKEDGKVKKVYHIQYKSWPDFGVPDSPEDLLTLIKLKRElnDSASLDPPIIVHCSAGVGRT 156

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1720354236 624 GVLITMETAM-----------CLIECNQPVYplDIVRTMRDQRAMMIQTPSQYRFV 668
Cdd:cd18533   157 GTFIALDSLLdelkrglsdsqDLEDSEDPVY--EIVNQLRKQRMSMVQTLRQYIFL 210
R5-PTPc-1 cd14549
catalytic domain of R5 subfamily receptor-type tyrosine-protein phosphatases, repeat 1; The R5 ...
 468-668 3.38e-67

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: 219.53  E-value: 3.38e-67
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720354236 468 YINANYInmeiPSSSIINQYIACQGPLPHTCKDFWQMTWEQGSSMVVMLTTQVERGRVKCHQYWPEpSESSSYGCYQVTC 547
Cdd:cd14549     1 YINANYV----DGYNKARAYIATQGPLPSTFDDFWRMVWEQNSAIIVMITNLVERGRRKCDQYWPK-EGTETYGNIQVTL 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720354236 548 HSEEGNPAYIFRKMTLFNQE------KNESRQLTQIQYTAWPDHGVPDDSSDFLDFvchVRDQRAGKEE---PIIVHCSA 618
Cdd:cd14549    76 LSTEVLATYTVRTFSLKNLKlkkvkgRSSERVVYQYHYTQWPDHGVPDYTLPVLSF---VRKSSAANPPgagPIVVHCSA 152

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|
gi 1720354236 619 GIGRTGVLITMETAMCLIECNQPVYPLDIVRTMRDQRAMMIQTPSQYRFV 668
Cdd:cd14549   153 GVGRTGTYIVIDSMLQQIQDKGTVNVFGFLKHIRTQRNYLVQTEEQYIFI 202
PTPc-N14 cd14599
catalytic domain of tyrosine-protein phosphatase non-receptor type 14; Tyrosine-protein ...
 417-674 5.94e-67

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: 221.79  E-value: 5.94e-67
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720354236 417 GTVLAQFDQLYRKKPGMTMSCAKLPQNISKNRYRDISPYDATRVLL----KGNEDYINANYINMEIPSSSIinQYIACQG 492
Cdd:cd14599    12 GMVFTEYEQIPKKKADGVFTTATLPENAERNRIREVVPYEENRVELvptkENNTGYINASHIKVTVGGEEW--HYIATQG 89

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720354236 493 PLPHTCKDFWQMTWEQGSSMVVMLTTQVERGRVKCHQYWPE---PSESSSYGCYQVTCHSEEGNPAYIFRKMTLFNQEKN 569
Cdd:cd14599    90 PLPHTCHDFWQMVWEQGVNVIAMVTAEEEGGRSKSHRYWPKlgsKHSSATYGKFKVTTKFRTDSGCYATTGLKVKHLLSG 169

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720354236 570 ESRQLTQIQYTAWPDHGVPDDSSDFLDFVCHVR----------DQRAGKEEPIIVHCSAGIGRTGVLITMETAMCLIECN 639
Cdd:cd14599   170 QERTVWHLQYTDWPDHGCPEEVQGFLSYLEEIQsvrrhtnsmlDSTKNCNPPIVVHCSAGVGRTGVVILTELMIGCLEHN 249

                         250       260       270
                  ....*....|....*....|....*....|....*
gi 1720354236 640 QPVYPLDIVRTMRDQRAMMIQTPSQYRFVCEAILK 674
Cdd:cd14599   250 EKVEVPVMLRHLREQRMFMIQTIAQYKFVYQVLIQ 284
PTPc-N1_2 cd14545
catalytic domain of tyrosine-protein phosphatase non-receptor type 1 and type 2; ...
 446-667 3.50e-66

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: 217.64  E-value: 3.50e-66
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720354236 446 KNRYRDISPYDATRVLLK---GNEDYINANYINMEipssSIINQYIACQGPLPHTCKDFWQMTWEQGSSMVVMLTTQVER 522
Cdd:cd14545     1 LNRYRDRDPYDHDRSRVKlkqGDNDYINASLVEVE----EAKRSYILTQGPLPNTSGHFWQMVWEQNSKAVIMLNKLMEK 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720354236 523 GRVKCHQYWPePSESSSYGC----YQVTCHSEEGNPAYIFRKMTLFNQEKNESRQLTQIQYTAWPDHGVPDDSSDFLDFV 598
Cdd:cd14545    77 GQIKCAQYWP-QGEGNAMIFedtgLKVTLLSEEDKSYYTVRTLELENLKTQETREVLHFHYTTWPDFGVPESPAAFLNFL 155

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1720354236 599 CHVRDQRAGKEE--PIIVHCSAGIGRTGVLITMETAMCLIECNQPVyPLD---IVRTMRDQRAMMIQTPSQYRF 667
Cdd:cd14545   156 QKVRESGSLSSDvgPPVVHCSAGIGRSGTFCLVDTCLVLIEKGNPS-SVDvkkVLLEMRKYRMGLIQTPDQLRF 228
PTPc-N20 cd14596
catalytic domain of tyrosine-protein phosphatase non-receptor type 20; Tyrosine-protein ...
 468-675 6.32e-65

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: 213.46  E-value: 6.32e-65
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720354236 468 YINANYINMEIPSSSIInqYIACQGPLPHTCKDFWQMTWEQGSSMVVMLTTQVERGRVKCHQYWPEP-SESSSYGCYQVT 546
Cdd:cd14596     1 YINASYITMPVGEEELF--YIATQGPLPSTIDDFWQMVWENRSDVIAMMTREVERGKVKCHRYWPETlQEPMELENYQLR 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720354236 547 CHSEEGNPAYIFRKMTLFNQEKNESRQLTQIQYTAWPDHGVPDDSSDFLDFVCHVRdqRAGKEEPIIVHCSAGIGRTGVL 626
Cdd:cd14596    79 LENYQALQYFIIRIIKLVEKETGENRLIKHLQFTTWPDHGTPQSSDQLVKFICYMR--KVHNTGPIVVHCSAGIGRAGVL 156

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*....
gi 1720354236 627 ITMETAMCLIECNQPVYPLDIVRTMRDQRAMMIQTPSQYRFVCEAILKV 675
Cdd:cd14596   157 ICVDVLLSLIEKDLSFNIKDIVREMRQQRYGMIQTKDQYLFCYKVVLEV 205
PTPc-N11_6 cd14544
catalytic domain of tyrosine-protein phosphatase non-receptor type 11 and type 6; ...
 443-672 1.44e-64

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: 214.25  E-value: 1.44e-64
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720354236 443 NISKNRYRDISPYDATRVLLKGNE------DYINANYI---NMEIPSSSIINQYIACQGPLPHTCKDFWQMTWEQGSSMV 513
Cdd:cd14544     1 NKGKNRYKNILPFDHTRVILKDRDpnvpgsDYINANYIrneNEGPTTDENAKTYIATQGCLENTVSDFWSMVWQENSRVI 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720354236 514 VMLTTQVERGRVKCHQYWPEPSESSSYGCYQVTCHSEEGNPAYIFRKMTLFN-QEKNESRQLTQIQYTAWPDHGVPDDSS 592
Cdd:cd14544    81 VMTTKEVERGKNKCVRYWPDEGMQKQYGPYRVQNVSEHDTTDYTLRELQVSKlDQGDPIREIWHYQYLSWPDHGVPSDPG 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720354236 593 DFLDFVCHV-RDQRAGKEE-PIIVHCSAGIGRTGVLITMETAMCLIECNQPVYPLDIVRTM---RDQRAMMIQTPSQYRF 667
Cdd:cd14544   161 GVLNFLEDVnQRQESLPHAgPIVVHCSAGIGRTGTFIVIDMLLDQIKRKGLDCDIDIQKTIqmvRSQRSGMVQTEAQYKF 240


                  ....*
gi 1720354236 668 VCEAI 672
Cdd:cd14544   241 IYVAV 245
PTPc-N21_14 cd14540
catalytic domain of tyrosine-protein phosphatase non-receptor type 21 and type 14; ...
 468-668 2.40e-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: 212.32  E-value: 2.40e-64
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720354236 468 YINANYINMEIPSSSIinQYIACQGPLPHTCKDFWQMTWEQGSSMVVMLTTQVERGRVKCHQYWPE---PSESSSYGCYQ 544
Cdd:cd14540     1 YINASHITATVGGKQR--FYIAAQGPLQNTVGDFWQMVWEQGVYLVVMVTAEEEGGREKCFRYWPTlggEHDALTFGEYK 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720354236 545 VTCHSEEGNPAYIFRKMTLFNQEKNESRQLTQIQYTAWPDHGVPDDSSDFLDFVCHVRDQR-------AGK--EEPIIVH 615
Cdd:cd14540    79 VSTKFSVSSGCYTTTGLRVKHTLSGQSRTVWHLQYTDWPDHGCPEDVSGFLDFLEEINSVRrhtnqdvAGHnrNPPTLVH 158

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1720354236 616 CSAGIGRTGVLITMETAMCLIECNQPVYPLDIVRTMRDQRAMMIQTPSQYRFV 668
Cdd:cd14540   159 CSAGVGRTGVVILADLMLYCLDHNEELDIPRVLALLRHQRMLLVQTLAQYKFV 211
R-PTPc-H cd14619
catalytic domain of receptor-type tyrosine-protein phosphatase H; Receptor-type ...
 447-674 7.20e-64

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: 211.67  E-value: 7.20e-64
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720354236 447 NRYRDISPYDATRVLLK-----GNEDYINANYInmeiPSSSIINQYIACQGPLPHTCKDFWQMTWEQGSSMVVMLTTQVE 521
Cdd:cd14619     1 NRFRNVLPYDWSRVPLKpiheePGSDYINANYM----PGYWSSQEFIATQGPLPQTVGDFWRMIWEQQSSTIVMLTNCME 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720354236 522 RGRVKCHQYWPEPSESSSYGCYQVTCHSEEGNPAYIFRKMTLFNQEKNESRQLTQIQYTAWPDHGVPDDSSDFLDFVCHV 601
Cdd:cd14619    77 AGRVKCEHYWPLDYTPCTYGHLRVTVVSEEVMENWTVREFLLKQVEEQKTLSVRHFHFTAWPDHGVPSSTDTLLAFRRLL 156

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1720354236 602 RDQRAGKEE--PIIVHCSAGIGRTGVLITMETAMCLIECNQPVYPLDIVRTMRDQRAMMIQTPSQYRFVCEAILK 674
Cdd:cd14619   157 RQWLDQTMSggPTVVHCSAGVGRTGTLIALDVLLQQLQSEGLLGPFSFVQKMRENRPLMVQTESQYVFLHQCILD 231
PTPc-N1 cd14608
catalytic domain of tyrosine-protein phosphatase non-receptor type 1; Tyrosine-protein ...
 438-674 5.43e-63

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: 211.04  E-value: 5.43e-63
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720354236 438 AKLPQNISKNRYRDISPYDATRVLL-KGNEDYINANYINMEIPSSSiinqYIACQGPLPHTCKDFWQMTWEQGSSMVVML 516
Cdd:cd14608    20 AKLPKNKNRNRYRDVSPFDHSRIKLhQEDNDYINASLIKMEEAQRS----YILTQGPLPNTCGHFWEMVWEQKSRGVVML 95

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720354236 517 TTQVERGRVKCHQYWPEPSESSSY---GCYQVTCHSEEGNPAYIFRKMTLFNQEKNESRQLTQIQYTAWPDHGVPDDSSD 593
Cdd:cd14608    96 NRVMEKGSLKCAQYWPQKEEKEMIfedTNLKLTLISEDIKSYYTVRQLELENLTTQETREILHFHYTTWPDFGVPESPAS 175

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720354236 594 FLDFVCHVRDQRAGKEE--PIIVHCSAGIGRTGVLITMETAMCLIECNQPVYPLDIVRT---MRDQRAMMIQTPSQYRFV 668
Cdd:cd14608   176 FLNFLFKVRESGSLSPEhgPVVVHCSAGIGRSGTFCLADTCLLLMDKRKDPSSVDIKKVlleMRKFRMGLIQTADQLRFS 255


                  ....*.
gi 1720354236 669 CEAILK 674
Cdd:cd14608   256 YLAVIE 261
R-PTP-LAR-2 cd14554
PTP-like domain of the LAR family receptor-type tyrosine-protein phosphatases, repeat 2; The ...
 438-673 9.71e-63

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: 208.92  E-value: 9.71e-63
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720354236 438 AKLPQNISKNRYRDISPYDATRV---LLKGNE--DYINANYINmeipSSSIINQYIACQGPLPHTCKDFWQMTWEQGSSM 512
Cdd:cd14554     1 ANLPCNKFKNRLVNILPYESTRVclqPIRGVEgsDYINASFID----GYRQRGAYIATQGPLAETTEDFWRMLWEHNSTI 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720354236 513 VVMLTTQVERGRVKCHQYWPEpSESSSYGCYQVTCHSEEGNPAYIFRKMTLFNQEKNESRQLTQIQYTAWPDHGVPDDSS 592
Cdd:cd14554    77 IVMLTKLREMGREKCHQYWPA-ERSARYQYFVVDPMAEYNMPQYILREFKVTDARDGQSRTVRQFQFTDWPEQGVPKSGE 155

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720354236 593 DFLDFVCHVRDQRA--GKEEPIIVHCSAGIGRTGVLITMETAMCLIECNQPVYPLDIVRTMRDQRAMMIQTPSQYRFVCE 670
Cdd:cd14554   156 GFIDFIGQVHKTKEqfGQEGPITVHCSAGVGRTGVFITLSIVLERMRYEGVVDVFQTVKLLRTQRPAMVQTEDQYQFCYR 235


                  ...
gi 1720354236 671 AIL 673
Cdd:cd14554   236 AAL 238
PDZ_PTPN3-4-like cd06706
PDZ domain of tyrosine-protein phosphatase non-receptor type 3 (PTPN3), tyrosine-protein ...
 277-366 4.38e-62

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: 201.39  E-value: 4.38e-62
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720354236 277 DNLVLIKMKPDENGRFGFNVKGGYDQKMPVIVSRVAPGTPADLCVPRLNEGDQVVLINGRDIAEHTHDQVVLFIKASCEK 356
Cdd:cd06706     1 DGLVLIRMKPDENGRFGFNVKGGVDQKMPVIVSRVAPGTPADLCIPRLNEGDQVLLINGRDISEHTHDQVVMFIKASRER 80

                          90
                  ....*....|
gi 1720354236 357 HSGELVLLVR 366
Cdd:cd06706    81 HSGELVLLVR 90
R-PTPc-J cd14615
catalytic domain of receptor-type tyrosine-protein phosphatase J; Receptor-type ...
 447-668 1.13e-61

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: 205.82  E-value: 1.13e-61
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720354236 447 NRYRDISPYDATRVLLK----GNEDYINANYInmeiPSSSIINQYIACQGPLPHTCKDFWQMTWEQGSSMVVMLTTQVER 522
Cdd:cd14615     1 NRYNNVLPYDISRVKLSvqshSTDDYINANYM----PGYNSKKEFIAAQGPLPNTVKDFWRMVWEKNVYAIVMLTKCVEQ 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720354236 523 GRVKCHQYWPEpSESSSYGCYQVTCHSEEGNPAYIFRKMTLFNQEKNESRQLTQIQYTAWPDHGVPDDSSDFLDFVCHVR 602
Cdd:cd14615    77 GRTKCEEYWPS-KQKKDYGDITVTMTSEIVLPEWTIRDFTVKNAQTNESRTVRHFHFTSWPDHGVPETTDLLINFRHLVR 155

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1720354236 603 D--QRAGKEEPIIVHCSAGIGRTGVLITMETAMCLIECNQPVYPLDIVRTMRDQRAMMIQTPSQYRFV 668
Cdd:cd14615   156 EymKQNPPNSPILVHCSAGVGRTGTFIAIDRLIYQIENENVVDVYGIVYDLRMHRPLMVQTEDQYVFL 223
PTPc-KIM cd14547
catalytic domain of the kinase interaction motif (KIM) family of protein-tyrosine phosphatases; ...
 447-668 1.90e-61

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: 204.94  E-value: 1.90e-61
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720354236 447 NRYRDISPYDATRVLLKGNED-----YINANYI---NMEIPSssiinqYIACQGPLPHTCKDFWQMTWEQGSSMVVMLTT 518
Cdd:cd14547     1 NRYKTILPNEHSRVCLPSVDDdplssYINANYIrgyDGEEKA------YIATQGPLPNTVADFWRMVWQEKTPIIVMITN 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720354236 519 QVERgRVKCHQYWPEpSESSSYGCYQVTCHSEEGNPAYIFRKMTLfnQEKNESRQLTQIQYTAWPDHGVPDDSSDFLDFV 598
Cdd:cd14547    75 LTEA-KEKCAQYWPE-EENETYGDFEVTVQSVKETDGYTVRKLTL--KYGGEKRYLKHYWYTSWPDHKTPEAAQPLLSLV 150

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1720354236 599 CHVR--DQRAGKEEPIIVHCSAGIGRTGVLITMETAMCLIECNQPVYPLDIVRTMRDQRAMMIQTPSQYRFV 668
Cdd:cd14547   151 QEVEeaRQTEPHRGPIVVHCSAGIGRTGCFIATSIGCQQLREEGVVDVLGIVCQLRLDRGGMVQTAEQYEFV 222
PTPc-N6 cd14606
catalytic domain of tyrosine-protein phosphatase non-receptor type 6; Tyrosine-protein ...
 441-677 2.76e-61

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: 205.88  E-value: 2.76e-61
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720354236 441 PQNISKNRYRDISPYDATRVLLKGNE------DYINANYI-NMEIPSSSIINQYIACQGPLPHTCKDFWQMTWEQGSSMV 513
Cdd:cd14606    16 PENKSKNRYKNILPFDHSRVILQGRDsnipgsDYINANYVkNQLLGPDENAKTYIASQGCLEATVNDFWQMAWQENSRVI 95

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720354236 514 VMLTTQVERGRVKCHQYWPEPSESSSYGCYQVTCHSEEGNPAYIFRKMTLFNQEKNES-RQLTQIQYTAWPDHGVPDDSS 592
Cdd:cd14606    96 VMTTREVEKGRNKCVPYWPEVGMQRAYGPYSVTNCGEHDTTEYKLRTLQVSPLDNGELiREIWHYQYLSWPDHGVPSEPG 175

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720354236 593 DFLDFVCHV--RDQRAGKEEPIIVHCSAGIGRTGVLITMETAMCLIECNQPVYPLDIVRTM---RDQRAMMIQTPSQYRF 667
Cdd:cd14606   176 GVLSFLDQInqRQESLPHAGPIIVHCSAGIGRTGTIIVIDMLMENISTKGLDCDIDIQKTIqmvRAQRSGMVQTEAQYKF 255

                         250
                  ....*....|
gi 1720354236 668 VCEAILKVYE 677
Cdd:cd14606   256 IYVAIAQFIE 265
R-PTPc-O cd14614
catalytic domain of receptor-type tyrosine-protein phosphatase O; Receptor-type ...
 438-668 1.96e-60

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: 202.81  E-value: 1.96e-60
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720354236 438 AKLPQNISKNRYRDISPYDATRV-LLKGNE----DYINANYInmeiPSSSIINQYIACQGPLPHTCKDFWQMTWEQGSSM 512
Cdd:cd14614     7 ADLPVNRCKNRYTNILPYDFSRVkLVSMHEeegsDYINANYI----PGYNSPQEYIATQGPLPETRNDFWKMVLQQKSQI 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720354236 513 VVMLTTQVERGRVKCHQYWPEPSESSSYGCYQVTCHSEEGNPAYIFRKMTLfnQEKNESRQLTQIQYTAWPDHGVP--DD 590
Cdd:cd14614    83 IVMLTQCNEKRRVKCDHYWPFTEEPVAYGDITVEMLSEEEQPDWAIREFRV--SYADEVQDVMHFNYTAWPDHGVPtaNA 160

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1720354236 591 SSDFLDFVCHVRDQRAGKEEPIIVHCSAGIGRTGVLITMETAMCLIECNQPVYPLDIVRTMRDQRAMMIQTPSQYRFV 668
Cdd:cd14614   161 AESILQFVQMVRQQAVKSKGPMIIHCSAGVGRTGTFIALDRLLQHIRDHEFVDILGLVSEMRSYRMSMVQTEEQYIFI 238
PTPc-N2 cd14607
catalytic domain of tyrosine-protein phosphatase non-receptor type 2; Tyrosine-protein ...
 429-672 2.32e-60

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: 203.27  E-value: 2.32e-60
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720354236 429 KKPGMTMSCAKLPQNISKNRYRDISPYDATRVLLKGNE-DYINANYINMEIPSSSiinqYIACQGPLPHTCKDFWQMTWE 507
Cdd:cd14607    10 ESHDYPHRVAKYPENRNRNRYRDVSPYDHSRVKLQNTEnDYINASLVVIEEAQRS----YILTQGPLPNTCCHFWLMVWQ 85

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720354236 508 QGSSMVVMLTTQVERGRVKCHQYWPEPSE---SSSYGCYQVTCHSEEGNPAYIFRKMTLFNQEKNESRQLTQIQYTAWPD 584
Cdd:cd14607    86 QKTKAVVMLNRIVEKDSVKCAQYWPTDEEevlSFKETGFSVKLLSEDVKSYYTVHLLQLENINSGETRTISHFHYTTWPD 165

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720354236 585 HGVPDDSSDFLDFVCHVRDQRAGKEE--PIIVHCSAGIGRTGVLITMETAMCLIECNQP--VYPLDIVRTMRDQRAMMIQ 660
Cdd:cd14607   166 FGVPESPASFLNFLFKVRESGSLSPEhgPAVVHCSAGIGRSGTFSLVDTCLVLMEKKDPdsVDIKQVLLDMRKYRMGLIQ 245

                         250
                  ....*....|..
gi 1720354236 661 TPSQYRFVCEAI 672
Cdd:cd14607   246 TPDQLRFSYMAV 257
R-PTPc-B cd14617
catalytic domain of receptor-type tyrosine-protein phosphatase B; Receptor-type ...
 447-668 1.72e-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: 199.76  E-value: 1.72e-59
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720354236 447 NRYRDISPYDATRVLLKGNE-----DYINANYInmeiPSSSIINQYIACQGPLPHTCKDFWQMTWEQGSSMVVMLTTQVE 521
Cdd:cd14617     1 NRYNNILPYDSTRVKLSNVDddpcsDYINASYI----PGNNFRREYIATQGPLPGTKDDFWKMVWEQNVHNIVMVTQCVE 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720354236 522 RGRVKCHQYWPEPSESSSYGCYQVTCHSEEGNPAYIFRKMTLFNQEKNES-RQLTQIQYTAWPDHGVPDDSSDFLDFVCH 600
Cdd:cd14617    77 KGRVKCDHYWPADQDSLYYGDLIVQMLSESVLPEWTIREFKICSEEQLDApRLVRHFHYTVWPDHGVPETTQSLIQFVRT 156

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720354236 601 VRD--QRAGKEEPIIVHCSAGIGRTGVLITMETAMCLIECNQPVYPLDIVRTMRDQRAMMIQTPSQYRFV 668
Cdd:cd14617   157 VRDyiNRTPGSGPTVVHCSAGVGRTGTFIALDRILQQLDSKDSVDIYGAVHDLRLHRVHMVQTECQYVYL 226
R-PTPc-F-1 cd14626
catalytic domain of receptor-type tyrosine-protein phosphatase F, repeat 1; Receptor-type ...
 422-674 6.68e-59

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: 199.88  E-value: 6.68e-59
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720354236 422 QFDQLYRK-KPG--MTMSCAKLPQNISKNRYRDISPYDATRVLLKG-----NEDYINANYINmeipSSSIINQYIACQGP 493
Cdd:cd14626    17 KFSQEYESiDPGqqFTWENSNLEVNKPKNRYANVIAYDHSRVILTSvdgvpGSDYINANYID----GYRKQNAYIATQGP 92

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720354236 494 LPHTCKDFWQMTWEQGSSMVVMLTTQVERGRVKCHQYWPEPSeSSSYGCYQVTCHSEEGNPAYIFRKMTLFNQEKNESRQ 573
Cdd:cd14626    93 LPETLSDFWRMVWEQRTATIVMMTRLEEKSRVKCDQYWPIRG-TETYGMIQVTLLDTVELATYSVRTFALYKNGSSEKRE 171

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720354236 574 LTQIQYTAWPDHGVPDDSSDFLDFVCHVRDQRAGKEEPIIVHCSAGIGRTGVLITMETAMCLIECNQPVYPLDIVRTMRD 653
Cdd:cd14626   172 VRQFQFMAWPDHGVPEYPTPILAFLRRVKACNPPDAGPMVVHCSAGVGRTGCFIVIDAMLERMKHEKTVDIYGHVTCMRS 251

                         250       260
                  ....*....|....*....|.
gi 1720354236 654 QRAMMIQTPSQYRFVCEAILK 674
Cdd:cd14626   252 QRNYMVQTEDQYIFIHEALLE 272
R-PTPc-V cd14618
catalytic domain of receptor-type tyrosine-protein phosphatase V; Receptor-type ...
 447-673 2.77e-57

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: 194.01  E-value: 2.77e-57
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720354236 447 NRYRDISPYDATRVLLK--GNE---DYINANYInmeiPSSSIINQYIACQGPLPHTCKDFWQMTWEQGSSMVVMLTTQVE 521
Cdd:cd14618     1 NRYPHVLPYDHSRVRLSqlGGEphsDYINANFI----PGYTSPQEFIATQGPLKKTIEDFWRLVWEQQVCNIIMLTVGME 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720354236 522 RGRVKCHQYWPEPSESSSYGCYQVTCHSEEGNPAYIFRKMTLFNQEKNESRQLTQIQYTAWPDHGVPDDSSDFLDFVCHV 601
Cdd:cd14618    77 NGRVLCDHYWPSESTPVSYGHITVHLLAQSSEDEWTRREFKLWHEDLRKERRVKHLHYTAWPDHGIPESTSSLMAFRELV 156

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1720354236 602 RD--QRAGKEEPIIVHCSAGIGRTGVLITMETAMCLIECNQPVYPLDIVRTMRDQRAMMIQTPSQYRFVCEAIL 673
Cdd:cd14618   157 REhvQATKGKGPTLVHCSAGVGRSGTFIALDRLLRQLKEEKVVDVFNTVYILRMHRYLMIQTLSQYIFLHSCIL 230
PTPc-N11 cd14605
catalytic domain of tyrosine-protein phosphatase non-receptor type 11; Tyrosine-protein ...
 442-672 1.55e-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: 192.93  E-value: 1.55e-56
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720354236 442 QNISKNRYRDISPYDATRVLLKG---NE---DYINANYI----NMEIPSSSIINQYIACQGPLPHTCKDFWQMTWEQGSS 511
Cdd:cd14605     1 ENKNKNRYKNILPFDHTRVVLHDgdpNEpvsDYINANIImpefETKCNNSKPKKSYIATQGCLQNTVNDFWRMVFQENSR 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720354236 512 MVVMLTTQVERGRVKCHQYWPEPSESSSYGCYQVTCHSEEGNPAYIFRKMTLFN-QEKNESRQLTQIQYTAWPDHGVPDD 590
Cdd:cd14605    81 VIVMTTKEVERGKSKCVKYWPDEYALKEYGVMRVRNVKESAAHDYILRELKLSKvGQGNTERTVWQYHFRTWPDHGVPSD 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720354236 591 SSDFLDFVCHVRDQRAGKEE--PIIVHCSAGIGRTGVLITMETAMCLIECNQPVYPLDIVRTM---RDQRAMMIQTPSQY 665
Cdd:cd14605   161 PGGVLDFLEEVHHKQESIMDagPVVVHCSAGIGRTGTFIVIDILIDIIREKGVDCDIDVPKTIqmvRSQRSGMVQTEAQY 240


                  ....*..
gi 1720354236 666 RFVCEAI 672
Cdd:cd14605   241 RFIYMAV 247
PTPc-N22_18_12 cd14542
catalytic domain of tyrosine-protein phosphatase non-receptor type 22, type 18 and type 12; ...
 468-668 2.16e-56

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: 190.33  E-value: 2.16e-56
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720354236 468 YINANYINMeiPSSSIInqYIACQGPLPHTCKDFWQMTWEQGSSMVVMLTTQVERGRVKCHQYWPEPSESS-SYGCYQVT 546
Cdd:cd14542     1 YINANFIKG--VSGSKA--YIATQGPLPNTVLDFWRMIWEYNVQVIVMACREFEMGKKKCERYWPEEGEEQlQFGPFKIS 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720354236 547 CHSEEG-NPAYIFRkmTLFNQEKNESRQLTQIQYTAWPDHGVPDDSSDFLDFVCHVRDQRAGKEEPIIVHCSAGIGRTGV 625
Cdd:cd14542    77 LEKEKRvGPDFLIR--TLKVTFQKESRTVYQFHYTAWPDHGVPSSVDPILDLVRLVRDYQGSEDVPICVHCSAGCGRTGT 154

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*.
gi 1720354236 626 LITMETAMCLIEC---NQPVYPLDIVRTMRDQRAMMIQTPSQYRFV 668
Cdd:cd14542   155 ICAIDYVWNLLKTgkiPEEFSLFDLVREMRKQRPAMVQTKEQYELV 200
R-PTP-D-2 cd14628
PTP-like domain of receptor-type tyrosine-protein phosphatase D, repeat 2; Receptor-type ...
 438-674 3.16e-56

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: 193.41  E-value: 3.16e-56
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720354236 438 AKLPQNISKNRYRDISPYDATRVLL---KGNE--DYINANYINMEIPSSSiinqYIACQGPLPHTCKDFWQMTWEQGSSM 512
Cdd:cd14628    47 ANLPCNKFKNRLVNIMPYESTRVCLqpiRGVEgsDYINASFIDGYRQQKA----YIATQGPLAETTEDFWRMLWEHNSTI 122

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720354236 513 VVMLTTQVERGRVKCHQYWPePSESSSYGCYQVTCHSEEGNPAYIFRKMTLFNQEKNESRQLTQIQYTAWPDHGVPDDSS 592
Cdd:cd14628   123 VVMLTKLREMGREKCHQYWP-AERSARYQYFVVDPMAEYNMPQYILREFKVTDARDGQSRTVRQFQFTDWPEQGVPKSGE 201

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720354236 593 DFLDFV--CHVRDQRAGKEEPIIVHCSAGIGRTGVLITMETAMCLIECNQPVYPLDIVRTMRDQRAMMIQTPSQYRFVCE 670
Cdd:cd14628   202 GFIDFIgqVHKTKEQFGQDGPISVHCSAGVGRTGVFITLSIVLERMRYEGVVDIFQTVKMLRTQRPAMVQTEDQYQFCYR 281


                  ....
gi 1720354236 671 AILK 674
Cdd:cd14628   282 AALE 285
PTPc-N22 cd14602
catalytic domain of tyrosine-protein phosphatase non-receptor type 22; Tyrosine-protein ...
 446-676 4.33e-56

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: 190.82  E-value: 4.33e-56
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720354236 446 KNRYRDISPYDATRVLLK-----GNEDYINANYIN-MEIPSSsiinqYIACQGPLPHTCKDFWQMTWEQGSSMVVMLTTQ 519
Cdd:cd14602     1 KNRYKDILPYDHSRVELSlitsdEDSDYINANFIKgVYGPRA-----YIATQGPLSTTLLDFWRMIWEYSVLIIVMACME 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720354236 520 VERGRVKCHQYWPEPSESS-SYGCYQVTCHSEEGNPAYIFRkmTLFNQEKNESRQLTQIQYTAWPDHGVPDDSSDFLDFV 598
Cdd:cd14602    76 FEMGKKKCERYWAEPGEMQlEFGPFSVTCEAEKRKSDYIIR--TLKVKFNSETRTIYQFHYKNWPDHDVPSSIDPILELI 153

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720354236 599 CHVRDQRAGKEEPIIVHCSAGIGRTGVLITME-TAMCL----IECNQPVYplDIVRTMRDQRAMMIQTPSQYRFVCEAIL 673
Cdd:cd14602   154 WDVRCYQEDDSVPICIHCSAGCGRTGVICAIDyTWMLLkdgiIPENFSVF--SLIQEMRTQRPSLVQTKEQYELVYNAVI 231


                  ...
gi 1720354236 674 KVY 676
Cdd:cd14602   232 ELF 234
R-PTP-S-2 cd14627
PTP-like domain of receptor-type tyrosine-protein phosphatase S, repeat 2; Receptor-type ...
 415-674 5.63e-56

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: 192.64  E-value: 5.63e-56
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720354236 415 ITGTVLaQFDQLYRKKPGMT-MSCAKLPQNISKNRYRDISPYDATRVLL---KGNE--DYINANYINMEIPSSSiinqYI 488
Cdd:cd14627    25 VTGMEL-EFKRLANSKAHTSrFISANLPCNKFKNRLVNIMPYETTRVCLqpiRGVEgsDYINASFIDGYRQQKA----YI 99

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720354236 489 ACQGPLPHTCKDFWQMTWEQGSSMVVMLTTQVERGRVKCHQYWPePSESSSYGCYQVTCHSEEGNPAYIFRKMTLFNQEK 568
Cdd:cd14627   100 ATQGPLAETTEDFWRMLWENNSTIVVMLTKLREMGREKCHQYWP-AERSARYQYFVVDPMAEYNMPQYILREFKVTDARD 178

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720354236 569 NESRQLTQIQYTAWPDHGVPDDSSDFLDFV--CHVRDQRAGKEEPIIVHCSAGIGRTGVLITMETAMCLIECNQPVYPLD 646
Cdd:cd14627   179 GQSRTVRQFQFTDWPEQGVPKSGEGFIDFIgqVHKTKEQFGQDGPISVHCSAGVGRTGVFITLSIVLERMRYEGVVDIFQ 258

                         250       260
                  ....*....|....*....|....*...
gi 1720354236 647 IVRTMRDQRAMMIQTPSQYRFVCEAILK 674
Cdd:cd14627   259 TVKMLRTQRPAMVQTEDEYQFCYQAALE 286
R-PTPc-typeIIb-1 cd14555
catalytic domain of type IIb (or R2B) subfamily receptor-type tyrosine-protein phosphatases, ...
 468-674 8.39e-56

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: 188.97  E-value: 8.39e-56
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720354236 468 YINANYINMEIPSssiiNQYIACQGPLPHTCKDFWQMTWEQGSSMVVMLTTQVERGRVKCHQYWPEPSESssYGCYQVTC 547
Cdd:cd14555     1 YINANYIDGYHRP----NHYIATQGPMQETVYDFWRMVWQENSASIVMVTNLVEVGRVKCSRYWPDDTEV--YGDIKVTL 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720354236 548 HSEEGNPAYIFRKMTLFNQEKNESRQLTQIQYTAWPDHGVPDDSSDFLDFVCHVRDQRAGKEEPIIVHCSAGIGRTGVLI 627
Cdd:cd14555    75 VETEPLAEYVVRTFALERRGYHEIREVRQFHFTGWPDHGVPYHATGLLGFIRRVKASNPPSAGPIVVHCSAGAGRTGCYI 154

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*..
gi 1720354236 628 TMETAMCLIECNQPVYPLDIVRTMRDQRAMMIQTPSQYRFVCEAILK 674
Cdd:cd14555   155 VIDIMLDMAEREGVVDIYNCVKELRSRRVNMVQTEEQYIFIHDAILE 201
R-PTPc-D-1 cd14624
catalytic domain of receptor-type tyrosine-protein phosphatase D, repeat 1; Receptor-type ...
 422-674 1.12e-55

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: 191.48  E-value: 1.12e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720354236 422 QFDQLYRK-KPG--MTMSCAKLPQNISKNRYRDISPYDATRVLLKGNE-----DYINANYINmeipSSSIINQYIACQGP 493
Cdd:cd14624    23 KFSQEYESiDPGqqFTWEHSNLEVNKPKNRYANVIAYDHSRVLLSAIEgipgsDYINANYID----GYRKQNAYIATQGA 98

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720354236 494 LPHTCKDFWQMTWEQGSSMVVMLTTQVERGRVKCHQYWPEPSeSSSYGCYQVTCHSEEGNPAYIFRKMTLFNQEKNESRQ 573
Cdd:cd14624    99 LPETFGDFWRMIWEQRSATVVMMTKLEERSRVKCDQYWPSRG-TETYGLIQVTLLDTVELATYCVRTFALYKNGSSEKRE 177

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720354236 574 LTQIQYTAWPDHGVPDDSSDFLDFVCHVRDQRAGKEEPIIVHCSAGIGRTGVLITMETAMCLIECNQPVYPLDIVRTMRD 653
Cdd:cd14624   178 VRQFQFTAWPDHGVPEHPTPFLAFLRRVKTCNPPDAGPMVVHCSAGVGRTGCFIVIDAMLERIKHEKTVDIYGHVTLMRA 257

                         250       260
                  ....*....|....*....|.
gi 1720354236 654 QRAMMIQTPSQYRFVCEAILK 674
Cdd:cd14624   258 QRNYMVQTEDQYIFIHDALLE 278
PTPc-N12 cd14604
catalytic domain of tyrosine-protein phosphatase non-receptor type 12; Tyrosine-protein ...
 442-678 1.69e-55

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: 191.30  E-value: 1.69e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720354236 442 QNISKNRYRDISPYDATRVLL-----KGNEDYINANYIN-MEIPSSsiinqYIACQGPLPHTCKDFWQMTWEQGSSMVVM 515
Cdd:cd14604    56 ENVKKNRYKDILPFDHSRVKLtlktsSQDSDYINANFIKgVYGPKA-----YIATQGPLANTVIDFWRMIWEYNVAIIVM 130

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720354236 516 LTTQVERGRVKCHQYWPEPSESS-SYGCYQVTCHSEEGNPAYIFRkmTLFNQEKNESRQLTQIQYTAWPDHGVPDDSSDF 594
Cdd:cd14604   131 ACREFEMGRKKCERYWPLYGEEPmTFGPFRISCEAEQARTDYFIR--TLLLEFQNETRRLYQFHYVNWPDHDVPSSFDSI 208

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720354236 595 LDFVCHVRDQRAGKEEPIIVHCSAGIGRTGVLITMETAMCLIECNQ-----PVYPLdiVRTMRDQRAMMIQTPSQYRFVC 669
Cdd:cd14604   209 LDMISLMRKYQEHEDVPICIHCSAGCGRTGAICAIDYTWNLLKAGKipeefNVFNL--IQEMRTQRHSAVQTKEQYELVH 286


                  ....*....
gi 1720354236 670 EAILKVYEE 678
Cdd:cd14604   287 RAIAQLFEK 295
R-PTP-N cd14609
PTP-like domain of receptor-type tyrosine-protein phosphatase N; Receptor-type ...
 427-672 2.65e-55

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: 190.25  E-value: 2.65e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720354236 427 YRKKPGmTMSCAKLPQNISKNRYRDISPYDATRVLLKGNEDYINANYINmeipSSSIINQ------YIACQGPLPHTCKD 500
Cdd:cd14609    27 YQAEPN-TCSTAQGEANVKKNRNPDFVPYDHARIKLKAESNPSRSDYIN----ASPIIEHdprmpaYIATQGPLSHTIAD 101

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720354236 501 FWQMTWEQGSSMVVMLTTQVERGRVKCHQYWPEPSeSSSYGCYQVTCHSEE-GNPAYIFRKMTLFNQEKNESRQLTQIQY 579
Cdd:cd14609   102 FWQMVWENGCTVIVMLTPLVEDGVKQCDRYWPDEG-SSLYHIYEVNLVSEHiWCEDFLVRSFYLKNVQTQETRTLTQFHF 180

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720354236 580 TAWPDHGVPDDSSDFLDFVCHVRDQRAGKEEPIIVHCSAGIGRTGVLITMEtaMCLIECNQPVYPLDIVRTM---RDQRA 656
Cdd:cd14609   181 LSWPAEGIPSSTRPLLDFRRKVNKCYRGRSCPIIVHCSDGAGRTGTYILID--MVLNRMAKGVKEIDIAATLehvRDQRP 258

                         250
                  ....*....|....*.
gi 1720354236 657 MMIQTPSQYRFVCEAI 672
Cdd:cd14609   259 GMVRTKDQFEFALTAV 274
R-PTPc-S-1 cd14625
catalytic domain of receptor-type tyrosine-protein phosphatase S, repeat 1; Receptor-type ...
 431-674 3.03e-55

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: 190.30  E-value: 3.03e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720354236 431 PG--MTMSCAKLPQNISKNRYRDISPYDATRVLLKGNE-----DYINANYINmeipSSSIINQYIACQGPLPHTCKDFWQ 503
Cdd:cd14625    33 PGqqFTWEHSNLEVNKPKNRYANVIAYDHSRVILQPIEgimgsDYINANYID----GYRKQNAYIATQGPLPETFGDFWR 108

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720354236 504 MTWEQGSSMVVMLTTQVERGRVKCHQYWPEPSeSSSYGCYQVTCHSEEGNPAYIFRKMTLFNQEKNESRQLTQIQYTAWP 583
Cdd:cd14625   109 MVWEQRSATVVMMTKLEEKSRIKCDQYWPSRG-TETYGMIQVTLLDTIELATFCVRTFSLHKNGSSEKREVRQFQFTAWP 187

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720354236 584 DHGVPDDSSDFLDFVCHVRDQRAGKEEPIIVHCSAGIGRTGVLITMETAMCLIECNQPVYPLDIVRTMRDQRAMMIQTPS 663
Cdd:cd14625   188 DHGVPEYPTPFLAFLRRVKTCNPPDAGPIVVHCSAGVGRTGCFIVIDAMLERIKHEKTVDIYGHVTLMRSQRNYMVQTED 267

                         250
                  ....*....|.
gi 1720354236 664 QYRFVCEAILK 674
Cdd:cd14625   268 QYSFIHDALLE 278
R-PTP-F-2 cd14629
PTP-like domain of receptor-type tyrosine-protein phosphatase F, repeat 2; Receptor-type ...
 438-674 9.28e-55

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: 189.17  E-value: 9.28e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720354236 438 AKLPQNISKNRYRDISPYDATRVLL---KGNE--DYINANYINMEIPSSSiinqYIACQGPLPHTCKDFWQMTWEQGSSM 512
Cdd:cd14629    48 ANLPCNKFKNRLVNIMPYELTRVCLqpiRGVEgsDYINASFIDGYRQQKA----YIATQGPLAETTEDFWRMLWEHNSTI 123

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720354236 513 VVMLTTQVERGRVKCHQYWPePSESSSYGCYQVTCHSEEGNPAYIFRKMTLFNQEKNESRQLTQIQYTAWPDHGVPDDSS 592
Cdd:cd14629   124 VVMLTKLREMGREKCHQYWP-AERSARYQYFVVDPMAEYNMPQYILREFKVTDARDGQSRTIRQFQFTDWPEQGVPKTGE 202

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720354236 593 DFLDFV--CHVRDQRAGKEEPIIVHCSAGIGRTGVLITMETAMCLIECNQPVYPLDIVRTMRDQRAMMIQTPSQYRFVCE 670
Cdd:cd14629   203 GFIDFIgqVHKTKEQFGQDGPITVHCSAGVGRTGVFITLSIVLERMRYEGVVDMFQTVKTLRTQRPAMVQTEDQYQLCYR 282


                  ....
gi 1720354236 671 AILK 674
Cdd:cd14629   283 AALE 286
R-PTP-N2 cd14610
PTP-like domain of receptor-type tyrosine-protein phosphatase N2; Receptor-type ...
 427-672 1.01e-54

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: 189.11  E-value: 1.01e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720354236 427 YRKKPGMTmSCAKLPQNISKNRYRDISPYDATRVLLKGNEDYINANYINmeipSSSIINQ------YIACQGPLPHTCKD 500
Cdd:cd14610    29 YQAEPNAT-NVAQREENVQKNRSLAVLPYDHSRIILKAENSHSHSDYIN----ASPIMDHdprnpaYIATQGPLPATVAD 103

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720354236 501 FWQMTWEQGSSMVVMLTTQVERGRVKCHQYWPEPSeSSSYGCYQVTCHSEE-GNPAYIFRKMTLFNQEKNESRQLTQIQY 579
Cdd:cd14610   104 FWQMVWESGCVVIVMLTPLAENGVKQCYHYWPDEG-SNLYHIYEVNLVSEHiWCEDFLVRSFYLKNLQTNETRTVTQFHF 182

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720354236 580 TAWPDHGVPDDSSDFLDFVCHVRDQRAGKEEPIIVHCSAGIGRTGVLITMEtaMCLIECNQPVYPLDIVRT---MRDQRA 656
Cdd:cd14610   183 LSWNDQGVPASTRSLLDFRRKVNKCYRGRSCPIIVHCSDGAGRSGTYILID--MVLNKMAKGAKEIDIAATlehLRDQRP 260

                         250
                  ....*....|....*.
gi 1720354236 657 MMIQTPSQYRFVCEAI 672
Cdd:cd14610   261 GMVQTKEQFEFALTAV 276
R-PTPc-T-1 cd14630
catalytic domain of receptor-type tyrosine-protein phosphatase T, repeat 1; Receptor-type ...
 442-674 1.42e-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: 186.77  E-value: 1.42e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720354236 442 QNISKNRYRDISPYDATRV---LLKGN--EDYINANYINmeipSSSIINQYIACQGPLPHTCKDFWQMTWEQGSSMVVML 516
Cdd:cd14630     2 ENRNKNRYGNIISYDHSRVrlqLLDGDphSDYINANYID----GYHRPRHYIATQGPMQETVKDFWRMIWQENSASVVMV 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720354236 517 TTQVERGRVKCHQYWPEPSESssYGCYQVTCHSEEGNPAYIFRKMTLFNQEKNESRQLTQIQYTAWPDHGVPDDSSDFLD 596
Cdd:cd14630    78 TNLVEVGRVKCVRYWPDDTEV--YGDIKVTLIETEPLAEYVIRTFTVQKKGYHEIREIRQFHFTSWPDHGVPCYATGLLG 155

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1720354236 597 FVCHVRDQRAGKEEPIIVHCSAGIGRTGVLITMETAMCLIECNQPVYPLDIVRTMRDQRAMMIQTPSQYRFVCEAILK 674
Cdd:cd14630   156 FVRQVKFLNPPDAGPIVVHCSAGAGRTGCFIAIDIMLDMAENEGVVDIFNCVRELRAQRVNMVQTEEQYVFVHDAILE 233
R-PTPc-G-1 cd17667
catalytic domain of receptor-type tyrosine-protein phosphatase G, repeat 1; Receptor-type ...
 421-674 1.14e-53

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: 185.62  E-value: 1.14e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720354236 421 AQFDQLYRKKPGMTMSC--AKLPQNISKNRYRDISPYDATRVLLK-------GNEDYINANYINmeipSSSIINQYIACQ 491
Cdd:cd17667     3 EDFEEVQRCTADMNITAehSNHPDNKHKNRYINILAYDHSRVKLRplpgkdsKHSDYINANYVD----GYNKAKAYIATQ 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720354236 492 GPLPHTCKDFWQMTWEQGSSMVVMLTTQVERGRVKCHQYWPEpSESSSYGCYQVTCHSEEGNPAYIFRKMTLFN------ 565
Cdd:cd17667    79 GPLKSTFEDFWRMIWEQNTGIIVMITNLVEKGRRKCDQYWPT-ENSEEYGNIIVTLKSTKIHACYTVRRFSIRNtkvkkg 157

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720354236 566 QEKN-----ESRQLTQIQYTAWPDHGVPDDSSDFLDFVCHVRDQRAGKEEPIIVHCSAGIGRTGVLITMETAMCLIECNQ 640
Cdd:cd17667   158 QKGNpkgrqNERTVIQYHYTQWPDMGVPEYALPVLTFVRRSSAARTPEMGPVLVHCSAGVGRTGTYIVIDSMLQQIKDKS 237

                         250       260       270
                  ....*....|....*....|....*....|....
gi 1720354236 641 PVYPLDIVRTMRDQRAMMIQTPSQYRFVCEAILK 674
Cdd:cd17667   238 TVNVLGFLKHIRTQRNYLVQTEEQYIFIHDALLE 271
PTPc-N7 cd14612
catalytic domain of tyrosine-protein phosphatase non-receptor type 7; Tyrosine-protein ...
 440-668 1.73e-53

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: 184.27  E-value: 1.73e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720354236 440 LPQNISKNRYRDISPYDATRVLLKG------NEDYINANYINMEIPSSSIinqYIACQGPLPHTCKDFWQMTWEQGSSMV 513
Cdd:cd14612    12 IPGHASKDRYKTILPNPQSRVCLRRagsqeeEGSYINANYIRGYDGKEKA---YIATQGPMLNTVSDFWEMVWQEECPII 88

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720354236 514 VMLtTQVERGRVKCHQYWPEpsESSSYGCYQVTCHSEEGNPAYIFRKMTLfnQEKNESRQLTQIQYTAWPDHGVPDDSSD 593
Cdd:cd14612    89 VMI-TKLKEKKEKCVHYWPE--KEGTYGRFEIRVQDMKECDGYTIRDLTI--QLEEESRSVKHYWFSSWPDHQTPESAGP 163

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1720354236 594 FLDFVCHVRDQR--AGKEEPIIVHCSAGIGRTGVLITMETAMCLIECNQPVYPLDIVRTMRDQRAMMIQTPSQYRFV 668
Cdd:cd14612   164 LLRLVAEVEESRqtAASPGPIVVHCSAGIGRTGCFIATSIGCQQLKDTGKVDILGIVCQLRLDRGGMIQTSEQYQFL 240
R-PTP-N-N2 cd14546
PTP-like domain of receptor-type tyrosine-protein phosphatase-like N and N2; Receptor-type ...
 468-672 3.96e-53

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: 181.87  E-value: 3.96e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720354236 468 YINANYINMEIPSSSIinqYIACQGPLPHTCKDFWQMTWEQGSSMVVMLTTQVERGRVKCHQYWPEpSESSSYGCYQVTC 547
Cdd:cd14546     1 YINASTIYDHDPRNPA---YIATQGPLPHTIADFWQMIWEQGCVVIVMLTRLQENGVKQCARYWPE-EGSEVYHIYEVHL 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720354236 548 HSEEG-NPAYIFRKMTLFNQEKNESRQLTQIQYTAWPDHGVPDDSSDFLDFVCHVRDQRAGKEEPIIVHCSAGIGRTGVL 626
Cdd:cd14546    77 VSEHIwCDDYLVRSFYLKNLQTSETRTVTQFHFLSWPDEGIPASAKPLLEFRRKVNKSYRGRSCPIVVHCSDGAGRTGTY 156

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*....
gi 1720354236 627 ITMEtaMCLIECNQPVYPLDIVRT---MRDQRAMMIQTPSQYRFVCEAI 672
Cdd:cd14546   157 ILID--MVLNRMAKGAKEIDIAATlehLRDQRPGMVKTKDQFEFVLTAV 203
R-PTPc-K-1 cd14631
catalytic domain of receptor-type tyrosine-protein phosphatase K, repeat 1; Receptor-type ...
 459-674 4.36e-51

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: 176.75  E-value: 4.36e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720354236 459 RVLLKGNE-----DYINANYIN-MEIPSssiinQYIACQGPLPHTCKDFWQMTWEQGSSMVVMLTTQVERGRVKCHQYWP 532
Cdd:cd14631     1 RVILQPVEddpssDYINANYIDgYQRPS-----HYIATQGPVHETVYDFWRMIWQEQSACIVMVTNLVEVGRVKCYKYWP 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720354236 533 EPSESssYGCYQVTCHSEEGNPAYIFRKMTLFNQEKNESRQLTQIQYTAWPDHGVPDDSSDFLDFVCHVRDQRAGKEEPI 612
Cdd:cd14631    76 DDTEV--YGDFKVTCVEMEPLAEYVVRTFTLERRGYNEIREVKQFHFTGWPDHGVPYHATGLLSFIRRVKLSNPPSAGPI 153

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1720354236 613 IVHCSAGIGRTGVLITMETAMCLIECNQPVYPLDIVRTMRDQRAMMIQTPSQYRFVCEAILK 674
Cdd:cd14631   154 VVHCSAGAGRTGCYIVIDIMLDMAEREGVVDIYNCVKALRSRRINMVQTEEQYIFIHDAILE 215
R-PTPc-Q cd14616
catalytic domain of receptor-type tyrosine-protein phosphatase Q; Receptor-type ...
 447-670 5.78e-51

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: 176.64  E-value: 5.78e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720354236 447 NRYRDISPYDATRVLLKGN-----EDYINANYINMEIPSssiiNQYIACQGPLPHTCKDFWQMTWEQGSSMVVMLTTQVE 521
Cdd:cd14616     1 NRFPNIKPYNNNRVKLIADagvpgSDYINASYISGYLCP----NEFIATQGPLPGTVGDFWRMVWETRAKTIVMLTQCFE 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720354236 522 RGRVKCHQYWPEPSESSS-YGCYQVTCHSEEGNPAYIFRKMTLfnQEKNESRQLTQIQYTAWPDHGVPDDSSDFLDFVCH 600
Cdd:cd14616    77 KGRIRCHQYWPEDNKPVTvFGDIVITKLMEDVQIDWTIRDLKI--ERHGDYMMVRQCNFTSWPEHGVPESSAPLIHFVKL 154

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720354236 601 VRDQRAGKEEPIIVHCSAGIGRTGVLITMETAMCLIECNQPVYPLDIVRTMRDQRAMMIQTPSQYRFVCE 670
Cdd:cd14616   155 VRASRAHDNTPMIVHCSAGVGRTGVFIALDHLTQHINDHDFVDIYGLVAELRSERMCMVQNLAQYIFLHQ 224
R-PTPc-E-1 cd14620
catalytic domain of receptor-type tyrosine-protein phosphatase E, repeat 1; Receptor-type ...
 449-674 4.32e-50

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: 174.36  E-value: 4.32e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720354236 449 YRDISPYDATRVLL---KGN--EDYINANYINmeipSSSIINQYIACQGPLPHTCKDFWQMTWEQGSSMVVMLTTQVERG 523
Cdd:cd14620     1 YPNILPYDHSRVILsqlDGIpcSDYINASYID----GYKEKNKFIAAQGPKQETVNDFWRMVWEQKSATIVMLTNLKERK 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720354236 524 RVKCHQYWPEPSeSSSYGCYQVTCHSEEGNPAYIFRKMTLFNQEKNES---RQLTQIQYTAWPDHGVPDDSSDFLDFVCH 600
Cdd:cd14620    77 EEKCYQYWPDQG-CWTYGNIRVAVEDCVVLVDYTIRKFCIQPQLPDGCkapRLVTQLHFTSWPDFGVPFTPIGMLKFLKK 155

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1720354236 601 VRDQRAGKEEPIIVHCSAGIGRTGVLITMETAMCLIECNQPVYPLDIVRTMRDQRAMMIQTPSQYRFVCEAILK 674
Cdd:cd14620   156 VKSVNPVHAGPIVVHCSAGVGRTGTFIVIDAMIDMMHAEQKVDVFEFVSRIRNQRPQMVQTDMQYSFIYQALLE 229
R-PTPc-U-1 cd14632
catalytic domain of receptor-type tyrosine-protein phosphatase U, repeat 1; Receptor-type ...
 468-674 7.19e-50

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: 172.93  E-value: 7.19e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720354236 468 YINANYINMEIPSssiiNQYIACQGPLPHTCKDFWQMTWEQGSSMVVMLTTQVERGRVKCHQYWPEpsESSSYGCYQVTC 547
Cdd:cd14632     1 YINANYIDGYHRS----NHFIATQGPKQEMVYDFWRMVWQEHCSSIVMITKLVEVGRVKCSKYWPD--DSDTYGDIKITL 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720354236 548 HSEEGNPAYIFRKMTLFNQEKNESRQLTQIQYTAWPDHGVPDDSSDFLDFVCHVRDQRAGKEEPIIVHCSAGIGRTGVLI 627
Cdd:cd14632    75 LKTETLAEYSVRTFALERRGYSARHEVKQFHFTSWPEHGVPYHATGLLAFIRRVKASTPPDAGPVVVHCSAGAGRTGCYI 154

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*..
gi 1720354236 628 TMETAMCLIECNQPVYPLDIVRTMRDQRAMMIQTPSQYRFVCEAILK 674
Cdd:cd14632   155 VLDVMLDMAECEGVVDIYNCVKTLCSRRINMIQTEEQYIFIHDAILE 201
R-PTPc-M-1 cd14633
catalytic domain of receptor-type tyrosine-protein phosphatase M, repeat 1; Receptor-type ...
 438-674 1.09e-49

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: 174.85  E-value: 1.09e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720354236 438 AKLPQNISKNRYRDISPYDATRVLLK-----GNEDYINANYINmeipSSSIINQYIACQGPLPHTCKDFWQMTWEQGSSM 512
Cdd:cd14633    35 AKKDENRMKNRYGNIIAYDHSRVRLQpiegeTSSDYINGNYID----GYHRPNHYIATQGPMQETIYDFWRMVWHENTAS 110

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720354236 513 VVMLTTQVERGRVKCHQYWPEPSESssYGCYQVTCHSEEGNPAYIFRKMTLFNQEKNESRQLTQIQYTAWPDHGVPDDSS 592
Cdd:cd14633   111 IIMVTNLVEVGRVKCCKYWPDDTEI--YKDIKVTLIETELLAEYVIRTFAVEKRGVHEIREIRQFHFTGWPDHGVPYHAT 188

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720354236 593 DFLDFVCHVRDQRAGKEEPIIVHCSAGIGRTGVLITMETAMCLIECNQPVYPLDIVRTMRDQRAMMIQTPSQYRFVCEAI 672
Cdd:cd14633   189 GLLGFVRQVKSKSPPNAGPLVVHCSAGAGRTGCFIVIDIMLDMAEREGVVDIYNCVRELRSRRVNMVQTEEQYVFIHDAI 268


                  ..
gi 1720354236 673 LK 674
Cdd:cd14633   269 LE 270
R-PTPc-C-1 cd14557
catalytic domain of receptor-type tyrosine-protein phosphatase C, repeat 1; Receptor-type ...
 468-668 2.39e-49

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: 171.55  E-value: 2.39e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720354236 468 YINANYIN-MEIPsssiiNQYIACQGPLPHTCKDFWQMTWEQGSSMVVMLTTQVERGRVKCHQYWPEPSE-SSSYGCYQV 545
Cdd:cd14557     1 YINASYIDgFKEP-----RKYIAAQGPKDETVDDFWRMIWEQKSTVIVMVTRCEEGNRNKCAQYWPSMEEgSRAFGDVVV 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720354236 546 TCHSEEGNPAYIFRKMTLFN-QEKNESRQLTQIQYTAWPDHGVPDDSSDFLDFVCHVRDQRAGKEEPIIVHCSAGIGRTG 624
Cdd:cd14557    76 KINEEKICPDYIIRKLNINNkKEKGSGREVTHIQFTSWPDHGVPEDPHLLLKLRRRVNAFNNFFSGPIVVHCSAGVGRTG 155

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....
gi 1720354236 625 VLITMETAMCLIECNQPVYPLDIVRTMRDQRAMMIQTPSQYRFV 668
Cdd:cd14557   156 TYIGIDAMLEGLEAEGRVDVYGYVVKLRRQRCLMVQVEAQYILI 199
PTPc-N21 cd14598
catalytic domain of tyrosine-protein phosphatase non-receptor type 21; Tyrosine-protein ...
 468-674 2.25e-48

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: 169.39  E-value: 2.25e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720354236 468 YINANYINMEIpsSSIINQYIACQGPLPHTCKDFWQMTWEQGSSMVVMLTTQVERGRVKCHQYWP---EPSESSSYGCYQ 544
Cdd:cd14598     1 YINASHIKVTV--GGKEWDYIATQGPLQNTCQDFWQMVWEQGVAIIAMVTAEEEGGREKSFRYWPrlgSRHNTVTYGRFK 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720354236 545 VTCHSEEGNPAYIFRKMTLFNQEKNESRQLTQIQYTAWPDHGVPDDSSDFLDFVCHVRDQR---------AGKEEPIIVH 615
Cdd:cd14598    79 ITTRFRTDSGCYATTGLKIKHLLTGQERTVWHLQYTDWPEHGCPEDLKGFLSYLEEIQSVRrhtnstidpKSPNPPVLVH 158

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1720354236 616 CSAGIGRTGVLITMETAMCLIECNQpvyPLDIVRT---MRDQRAMMIQTPSQYRFVCEAILK 674
Cdd:cd14598   159 CSAGVGRTGVVILSEIMIACLEHNE---MLDIPRVldmLRQQRMMMVQTLSQYTFVYKVLIQ 217
R-PTPc-Z-1 cd17668
catalytic domain of receptor-type tyrosine-protein phosphatase Z, repeat 1; Receptor-type ...
 468-673 8.68e-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: 167.46  E-value: 8.68e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720354236 468 YINANYIN-MEIPSSsiinqYIACQGPLPHTCKDFWQMTWEQGSSMVVMLTTQVERGRVKCHQYWPEPSeSSSYGCYQVT 546
Cdd:cd17668     1 YINANYVDgYNKPKA-----YIAAQGPLKSTAEDFWRMIWEHNVEVIVMITNLVEKGRRKCDQYWPADG-SEEYGNFLVT 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720354236 547 CHSEEGNPAYIFRKMTLFNQE--------KNESRQLTQIQYTAWPDHGVPDDSSDFLDFVCHVRDQRAGKEEPIIVHCSA 618
Cdd:cd17668    75 QKSVQVLAYYTVRNFTLRNTKikkgsqkgRPSGRVVTQYHYTQWPDMGVPEYTLPVLTFVRKASYAKRHAVGPVVVHCSA 154

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1720354236 619 GIGRTGVLITMETAMCLIECNQPVYPLDIVRTMRDQRAMMIQTPSQYRFVCEAIL 673
Cdd:cd17668   155 GVGRTGTYIVLDSMLQQIQHEGTVNIFGFLKHIRSQRNYLVQTEEQYVFIHDALV 209
R-PTPc-A-2 cd14623
catalytic domain of receptor-type tyrosine-protein phosphatase A, repeat 2; Receptor-type ...
 448-667 2.33e-47

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: 167.14  E-value: 2.33e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720354236 448 RYRDISPYDATRVLL-----KGNEDYINANYINMEIPSSSiinqYIACQGPLPHTCKDFWQMTWEQGSSMVVMLTTQVER 522
Cdd:cd14623     1 RVLQIIPYEFNRVIIpvkrgEENTDYVNASFIDGYRQKDS----YIASQGPLQHTIEDFWRMIWEWKSCSIVMLTELEER 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720354236 523 GRVKCHQYWPEPSeSSSYGCYQVTCHSEEGNPAYIFRKMTLFNQEKNESRQLTQIQYTAWPDHGVPDDSSDFLDFVCHV- 601
Cdd:cd14623    77 GQEKCAQYWPSDG-SVSYGDITIELKKEEECESYTVRDLLVTNTRENKSRQIRQFHFHGWPEVGIPSDGKGMINIIAAVq 155

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1720354236 602 RDQRAGKEEPIIVHCSAGIGRTGVLITMETAMCLIECNQPVYPLDIVRTMRDQRAMMIQTPSQYRF 667
Cdd:cd14623   156 KQQQQSGNHPITVHCSAGAGRTGTFCALSTVLERVKAEGILDVFQTVKSLRLQRPHMVQTLEQYEF 221
R-PTPc-A-E-2 cd14552
catalytic domain of receptor-type tyrosine-protein phosphatase A and E, repeat 2; ...
 468-672 5.90e-47

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: 164.75  E-value: 5.90e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720354236 468 YINANYINmeipSSSIINQYIACQGPLPHTCKDFWQMTWEQGSSMVVMLTTQVERGRVKCHQYWPEPSeSSSYGCYQVTC 547
Cdd:cd14552     1 YINASFID----GYRQKDAYIATQGPLDHTVEDFWRMIWEWKSCSIVMLTEIKERSQNKCAQYWPEDG-SVSSGDITVEL 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720354236 548 HSEEGNPAYIFRKMTLFNQEKNESRQLTQIQYTAWPDHGVPDDSSDFLDFVCHV-RDQRAGKEEPIIVHCSAGIGRTGVL 626
Cdd:cd14552    76 KDQTDYEDYTLRDFLVTKGKGGSTRTVRQFHFHGWPEVGIPDNGKGMIDLIAAVqKQQQQSGNHPITVHCSAGAGRTGTF 155

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*.
gi 1720354236 627 ITMETAMCLIECNQPVYPLDIVRTMRDQRAMMIQTPSQYRFVCEAI 672
Cdd:cd14552   156 CALSTVLERVKAEGVLDVFQVVKSLRLQRPHMVQTLEQYEFCYKVV 201
PTP-N23 cd14539
PTP-like domain of tyrosine-protein phosphatase non-receptor type 23; Tyrosine-protein ...
 468-667 6.56e-47

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: 164.86  E-value: 6.56e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720354236 468 YINANYINMEIPSSSiinQYIACQGPLPHTCKDFWQMTWEQGSSMVVMLTTQVERGRVKCHQYWP-EPSESSSYGCYQVT 546
Cdd:cd14539     1 YINASLIEDLTPYCP---RFIATQAPLPGTAADFWLMVYEQQVSVIVMLVSEQENEKQKVHRYWPtERGQALVYGAITVS 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720354236 547 CHSEEGNPAYIFRKMTLFNQEKNESRQLTQIQYTAWPDHGVPDDSSDFLDFV----CHVRDQRaGKEEPIIVHCSAGIGR 622
Cdd:cd14539    78 LQSVRTTPTHVERIISIQHKDTRLSRSVVHLQFTTWPELGLPDSPNPLLRFIeevhSHYLQQR-SLQTPIVVHCSSGVGR 156

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*.
gi 1720354236 623 TGVLITMETAMCLIECNQPVYPL-DIVRTMRDQRAMMIQTPSQYRF 667
Cdd:cd14539   157 TGAFCLLYAAVQEIEAGNGIPDLpQLVRKMRQQRKYMLQEKEHLKF 202
FERM_C_PTPN4_PTPN3_like cd13189
FERM domain C-lobe of Protein tyrosine phosphatase non-receptor proteins 3 and 4 (PTPN4 and ...
 1-74 6.86e-46

FERM domain C-lobe of Protein tyrosine phosphatase non-receptor proteins 3 and 4 (PTPN4 and PTPN3); PTPN4 (also called PTPMEG, protein tyrosine phosphatase, megakaryocyte) is a cytoplasmic protein-tyrosine phosphatase (PTP) thought to play a role in cerebellar function. PTPMEG-knockout mice have impaired memory formation and cerebellar long-term depression. PTPN3/PTPH1 is a membrane-associated PTP that is implicated in regulating tyrosine phosphorylation of growth factor receptors, p97 VCP (valosin-containing protein, or Cdc48 in Saccharomyces cerevisiae), and HBV (Hepatitis B Virus) gene expression; it is mutated in a subset of colon cancers. PTPMEG and PTPN3/PTPH1 contains a N-terminal FERM domain, a middle PDZ domain, and a C-terminal phosphatase domain. PTP1/Tyrosine-protein phosphatase 1 from nematodes and a FERM_C repeat 1 from Tetraodon nigroviridis are also included in this cd. The FERM domain has a cloverleaf tripart structure composed of: (1) FERM_N (A-lobe or F1); (2) FERM_M (B-lobe, or F2); and (3) FERM_C (C-lobe or F3). The C-lobe within the FERM domain is part of the PH domain family. The FERM domain is found in the cytoskeletal-associated proteins such as ezrin, moesin, radixin, 4.1R, and merlin. These proteins provide a link between the membrane and cytoskeleton and are involved in signal transduction pathways. The FERM domain is also found in protein tyrosine phosphatases (PTPs) , the tyrosine kinases FAK and JAK, in addition to other proteins involved in signaling. This domain is structurally similar to the PH and PTB domains and consequently is capable of binding to both peptides and phospholipids at different sites.


Pssm-ID: 270010  Cd Length: 95  Bit Score: 157.86  E-value: 6.86e-46
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1720354236   1 MSGGILIYKNRVRMNTFLWLKIVKISFKCKQFFIQLRKELHESRETLLGFNMVNYRACKTLWKACVEHHTFFRL 74
Cdd:cd13189    22 SSAGILVFQNGIRINTFPWSKIVKISFKRKQFFIQLRREPNESRDTILGFNMLSYRACKNLWKSCVEHHTFFRL 95
PTPc-N5 cd14613
catalytic domain of tyrosine-protein phosphatase non-receptor type 5; Tyrosine-protein ...
 440-668 5.23e-45

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: 161.57  E-value: 5.23e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720354236 440 LPQNISKNRYRDISPYDATRVLLKGNED------YINANYINMEIPSSSIinqYIACQGPLPHTCKDFWQMTWEQGSSMV 513
Cdd:cd14613    22 IPGLVRKNRYKTILPNPHSRVCLTSPDQddplssYINANYIRGYGGEEKV---YIATQGPTVNTVGDFWRMVWQERSPII 98

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720354236 514 VMLtTQVERGRVKCHQYWPEpsESSSYGCYQVTCHSEEGNPAYIFRKMTLfnQEKNESRQLTQIQYTAWPDHGVPDDSSD 593
Cdd:cd14613    99 VMI-TNIEEMNEKCTEYWPE--EQVTYEGIEITVKQVIHADDYRLRLITL--KSGGEERGLKHYWYTSWPDQKTPDNAPP 173

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720354236 594 FLDFVCHVRDQRAGKEE---PIIVHCSAGIGRTGVLITmeTAMCLIEC-NQPVypLDIVRT---MRDQRAMMIQTPSQYR 666
Cdd:cd14613   174 LLQLVQEVEEARQQAEPncgPVIVHCSAGIGRTGCFIA--TSICCKQLrNEGV--VDILRTtcqLRLDRGGMIQTCEQYQ 249


                  ..
gi 1720354236 667 FV 668
Cdd:cd14613   250 FV 251
R-PTPc-A-1 cd14621
catalytic domain of receptor-type tyrosine-protein phosphatase A, repeat 1; Receptor-type ...
 434-679 1.72e-44

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: 161.34  E-value: 1.72e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720354236 434 TMSCAKLPQNISKNRYRDISPYDATRVLLKGNE-----DYINANYINmeipSSSIINQYIACQGPLPHTCKDFWQMTWEQ 508
Cdd:cd14621    43 TCEAASKEENKEKNRYVNILPYDHSRVHLTPVEgvpdsDYINASFIN----GYQEKNKFIAAQGPKEETVNDFWRMIWEQ 118

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720354236 509 GSSMVVMLTTQVERGRVKCHQYWPEPSeSSSYGCYQVTCHSEEGNPAYIFRKMTLFN----QEKNESRQLTQIQYTAWPD 584
Cdd:cd14621   119 NTATIVMVTNLKERKECKCAQYWPDQG-CWTYGNIRVSVEDVTVLVDYTVRKFCIQQvgdvTNKKPQRLITQFHFTSWPD 197

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720354236 585 HGVPDDSSDFLDFVCHVRDQRAGKEEPIIVHCSAGIGRTGVLITMETAMCLIECNQPVYPLDIVRTMRDQRAMMIQTPSQ 664
Cdd:cd14621   198 FGVPFTPIGMLKFLKKVKNCNPQYAGAIVVHCSAGVGRTGTFIVIDAMLDMMHAERKVDVYGFVSRIRAQRCQMVQTDMQ 277

                         250
                  ....*....|....*
gi 1720354236 665 YRFVCEAILKVYEEG 679
Cdd:cd14621   278 YVFIYQALLEHYLYG 292
R-PTPc-A-E-1 cd14551
catalytic domain of receptor-type tyrosine-protein phosphatase A and E, repeat 1; ...
 468-668 6.53e-44

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: 156.61  E-value: 6.53e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720354236 468 YINANYINmeipSSSIINQYIACQGPLPHTCKDFWQMTWEQGSSMVVMLTTQVERGRVKCHQYWPEPSESSsYGCYQVTC 547
Cdd:cd14551     1 YINASYID----GYQEKNKFIAAQGPKDETVNDFWRMIWEQGSATIVMVTNLKERKEKKCSQYWPDQGCWT-YGNLRVRV 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720354236 548 HSEEGNPAYIFRKMTL--FNQEKNESRQ--LTQIQYTAWPDHGVPDDSSDFLDFVCHVRDQRAGKEEPIIVHCSAGIGRT 623
Cdd:cd14551    76 EDTVVLVDYTTRKFCIqkVNRGIGEKRVrlVTQFHFTSWPDFGVPFTPIGMLKFLKKVKSANPPRAGPIVVHCSAGVGRT 155

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*
gi 1720354236 624 GVLITMETAMCLIECNQPVYPLDIVRTMRDQRAMMIQTPSQYRFV 668
Cdd:cd14551   156 GTFIVIDAMLDMMHAEGKVDVFGFVSRIRQQRSQMVQTDMQYVFI 200
PHA02738 PHA02738
hypothetical protein; Provisional
 442-676 1.15e-43

hypothetical protein; Provisional


Pssm-ID: 222923 [Multi-domain]  Cd Length: 320  Bit Score: 159.71  E-value: 1.15e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720354236 442 QNISKNRYRDISPYDATRVLL---KGNEDYINANYINmeipSSSIINQYIACQGPLPHTCKDFWQMTWEQGSSMVVMLTT 518
Cdd:PHA02738   48 KNRKLNRYLDAVCFDHSRVILpaeRNRGDYINANYVD----GFEYKKKFICGQAPTRQTCYDFYRMLWMEHVQIIVMLCK 123

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720354236 519 QVERGRVKCHQYWPEPSESS-SYGCYQVTCHSEEGNPAYIfrKMTLFNQEKNESRQ-LTQIQYTAWPDHGVPDDSSDFLD 596
Cdd:PHA02738  124 KKENGREKCFPYWSDVEQGSiRFGKFKITTTQVETHPHYV--KSTLLLTDGTSATQtVTHFNFTAWPDHDVPKNTSEFLN 201

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720354236 597 FVCHVRD-QRAGKEE------------PIIVHCSAGIGRTGVLITMETAMCLIECNQPVYPLDIVRTMRDQRAMMIQTPS 663
Cdd:PHA02738  202 FVLEVRQcQKELAQEslqighnrlqppPIVVHCNAGLGRTPCYCVVDISISRFDACATVSIPSIVSSIRNQRYYSLFIPF 281

                         250
                  ....*....|...
gi 1720354236 664 QYrFVCEAILKVY 676
Cdd:PHA02738  282 QY-FFCYRAVKRY 293
R-PTPc-R cd14611
catalytic domain of receptor-type tyrosine-protein phosphatase R; Receptor-type ...
 445-668 7.43e-43

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: 154.31  E-value: 7.43e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720354236 445 SKNRYRDISPYDATRVLLKGN------EDYINANYINmeiPSSSIINQYIACQGPLPHTCKDFWQMTWEQGSSMVVMLTT 518
Cdd:cd14611     1 TKNRYKTILPNPHSRVCLKPKnsndslSTYINANYIR---GYGGKEKAFIATQGPMINTVNDFWQMVWQEDSPVIVMITK 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720354236 519 QVERGRvKCHQYWPEpsESSSYGCYQVTCHSEEGNPAYIFRKMTLfnQEKNESRQLTQIQYTAWPDHGVPDDSSDFLDFV 598
Cdd:cd14611    78 LKEKNE-KCVLYWPE--KRGIYGKVEVLVNSVKECDNYTIRNLTL--KQGSQSRSVKHYWYTSWPDHKTPDSAQPLLQLM 152

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1720354236 599 CHVRDQRAGKEE--PIIVHCSAGIGRTGVLITMETAMCLIECNQPVYPLDIVRTMRDQRAMMIQTPSQYRFV 668
Cdd:cd14611   153 LDVEEDRLASPGrgPVVVHCSAGIGRTGCFIATTIGCQQLKEEGVVDVLSIVCQLRVDRGGMVQTSEQYEFV 224
R-PTP-C-2 cd14558
PTP-like domain of receptor-type tyrosine-protein phosphatase C, repeat 2; Receptor-type ...
 468-667 1.97e-40

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: 146.77  E-value: 1.97e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720354236 468 YINANYINMEIPSSSIInqyiACQGPLPHTCKDFWQMTWEQGSSMVVMLTTQVERGRVKCHQYWPEpsESSSYGCYQVTC 547
Cdd:cd14558     1 YINASFIDGYWGPKSLI----ATQGPLPDTIADFWQMIFQKKVKVIVMLTELKEGDQEQCAQYWGD--EKKTYGDIEVEL 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720354236 548 HSEEGNPAYIFRKMTLFNQEKNESRQLTQIQYTAWPDHGVPDDSSDFLDFV------CHVRDQRAGKEEPIIVHCSAGIG 621
Cdd:cd14558    75 KDTEKSPTYTVRVFEITHLKRKDSRTVYQYQYHKWKGEELPEKPKDLVDMIksikqkLPYKNSKHGRSVPIVVHCSDGSS 154

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|
gi 1720354236 622 RTGV----LITMETAmcliECNQPVYPLDIVRTMRDQRAMMIQTPSQYRF 667
Cdd:cd14558   155 RTGIfcalWNLLESA----ETEKVVDVFQVVKALRKQRPGMVSTLEQYQF 200
R-PTPc-E-2 cd14622
catalytic domain of receptor-type tyrosine-protein phosphatase E, repeat 2; Receptor-type ...
 467-667 2.03e-40

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: 147.07  E-value: 2.03e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720354236 467 DYINANYINmeipSSSIINQYIACQGPLPHTCKDFWQMTWEQGSSMVVMLTTQVERGRVKCHQYWpePSESS-SYGCYQV 545
Cdd:cd14622     1 DYINASFID----GYRQKDYFIATQGPLAHTVEDFWRMVWEWKCHTIVMLTELQEREQEKCVQYW--PSEGSvTHGEITI 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720354236 546 TCHSEEGNPAYIFRKMTL-FNQEKnESRQLTQIQYTAWPDHGVPDDSSDFLDFVCHV-RDQRAGKEEPIIVHCSAGIGRT 623
Cdd:cd14622    75 EIKNDTLLETISIRDFLVtYNQEK-QTRLVRQFHFHGWPEIGIPAEGKGMIDLIAAVqKQQQQTGNHPIVVHCSAGAGRT 153

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....
gi 1720354236 624 GVLITMETAMCLIECNQPVYPLDIVRTMRDQRAMMIQTPSQYRF 667
Cdd:cd14622   154 GTFIALSNILERVKAEGLLDVFQTVKSLRLQRPHMVQTLEQYEF 197
PHA02742 PHA02742
protein tyrosine phosphatase; Provisional
 442-676 1.24e-39

protein tyrosine phosphatase; Provisional


Pssm-ID: 165109 [Multi-domain]  Cd Length: 303  Bit Score: 147.84  E-value: 1.24e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720354236 442 QNISKNRYRDISPYDATRVLL---KGNEDYINANYINmeipSSSIINQYIACQGPLPHTCKDFWQMTWEQGSSMVVMLTT 518
Cdd:PHA02742   51 KNMKKCRYPDAPCFDRNRVILkieDGGDDFINASYVD----GHNAKGRFICTQAPLEETALDFWQAIFQDQVRVIVMITK 126

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720354236 519 QVERGRVKCHQYW-PEPSESSSYGCYQVTCHSEEGNPAYIFRKMTLFNQEKNESRQLTQIQYTAWPDHGVPDDSSDFLDF 597
Cdd:PHA02742  127 IMEDGKEACYPYWmPHERGKATHGEFKIKTKKIKSFRNYAVTNLCLTDTNTGASLDIKHFAYEDWPHGGLPRDPNKFLDF 206

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720354236 598 VCHVRD-----------QRAGKEEPIIVHCSAGIGRTGVLITMETAMCLIECNQPVYPLDIVRTMRDQRAMMIQTPSQYR 666
Cdd:PHA02742  207 VLAVREadlkadvdikgENIVKEPPILVHCSAGLDRAGAFCAIDICISKYNERAIIPLLSIVRDLRKQRHNCLSLPQQYI 286

                         250
                  ....*....|
gi 1720354236 667 FvCEAILKVY 676
Cdd:PHA02742  287 F-CYFIVLIF 295
PHA02747 PHA02747
protein tyrosine phosphatase; Provisional
 441-668 5.92e-39

protein tyrosine phosphatase; Provisional


Pssm-ID: 165114 [Multi-domain]  Cd Length: 312  Bit Score: 146.30  E-value: 5.92e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720354236 441 PQNISKNRYRDISPYDATRVLLK----GNEDYINANYIN-MEIPSssiinQYIACQGPLPHTCKDFWQMTWEQGSSMVVM 515
Cdd:PHA02747   49 PENQPKNRYWDIPCWDHNRVILDsgggSTSDYIHANWIDgFEDDK-----KFIATQGPFAETCADFWKAVWQEHCSIIVM 123

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720354236 516 LT-TQVERGRVKCHQYWpEPSESSSYGC--YQVTCHSEEGNPAYIFRKMTLFNQEKNESRQLTQIQYTAWPDHGVPDDSS 592
Cdd:PHA02747  124 LTpTKGTNGEEKCYQYW-CLNEDGNIDMedFRIETLKTSVRAKYILTLIEITDKILKDSRKISHFQCSEWFEDETPSDHP 202

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720354236 593 DFLDFV--CHVRDQRAGKE--------EPIIVHCSAGIGRTGVLITMETAMCLIECNQPVYPLDIVRTMRDQRAMMIQTP 662
Cdd:PHA02747  203 DFIKFIkiIDINRKKSGKLfnpkdallCPIVVHCSDGVGKTGIFCAVDICLNQLVKRKAICLAKTAEKIREQRHAGIMNF 282


                  ....*.
gi 1720354236 663 SQYRFV 668
Cdd:PHA02747  283 DDYLFI 288
PHA02746 PHA02746
protein tyrosine phosphatase; Provisional
 441-674 9.93e-39

protein tyrosine phosphatase; Provisional


Pssm-ID: 165113 [Multi-domain]  Cd Length: 323  Bit Score: 145.94  E-value: 9.93e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720354236 441 PQNISKNRYRDISPYDATRVLLKG------------------------NEDYINANYINmeipSSSIINQYIACQGPLPH 496
Cdd:PHA02746   49 KENLKKNRFHDIPCWDHSRVVINAheslkmfdvgdsdgkkievtsednAENYIHANFVD----GFKEANKFICAQGPKED 124

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720354236 497 TCKDFWQMTWEQGSSMVVMLTtQVERGRVKCHQYWPEPSES-SSYGCYQVTCHSEEGNPAYIFRKMTLFNQEKNESRQLT 575
Cdd:PHA02746  125 TSEDFFKLISEHESQVIVSLT-DIDDDDEKCFELWTKEEDSeLAFGRFVAKILDIIEELSFTKTRLMITDKISDTSREIH 203

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720354236 576 QIQYTAWPDHGVPDDSSDFLDFVCHVRDQRA----------GKEEPIIVHCSAGIGRTGVLITMETAMCLIECNQPVYPL 645
Cdd:PHA02746  204 HFWFPDWPDNGIPTGMAEFLELINKVNEEQAelikqadndpQTLGPIVVHCSAGIGRAGTFCAIDNALEQLEKEKEVCLG 283

                         250       260
                  ....*....|....*....|....*....
gi 1720354236 646 DIVRTMRDQRAMMIQTPSQYRFvCEAILK 674
Cdd:PHA02746  284 EIVLKIRKQRHSSVFLPEQYAF-CYKALK 311
PTPc_plant_PTP1 cd17658
protein tyrosine phosphatase 1 from Arabidopsis thaliana and similar plant PTPs; Arabidopsis ...
 468-667 1.66e-38

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: 141.83  E-value: 1.66e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720354236 468 YINANYInmEIPSSSIINQYIACQGPLPHTCKDFWQMTWEQGSSMVVMLTTQVERGR-VKCHQYWP-EPSESSSYGCYQV 545
Cdd:cd17658     1 YINASLV--ETPASESLPKFIATQGPLPHTFEDFWEMVIQQRCPVIIMLTRLVDNYStAKCADYFPaEENESREFGRISV 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720354236 546 TCHSEEGNPAYIFRKMTLFNQEKNESRQLT--QIQYTAWPDHGVPDDSSdfldFVCHVRDQRAG---KEEPIIVHCSAGI 620
Cdd:cd17658    79 TNKKLKHSQHSITLRVLEVQYIESEEPPLSvlHIQYPEWPDHGVPKDTR----SVRELLKRLYGippSAGPIVVHCSAGI 154

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|
gi 1720354236 621 GRTGVLITMETAMCLIECNQpVYPLDI---VRTMRDQRAMMIQTPSQYRF 667
Cdd:cd17658   155 GRTGAYCTIHNTIRRILEGD-MSAVDLsktVRKFRSQRIGMVQTQDQYIF 203
R-PTPc-typeIIb-2 cd14556
PTP domain of type IIb (or R2B) subfamily receptor-type tyrosine-protein phosphatases, repeat ...
 468-670 1.79e-38

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: 141.39  E-value: 1.79e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720354236 468 YINANYINmeipSSSIINQYIACQGPLPHTCKDFWQMTWEQGSSMVVMLTtQVERGRVKCHQYWPEPsESSSYGCYQVTC 547
Cdd:cd14556     1 YINAALLD----SYKQPAAFIVTQHPLPNTVTDFWRLVYDYGCTSIVMLN-QLDPKDQSCPQYWPDE-GSGTYGPIQVEF 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720354236 548 HSEEGNPAYIFRKMTLFNQEKNE--SRQLTQIQYTAWPDHG-VPDDSSDFLDFVCHV-RDQRAGKEEPIIVHCSAGIGRT 623
Cdd:cd14556    75 VSTTIDEDVISRIFRLQNTTRPQegYRMVQQFQFLGWPRDRdTPPSKRALLKLLSEVeKWQEQSGEGPIVVHCLNGVGRS 154

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*..
gi 1720354236 624 GVLITMETAMCLIECNQPVYPLDIVRTMRDQRAMMIQTPSQYRFVCE 670
Cdd:cd14556   155 GVFCAISSVCERIKVENVVDVFQAVKTLRNHRPNMVETEEQYKFCYD 201
COG5599 COG5599
Protein tyrosine phosphatase [Signal transduction mechanisms];
439-665 1.53e-37

Protein tyrosine phosphatase [Signal transduction mechanisms];


Pssm-ID: 444335 [Multi-domain]  Cd Length: 282  Bit Score: 141.38  E-value: 1.53e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720354236 439 KLPQNISKNRYRDISPYDATRVllKGNEDYINANYINMEIPsssiiNQYIACQGPLPHTCKDFWQMTWEQGSSMVVMLTT 518
Cdd:COG5599    38 QNINGSPLNRFRDIQPYKETAL--RANLGYLNANYIQVIGN-----HRYIATQYPLEEQLEDFFQMLFDNNTPVLVVLAS 110

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720354236 519 QVE--RGRVKCHQYWPEPSESSSYgcyqvTCHSEEGNPAYIFRKMTLFN------QEKNESRQLTQIQYTAWPDHGVPDD 590
Cdd:COG5599   111 DDEisKPKVKMPVYFRQDGEYGKY-----EVSSELTESIQLRDGIEARTyvltikGTGQKKIEIPVLHVKNWPDHGAISA 185

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720354236 591 S--SDFLDFVCHVRDQRAGKEEPIIVHCSAGIGRTGVLITMETAMCLIECNQPVYP--LDIVRTMRDQRAM-MIQTPSQY 665
Cdd:COG5599   186 EalKNLADLIDKKEKIKDPDKLLPVVHCRAGVGRTGTLIACLALSKSINALVQITLsvEEIVIDMRTSRNGgMVQTSEQL 265
PTPc_motif smart00404
Protein tyrosine phosphatase, catalytic domain motif;
573-674 3.25e-33

Protein tyrosine phosphatase, catalytic domain motif;


Pssm-ID: 214649 [Multi-domain]  Cd Length: 105  Bit Score: 123.24  E-value: 3.25e-33
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720354236  573 QLTQIQYTAWPDHGVPDDSSDFLDFVCHVRDQRAGKEE--PIIVHCSAGIGRTGVLITMETAMCLIECNQP-VYPLDIVR 649
Cdd:smart00404   1 TVKHYHYTGWPDHGVPESPDSILELLRAVKKNLNQSESsgPVVVHCSAGVGRTGTFVAIDILLQQLEAEAGeVDIFDTVK 80

                           90       100
                   ....*....|....*....|....*
gi 1720354236  650 TMRDQRAMMIQTPSQYRFVCEAILK 674
Cdd:smart00404  81 ELRSQRPGMVQTEEQYLFLYRALLE 105
PTPc_DSPc smart00012
Protein tyrosine phosphatase, catalytic domain, undefined specificity; Protein tyrosine ...
 573-674 3.25e-33

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: 123.24  E-value: 3.25e-33
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720354236  573 QLTQIQYTAWPDHGVPDDSSDFLDFVCHVRDQRAGKEE--PIIVHCSAGIGRTGVLITMETAMCLIECNQP-VYPLDIVR 649
Cdd:smart00012   1 TVKHYHYTGWPDHGVPESPDSILELLRAVKKNLNQSESsgPVVVHCSAGVGRTGTFVAIDILLQQLEAEAGeVDIFDTVK 80

                           90       100
                   ....*....|....*....|....*
gi 1720354236  650 TMRDQRAMMIQTPSQYRFVCEAILK 674
Cdd:smart00012  81 ELRSQRPGMVQTEEQYLFLYRALLE 105
FERM_C_4_1_family cd13184
FERM domain C-lobe of Protein 4.1 family; The protein 4.1 family includes four well-defined ...
 2-74 9.70e-29

FERM domain C-lobe of Protein 4.1 family; The protein 4.1 family includes four well-defined members: erythroid protein 4.1 (4.1R), the best known and characterized member, 4.1G (general), 4.1N (neuronal), and 4.1 B (brain). The less well understood 4.1O/FRMD3 is not a true member of this family and is not included in this hierarchy. Besides three highly conserved domains, FERM, SAB (spectrin and actin binding domain) and CTD (C-terminal domain), the proteins from this family contain several unique domains: U1, U2 and U3. FERM domains like other members of the FERM domain superfamily have a cloverleaf architecture with three distinct lobes: (1) FERM_N (A-lobe or F1); (2) FERM_M (B-lobe, or F2); and (3) FERM_C (C-lobe or F3). The C-lobe/F3 within the FERM domain is part of the PH domain family. The brain is a particularly rich source of protein 4.1 isoforms. The various 4.1R, 4.1G, 4.1N, and 4.1B mRNAs are all expressed in distinct patterns within the brain. It is likely that 4.1 proteins play important functional roles in the brain including motor coordination and spatial learning, postmitotic differentiation, and synaptic architecture and function. In addition they are found in nonerythroid, nonneuronal cells where they may play a general structural role in nuclear architecture and/or may interact with splicing factors. The FERM C domain is the third structural domain within the FERM domain. The FERM domain is found in the cytoskeletal-associated proteins such as ezrin, moesin, radixin, 4.1R, and merlin. These proteins provide a link between the membrane and cytoskeleton and are involved in signal transduction pathways. The FERM domain is also found in protein tyrosine phosphatases (PTPs) , the tyrosine kinases FAK and JAK, in addition to other proteins involved in signaling. This domain is structurally similar to the PH and PTB domains and consequently is capable of binding to both peptides and phospholipids at different sites.


Pssm-ID: 270005  Cd Length: 94  Bit Score: 110.11  E-value: 9.70e-29
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1720354236   2 SGGILIYKNRVRMNTFLWLKIVKISFKCKQFFIQLRKELHESRETLLGFNMVNYRACKTLWKACVEHHTFFRL 74
Cdd:cd13184    22 SSGLLVYRDRLRINRFAWPKVLKISYKRNNFYIKIRPGEFEQYETTIGFKLPNHRAAKRLWKVCVEHHTFFRL 94
FERM_C pfam09380
FERM C-terminal PH-like domain;
1-76 1.00e-28

FERM C-terminal PH-like domain;


Pssm-ID: 462779 [Multi-domain]  Cd Length: 85  Bit Score: 109.65  E-value: 1.00e-28
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1720354236   1 MSGGILIYKNRVRM-NTFLWLKIVKISFKCKQFFIQLRkelHESRETLLGFNMVNYRACKTLWKACVEHHTFFRLDR 76
Cdd:pfam09380  12 SAKGILVYEDNNKIlNLFPWREIRKISFKRKKFLIKLR---DKSSEETLGFYTESSRACKYLWKLCVEQHTFFRLRR 85
R-PTPc-T-2 cd14634
PTP domain of receptor-type tyrosine-protein phosphatase T, repeat 2; Receptor-type ...
 468-674 2.85e-23

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: 98.17  E-value: 2.85e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720354236 468 YINANYINM-EIPSSSIINQYiacqgPLPHTCKDFWQMTWEQGSSMVVML----TTQVergrvkCHQYWPEPSeSSSYGC 542
Cdd:cd14634     1 YINAALMDShKQPAAFIVTQH-----PLPNTVADFWRLVFDYNCSSVVMLnemdAAQL------CMQYWPEKT-SCCYGP 68

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720354236 543 YQVTCHS---EEGNPAYIFRKMTLfNQEKNESRQLTQIQYTAWPDH-GVPDDSSDFLDFVCHV---RDQRAGKEEPIIVH 615
Cdd:cd14634    69 IQVEFVSadiDEDIISRIFRICNM-ARPQDGYRIVQHLQYIGWPAYrDTPPSKRSILKVVRRLekwQEQYDGREGRTVVH 147

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1720354236 616 CSAGIGRTGVLITMETAMCLIECNQPVYPLDIVRTMRDQRAMMIQTPSQYRFVCEAILK 674
Cdd:cd14634   148 CLNGGGRSGTFCAICSVCEMIQQQNIIDVFHTVKTLRNNKSNMVETLEQYKFVYEVALE 206
FERM_C_FARP1-like cd13193
FERM domain C-lobe of FERM, RhoGEF and pleckstrin domain-containing protein 1 and related ...
 4-95 1.01e-22

FERM domain C-lobe of FERM, RhoGEF and pleckstrin domain-containing protein 1 and related proteins; Members here include FARP1 (also called Chondrocyte-derived ezrin-like protein; PH domain-containing family C member 2), FARP2 (also called FIR/FERM domain including RhoGEF; FGD1-related Cdc42-GEF/FRG), and FRMD7(FERM domain containing 7). FARP1 and FARP2 are members of the Dbl family guanine nucleotide exchange factors (GEFs) which are upstream positive regulators of Rho GTPases. FARP1 has increased expression in differentiated chondrocytes. FARP2 is thought to regulate neurite remodeling by mediating the signaling pathways from membrane proteins to Rac. It is found in brain, lung, and testis, as well as embryonic hippocampal and cortical neurons. These members are composed of a N-terminal FERM domain, a proline-rich (PR) domain, Dbl-homology (DH), and two C-terminal PH domains. Other members in this family do not contain the DH domains such as the Human FERM domain containing protein 7 and Caenorhabditis elegans CFRM3, both of which have unknown functions. They contain an N-terminal FERM domain, a PH domain, followed by a FA (FERM adjacent) domain. The FERM domain has a cloverleaf tripart structure composed of: (1) FERM_N (A-lobe or F1); (2) FERM_M (B-lobe, or F2); and (3) FERM_C (C-lobe or F3). The C-lobe/F3 within the FERM domain is part of the PH domain family. The FERM domain is found in the cytoskeletal-associated proteins such as ezrin, moesin, radixin, 4.1R, and merlin. These proteins provide a link between the membrane and cytoskeleton and are involved in signal transduction pathways. The FERM domain is also found in protein tyrosine phosphatases (PTPs), the tyrosine kinases FAK and JAK, in addition to other proteins involved in signaling. This domain is structurally similar to the PH and PTB domains and consequently is capable of binding to both peptides and phospholipids at different sites.


Pssm-ID: 270014  Cd Length: 122  Bit Score: 93.95  E-value: 1.01e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720354236   4 GILIYKNRVRMNTFLWLKIVKISFKCKQFFIQLRKELHESRETLLGFNMVNYRACKTLWKACVEHHTFFRLD--RPLPPQ 81
Cdd:cd13193    32 GILVFQGFTKINTFSWAKIRKLSFKRKRFLIKLHPEAYGSYKDTVEFSFESRNECKSFWKKCIEHHAFFRCSevPKPPSP 111

                          90
                  ....*....|....
gi 1720354236  82 KNFFahyFTLGSKF 95
Cdd:cd13193   112 KLRL---FSRGSSF 122
R-PTPc-K-2 cd14636
PTP domain of receptor-type tyrosine-protein phosphatase K, repeat 2; Receptor-type ...
 468-667 1.37e-22

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: 96.25  E-value: 1.37e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720354236 468 YINANYIN-MEIPSSSIINQYiacqgPLPHTCKDFWQMTWEQGSSMVVMLT-TQVERGrvkCHQYWPEPSeSSSYGCYQV 545
Cdd:cd14636     1 YINAALMDsYRQPAAFIVTQH-----PLPNTVKDFWRLVYDYGCTSIVMLNeVDLAQG---CPQYWPEEG-MLRYGPIQV 71

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720354236 546 TCHSEEGNPAYIFRKMTLFNQEKNESRQLT--QIQYTAWPDH-GVPDDSSDFLDFVCHVRDQRAGKEE---PIIVHCSAG 619
Cdd:cd14636    72 ECMSCSMDCDVISRIFRICNLTRPQEGYLMvqQFQYLGWASHrEVPGSKRSFLKLILQVEKWQEECDEgegRTIIHCLNG 151

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*...
gi 1720354236 620 IGRTGVLITMETAMCLIECNQPVYPLDIVRTMRDQRAMMIQTPSQYRF 667
Cdd:cd14636   152 GGRSGMFCAISIVCEMIKRQNVVDVFHAVKTLRNSKPNMVETPEQYRF 199
R-PTPc-U-2 cd14637
PTP domain of receptor-type tyrosine-protein phosphatase U, repeat 2; Receptor-type ...
 468-674 4.83e-21

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: 91.89  E-value: 4.83e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720354236 468 YINANYINMEIPSSSiinqYIACQGPLPHTCKDFWQMTWEQGSSMVVMLTtQVERGRVK--CHQYWPEPSeSSSYGCYQV 545
Cdd:cd14637     1 YINAALTDSYTRSAA----FIVTLHPLQNTTTDFWRLVYDYGCTSVVMLN-QLNQSNSAwpCLQYWPEPG-LQQYGPMEV 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720354236 546 TCHSEEGNPAYIFRKMTLFNQEKNESRQLT--QIQYTAW-PDHGVPDDSSDFLDFVCHV-RDQRAGKEEPIIVHCSAGIG 621
Cdd:cd14637    75 EFVSGSADEDIVTRLFRVQNITRLQEGHLMvrHFQFLRWsAYRDTPDSKKAFLHLLASVeKWQRESGEGRTVVHCLNGGG 154

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1720354236 622 RTGVLITMETAMCLIECNQPVYPLDIVRTMRDQRAMMIQTPSQYRFVCEAILK 674
Cdd:cd14637   155 RSGTYCASAMILEMIRCHNIVDVFYAVKTLRNYKPNMVETLEQYRFCYEIALE 207
R5-PTP-2 cd14550
PTP-like domain of R5 subfamily receptor-type tyrosine-protein phosphatases, repeat 2; The R5 ...
 468-619 5.58e-21

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: 91.23  E-value: 5.58e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720354236 468 YINANYINmeipSSSIINQYIACQGPLPHTCKDFWQMTWEQGSSMVVMLTTQVERGrvKCHQYWPEPSESSSYGCYQVTC 547
Cdd:cd14550     1 YINASYLQ----GYRRSNEFIITQHPLEHTIKDFWQMIWDHNSQTIVMLTDNELNE--DEPIYWPTKEKPLECETFKVTL 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720354236 548 HSEE-----GNPAYIFRKMTLfnQEKNESRQLT--QIQYTAWPDHGVPddSSDFLDFVCHVRDQRAGKEEPIIVH----- 615
Cdd:cd14550    75 SGEDhsclsNEIRLIVRDFIL--ESTQDDYVLEvrQFQCPSWPNPCSP--IHTVFELINTVQEWAQQRDGPIVVHdrygg 150


                  ....
gi 1720354236 616 CSAG 619
Cdd:cd14550   151 VQAA 154
FERM_C_NBL4_NBL5 cd13186
FERM domain C-lobe of Novel band 4.1-like protein 4 and 5 (NBL4 and 5); NBL4 (also called ...
 4-73 7.19e-21

FERM domain C-lobe of Novel band 4.1-like protein 4 and 5 (NBL4 and 5); NBL4 (also called Erythrocyte protein band 4.1-like 4; Epb4 1l4) plays a role the beta-catenin/Tcf signaling pathway and is thought to be involved in establishing the cell polarity or proliferation. NBL4 may be also involved in adhesion, in cell motility and/or in cell-to-cell communication. No role for NBL5 has been proposed to date. Both NBL4 and NBL5 contain a N-terminal FERM domain which has a cloverleaf tripart structure composed of: (1) FERM_N (A-lobe or F1); (2) FERM_M (B-lobe, or F2); and (3) FERM_C (C-lobe or F3). The C-lobe is a member of the PH superfamily. The FERM domain is found in the cytoskeletal-associated proteins such as ezrin, moesin, radixin, 4.1R, and merlin. These proteins provide a link between the membrane and cytoskeleton and are involved in signal transduction pathways. The FERM domain is also found in protein tyrosine phosphatases (PTPs) , the tyrosine kinases FAK and JAK, in addition to other proteins involved in signaling. This domain is structurally similar to the PH and PTB domains and consequently is capable of binding to both peptides and phospholipids at different sites.


Pssm-ID: 270007  Cd Length: 92  Bit Score: 87.34  E-value: 7.19e-21
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720354236   4 GILIYKNRVRMNTFLWLKIVKISFKCKQFFIQLRKELHESRETLLGFNMVNYRACKTLWKACVEHHTFFR 73
Cdd:cd13186    23 GILVFENKTKIGLFFWPRITKLDFKGKKLKLVVKEKDDQEQEHTFVFRLPNKKACKHLWKCAVEHHAFFR 92
PDZ_canonical cd00136
canonical PDZ domain; Canonical PDZ (PSD-95 (Postsynaptic density protein 95), Dlg (Discs ...
 281-366 3.58e-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: 3.58e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720354236 281 LIKMKPDENGRFGFNVKGGYDQKMPVIVSRVAPGTPADLCvPRLNEGDQVVLINGRDIAEHTHDQVVLFIKASCekhsGE 360
Cdd:cd00136     1 TVTLEKDPGGGLGFSIRGGKDGGGGIFVSRVEPGGPAARD-GRLRVGDRILEVNGVSLEGLTHEEAVELLKSAG----GE 75


                  ....*.
gi 1720354236 361 LVLLVR 366
Cdd:cd00136    76 VTLTVR 81
PDZ pfam00595
PDZ domain; PDZ domains are found in diverse signaling proteins.
 281-366 1.46e-18

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


Pssm-ID: 395476 [Multi-domain]  Cd Length: 81  Bit Score: 80.40  E-value: 1.46e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720354236 281 LIKMKPDENGRFGFNVKGGYDQK-MPVIVSRVAPGTPADlcVPRLNEGDQVVLINGRDIAEHTHDQVVLFIKAScekhSG 359
Cdd:pfam00595   1 QVTLEKDGRGGLGFSLKGGSDQGdPGIFVSEVLPGGAAE--AGGLKVGDRILSINGQDVENMTHEEAVLALKGS----GG 74


                  ....*..
gi 1720354236 360 ELVLLVR 366
Cdd:pfam00595  75 KVTLTIL 81
R-PTP-Z-2 cd17669
catalytic domain of receptor-type tyrosine-protein phosphatase Z, repeat 2; Receptor-type ...
 468-673 2.32e-18

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: 83.89  E-value: 2.32e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720354236 468 YINANYINMEIPSssiiNQYIACQGPLPHTCKDFWQMTWEQGSSMVVMLTTQVERGRVKChQYWPEPSESSSYGCYQVT- 546
Cdd:cd17669     1 YINASYIMGYYQS----NEFIITQHPLLHTIKDFWRMIWDHNAQLIVMLPDGQNMAEDEF-VYWPNKDEPINCETFKVTl 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720354236 547 ------CHSEEGNpaYIFRKMTLFNQEKNESRQLTQIQYTAWPDhgvPDDS-SDFLDFVCHVRDQRAGKEEPIIVHCSAG 619
Cdd:cd17669    76 iaeehkCLSNEEK--LIIQDFILEATQDDYVLEVRHFQCPKWPN---PDSPiSKTFELISIIKEEAANRDGPMIVHDEHG 150

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1720354236 620 IGRTGVLITMETAMCLIECNQPVYPLDIVRTMRDQRAMMIQTPSQYRFVCEAIL 673
Cdd:cd17669   151 GVTAGTFCALTTLMHQLEKENSVDVYQVAKMINLMRPGVFTDIEQYQFLYKAIL 204
R-PTPc-M-2 cd14635
PTP domain of receptor-type tyrosine-protein phosphatase M, repeat 2; Receptor-type ...
 468-674 3.74e-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: 83.58  E-value: 3.74e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720354236 468 YINANYIN-MEIPSSSIINQYiacqgPLPHTCKDFWQMTWEQGSSMVVMLTtQVERGRVkCHQYWPEpSESSSYGCYQVT 546
Cdd:cd14635     1 YINAALMDsYKQPSAFIVTQH-----PLPNTVKDFWRLVLDYHCTSIVMLN-DVDPAQL-CPQYWPE-NGVHRHGPIQVE 72

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720354236 547 CHSEEGNPAYIFRKMTLFNQEKNES--RQLTQIQYTAWPDH-GVPDDSSDFLDFVCHV---RDQRAGKEEPIIVHCSAGI 620
Cdd:cd14635    73 FVSADLEEDIISRIFRIYNAARPQDgyRMVQQFQFLGWPMYrDTPVSKRSFLKLIRQVdkwQEEYNGGEGRTVVHCLNGG 152

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1720354236 621 GRTGVLITMETAMCLIECNQPVYPLDIVRTMRDQRAMMIQTPSQYRFVCEAILK 674
Cdd:cd14635   153 GRSGTFCAISIVCEMLRHQRAVDVFHAVKTLRNNKPNMVDLLDQYKFCYEVALE 206
R-PTP-G-2 cd17670
PTP-like domain of receptor-type tyrosine-protein phosphatase G, repeat 2; Receptor-type ...
 468-673 8.22e-17

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: 79.72  E-value: 8.22e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720354236 468 YINANYINMEIPSssiiNQYIACQGPLPHTCKDFWQMTWEQGSSMVVMLTTQVERGRVKcHQYWPEPSESSSYGCYQVT- 546
Cdd:cd17670     1 YINASYIMGYYRS----NEFIITQHPLPHTTKDFWRMIWDHNAQIIVMLPDNQGLAEDE-FVYWPSREESMNCEAFTVTl 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720354236 547 ------CHSEEgnPAYIFRKMTLFNQEKNESRQLTQIQYTAWPDHGVPDDSSdfLDFVCHVRDQRAGKEEPIIVHCSAGI 620
Cdd:cd17670    76 iskdrlCLSNE--EQIIIHDFILEATQDDYVLEVRHFQCPKWPNPDAPISST--FELINVIKEEALTRDGPTIVHDEFGA 151

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1720354236 621 GRTGVLITMETAMCLIECNQPVYPLDIVRTMRDQRAMMIQTPSQYRFVCEAIL 673
Cdd:cd17670   152 VSAGTLCALTTLSQQLENENAVDVYQVAKMINLMRPGVFTDIEQYQFLYKAML 204
PTP_YopH-like cd14559
YopH and related bacterial protein tyrosine phosphatases; Yersinia outer protein H (YopH) ...
 447-665 1.05e-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: 73.97  E-value: 1.05e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720354236 447 NRYRDISpydaTRVLLKGNEDyINANYI---NMEIpsssiinqYIACQGPLPHTCKDFWQMTWEQGSSMVVMLTTQVERG 523
Cdd:cd14559     1 NRFTNIQ----TRVSTPVGKN-LNANRVqigNKNV--------AIACQYPKNEQLEDHLKMLADNRTPCLVVLASNKDIQ 67

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720354236 524 RVKCHQYWpepSESSSYGcyQVTCHSEEGNPAYIFRKmTLFNQ------EKNESRQLTQIQYTAWPDHG-VPDDSSDFL- 595
Cdd:cd14559    68 RKGLPPYF---RQSGTYG--SVTVKSKKTGKDELVDG-LKADMynlkitDGNKTITIPVVHVTNWPDHTaISSEGLKELa 141

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720354236 596 DFVCHVRDQRAGKEE--------------PIIvHCSAGIGRTGVLItmeTAMCLIECNQPVYPLDIVRTMRDQR-AMMIQ 660
Cdd:cd14559   142 DLVNKSAEEKRNFYKskgssaindknkllPVI-HCRAGVGRTGQLA---AAMELNKSPNNLSVEDIVSDMRTSRnGKMVQ 217


                  ....*
gi 1720354236 661 TPSQY 665
Cdd:cd14559   218 KDEQL 222
PDZ smart00228
Domain present in PSD-95, Dlg, and ZO-1/2; Also called DHR (Dlg homologous region) or GLGF ...
 288-368 2.08e-14

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: 68.94  E-value: 2.08e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720354236  288 ENGRFGFNVKGGYDQKMPVIVSRVAPGTPADLCvpRLNEGDQVVLINGRDIAEHTHDQVVLFIKASCEKhsgeLVLLVRP 367
Cdd:smart00228  10 GGGGLGFSLVGGKDEGGGVVVSSVVPGSPAAKA--GLRVGDVILEVNGTSVEGLTHLEAVDLLKKAGGK----VTLTVLR 83


                   .
gi 1720354236  368 N 368
Cdd:smart00228  84 G 84
PHA02740 PHA02740
protein tyrosine phosphatase; Provisional
 428-676 9.11e-14

protein tyrosine phosphatase; Provisional


Pssm-ID: 165107 [Multi-domain]  Cd Length: 298  Bit Score: 72.69  E-value: 9.11e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720354236 428 RKKPGMTMSCAklpQNISK----NRYRDISPYDATRVLLKGNEDYINANYINmeipSSSIINQYIACQGPLPHTCKDFWQ 503
Cdd:PHA02740   37 EHEDEANKACA---QAENKakdeNLALHITRLLHRRIKLFNDEKVLDARFVD----GYDFEQKFICIINLCEDACDKFLQ 109

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720354236 504 MTWEQGSSMVVMLTTQVERgrvKCH-QYWpepseSSSYGC------YQVTCHSEEGNPAYIFRKMTLFNQeKNESRQLTQ 576
Cdd:PHA02740  110 ALSDNKVQIIVLISRHADK---KCFnQFW-----SLKEGCvitsdkFQIETLEIIIKPHFNLTLLSLTDK-FGQAQKISH 180

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720354236 577 IQYTAWPDHGVPDDSSDFLDFVCHVRDQRA--------GKEEPIIVHCSAGIGRTGVLITMEtaMCLIECNQP--VYPLD 646
Cdd:PHA02740  181 FQYTAWPADGFSHDPDAFIDFFCNIDDLCAdlekhkadGKIAPIIIDCIDGISSSAVFCVFD--ICATEFDKTgmLSIAN 258

                         250       260       270
                  ....*....|....*....|....*....|
gi 1720354236 647 IVRTMRDQRAMMIQTPSQYRFvCEAILKVY 676
Cdd:PHA02740  259 ALKKVRQKKYGCMNCLDDYVF-CYHLIAAY 287
PDZ_syntrophin-like cd06801
PDZ domain of syntrophins, and related domains; PDZ (PSD-95 (Postsynaptic density protein 95), ...
 282-364 1.76e-13

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: 66.06  E-value: 1.76e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720354236 282 IKMKPDENGRFGFNVKGGYDQKMPVIVSRVAPGTPADLCvPRLNEGDQVVLINGRDIAEHTHDQVVLFIKAscekhSGEL 361
Cdd:cd06801     3 VRVVKQDVGGLGISIKGGAEHKMPILISKIFKGQAADQT-GQLFVGDAILSVNGENLEDATHDEAVQALKN-----AGDE 76


                  ...
gi 1720354236 362 VLL 364
Cdd:cd06801    77 VTL 79
FA pfam08736
FERM adjacent (FA); This region is found adjacent to Band 4.1 / FERM domains (pfam00373) in a ...
 88-129 1.91e-12

FERM adjacent (FA); This region is found adjacent to Band 4.1 / FERM domains (pfam00373) in a subset of FERM containing protein. The region has been hypothesized to play a role in regulatory adaptation, based on similarity to other protein kinase substrates.


Pssm-ID: 462582  Cd Length: 44  Bit Score: 61.80  E-value: 1.91e-12
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|..
gi 1720354236  88 YFTLGSKFRYCGRTEVQSVQYGKEKANKDRVFARSPSKPLAR 129
Cdd:pfam08736   2 FFSLGSKFRYSGRTQKQTVEDSSEILRPQPEFERSPSKRYPS 43
CDC14 COG2453
Protein-tyrosine phosphatase [Signal transduction mechanisms];
582-670 5.91e-12

Protein-tyrosine phosphatase [Signal transduction mechanisms];


Pssm-ID: 441989 [Multi-domain]  Cd Length: 140  Bit Score: 63.45  E-value: 5.91e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720354236 582 WPDHGVPDDSsDFLDFVCHVRDQRAgKEEPIIVHCSAGIGRTGVLItmetAMCLIECNQPvyPLDIVRTMRDQRAMMIQT 661
Cdd:COG2453    55 IPDFGAPDDE-QLQEAVDFIDEALR-EGKKVLVHCRGGIGRTGTVA----AAYLVLLGLS--AEEALARVRAARPGAVET 126


                  ....*....
gi 1720354236 662 PSQYRFVCE 670
Cdd:COG2453   127 PAQRAFLER 135
PDZ_ZASP52-like cd23068
PDZ domain of Drosophila melanogaster PDZ and LIM domain protein Zasp52 (also known as Zasp), ...
 285-366 2.21e-11

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: 60.23  E-value: 2.21e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720354236 285 KPDENGRFGFNVKGGYDQKMPVIVSRVAPGTPADLCvpRLNEGDQVVLINGRDIAEHTHDQVVLFIKASCekhsGELVLL 364
Cdd:cd23068     6 RDDSNTPWGFRLQGGADFGQPLSIQKVNPGSPADKA--GLRRGDVILRINGTDTSNLTHKQAQDLIKRAG----NDLQLT 79


                  ..
gi 1720354236 365 VR 366
Cdd:cd23068    80 VQ 81
PTP_DSP_cys cd14494
cys-based protein tyrosine phosphatase and dual-specificity phosphatase superfamily; This ...
 593-670 4.90e-11

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: 60.06  E-value: 4.90e-11
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1720354236 593 DFLDFVCHVRDQRAGKEEPIIVHCSAGIGRTGVLITMETAMCLIECnqpvyPLDIVRTMRDQR-AMMIQTPSQYRFVCE 670
Cdd:cd14494    40 AMVDRFLEVLDQAEKPGEPVLVHCKAGVGRTGTLVACYLVLLGGMS-----AEEAVRIVRLIRpGGIPQTIEQLDFLIK 113
PDZ_Lin-7-like cd06796
PDZ domain of protein Lin-7 and related domains; PDZ (PSD-95 (Postsynaptic density protein 95), ...
 292-366 5.97e-11

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: 58.99  E-value: 5.97e-11
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1720354236 292 FGFNVKGGYDQKMPVIVSRVAPGTPADLcVPRLNEGDQVVLINGRDIAEHTHDQVVLFIKAScekhSGELVLLVR 366
Cdd:cd06796    14 LGFNVMGGKEQNSPIYISRIIPGGVADR-HGGLKRGDQLLSVNGVSVEGEHHEKAVELLKAA----QGSVKLVVR 83
FERM_C-lobe cd00836
FERM domain C-lobe; The FERM domain has a cloverleaf tripart structure composed of: (1) FERM_N ...
 4-73 1.26e-10

FERM domain C-lobe; The FERM domain has a cloverleaf tripart structure composed of: (1) FERM_N (A-lobe or F1); (2) FERM_M (B-lobe, or F2); and (3) FERM_C (C-lobe or F3). The C-lobe/F3 within the FERM domain is part of the PH domain family. The FERM domain is found in the cytoskeletal-associated proteins such as ezrin, moesin, radixin, 4.1R, and merlin. These proteins provide a link between the membrane and cytoskeleton and are involved in signal transduction pathways. The FERM domain is also found in protein tyrosine phosphatases (PTPs), the tyrosine kinases FAK and JAK, in addition to other proteins involved in signaling. This domain is structurally similar to the PH and PTB domains and consequently is capable of binding to both peptides and phospholipids at different sites.


Pssm-ID: 275389  Cd Length: 93  Bit Score: 58.54  E-value: 1.26e-10
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1720354236   4 GILIYKNRV--RMNTFLWLKIVKISFKC-KQFFIQLRKElheSRETLLGFNMVNyRACKTLWKACVEHHTFFR 73
Cdd:cd00836    25 GISVYDELTgqPLVLFPWPNIKKISFSGaKKFTIVVADE---DKQSKLLFQTPS-RQAKEIWKLIVGYHRFLL 93
PDZ_NHERF-like cd06768
PDZ domains of the Na+/H+ exchange regulatory cofactor (NHERF) family (NHERF1-4), and related ...
 281-365 3.46e-10

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: 56.68  E-value: 3.46e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720354236 281 LIKMKPDENGrFGFNVKGGYDQKMPVIVSrVAPGTPADLCvpRLNEGDQVVLINGRDIAEHTHDQVVLFIKAScekhSGE 360
Cdd:cd06768     2 LCHLVKGPEG-YGFNLHAEKGRPGHFIRE-VDPGSPAERA--GLKDGDRLVEVNGENVEGESHEQVVEKIKAS----GNQ 73


                  ....*
gi 1720354236 361 LVLLV 365
Cdd:cd06768    74 VTLLV 78
PDZ_SYNJ2BP-like cd06709
PDZ domain of synaptojanin-2-binding protein (SYNJ2BP), and related domains; PDZ (PSD-95 ...
 282-364 5.54e-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: 56.15  E-value: 5.54e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720354236 282 IKMKPDENGrFGFNVKGGYDQK-MP----VIVSRVAPGTPADLcVPRLNEGDQVVLINGRDIAEHTHDQVV-LFIKAsce 355
Cdd:cd06709     3 ITLKRGPSG-LGFNIVGGTDQPyIPndsgIYVAKIKEDGAAAI-DGRLQEGDKILEINGQSLENLTHQDAVeLFRNA--- 77


                  ....*....
gi 1720354236 356 khsGELVLL 364
Cdd:cd06709    78 ---GEDVKL 83
FERM_C_FRMD3_FRMD5 cd13192
FERM domain C-lobe of FERM domain-containing protein 3 and 5 (FRMD3 and 5); FRMD3 (also called ...
 4-73 7.17e-10

FERM domain C-lobe of FERM domain-containing protein 3 and 5 (FRMD3 and 5); FRMD3 (also called Band 4.1-like protein 4O/4.1O though it is not a true member of that family) is a novel putative tumor suppressor gene that is implicated in the origin and progression of lung cancer. In humans there are 5 isoforms that are produced by alternative splicing. Less is known about FRMD5, though there are 2 isoforms of the human protein are produced by alternative splicing. Both FRMD3 and FRMD5 contain a N-terminal FERM domain, followed by a FERM adjacent (FA) domain, and 4.1 protein C-terminal domain (CTD). The FERM domain has a cloverleaf tripart structure composed of: (1) FERM_N (A-lobe or F1); (2) FERM_M (B-lobe, or F2); and (3) FERM_C (C-lobe or F3). The C-lobe/F3 within the FERM domain is part of the PH domain family. The FERM domain is found in the cytoskeletal-associated proteins such as ezrin, moesin, radixin, 4.1R, and merlin. These proteins provide a link between the membrane and cytoskeleton and are involved in signal transduction pathways. The FERM domain is also found in protein tyrosine phosphatases (PTPs), the tyrosine kinases FAK and JAK, in addition to other proteins involved in signaling. This domain is structurally similar to the PH and PTB domains and consequently is capable of binding to both peptides and phospholipids at different sites.


Pssm-ID: 270013  Cd Length: 105  Bit Score: 56.63  E-value: 7.17e-10
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720354236   4 GILIYKNRVRMNTFLWLKIVKISFKCKQFFIQLRKElhESRETLLGFNMVNYRACKTLWKACVEHHTFFR 73
Cdd:cd13192    38 GIVTFQGGKRVHHFRWNDITKFNYEGKMFILHVMQK--EEKKHTLGFKCPTPAACKHLWKCAVEQQAFYT 105
PDZ1_harmonin cd06737
PDZ domain 1 of harmonin isoforms a, b, and c, and related domains; PDZ (PSD-95 (Postsynaptic ...
 279-352 1.10e-09

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: 55.34  E-value: 1.10e-09
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                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1720354236 279 LVLIKMKPDENGRFGFNVKGGYDQKMPVIVSRVAPGTPADLcvPRLNEGDQVVLINGRDIAEHTHDQVVLFIKA 352
Cdd:cd06737     2 LRLVRLDRRGPESLGFSVRGGLEHGCGLFVSHVSPGSQADN--KGLRVGDEIVRINGYSISQCTHEEVINLIKT 73
PDZ_PDLIM-like cd06753
PDZ domain of PDZ-LIM family proteins, and related domains; PDZ (PSD-95 (Postsynaptic density ...
 292-366 2.39e-09

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: 54.46  E-value: 2.39e-09
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1720354236 292 FGFNVKGGYDQKMPVIVSRVAPGTPADLCvpRLNEGDQVVLINGRDIAEHTHDQVVLFIKAScekhSGELVLLVR 366
Cdd:cd06753    10 WGFRLQGGKDFNQPLTISRVTPGGKAAQA--NLRPGDVILAINGESTEGMTHLEAQNKIKAA----TGSLSLTLE 78
PDZ5_MAGI-1_3-like cd06735
PDZ domain 5 of membrane-associated guanylate kinase inverted 1 (MAGI-1), MAGI-2, and MAGI-3, ...
 292-367 3.02e-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: 54.12  E-value: 3.02e-09
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gi 1720354236 292 FGFNVKGGYD-QKMPVIVSRVAPGTPADLCvPRLNEGDQVVLINGRDIAEHTHDQVVLFIKASCEKhsgeLVLLVRP 367
Cdd:cd06735    13 FGFSIRGGREyNNMPLYVLRLAEDGPAQRD-GRLRVGDQILEINGESTQGMTHAQAIELIRSGGSV----VRLLLRR 84
CDKN3-like cd14505
cyclin-dependent kinase inhibitor 3 and similar proteins; This family is composed of ...
 574-668 5.84e-09

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: 55.73  E-value: 5.84e-09
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gi 1720354236 574 LTQIQYtAWPDHGVPDDSSDFLDFVCHVRDQ-RAGKEepIIVHCSAGIGRTGVLItmetAMCLIECNQPVYPLDIVRTMR 652
Cdd:cd14505    73 ITWHHL-PIPDGGVPSDIAQWQELLEELLSAlENGKK--VLIHCKGGLGRTGLIA----ACLLLELGDTLDPEQAIAAVR 145

                          90
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gi 1720354236 653 DQRAMMIQTPSQYRFV 668
Cdd:cd14505   146 ALRPGAIQTPKQENFL 161
PDZ_TAX1BP3-like cd10822
PDZ domain of tax1-binding protein 3 (TAX1BP3), and related domains; PDZ (PSD-95 (Postsynaptic ...
 281-351 6.68e-09

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: 53.50  E-value: 6.68e-09
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gi 1720354236 281 LIKMKPDENGRFGFNVKGGYDQ---KMP-------VIVSRVAPGTPADLCvpRLNEGDQVVLINGRDIAEHTHDQVVLFI 350
Cdd:cd10822     4 IHKLRQGENLILGFSIGGGIDQdpsKNPfsytdkgIYVTRVSEGGPAEKA--GLQVGDKILQVNGWDMTMVTHKQAVKRL 81


                  .
gi 1720354236 351 K 351
Cdd:cd10822    82 T 82
PTP_PTPDC1 cd14506
protein tyrosine phosphatase domain of PTP domain-containing protein 1; protein tyrosine ...
 581-670 1.13e-08

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: 55.82  E-value: 1.13e-08
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gi 1720354236 581 AWPDHGVPddSSDFLDFVCHVRDQRAGKEEPIIVHCSAGIGRTGVLItmetAMCLIECNQpVYPLDIVRTMRDQRAMMIQ 660
Cdd:cd14506    83 GWKDYGVP--SLTTILDIVKVMAFALQEGGKVAVHCHAGLGRTGVLI----ACYLVYALR-MSADQAIRLVRSKRPNSIQ 155

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gi 1720354236 661 TPSQYRFVCE 670
Cdd:cd14506   156 TRGQVLCVRE 165
PDZ3_Dlg1-2-4-like cd06795
PDZ domain 3 of human discs large homolog 1 (Dlg1), Dlg2, and Dlg4, Drosophila disc large (Dlg) ...
 293-372 2.21e-08

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: 51.97  E-value: 2.21e-08
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gi 1720354236 293 GFNVKGGYDQKmPVIVSRVAPGTPADLCvPRLNEGDQVVLINGRDIAEHTHDQVVLFIkasceKHSGELVLLVrpnAVYD 372
Cdd:cd06795    15 GFNIVGGEDGE-GIFISFILAGGPADLS-GELRRGDQILSVNGVDLRNATHEQAAAAL-----KNAGQTVTII---AQYK 84
PDZ3_MAGI-1_3-like cd06733
PDZ domain 3 of membrane-associated guanylate kinase inverted 1 (MAGI-1), MAGI-2, and MAGI-3, ...
 279-366 2.73e-08

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: 51.46  E-value: 2.73e-08
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gi 1720354236 279 LVLIKMKPDENGrFGFNVKGGYDQKMPVIVSRVAPGTPADLcVPRLNEGDQVVLINGRDIAEHTHDQVVLFIKASCekHS 358
Cdd:cd06733     1 ELTVFLRRQETG-FGFRILGGTEEGSQVSIGAIVPGGAADL-DGRLRTGDELLSVDGVNVVGASHHKVVDLMGNAA--RN 76


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gi 1720354236 359 GELVLLVR 366
Cdd:cd06733    77 GQVNLTVR 84
PDZ_rhophilin-like cd06712
PDZ domain of rhophilin-1, rhophilin-2, and related domains; PDZ (PSD-95 (Postsynaptic density ...
 282-353 3.36e-08

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: 51.05  E-value: 3.36e-08
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gi 1720354236 282 IKMKPDENGrFGFNVKGGydqkMPVIVSRVAPGTPADLCvpRLNEGDQVVLINGRDIAEHTHDQVVLFIKAS 353
Cdd:cd06712     4 VHLTKEEGG-FGFTLRGD----SPVQVASVDPGSCAAEA--GLKEGDYIVSVGGVDCKWSKHSEVVKLLKSA 68
PDZ4_MAGI-1_3-like cd06734
PDZ domain 4 of membrane-associated guanylate kinase inverted 1 (MAGI-1), MAGI-2, and MAGI-3, ...
 275-353 3.59e-08

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: 51.08  E-value: 3.59e-08
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gi 1720354236 275 PHDnlVLIKMKPDENgrFGFNVKGGYDQKMPVIVSRVAPGTPADLCvPRLNEGDQVVLINGRDIAEHTHDQVVLFIKAS 353
Cdd:cd06734     1 PYD--VTLTRRENEG--FGFVIISSVNKKSGSKIGRIIPGSPADRC-GQLKVGDRILAVNGISILNLSHGDIVNLIKDS 74
PDZ_SYNPO2-like cd10820
PDZ domain of synaptopodin 2 (SYNPO2), synaptopodin 2-like protein (SYNPO2L), and related ...
 292-365 3.97e-08

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: 50.77  E-value: 3.97e-08
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1720354236 292 FGFNVKGGYDQKMPVIVSRVAPGTPADLCVprLNEGDQVVLINGRDIAEHTHDQVVLFIKASCekhsGELVLLV 365
Cdd:cd10820    10 WGFRLQGGSEQKKPLQVAKIRKKSKAALAG--LCEGDELLSINGKPCADLSHSEAMDLIDSSG----DTLQLLI 77
PTP_VSP_TPTE cd14510
protein tyrosine phosphatase-like catalytic domain of voltage-sensitive phosphatase ...
 583-668 4.66e-08

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: 53.52  E-value: 4.66e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720354236 583 PDHGVPDdSSDFLDFVCHVRDQRAGKEEPII-VHCSAGIGRTGvlitmeTAMC--LIECNQ---PVYPLDIVRTMRDQRA 656
Cdd:cd14510    82 DDHNVPT-LDEMLSFTAEVREWMAADPKNVVaIHCKGGKGRTG------TMVCawLIYSGQfesAKEALEYFGERRTDKS 154

                          90
                  ....*....|....*..
gi 1720354236 657 MM-----IQTPSQYRFV 668
Cdd:cd14510   155 VSskfqgVETPSQSRYV 171
PDZ_PDZD11-like cd06752
PDZ domain of PDZ domain-containing protein 11, and related domains; PDZ (PSD-95 (Postsynaptic ...
 282-357 7.28e-08

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: 50.39  E-value: 7.28e-08
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1720354236 282 IKMKPDENGRFGFNVKGGYDQKMPVIVSRVAPGTPADlcvpR--LNEGDQVVLINGRDIAEHTHDQVVLFIKASCEKH 357
Cdd:cd06752     3 VVLKRPPGEQLGFNIRGGKASGLGIFISKVIPDSDAH----RlgLKEGDQILSVNGVDFEDIEHSEAVKVLKTAREIQ 76
PDZ2-PTPN13_FRMPD2-like cd06792
PDZ domain 2 of tyrosine kinase PTPN13, FERM and PDZ domain-containing protein 2 (FRMPD2), and ...
 279-365 1.72e-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: 49.13  E-value: 1.72e-07
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                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720354236 279 LVLIKMkpdeNGRFGFNVKGGYDQKMP---VIVSRVAPGTPADlCVPRLNEGDQVVLINGRDIAEHTHDQVVlfikaSCE 355
Cdd:cd06792     5 VELSKK----DGSLGISVTGGINTSVRhggIYVKSLVPGGAAE-QDGRIQKGDRLLEVNGVSLEGVTHKQAV-----ECL 74

                          90
                  ....*....|
gi 1720354236 356 KHSGELVLLV 365
Cdd:cd06792    75 KNAGQVVTLV 84
PDZ2_L-delphilin-like cd06744
PDZ domain 2 of delphilin (L-delphilin isoform), and related domains; PDZ (PSD-95 ...
 288-353 5.13e-07

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: 47.66  E-value: 5.13e-07
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1720354236 288 ENGRFGFNVKGgydqKMPVIVSRVAPGTPADLCvpRLNEGDQVVLINGRDIAEHTHDQVVLFIKAS 353
Cdd:cd06744     7 GNGSFGFTLRG----HAPVYIESVDPGSAAERA--GLKPGDRILFLNGLDVRNCSHDKVVSLLQGS 66
PDZ1_FL-whirlin cd06740
PDZ domain 1 of the full-length isoform of whirlin and related domains; PDZ (PSD-95 ...
 278-366 8.05e-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: 47.36  E-value: 8.05e-07
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                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720354236 278 NLVLIKMKPDENGrFGFNVKGGYDQKMPVIVSRVAPGTPAD---LCVprlneGDQVVLINGRDIAEHTHDQVVLFIKAsc 354
Cdd:cd06740     2 RQVTLKRSKSHEG-LGFSIRGGAEHGVGIYVSLVEPGSLAEkegLRV-----GDQILRVNDVSFEKVTHAEAVKILRV-- 73

                          90
                  ....*....|..
gi 1720354236 355 ekhSGELVLLVR 366
Cdd:cd06740    74 ---SKKLVLSVR 82
PDZ1_INAD-like cd23063
PDZ domain 1 of inactivation-no-after-potential D (INAD), and related domains; PDZ (PSD-95 ...
 287-351 1.16e-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: 47.12  E-value: 1.16e-06
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gi 1720354236 287 DENGRFGF-----NVKGGYDQKMPVI-VSRVAPGTPADLCvPRLNEGDQVVLINGRDIAEHTHDQVVLFIK 351
Cdd:cd23063     7 TEKKSFGIcivrgEVKVSPNTKTTGIfIKGIIPDSPAHKC-GRLKVGDRILSVNGNDVRNSTEQAAIDLIK 76
PDZ4_LNX1_2-like cd06680
PDZ domain 4 of human Ligand of Numb protein X 1 (LNX1) and LNX2, and related domains; PDZ ...
 289-352 1.17e-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: 46.96  E-value: 1.17e-06
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1720354236 289 NGRFGFNVKGGYDQ---KMPVIVSRVAPGTPADLcVPRLNEGDQVVLINGRDIAEHTHDQVVLFIKA 352
Cdd:cd06680    10 SGSLGFSIVGGYEEshgNQPFFVKSIVPGTPAYN-DGRLKCGDIILAVNGVSTVGMSHAALVPLLKE 75
PDZ_tamalin_CYTIP-like cd06713
PDZ domain of tamalin, cytohesin-1-interacting protein (CYTIP), and related domains; PDZ ...
 279-354 1.74e-06

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: 46.46  E-value: 1.74e-06
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                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720354236 279 LVLIKmkpDENGRFGFNV-------KGGYDQKMPVIVSRVAPGTPADLCvpRLNEGDQVVLINGRDIAEHTHDQVVLFIK 351
Cdd:cd06713     6 IILEK---QDNETFGFEIqtyglhhKNSNEVEMCTYVCRVHEDSPAYLA--GLTAGDVILSVNGVSVEGASHQEIVELIR 80


                  ...
gi 1720354236 352 ASC 354
Cdd:cd06713    81 SSG 83
PDZ_RGS12-like cd06710
PDZ domain of regulator of G-protein signaling 12 (RGS12), and related domains; PDZ (PSD-95 ...
 292-356 2.03e-06

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: 45.70  E-value: 2.03e-06
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                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1720354236 292 FGFNVKGgydqKMPVIVSRVAPGTPADlcVPRLNEGDQVVLINGRDIAEHTHDQVVLFIkASCEK 356
Cdd:cd06710    12 YGFTISG----QAPCVLSCVVRGSPAD--VAGLKAGDQILAVNGINVSKASHEDVVKLI-GKCTG 69
PDZ1_PTPN13-like cd23072
PDZ domain 1 of protein tyrosine phosphatase non-receptor type 13 (PTPN13), and related ...
 279-347 2.91e-06

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: 45.94  E-value: 2.91e-06
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1720354236 279 LVLIKMKPDENGRFGFNVKGGYD---QKMPVIVSRVAPGTPADLcVPRLNEGDQVVLINGRDIAEHTHDQVV 347
Cdd:cd23072     2 ITLVNLKKDAKYGLGFQIVGGEKsgrLDLGIFISSITPGGPADL-DGRLKPGDRLISVNDVSLEGLSHDAAV 72
PDZ2_Scribble-like cd06703
PDZ domain 2 of Drosophila Scribble, human Scribble homolog, and related domains; PDZ (PSD-95 ...
 282-347 3.69e-06

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: 45.71  E-value: 3.69e-06
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                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1720354236 282 IKMKPDENGrFGFNVKGG------YDQKMPVIVSRVAPGTPADLcVPRLNEGDQVVLINGRDIAEHTHDQVV 347
Cdd:cd06703     5 TTLIRDGKG-LGFSIAGGkgstpfRDGDEGIFISRITEGGAADR-DGKLQVGDRVLSINGVDVTEARHDQAV 74
PDZ2_PDZD7-like cd10834
PDZ domain 2 of the canonical isoform 1 of PDZ domain containing 7 (PDZD7), and related ...
 293-366 4.78e-06

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: 45.07  E-value: 4.78e-06
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gi 1720354236 293 GFNVKGGYDQKMPVIVSRVAPGTPADlcVPRLNEGDQVVLINGRDIAEHTHDQVVLFIKasCEKHsgeLVLLVR 366
Cdd:cd10834    16 GFNIRGGSEYGLGIYVSKVDPGGLAE--QNGIKVGDQILAVNGVSFEDITHSKAVEVLK--SQTH---LMLTIK 82
PDZ1_MAGI-1_3-like cd06731
PDZ domain 1 of membrane-associated guanylate kinase inverted 1 (MAGI-1), MAGI-2, and MAGI-3, ...
 292-349 5.84e-06

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: 44.89  E-value: 5.84e-06
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gi 1720354236 292 FGFNVKGGYDQKMPVIVSRVAPGTPADLcVPRLNEGDQVVLINGRDIAEHTHDQVV-LF 349
Cdd:cd06731    13 FGFTIIGGDEPDEFLQIKSVVPDGPAAL-DGKLRTGDVLVSVNDTCVLGYTHADVVkLF 70
DUSP23 cd14504
dual specificity phosphatase 23; Dual specificity phosphatase 23 (DUSP23), also known as ...
 583-668 1.02e-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: 45.73  E-value: 1.02e-05
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gi 1720354236 583 PDHGVPDDSS--DFLDFVchvRDQRAgKEEPIIVHCSAGIGRTGvliTMetAMCLIECNQPVYPLDIVRTMRDQRAMMIQ 660
Cdd:cd14504    58 EDYTPPTLEQidEFLDIV---EEANA-KNEAVLVHCLAGKGRTG---TM--LACYLVKTGKISAVDAINEIRRIRPGSIE 128


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gi 1720354236 661 TPSQYRFV 668
Cdd:cd14504   129 TSEQEKFV 136
PDZ1_PTPN13_FRMPD2-like cd06694
PDZ domain 1 of protein tyrosine phosphatase non-receptor type 13 (PTPN13),FERM and PDZ ...
 279-356 1.04e-05

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: 44.31  E-value: 1.04e-05
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gi 1720354236 279 LVLIKMKPDENGRFGFNVKGGYDQK---MPVIVSRVAPGTPADLcVPRLNEGDQVVLINGRDIAEHTHDQVVLFIKASCE 355
Cdd:cd06694     2 IVIVTLKKDPQKGLGFTIVGGENSGsldLGIFVKSIIPGGPADK-DGRIKPGDRIIAINGQSLEGKTHHAAVEIIQNAPD 80


                  .
gi 1720354236 356 K 356
Cdd:cd06694    81 K 81
PDZ_FRMPD1_3_4-like cd06769
PDZ domain of FERM and PDZ domain-containing protein 1 (FRMPD1), FRMPD3, FRMPD4, and related ...
 282-365 1.71e-05

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: 43.39  E-value: 1.71e-05
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gi 1720354236 282 IKMKPDENGRFGFNVKGgydqKMPVIVSRVAPGTPADlcvPRLNEGDQVVLINGRDIAEHTHDQVVLFIKaSCEKhsgEL 361
Cdd:cd06769     2 VEIQRDAVLGFGFVAGS----ERPVVVRSVTPGGPSE---GKLLPGDQILKINNEPVEDLPRERVIDLIR-ECKD---SI 70


                  ....
gi 1720354236 362 VLLV 365
Cdd:cd06769    71 VLTV 74
PTP-IVa cd14500
protein tyrosine phosphatase type IVA family; Protein tyrosine phosphatases type IVA (PTP-IVa), ...
 577-655 1.89e-05

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: 45.29  E-value: 1.89e-05
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gi 1720354236 577 IQYTAWP--DHGVPDDS--SDFLDfVCHVRDQRAGKEEPII-VHCSAGIGRTGVLItmetAMCLIECNQPvyPLDIVRTM 651
Cdd:cd14500    59 IKVHDWPfdDGSPPPDDvvDDWLD-LLKTRFKEEGKPGACIaVHCVAGLGRAPVLV----AIALIELGMK--PEDAVEFI 131


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gi 1720354236 652 RDQR 655
Cdd:cd14500   132 RKKR 135
PDZ2_GRIP1-2-like cd06681
PDZ domain 2 of glutamate receptor-interacting protein 1 (GRIP1) and GRIP2, and related ...
 288-365 3.24e-05

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: 42.99  E-value: 3.24e-05
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gi 1720354236 288 ENGRFGFNVKGGYDQKM----PVIVSRVAPGTPADlCVPRLNEGDQVVLINGRDIAEHTHDQVVLFIKAScekhSGELVL 363
Cdd:cd06681    10 EGNSFGFVIRGGAHEDRnksrPLTVTHVRPGGPAD-REGTIKPGDRLLSVDGISLHGATHAEAMSILKQC----GQEATL 84


                  ..
gi 1720354236 364 LV 365
Cdd:cd06681    85 LI 86
PDZ1_ZO1-like cd06727
PDZ domain 1 of Zonula Occludens-1 (ZO-1), homologs ZO-2 and ZO-3, and related domains; PDZ ...
 292-353 3.91e-05

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: 42.65  E-value: 3.91e-05
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gi 1720354236 292 FGFNVKGGYDQKMP------VIVSRVAPGTPADlcvPRLNEGDQVVLINGRDIAEHTHDQVVLFIKAS 353
Cdd:cd06727    13 FGIAVSGGRDNPHFqsgdtsIVISDVLKGGPAE---GKLQENDRVVSVNGVSMENVEHSFAVQILRKC 77
PDZ1-PDZRN4-like cd06715
PDZ domain 1 of PDZ domain-containing RING finger protein 4 (PDZRN4), PDZRN3-B, and related ...
 288-347 5.45e-05

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: 42.38  E-value: 5.45e-05
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gi 1720354236 288 ENGRFGFNVKGGY----DQKMP----VIVSRVAPGTPAD----LCVprlneGDQVVLINGRDIAEHTHDQVV 347
Cdd:cd06715    10 ENGSLGFNIIGGRpcenNQEGSssegIYVSKIVENGPAAdeggLQV-----HDRIIEVNGKDLSKATHEEAV 76
PTZ00242 PTZ00242
protein tyrosine phosphatase; Provisional
 576-655 5.78e-05

protein tyrosine phosphatase; Provisional


Pssm-ID: 185524 [Multi-domain]  Cd Length: 166  Bit Score: 44.24  E-value: 5.78e-05
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gi 1720354236 576 QIQYTAWP--DHGVPDDS--SDFLDFVCHVRDQRAGKEEPIIVHCSAGIGRTGVLItmetAMCLIE-CNQPvyPLDIVRT 650
Cdd:PTZ00242   61 GIEVHDWPfdDGAPPPKAviDNWLRLLDQEFAKQSTPPETIAVHCVAGLGRAPILV----ALALVEyGGME--PLDAVGF 134


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gi 1720354236 651 MRDQR 655
Cdd:PTZ00242  135 VREKR 139
PDZ2_FL-whirlin cd06741
PDZ domain 2 of the full-length isoform of whirlin and related domains; PDZ (PSD-95 ...
 278-366 6.09e-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: 41.87  E-value: 6.09e-05
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gi 1720354236 278 NLVLikmkpDENGRFGFNVKGGYDQKMPVIVSRVAPGTPADLCvpRLNEGDQVVLINGRDIAEHTHDQVVLFIKASceKH 357
Cdd:cd06741     5 NLVV-----EDGQSLGLMIRGGAEYGLGIYVTGVDPGSVAENA--GLKVGDQILEVNGRSFLDITHDEAVKILKSS--KH 75


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gi 1720354236 358 sgeLVLLVR 366
Cdd:cd06741    76 ---LIMTVK 81
PDZ1_PDZD7-like cd10833
PDZ domain 1 of the canonical isoform 1 of PDZ domain containing 7 (PDZD7), and related ...
 282-335 6.40e-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: 42.04  E-value: 6.40e-05
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gi 1720354236 282 IKMKPDENGRFGFNVKGGYDQKMPVIVSRVAPGTPAD---LCVprlneGDQVVLING 335
Cdd:cd10833     4 VTVEKSPDGSLGFSVRGGSEHGLGIFVSKVEEGSAAEragLCV-----GDKITEVNG 55
PDZ_ARHGEF11-12-like cd23069
PDZ domain of ARHGEF11, ARHGEF12, and related domains; PDZ (PSD-95 (Postsynaptic density ...
 287-364 6.57e-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: 41.61  E-value: 6.57e-05
                          10        20        30        40        50        60        70
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gi 1720354236 287 DENGrFGFNVKGgydqKMPVIVSRVAPGTPADlcVPRLNEGDQVVLINGRDIAEHTHDQVVLFIKAScekHSGELVLL 364
Cdd:cd23069     9 DENG-YGLTVSG----DNPVFVQSVKEGGAAY--RAGVQEGDRIIKVNGTLVTHSNHLEVVKLIKSG---SYVALTLL 76
PDZ3_Scribble-like cd06702
PDZ domain 3 of Drosophila Scribble, human Scribble homolog, and related domains; PDZ (PSD-95 ...
 286-366 8.00e-05

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: 41.86  E-value: 8.00e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720354236 286 PDENGRFGFNVKGGYD-------QKMP-VIVSRVAPGTPADLCVPRLneGDQVVLINGRDIAEHTHDQVVLFIKASCekh 357
Cdd:cd06702     6 VKAGGPLGLSIVGGSDhsshpfgVDEPgIFISKVIPDGAAAKSGLRI--GDRILSVNGKDLRHATHQEAVSALLSPG--- 80


                  ....*....
gi 1720354236 358 sGELVLLVR 366
Cdd:cd06702    81 -QEIKLLVR 88
PDZ_GOPC-like cd06800
PDZ domain of Golgi-associated PDZ and coiled-coil motif-containing protein (GOPC), and ...
 284-347 9.73e-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: 41.20  E-value: 9.73e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1720354236 284 MKPDENGrFGFNVKGGYDQKMPVIVSRVAPGTPADLCvPRLNEGDQVVLINGRDIAEHTHDQVV 347
Cdd:cd06800     6 SKEPHEG-LGISITGGKEHGVPILISEIHEGQPADRC-GGLYVGDAILSVNGIDLRDAKHKEAV 67
PDZ_SNX27-like cd23070
PDZ domain of sorting nexin-27 (SNX27), and related domains; PDZ (PSD-95 (Postsynaptic density ...
 281-365 1.91e-04

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: 40.85  E-value: 1.91e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720354236 281 LIKMKPDENGrFGFNVKGGYDQ--KMPVI----------VSRVAPGTPADLCvpRLNEGDQVVLINGRDIAEHTHDQVVL 348
Cdd:cd23070     2 VVTIVKSETG-FGFNVRGQVSEggQLRSIngelyaplqhVSAVLEGGAADKA--GVRKGDRILEVNGVNVEGATHKQVVD 78

                          90
                  ....*....|....*..
gi 1720354236 349 FIKAScekhSGELVLLV 365
Cdd:cd23070    79 LIKSG----GDELTLTV 91
FERM_C_PTPN14_PTPN21 cd13188
FERM domain C-lobe of Protein tyrosine phosphatase non-receptor proteins 14 and 21 (PTPN14 and ...
 4-74 1.96e-04

FERM domain C-lobe of Protein tyrosine phosphatase non-receptor proteins 14 and 21 (PTPN14 and 21); This CD contains PTP members: pez/PTPN14 and PTPN21. A number of mutations in Pez have been shown to be associated with breast and colorectal cancer. The PTPN protein family belong to larger family of PTPs. PTPs are known to be signaling molecules that regulate a variety of cellular processes including cell growth, differentiation, mitotic cycle, and oncogenic transformation. The members are composed of a N-terminal FERM domain and a C-terminal PTP catalytic domain. The FERM domain has a cloverleaf tripart structure composed of: (1) FERM_N (A-lobe or F1); (2) FERM_M (B-lobe, or F2); and (3) FERM_C (C-lobe or F3). The C-lobe/F3 within the FERM domain is part of the PH domain family. Like most other ERM members they have a phosphoinositide-binding site in their FERM domain. The FERM C domain is the third structural domain within the FERM domain. The FERM domain is found in the cytoskeletal-associated proteins such as ezrin, moesin, radixin, 4.1R, and merlin. These proteins provide a link between the membrane and cytoskeleton and are involved in signal transduction pathways. The FERM domain is also found in protein tyrosine phosphatases (PTPs) , the tyrosine kinases FAK and JAK, in addition to other proteins involved in signaling. This domain is structurally similar to the PH and PTB domains and consequently is capable of binding to both peptides and phospholipids at different sites.


Pssm-ID: 270009  Cd Length: 91  Bit Score: 40.73  E-value: 1.96e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1720354236   4 GILI-YKNRVRMNTFLWLKIVKISFKCKQFFIqlrkELHESRETLlGFNMVNYRACKTLWKACVEHHTFFRL 74
Cdd:cd13188    24 GIFVkHDNGRPPVFFRWEDIKNVINHKRTFSI----ECQNSEETV-QFQFEDAETAKYVWKLCVLQHKFYRQ 90
PDZ2_PDZD2-like cd06758
PDZ domain 2 of PDZ domain containing 2 (PDZD2), and related domains; PDZ (PSD-95 ...
 288-353 2.00e-04

PDZ domain 2 of PDZ domain containing 2 (PDZD2), and related domains; PDZ (PSD-95 (Postsynaptic density protein 95), Dlg (Discs large protein), and ZO-1 (Zonula occludens-1)) domain 2 of PDZD2, also known as KIAA0300, PIN-1, activated in prostate cancer (AIPC) and PDZ domain-containing protein 3 (PDZK3). PDZD2 has seven PDZ domains, and is expressed at exceptionally high levels in the pancreas and certain cancer tissues such as prostate cancer. It promotes the proliferation of insulinoma cells and is upregulated during prostate tumorigenesis. In osteosarcoma (OS), the microRNA miR-363 acts as a tumor suppressor by inhibiting PDZD2. PDZ domains usually bind in a sequence-specific manner to short peptide sequences located at the C-terminal end of their partner proteins (known as PDZ binding motifs). The PDZ superfamily includes canonical PDZ domains as well as those with circular permutations and domain swapping mediated by beta-strands. This PDZD2-like family PDZ2 domain is a canonical PDZ domain containing six beta-strands A-F and two alpha-helices (alpha-helix 1 and 2), arranged in the order: beta-strands A, B, C, alpha-helix 1, beta-strands D, E, alpha-helix 2 and beta-strand F.


Pssm-ID: 467239 [Multi-domain]  Cd Length: 88  Bit Score: 40.80  E-value: 2.00e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1720354236 288 ENGRFGFNVKGGYDQKMP---VIVSRVAPGTPADLCvPRLNEGDQVVLINGRDIAEHTHDQVVLFIKAS 353
Cdd:cd06758    10 EKGGLGIQITGGKGSKRGdigIFVAGVEEGGSADRD-GRLKKGDELLMINGQSLIGLSHQEAVAILRSS 77
PTPlike_phytase pfam14566
Inositol hexakisphosphate; Inositol hexakisphosphate, often called phytate, is found in ...
 541-636 2.34e-04

Inositol hexakisphosphate; Inositol hexakisphosphate, often called phytate, is found in abundance in seeds and acting as an inorganic phosphate reservoir. Phytases are phosphatases that hydrolyze phytate to less-phosphorylated myo-inositol derivatives and inorganic phosphate. The active-site sequence (HCXXGXGR) of the phytase identified from the gut micro-organizm Selenomonas ruminantium forms a loop (P loop) at the base of a substrate binding pocket that is characteriztic of protein tyrosine phosphatases (PTPs). The depth of this pocket is an important determinant of the substrate specificity of PTPs. In humans this enzyme is thought to aid bone mineralization and salvage the inositol moiety prior to apoptosis.


Pssm-ID: 464208 [Multi-domain]  Cd Length: 157  Bit Score: 42.30  E-value: 2.34e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720354236 541 GCYQVTCHSEEGnpayIFRKMTLFNQEKNESrqlTQIQYT--AWPDHGVPDDSsDFLDFVCHVRDqrAGKEEPIIVHCSA 618
Cdd:pfam14566  72 GVLTVVDVWESD----VQTPEEVYERLKAEG---PGVDYRriPITDEKAPLEE-DFDALISIVKD--APEDTALVFNCQM 141

                          90       100
                  ....*....|....*....|.
gi 1720354236 619 GIGRTgvliTmeTAM---CLI 636
Cdd:pfam14566 142 GRGRT----T--TAMviaDLV 156
PDZ_shroom2_3_4-like cd06750
PDZ domain of shroom2, shroom3, shroom4, and related domains; PDZ (PSD-95 (Postsynaptic ...
 293-353 3.58e-04

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: 39.63  E-value: 3.58e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1720354236 293 GFNVKGGYDQKMPVIVSRVAPGTPADLcVPRLNEGDQVVLINGRDIAEhTHDQVVLFIKAS 353
Cdd:cd06750    14 GFTLKGGLEHGEPLVISKIEEGGKAAS-VGKLQVGDEVVNINGVPLSG-SRQEAIQLVKGS 72
PDZ5_DrPTPN13-like cd23060
PDZ domain 5 of Danio rerio tyrosine-protein phosphatase non-receptor type 13 (Ptpn13) and ...
 285-365 4.27e-04

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: 39.64  E-value: 4.27e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720354236 285 KPdENGRFGFNVKGGyDQKMPVIVSRVAPGTPADLcVPRLNEGDQVVLINGRDIAEHTHDQVVLFIKasceKHSGELVLL 364
Cdd:cd23060     6 KP-ANGGLGFSLVGG-EGGSGIFVKSISPGGVADR-DGRLQVGDRLLQVNGESVIGLSHSKAVNILR----KAKGTVQLT 78


                  .
gi 1720354236 365 V 365
Cdd:cd23060    79 V 79
PDZ_densin_erbin-like cd06749
PDZ domain of densin, erbin, and related domains; PDZ (PSD-95 (Postsynaptic density protein 95) ...
 289-353 4.61e-04

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: 39.62  E-value: 4.61e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1720354236 289 NGRFGFNVKGGYDQK--------MPVIVSRVAPGTPADLCvprLNEGDQVVLINGRDIAEHTHDQVVLFIKAS 353
Cdd:cd06749     8 NPGLGFSISGGIGSQgnpfrpddDGIFVTKVQPDGPASKL---LQPGDKILEVNGYDFVNIEHGQAVSLLKSF 77
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 ...
 287-347 5.52e-04

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: 39.16  E-value: 5.52e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1720354236 287 DENGRFGFNVKGGYDQKMPVI-VSRVAPGTPADLcVPRLNEGDQVVLINGRDIAEHTHDQVV 347
Cdd:cd06762     9 EEGSGLGFSLAGGSDLENKSItVHRVFPSGLAAQ-EGTIQKGDRILSINGKSLKGVTHGDAL 69
PDZ_RapGEF2_RapGEF6-like cd06755
PDZ domain of Rap guanine nucleotide exchange factor 2 and Rap guanine nucleotide exchange ...
 284-353 7.08e-04

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: 38.78  E-value: 7.08e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1720354236 284 MKPDENGRFGFNVKGGYDQKMPVIVSRVAPGTPA-DLCVPRlneGDQVVLINGRDIAEHTHDQVVLFIKAS 353
Cdd:cd06755     6 TRPSRESPLHFSLLGGSEKGFGIFVSKVEKGSKAaEAGLKR---GDQILEVNGQNFENITLKKALEILRNN 73
PDZ_Par6-like cd06718
PDZ domain of partitioning defective 6 (Par6), Drosophila Rho GTPase-activating protein 100F ...
 292-367 1.15e-03

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: 38.32  E-value: 1.15e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720354236 292 FGFNVKGGYDQ-KMP-VIVSRVAPGTPAD----LCVprlneGDQVVLINGRDIAEHTHDQVVLFIKAscekhSGELVLLV 365
Cdd:cd06718    13 LGFYIRDGNGVeRVPgIFISRLVLGSLADstglLAV-----GDEILEVNGVEVTGKSLDDVTDMMVA-----PTRLIITV 82


                  ..
gi 1720354236 366 RP 367
Cdd:cd06718    83 KP 84
PDZ4_GRIP1-2-like cd06686
PDZ domain 4 of glutamate receptor-interacting protein 1 (GRIP1) and GRIP2, and related ...
 276-375 1.17e-03

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: 38.87  E-value: 1.17e-03
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                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720354236 276 HDNLVLIKMKPDENGRFGFNVKGG-YDQKM---PVIVSRVAPGTPADLC-VprLNEGDQVVLINGRDIAEHTHDQVVLFI 350
Cdd:cd06686     4 HTETTEVILRGDPLKGFGIQLQGGvFATETlssPPLISFIEPDSPAERCgV--LQVGDRVLSINGIPTEDRTLEEANQLL 81

                          90       100
                  ....*....|....*....|....*
gi 1720354236 351 KAScekhSGELVLLVRpnavYDVVE 375
Cdd:cd06686    82 RDS----ASKVTLEIE----FDVAE 98
FERM_C_MYLIP_IDOL cd13195
FERM domain C-lobe of E3 ubiquitin ligase myosin regulatory light chain-interacting protein ...
 4-75 1.32e-03

FERM domain C-lobe of E3 ubiquitin ligase myosin regulatory light chain-interacting protein (MYLIP; also called inducible degrader of the LDL receptor, IDOL); MYLIP/IDOL is a regulator of the LDL receptor (LDLR) pathway via the nuclear receptor liver X receptor (LXR). In response to cellular cholesterol loading, the activation of LXR leads to the induction of MYLIP expression. MYLIP stimulates ubiquitination of the LDLR on its cytoplasmic tail, directing its degradation. The LXR-MYLIP-LDLR pathway provides a complementary pathway to sterol regulatory element-binding proteins for the feedback inhibition of cholesterol uptake. MYLIP has an N-terminal FERM domain and in some cases a C-terminal RING domain. The FERM domain has a cloverleaf tripart structure composed of: (1) FERM_N (A-lobe or F1); (2) FERM_M (B-lobe, or F2); and (3) FERM_C (C-lobe or F3). The C-lobe/F3 within the FERM domain is part of the PH domain family. The FERM domain is found in the cytoskeletal-associated proteins such as ezrin, moesin, radixin, 4.1R, and merlin. These proteins provide a link between the membrane and cytoskeleton and are involved in signal transduction pathways. The FERM domain is also found in protein tyrosine phosphatases (PTPs), the tyrosine kinases FAK and JAK, in addition to other proteins involved in signaling. This domain is structurally similar to the PH and PTB domains and consequently is capable of binding to both peptides and phospholipids at different sites.


Pssm-ID: 270016  Cd Length: 111  Bit Score: 38.77  E-value: 1.32e-03
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                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1720354236   4 GILIYKNRVRM-NTFLWLKIVKISFKCKQFFIQLRKELHEsrETLLGFNMVNYRACKTLWKACVEHHTFFRLD 75
Cdd:cd13195    24 GITICNDDFEViERIPYTAIQMATSSGRVFTLTYLSDDGS--VKVLEFKLPSTRAASGLYRAITEKHAFYRCE 94
PDZ_RIM-like cd06714
PDZ domain of Rab3-interacting molecule 1 (RIM), RIM2, piccolo and related domains; PDZ ...
 283-366 1.37e-03

PDZ domain of Rab3-interacting molecule 1 (RIM), RIM2, piccolo and related domains; PDZ (PSD-95 (Postsynaptic density protein 95), Dlg (Discs large protein), and ZO-1 (Zonula occludens-1)) domain of RIM, RIM2, piccolo and related domains. RIM proteins and Gallus gallus protein piccolo (also called aczonin) are involved in neurotransmitter release at presynaptic active zones, the site of vesicle fusion. A protein complex containing RIM proteins positions synaptic vesicles containing synaptotagmin at the active zone. RIM proteins simultaneously activate docking and priming of synaptic vesicles and recruit Ca2+-channels to active zones, thereby connecting primed synaptic vesicles to Ca2+-channels. RIM binding to vesicular Rab proteins (Rab3 and Rab27 isoforms) mediates vesicle docking; RIM binding to Munc13 activates vesicle priming; RIM binding to the Ca2+-channel, both directly and indirectly via RIM-BP, recruits the Ca2+-channels. The RIM PDZ domain interacts with the C-termini of N- and P/Q-type voltage-gated Ca2+-channels. RIM1, RIM2 and piccolo also participate in regulated exocytosis through binding cAMP-GEFII (cAMP-binding protein-guanidine nucleotide exchange factor II). The piccolo PDZ domain binds cAMP-GEFII. RIM2 also plays a role in dendrite formation by melanocytes. Caenorhabditis elegans RIM (also known as unc-10) may be involved in the regulation of defecation and daumone response. 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 RIM-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: 467198 [Multi-domain]  Cd Length: 95  Bit Score: 38.30  E-value: 1.37e-03
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                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720354236 283 KMKPDENGRFGFNVKGGY---DQKMPVIVSRVAPGTPADLcVPRLNEGDQVVLINGRDIAEHTHDQVVLFIKASCekhsG 359
Cdd:cd06714    14 KDGSVSGNGLGLKVVGGKmteSGRLGAYVTKVKPGSVADT-VGHLREGDEVLEWNGISLQGKTFEEVQDIISQSK----G 88


                  ....*..
gi 1720354236 360 ELVLLVR 366
Cdd:cd06714    89 EVELVVS 95
CDC14_C cd14499
C-terminal dual-specificity phosphatase domain of CDC14 family proteins; The cell division ...
 583-627 1.60e-03

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: 39.74  E-value: 1.60e-03
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                  ....*....|....*....|....*....|....*....|....*....
gi 1720354236 583 PDHGVPDDS--SDFLDfVCHvrdqragkEEP--IIVHCSAGIGRTGVLI 627
Cdd:cd14499    88 PDGSTPSDDivKKFLD-ICE--------NEKgaIAVHCKAGLGRTGTLI 127
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 ...
 293-366 1.64e-03

PDZ domain 3 of PDZ domain containing 2 (PDZD2), PDZ domain 1 of human pro-interleukin-16 (isoform 1, 1332 AA), and related domains; PDZ (PSD-95 (Postsynaptic density protein 95), Dlg (Discs large protein), and ZO-1 (Zonula occludens-1)) domain 3 of PDZD2, also known as KIAA0300, PIN-1, activated in prostate cancer (AIPC) and PDZ domain-containing protein 3 (PDZK3). PDZD2 has seven PDZ domains. PDZD2 is expressed at exceptionally high levels in the pancreas and certain cancer tissues, such as prostate cancer. It promotes the proliferation of insulinoma cells and is upregulated during prostate tumorigenesis. In osteosarcoma (OS), the microRNA miR-363 acts as a tumor suppressor by inhibiting PDZD2. This family also includes the first PDZ domain (PDZ1) of human pro-interleukin-16 (isoform 1, also known as nPro-Il-16; 1332 amino-acid protein). Precursor IL-16 is cleaved to produce pro-IL-16 and mature IL-16 (derived from the C-terminal 121 AA). Pro-IL-16 functions as a regulator of T cell growth; mature IL-16 is a CD4 ligand that induces chemotaxis and CD25 expression in CD4+ T cells. IL-16 bioactivity has been closely associated with the progression of several different cancers. PDZ domains usually bind in a sequence-specific manner to short peptide sequences located at the C-terminal end of their partner proteins (known as PDZ binding motifs). The PDZ superfamily includes canonical PDZ domains as well as those with circular permutations and domain swapping mediated by beta-strands. This PDZD2-like family PDZ3 domain is a canonical PDZ domain containing six beta-strands A-F and two alpha-helices (alpha-helix 1 and 2), arranged in the order: beta-strands A, B, C, alpha-helix 1, beta-strands D, E, alpha-helix 2 and beta-strand F.


Pssm-ID: 467240 [Multi-domain]  Cd Length: 87  Bit Score: 38.02  E-value: 1.64e-03
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                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1720354236 293 GFNVKGGYDQK---MPVIVSRVAPGTPA--DlcvPRLNEGDQVVLINGRDIAEHTHDQVVLFIKascEKHSGELVLLVR 366
Cdd:cd06759    15 GFSIVGGRDSPrgpMGIYVKTIFPGGAAaeD---GRLKEGDEILEVNGESLQGLTHQEAIQKFK---QIKKGLVVLTVR 87
FERM_C_PTPH13 cd13187
FERM domain C-lobe of Protein tyrosine phosphatase non-receptor 13 (PTPH13); There are many ...
 1-71 1.92e-03

FERM domain C-lobe of Protein tyrosine phosphatase non-receptor 13 (PTPH13); There are many functions of PTPN13 (also called PTPL1, PTP-BAS, hPTP1E, FAP1, or PTPL1). Mice lacking PTPN13 activity have abnormal regulation of signal transducer and activator of transcription signaling in their T cells, mild impairment of motor nerve repair, and a significant reduction in the growth of retinal glia cultures. It also plays a role in adipocyte differentiation. PTPN13 contains a kinase non-catalytic C-lobe domain (KIND), a FERM domain with two potential phosphatidylinositol 4,5-biphosphate [PtdIns(4,5)P2]-binding motifs, 5 PDZ domains, and a carboxy-terminal catalytic domain. There is an nteraction between the FERM domain of PTPL1 and PtdIns(4,5)P2 which is thought to regulate the membrane localization of PTPN13. PDZ are protein/protein interaction domains so there is the potential for numerous partners that can actively participate in the regulation of its phosphatase activity or can permit direct or indirect recruitment of tyrosine phosphorylated PTPL1 substrates. The FERM domain has a cloverleaf tripart structure composed of: (1) FERM_N (A-lobe or F1); (2) FERM_M (B-lobe, or F2); and (3) FERM_C (C-lobe or F3). The C-lobe/F3 within the FERM domain is part of the PH domain family. The FERM domain is found in the cytoskeletal-associated proteins such as ezrin, moesin, radixin, 4.1R, and merlin. These proteins provide a link between the membrane and cytoskeleton and are involved in signal transduction pathways. The FERM domain is also found in protein tyrosine phosphatases (PTPs), the tyrosine kinases FAK and JAK, in addition to other proteins involved in signaling. This domain is structurally similar to the PH and PTB domains and consequently is capable of binding to both peptides and phospholipids at different sites.


Pssm-ID: 270008  Cd Length: 103  Bit Score: 38.07  E-value: 1.92e-03
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gi 1720354236   1 MSGGILIY--KNRVRMNT--FLWLKIVKISFKCKQFFIQLRKELHESretlLGFNMVNYRACKTLWKACVEHHTF 71
Cdd:cd13187    23 CSRGIIIYeeKNGARTPVlrFPWRETQKISFDKKKFTIESRGGSGIK----HTFYTDSYKKSQYLLQLCSAQHKF 93
PDZ3_LNX1_2-like cd06679
PDZ domain 3 of human Ligand of Numb protein X 1 (LNX1) and LNX2, and related domains; PDZ ...
 279-365 2.29e-03

PDZ domain 3 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 3 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 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: 467167 [Multi-domain]  Cd Length: 88  Bit Score: 37.62  E-value: 2.29e-03
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gi 1720354236 279 LVLIKMKPDENgrFGFNVKGGYDQK---MPVIVSRVAPgtpaDLCVPR---LNEGDQVVLINGRDIAEHTHDQVVLFIKA 352
Cdd:cd06679     2 TVTIKKEPSES--LGISVAGGRGSRrgdLPIYVTNVQP----DGCLGRdgrIKKGDVLLSINGISLTNLSHSEAVAVLKA 75

                          90
                  ....*....|...
gi 1720354236 353 SCEkhSGELVLLV 365
Cdd:cd06679    76 SAA--SSSIVLKV 86
PDZ_RGS3-like cd06711
PDZ domain of regulator of G-protein signaling 3 (RGS3), and related domains; PDZ (PSD-95 ...
 292-363 2.89e-03

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: 36.98  E-value: 2.89e-03
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gi 1720354236 292 FGFNVKGgydqKMPVIVSRVAPGTPADLCvpRLNEGDQVVLINGRDIAEHTHDQVVLFIKaSCEKHSGELVL 363
Cdd:cd06711    12 FGFTICD----DSPVRVQAVDPGGPAEQA--GLQQGDTVLQINGQPVERSKCVELAHAIR-NCPSEIILLVW 76
PDZ1_syntenin-like cd06721
PDZ domain 1 of syntenin-1, syntenin-2, and related domains; PDZ (PSD-95 (Postsynaptic density ...
 279-366 3.18e-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: 36.83  E-value: 3.18e-03
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gi 1720354236 279 LVLIKmkpDENGRFGFNVKggyDQKMPVIVSRVAPGTPADLCVPRLneGDQVVLINGRDIAEHTHDQVVLFIKasceKHS 358
Cdd:cd06721     3 VILCK---DQDGKIGLRVK---SIDKGVFVQLVQANSPAALAGLRF--GDQILQINGENVAGWSSDKAHKVLK----KAS 70


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gi 1720354236 359 GE-LVLLVR 366
Cdd:cd06721    71 PErITLAVR 79
DSP_DUSP11 cd17665
dual-specificity phosphatase domain of dual specificity protein phosphatase 11 and similar ...
 583-627 3.44e-03

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: 38.80  E-value: 3.44e-03
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gi 1720354236 583 PDHGVPDDS--SDFLDFVCHVRDQRAGKEEPIIVHCSAGIGRTGVLI 627
Cdd:cd17665    85 PGHQVPDDKtiQSFKDAVKDFLEKNKDNDKLIGVHCTHGLNRTGYLI 131
PDZ4_PTPN13-like cd06696
PDZ domain 4 of protein tyrosine phosphatase non-receptor type 13 (PTPN13), and related ...
 284-353 3.59e-03

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: 36.90  E-value: 3.59e-03
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gi 1720354236 284 MKPdENGRFGFNVKGGYDQKMPVIVSRVAPGTPADlcvPRLNEGDQVVLINGRDIAEHTHDQVVLFIKAS 353
Cdd:cd06696     9 TKS-EKGSLGFTVTKGKDDNGCYIHDIVQDPAKSD---GRLRPGDRLIMVNGVDVTNMSHTEAVSLLRAA 74
TpbA-like cd14529
bacterial protein tyrosine and dual-specificity phosphatases related to Pseudomonas aeruginosa ...
 575-637 3.60e-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: 38.51  E-value: 3.60e-03
                          10        20        30        40        50        60
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gi 1720354236 575 TQIQYTAWPDHGVPDDSSDfLDFVCHVRDqRAGKEEPIIVHCSAGIGRTGVLitmeTAMCLIE 637
Cdd:cd14529    57 DGVKYVNLPLSATRPTESD-VQSFLLIMD-LKLAPGPVLIHCKHGKDRTGLV----SALYRIV 113
CtpA COG0793
C-terminal processing protease CtpA/Prc, contains a PDZ domain [Posttranslational modification, ...
 284-351 4.44e-03

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: 39.85  E-value: 4.44e-03
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                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1720354236 284 MKPDENGRFG-----FNVKGGYdqkmpVIVSRVAPGTPADLcvPRLNEGDQVVLINGRDIAEHTHDQVVLFIK 351
Cdd:COG0793    51 FQESTSGEFGglgaeLGEEDGK-----VVVVSVIPGSPAEK--AGIKPGDIILAIDGKSVAGLTLDDAVKLLR 116
PDZ_CNK1_2_3-like cd06748
PDZ domain of connector enhancer of kinase suppressor of ras 1 (CNK1), CNK2, CNK3, and related ...
 280-336 6.31e-03

PDZ domain of connector enhancer of kinase suppressor of ras 1 (CNK1), CNK2, CNK3, and related domains; PDZ (PSD-95 (Postsynaptic density protein 95), Dlg (Discs large protein), and ZO-1 (Zonula occludens-1)) domain of CNK1 (also known as connector enhancer of KSR 1 (CNKSR1), CNK homolog protein 1, connector enhancer of KSR-like), CNK2 (also known as CNKSR2, CNK homolog protein 2), and CNK3 (also known as CNKSR3, CNK homolog protein 3, CNKSR family member 3, maguin-like). CNK proteins modulate Ras-mediated signaling, acting downstream of Ras as a scaffold for the Raf/MEK/ERK kinase cascade. They also modulate signaling mediated via Rho family small GTPases, through interactions with various guanine nucleotide exchange factors (GEFs) and GTPase activating proteins (GAPs), and modulate the insulin signaling pathway through interactions with the Arf guanine nucleotide exchange factors. CNK proteins also regulate cell proliferation and migration by acting as scaffolds for the PI3K/Akt and JNK signaling cascades. CNK2 plays a role in the molecular processes that govern morphology of the postsynaptic density (PSD), and influences subcellular localization of the regulatory NCK-interacting kinase TNIK. TNIK binds a region of CNK2 including the PDZ and the DUF domain; this region also binds the kinase MINK1. CNK2 may also influence the membrane localization of MINK1. CNK3 plays a part in transepithelial sodium transport; it coordinates assembly of an epithelial sodium channel (ENaC)-regulatory complex. PDZ domains usually bind in a sequence-specific manner to short peptide sequences located at the C-terminal end of their partner proteins (known as PDZ binding motifs). The PDZ superfamily includes canonical PDZ domains as well as those with circular permutations and domain swapping mediated by beta-strands. This CNK1-like family domain is a canonical PDZ domain containing six beta-strands A-F and two alpha-helices (alpha-helix 1 and 2), arranged as beta-strands A, B, C, alpha-helix 1, beta-strands D, E, alpha-helix 2 and beta- strand F.


Pssm-ID: 467230 [Multi-domain]  Cd Length: 81  Bit Score: 36.05  E-value: 6.31e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1720354236 280 VLIKMKPDENgrFGFNVKGGYDQKMpvIVSRVAPGTPADLCvPRLNEGDQVVLINGR 336
Cdd:cd06748     4 QLTNKKPEEG--LGLEIKSTYNGLH--VITGTKENSPADRC-GKIHAGDEVIQVNYQ 55
PDZ2_MAGI-1_3-like cd06732
PDZ domain 2 of membrane-associated guanylate kinase inverted 1 (MAGI-1), MAGI-2, and MAGI-3, ...
 279-365 7.68e-03

PDZ domain 2 of membrane-associated guanylate kinase inverted 1 (MAGI-1), MAGI-2, and MAGI-3, and related domains; PDZ (PSD-95 (Postsynaptic density protein 95), Dlg (Discs large protein), and ZO-1 (Zonula occludens-1)) domain 2 of MAGI1, 2, 3 (MAGI is also known as Membrane-associated guanylate kinase, WW and PDZ domain-containing protein) and related domains. MAGI proteins have been implicated in the control of cell migration and invasion through altering the activity of phosphatase and tensin homolog (PTEN) and modulating Akt signaling. Four MAGI proteins have been identified (MAGI1-3 and MAGIX). MAGI1-3 have 6 PDZ domains and bind to the C-terminus of PTEN via their PDZ2 domain. MAGIX has a single PDZ domain that is related to MAGI1-3 PDZ domain 5. Other binding partners for MAGI1 include JAM4, C-terminal tail of high risk HPV-18 E6, megalin, TRAF6, Kir4.1 (basolateral K+ channel subunit), and cadherin 23; for MAGI2, include DASM1, dendrin, axin, beta- and delta-catenin, neuroligin, hyperpolarization-activated cation channels, beta1-adrenergic receptors, NMDA receptor, and TARPs; and for MAGI3 includes LPA2. PDZ domains usually bind in a sequence-specific manner to short peptide sequences located at the C-terminal end of their partner proteins (known as PDZ binding motifs). The PDZ superfamily includes canonical PDZ domains as well as those with circular permutations and domain swapping mediated by beta-strands. This MAGI family PDZ2 domain is a canonical PDZ domain containing six beta-strands A-F and two alpha-helices (alpha-helix 1 and 2); arranged as beta-strands A, -B, C, alpha-helix 1, beta-strands D, E, alpha-helix 2 and beta-strand F.


Pssm-ID: 467214 [Multi-domain]  Cd Length: 82  Bit Score: 35.99  E-value: 7.68e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720354236 279 LVLIKMKPDENGrFGFNVKG-GYDQKMPVIVSRVapgtpadlCVPRLNEGDQVVLINGRDIAEHTHDQVVLFIKaSCEKh 357
Cdd:cd06732     3 LVTVPIVKGPMG-FGFTIADsPQGQRVKQILDPQ--------RCRGLQEGDLIVEINGQNVQNLSHAQVVDVLK-ECPK- 71


                  ....*...
gi 1720354236 358 SGELVLLV 365
Cdd:cd06732    72 GSEVTLLV 79
PTP_PTEN cd14509
protein tyrosine phosphatase-like catalytic domain of phosphatase and tensin homolog; ...
 612-668 9.46e-03

protein tyrosine phosphatase-like catalytic domain of phosphatase and tensin homolog; Phosphatase and tensin homolog (PTEN), also phosphatidylinositol 3,4,5-trisphosphate 3-phosphatase and dual-specificity protein phosphatase PTEN or mutated in multiple advanced cancers 1 (MMAC1), is a tumor suppressor that acts as a dual-specificity protein phosphatase and as a lipid phosphatase. It is a critical endogenous inhibitor of phosphoinositide signaling. It dephosphorylates phosphoinositide trisphosphate, and therefore, has the function of negatively regulating Akt. The PTEN/PI3K/AKT pathway regulates the signaling of multiple biological processes such as apoptosis, metabolism, cell proliferation, and cell growth. PTEN contains an N-terminal PIP-binding domain, a protein tyrosine phosphatase (PTP)-like catalytic domain, a regulatory C2 domain responsible for its cellular location, a C-tail containing phosphorylation sites, and a C-terminal PDZ domain.


Pssm-ID: 350359 [Multi-domain]  Cd Length: 158  Bit Score: 37.57  E-value: 9.46e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1720354236 612 IIVHCSAGIGRTGVLItmetAMCLIECNQPVYPLD------IVRTmRDQRAMMIqtPSQYRFV 668
Cdd:cd14509    97 AAVHCKAGKGRTGVMI----CCYLLYLGKFPSAKEaldfygAKRT-KNKKGVTI--PSQRRYV 152
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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