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Conserved domains on  [gi|45553601|ref|NP_996302|]
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protein tyrosine phosphatase 99A, isoform C [Drosophila melanogaster]

Protein Classification

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
R5-PTPc-1 cd14549
catalytic domain of R5 subfamily receptor-type tyrosine-protein phosphatases, repeat 1; The R5 ...
548-751 4.30e-143

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: 431.00  E-value: 4.30e-143
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45553601  548 YINANFIDGYQKGHAFIGTQGPLPDTFDCFWRMIWEQRVAIIVMITNLVERGRRKCDMYWPKDGVETYGVIQVKLIEEEV 627
Cdd:cd14549    1 YINANYVDGYNKARAYIATQGPLPSTFDDFWRMVWEQNSAIIVMITNLVERGRRKCDQYWPKEGTETYGNIQVTLLSTEV 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45553601  628 MSTYTVRTLQIKHLKLKKKKQCNTEKLVYQYHYTNWPDHGTPDHPLPVLNFVKKSSAANPAEAGPIVVHCSAGVGRTGTY 707
Cdd:cd14549   81 LATYTVRTFSLKNLKLKKVKGRSSERVVYQYHYTQWPDHGVPDYTLPVLSFVRKSSAANPPGAGPIVVHCSAGVGRTGTY 160
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....
gi 45553601  708 IVLDAMLKQIQQKNIVNVFGFLRHIRAQRNFLVQTEEQYIFLHD 751
Cdd:cd14549  161 IVIDSMLQQIQDKGTVNVFGFLKHIRTQRNYLVQTEEQYIFIHD 204
R5-PTP-2 cd14550
PTP-like domain of R5 subfamily receptor-type tyrosine-protein phosphatases, repeat 2; The R5 ...
833-1026 1.09e-101

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: 320.42  E-value: 1.09e-101
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45553601  833 YINASWLHGFRRLRDFIVTQHPMAHTIKDFWQMVWDHNAQTVVLLSSLD-DINFAQFWPDEATPIESDHYRVKFLNKTNK 911
Cdd:cd14550    1 YINASYLQGYRRSNEFIITQHPLEHTIKDFWQMIWDHNSQTIVMLTDNElNEDEPIYWPTKEKPLECETFKVTLSGEDHS 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45553601  912 S-----DYVSRDFVIQSIQDDYELTVKMLHCPSWPEMSNP-NSIYDFIVDVHERCNDyRNGPIVIVDRYGGAQACTFCAI 985
Cdd:cd14550   81 ClsneiRLIVRDFILESTQDDYVLEVRQFQCPSWPNPCSPiHTVFELINTVQEWAQQ-RDGPIVVHDRYGGVQAATFCAL 159
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|.
gi 45553601  986 SSLAIEMEYCSTANVYQYAKLYHNKRPGVWTSSEDIRVIYN 1026
Cdd:cd14550  160 TTLHQQLEHESSVDVYQVAKLYHLMRPGVFTSKEDYQFLYK 200
fn3 pfam00041
Fibronectin type III domain;
172-274 6.53e-16

Fibronectin type III domain;


:

Pssm-ID: 394996 [Multi-domain]  Cd Length: 85  Bit Score: 73.99  E-value: 6.53e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45553601    172 SKPQNLTILDVSANSITMSWHPPKNQNGAIAGYHVFHIHDNQTGVEivkNSRNSVETLIHFELQNLRefnyvfiwglfgv 251
Cdd:pfam00041    1 SAPSNLTVTDVTSTSLTVSWTPPPDGNGPITGYEVEYRPKNSGEPW---NEITVPGTTTSVTLTGLK------------- 64
                           90       100
                   ....*....|....*....|...
gi 45553601    252 kgPYTDYRVIVKAFTTKNEGEPS 274
Cdd:pfam00041   65 --PGTEYEVRVQAVNGGGEGPPS 85
FN3 super family cl27307
Fibronectin type 3 domain [General function prediction only];
111-364 4.27e-09

Fibronectin type 3 domain [General function prediction only];


The actual alignment was detected with superfamily member COG3401:

Pssm-ID: 442628 [Multi-domain]  Cd Length: 603  Bit Score: 60.79  E-value: 4.27e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45553601  111 PVLGTVATSIEQQDQPPDVPATTLAFANAFPVPVAGEmgngnGNYNDATPPYAAVDDNYVPSKPQNLTILDVSANSITMS 190
Cdd:COG3401  178 AAVATTSLTVTSTTLVDGGGDIEPGTTYYYRVAATDT-----GGESAPSNEVSVTTPTTPPSAPTGLTATADTPGSVTLS 252
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45553601  191 WHPpkNQNGAIAGYHVFHIHDNQTGVEIVKNSRNSveTLIHFELQNLREFNYVfiwglfgvkgpytdyrviVKAFTT-KN 269
Cdd:COG3401  253 WDP--VTESDATGYRVYRSNSGDGPFTKVATVTTT--SYTDTGLTNGTTYYYR------------------VTAVDAaGN 310
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45553601  270 EGEPSDQIAQRTDVGGPSAPAIVNLTCHSQESITIRWRRPYEfyNTIDFYII--KTRLAGQDThrdiRINASAKelETAM 347
Cdd:COG3401  311 ESAPSNVVSVTTDLTPPAAPSGLTATAVGSSSITLSWTASSD--ADVTGYNVyrSTSGGGTYT----KIAETVT--TTSY 382
                        250
                 ....*....|....*..
gi 45553601  348 ILQNLTTNSYYEVKVAA 364
Cdd:COG3401  383 TDTGLTPGTTYYYKVTA 399
 
Name Accession Description Interval E-value
R5-PTPc-1 cd14549
catalytic domain of R5 subfamily receptor-type tyrosine-protein phosphatases, repeat 1; The R5 ...
548-751 4.30e-143

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: 431.00  E-value: 4.30e-143
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45553601  548 YINANFIDGYQKGHAFIGTQGPLPDTFDCFWRMIWEQRVAIIVMITNLVERGRRKCDMYWPKDGVETYGVIQVKLIEEEV 627
Cdd:cd14549    1 YINANYVDGYNKARAYIATQGPLPSTFDDFWRMVWEQNSAIIVMITNLVERGRRKCDQYWPKEGTETYGNIQVTLLSTEV 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45553601  628 MSTYTVRTLQIKHLKLKKKKQCNTEKLVYQYHYTNWPDHGTPDHPLPVLNFVKKSSAANPAEAGPIVVHCSAGVGRTGTY 707
Cdd:cd14549   81 LATYTVRTFSLKNLKLKKVKGRSSERVVYQYHYTQWPDHGVPDYTLPVLSFVRKSSAANPPGAGPIVVHCSAGVGRTGTY 160
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....
gi 45553601  708 IVLDAMLKQIQQKNIVNVFGFLRHIRAQRNFLVQTEEQYIFLHD 751
Cdd:cd14549  161 IVIDSMLQQIQDKGTVNVFGFLKHIRTQRNYLVQTEEQYIFIHD 204
PTPc smart00194
Protein tyrosine phosphatase, catalytic domain;
490-755 5.04e-117

Protein tyrosine phosphatase, catalytic domain;


Pssm-ID: 214550 [Multi-domain]  Cd Length: 259  Bit Score: 364.29  E-value: 5.04e-117
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45553601     490 GFSREYEAIQNECIsDDLPCEHSQHPENKRKNRYLNITAYDHSRVHLHPTPGQkkNLDYINANFIDGYQKGHAFIGTQGP 569
Cdd:smart00194    1 GLEEEFEKLDRLKP-DDESCTVAAFPENRDKNRYKDVLPYDHTRVKLKPPPGE--GSDYINASYIDGPNGPKAYIATQGP 77
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45553601     570 LPDTFDCFWRMIWEQRVAIIVMITNLVERGRRKCDMYWPKDGVE--TYGVIQVKLIEEEVMSTYTVRTLQIKHLklkkkk 647
Cdd:smart00194   78 LPSTVEDFWRMVWEQKVTVIVMLTELVEKGREKCAQYWPDEEGEplTYGDITVTLKSVEKVDDYTIRTLEVTNT------ 151
                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45553601     648 QCNTEKLVYQYHYTNWPDHGTPDHPLPVLNFVKKSSAANPAEAGPIVVHCSAGVGRTGTYIVLDAMLKQIQQKNIVNVFG 727
Cdd:smart00194  152 GCSETRTVTHYHYTNWPDHGVPESPESILDLIRAVRKSQSTSTGPIVVHCSAGVGRTGTFIAIDILLQQLEAGKEVDIFE 231
                           250       260
                    ....*....|....*....|....*...
gi 45553601     728 FLRHIRAQRNFLVQTEEQYIFLHDALVE 755
Cdd:smart00194  232 IVKELRSQRPGMVQTEEQYIFLYRAILE 259
Y_phosphatase pfam00102
Protein-tyrosine phosphatase;
517-755 9.81e-106

Protein-tyrosine phosphatase;


Pssm-ID: 459674 [Multi-domain]  Cd Length: 234  Bit Score: 333.05  E-value: 9.81e-106
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45553601    517 NKRKNRYLNITAYDHSRVHLHPTPGQKknlDYINANFIDGYQKGHAFIGTQGPLPDTFDCFWRMIWEQRVAIIVMITNLV 596
Cdd:pfam00102    1 NLEKNRYKDVLPYDHTRVKLTGDPGPS---DYINASYIDGYKKPKKYIATQGPLPNTVEDFWRMVWEEKVTIIVMLTELE 77
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45553601    597 ERGRRKCDMYWP--KDGVETYGVIQVKLI-EEEVMSTYTVRTLQIkhlklkKKKQCNTEKLVYQYHYTNWPDHGTPDHPL 673
Cdd:pfam00102   78 EKGREKCAQYWPeeEGESLEYGDFTVTLKkEKEDEKDYTVRTLEV------SNGGSEETRTVKHFHYTGWPDHGVPESPN 151
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45553601    674 PVLNFVKK-SSAANPAEAGPIVVHCSAGVGRTGTYIVLDAMLKQIQQKNIVNVFGFLRHIRAQRNFLVQTEEQYIFLHDA 752
Cdd:pfam00102  152 SLLDLLRKvRKSSLDGRSGPIVVHCSAGIGRTGTFIAIDIALQQLEAEGEVDIFQIVKELRSQRPGMVQTLEQYIFLYDA 231

                   ...
gi 45553601    753 LVE 755
Cdd:pfam00102  232 ILE 234
R5-PTP-2 cd14550
PTP-like domain of R5 subfamily receptor-type tyrosine-protein phosphatases, repeat 2; The R5 ...
833-1026 1.09e-101

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: 320.42  E-value: 1.09e-101
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45553601  833 YINASWLHGFRRLRDFIVTQHPMAHTIKDFWQMVWDHNAQTVVLLSSLD-DINFAQFWPDEATPIESDHYRVKFLNKTNK 911
Cdd:cd14550    1 YINASYLQGYRRSNEFIITQHPLEHTIKDFWQMIWDHNSQTIVMLTDNElNEDEPIYWPTKEKPLECETFKVTLSGEDHS 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45553601  912 S-----DYVSRDFVIQSIQDDYELTVKMLHCPSWPEMSNP-NSIYDFIVDVHERCNDyRNGPIVIVDRYGGAQACTFCAI 985
Cdd:cd14550   81 ClsneiRLIVRDFILESTQDDYVLEVRQFQCPSWPNPCSPiHTVFELINTVQEWAQQ-RDGPIVVHDRYGGVQAATFCAL 159
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|.
gi 45553601  986 SSLAIEMEYCSTANVYQYAKLYHNKRPGVWTSSEDIRVIYN 1026
Cdd:cd14550  160 TTLHQQLEHESSVDVYQVAKLYHLMRPGVFTSKEDYQFLYK 200
PTPc smart00194
Protein tyrosine phosphatase, catalytic domain;
779-1030 1.57e-69

Protein tyrosine phosphatase, catalytic domain;


Pssm-ID: 214550 [Multi-domain]  Cd Length: 259  Bit Score: 233.71  E-value: 1.57e-69
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45553601     779 LEQQYKNIIQFQPKDIHIASAMKQVNSIKNR-GAIFPIEGSRVHLTPKPGEdGSDYINASWLHGFRRLRDFIVTQHPMAH 857
Cdd:smart00194    2 LEEEFEKLDRLKPDDESCTVAAFPENRDKNRyKDVLPYDHTRVKLKPPPGE-GSDYINASYIDGPNGPKAYIATQGPLPS 80
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45553601     858 TIKDFWQMVWDHNAQTVVLLSSLDD---INFAQFWPDEA-TPIESDHYRVKFLNKTNKSDYVSRDFVIQSIQDDYELTVK 933
Cdd:smart00194   81 TVEDFWRMVWEQKVTVIVMLTELVEkgrEKCAQYWPDEEgEPLTYGDITVTLKSVEKVDDYTIRTLEVTNTGCSETRTVT 160
                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45553601     934 MLHCPSWPEMSNPNS---IYDFIVDVHERCNDYrNGPIVIVDRYGGAQACTFCAISSLAIEMEYCSTANVYQYAKLYHNK 1010
Cdd:smart00194  161 HYHYTNWPDHGVPESpesILDLIRAVRKSQSTS-TGPIVVHCSAGVGRTGTFIAIDILLQQLEAGKEVDIFEIVKELRSQ 239
                           250       260
                    ....*....|....*....|
gi 45553601    1011 RPGVWTSSEDIRVIYNILSF 1030
Cdd:smart00194  240 RPGMVQTEEQYIFLYRAILE 259
Y_phosphatase pfam00102
Protein-tyrosine phosphatase;
804-1028 6.69e-68

Protein-tyrosine phosphatase;


Pssm-ID: 459674 [Multi-domain]  Cd Length: 234  Bit Score: 228.28  E-value: 6.69e-68
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45553601    804 NSIKNR-GAIFPIEGSRVHLTPKPGedGSDYINASWLHGFRRLRDFIVTQHPMAHTIKDFWQMVWDHNAQTVVLLSSLDD 882
Cdd:pfam00102    1 NLEKNRyKDVLPYDHTRVKLTGDPG--PSDYINASYIDGYKKPKKYIATQGPLPNTVEDFWRMVWEEKVTIIVMLTELEE 78
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45553601    883 IN---FAQFWPDEA-TPIESDHYRVKFLN-KTNKSDYVSRDFVIQSIQDDYELTVKMLHCPSWPEM---SNPNSIYDFIV 954
Cdd:pfam00102   79 KGrekCAQYWPEEEgESLEYGDFTVTLKKeKEDEKDYTVRTLEVSNGGSEETRTVKHFHYTGWPDHgvpESPNSLLDLLR 158
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 45553601    955 DVHERCNDYRNGPIVIVDRYGGAQACTFCAISSLAIEMEYCSTANVYQYAKLYHNKRPGVWTSSEDIRVIYNIL 1028
Cdd:pfam00102  159 KVRKSSLDGRSGPIVVHCSAGIGRTGTFIAIDIALQQLEAEGEVDIFQIVKELRSQRPGMVQTLEQYIFLYDAI 232
PHA02746 PHA02746
protein tyrosine phosphatase; Provisional
511-774 1.25e-47

protein tyrosine phosphatase; Provisional


Pssm-ID: 165113 [Multi-domain]  Cd Length: 323  Bit Score: 173.29  E-value: 1.25e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45553601   511 HSQHPENKRKNRYLNITAYDHSRVHLHpTPGQKKNLD-------------------YINANFIDGYQKGHAFIGTQGPLP 571
Cdd:PHA02746   45 HFLKKENLKKNRFHDIPCWDHSRVVIN-AHESLKMFDvgdsdgkkievtsednaenYIHANFVDGFKEANKFICAQGPKE 123
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45553601   572 DTFDCFWRMIWEQRVAIIVMITNlVERGRRKCDMYW--PKDGVETYGVIQVKLIEEEVMSTYTVRTLQIKHLKLkkkkqc 649
Cdd:PHA02746  124 DTSEDFFKLISEHESQVIVSLTD-IDDDDEKCFELWtkEEDSELAFGRFVAKILDIIEELSFTKTRLMITDKIS------ 196
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45553601   650 NTEKLVYQYHYTNWPDHGTPDHPLPVLNFV----------KKSSAANPAEAGPIVVHCSAGVGRTGTYIVLDAMLKQIQQ 719
Cdd:PHA02746  197 DTSREIHHFWFPDWPDNGIPTGMAEFLELInkvneeqaelIKQADNDPQTLGPIVVHCSAGIGRAGTFCAIDNALEQLEK 276
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 45553601   720 KNIVNVFGFLRHIRAQRNFLVQTEEQYIFLHDALVEAIasgetnlmaeqVEELKN 774
Cdd:PHA02746  277 EKEVCLGEIVLKIRKQRHSSVFLPEQYAFCYKALKYAI-----------IEEAKK 320
COG5599 COG5599
Protein tyrosine phosphatase [Signal transduction mechanisms];
511-749 1.56e-41

Protein tyrosine phosphatase [Signal transduction mechanisms];


Pssm-ID: 444335 [Multi-domain]  Cd Length: 282  Bit Score: 154.48  E-value: 1.56e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45553601  511 HSQHPENKRKNRYLNITAYDHSRVhlhptpgqKKNLDYINANFIDGYQKgHAFIGTQGPLPDTFDCFWRMIWEQRVAIIV 590
Cdd:COG5599   36 YLQNINGSPLNRFRDIQPYKETAL--------RANLGYLNANYIQVIGN-HRYIATQYPLEEQLEDFFQMLFDNNTPVLV 106
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45553601  591 MITNLVERGRRKCDM--YWPKDGVETYGVIQVKLIEEEVMST-YTVRTLQIKHLklkkkkQCNTEKL-VYQYHYTNWPDH 666
Cdd:COG5599  107 VLASDDEISKPKVKMpvYFRQDGEYGKYEVSSELTESIQLRDgIEARTYVLTIK------GTGQKKIeIPVLHVKNWPDH 180
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45553601  667 GTPD----HPLpvLNFVKKSSAANPAEAGPIVVHCSAGVGRTGTYIVLDAMLKQIQQKNI--VNVFGFLRHIRAQRNF-L 739
Cdd:COG5599  181 GAISaealKNL--ADLIDKKEKIKDPDKLLPVVHCRAGVGRTGTLIACLALSKSINALVQitLSVEEIVIDMRTSRNGgM 258
                        250
                 ....*....|
gi 45553601  740 VQTEEQYIFL 749
Cdd:COG5599  259 VQTSEQLDVL 268
PHA02747 PHA02747
protein tyrosine phosphatase; Provisional
774-1039 7.05e-24

protein tyrosine phosphatase; Provisional


Pssm-ID: 165114 [Multi-domain]  Cd Length: 312  Bit Score: 103.93  E-value: 7.05e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45553601   774 NCTPYLEQQYKNIIqFQPKDIHIASAMKQVNSIKNRGAIFPI-EGSRVHLTPKPGEDgSDYINASWLHGFRRLRDFIVTQ 852
Cdd:PHA02747   22 NCFGIIRDEHHQII-LKPFDGLIANFEKPENQPKNRYWDIPCwDHNRVILDSGGGST-SDYIHANWIDGFEDDKKFIATQ 99
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45553601   853 HPMAHTIKDFWQMVWDHNAQTVVLLSSLDDINFA----QFW-PDEATPIESDHYRVKFLNKTNKSDYVSRDFVIQSIQDD 927
Cdd:PHA02747  100 GPFAETCADFWKAVWQEHCSIIVMLTPTKGTNGEekcyQYWcLNEDGNIDMEDFRIETLKTSVRAKYILTLIEITDKILK 179
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45553601   928 YELTVKMLHCPSWPEMSNPNSIYDFI-----VDVHER-------CNDYRNGPIVIVDRYGGAQACTFCAISSLAIEMEYC 995
Cdd:PHA02747  180 DSRKISHFQCSEWFEDETPSDHPDFIkfikiIDINRKksgklfnPKDALLCPIVVHCSDGVGKTGIFCAVDICLNQLVKR 259
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*...
gi 45553601   996 STANVYQYAKLYHNKRPGVWTSSEDIRVI----YNILSFLPGNLNLLK 1039
Cdd:PHA02747  260 KAICLAKTAEKIREQRHAGIMNFDDYLFIqpgyEVLHYFLSKIKAIDK 307
fn3 pfam00041
Fibronectin type III domain;
172-274 6.53e-16

Fibronectin type III domain;


Pssm-ID: 394996 [Multi-domain]  Cd Length: 85  Bit Score: 73.99  E-value: 6.53e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45553601    172 SKPQNLTILDVSANSITMSWHPPKNQNGAIAGYHVFHIHDNQTGVEivkNSRNSVETLIHFELQNLRefnyvfiwglfgv 251
Cdd:pfam00041    1 SAPSNLTVTDVTSTSLTVSWTPPPDGNGPITGYEVEYRPKNSGEPW---NEITVPGTTTSVTLTGLK------------- 64
                           90       100
                   ....*....|....*....|...
gi 45553601    252 kgPYTDYRVIVKAFTTKNEGEPS 274
Cdd:pfam00041   65 --PGTEYEVRVQAVNGGGEGPPS 85
FN3 cd00063
Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein ...
171-281 1.67e-15

Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein fibronectin. Its tenth fibronectin type III repeat contains an RGD cell recognition sequence in a flexible loop between 2 strands. Approximately 2% of all animal proteins contain the FN3 repeat; including extracellular and intracellular proteins, membrane spanning cytokine receptors, growth hormone receptors, tyrosine phosphatase receptors, and adhesion molecules. FN3-like domains are also found in bacterial glycosyl hydrolases.


Pssm-ID: 238020 [Multi-domain]  Cd Length: 93  Bit Score: 72.91  E-value: 1.67e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45553601  171 PSKPQNLTILDVSANSITMSWHPPKNQNGAIAGYHVFHIHDNQTGVEIVKNSRNSVEtliHFELQNLRefnyvfiwglfg 250
Cdd:cd00063    1 PSPPTNLRVTDVTSTSVTLSWTPPEDDGGPITGYVVEYREKGSGDWKEVEVTPGSET---SYTLTGLK------------ 65
                         90       100       110
                 ....*....|....*....|....*....|.
gi 45553601  251 vkgPYTDYRVIVKAFTTKNEGEPSDQIAQRT 281
Cdd:cd00063   66 ---PGTEYEFRVRAVNGGGESPPSESVTVTT 93
FN3 smart00060
Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, ...
171-271 2.02e-09

Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, fibronectin. The tenth fibronectin type III repeat contains a RGD cell recognition sequence in a flexible loop between 2 strands. Type III modules are present in both extracellular and intracellular proteins.


Pssm-ID: 214495 [Multi-domain]  Cd Length: 83  Bit Score: 55.31  E-value: 2.02e-09
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45553601     171 PSKPQNLTILDVSANSITMSWHPPKNQNGaiAGYHV-FHIHDNQTGVEIVKNSRNSVETliHFELQNLRefnyvfiwglf 249
Cdd:smart00060    1 PSPPSNLRVTDVTSTSVTLSWEPPPDDGI--TGYIVgYRVEYREEGSEWKEVNVTPSST--SYTLTGLK----------- 65
                            90       100
                    ....*....|....*....|..
gi 45553601     250 gvkgPYTDYRVIVKAFTTKNEG 271
Cdd:smart00060   66 ----PGTEYEFRVRAVNGAGEG 83
FN3 COG3401
Fibronectin type 3 domain [General function prediction only];
111-364 4.27e-09

Fibronectin type 3 domain [General function prediction only];


Pssm-ID: 442628 [Multi-domain]  Cd Length: 603  Bit Score: 60.79  E-value: 4.27e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45553601  111 PVLGTVATSIEQQDQPPDVPATTLAFANAFPVPVAGEmgngnGNYNDATPPYAAVDDNYVPSKPQNLTILDVSANSITMS 190
Cdd:COG3401  178 AAVATTSLTVTSTTLVDGGGDIEPGTTYYYRVAATDT-----GGESAPSNEVSVTTPTTPPSAPTGLTATADTPGSVTLS 252
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45553601  191 WHPpkNQNGAIAGYHVFHIHDNQTGVEIVKNSRNSveTLIHFELQNLREFNYVfiwglfgvkgpytdyrviVKAFTT-KN 269
Cdd:COG3401  253 WDP--VTESDATGYRVYRSNSGDGPFTKVATVTTT--SYTDTGLTNGTTYYYR------------------VTAVDAaGN 310
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45553601  270 EGEPSDQIAQRTDVGGPSAPAIVNLTCHSQESITIRWRRPYEfyNTIDFYII--KTRLAGQDThrdiRINASAKelETAM 347
Cdd:COG3401  311 ESAPSNVVSVTTDLTPPAAPSGLTATAVGSSSITLSWTASSD--ADVTGYNVyrSTSGGGTYT----KIAETVT--TTSY 382
                        250
                 ....*....|....*..
gi 45553601  348 ILQNLTTNSYYEVKVAA 364
Cdd:COG3401  383 TDTGLTPGTTYYYKVTA 399
FN3 cd00063
Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein ...
286-364 8.87e-09

Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein fibronectin. Its tenth fibronectin type III repeat contains an RGD cell recognition sequence in a flexible loop between 2 strands. Approximately 2% of all animal proteins contain the FN3 repeat; including extracellular and intracellular proteins, membrane spanning cytokine receptors, growth hormone receptors, tyrosine phosphatase receptors, and adhesion molecules. FN3-like domains are also found in bacterial glycosyl hydrolases.


Pssm-ID: 238020 [Multi-domain]  Cd Length: 93  Bit Score: 54.04  E-value: 8.87e-09
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 45553601  286 PSAPAIVNLTCHSQESITIRWRRPYEFYNTIDFYIIKTRLAGQDTHRDIRINASAkelETAMILQNLTTNSYYEVKVAA 364
Cdd:cd00063    1 PSPPTNLRVTDVTSTSVTLSWTPPEDDGGPITGYVVEYREKGSGDWKEVEVTPGS---ETSYTLTGLKPGTEYEFRVRA 76
FN3 smart00060
Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, ...
286-366 1.07e-05

Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, fibronectin. The tenth fibronectin type III repeat contains a RGD cell recognition sequence in a flexible loop between 2 strands. Type III modules are present in both extracellular and intracellular proteins.


Pssm-ID: 214495 [Multi-domain]  Cd Length: 83  Bit Score: 44.91  E-value: 1.07e-05
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45553601     286 PSAPAIVNLTCHSQESITIRWRRPYEfyNTIDFYIIKTRLAGQDTHRDiRINASAKELETAMILQNLTTNSYYEVKVAAA 365
Cdd:smart00060    1 PSPPSNLRVTDVTSTSVTLSWEPPPD--DGITGYIVGYRVEYREEGSE-WKEVNVTPSSTSYTLTGLKPGTEYEFRVRAV 77

                    .
gi 45553601     366 T 366
Cdd:smart00060   78 N 78
fn3 pfam00041
Fibronectin type III domain;
287-366 2.50e-04

Fibronectin type III domain;


Pssm-ID: 394996 [Multi-domain]  Cd Length: 85  Bit Score: 40.86  E-value: 2.50e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45553601    287 SAPAIVNLTCHSQESITIRWRRPYEFYNTIDFYIIKTRLAG-QDTHRDIRINASakelETAMILQNLTTNSYYEVKVAAA 365
Cdd:pfam00041    1 SAPSNLTVTDVTSTSLTVSWTPPPDGNGPITGYEVEYRPKNsGEPWNEITVPGT----TTSVTLTGLKPGTEYEVRVQAV 76

                   .
gi 45553601    366 T 366
Cdd:pfam00041   77 N 77
 
Name Accession Description Interval E-value
R5-PTPc-1 cd14549
catalytic domain of R5 subfamily receptor-type tyrosine-protein phosphatases, repeat 1; The R5 ...
548-751 4.30e-143

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: 431.00  E-value: 4.30e-143
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45553601  548 YINANFIDGYQKGHAFIGTQGPLPDTFDCFWRMIWEQRVAIIVMITNLVERGRRKCDMYWPKDGVETYGVIQVKLIEEEV 627
Cdd:cd14549    1 YINANYVDGYNKARAYIATQGPLPSTFDDFWRMVWEQNSAIIVMITNLVERGRRKCDQYWPKEGTETYGNIQVTLLSTEV 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45553601  628 MSTYTVRTLQIKHLKLKKKKQCNTEKLVYQYHYTNWPDHGTPDHPLPVLNFVKKSSAANPAEAGPIVVHCSAGVGRTGTY 707
Cdd:cd14549   81 LATYTVRTFSLKNLKLKKVKGRSSERVVYQYHYTQWPDHGVPDYTLPVLSFVRKSSAANPPGAGPIVVHCSAGVGRTGTY 160
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....
gi 45553601  708 IVLDAMLKQIQQKNIVNVFGFLRHIRAQRNFLVQTEEQYIFLHD 751
Cdd:cd14549  161 IVIDSMLQQIQDKGTVNVFGFLKHIRTQRNYLVQTEEQYIFIHD 204
R-PTPc-G-1 cd17667
catalytic domain of receptor-type tyrosine-protein phosphatase G, repeat 1; Receptor-type ...
491-757 5.49e-125

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: 386.31  E-value: 5.49e-125
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45553601  491 FSREYEAIQnECISD-DLPCEHSQHPENKRKNRYLNITAYDHSRVHLHPTPGQ-KKNLDYINANFIDGYQKGHAFIGTQG 568
Cdd:cd17667    1 FSEDFEEVQ-RCTADmNITAEHSNHPDNKHKNRYINILAYDHSRVKLRPLPGKdSKHSDYINANYVDGYNKAKAYIATQG 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45553601  569 PLPDTFDCFWRMIWEQRVAIIVMITNLVERGRRKCDMYWPKDGVETYGVIQVKLIEEEVMSTYTVRTLQIKHLKLKKKKQ 648
Cdd:cd17667   80 PLKSTFEDFWRMIWEQNTGIIVMITNLVEKGRRKCDQYWPTENSEEYGNIIVTLKSTKIHACYTVRRFSIRNTKVKKGQK 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45553601  649 CNT-----EKLVYQYHYTNWPDHGTPDHPLPVLNFVKKSSAANPAEAGPIVVHCSAGVGRTGTYIVLDAMLKQIQQKNIV 723
Cdd:cd17667  160 GNPkgrqnERTVIQYHYTQWPDMGVPEYALPVLTFVRRSSAARTPEMGPVLVHCSAGVGRTGTYIVIDSMLQQIKDKSTV 239
                        250       260       270
                 ....*....|....*....|....*....|....
gi 45553601  724 NVFGFLRHIRAQRNFLVQTEEQYIFLHDALVEAI 757
Cdd:cd17667  240 NVLGFLKHIRTQRNYLVQTEEQYIFIHDALLEAI 273
R-PTPc-LAR-1 cd14553
catalytic domain of LAR family receptor-type tyrosine-protein phosphatases, repeat 1; The LAR ...
517-759 1.09e-117

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: 365.18  E-value: 1.09e-117
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45553601  517 NKRKNRYLNITAYDHSRVHLHPTPGQKKNlDYINANFIDGYQKGHAFIGTQGPLPDTFDCFWRMIWEQRVAIIVMITNLV 596
Cdd:cd14553    3 NKPKNRYANVIAYDHSRVILQPIEGVPGS-DYINANYCDGYRKQNAYIATQGPLPETFGDFWRMVWEQRSATIVMMTKLE 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45553601  597 ERGRRKCDMYWPKDGVETYGVIQVKLIEEEVMSTYTVRTLQIKHLKlkkkkqCNTEKLVYQYHYTNWPDHGTPDHPLPVL 676
Cdd:cd14553   82 ERSRVKCDQYWPTRGTETYGLIQVTLLDTVELATYTVRTFALHKNG------SSEKREVRQFQFTAWPDHGVPEHPTPFL 155
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45553601  677 NFVKKSSAANPAEAGPIVVHCSAGVGRTGTYIVLDAMLKQIQQKNIVNVFGFLRHIRAQRNFLVQTEEQYIFLHDALVEA 756
Cdd:cd14553  156 AFLRRVKACNPPDAGPIVVHCSAGVGRTGCFIVIDSMLERIKHEKTVDIYGHVTCLRAQRNYMVQTEDQYIFIHDALLEA 235

                 ...
gi 45553601  757 IAS 759
Cdd:cd14553  236 VTC 238
PTPc smart00194
Protein tyrosine phosphatase, catalytic domain;
490-755 5.04e-117

Protein tyrosine phosphatase, catalytic domain;


Pssm-ID: 214550 [Multi-domain]  Cd Length: 259  Bit Score: 364.29  E-value: 5.04e-117
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45553601     490 GFSREYEAIQNECIsDDLPCEHSQHPENKRKNRYLNITAYDHSRVHLHPTPGQkkNLDYINANFIDGYQKGHAFIGTQGP 569
Cdd:smart00194    1 GLEEEFEKLDRLKP-DDESCTVAAFPENRDKNRYKDVLPYDHTRVKLKPPPGE--GSDYINASYIDGPNGPKAYIATQGP 77
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45553601     570 LPDTFDCFWRMIWEQRVAIIVMITNLVERGRRKCDMYWPKDGVE--TYGVIQVKLIEEEVMSTYTVRTLQIKHLklkkkk 647
Cdd:smart00194   78 LPSTVEDFWRMVWEQKVTVIVMLTELVEKGREKCAQYWPDEEGEplTYGDITVTLKSVEKVDDYTIRTLEVTNT------ 151
                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45553601     648 QCNTEKLVYQYHYTNWPDHGTPDHPLPVLNFVKKSSAANPAEAGPIVVHCSAGVGRTGTYIVLDAMLKQIQQKNIVNVFG 727
Cdd:smart00194  152 GCSETRTVTHYHYTNWPDHGVPESPESILDLIRAVRKSQSTSTGPIVVHCSAGVGRTGTFIAIDILLQQLEAGKEVDIFE 231
                           250       260
                    ....*....|....*....|....*...
gi 45553601     728 FLRHIRAQRNFLVQTEEQYIFLHDALVE 755
Cdd:smart00194  232 IVKELRSQRPGMVQTEEQYIFLYRAILE 259
Y_phosphatase pfam00102
Protein-tyrosine phosphatase;
517-755 9.81e-106

Protein-tyrosine phosphatase;


Pssm-ID: 459674 [Multi-domain]  Cd Length: 234  Bit Score: 333.05  E-value: 9.81e-106
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45553601    517 NKRKNRYLNITAYDHSRVHLHPTPGQKknlDYINANFIDGYQKGHAFIGTQGPLPDTFDCFWRMIWEQRVAIIVMITNLV 596
Cdd:pfam00102    1 NLEKNRYKDVLPYDHTRVKLTGDPGPS---DYINASYIDGYKKPKKYIATQGPLPNTVEDFWRMVWEEKVTIIVMLTELE 77
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45553601    597 ERGRRKCDMYWP--KDGVETYGVIQVKLI-EEEVMSTYTVRTLQIkhlklkKKKQCNTEKLVYQYHYTNWPDHGTPDHPL 673
Cdd:pfam00102   78 EKGREKCAQYWPeeEGESLEYGDFTVTLKkEKEDEKDYTVRTLEV------SNGGSEETRTVKHFHYTGWPDHGVPESPN 151
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45553601    674 PVLNFVKK-SSAANPAEAGPIVVHCSAGVGRTGTYIVLDAMLKQIQQKNIVNVFGFLRHIRAQRNFLVQTEEQYIFLHDA 752
Cdd:pfam00102  152 SLLDLLRKvRKSSLDGRSGPIVVHCSAGIGRTGTFIAIDIALQQLEAEGEVDIFQIVKELRSQRPGMVQTLEQYIFLYDA 231

                   ...
gi 45553601    753 LVE 755
Cdd:pfam00102  232 ILE 234
R5-PTP-2 cd14550
PTP-like domain of R5 subfamily receptor-type tyrosine-protein phosphatases, repeat 2; The R5 ...
833-1026 1.09e-101

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: 320.42  E-value: 1.09e-101
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45553601  833 YINASWLHGFRRLRDFIVTQHPMAHTIKDFWQMVWDHNAQTVVLLSSLD-DINFAQFWPDEATPIESDHYRVKFLNKTNK 911
Cdd:cd14550    1 YINASYLQGYRRSNEFIITQHPLEHTIKDFWQMIWDHNSQTIVMLTDNElNEDEPIYWPTKEKPLECETFKVTLSGEDHS 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45553601  912 S-----DYVSRDFVIQSIQDDYELTVKMLHCPSWPEMSNP-NSIYDFIVDVHERCNDyRNGPIVIVDRYGGAQACTFCAI 985
Cdd:cd14550   81 ClsneiRLIVRDFILESTQDDYVLEVRQFQCPSWPNPCSPiHTVFELINTVQEWAQQ-RDGPIVVHDRYGGVQAATFCAL 159
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|.
gi 45553601  986 SSLAIEMEYCSTANVYQYAKLYHNKRPGVWTSSEDIRVIYN 1026
Cdd:cd14550  160 TTLHQQLEHESSVDVYQVAKLYHLMRPGVFTSKEDYQFLYK 200
R-PTPc-F-1 cd14626
catalytic domain of receptor-type tyrosine-protein phosphatase F, repeat 1; Receptor-type ...
474-757 6.48e-101

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: 321.60  E-value: 6.48e-101
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45553601  474 NEFAKHVASLHADGDIGFSREYEAIQNeciSDDLPCEHSQHPENKRKNRYLNITAYDHSRVHLHPTPGQKKNlDYINANF 553
Cdd:cd14626    1 SDLADNIERLKANDGLKFSQEYESIDP---GQQFTWENSNLEVNKPKNRYANVIAYDHSRVILTSVDGVPGS-DYINANY 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45553601  554 IDGYQKGHAFIGTQGPLPDTFDCFWRMIWEQRVAIIVMITNLVERGRRKCDMYWPKDGVETYGVIQVKLIEEEVMSTYTV 633
Cdd:cd14626   77 IDGYRKQNAYIATQGPLPETLSDFWRMVWEQRTATIVMMTRLEEKSRVKCDQYWPIRGTETYGMIQVTLLDTVELATYSV 156
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45553601  634 RTLQIKHLKLkkkkqcNTEKLVYQYHYTNWPDHGTPDHPLPVLNFVKKSSAANPAEAGPIVVHCSAGVGRTGTYIVLDAM 713
Cdd:cd14626  157 RTFALYKNGS------SEKREVRQFQFMAWPDHGVPEYPTPILAFLRRVKACNPPDAGPMVVHCSAGVGRTGCFIVIDAM 230
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....
gi 45553601  714 LKQIQQKNIVNVFGFLRHIRAQRNFLVQTEEQYIFLHDALVEAI 757
Cdd:cd14626  231 LERMKHEKTVDIYGHVTCMRSQRNYMVQTEDQYIFIHEALLEAA 274
R-PTPc-D-1 cd14624
catalytic domain of receptor-type tyrosine-protein phosphatase D, repeat 1; Receptor-type ...
471-760 4.29e-98

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: 314.36  E-value: 4.29e-98
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45553601  471 VPVNEFAKHVASLHADGDIGFSREYEAIQNeciSDDLPCEHSQHPENKRKNRYLNITAYDHSRVHLHPTPGQKKNlDYIN 550
Cdd:cd14624    4 IPILELADHIERLKANDNLKFSQEYESIDP---GQQFTWEHSNLEVNKPKNRYANVIAYDHSRVLLSAIEGIPGS-DYIN 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45553601  551 ANFIDGYQKGHAFIGTQGPLPDTFDCFWRMIWEQRVAIIVMITNLVERGRRKCDMYWPKDGVETYGVIQVKLIEEEVMST 630
Cdd:cd14624   80 ANYIDGYRKQNAYIATQGALPETFGDFWRMIWEQRSATVVMMTKLEERSRVKCDQYWPSRGTETYGLIQVTLLDTVELAT 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45553601  631 YTVRTLQIKHLKLkkkkqcNTEKLVYQYHYTNWPDHGTPDHPLPVLNFVKKSSAANPAEAGPIVVHCSAGVGRTGTYIVL 710
Cdd:cd14624  160 YCVRTFALYKNGS------SEKREVRQFQFTAWPDHGVPEHPTPFLAFLRRVKTCNPPDAGPMVVHCSAGVGRTGCFIVI 233
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|
gi 45553601  711 DAMLKQIQQKNIVNVFGFLRHIRAQRNFLVQTEEQYIFLHDALVEAIASG 760
Cdd:cd14624  234 DAMLERIKHEKTVDIYGHVTLMRAQRNYMVQTEDQYIFIHDALLEAVTCG 283
R-PTPc-Z-1 cd17668
catalytic domain of receptor-type tyrosine-protein phosphatase Z, repeat 1; Receptor-type ...
548-754 2.27e-97

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: 309.22  E-value: 2.27e-97
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45553601  548 YINANFIDGYQKGHAFIGTQGPLPDTFDCFWRMIWEQRVAIIVMITNLVERGRRKCDMYWPKDGVETYGVIQVKLIEEEV 627
Cdd:cd17668    1 YINANYVDGYNKPKAYIAAQGPLKSTAEDFWRMIWEHNVEVIVMITNLVEKGRRKCDQYWPADGSEEYGNFLVTQKSVQV 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45553601  628 MSTYTVRTLQIKHLKLKKKKQC--NTEKLVYQYHYTNWPDHGTPDHPLPVLNFVKKSSAANPAEAGPIVVHCSAGVGRTG 705
Cdd:cd17668   81 LAYYTVRNFTLRNTKIKKGSQKgrPSGRVVTQYHYTQWPDMGVPEYTLPVLTFVRKASYAKRHAVGPVVVHCSAGVGRTG 160
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*....
gi 45553601  706 TYIVLDAMLKQIQQKNIVNVFGFLRHIRAQRNFLVQTEEQYIFLHDALV 754
Cdd:cd17668  161 TYIVLDSMLQQIQHEGTVNIFGFLKHIRSQRNYLVQTEEQYVFIHDALV 209
R-PTPc-S-1 cd14625
catalytic domain of receptor-type tyrosine-protein phosphatase S, repeat 1; Receptor-type ...
471-758 5.62e-97

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: 311.26  E-value: 5.62e-97
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45553601  471 VPVNEFAKHVASLHADGDIGFSREYEAIQNeciSDDLPCEHSQHPENKRKNRYLNITAYDHSRVHLHPTPGQKKNlDYIN 550
Cdd:cd14625    4 IPISELAEHTERLKANDNLKLSQEYESIDP---GQQFTWEHSNLEVNKPKNRYANVIAYDHSRVILQPIEGIMGS-DYIN 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45553601  551 ANFIDGYQKGHAFIGTQGPLPDTFDCFWRMIWEQRVAIIVMITNLVERGRRKCDMYWPKDGVETYGVIQVKLIEEEVMST 630
Cdd:cd14625   80 ANYIDGYRKQNAYIATQGPLPETFGDFWRMVWEQRSATVVMMTKLEEKSRIKCDQYWPSRGTETYGMIQVTLLDTIELAT 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45553601  631 YTVRTLQIKHLKLkkkkqcNTEKLVYQYHYTNWPDHGTPDHPLPVLNFVKKSSAANPAEAGPIVVHCSAGVGRTGTYIVL 710
Cdd:cd14625  160 FCVRTFSLHKNGS------SEKREVRQFQFTAWPDHGVPEYPTPFLAFLRRVKTCNPPDAGPIVVHCSAGVGRTGCFIVI 233
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*...
gi 45553601  711 DAMLKQIQQKNIVNVFGFLRHIRAQRNFLVQTEEQYIFLHDALVEAIA 758
Cdd:cd14625  234 DAMLERIKHEKTVDIYGHVTLMRSQRNYMVQTEDQYSFIHDALLEAVA 281
PTPc cd00047
catalytic domain of protein tyrosine phosphatases; Protein tyrosine phosphatases (PTP, EC 3.1. ...
548-751 3.10e-90

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: 289.19  E-value: 3.10e-90
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45553601  548 YINANFIDGYQKGHAFIGTQGPLPDTFDCFWRMIWEQRVAIIVMITNLVERGRRKCDMYWPKDGVET--YGVIQVKLIEE 625
Cdd:cd00047    1 YINASYIDGYRGPKEYIATQGPLPNTVEDFWRMVWEQKVSVIVMLTNLVEKGREKCERYWPEEGGKPleYGDITVTLVSE 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45553601  626 EVMSTYTVRTLQIKHLklkkkkQCNTEKLVYQYHYTNWPDHGTPDHPLPVLNFVKKSSAANPAEAGPIVVHCSAGVGRTG 705
Cdd:cd00047   81 EELSDYTIRTLELSPK------GCSESREVTHLHYTGWPDHGVPSSPEDLLALVRRVRKEARKPNGPIVVHCSAGVGRTG 154
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*.
gi 45553601  706 TYIVLDAMLKQIQQKNIVNVFGFLRHIRAQRNFLVQTEEQYIFLHD 751
Cdd:cd00047  155 TFIAIDILLERLEAEGEVDVFEIVKALRKQRPGMVQTLEQYEFIYE 200
R3-PTPc cd14548
catalytic domain of R3 subfamily receptor-type tyrosine-protein phosphatases and similar ...
522-750 3.80e-87

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: 281.55  E-value: 3.80e-87
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45553601  522 RYLNITAYDHSRVHLHPTPGQKKNlDYINANFIDGYQKGHAFIGTQGPLPDTFDCFWRMIWEQRVAIIVMITNLVERGRR 601
Cdd:cd14548    1 RYTNILPYDHSRVKLIPINEEEGS-DYINANYIPGYNSPREFIATQGPLPGTKDDFWRMVWEQNSHTIVMLTQCMEKGRV 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45553601  602 KCDMYWPKDGVET-YGVIQVKLIEEEVMSTYTVRTLQIkhlklkkkkqCNTEK--LVYQYHYTNWPDHGTPDHPLPVLNF 678
Cdd:cd14548   80 KCDHYWPFDQDPVyYGDITVTMLSESVLPDWTIREFKL----------ERGDEvrSVRQFHFTAWPDHGVPEAPDSLLRF 149
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 45553601  679 VKKSSAANPAEAGPIVVHCSAGVGRTGTYIVLDAMLKQIQQKNIVNVFGFLRHIRAQRNFLVQTEEQYIFLH 750
Cdd:cd14548  150 VRLVRDYIKQEKGPTIVHCSAGVGRTGTFIALDRLLQQIESEDYVDIFGIVYDLRKHRPLMVQTEAQYIFLH 221
PTPc-N9 cd14543
catalytic domain of tyrosine-protein phosphatase non-receptor type 9; Tyrosine-protein ...
490-750 5.73e-85

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: 277.71  E-value: 5.73e-85
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45553601  490 GFSREYEAIQNECISDDLPCehSQHPENKRKNRYLNITAYDHSRVHLhPTPGQKKNLDYINANFIDGYQKGHAFIGTQGP 569
Cdd:cd14543    4 GIYEEYEDIRREPPAGTFLC--SLAPANQEKNRYGDVLCLDQSRVKL-PKRNGDERTDYINANFMDGYKQKNAYIATQGP 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45553601  570 LPDTFDCFWRMIWEQRVAIIVMITNLVERGRRKCDMYWP--KDGVETYGVIQVKLIEEEVMSTYTVRTLQIkhlklkKKK 647
Cdd:cd14543   81 LPKTYSDFWRMVWEQKVLVIVMTTRVVERGRVKCGQYWPleEGSSLRYGDLTVTNLSVENKEHYKKTTLEI------HNT 154
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45553601  648 QCNTEKLVYQYHYTNWPDHGTPDHPLPVLNF-----------VKKSSAANPAEAG--PIVVHCSAGVGRTGTYIVLDAML 714
Cdd:cd14543  155 ETDESRQVTHFQFTSWPDFGVPSSAAALLDFlgevrqqqalaVKAMGDRWKGHPPgpPIVVHCSAGIGRTGTFCTLDICL 234
                        250       260       270
                 ....*....|....*....|....*....|....*.
gi 45553601  715 KQIQQKNIVNVFGFLRHIRAQRNFLVQTEEQYIFLH 750
Cdd:cd14543  235 SQLEDVGTLNVMQTVRRMRTQRAFSIQTPDQYYFCY 270
R-PTPc-A-1 cd14621
catalytic domain of receptor-type tyrosine-protein phosphatase A, repeat 1; Receptor-type ...
471-764 3.98e-83

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: 273.44  E-value: 3.98e-83
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45553601  471 VPVNEFAKHVASLHADGDIGFSREYEAIQNECISDDlpCEHSQHPENKRKNRYLNITAYDHSRVHLHPTPGQKKNlDYIN 550
Cdd:cd14621    8 LPVDKLEEEINRRMADDNKLFREEFNALPACPIQAT--CEAASKEENKEKNRYVNILPYDHSRVHLTPVEGVPDS-DYIN 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45553601  551 ANFIDGYQKGHAFIGTQGPLPDTFDCFWRMIWEQRVAIIVMITNLVERGRRKCDMYWPKDGVETYGVIQVKLIEEEVMST 630
Cdd:cd14621   85 ASFINGYQEKNKFIAAQGPKEETVNDFWRMIWEQNTATIVMVTNLKERKECKCAQYWPDQGCWTYGNIRVSVEDVTVLVD 164
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45553601  631 YTVRTLQIKHLKLKKKKQcnTEKLVYQYHYTNWPDHGTPDHPLPVLNFVKKSSAANPAEAGPIVVHCSAGVGRTGTYIVL 710
Cdd:cd14621  165 YTVRKFCIQQVGDVTNKK--PQRLITQFHFTSWPDFGVPFTPIGMLKFLKKVKNCNPQYAGAIVVHCSAGVGRTGTFIVI 242
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....
gi 45553601  711 DAMLKQIQQKNIVNVFGFLRHIRAQRNFLVQTEEQYIFLHDALVEAIASGETNL 764
Cdd:cd14621  243 DAMLDMMHAERKVDVYGFVSRIRAQRCQMVQTDMQYVFIYQALLEHYLYGDTEL 296
R-PTPc-M-1 cd14633
catalytic domain of receptor-type tyrosine-protein phosphatase M, repeat 1; Receptor-type ...
475-756 4.67e-79

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: 261.52  E-value: 4.67e-79
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45553601  475 EFAKHVASLHADGDIGFSREYEAIQNeciSDDLPCEHSQHPENKRKNRYLNITAYDHSRVHLHPTPGQKkNLDYINANFI 554
Cdd:cd14633    1 DLLQHITQMKCAEGYGFKEEYESFFE---GQSAPWDSAKKDENRMKNRYGNIIAYDHSRVRLQPIEGET-SSDYINGNYI 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45553601  555 DGYQKGHAFIGTQGPLPDTFDCFWRMIWEQRVAIIVMITNLVERGRRKCDMYWPKDgVETYGVIQVKLIEEEVMSTYTVR 634
Cdd:cd14633   77 DGYHRPNHYIATQGPMQETIYDFWRMVWHENTASIIMVTNLVEVGRVKCCKYWPDD-TEIYKDIKVTLIETELLAEYVIR 155
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45553601  635 TLQIKHLKLKKKKQcnteklVYQYHYTNWPDHGTPDHPLPVLNFVKKSSAANPAEAGPIVVHCSAGVGRTGTYIVLDAML 714
Cdd:cd14633  156 TFAVEKRGVHEIRE------IRQFHFTGWPDHGVPYHATGLLGFVRQVKSKSPPNAGPLVVHCSAGAGRTGCFIVIDIML 229
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|..
gi 45553601  715 KQIQQKNIVNVFGFLRHIRAQRNFLVQTEEQYIFLHDALVEA 756
Cdd:cd14633  230 DMAEREGVVDIYNCVRELRSRRVNMVQTEEQYVFIHDAILEA 271
R-PTPc-E-1 cd14620
catalytic domain of receptor-type tyrosine-protein phosphatase E, repeat 1; Receptor-type ...
523-755 8.45e-78

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: 256.02  E-value: 8.45e-78
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45553601  523 YLNITAYDHSRVHLHPTPGQKKNlDYINANFIDGYQKGHAFIGTQGPLPDTFDCFWRMIWEQRVAIIVMITNLVERGRRK 602
Cdd:cd14620    1 YPNILPYDHSRVILSQLDGIPCS-DYINASYIDGYKEKNKFIAAQGPKQETVNDFWRMVWEQKSATIVMLTNLKERKEEK 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45553601  603 CDMYWPKDGVETYGVIQVKLIEEEVMSTYTVRTLQIKHLKLKKkkqCNTEKLVYQYHYTNWPDHGTPDHPLPVLNFVKKS 682
Cdd:cd14620   80 CYQYWPDQGCWTYGNIRVAVEDCVVLVDYTIRKFCIQPQLPDG---CKAPRLVTQLHFTSWPDFGVPFTPIGMLKFLKKV 156
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 45553601  683 SAANPAEAGPIVVHCSAGVGRTGTYIVLDAMLKQIQQKNIVNVFGFLRHIRAQRNFLVQTEEQYIFLHDALVE 755
Cdd:cd14620  157 KSVNPVHAGPIVVHCSAGVGRTGTFIVIDAMIDMMHAEQKVDVFEFVSRIRNQRPQMVQTDMQYSFIYQALLE 229
R-PTPc-T-1 cd14630
catalytic domain of receptor-type tyrosine-protein phosphatase T, repeat 1; Receptor-type ...
516-756 1.70e-77

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: 255.34  E-value: 1.70e-77
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45553601  516 ENKRKNRYLNITAYDHSRVHLHPTPGQKKNlDYINANFIDGYQKGHAFIGTQGPLPDTFDCFWRMIWEQRVAIIVMITNL 595
Cdd:cd14630    2 ENRNKNRYGNIISYDHSRVRLQLLDGDPHS-DYINANYIDGYHRPRHYIATQGPMQETVKDFWRMIWQENSASVVMVTNL 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45553601  596 VERGRRKCDMYWPkDGVETYGVIQVKLIEEEVMSTYTVRTLQIKHLKLKKKKQcnteklVYQYHYTNWPDHGTPDHPLPV 675
Cdd:cd14630   81 VEVGRVKCVRYWP-DDTEVYGDIKVTLIETEPLAEYVIRTFTVQKKGYHEIRE------IRQFHFTSWPDHGVPCYATGL 153
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45553601  676 LNFVKKSSAANPAEAGPIVVHCSAGVGRTGTYIVLDAMLKQIQQKNIVNVFGFLRHIRAQRNFLVQTEEQYIFLHDALVE 755
Cdd:cd14630  154 LGFVRQVKFLNPPDAGPIVVHCSAGAGRTGCFIAIDIMLDMAENEGVVDIFNCVRELRAQRVNMVQTEEQYVFVHDAILE 233

                 .
gi 45553601  756 A 756
Cdd:cd14630  234 A 234
R-PTPc-typeIIb-1 cd14555
catalytic domain of type IIb (or R2B) subfamily receptor-type tyrosine-protein phosphatases, ...
548-756 1.32e-74

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: 245.98  E-value: 1.32e-74
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45553601  548 YINANFIDGYQKGHAFIGTQGPLPDTFDCFWRMIWEQRVAIIVMITNLVERGRRKCDMYWPKDgVETYGVIQVKLIEEEV 627
Cdd:cd14555    1 YINANYIDGYHRPNHYIATQGPMQETVYDFWRMVWQENSASIVMVTNLVEVGRVKCSRYWPDD-TEVYGDIKVTLVETEP 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45553601  628 MSTYTVRTLQIKHLKLKKKKQcnteklVYQYHYTNWPDHGTPDHPLPVLNFVKKSSAANPAEAGPIVVHCSAGVGRTGTY 707
Cdd:cd14555   80 LAEYVVRTFALERRGYHEIRE------VRQFHFTGWPDHGVPYHATGLLGFIRRVKASNPPSAGPIVVHCSAGAGRTGCY 153
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*....
gi 45553601  708 IVLDAMLKQIQQKNIVNVFGFLRHIRAQRNFLVQTEEQYIFLHDALVEA 756
Cdd:cd14555  154 IVIDIMLDMAEREGVVDIYNCVKELRSRRVNMVQTEEQYIFIHDAILEA 202
R-PTPc-A-E-1 cd14551
catalytic domain of receptor-type tyrosine-protein phosphatase A and E, repeat 1; ...
548-750 3.48e-74

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: 244.82  E-value: 3.48e-74
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45553601  548 YINANFIDGYQKGHAFIGTQGPLPDTFDCFWRMIWEQRVAIIVMITNLVERGRRKCDMYWPKDGVETYGVIQVKLIEEEV 627
Cdd:cd14551    1 YINASYIDGYQEKNKFIAAQGPKDETVNDFWRMIWEQGSATIVMVTNLKERKEKKCSQYWPDQGCWTYGNLRVRVEDTVV 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45553601  628 MSTYTVRTLQIKHLKLKKKkqCNTEKLVYQYHYTNWPDHGTPDHPLPVLNFVKKSSAANPAEAGPIVVHCSAGVGRTGTY 707
Cdd:cd14551   81 LVDYTTRKFCIQKVNRGIG--EKRVRLVTQFHFTSWPDFGVPFTPIGMLKFLKKVKSANPPRAGPIVVHCSAGVGRTGTF 158
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|...
gi 45553601  708 IVLDAMLKQIQQKNIVNVFGFLRHIRAQRNFLVQTEEQYIFLH 750
Cdd:cd14551  159 IVIDAMLDMMHAEGKVDVFGFVSRIRQQRSQMVQTDMQYVFIY 201
R-PTPc-J cd14615
catalytic domain of receptor-type tyrosine-protein phosphatase J; Receptor-type ...
521-749 6.52e-72

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: 239.33  E-value: 6.52e-72
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45553601  521 NRYLNITAYDHSRVHL----HPTPgqkknlDYINANFIDGYQKGHAFIGTQGPLPDTFDCFWRMIWEQRVAIIVMITNLV 596
Cdd:cd14615    1 NRYNNVLPYDISRVKLsvqsHSTD------DYINANYMPGYNSKKEFIAAQGPLPNTVKDFWRMVWEKNVYAIVMLTKCV 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45553601  597 ERGRRKCDMYWPKDGVETYGVIQVKLIEEEVMSTYTVRTLQIkhlklkKKKQCNTEKLVYQYHYTNWPDHGTPDHPLPVL 676
Cdd:cd14615   75 EQGRTKCEEYWPSKQKKDYGDITVTMTSEIVLPEWTIRDFTV------KNAQTNESRTVRHFHFTSWPDHGVPETTDLLI 148
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 45553601  677 NF---VKKSSAANPAEaGPIVVHCSAGVGRTGTYIVLDAMLKQIQQKNIVNVFGFLRHIRAQRNFLVQTEEQYIFL 749
Cdd:cd14615  149 NFrhlVREYMKQNPPN-SPILVHCSAGVGRTGTFIAIDRLIYQIENENVVDVYGIVYDLRMHRPLMVQTEDQYVFL 223
R-PTPc-U-1 cd14632
catalytic domain of receptor-type tyrosine-protein phosphatase U, repeat 1; Receptor-type ...
548-756 6.62e-71

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: 235.72  E-value: 6.62e-71
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45553601  548 YINANFIDGYQKGHAFIGTQGPLPDTFDCFWRMIWEQRVAIIVMITNLVERGRRKCDMYWPKDGvETYGVIQVKLIEEEV 627
Cdd:cd14632    1 YINANYIDGYHRSNHFIATQGPKQEMVYDFWRMVWQEHCSSIVMITKLVEVGRVKCSKYWPDDS-DTYGDIKITLLKTET 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45553601  628 MSTYTVRTLQIKHLKLKKKKQcnteklVYQYHYTNWPDHGTPDHPLPVLNFVKKSSAANPAEAGPIVVHCSAGVGRTGTY 707
Cdd:cd14632   80 LAEYSVRTFALERRGYSARHE------VKQFHFTSWPEHGVPYHATGLLAFIRRVKASTPPDAGPVVVHCSAGAGRTGCY 153
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*....
gi 45553601  708 IVLDAMLKQIQQKNIVNVFGFLRHIRAQRNFLVQTEEQYIFLHDALVEA 756
Cdd:cd14632  154 IVLDVMLDMAECEGVVDIYNCVKTLCSRRINMIQTEEQYIFIHDAILEA 202
PTPc-N11_6 cd14544
catalytic domain of tyrosine-protein phosphatase non-receptor type 11 and type 6; ...
517-757 2.43e-70

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: 235.82  E-value: 2.43e-70
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45553601  517 NKRKNRYLNITAYDHSRVHLHPTPGQKKNLDYINANFI--DGYQKGH-----AFIGTQGPLPDTFDCFWRMIWEQRVAII 589
Cdd:cd14544    1 NKGKNRYKNILPFDHTRVILKDRDPNVPGSDYINANYIrnENEGPTTdenakTYIATQGCLENTVSDFWSMVWQENSRVI 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45553601  590 VMITNLVERGRRKCDMYWPKDG-VETYGVIQVKLIEEEVMSTYTVRTLQIkhlklKKKKQCNTEKLVYQYHYTNWPDHGT 668
Cdd:cd14544   81 VMTTKEVERGKNKCVRYWPDEGmQKQYGPYRVQNVSEHDTTDYTLRELQV-----SKLDQGDPIREIWHYQYLSWPDHGV 155
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45553601  669 PDHPLPVLNFV----KKSSAANpaEAGPIVVHCSAGVGRTGTYIVLDAMLKQIQQKNI---VNVFGFLRHIRAQRNFLVQ 741
Cdd:cd14544  156 PSDPGGVLNFLedvnQRQESLP--HAGPIVVHCSAGIGRTGTFIVIDMLLDQIKRKGLdcdIDIQKTIQMVRSQRSGMVQ 233
                        250
                 ....*....|....*.
gi 45553601  742 TEEQYIFLHDALVEAI 757
Cdd:cd14544  234 TEAQYKFIYVAVAQYI 249
R-PTPc-H cd14619
catalytic domain of receptor-type tyrosine-protein phosphatase H; Receptor-type ...
521-757 2.75e-70

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: 235.17  E-value: 2.75e-70
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45553601  521 NRYLNITAYDHSRVHLHPTPGQKKNlDYINANFIDGYQKGHAFIGTQGPLPDTFDCFWRMIWEQRVAIIVMITNLVERGR 600
Cdd:cd14619    1 NRFRNVLPYDWSRVPLKPIHEEPGS-DYINANYMPGYWSSQEFIATQGPLPQTVGDFWRMIWEQQSSTIVMLTNCMEAGR 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45553601  601 RKCDMYWPKDGVE-TYGVIQVKLIEEEVMSTYTVRTLQIKHLKLKKKkqcnteKLVYQYHYTNWPDHGTPDHPLPVLNF- 678
Cdd:cd14619   80 VKCEHYWPLDYTPcTYGHLRVTVVSEEVMENWTVREFLLKQVEEQKT------LSVRHFHFTAWPDHGVPSSTDTLLAFr 153
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45553601  679 -VKKSSAANPAEAGPIVVHCSAGVGRTGTYIVLDAMLKQIQQKNIVNVFGFLRHIRAQRNFLVQTEEQYIFLHDALVEAI 757
Cdd:cd14619  154 rLLRQWLDQTMSGGPTVVHCSAGVGRTGTLIALDVLLQQLQSEGLLGPFSFVQKMRENRPLMVQTESQYVFLHQCILDFL 233
PTPc smart00194
Protein tyrosine phosphatase, catalytic domain;
779-1030 1.57e-69

Protein tyrosine phosphatase, catalytic domain;


Pssm-ID: 214550 [Multi-domain]  Cd Length: 259  Bit Score: 233.71  E-value: 1.57e-69
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45553601     779 LEQQYKNIIQFQPKDIHIASAMKQVNSIKNR-GAIFPIEGSRVHLTPKPGEdGSDYINASWLHGFRRLRDFIVTQHPMAH 857
Cdd:smart00194    2 LEEEFEKLDRLKPDDESCTVAAFPENRDKNRyKDVLPYDHTRVKLKPPPGE-GSDYINASYIDGPNGPKAYIATQGPLPS 80
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45553601     858 TIKDFWQMVWDHNAQTVVLLSSLDD---INFAQFWPDEA-TPIESDHYRVKFLNKTNKSDYVSRDFVIQSIQDDYELTVK 933
Cdd:smart00194   81 TVEDFWRMVWEQKVTVIVMLTELVEkgrEKCAQYWPDEEgEPLTYGDITVTLKSVEKVDDYTIRTLEVTNTGCSETRTVT 160
                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45553601     934 MLHCPSWPEMSNPNS---IYDFIVDVHERCNDYrNGPIVIVDRYGGAQACTFCAISSLAIEMEYCSTANVYQYAKLYHNK 1010
Cdd:smart00194  161 HYHYTNWPDHGVPESpesILDLIRAVRKSQSTS-TGPIVVHCSAGVGRTGTFIAIDILLQQLEAGKEVDIFEIVKELRSQ 239
                           250       260
                    ....*....|....*....|
gi 45553601    1011 RPGVWTSSEDIRVIYNILSF 1030
Cdd:smart00194  240 RPGMVQTEEQYIFLYRAILE 259
R-PTPc-B cd14617
catalytic domain of receptor-type tyrosine-protein phosphatase B; Receptor-type ...
521-750 7.08e-69

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: 230.96  E-value: 7.08e-69
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45553601  521 NRYLNITAYDHSRVHL---HPTPGQkknlDYINANFIDGYQKGHAFIGTQGPLPDTFDCFWRMIWEQRVAIIVMITNLVE 597
Cdd:cd14617    1 NRYNNILPYDSTRVKLsnvDDDPCS----DYINASYIPGNNFRREYIATQGPLPGTKDDFWKMVWEQNVHNIVMVTQCVE 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45553601  598 RGRRKCDMYWPKDGVET-YGVIQVKLIEEEVMSTYTVRTLQIkhlklKKKKQCNTEKLVYQYHYTNWPDHGTPDHPLPVL 676
Cdd:cd14617   77 KGRVKCDHYWPADQDSLyYGDLIVQMLSESVLPEWTIREFKI-----CSEEQLDAPRLVRHFHYTVWPDHGVPETTQSLI 151
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 45553601  677 NFVK--KSSAANPAEAGPIVVHCSAGVGRTGTYIVLDAMLKQIQQKNIVNVFGFLRHIRAQRNFLVQTEEQYIFLH 750
Cdd:cd14617  152 QFVRtvRDYINRTPGSGPTVVHCSAGVGRTGTFIALDRILQQLDSKDSVDIYGAVHDLRLHRVHMVQTECQYVYLH 227
R-PTPc-K-1 cd14631
catalytic domain of receptor-type tyrosine-protein phosphatase K, repeat 1; Receptor-type ...
533-756 4.53e-68

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: 227.98  E-value: 4.53e-68
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45553601  533 RVHLHPTPGQKKNlDYINANFIDGYQKGHAFIGTQGPLPDTFDCFWRMIWEQRVAIIVMITNLVERGRRKCDMYWPKDgV 612
Cdd:cd14631    1 RVILQPVEDDPSS-DYINANYIDGYQRPSHYIATQGPVHETVYDFWRMIWQEQSACIVMVTNLVEVGRVKCYKYWPDD-T 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45553601  613 ETYGVIQVKLIEEEVMSTYTVRTLQIKHLKLkkkkqcNTEKLVYQYHYTNWPDHGTPDHPLPVLNFVKKSSAANPAEAGP 692
Cdd:cd14631   79 EVYGDFKVTCVEMEPLAEYVVRTFTLERRGY------NEIREVKQFHFTGWPDHGVPYHATGLLSFIRRVKLSNPPSAGP 152
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 45553601  693 IVVHCSAGVGRTGTYIVLDAMLKQIQQKNIVNVFGFLRHIRAQRNFLVQTEEQYIFLHDALVEA 756
Cdd:cd14631  153 IVVHCSAGAGRTGCYIVIDIMLDMAEREGVVDIYNCVKALRSRRINMVQTEEQYIFIHDAILEA 216
Y_phosphatase pfam00102
Protein-tyrosine phosphatase;
804-1028 6.69e-68

Protein-tyrosine phosphatase;


Pssm-ID: 459674 [Multi-domain]  Cd Length: 234  Bit Score: 228.28  E-value: 6.69e-68
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45553601    804 NSIKNR-GAIFPIEGSRVHLTPKPGedGSDYINASWLHGFRRLRDFIVTQHPMAHTIKDFWQMVWDHNAQTVVLLSSLDD 882
Cdd:pfam00102    1 NLEKNRyKDVLPYDHTRVKLTGDPG--PSDYINASYIDGYKKPKKYIATQGPLPNTVEDFWRMVWEEKVTIIVMLTELEE 78
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45553601    883 IN---FAQFWPDEA-TPIESDHYRVKFLN-KTNKSDYVSRDFVIQSIQDDYELTVKMLHCPSWPEM---SNPNSIYDFIV 954
Cdd:pfam00102   79 KGrekCAQYWPEEEgESLEYGDFTVTLKKeKEDEKDYTVRTLEVSNGGSEETRTVKHFHYTGWPDHgvpESPNSLLDLLR 158
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 45553601    955 DVHERCNDYRNGPIVIVDRYGGAQACTFCAISSLAIEMEYCSTANVYQYAKLYHNKRPGVWTSSEDIRVIYNIL 1028
Cdd:pfam00102  159 KVRKSSLDGRSGPIVVHCSAGIGRTGTFIAIDIALQQLEAEGEVDIFQIVKELRSQRPGMVQTLEQYIFLYDAI 232
PTPc-KIM cd14547
catalytic domain of the kinase interaction motif (KIM) family of protein-tyrosine phosphatases; ...
521-750 1.10e-67

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: 227.28  E-value: 1.10e-67
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45553601  521 NRYLNITAYDHSRVHLHPTPGQKKnLDYINANFIDGYQ-KGHAFIGTQGPLPDTFDCFWRMIWEQRVAIIVMITNLVERg 599
Cdd:cd14547    1 NRYKTILPNEHSRVCLPSVDDDPL-SSYINANYIRGYDgEEKAYIATQGPLPNTVADFWRMVWQEKTPIIVMITNLTEA- 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45553601  600 RRKCDMYWPKDGVETYGVIQVKLIEEEVMSTYTVRTLQIKhlklkkkkQCNTEKLVYQYHYTNWPDHGTPDHPLPVLNFV 679
Cdd:cd14547   79 KEKCAQYWPEEENETYGDFEVTVQSVKETDGYTVRKLTLK--------YGGEKRYLKHYWYTSWPDHKTPEAAQPLLSLV 150
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 45553601  680 KK--SSAANPAEAGPIVVHCSAGVGRTGTYIVLDAMLKQIQQKNIVNVFGFLRHIRAQRNFLVQTEEQYIFLH 750
Cdd:cd14547  151 QEveEARQTEPHRGPIVVHCSAGIGRTGCFIATSIGCQQLREEGVVDVLGIVCQLRLDRGGMVQTAEQYEFVH 223
R-PTP-LAR-2 cd14554
PTP-like domain of the LAR family receptor-type tyrosine-protein phosphatases, repeat 2; The ...
515-752 4.35e-67

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: 226.25  E-value: 4.35e-67
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45553601  515 PENKRKNRYLNITAYDHSRVHLHPTPGQKKNlDYINANFIDGYQKGHAFIGTQGPLPDTFDCFWRMIWEQRVAIIVMITN 594
Cdd:cd14554    4 PCNKFKNRLVNILPYESTRVCLQPIRGVEGS-DYINASFIDGYRQRGAYIATQGPLAETTEDFWRMLWEHNSTIIVMLTK 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45553601  595 LVERGRRKCDMYWPKDGVETYGVIQVKLIEEEVMSTYTVRTLQIKHLKLkkkkqcNTEKLVYQYHYTNWPDHGTPDHPLP 674
Cdd:cd14554   83 LREMGREKCHQYWPAERSARYQYFVVDPMAEYNMPQYILREFKVTDARD------GQSRTVRQFQFTDWPEQGVPKSGEG 156
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45553601  675 VLNFVKK--SSAANPAEAGPIVVHCSAGVGRTGTYIVLDAMLKQIQQKNIVNVFGFLRHIRAQRNFLVQTEEQYIFLHDA 752
Cdd:cd14554  157 FIDFIGQvhKTKEQFGQEGPITVHCSAGVGRTGVFITLSIVLERMRYEGVVDVFQTVKLLRTQRPAMVQTEDQYQFCYRA 236
R-PTPc-V cd14618
catalytic domain of receptor-type tyrosine-protein phosphatase V; Receptor-type ...
521-754 1.34e-66

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: 224.44  E-value: 1.34e-66
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45553601  521 NRYLNITAYDHSRVHLHPTPGQKKNlDYINANFIDGYQKGHAFIGTQGPLPDTFDCFWRMIWEQRVAIIVMITNLVERGR 600
Cdd:cd14618    1 NRYPHVLPYDHSRVRLSQLGGEPHS-DYINANFIPGYTSPQEFIATQGPLKKTIEDFWRLVWEQQVCNIIMLTVGMENGR 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45553601  601 RKCDMYWPKDGVE-TYGVIQVKLIEEEVMSTYTVRTLQIKHLKLkkkkqcNTEKLVYQYHYTNWPDHGTPDHPLPVLNFV 679
Cdd:cd14618   80 VLCDHYWPSESTPvSYGHITVHLLAQSSEDEWTRREFKLWHEDL------RKERRVKHLHYTAWPDHGIPESTSSLMAFR 153
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 45553601  680 K--KSSAANPAEAGPIVVHCSAGVGRTGTYIVLDAMLKQIQQKNIVNVFGFLRHIRAQRNFLVQTEEQYIFLHDALV 754
Cdd:cd14618  154 ElvREHVQATKGKGPTLVHCSAGVGRSGTFIALDRLLRQLKEEKVVDVFNTVYILRMHRYLMIQTLSQYIFLHSCIL 230
R-PTPc-O cd14614
catalytic domain of receptor-type tyrosine-protein phosphatase O; Receptor-type ...
506-750 3.78e-66

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: 223.61  E-value: 3.78e-66
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45553601  506 DLPCEHSQHPENKRKNRYLNITAYDHSRVHLhPTPGQKKNLDYINANFIDGYQKGHAFIGTQGPLPDTFDCFWRMIWEQR 585
Cdd:cd14614    1 DIPHFAADLPVNRCKNRYTNILPYDFSRVKL-VSMHEEEGSDYINANYIPGYNSPQEYIATQGPLPETRNDFWKMVLQQK 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45553601  586 VAIIVMITNLVERGRRKCDMYWP--KDGVeTYGVIQVKLIEEEVMSTYTVRTLQIkhlKLKKKKQCnteklVYQYHYTNW 663
Cdd:cd14614   80 SQIIVMLTQCNEKRRVKCDHYWPftEEPV-AYGDITVEMLSEEEQPDWAIREFRV---SYADEVQD-----VMHFNYTAW 150
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45553601  664 PDHGTP--DHPLPVLNFVKKSSAANPAEAGPIVVHCSAGVGRTGTYIVLDAMLKQIQQKNIVNVFGFLRHIRAQRNFLVQ 741
Cdd:cd14614  151 PDHGVPtaNAAESILQFVQMVRQQAVKSKGPMIIHCSAGVGRTGTFIALDRLLQHIRDHEFVDILGLVSEMRSYRMSMVQ 230

                 ....*....
gi 45553601  742 TEEQYIFLH 750
Cdd:cd14614  231 TEEQYIFIH 239
PTPc-N11 cd14605
catalytic domain of tyrosine-protein phosphatase non-receptor type 11; Tyrosine-protein ...
516-759 1.55e-65

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: 222.20  E-value: 1.55e-65
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45553601  516 ENKRKNRYLNITAYDHSRVHLHPTPGQKKNLDYINANFI--------DGYQKGHAFIGTQGPLPDTFDCFWRMIWEQRVA 587
Cdd:cd14605    1 ENKNKNRYKNILPFDHTRVVLHDGDPNEPVSDYINANIImpefetkcNNSKPKKSYIATQGCLQNTVNDFWRMVFQENSR 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45553601  588 IIVMITNLVERGRRKCDMYWPKD-GVETYGVIQVKLIEEEVMSTYTVRTLQIkhlklKKKKQCNTEKLVYQYHYTNWPDH 666
Cdd:cd14605   81 VIVMTTKEVERGKSKCVKYWPDEyALKEYGVMRVRNVKESAAHDYILRELKL-----SKVGQGNTERTVWQYHFRTWPDH 155
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45553601  667 GTPDHPLPVLNFVK--KSSAANPAEAGPIVVHCSAGVGRTGTYIVLDAMLKQIQQKNI---VNVFGFLRHIRAQRNFLVQ 741
Cdd:cd14605  156 GVPSDPGGVLDFLEevHHKQESIMDAGPVVVHCSAGIGRTGTFIVIDILIDIIREKGVdcdIDVPKTIQMVRSQRSGMVQ 235
                        250
                 ....*....|....*...
gi 45553601  742 TEEQYIFLHDALVEAIAS 759
Cdd:cd14605  236 TEAQYRFIYMAVQHYIET 253
PTP_fungal cd18533
fungal protein tyrosine phosphatases; This subfamily contains Saccharomyces cerevisiae ...
548-751 6.00e-64

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


Pssm-ID: 350509 [Multi-domain]  Cd Length: 212  Bit Score: 215.96  E-value: 6.00e-64
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45553601  548 YINANFID-GYQKGHAFIGTQGPLPDTFDCFWRMIWEQRVAIIVMITNLVERGRRKCDMYWPKDGVET-YGVIQVKLIEE 625
Cdd:cd18533    1 YINASYITlPGTSSKRYIATQGPLPATIGDFWKMIWQNNVGVIVMLTPLVENGREKCDQYWPSGEYEGeYGDLTVELVSE 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45553601  626 EV--MSTYTVRTLQIKHLKlkkkkqcNTEKLVYQYHYTNWPDHGTPDHPLPVLN--FVKKSSAANPAEAGPIVVHCSAGV 701
Cdd:cd18533   81 EEndDGGFIVREFELSKED-------GKVKKVYHIQYKSWPDFGVPDSPEDLLTliKLKRELNDSASLDPPIIVHCSAGV 153
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 45553601  702 GRTGTYIVLDAMLKQIQ-QKNIVN--------VFGFLRHIRAQRNFLVQTEEQYIFLHD 751
Cdd:cd18533  154 GRTGTFIALDSLLDELKrGLSDSQdledsedpVYEIVNQLRKQRMSMVQTLRQYIFLYD 212
R-PTPc-C-1 cd14557
catalytic domain of receptor-type tyrosine-protein phosphatase C, repeat 1; Receptor-type ...
548-750 6.53e-63

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: 212.76  E-value: 6.53e-63
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45553601  548 YINANFIDGYQKGHAFIGTQGPLPDTFDCFWRMIWEQRVAIIVMITNLVERGRRKCDMYWP--KDGVETYGVIQVKLIEE 625
Cdd:cd14557    1 YINASYIDGFKEPRKYIAAQGPKDETVDDFWRMIWEQKSTVIVMVTRCEEGNRNKCAQYWPsmEEGSRAFGDVVVKINEE 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45553601  626 EVMSTYTVRTLQIKHLKLKKkkqcnTEKLVYQYHYTNWPDHGTPDHPLPVLNFVKKSSAANPAEAGPIVVHCSAGVGRTG 705
Cdd:cd14557   81 KICPDYIIRKLNINNKKEKG-----SGREVTHIQFTSWPDHGVPEDPHLLLKLRRRVNAFNNFFSGPIVVHCSAGVGRTG 155
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*
gi 45553601  706 TYIVLDAMLKQIQQKNIVNVFGFLRHIRAQRNFLVQTEEQYIFLH 750
Cdd:cd14557  156 TYIGIDAMLEGLEAEGRVDVYGYVVKLRRQRCLMVQVEAQYILIH 200
PTPc-N22_18_12 cd14542
catalytic domain of tyrosine-protein phosphatase non-receptor type 22, type 18 and type 12; ...
548-750 6.17e-62

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: 209.97  E-value: 6.17e-62
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45553601  548 YINANFIDGYQKGHAFIGTQGPLPDTFDCFWRMIWEQRVAIIVMITNLVERGRRKCDMYWPKDGVE--TYGVIQVKLIEE 625
Cdd:cd14542    1 YINANFIKGVSGSKAYIATQGPLPNTVLDFWRMIWEYNVQVIVMACREFEMGKKKCERYWPEEGEEqlQFGPFKISLEKE 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45553601  626 EVMST-YTVRTLQIKHLklkkkkqcNTEKLVYQYHYTNWPDHGTPDHPLPVLNFVKKSSAANPAEAGPIVVHCSAGVGRT 704
Cdd:cd14542   81 KRVGPdFLIRTLKVTFQ--------KESRTVYQFHYTAWPDHGVPSSVDPILDLVRLVRDYQGSEDVPICVHCSAGCGRT 152
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|
gi 45553601  705 GTYIVLD----AMLKQIQQKNIvNVFGFLRHIRAQRNFLVQTEEQYIFLH 750
Cdd:cd14542  153 GTICAIDyvwnLLKTGKIPEEF-SLFDLVREMRKQRPAMVQTKEQYELVY 201
PTPc-N1 cd14608
catalytic domain of tyrosine-protein phosphatase non-receptor type 1; Tyrosine-protein ...
495-755 8.24e-62

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: 212.58  E-value: 8.24e-62
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45553601  495 YEAIQNEciSDDLPCEHSQHPENKRKNRYLNITAYDHSRVHLHptpgQKKNlDYINANFIDGYQKGHAFIGTQGPLPDTF 574
Cdd:cd14608    5 YQDIRHE--ASDFPCRVAKLPKNKNRNRYRDVSPFDHSRIKLH----QEDN-DYINASLIKMEEAQRSYILTQGPLPNTC 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45553601  575 DCFWRMIWEQRVAIIVMITNLVERGRRKCDMYWP----KDGVETYGVIQVKLIEEEVMSTYTVRTLQIKHLKLKKKKQcn 650
Cdd:cd14608   78 GHFWEMVWEQKSRGVVMLNRVMEKGSLKCAQYWPqkeeKEMIFEDTNLKLTLISEDIKSYYTVRQLELENLTTQETRE-- 155
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45553601  651 teklVYQYHYTNWPDHGTPDHPLPVLNF---VKKSSAANPaEAGPIVVHCSAGVGRTGTYIVLDAMLKQIQQK---NIVN 724
Cdd:cd14608  156 ----ILHFHYTTWPDFGVPESPASFLNFlfkVRESGSLSP-EHGPVVVHCSAGIGRSGTFCLADTCLLLMDKRkdpSSVD 230
                        250       260       270
                 ....*....|....*....|....*....|.
gi 45553601  725 VFGFLRHIRAQRNFLVQTEEQYIFLHDALVE 755
Cdd:cd14608  231 IKKVLLEMRKFRMGLIQTADQLRFSYLAVIE 261
R-PTPc-Q cd14616
catalytic domain of receptor-type tyrosine-protein phosphatase Q; Receptor-type ...
521-750 4.27e-61

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: 208.61  E-value: 4.27e-61
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45553601  521 NRYLNITAYDHSRVHLHPTPGQKKNlDYINANFIDGYQKGHAFIGTQGPLPDTFDCFWRMIWEQRVAIIVMITNLVERGR 600
Cdd:cd14616    1 NRFPNIKPYNNNRVKLIADAGVPGS-DYINASYISGYLCPNEFIATQGPLPGTVGDFWRMVWETRAKTIVMLTQCFEKGR 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45553601  601 RKCDMYWPKDG--VETYGVIQVKLIEEEVMSTYTVRTLQIKHLKLKKkkqcntekLVYQYHYTNWPDHGTPDHPLPVLNF 678
Cdd:cd14616   80 IRCHQYWPEDNkpVTVFGDIVITKLMEDVQIDWTIRDLKIERHGDYM--------MVRQCNFTSWPEHGVPESSAPLIHF 151
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 45553601  679 VKKSSAANPAEAGPIVVHCSAGVGRTGTYIVLDAMLKQIQQKNIVNVFGFLRHIRAQRNFLVQTEEQYIFLH 750
Cdd:cd14616  152 VKLVRASRAHDNTPMIVHCSAGVGRTGVFIALDHLTQHINDHDFVDIYGLVAELRSERMCMVQNLAQYIFLH 223
PTPc-N18 cd14603
catalytic domain of tyrosine-protein phosphatase non-receptor type 18; Tyrosine-protein ...
492-755 1.91e-59

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: 205.44  E-value: 1.91e-59
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45553601  492 SREYEAIQNECIS----DDLPCEHSQHPENKRKNRYLNITAYDHSRVHLHPTPGQKKNlDYINANFIDGYQKGHAFIGTQ 567
Cdd:cd14603    1 AGEFSEIRACSAAfkadYVCSTVAGGRKENVKKNRYKDILPYDQTRVILSLLQEEGHS-DYINANFIKGVDGSRAYIATQ 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45553601  568 GPLPDTFDCFWRMIWEQRVAIIVMITNLVERGRRKCDMYWP-KDGVETYGVIQVKLIEEEVMSTYTV-RTLQIKHlklkk 645
Cdd:cd14603   80 GPLSHTVLDFWRMIWQYGVKVILMACREIEMGKKKCERYWAqEQEPLQTGPFTITLVKEKRLNEEVIlRTLKVTF----- 154
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45553601  646 kkqCNTEKLVYQYHYTNWPDHGTPDHPLPVLNFVKKSSAANPAEAGPIVVHCSAGVGRTGTYIVLD----AMLKQIQQKN 721
Cdd:cd14603  155 ---QKESRSVSHFQYMAWPDHGIPDSPDCMLAMIELARRLQGSGPEPLCVHCSAGCGRTGVICTVDyvrqLLLTQRIPPD 231
                        250       260       270
                 ....*....|....*....|....*....|....
gi 45553601  722 IvNVFGFLRHIRAQRNFLVQTEEQYIFLHDALVE 755
Cdd:cd14603  232 F-SIFDVVLEMRKQRPAAVQTEEQYEFLYHTVAQ 264
PTPc-N1_2 cd14545
catalytic domain of tyrosine-protein phosphatase non-receptor type 1 and type 2; ...
518-748 5.09e-59

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: 202.62  E-value: 5.09e-59
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45553601  518 KRKNRYLNITAYDHSRVHLHptpgQKKNlDYINANFIDGYQKGHAFIGTQGPLPDTFDCFWRMIWEQRVAIIVMITNLVE 597
Cdd:cd14545    1 LNRYRDRDPYDHDRSRVKLK----QGDN-DYINASLVEVEEAKRSYILTQGPLPNTSGHFWQMVWEQNSKAVIMLNKLME 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45553601  598 RGRRKCDMYWPKDGVETYGV----IQVKLIEEEVMSTYTVRTLQIKHLKLkkkkqcNTEKLVYQYHYTNWPDHGTPDHPL 673
Cdd:cd14545   76 KGQIKCAQYWPQGEGNAMIFedtgLKVTLLSEEDKSYYTVRTLELENLKT------QETREVLHFHYTTWPDFGVPESPA 149
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45553601  674 PVLNF---VKKSSAANPaEAGPIVVHCSAGVGRTGTYIVLDAMLKQIQQKNI--VNVFGFLRHIRAQRNFLVQTEEQYIF 748
Cdd:cd14545  150 AFLNFlqkVRESGSLSS-DVGPPVVHCSAGIGRSGTFCLVDTCLVLIEKGNPssVDVKKVLLEMRKYRMGLIQTPDQLRF 228
PTPc-N6 cd14606
catalytic domain of tyrosine-protein phosphatase non-receptor type 6; Tyrosine-protein ...
513-759 6.72e-59

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: 203.96  E-value: 6.72e-59
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45553601  513 QHPENKRKNRYLNITAYDHSRVHLHPTPGQKKNLDYINANFIDGYQKG-----HAFIGTQGPLPDTFDCFWRMIWEQRVA 587
Cdd:cd14606   14 QRPENKSKNRYKNILPFDHSRVILQGRDSNIPGSDYINANYVKNQLLGpdenaKTYIASQGCLEATVNDFWQMAWQENSR 93
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45553601  588 IIVMITNLVERGRRKCDMYWPKDGVE-TYGVIQVKLIEEEVMSTYTVRTLQIKHLKlkkkkqcNTEKL--VYQYHYTNWP 664
Cdd:cd14606   94 VIVMTTREVEKGRNKCVPYWPEVGMQrAYGPYSVTNCGEHDTTEYKLRTLQVSPLD-------NGELIreIWHYQYLSWP 166
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45553601  665 DHGTPDHPLPVLNFVKKSSAANPA--EAGPIVVHCSAGVGRTGTYIVLDAMLKQIQQKNI---VNVFGFLRHIRAQRNFL 739
Cdd:cd14606  167 DHGVPSEPGGVLSFLDQINQRQESlpHAGPIIVHCSAGIGRTGTIIVIDMLMENISTKGLdcdIDIQKTIQMVRAQRSGM 246
                        250       260
                 ....*....|....*....|
gi 45553601  740 VQTEEQYIFLHDALVEAIAS 759
Cdd:cd14606  247 VQTEAQYKFIYVAIAQFIET 266
PTPc-N12 cd14604
catalytic domain of tyrosine-protein phosphatase non-receptor type 12; Tyrosine-protein ...
508-755 7.55e-59

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: 204.78  E-value: 7.55e-59
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45553601  508 PCEHSQHPENKRKNRYLNITAYDHSRVHLH-PTPGQKKnlDYINANFIDGYQKGHAFIGTQGPLPDTFDCFWRMIWEQRV 586
Cdd:cd14604   48 PTATGEKEENVKKNRYKDILPFDHSRVKLTlKTSSQDS--DYINANFIKGVYGPKAYIATQGPLANTVIDFWRMIWEYNV 125
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45553601  587 AIIVMITNLVERGRRKCDMYWPKDGVE--TYGVIQVKLIEEEVMSTYTVRTLQIKHLklkkkkqcNTEKLVYQYHYTNWP 664
Cdd:cd14604  126 AIIVMACREFEMGRKKCERYWPLYGEEpmTFGPFRISCEAEQARTDYFIRTLLLEFQ--------NETRRLYQFHYVNWP 197
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45553601  665 DHGTPDHPLPVLNFVKKSSAANPAEAGPIVVHCSAGVGRTGTYIVLD---AMLKQIQQKNIVNVFGFLRHIRAQRNFLVQ 741
Cdd:cd14604  198 DHDVPSSFDSILDMISLMRKYQEHEDVPICIHCSAGCGRTGAICAIDytwNLLKAGKIPEEFNVFNLIQEMRTQRHSAVQ 277
                        250
                 ....*....|....
gi 45553601  742 TEEQYIFLHDALVE 755
Cdd:cd14604  278 TKEQYELVHRAIAQ 291
R-PTP-D-2 cd14628
PTP-like domain of receptor-type tyrosine-protein phosphatase D, repeat 2; Receptor-type ...
503-759 1.82e-58

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: 203.42  E-value: 1.82e-58
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45553601  503 ISDDLPCehsqhpeNKRKNRYLNITAYDHSRVHLHPTPGQKKNlDYINANFIDGYQKGHAFIGTQGPLPDTFDCFWRMIW 582
Cdd:cd14628   45 ISANLPC-------NKFKNRLVNIMPYESTRVCLQPIRGVEGS-DYINASFIDGYRQQKAYIATQGPLAETTEDFWRMLW 116
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45553601  583 EQRVAIIVMITNLVERGRRKCDMYWPKDGVETYGVIQVKLIEEEVMSTYTVRTLQIKHLKLkkkkqcNTEKLVYQYHYTN 662
Cdd:cd14628  117 EHNSTIVVMLTKLREMGREKCHQYWPAERSARYQYFVVDPMAEYNMPQYILREFKVTDARD------GQSRTVRQFQFTD 190
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45553601  663 WPDHGTPDHPLPVLNFVKK--SSAANPAEAGPIVVHCSAGVGRTGTYIVLDAMLKQIQQKNIVNVFGFLRHIRAQRNFLV 740
Cdd:cd14628  191 WPEQGVPKSGEGFIDFIGQvhKTKEQFGQDGPISVHCSAGVGRTGVFITLSIVLERMRYEGVVDIFQTVKMLRTQRPAMV 270
                        250
                 ....*....|....*....
gi 45553601  741 QTEEQYIFLHDALVEAIAS 759
Cdd:cd14628  271 QTEDQYQFCYRAALEYLGS 289
PTPc-N2 cd14607
catalytic domain of tyrosine-protein phosphatase non-receptor type 2; Tyrosine-protein ...
495-753 2.03e-58

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: 202.12  E-value: 2.03e-58
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45553601  495 YEAIQNEciSDDLPCEHSQHPENKRKNRYLNITAYDHSRVHLhptpgQKKNLDYINANFIDGYQKGHAFIGTQGPLPDTF 574
Cdd:cd14607    4 YLEIRNE--SHDYPHRVAKYPENRNRNRYRDVSPYDHSRVKL-----QNTENDYINASLVVIEEAQRSYILTQGPLPNTC 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45553601  575 DCFWRMIWEQRVAIIVMITNLVERGRRKCDMYWPKDGVETYGV----IQVKLIEEEVMSTYTVRTLQIkhlklkKKKQCN 650
Cdd:cd14607   77 CHFWLMVWQQKTKAVVMLNRIVEKDSVKCAQYWPTDEEEVLSFketgFSVKLLSEDVKSYYTVHLLQL------ENINSG 150
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45553601  651 TEKLVYQYHYTNWPDHGTPDHPLPVLNF---VKKSSAANPaEAGPIVVHCSAGVGRTGTYIVLDAMLKQIQQKN--IVNV 725
Cdd:cd14607  151 ETRTISHFHYTTWPDFGVPESPASFLNFlfkVRESGSLSP-EHGPAVVHCSAGIGRSGTFSLVDTCLVLMEKKDpdSVDI 229
                        250       260
                 ....*....|....*....|....*...
gi 45553601  726 FGFLRHIRAQRNFLVQTEEQYIFLHDAL 753
Cdd:cd14607  230 KQVLLDMRKYRMGLIQTPDQLRFSYMAV 257
R-PTP-S-2 cd14627
PTP-like domain of receptor-type tyrosine-protein phosphatase S, repeat 2; Receptor-type ...
503-759 2.78e-58

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: 203.04  E-value: 2.78e-58
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45553601  503 ISDDLPCehsqhpeNKRKNRYLNITAYDHSRVHLHPTPGQKKNlDYINANFIDGYQKGHAFIGTQGPLPDTFDCFWRMIW 582
Cdd:cd14627   46 ISANLPC-------NKFKNRLVNIMPYETTRVCLQPIRGVEGS-DYINASFIDGYRQQKAYIATQGPLAETTEDFWRMLW 117
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45553601  583 EQRVAIIVMITNLVERGRRKCDMYWPKDGVETYGVIQVKLIEEEVMSTYTVRTLQIKHLKLkkkkqcNTEKLVYQYHYTN 662
Cdd:cd14627  118 ENNSTIVVMLTKLREMGREKCHQYWPAERSARYQYFVVDPMAEYNMPQYILREFKVTDARD------GQSRTVRQFQFTD 191
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45553601  663 WPDHGTPDHPLPVLNFVKK--SSAANPAEAGPIVVHCSAGVGRTGTYIVLDAMLKQIQQKNIVNVFGFLRHIRAQRNFLV 740
Cdd:cd14627  192 WPEQGVPKSGEGFIDFIGQvhKTKEQFGQDGPISVHCSAGVGRTGVFITLSIVLERMRYEGVVDIFQTVKMLRTQRPAMV 271
                        250
                 ....*....|....*....
gi 45553601  741 QTEEQYIFLHDALVEAIAS 759
Cdd:cd14627  272 QTEDEYQFCYQAALEYLGS 290
PTPc-N22 cd14602
catalytic domain of tyrosine-protein phosphatase non-receptor type 22; Tyrosine-protein ...
520-755 5.80e-57

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: 196.98  E-value: 5.80e-57
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45553601  520 KNRYLNITAYDHSRVHLHPTPGQKKNlDYINANFIDGYQKGHAFIGTQGPLPDTFDCFWRMIWEQRVAIIVMITNLVERG 599
Cdd:cd14602    1 KNRYKDILPYDHSRVELSLITSDEDS-DYINANFIKGVYGPRAYIATQGPLSTTLLDFWRMIWEYSVLIIVMACMEFEMG 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45553601  600 RRKCDMYWPKDGVET--YGVIQVKLIEEEVMSTYTVRTLQIkhlklkkkkQCNTE-KLVYQYHYTNWPDHGTPDHPLPVL 676
Cdd:cd14602   80 KKKCERYWAEPGEMQleFGPFSVTCEAEKRKSDYIIRTLKV---------KFNSEtRTIYQFHYKNWPDHDVPSSIDPIL 150
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45553601  677 NFVKKSSAANPAEAGPIVVHCSAGVGRTGTYIVLDAMLKQIQQKNI---VNVFGFLRHIRAQRNFLVQTEEQYIFLHDAL 753
Cdd:cd14602  151 ELIWDVRCYQEDDSVPICIHCSAGCGRTGVICAIDYTWMLLKDGIIpenFSVFSLIQEMRTQRPSLVQTKEQYELVYNAV 230

                 ..
gi 45553601  754 VE 755
Cdd:cd14602  231 IE 232
R-PTPc-A-2 cd14623
catalytic domain of receptor-type tyrosine-protein phosphatase A, repeat 2; Receptor-type ...
522-755 1.16e-56

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: 196.03  E-value: 1.16e-56
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45553601  522 RYLNITAYDHSRVHLhPTPGQKKNLDYINANFIDGYQKGHAFIGTQGPLPDTFDCFWRMIWEQRVAIIVMITNLVERGRR 601
Cdd:cd14623    1 RVLQIIPYEFNRVII-PVKRGEENTDYVNASFIDGYRQKDSYIASQGPLQHTIEDFWRMIWEWKSCSIVMLTELEERGQE 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45553601  602 KCDMYWPKDGVETYGVIQVKLIEEEVMSTYTVRTLQIKHLKLkkkkqcNTEKLVYQYHYTNWPDHGTPDHPLPVLNFVKK 681
Cdd:cd14623   80 KCAQYWPSDGSVSYGDITIELKKEEECESYTVRDLLVTNTRE------NKSRQIRQFHFHGWPEVGIPSDGKGMINIIAA 153
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 45553601  682 SSAANPAEAG-PIVVHCSAGVGRTGTYIVLDAMLKQIQQKNIVNVFGFLRHIRAQRNFLVQTEEQYIFLHDALVE 755
Cdd:cd14623  154 VQKQQQQSGNhPITVHCSAGAGRTGTFCALSTVLERVKAEGILDVFQTVKSLRLQRPHMVQTLEQYEFCYKVVQE 228
R-PTP-F-2 cd14629
PTP-like domain of receptor-type tyrosine-protein phosphatase F, repeat 2; Receptor-type ...
503-759 1.94e-56

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: 197.64  E-value: 1.94e-56
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45553601  503 ISDDLPCehsqhpeNKRKNRYLNITAYDHSRVHLHPTPGQKKNlDYINANFIDGYQKGHAFIGTQGPLPDTFDCFWRMIW 582
Cdd:cd14629   46 ISANLPC-------NKFKNRLVNIMPYELTRVCLQPIRGVEGS-DYINASFIDGYRQQKAYIATQGPLAETTEDFWRMLW 117
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45553601  583 EQRVAIIVMITNLVERGRRKCDMYWPKDGVETYGVIQVKLIEEEVMSTYTVRTLQIKHLKLkkkkqcNTEKLVYQYHYTN 662
Cdd:cd14629  118 EHNSTIVVMLTKLREMGREKCHQYWPAERSARYQYFVVDPMAEYNMPQYILREFKVTDARD------GQSRTIRQFQFTD 191
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45553601  663 WPDHGTPDHPLPVLNFVKK--SSAANPAEAGPIVVHCSAGVGRTGTYIVLDAMLKQIQQKNIVNVFGFLRHIRAQRNFLV 740
Cdd:cd14629  192 WPEQGVPKTGEGFIDFIGQvhKTKEQFGQDGPITVHCSAGVGRTGVFITLSIVLERMRYEGVVDMFQTVKTLRTQRPAMV 271
                        250
                 ....*....|....*....
gi 45553601  741 QTEEQYIFLHDALVEAIAS 759
Cdd:cd14629  272 QTEDQYQLCYRAALEYLGS 290
R-PTPc-A-E-2 cd14552
catalytic domain of receptor-type tyrosine-protein phosphatase A and E, repeat 2; ...
548-754 4.81e-56

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: 193.25  E-value: 4.81e-56
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45553601  548 YINANFIDGYQKGHAFIGTQGPLPDTFDCFWRMIWEQRVAIIVMITNLVERGRRKCDMYWPKDGVETYGVIQVKLIEEEV 627
Cdd:cd14552    1 YINASFIDGYRQKDAYIATQGPLDHTVEDFWRMIWEWKSCSIVMLTEIKERSQNKCAQYWPEDGSVSSGDITVELKDQTD 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45553601  628 MSTYTVRTLQIkhlklkKKKQCNTEKLVYQYHYTNWPDHGTPDHPLPVLNFV-----KKSSAANpaeaGPIVVHCSAGVG 702
Cdd:cd14552   81 YEDYTLRDFLV------TKGKGGSTRTVRQFHFHGWPEVGIPDNGKGMIDLIaavqkQQQQSGN----HPITVHCSAGAG 150
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|..
gi 45553601  703 RTGTYIVLDAMLKQIQQKNIVNVFGFLRHIRAQRNFLVQTEEQYIFLHDALV 754
Cdd:cd14552  151 RTGTFCALSTVLERVKAEGVLDVFQVVKSLRLQRPHMVQTLEQYEFCYKVVQ 202
PTPc-N13 cd14597
catalytic domain of tyrosine-protein phosphatase non-receptor type 13; Tyrosine-protein ...
516-748 6.67e-56

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: 193.89  E-value: 6.67e-56
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45553601  516 ENKRKNRYLNITAYDHSRVHLhptpGQKKnlDYINANFIDGYQKG--HAFIGTQGPLPDTFDCFWRMIWEQRVAIIVMIT 593
Cdd:cd14597    2 ENRKKNRYKNILPYDTTRVPL----GDEG--GYINASFIKMPVGDeeFVYIACQGPLPTTVADFWQMVWEQKSTVIAMMT 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45553601  594 NLVERGRRKCDMYWPKDGVETYGV---IQVKLIEEEVMSTYTVRTLQIKHLklkkkkQCNTEKLVYQYHYTNWPDHGTPD 670
Cdd:cd14597   76 QEVEGGKIKCQRYWPEILGKTTMVdnrLQLTLVRMQQLKNFVIRVLELEDI------QTREVRHITHLNFTAWPDHDTPS 149
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 45553601  671 HPLPVLNFVkkSSAANPAEAGPIVVHCSAGVGRTGTYIVLDAMLKQIQQKNIVNVFGFLRHIRAQRNFLVQTEEQYIF 748
Cdd:cd14597  150 QPEQLLTFI--SYMRHIHKSGPIITHCSAGIGRSGTLICIDVVLGLISKDLDFDISDIVRTMRLQRHGMVQTEDQYIF 225
PTPc-N7 cd14612
catalytic domain of tyrosine-protein phosphatase non-receptor type 7; Tyrosine-protein ...
515-753 8.43e-56

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: 194.28  E-value: 8.43e-56
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45553601  515 PENKRKNRYLNITAYDHSRVHLHPTPGQKKNLDYINANFIDGYQ-KGHAFIGTQGPLPDTFDCFWRMIWEQRVAIIVMIT 593
Cdd:cd14612   13 PGHASKDRYKTILPNPQSRVCLRRAGSQEEEGSYINANYIRGYDgKEKAYIATQGPMLNTVSDFWEMVWQEECPIIVMIT 92
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45553601  594 NLVERgRRKCDMYWP-KDGveTYGVIQVKLIEEEVMSTYTVRTLQIkhlklkkkkQCNTE-KLVYQYHYTNWPDHGTPDH 671
Cdd:cd14612   93 KLKEK-KEKCVHYWPeKEG--TYGRFEIRVQDMKECDGYTIRDLTI---------QLEEEsRSVKHYWFSSWPDHQTPES 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45553601  672 PLPVLNFVKK-----SSAANPaeaGPIVVHCSAGVGRTGTYIVLDAMLKQIQQKNIVNVFGFLRHIRAQRNFLVQTEEQY 746
Cdd:cd14612  161 AGPLLRLVAEveesrQTAASP---GPIVVHCSAGIGRTGCFIATSIGCQQLKDTGKVDILGIVCQLRLDRGGMIQTSEQY 237

                 ....*..
gi 45553601  747 IFLHDAL 753
Cdd:cd14612  238 QFLHHTL 244
PTPc-N20_13 cd14538
catalytic domain of tyrosine-protein phosphatase non-receptor type 20 and type 13; ...
548-757 1.93e-55

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: 191.43  E-value: 1.93e-55
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45553601  548 YINANFID---GYQKGHaFIGTQGPLPDTFDCFWRMIWEQRVAIIVMITNLVERGRRKCDMYWPKDGVET---YGVIQVK 621
Cdd:cd14538    1 YINASHIRipvGGDTYH-YIACQGPLPNTTGDFWQMVWEQKSEVIAMVTQDVEGGKVKCHRYWPDSLNKPlicGGRLEVS 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45553601  622 LIEEEVMSTYTVRTLQIKHLklkkkkQCNTEKLVYQYHYTNWPDHGTPDHPLPVLNFVkkSSAANPAEAGPIVVHCSAGV 701
Cdd:cd14538   80 LEKYQSLQDFVIRRISLRDK------ETGEVHHITHLNFTTWPDHGTPQSADPLLRFI--RYMRRIHNSGPIVVHCSAGI 151
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 45553601  702 GRTGTYIVLDAMLKQIQQKNIVNVFGFLRHIRAQRNFLVQTEEQYIFLHDALVEAI 757
Cdd:cd14538  152 GRTGVLITIDVALGLIERDLPFDIQDIVKDLREQRQGMIQTKDQYIFCYKACLEVL 207
R-PTP-N cd14609
PTP-like domain of receptor-type tyrosine-protein phosphatase N; Receptor-type ...
491-757 2.73e-54

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: 191.02  E-value: 2.73e-54
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45553601  491 FSREYEAIqneCISDDLP--CEHSQHPENKRKNRYLNITAYDHSRVHLHPTPGQKKNlDYINAN-FIDGYQKGHAFIGTQ 567
Cdd:cd14609   17 LAKEWQAL---CAYQAEPntCSTAQGEANVKKNRNPDFVPYDHARIKLKAESNPSRS-DYINASpIIEHDPRMPAYIATQ 92
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45553601  568 GPLPDTFDCFWRMIWEQRVAIIVMITNLVERGRRKCDMYWPKDGVETYGVIQVKLIEEEV-MSTYTVRTLQIkhlklkKK 646
Cdd:cd14609   93 GPLSHTIADFWQMVWENGCTVIVMLTPLVEDGVKQCDRYWPDEGSSLYHIYEVNLVSEHIwCEDFLVRSFYL------KN 166
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45553601  647 KQCNTEKLVYQYHYTNWPDHGTPDHPLPVLNFVKKSSAANPAEAGPIVVHCSAGVGRTGTYIVLDAMLKQIQQ--KNIvN 724
Cdd:cd14609  167 VQTQETRTLTQFHFLSWPAEGIPSSTRPLLDFRRKVNKCYRGRSCPIIVHCSDGAGRTGTYILIDMVLNRMAKgvKEI-D 245
                        250       260       270
                 ....*....|....*....|....*....|...
gi 45553601  725 VFGFLRHIRAQRNFLVQTEEQYIFLHDALVEAI 757
Cdd:cd14609  246 IAATLEHVRDQRPGMVRTKDQFEFALTAVAEEV 278
R-PTP-N2 cd14610
PTP-like domain of receptor-type tyrosine-protein phosphatase N2; Receptor-type ...
493-757 5.14e-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: 190.27  E-value: 5.14e-54
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45553601  493 REYEAIqneCISDDLP--CEHSQHPENKRKNRYLNITAYDHSRVHLHPTPGQKKNlDYINANFI-DGYQKGHAFIGTQGP 569
Cdd:cd14610   21 KEWEAL---CAYQAEPnaTNVAQREENVQKNRSLAVLPYDHSRIILKAENSHSHS-DYINASPImDHDPRNPAYIATQGP 96
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45553601  570 LPDTFDCFWRMIWEQRVAIIVMITNLVERGRRKCDMYWPKDGVETYGVIQVKLIEEEV-MSTYTVRTLQIkhlklkKKKQ 648
Cdd:cd14610   97 LPATVADFWQMVWESGCVVIVMLTPLAENGVKQCYHYWPDEGSNLYHIYEVNLVSEHIwCEDFLVRSFYL------KNLQ 170
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45553601  649 CNTEKLVYQYHYTNWPDHGTPDHPLPVLNFVKKSSAANPAEAGPIVVHCSAGVGRTGTYIVLDAML-KQIQQKNIVNVFG 727
Cdd:cd14610  171 TNETRTVTQFHFLSWNDQGVPASTRSLLDFRRKVNKCYRGRSCPIIVHCSDGAGRSGTYILIDMVLnKMAKGAKEIDIAA 250
                        250       260       270
                 ....*....|....*....|....*....|
gi 45553601  728 FLRHIRAQRNFLVQTEEQYIFLHDALVEAI 757
Cdd:cd14610  251 TLEHLRDQRPGMVQTKEQFEFALTAVAEEV 280
R-PTPc-R cd14611
catalytic domain of receptor-type tyrosine-protein phosphatase R; Receptor-type ...
520-750 7.12e-53

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: 185.12  E-value: 7.12e-53
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45553601  520 KNRYLNITAYDHSRVHLHPTPGQKKNLDYINANFIDGYQ-KGHAFIGTQGPLPDTFDCFWRMIWEQRVAIIVMITNLVER 598
Cdd:cd14611    2 KNRYKTILPNPHSRVCLKPKNSNDSLSTYINANYIRGYGgKEKAFIATQGPMINTVNDFWQMVWQEDSPVIVMITKLKEK 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45553601  599 GRrKCDMYWP-KDGVetYGVIQVKLIEEEVMSTYTVRTLQIKhlklkkkkQCNTEKLVYQYHYTNWPDHGTPDHPLPVLN 677
Cdd:cd14611   82 NE-KCVLYWPeKRGI--YGKVEVLVNSVKECDNYTIRNLTLK--------QGSQSRSVKHYWYTSWPDHKTPDSAQPLLQ 150
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 45553601  678 F---VKKSSAANPAEaGPIVVHCSAGVGRTGTYIVLDAMLKQIQQKNIVNVFGFLRHIRAQRNFLVQTEEQYIFLH 750
Cdd:cd14611  151 LmldVEEDRLASPGR-GPVVVHCSAGIGRTGCFIATTIGCQQLKEEGVVDVLSIVCQLRVDRGGMVQTSEQYEFVH 225
PTPc-N5 cd14613
catalytic domain of tyrosine-protein phosphatase non-receptor type 5; Tyrosine-protein ...
519-753 1.76e-52

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: 185.07  E-value: 1.76e-52
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45553601  519 RKNRYLNITAYDHSRVHLhPTPGQKKNLD-YINANFIDGY-QKGHAFIGTQGPLPDTFDCFWRMIWEQRVAIIVMITNLV 596
Cdd:cd14613   27 RKNRYKTILPNPHSRVCL-TSPDQDDPLSsYINANYIRGYgGEEKVYIATQGPTVNTVGDFWRMVWQERSPIIVMITNIE 105
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45553601  597 ERGRrKCDMYWPKDGVeTYGVIQVKLIEEEVMSTYTVRTLQIKHLklkkkkqcNTEKLVYQYHYTNWPDHGTPDHPLPVL 676
Cdd:cd14613  106 EMNE-KCTEYWPEEQV-TYEGIEITVKQVIHADDYRLRLITLKSG--------GEERGLKHYWYTSWPDQKTPDNAPPLL 175
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45553601  677 NFVKKSSAAN---PAEAGPIVVHCSAGVGRTGTYIVLDAMLKQIQQKNIVNVFGFLRHIRAQRNFLVQTEEQYIFLHDAL 753
Cdd:cd14613  176 QLVQEVEEARqqaEPNCGPVIVHCSAGIGRTGCFIATSICCKQLRNEGVVDILRTTCQLRLDRGGMIQTCEQYQFVHHVL 255
R-PTP-C-2 cd14558
PTP-like domain of receptor-type tyrosine-protein phosphatase C, repeat 2; Receptor-type ...
548-751 9.07e-52

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: 181.05  E-value: 9.07e-52
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45553601  548 YINANFIDGYQKGHAFIGTQGPLPDTFDCFWRMIWEQRVAIIVMITNLVERGRRKCDMYWPkDGVETYGVIQVKLIEEEV 627
Cdd:cd14558    1 YINASFIDGYWGPKSLIATQGPLPDTIADFWQMIFQKKVKVIVMLTELKEGDQEQCAQYWG-DEKKTYGDIEVELKDTEK 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45553601  628 MSTYTVRTLQIKHLKLKKKKQcnteklVYQYHYTNWPDHGTPDHPLPVLNF---VKKSSAANPAEAG---PIVVHCSAGV 701
Cdd:cd14558   80 SPTYTVRVFEITHLKRKDSRT------VYQYQYHKWKGEELPEKPKDLVDMiksIKQKLPYKNSKHGrsvPIVVHCSDGS 153
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|
gi 45553601  702 GRTGTYIVLDAMLKQIQQKNIVNVFGFLRHIRAQRNFLVQTEEQYIFLHD 751
Cdd:cd14558  154 SRTGIFCALWNLLESAETEKVVDVFQVVKALRKQRPGMVSTLEQYQFLYD 203
PTPc-N3_4 cd14541
catalytic domain of tyrosine-protein phosphatase non-receptor type 21 and type 14; ...
547-756 1.04e-51

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: 180.99  E-value: 1.04e-51
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45553601  547 DYINANFIDGYQKGHA----FIGTQGPLPDTFDCFWRMIWEQRVAIIVMITNLVERGRRKCDMYWPK-DGVETYGVIQVK 621
Cdd:cd14541    1 DYINANYVNMEIPGSGivnrYIAAQGPLPNTCADFWQMVWEQKSTLIVMLTTLVERGRVKCHQYWPDlGETMQFGNLQIT 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45553601  622 LIEEEVMSTYTVRTLQIkhlklkKKKQCNTEKLVYQYHYTNWPDHGTPDHPLPVLNFVKKSSAANPAEAGPIVVHCSAGV 701
Cdd:cd14541   81 CVSEEVTPSFAFREFIL------TNTNTGEERHITQMQYLAWPDHGVPDDSSDFLDFVKRVRQNRVGMVEPTVVHCSAGI 154
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 45553601  702 GRTGTYIVLDAMLKQIQQKNIVNVFGFLRHIRAQRNFLVQTEEQYIFLHDALVEA 756
Cdd:cd14541  155 GRTGVLITMETAMCLIEANEPVYPLDIVRTMRDQRAMLIQTPSQYRFVCEAILRV 209
PTPc-N3 cd14600
catalytic domain of tyrosine-protein phosphatase non-receptor type 3; Tyrosine-protein ...
515-754 2.80e-51

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: 182.36  E-value: 2.80e-51
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45553601  515 PENKRKNRYLNITAYDHSRVHLhptpgqKKNLDYINANFID----GYQKGHAFIGTQGPLPDTFDCFWRMIWEQRVAIIV 590
Cdd:cd14600   38 PQNMDKNRYKDVLPYDATRVVL------QGNEDYINASYVNmeipSANIVNKYIATQGPLPHTCAQFWQVVWEQKLSLIV 111
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45553601  591 MITNLVERGRRKCDMYWPK-DGVETYGVIQVKLIEEEVMSTYTVRTLQIkhlklkKKKQCNTEKLVYQYHYTNWPDHGTP 669
Cdd:cd14600  112 MLTTLTERGRTKCHQYWPDpPDVMEYGGFRVQCHSEDCTIAYVFREMLL------TNTQTGEERTVTHLQYVAWPDHGVP 185
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45553601  670 DHPLPVLNFVkKSSAANPAEAGPIVVHCSAGVGRTGTYIVLDAMLKQIQQKNIVNVFGFLRHIRAQRNFLVQTEEQYIFL 749
Cdd:cd14600  186 DDSSDFLEFV-NYVRSKRVENEPVLVHCSAGIGRTGVLVTMETAMCLTERNQPVYPLDIVRKMRDQRAMMVQTSSQYKFV 264

                 ....*
gi 45553601  750 HDALV 754
Cdd:cd14600  265 CEAIL 269
R-PTP-Z-2 cd17669
catalytic domain of receptor-type tyrosine-protein phosphatase Z, repeat 2; Receptor-type ...
833-1028 7.61e-51

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: 178.26  E-value: 7.61e-51
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45553601  833 YINASWLHGFRRLRDFIVTQHPMAHTIKDFWQMVWDHNAQTVVLLSslDDINFAQ----FWPDEATPIESDHYRVKFLNK 908
Cdd:cd17669    1 YINASYIMGYYQSNEFIITQHPLLHTIKDFWRMIWDHNAQLIVMLP--DGQNMAEdefvYWPNKDEPINCETFKVTLIAE 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45553601  909 -----TNKSDYVSRDFVIQSIQDDYELTVKMLHCPSWPEMSNPNS-IYDFIVDVHERCNDyRNGPIVIVDRYGGAQACTF 982
Cdd:cd17669   79 ehkclSNEEKLIIQDFILEATQDDYVLEVRHFQCPKWPNPDSPISkTFELISIIKEEAAN-RDGPMIVHDEHGGVTAGTF 157
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*.
gi 45553601  983 CAISSLAIEMEYCSTANVYQYAKLYHNKRPGVWTSSEDIRVIYNIL 1028
Cdd:cd17669  158 CALTTLMHQLEKENSVDVYQVAKMINLMRPGVFTDIEQYQFLYKAI 203
R-PTPc-E-2 cd14622
catalytic domain of receptor-type tyrosine-protein phosphatase E, repeat 2; Receptor-type ...
547-750 2.09e-50

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: 177.12  E-value: 2.09e-50
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45553601  547 DYINANFIDGYQKGHAFIGTQGPLPDTFDCFWRMIWEQRVAIIVMITNLVERGRRKCDMYWPKDGVETYGVIQVKLIEEE 626
Cdd:cd14622    1 DYINASFIDGYRQKDYFIATQGPLAHTVEDFWRMVWEWKCHTIVMLTELQEREQEKCVQYWPSEGSVTHGEITIEIKNDT 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45553601  627 VMSTYTVRTLQIkhlklkKKKQCNTEKLVYQYHYTNWPDHGTPDHPLPVLNFVKKSSAANPAEAG-PIVVHCSAGVGRTG 705
Cdd:cd14622   81 LLETISIRDFLV------TYNQEKQTRLVRQFHFHGWPEIGIPAEGKGMIDLIAAVQKQQQQTGNhPIVVHCSAGAGRTG 154
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*
gi 45553601  706 TYIVLDAMLKQIQQKNIVNVFGFLRHIRAQRNFLVQTEEQYIFLH 750
Cdd:cd14622  155 TFIALSNILERVKAEGLLDVFQTVKSLRLQRPHMVQTLEQYEFCY 199
R-PTP-N-N2 cd14546
PTP-like domain of receptor-type tyrosine-protein phosphatase-like N and N2; Receptor-type ...
548-757 1.37e-49

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: 174.94  E-value: 1.37e-49
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45553601  548 YINANFI-DGYQKGHAFIGTQGPLPDTFDCFWRMIWEQRVAIIVMITNLVERGRRKCDMYWPKDGVETYGVIQVKLIEEE 626
Cdd:cd14546    1 YINASTIyDHDPRNPAYIATQGPLPHTIADFWQMIWEQGCVVIVMLTRLQENGVKQCARYWPEEGSEVYHIYEVHLVSEH 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45553601  627 VMST-YTVRTLQIkhlklkKKKQCNTEKLVYQYHYTNWPDHGTPDHPLPVLNFVKKSSAANPAEAGPIVVHCSAGVGRTG 705
Cdd:cd14546   81 IWCDdYLVRSFYL------KNLQTSETRTVTQFHFLSWPDEGIPASAKPLLEFRRKVNKSYRGRSCPIVVHCSDGAGRTG 154
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....
gi 45553601  706 TYIVLDAMLKQIQQ--KNIvNVFGFLRHIRAQRNFLVQTEEQYIFLHDALVEAI 757
Cdd:cd14546  155 TYILIDMVLNRMAKgaKEI-DIAATLEHLRDQRPGMVKTKDQFEFVLTAVAEEV 207
PTPc-N14 cd14599
catalytic domain of tyrosine-protein phosphatase non-receptor type 14; Tyrosine-protein ...
515-755 1.83e-49

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: 177.50  E-value: 1.83e-49
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45553601  515 PENKRKNRYLNITAYDHSRVHLHPTpgQKKNLDYINANFIDGYQKGHA--FIGTQGPLPDTFDCFWRMIWEQRVAIIVMI 592
Cdd:cd14599   36 PENAERNRIREVVPYEENRVELVPT--KENNTGYINASHIKVTVGGEEwhYIATQGPLPHTCHDFWQMVWEQGVNVIAMV 113
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45553601  593 TNLVERGRRKCDMYWPKDGV----ETYGVIQVKLIEEEVMSTYTVRTLQIKHLKLkkkkqcNTEKLVYQYHYTNWPDHGT 668
Cdd:cd14599  114 TAEEEGGRSKSHRYWPKLGSkhssATYGKFKVTTKFRTDSGCYATTGLKVKHLLS------GQERTVWHLQYTDWPDHGC 187
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45553601  669 PDHPLPVLNFVKK--------------SSAANPaeagPIVVHCSAGVGRTGTYIVLDAMLKQIQQKNIVNVFGFLRHIRA 734
Cdd:cd14599  188 PEEVQGFLSYLEEiqsvrrhtnsmldsTKNCNP----PIVVHCSAGVGRTGVVILTELMIGCLEHNEKVEVPVMLRHLRE 263
                        250       260
                 ....*....|....*....|.
gi 45553601  735 QRNFLVQTEEQYIFLHDALVE 755
Cdd:cd14599  264 QRMFMIQTIAQYKFVYQVLIQ 284
PTPc-N21_14 cd14540
catalytic domain of tyrosine-protein phosphatase non-receptor type 21 and type 14; ...
548-755 1.19e-48

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: 172.64  E-value: 1.19e-48
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45553601  548 YINANFIDGYQKGHA--FIGTQGPLPDTFDCFWRMIWEQRVAIIVMITNLVERGRRKCDMYWPKDGVE----TYGVIQVK 621
Cdd:cd14540    1 YINASHITATVGGKQrfYIAAQGPLQNTVGDFWQMVWEQGVYLVVMVTAEEEGGREKCFRYWPTLGGEhdalTFGEYKVS 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45553601  622 LIEEEVMSTYTVRTLQIkhlklkKKKQCNTEKLVYQYHYTNWPDHGTPDHPLPVLNFVKKSSA----ANPAEAG-----P 692
Cdd:cd14540   81 TKFSVSSGCYTTTGLRV------KHTLSGQSRTVWHLQYTDWPDHGCPEDVSGFLDFLEEINSvrrhTNQDVAGhnrnpP 154
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 45553601  693 IVVHCSAGVGRTGTYIVLDAMLKQIQQKNIVNVFGFLRHIRAQRNFLVQTEEQYIFLHDALVE 755
Cdd:cd14540  155 TLVHCSAGVGRTGVVILADLMLYCLDHNEELDIPRVLALLRHQRMLLVQTLAQYKFVYNVLIQ 217
R-PTP-G-2 cd17670
PTP-like domain of receptor-type tyrosine-protein phosphatase G, repeat 2; Receptor-type ...
833-1028 1.33e-48

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: 171.79  E-value: 1.33e-48
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45553601  833 YINASWLHGFRRLRDFIVTQHPMAHTIKDFWQMVWDHNAQTVVLLSslDDINFAQ----FWPDEATPIESDHYRVKFLNK 908
Cdd:cd17670    1 YINASYIMGYYRSNEFIITQHPLPHTTKDFWRMIWDHNAQIIVMLP--DNQGLAEdefvYWPSREESMNCEAFTVTLISK 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45553601  909 -----TNKSDYVSRDFVIQSIQDDYELTVKMLHCPSWPEMSNP-NSIYDFIVDVHERCNDyRNGPIVIVDRYGGAQACTF 982
Cdd:cd17670   79 drlclSNEEQIIIHDFILEATQDDYVLEVRHFQCPKWPNPDAPiSSTFELINVIKEEALT-RDGPTIVHDEFGAVSAGTL 157
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*.
gi 45553601  983 CAISSLAIEMEYCSTANVYQYAKLYHNKRPGVWTSSEDIRVIYNIL 1028
Cdd:cd17670  158 CALTTLSQQLENENAVDVYQVAKMINLMRPGVFTDIEQYQFLYKAM 203
PHA02746 PHA02746
protein tyrosine phosphatase; Provisional
511-774 1.25e-47

protein tyrosine phosphatase; Provisional


Pssm-ID: 165113 [Multi-domain]  Cd Length: 323  Bit Score: 173.29  E-value: 1.25e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45553601   511 HSQHPENKRKNRYLNITAYDHSRVHLHpTPGQKKNLD-------------------YINANFIDGYQKGHAFIGTQGPLP 571
Cdd:PHA02746   45 HFLKKENLKKNRFHDIPCWDHSRVVIN-AHESLKMFDvgdsdgkkievtsednaenYIHANFVDGFKEANKFICAQGPKE 123
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45553601   572 DTFDCFWRMIWEQRVAIIVMITNlVERGRRKCDMYW--PKDGVETYGVIQVKLIEEEVMSTYTVRTLQIKHLKLkkkkqc 649
Cdd:PHA02746  124 DTSEDFFKLISEHESQVIVSLTD-IDDDDEKCFELWtkEEDSELAFGRFVAKILDIIEELSFTKTRLMITDKIS------ 196
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45553601   650 NTEKLVYQYHYTNWPDHGTPDHPLPVLNFV----------KKSSAANPAEAGPIVVHCSAGVGRTGTYIVLDAMLKQIQQ 719
Cdd:PHA02746  197 DTSREIHHFWFPDWPDNGIPTGMAEFLELInkvneeqaelIKQADNDPQTLGPIVVHCSAGIGRAGTFCAIDNALEQLEK 276
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 45553601   720 KNIVNVFGFLRHIRAQRNFLVQTEEQYIFLHDALVEAIasgetnlmaeqVEELKN 774
Cdd:PHA02746  277 EKEVCLGEIVLKIRKQRHSSVFLPEQYAFCYKALKYAI-----------IEEAKK 320
PTPc-N20 cd14596
catalytic domain of tyrosine-protein phosphatase non-receptor type 20; Tyrosine-protein ...
548-757 7.26e-47

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: 166.85  E-value: 7.26e-47
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45553601  548 YINANFID---GYQKgHAFIGTQGPLPDTFDCFWRMIWEQRVAIIVMITNLVERGRRKCDMYWPKDGVETYGV--IQVKL 622
Cdd:cd14596    1 YINASYITmpvGEEE-LFYIATQGPLPSTIDDFWQMVWENRSDVIAMMTREVERGKVKCHRYWPETLQEPMELenYQLRL 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45553601  623 IEEEVMSTYTVRTLQIkhlklkKKKQCNTEKLVYQYHYTNWPDHGTPDHPLPVLNFVKKSSAANpaEAGPIVVHCSAGVG 702
Cdd:cd14596   80 ENYQALQYFIIRIIKL------VEKETGENRLIKHLQFTTWPDHGTPQSSDQLVKFICYMRKVH--NTGPIVVHCSAGIG 151
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 45553601  703 RTGTYIVLDAMLKQIQQKNIVNVFGFLRHIRAQRNFLVQTEEQYIFLHDALVEAI 757
Cdd:cd14596  152 RAGVLICVDVLLSLIEKDLSFNIKDIVREMRQQRYGMIQTKDQYLFCYKVVLEVL 206
PTPc-N4 cd14601
catalytic domain of tyrosine-protein phosphatase non-receptor type 4; Tyrosine-protein ...
547-755 7.85e-46

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: 164.35  E-value: 7.85e-46
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45553601  547 DYINANFID----GYQKGHAFIGTQGPLPDTFDCFWRMIWEQRVAIIVMITNLVERGRRKCDMYWPK-DGVETYGVIQVK 621
Cdd:cd14601    1 DYINANYINmeipSSSIINRYIACQGPLPNTCSDFWQMTWEQGSSMVVMLTTQVERGRVKCHQYWPEpSGSSSYGGFQVT 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45553601  622 LIEEEVMSTYTVRTLQIkhlklkKKKQCNTEKLVYQYHYTNWPDHGTPDHPLPVLNFVKKSSAANPAEAGPIVVHCSAGV 701
Cdd:cd14601   81 CHSEEGNPAYVFREMTL------TNLEKNESRPLTQIQYIAWPDHGVPDDSSDFLDFVCLVRNKRAGKDEPVVVHCSAGI 154
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....
gi 45553601  702 GRTGTYIVLDAMLKQIQQKNIVNVFGFLRHIRAQRNFLVQTEEQYIFLHDALVE 755
Cdd:cd14601  155 GRTGVLITMETAMCLIECNQPVYPLDIVRTMRDQRAMMIQTPSQYRFVCEAILK 208
PTP-N23 cd14539
PTP-like domain of tyrosine-protein phosphatase non-receptor type 23; Tyrosine-protein ...
548-751 6.15e-45

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: 161.40  E-value: 6.15e-45
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45553601  548 YINANFIDGYQKGHA-FIGTQGPLPDTFDCFWRMIWEQRVAIIVMITNLVERGRRKCDMYWPKD-GVE-TYGVIQVKLIE 624
Cdd:cd14539    1 YINASLIEDLTPYCPrFIATQAPLPGTAADFWLMVYEQQVSVIVMLVSEQENEKQKVHRYWPTErGQAlVYGAITVSLQS 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45553601  625 EEVMSTYTVRTLQIkhlklkkkkQCNTEKL---VYQYHYTNWPDHGTPDHPLPVLNFVKKSSA---ANPAEAGPIVVHCS 698
Cdd:cd14539   81 VRTTPTHVERIISI---------QHKDTRLsrsVVHLQFTTWPELGLPDSPNPLLRFIEEVHShylQQRSLQTPIVVHCS 151
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....
gi 45553601  699 AGVGRTGTYIVLDAMLKQIQQKN-IVNVFGFLRHIRAQRNFLVQTEEQYIFLHD 751
Cdd:cd14539  152 SGVGRTGAFCLLYAAVQEIEAGNgIPDLPQLVRKMRQQRKYMLQEKEHLKFCYE 205
PHA02747 PHA02747
protein tyrosine phosphatase; Provisional
510-750 6.24e-45

protein tyrosine phosphatase; Provisional


Pssm-ID: 165114 [Multi-domain]  Cd Length: 312  Bit Score: 165.17  E-value: 6.24e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45553601   510 EHSQHPENKRKNRYLNITAYDHSRVHLHPTPGQKKNldYINANFIDGYQKGHAFIGTQGPLPDTFDCFWRMIWEQRVAII 589
Cdd:PHA02747   44 ANFEKPENQPKNRYWDIPCWDHNRVILDSGGGSTSD--YIHANWIDGFEDDKKFIATQGPFAETCADFWKAVWQEHCSII 121
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45553601   590 VMIT-NLVERGRRKCDMYW--PKDGVETYGVIQVKLIEEEVMSTYTVRTLQIKHLKLkkkkqcNTEKLVYQYHYTNWPDH 666
Cdd:PHA02747  122 VMLTpTKGTNGEEKCYQYWclNEDGNIDMEDFRIETLKTSVRAKYILTLIEITDKIL------KDSRKISHFQCSEWFED 195
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45553601   667 GTP-DHP-----LPVLNFVKKSSAA--NPAEA--GPIVVHCSAGVGRTGTYIVLDAMLKQIQQKNIVNVFGFLRHIRAQR 736
Cdd:PHA02747  196 ETPsDHPdfikfIKIIDINRKKSGKlfNPKDAllCPIVVHCSDGVGKTGIFCAVDICLNQLVKRKAICLAKTAEKIREQR 275
                         250
                  ....*....|....
gi 45553601   737 NFLVQTEEQYIFLH 750
Cdd:PHA02747  276 HAGIMNFDDYLFIQ 289
R-PTPc-typeIIb-2 cd14556
PTP domain of type IIb (or R2B) subfamily receptor-type tyrosine-protein phosphatases, repeat ...
548-751 2.66e-44

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: 159.49  E-value: 2.66e-44
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45553601  548 YINANFIDGYQKGHAFIGTQGPLPDTFDCFWRMIWEQRVAIIVMItNLVERGRRKCDMYWPKDGVETYGVIQVKLIEEEV 627
Cdd:cd14556    1 YINAALLDSYKQPAAFIVTQHPLPNTVTDFWRLVYDYGCTSIVML-NQLDPKDQSCPQYWPDEGSGTYGPIQVEFVSTTI 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45553601  628 MSTYTVRTLQIkhlklkkkkqCNTEK------LVYQYHYTNWPDHG----TPDHPLPVLNFVKKSSAAnpAEAGPIVVHC 697
Cdd:cd14556   80 DEDVISRIFRL----------QNTTRpqegyrMVQQFQFLGWPRDRdtppSKRALLKLLSEVEKWQEQ--SGEGPIVVHC 147
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....
gi 45553601  698 SAGVGRTGTYIVLDAMLKQIQQKNIVNVFGFLRHIRAQRNFLVQTEEQYIFLHD 751
Cdd:cd14556  148 LNGVGRSGVFCAISSVCERIKVENVVDVFQAVKTLRNHRPNMVETEEQYKFCYD 201
PHA02738 PHA02738
hypothetical protein; Provisional
492-753 1.23e-43

hypothetical protein; Provisional


Pssm-ID: 222923 [Multi-domain]  Cd Length: 320  Bit Score: 161.63  E-value: 1.23e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45553601   492 SREYEAIqnecISDDLPCEHSQHPENKRKNRYLNITAYDHSRVHLhptPGQKKNLDYINANFIDGYQKGHAFIGTQGPLP 571
Cdd:PHA02738   28 TREHQKV----ISEKVDGTFNAEKKNRKLNRYLDAVCFDHSRVIL---PAERNRGDYINANYVDGFEYKKKFICGQAPTR 100
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45553601   572 DTFDCFWRMIWEQRVAIIVMITNLVERGRRKCDMYWP--KDGVETYGVIQVKLIEEEVMSTYTVRTLQIKHLKLKKkkqc 649
Cdd:PHA02738  101 QTCYDFYRMLWMEHVQIIVMLCKKKENGREKCFPYWSdvEQGSIRFGKFKITTTQVETHPHYVKSTLLLTDGTSAT---- 176
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45553601   650 nteKLVYQYHYTNWPDHGTPDHPLPVLNFV------KKSSAANPAEAG-------PIVVHCSAGVGRTGTYIVLDAMLKQ 716
Cdd:PHA02738  177 ---QTVTHFNFTAWPDHDVPKNTSEFLNFVlevrqcQKELAQESLQIGhnrlqppPIVVHCNAGLGRTPCYCVVDISISR 253
                         250       260       270
                  ....*....|....*....|....*....|....*..
gi 45553601   717 IQQKNIVNVFGFLRHIRAQRNFLVQTEEQYIFLHDAL 753
Cdd:PHA02738  254 FDACATVSIPSIVSSIRNQRYYSLFIPFQYFFCYRAV 290
PHA02742 PHA02742
protein tyrosine phosphatase; Provisional
474-748 1.44e-43

protein tyrosine phosphatase; Provisional


Pssm-ID: 165109 [Multi-domain]  Cd Length: 303  Bit Score: 160.94  E-value: 1.44e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45553601   474 NEFAKHVASLHADGDIG--FSREYEAIQNECISddLPCEHSQHPENKRKNRYLNITAYDHSRVHLhptPGQKKNLDYINA 551
Cdd:PHA02742    9 NSFAKNCEQLIEESNLAeiLKEEHEHIMQEIVA--FSCNESLELKNMKKCRYPDAPCFDRNRVIL---KIEDGGDDFINA 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45553601   552 NFIDGYQKGHAFIGTQGPLPDTFDCFWRMIWEQRVAIIVMITNLVERGRRKCDMYW--PKDGVETYGVIQVKLIEEEVMS 629
Cdd:PHA02742   84 SYVDGHNAKGRFICTQAPLEETALDFWQAIFQDQVRVIVMITKIMEDGKEACYPYWmpHERGKATHGEFKIKTKKIKSFR 163
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45553601   630 TYTVRTLQIkhlklkkkKQCNTEKL--VYQYHYTNWPDHGTPDHPLPVLNFV-----------KKSSAANPAEAGPIVVH 696
Cdd:PHA02742  164 NYAVTNLCL--------TDTNTGASldIKHFAYEDWPHGGLPRDPNKFLDFVlavreadlkadVDIKGENIVKEPPILVH 235
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|..
gi 45553601   697 CSAGVGRTGTYIVLDAMLKQIQQKNIVNVFGFLRHIRAQRNFLVQTEEQYIF 748
Cdd:PHA02742  236 CSAGLDRAGAFCAIDICISKYNERAIIPLLSIVRDLRKQRHNCLSLPQQYIF 287
PTPc cd00047
catalytic domain of protein tyrosine phosphatases; Protein tyrosine phosphatases (PTP, EC 3.1. ...
833-1025 1.74e-43

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: 157.06  E-value: 1.74e-43
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45553601  833 YINASWLHGFRRLRDFIVTQHPMAHTIKDFWQMVWDHNAQTVVLLSSLDDIN---FAQFWPDE-ATPIESDHYRVKFLNK 908
Cdd:cd00047    1 YINASYIDGYRGPKEYIATQGPLPNTVEDFWRMVWEQKVSVIVMLTNLVEKGrekCERYWPEEgGKPLEYGDITVTLVSE 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45553601  909 TNKSDYVSRDFVIQSIQDDYELTVKMLHCPSWPEMSNPNSIYDFI--VDVHERCNDYRNGPIVIVDRYGGAQACTFCAIS 986
Cdd:cd00047   81 EELSDYTIRTLELSPKGCSESREVTHLHYTGWPDHGVPSSPEDLLalVRRVRKEARKPNGPIVVHCSAGVGRTGTFIAID 160
                        170       180       190
                 ....*....|....*....|....*....|....*....
gi 45553601  987 SLAIEMEYCSTANVYQYAKLYHNKRPGVWTSSEDIRVIY 1025
Cdd:cd00047  161 ILLERLEAEGEVDVFEIVKALRKQRPGMVQTLEQYEFIY 199
PTPc_plant_PTP1 cd17658
protein tyrosine phosphatase 1 from Arabidopsis thaliana and similar plant PTPs; Arabidopsis ...
548-748 2.37e-43

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


Pssm-ID: 350496 [Multi-domain]  Cd Length: 206  Bit Score: 156.86  E-value: 2.37e-43
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45553601  548 YINANFI--DGYQKGHAFIGTQGPLPDTFDCFWRMIWEQRVAIIVMITNLVERGRR-KCDMYWPKD--GVETYGVIQVKL 622
Cdd:cd17658    1 YINASLVetPASESLPKFIATQGPLPHTFEDFWEMVIQQRCPVIIMLTRLVDNYSTaKCADYFPAEenESREFGRISVTN 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45553601  623 IEEEVMST-YTVRTLQIKHLKLKKKKQCnteklVYQYHYTNWPDHGTPDHPLPVLNFVKKSSAAnPAEAGPIVVHCSAGV 701
Cdd:cd17658   81 KKLKHSQHsITLRVLEVQYIESEEPPLS-----VLHIQYPEWPDHGVPKDTRSVRELLKRLYGI-PPSAGPIVVHCSAGI 154
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*....
gi 45553601  702 GRTGTYIVLDAMLKQIQQKNI--VNVFGFLRHIRAQRNFLVQTEEQYIF 748
Cdd:cd17658  155 GRTGAYCTIHNTIRRILEGDMsaVDLSKTVRKFRSQRIGMVQTQDQYIF 203
R-PTP-LAR-2 cd14554
PTP-like domain of the LAR family receptor-type tyrosine-protein phosphatases, repeat 2; The ...
803-1025 5.09e-42

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: 154.22  E-value: 5.09e-42
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45553601  803 VNSIKNRGA-IFPIEGSRVHLTPKPGEDGSDYINASWLHGFRRLRDFIVTQHPMAHTIKDFWQMVWDHNAQTVVLLSSLD 881
Cdd:cd14554    5 CNKFKNRLVnILPYESTRVCLQPIRGVEGSDYINASFIDGYRQRGAYIATQGPLAETTEDFWRMLWEHNSTIIVMLTKLR 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45553601  882 DINF---AQFWPDEaTPIESDHYRVKFLNKTNKSDYVSRDFVIQSIQDDYELTVKMLHCPSWPEMSNPNS---IYDFIVD 955
Cdd:cd14554   85 EMGRekcHQYWPAE-RSARYQYFVVDPMAEYNMPQYILREFKVTDARDGQSRTVRQFQFTDWPEQGVPKSgegFIDFIGQ 163
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 45553601  956 VHERCNDY-RNGPIVIVDRYGGAQACTFCAISSLAIEMEYCSTANVYQYAKLYHNKRPGVWTSSEDIRVIY 1025
Cdd:cd14554  164 VHKTKEQFgQEGPITVHCSAGVGRTGVFITLSIVLERMRYEGVVDVFQTVKLLRTQRPAMVQTEDQYQFCY 234
COG5599 COG5599
Protein tyrosine phosphatase [Signal transduction mechanisms];
511-749 1.56e-41

Protein tyrosine phosphatase [Signal transduction mechanisms];


Pssm-ID: 444335 [Multi-domain]  Cd Length: 282  Bit Score: 154.48  E-value: 1.56e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45553601  511 HSQHPENKRKNRYLNITAYDHSRVhlhptpgqKKNLDYINANFIDGYQKgHAFIGTQGPLPDTFDCFWRMIWEQRVAIIV 590
Cdd:COG5599   36 YLQNINGSPLNRFRDIQPYKETAL--------RANLGYLNANYIQVIGN-HRYIATQYPLEEQLEDFFQMLFDNNTPVLV 106
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45553601  591 MITNLVERGRRKCDM--YWPKDGVETYGVIQVKLIEEEVMST-YTVRTLQIKHLklkkkkQCNTEKL-VYQYHYTNWPDH 666
Cdd:COG5599  107 VLASDDEISKPKVKMpvYFRQDGEYGKYEVSSELTESIQLRDgIEARTYVLTIK------GTGQKKIeIPVLHVKNWPDH 180
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45553601  667 GTPD----HPLpvLNFVKKSSAANPAEAGPIVVHCSAGVGRTGTYIVLDAMLKQIQQKNI--VNVFGFLRHIRAQRNF-L 739
Cdd:COG5599  181 GAISaealKNL--ADLIDKKEKIKDPDKLLPVVHCRAGVGRTGTLIACLALSKSINALVQitLSVEEIVIDMRTSRNGgM 258
                        250
                 ....*....|
gi 45553601  740 VQTEEQYIFL 749
Cdd:COG5599  259 VQTSEQLDVL 268
PTPc_motif smart00404
Protein tyrosine phosphatase, catalytic domain motif;
655-755 1.11e-37

Protein tyrosine phosphatase, catalytic domain motif;


Pssm-ID: 214649 [Multi-domain]  Cd Length: 105  Bit Score: 136.72  E-value: 1.11e-37
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45553601     655 VYQYHYTNWPDHGTPDHPLPVLNFVKKSSAANPAEA--GPIVVHCSAGVGRTGTYIVLDAMLKQIQQKNI-VNVFGFLRH 731
Cdd:smart00404    2 VKHYHYTGWPDHGVPESPDSILELLRAVKKNLNQSEssGPVVVHCSAGVGRTGTFVAIDILLQQLEAEAGeVDIFDTVKE 81
                            90       100
                    ....*....|....*....|....
gi 45553601     732 IRAQRNFLVQTEEQYIFLHDALVE 755
Cdd:smart00404   82 LRSQRPGMVQTEEQYLFLYRALLE 105
PTPc_DSPc smart00012
Protein tyrosine phosphatase, catalytic domain, undefined specificity; Protein tyrosine ...
655-755 1.11e-37

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: 136.72  E-value: 1.11e-37
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45553601     655 VYQYHYTNWPDHGTPDHPLPVLNFVKKSSAANPAEA--GPIVVHCSAGVGRTGTYIVLDAMLKQIQQKNI-VNVFGFLRH 731
Cdd:smart00012    2 VKHYHYTGWPDHGVPESPDSILELLRAVKKNLNQSEssGPVVVHCSAGVGRTGTFVAIDILLQQLEAEAGeVDIFDTVKE 81
                            90       100
                    ....*....|....*....|....
gi 45553601     732 IRAQRNFLVQTEEQYIFLHDALVE 755
Cdd:smart00012   82 LRSQRPGMVQTEEQYLFLYRALLE 105
R-PTP-D-2 cd14628
PTP-like domain of receptor-type tyrosine-protein phosphatase D, repeat 2; Receptor-type ...
768-1025 1.15e-37

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: 143.72  E-value: 1.15e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45553601  768 QVEELKNCTPyLEQQYKNIIQFQPKDIHIASAMKQVNSIKNRGA-IFPIEGSRVHLTPKPGEDGSDYINASWLHGFRRLR 846
Cdd:cd14628   17 QIETGENVTG-MELEFKRLASSKAHTSRFISANLPCNKFKNRLVnIMPYESTRVCLQPIRGVEGSDYINASFIDGYRQQK 95
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45553601  847 DFIVTQHPMAHTIKDFWQMVWDHNAQTVVLLSSLDDINFA---QFWPDEATPiESDHYRVKFLNKTNKSDYVSRDFVIQS 923
Cdd:cd14628   96 AYIATQGPLAETTEDFWRMLWEHNSTIVVMLTKLREMGREkchQYWPAERSA-RYQYFVVDPMAEYNMPQYILREFKVTD 174
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45553601  924 IQDDYELTVKMLHCPSWPEMSNPNS---IYDFIVDVHERCNDY-RNGPIVIVDRYGGAQACTFCAISSLAIEMEYCSTAN 999
Cdd:cd14628  175 ARDGQSRTVRQFQFTDWPEQGVPKSgegFIDFIGQVHKTKEQFgQDGPISVHCSAGVGRTGVFITLSIVLERMRYEGVVD 254
                        250       260
                 ....*....|....*....|....*.
gi 45553601 1000 VYQYAKLYHNKRPGVWTSSEDIRVIY 1025
Cdd:cd14628  255 IFQTVKMLRTQRPAMVQTEDQYQFCY 280
PTPc-N21 cd14598
catalytic domain of tyrosine-protein phosphatase non-receptor type 21; Tyrosine-protein ...
548-755 4.35e-37

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: 139.34  E-value: 4.35e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45553601  548 YINANFIDGYQKGHA--FIGTQGPLPDTFDCFWRMIWEQRVAIIVMITNLVERGRRKCDMYWPKDGVE----TYGVIQVK 621
Cdd:cd14598    1 YINASHIKVTVGGKEwdYIATQGPLQNTCQDFWQMVWEQGVAIIAMVTAEEEGGREKSFRYWPRLGSRhntvTYGRFKIT 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45553601  622 LIEEEVMSTYTVRTLQIKHLKLkkkkqcNTEKLVYQYHYTNWPDHGTPDHPLPVLNFVKK--------SSAANPAEAG-P 692
Cdd:cd14598   81 TRFRTDSGCYATTGLKIKHLLT------GQERTVWHLQYTDWPEHGCPEDLKGFLSYLEEiqsvrrhtNSTIDPKSPNpP 154
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 45553601  693 IVVHCSAGVGRTGTYIVLDAMLKQIQQKNIVNVFGFLRHIRAQRNFLVQTEEQYIFLHDALVE 755
Cdd:cd14598  155 VLVHCSAGVGRTGVVILSEIMIACLEHNEMLDIPRVLDMLRQQRMMMVQTLSQYTFVYKVLIQ 217
R-PTP-S-2 cd14627
PTP-like domain of receptor-type tyrosine-protein phosphatase S, repeat 2; Receptor-type ...
768-1025 1.65e-36

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: 140.25  E-value: 1.65e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45553601  768 QVEELKNCTPyLEQQYKNIIQFQPKDIHIASAMKQVNSIKNRGA-IFPIEGSRVHLTPKPGEDGSDYINASWLHGFRRLR 846
Cdd:cd14627   18 QVEVGEHVTG-MELEFKRLANSKAHTSRFISANLPCNKFKNRLVnIMPYETTRVCLQPIRGVEGSDYINASFIDGYRQQK 96
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45553601  847 DFIVTQHPMAHTIKDFWQMVWDHNAQTVVLLSSLDDINFA---QFWPDEATPiESDHYRVKFLNKTNKSDYVSRDFVIQS 923
Cdd:cd14627   97 AYIATQGPLAETTEDFWRMLWENNSTIVVMLTKLREMGREkchQYWPAERSA-RYQYFVVDPMAEYNMPQYILREFKVTD 175
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45553601  924 IQDDYELTVKMLHCPSWPEMSNPNS---IYDFIVDVHERCNDY-RNGPIVIVDRYGGAQACTFCAISSLAIEMEYCSTAN 999
Cdd:cd14627  176 ARDGQSRTVRQFQFTDWPEQGVPKSgegFIDFIGQVHKTKEQFgQDGPISVHCSAGVGRTGVFITLSIVLERMRYEGVVD 255
                        250       260
                 ....*....|....*....|....*.
gi 45553601 1000 VYQYAKLYHNKRPGVWTSSEDIRVIY 1025
Cdd:cd14627  256 IFQTVKMLRTQRPAMVQTEDEYQFCY 281
R-PTP-F-2 cd14629
PTP-like domain of receptor-type tyrosine-protein phosphatase F, repeat 2; Receptor-type ...
779-1025 6.54e-35

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: 135.62  E-value: 6.54e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45553601  779 LEQQYKNIIQFQPKDIHIASAMKQVNSIKNRGA-IFPIEGSRVHLTPKPGEDGSDYINASWLHGFRRLRDFIVTQHPMAH 857
Cdd:cd14629   28 MELEFKLLANSKAHTSRFISANLPCNKFKNRLVnIMPYELTRVCLQPIRGVEGSDYINASFIDGYRQQKAYIATQGPLAE 107
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45553601  858 TIKDFWQMVWDHNAQTVVLLSSLDDINFA---QFWPDEATPiESDHYRVKFLNKTNKSDYVSRDFVIQSIQDDYELTVKM 934
Cdd:cd14629  108 TTEDFWRMLWEHNSTIVVMLTKLREMGREkchQYWPAERSA-RYQYFVVDPMAEYNMPQYILREFKVTDARDGQSRTIRQ 186
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45553601  935 LHCPSWPEMSNPNS---IYDFIVDVHERCNDY-RNGPIVIVDRYGGAQACTFCAISSLAIEMEYCSTANVYQYAKLYHNK 1010
Cdd:cd14629  187 FQFTDWPEQGVPKTgegFIDFIGQVHKTKEQFgQDGPITVHCSAGVGRTGVFITLSIVLERMRYEGVVDMFQTVKTLRTQ 266
                        250
                 ....*....|....*
gi 45553601 1011 RPGVWTSSEDIRVIY 1025
Cdd:cd14629  267 RPAMVQTEDQYQLCY 281
R-PTPc-T-2 cd14634
PTP domain of receptor-type tyrosine-protein phosphatase T, repeat 2; Receptor-type ...
548-755 1.03e-30

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: 120.51  E-value: 1.03e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45553601  548 YINANFIDGYQKGHAFIGTQGPLPDTFDCFWRMIWEQRVAIIVMITNLveRGRRKCDMYWPKDGVETYGVIQVKLIEEEV 627
Cdd:cd14634    1 YINAALMDSHKQPAAFIVTQHPLPNTVADFWRLVFDYNCSSVVMLNEM--DAAQLCMQYWPEKTSCCYGPIQVEFVSADI 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45553601  628 MSTYTVRTLQIkhlklkkkkqCNTEK------LVYQYHYTNWPDH-GTPDHPLPVLNFVK---KSSAANPAEAGPIVVHC 697
Cdd:cd14634   79 DEDIISRIFRI----------CNMARpqdgyrIVQHLQYIGWPAYrDTPPSKRSILKVVRrleKWQEQYDGREGRTVVHC 148
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 45553601  698 SAGVGRTGTYIVLDAMLKQIQQKNIVNVFGFLRHIRAQRNFLVQTEEQYIFLHDALVE 755
Cdd:cd14634  149 LNGGGRSGTFCAICSVCEMIQQQNIIDVFHTVKTLRNNKSNMVETLEQYKFVYEVALE 206
R-PTPc-A-2 cd14623
catalytic domain of receptor-type tyrosine-protein phosphatase A, repeat 2; Receptor-type ...
812-1028 1.48e-30

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: 120.92  E-value: 1.48e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45553601  812 IFPIEGSRVHLTPKPGEDGSDYINASWLHGFRRLRDFIVTQHPMAHTIKDFWQMVWDHNAQTVVLLSSLDDI---NFAQF 888
Cdd:cd14623    5 IIPYEFNRVIIPVKRGEENTDYVNASFIDGYRQKDSYIASQGPLQHTIEDFWRMIWEWKSCSIVMLTELEERgqeKCAQY 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45553601  889 WPDEATPIESDhYRVKFLNKTNKSDYVSRDFVIQSIQDDYELTVKMLHCPSWPEMSNPNS---IYDFIVDVHERCNDYRN 965
Cdd:cd14623   85 WPSDGSVSYGD-ITIELKKEEECESYTVRDLLVTNTRENKSRQIRQFHFHGWPEVGIPSDgkgMINIIAAVQKQQQQSGN 163
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 45553601  966 GPIVIVDRYGGAQACTFCAISSLAIEMEYCSTANVYQYAKLYHNKRPGVWTSSEDIRVIYNIL 1028
Cdd:cd14623  164 HPITVHCSAGAGRTGTFCALSTVLERVKAEGILDVFQTVKSLRLQRPHMVQTLEQYEFCYKVV 226
R-PTPc-typeIIb-2 cd14556
PTP domain of type IIb (or R2B) subfamily receptor-type tyrosine-protein phosphatases, repeat ...
833-1025 2.45e-30

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: 119.43  E-value: 2.45e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45553601  833 YINASWLHGFRRLRDFIVTQHPMAHTIKDFWQMVWDHNAQTVVLLSSLDDIN--FAQFWPDEAT----PIEsdhyrVKFL 906
Cdd:cd14556    1 YINAALLDSYKQPAAFIVTQHPLPNTVTDFWRLVYDYGCTSIVMLNQLDPKDqsCPQYWPDEGSgtygPIQ-----VEFV 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45553601  907 NKTNKSDYVSRDFVIQSIQDDYE--LTVKMLHCPSWPE-----MSnPNSIYDFIVDVHERCNDYRNGPIVIVDRYGGAQA 979
Cdd:cd14556   76 STTIDEDVISRIFRLQNTTRPQEgyRMVQQFQFLGWPRdrdtpPS-KRALLKLLSEVEKWQEQSGEGPIVVHCLNGVGRS 154
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*.
gi 45553601  980 CTFCAISSLAIEMEYCSTANVYQYAKLYHNKRPGVWTSSEDIRVIY 1025
Cdd:cd14556  155 GVFCAISSVCERIKVENVVDVFQAVKTLRNHRPNMVETEEQYKFCY 200
R-PTPc-A-E-2 cd14552
catalytic domain of receptor-type tyrosine-protein phosphatase A and E, repeat 2; ...
833-1028 1.31e-29

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: 117.37  E-value: 1.31e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45553601  833 YINASWLHGFRRLRDFIVTQHPMAHTIKDFWQMVWDHNAQTVVLLSSLDDIN---FAQFWPDEATpIESDHYRVKFLNKT 909
Cdd:cd14552    1 YINASFIDGYRQKDAYIATQGPLDHTVEDFWRMIWEWKSCSIVMLTEIKERSqnkCAQYWPEDGS-VSSGDITVELKDQT 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45553601  910 NKSDYVSRDFVIQSIQDDYELTVKMLHCPSWPEM---SNPNSIYDFIVDVHERCNDYRNGPIVIVDRYGGAQACTFCAIS 986
Cdd:cd14552   80 DYEDYTLRDFLVTKGKGGSTRTVRQFHFHGWPEVgipDNGKGMIDLIAAVQKQQQQSGNHPITVHCSAGAGRTGTFCALS 159
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|..
gi 45553601  987 SLAIEMEYCSTANVYQYAKLYHNKRPGVWTSSEDIRVIYNIL 1028
Cdd:cd14552  160 TVLERVKAEGVLDVFQVVKSLRLQRPHMVQTLEQYEFCYKVV 201
R3-PTPc cd14548
catalytic domain of R3 subfamily receptor-type tyrosine-protein phosphatases and similar ...
812-1001 4.47e-29

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: 116.30  E-value: 4.47e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45553601  812 IFPIEGSRVHLTPKPGEDGSDYINASWLHGFRRLRDFIVTQHPMAHTIKDFWQMVWDHNAQTVVLLSSLDD---INFAQF 888
Cdd:cd14548    5 ILPYDHSRVKLIPINEEEGSDYINANYIPGYNSPREFIATQGPLPGTKDDFWRMVWEQNSHTIVMLTQCMEkgrVKCDHY 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45553601  889 WPDEATPIESDHYRVKFLNKTNKSDYVSRDFVIQSIQDdyELTVKMLHCPSWPEMSNPN---SIYDFIVDVHERCNDyRN 965
Cdd:cd14548   85 WPFDQDPVYYGDITVTMLSESVLPDWTIREFKLERGDE--VRSVRQFHFTAWPDHGVPEapdSLLRFVRLVRDYIKQ-EK 161
                        170       180       190
                 ....*....|....*....|....*....|....*.
gi 45553601  966 GPIVIVDRYGGAQACTFCAISSLAIEMEYCSTANVY 1001
Cdd:cd14548  162 GPTIVHCSAGVGRTGTFIALDRLLQQIESEDYVDIF 197
R-PTPc-K-2 cd14636
PTP domain of receptor-type tyrosine-protein phosphatase K, repeat 2; Receptor-type ...
548-755 1.46e-27

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: 111.66  E-value: 1.46e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45553601  548 YINANFIDGYQKGHAFIGTQGPLPDTFDCFWRMIWEQRVAIIVMITNL-VERGrrkCDMYWPKDGVETYGVIQVKLIEEE 626
Cdd:cd14636    1 YINAALMDSYRQPAAFIVTQHPLPNTVKDFWRLVYDYGCTSIVMLNEVdLAQG---CPQYWPEEGMLRYGPIQVECMSCS 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45553601  627 VMSTYTVRTLQIkhlklkkkkqCNTEK------LVYQYHYTNWPDH----GTPDHPLPVLNFVKKSSAANPAEAGPIVVH 696
Cdd:cd14636   78 MDCDVISRIFRI----------CNLTRpqegylMVQQFQYLGWASHrevpGSKRSFLKLILQVEKWQEECDEGEGRTIIH 147
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 45553601  697 CSAGVGRTGTYIVLDAMLKQIQQKNIVNVFGFLRHIRAQRNFLVQTEEQYIFLHDALVE 755
Cdd:cd14636  148 CLNGGGRSGMFCAISIVCEMIKRQNVVDVFHAVKTLRNSKPNMVETPEQYRFCYDVALE 206
R-PTPc-E-2 cd14622
catalytic domain of receptor-type tyrosine-protein phosphatase E, repeat 2; Receptor-type ...
832-1028 2.00e-27

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: 111.25  E-value: 2.00e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45553601  832 DYINASWLHGFRRLRDFIVTQHPMAHTIKDFWQMVWDHNAQTVVLLSSLDDI---NFAQFWPDEATPIESDhYRVKFLNK 908
Cdd:cd14622    1 DYINASFIDGYRQKDYFIATQGPLAHTVEDFWRMVWEWKCHTIVMLTELQEReqeKCVQYWPSEGSVTHGE-ITIEIKND 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45553601  909 TNKSDYVSRDFVIQSIQDDYELTVKMLHCPSWPEMSNP---NSIYDFIVDVHERCNDYRNGPIVIVDRYGGAQACTFCAI 985
Cdd:cd14622   80 TLLETISIRDFLVTYNQEKQTRLVRQFHFHGWPEIGIPaegKGMIDLIAAVQKQQQQTGNHPIVVHCSAGAGRTGTFIAL 159
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|...
gi 45553601  986 SSLAIEMEYCSTANVYQYAKLYHNKRPGVWTSSEDIRVIYNIL 1028
Cdd:cd14622  160 SNILERVKAEGLLDVFQTVKSLRLQRPHMVQTLEQYEFCYRVV 202
R-PTPc-V cd14618
catalytic domain of receptor-type tyrosine-protein phosphatase V; Receptor-type ...
812-1012 3.15e-27

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: 111.19  E-value: 3.15e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45553601  812 IFPIEGSRVHLTPKPGEDGSDYINASWLHGFRRLRDFIVTQHPMAHTIKDFWQMVWDHNAQTVVLLS-SLDD--INFAQF 888
Cdd:cd14618    6 VLPYDHSRVRLSQLGGEPHSDYINANFIPGYTSPQEFIATQGPLKKTIEDFWRLVWEQQVCNIIMLTvGMENgrVLCDHY 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45553601  889 WPDEATPIESDHYRVKFLNKTNKSDYVSRDFVIQSIQDDYELTVKMLHCPSWPEMS---NPNSIYDFIVDVHERCNDYRN 965
Cdd:cd14618   86 WPSESTPVSYGHITVHLLAQSSEDEWTRREFKLWHEDLRKERRVKHLHYTAWPDHGipeSTSSLMAFRELVREHVQATKG 165
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*...
gi 45553601  966 -GPIVIVDRYGGAQACTFCAISSLAIEMEYCSTANVYQYAKLYHNKRP 1012
Cdd:cd14618  166 kGPTLVHCSAGVGRSGTFIALDRLLRQLKEEKVVDVFNTVYILRMHRY 213
R-PTPc-A-1 cd14621
catalytic domain of receptor-type tyrosine-protein phosphatase A, repeat 1; Receptor-type ...
798-1011 3.66e-27

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: 113.19  E-value: 3.66e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45553601  798 SAMKQVNSIKNRGA-IFPIEGSRVHLTPKPGEDGSDYINASWLHGFRRLRDFIVTQHPMAHTIKDFWQMVWDHNAQTVVL 876
Cdd:cd14621   46 AASKEENKEKNRYVnILPYDHSRVHLTPVEGVPDSDYINASFINGYQEKNKFIAAQGPKEETVNDFWRMIWEQNTATIVM 125
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45553601  877 LSSL---DDINFAQFWPDEATPIESDhYRVKFLNKTNKSDYVSRDFVIQSIQD----DYELTVKMLHCPSWPEMS---NP 946
Cdd:cd14621  126 VTNLkerKECKCAQYWPDQGCWTYGN-IRVSVEDVTVLVDYTVRKFCIQQVGDvtnkKPQRLITQFHFTSWPDFGvpfTP 204
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 45553601  947 NSIYDFIVDVhERCNDYRNGPIVIVDRYGGAQACTFCAISSLAIEMEYCSTANVYQYAKLYHNKR 1011
Cdd:cd14621  205 IGMLKFLKKV-KNCNPQYAGAIVVHCSAGVGRTGTFIVIDAMLDMMHAERKVDVYGFVSRIRAQR 268
R-PTPc-E-1 cd14620
catalytic domain of receptor-type tyrosine-protein phosphatase E, repeat 1; Receptor-type ...
812-1028 4.22e-27

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: 110.80  E-value: 4.22e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45553601  812 IFPIEGSRVHLTPKPGEDGSDYINASWLHGFRRLRDFIVTQHPMAHTIKDFWQMVWDHNAQTVVLLSSL---DDINFAQF 888
Cdd:cd14620    4 ILPYDHSRVILSQLDGIPCSDYINASYIDGYKEKNKFIAAQGPKQETVNDFWRMVWEQKSATIVMLTNLkerKEEKCYQY 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45553601  889 WPDEATPIESDhYRVKFLNKTNKSDYVSRDFVIQSIQDDYELT---VKMLHCPSWPEMSNPNS---IYDFIVDVhERCND 962
Cdd:cd14620   84 WPDQGCWTYGN-IRVAVEDCVVLVDYTIRKFCIQPQLPDGCKAprlVTQLHFTSWPDFGVPFTpigMLKFLKKV-KSVNP 161
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 45553601  963 YRNGPIVIVDRYGGAQACTFCAISSLAIEMEYCSTANVYQYAKLYHNKRPGVWTSSEDIRVIYNIL 1028
Cdd:cd14620  162 VHAGPIVVHCSAGVGRTGTFIVIDAMIDMMHAEQKVDVFEFVSRIRNQRPQMVQTDMQYSFIYQAL 227
R-PTPc-F-1 cd14626
catalytic domain of receptor-type tyrosine-protein phosphatase F, repeat 1; Receptor-type ...
765-1011 1.37e-26

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: 110.90  E-value: 1.37e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45553601  765 MAEQVEELK-NCTPYLEQQYKNI---IQFQPKDIHIasamkQVNSIKNRGA-IFPIEGSRVHLTPKPGEDGSDYINASWL 839
Cdd:cd14626    3 LADNIERLKaNDGLKFSQEYESIdpgQQFTWENSNL-----EVNKPKNRYAnVIAYDHSRVILTSVDGVPGSDYINANYI 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45553601  840 HGFRRLRDFIVTQHPMAHTIKDFWQMVWDHNAQTVVLLSSLDD---INFAQFWPDEATPIESdHYRVKFLNKTNKSDYVS 916
Cdd:cd14626   78 DGYRKQNAYIATQGPLPETLSDFWRMVWEQRTATIVMMTRLEEksrVKCDQYWPIRGTETYG-MIQVTLLDTVELATYSV 156
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45553601  917 RDFVIQSIQDDYELTVKMLHCPSWPEM---SNPNSIYDFIVDVhERCNDYRNGPIVIVDRYGGAQACTFCAISSLAIEME 993
Cdd:cd14626  157 RTFALYKNGSSEKREVRQFQFMAWPDHgvpEYPTPILAFLRRV-KACNPPDAGPMVVHCSAGVGRTGCFIVIDAMLERMK 235
                        250
                 ....*....|....*...
gi 45553601  994 YCSTANVYQYAKLYHNKR 1011
Cdd:cd14626  236 HEKTVDIYGHVTCMRSQR 253
R-PTPc-LAR-1 cd14553
catalytic domain of LAR family receptor-type tyrosine-protein phosphatases, repeat 1; The LAR ...
802-1011 1.91e-26

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: 109.41  E-value: 1.91e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45553601  802 QVNSIKNRGA-IFPIEGSRVHLTPKPGEDGSDYINASWLHGFRRLRDFIVTQHPMAHTIKDFWQMVWDHNAQTVVLLSSL 880
Cdd:cd14553    1 EVNKPKNRYAnVIAYDHSRVILQPIEGVPGSDYINANYCDGYRKQNAYIATQGPLPETFGDFWRMVWEQRSATIVMMTKL 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45553601  881 DD---INFAQFWPDEATPIESDhYRVKFLNKTNKSDYVSRDFVIQSIQDDYELTVKMLHCPSWPEM---SNPNSIYDFIV 954
Cdd:cd14553   81 EErsrVKCDQYWPTRGTETYGL-IQVTLLDTVELATYTVRTFALHKNGSSEKREVRQFQFTAWPDHgvpEHPTPFLAFLR 159
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 45553601  955 DVhERCNDYRNGPIVIVDRYGGAQACTFCAISSLAIEMEYCSTANVYQYAKLYHNKR 1011
Cdd:cd14553  160 RV-KACNPPDAGPIVVHCSAGVGRTGCFIVIDSMLERIKHEKTVDIYGHVTCLRAQR 215
R-PTPc-H cd14619
catalytic domain of receptor-type tyrosine-protein phosphatase H; Receptor-type ...
812-1031 2.74e-26

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: 108.82  E-value: 2.74e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45553601  812 IFPIEGSRVHLTPKPGEDGSDYINASWLHGFRRLRDFIVTQHPMAHTIKDFWQMVWDHNAQTVVLLSSLDD---INFAQF 888
Cdd:cd14619    6 VLPYDWSRVPLKPIHEEPGSDYINANYMPGYWSSQEFIATQGPLPQTVGDFWRMIWEQQSSTIVMLTNCMEagrVKCEHY 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45553601  889 WPDEATPIESDHYRVKFLNKTNKSDYVSRDFVIQSIQDDYELTVKMLHCPSWPEM---SNPNSIYDFIVDVHERCNDYRN 965
Cdd:cd14619   86 WPLDYTPCTYGHLRVTVVSEEVMENWTVREFLLKQVEEQKTLSVRHFHFTAWPDHgvpSSTDTLLAFRRLLRQWLDQTMS 165
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 45553601  966 -GPIVIVDRYGGAQACTFCAISSLAIEMEYCSTANVYQYAKLYHNKRP-GVWTSSEDIRVIYNILSFL 1031
Cdd:cd14619  166 gGPTVVHCSAGVGRTGTLIALDVLLQQLQSEGLLGPFSFVQKMRENRPlMVQTESQYVFLHQCILDFL 233
R-PTPc-S-1 cd14625
catalytic domain of receptor-type tyrosine-protein phosphatase S, repeat 1; Receptor-type ...
765-1028 5.90e-26

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: 109.03  E-value: 5.90e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45553601  765 MAEQVEELK-NCTPYLEQQYKNI---IQFQPKDIHIasamkQVNSIKNRGA-IFPIEGSRVHLTPKPGEDGSDYINASWL 839
Cdd:cd14625    9 LAEHTERLKaNDNLKLSQEYESIdpgQQFTWEHSNL-----EVNKPKNRYAnVIAYDHSRVILQPIEGIMGSDYINANYI 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45553601  840 HGFRRLRDFIVTQHPMAHTIKDFWQMVWDHNAQTVVLLSSLDD---INFAQFWPDEATpiesDHY---RVKFLNKTNKSD 913
Cdd:cd14625   84 DGYRKQNAYIATQGPLPETFGDFWRMVWEQRSATVVMMTKLEEksrIKCDQYWPSRGT----ETYgmiQVTLLDTIELAT 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45553601  914 YVSRDFVIQSIQDDYELTVKMLHCPSWPEMSNPNSIYDFIVDVH--ERCNDYRNGPIVIVDRYGGAQACTFCAISSLAIE 991
Cdd:cd14625  160 FCVRTFSLHKNGSSEKREVRQFQFTAWPDHGVPEYPTPFLAFLRrvKTCNPPDAGPIVVHCSAGVGRTGCFIVIDAMLER 239
                        250       260       270
                 ....*....|....*....|....*....|....*..
gi 45553601  992 MEYCSTANVYQYAKLYHNKRPGVWTSSEDIRVIYNIL 1028
Cdd:cd14625  240 IKHEKTVDIYGHVTLMRSQRNYMVQTEDQYSFIHDAL 276
R-PTP-C-2 cd14558
PTP-like domain of receptor-type tyrosine-protein phosphatase C, repeat 2; Receptor-type ...
833-1025 8.17e-26

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: 106.32  E-value: 8.17e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45553601  833 YINASWLHGFRRLRDFIVTQHPMAHTIKDFWQMVWDHNAQTVVLLSSL---DDINFAQFWPDEATPIESDHYRVKflNKT 909
Cdd:cd14558    1 YINASFIDGYWGPKSLIATQGPLPDTIADFWQMIFQKKVKVIVMLTELkegDQEQCAQYWGDEKKTYGDIEVELK--DTE 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45553601  910 NKSDYVSRDFVIQSIQDDYELTVKMLHCPSW-----PEmsNPNSIYDFIVDVHERCNDY-----RNGPIVIVDRYGGAQA 979
Cdd:cd14558   79 KSPTYTVRVFEITHLKRKDSRTVYQYQYHKWkgeelPE--KPKDLVDMIKSIKQKLPYKnskhgRSVPIVVHCSDGSSRT 156
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*...
gi 45553601  980 CTFCAISSL--AIEMEycSTANVYQYAKLYHNKRPGVWTSSEDIRVIY 1025
Cdd:cd14558  157 GIFCALWNLleSAETE--KVVDVFQVVKALRKQRPGMVSTLEQYQFLY 202
R5-PTP-2 cd14550
PTP-like domain of R5 subfamily receptor-type tyrosine-protein phosphatases, repeat 2; The R5 ...
548-749 1.94e-25

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: 105.10  E-value: 1.94e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45553601  548 YINANFIDGYQKGHAFIGTQGPLPDTFDCFWRMIWEQRVAIIVMITNLVERGrrKCDMYWPKDG----VETYGVIQV--- 620
Cdd:cd14550    1 YINASYLQGYRRSNEFIITQHPLEHTIKDFWQMIWDHNSQTIVMLTDNELNE--DEPIYWPTKEkpleCETFKVTLSged 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45553601  621 -KLIEEEVMSTYTVRTLQikhlklkkKKQCNTEKLVYQYHYTNWPDHGTPDHplPVLNFVKKSSAANPAEAGPIVVHCSA 699
Cdd:cd14550   79 hSCLSNEIRLIVRDFILE--------STQDDYVLEVRQFQCPSWPNPCSPIH--TVFELINTVQEWAQQRDGPIVVHDRY 148
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|
gi 45553601  700 GVGRTGTYIVLDAMLKQIQQKNIVNVFGFLRHIRAQRNFLVQTEEQYIFL 749
Cdd:cd14550  149 GGVQAATFCALTTLHQQLEHESSVDVYQVAKLYHLMRPGVFTSKEDYQFL 198
R-PTPc-J cd14615
catalytic domain of receptor-type tyrosine-protein phosphatase J; Receptor-type ...
812-1001 2.19e-25

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: 106.05  E-value: 2.19e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45553601  812 IFPIEGSRVHLTpKPGEDGSDYINASWLHGFRRLRDFIVTQHPMAHTIKDFWQMVWDHNAQTVVLLS---SLDDINFAQF 888
Cdd:cd14615    6 VLPYDISRVKLS-VQSHSTDDYINANYMPGYNSKKEFIAAQGPLPNTVKDFWRMVWEKNVYAIVMLTkcvEQGRTKCEEY 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45553601  889 WPDEAtPIESDHYRVKFLNKTNKSDYVSRDFVIQSIQDDYELTVKMLHCPSWPEMSNPNS---IYDFIVDVHERCNDY-R 964
Cdd:cd14615   85 WPSKQ-KKDYGDITVTMTSEIVLPEWTIRDFTVKNAQTNESRTVRHFHFTSWPDHGVPETtdlLINFRHLVREYMKQNpP 163
                        170       180       190
                 ....*....|....*....|....*....|....*..
gi 45553601  965 NGPIVIVDRYGGAQACTFCAISSLAIEMEYCSTANVY 1001
Cdd:cd14615  164 NSPILVHCSAGVGRTGTFIAIDRLIYQIENENVVDVY 200
R-PTPc-M-2 cd14635
PTP domain of receptor-type tyrosine-protein phosphatase M, repeat 2; Receptor-type ...
548-755 2.50e-25

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: 105.15  E-value: 2.50e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45553601  548 YINANFIDGYQKGHAFIGTQGPLPDTFDCFWRMIWEQRVAIIVMITNLveRGRRKCDMYWPKDGVETYGVIQVKLIEEEV 627
Cdd:cd14635    1 YINAALMDSYKQPSAFIVTQHPLPNTVKDFWRLVLDYHCTSIVMLNDV--DPAQLCPQYWPENGVHRHGPIQVEFVSADL 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45553601  628 MSTYTVRTLQIKHLKLKKkkqcNTEKLVYQYHYTNWPDHgtPDHPLPVLNFVK------KSSAANPAEAGPIVVHCSAGV 701
Cdd:cd14635   79 EEDIISRIFRIYNAARPQ----DGYRMVQQFQFLGWPMY--RDTPVSKRSFLKlirqvdKWQEEYNGGEGRTVVHCLNGG 152
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....
gi 45553601  702 GRTGTYIVLDAMLKQIQQKNIVNVFGFLRHIRAQRNFLVQTEEQYIFLHDALVE 755
Cdd:cd14635  153 GRSGTFCAISIVCEMLRHQRAVDVFHAVKTLRNNKPNMVDLLDQYKFCYEVALE 206
R-PTPc-U-2 cd14637
PTP domain of receptor-type tyrosine-protein phosphatase U, repeat 2; Receptor-type ...
548-755 6.76e-25

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: 103.83  E-value: 6.76e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45553601  548 YINANFIDGYQKGHAFIGTQGPLPDTFDCFWRMIWEQRVAIIVMITNLVERGRR-KCDMYWPKDGVETYGVIQVKLIEEE 626
Cdd:cd14637    1 YINAALTDSYTRSAAFIVTLHPLQNTTTDFWRLVYDYGCTSVVMLNQLNQSNSAwPCLQYWPEPGLQQYGPMEVEFVSGS 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45553601  627 VMSTYTVRTLQIKHLKLKKKKQCntekLVYQYHYTNW-PDHGTPDHP---LPVLNFVKKSSAANpaEAGPIVVHCSAGVG 702
Cdd:cd14637   81 ADEDIVTRLFRVQNITRLQEGHL----MVRHFQFLRWsAYRDTPDSKkafLHLLASVEKWQRES--GEGRTVVHCLNGGG 154
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|...
gi 45553601  703 RTGTYIVLDAMLKQIQQKNIVNVFGFLRHIRAQRNFLVQTEEQYIFLHDALVE 755
Cdd:cd14637  155 RSGTYCASAMILEMIRCHNIVDVFYAVKTLRNYKPNMVETLEQYRFCYEIALE 207
PTPc-N9 cd14543
catalytic domain of tyrosine-protein phosphatase non-receptor type 9; Tyrosine-protein ...
798-1011 7.78e-25

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: 105.52  E-value: 7.78e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45553601  798 SAMKQVNSIKNR-GAIFPIEGSRVHLTPKPGEDGSDYINASWLHGFRRLRDFIVTQHPMAHTIKDFWQMVWDHNAQTVVL 876
Cdd:cd14543   23 CSLAPANQEKNRyGDVLCLDQSRVKLPKRNGDERTDYINANFMDGYKQKNAYIATQGPLPKTYSDFWRMVWEQKVLVIVM 102
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45553601  877 LSSLDD---INFAQFWP-DEATPIESDHYRVKFLNKTNKSDYVSRDFVIQSIQDDYELTVKMLHCPSWPEMSNPNS---I 949
Cdd:cd14543  103 TTRVVErgrVKCGQYWPlEEGSSLRYGDLTVTNLSVENKEHYKKTTLEIHNTETDESRQVTHFQFTSWPDFGVPSSaaaL 182
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 45553601  950 YDFIVDVHERCNDYRNG------------PIVI-----VDRYGgaqacTFCAISSLAIEMEYCSTANVYQYAKLYHNKR 1011
Cdd:cd14543  183 LDFLGEVRQQQALAVKAmgdrwkghppgpPIVVhcsagIGRTG-----TFCTLDICLSQLEDVGTLNVMQTVRRMRTQR 256
R-PTP-N cd14609
PTP-like domain of receptor-type tyrosine-protein phosphatase N; Receptor-type ...
764-1014 3.61e-24

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: 103.96  E-value: 3.61e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45553601  764 LMAEQVEELKNcTPYLEQQYKNIIQFQPKDIHIASAMKQVNSIKNRGAIF-PIEGSRVHLTPKPGEDGSDYINASWL--H 840
Cdd:cd14609    3 ILAYMEDHLRN-RDRLAKEWQALCAYQAEPNTCSTAQGEANVKKNRNPDFvPYDHARIKLKAESNPSRSDYINASPIieH 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45553601  841 GfRRLRDFIVTQHPMAHTIKDFWQMVWDHNAQTVVLLSSLDDINFAQ---FWPDEATPIesdhYRVKFLNKTNK----SD 913
Cdd:cd14609   82 D-PRMPAYIATQGPLSHTIADFWQMVWENGCTVIVMLTPLVEDGVKQcdrYWPDEGSSL----YHIYEVNLVSEhiwcED 156
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45553601  914 YVSRDFVIQSIQDDYELTVKMLHCPSWPEMSNPNS---IYDFIVDVHeRCNDYRNGPIVIVDRYGGAQACTFCAISSLAI 990
Cdd:cd14609  157 FLVRSFYLKNVQTQETRTLTQFHFLSWPAEGIPSStrpLLDFRRKVN-KCYRGRSCPIIVHCSDGAGRTGTYILIDMVLN 235
                        250       260
                 ....*....|....*....|....*.
gi 45553601  991 EMEYcSTANVYQYAKLYH--NKRPGV 1014
Cdd:cd14609  236 RMAK-GVKEIDIAATLEHvrDQRPGM 260
R-PTP-N2 cd14610
PTP-like domain of receptor-type tyrosine-protein phosphatase N2; Receptor-type ...
770-1019 4.76e-24

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: 103.60  E-value: 4.76e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45553601  770 EELKNcTPYLEQQYKNIIQFQPKDIHIASAMKQVNSIKNRG-AIFPIEGSRVHLTPKPGEDGSDYINASWL--HGFRRlR 846
Cdd:cd14610   11 DHLKN-KNRLEKEWEALCAYQAEPNATNVAQREENVQKNRSlAVLPYDHSRIILKAENSHSHSDYINASPImdHDPRN-P 88
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45553601  847 DFIVTQHPMAHTIKDFWQMVWDHNAQTVVLLSSLDDINFAQ---FWPDEAtpieSDHYRVKFLNKTNK----SDYVSRDF 919
Cdd:cd14610   89 AYIATQGPLPATVADFWQMVWESGCVVIVMLTPLAENGVKQcyhYWPDEG----SNLYHIYEVNLVSEhiwcEDFLVRSF 164
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45553601  920 VIQSIQDDYELTVKMLHCPSWPEMSNPNS---IYDFIVDVHeRCNDYRNGPIVIVDRYGGAQACTFCAISSLAIEMEYcS 996
Cdd:cd14610  165 YLKNLQTNETRTVTQFHFLSWNDQGVPAStrsLLDFRRKVN-KCYRGRSCPIIVHCSDGAGRSGTYILIDMVLNKMAK-G 242
                        250       260
                 ....*....|....*....|....*
gi 45553601  997 TANVYQYAKLYH--NKRPGVWTSSE 1019
Cdd:cd14610  243 AKEIDIAATLEHlrDQRPGMVQTKE 267
PHA02747 PHA02747
protein tyrosine phosphatase; Provisional
774-1039 7.05e-24

protein tyrosine phosphatase; Provisional


Pssm-ID: 165114 [Multi-domain]  Cd Length: 312  Bit Score: 103.93  E-value: 7.05e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45553601   774 NCTPYLEQQYKNIIqFQPKDIHIASAMKQVNSIKNRGAIFPI-EGSRVHLTPKPGEDgSDYINASWLHGFRRLRDFIVTQ 852
Cdd:PHA02747   22 NCFGIIRDEHHQII-LKPFDGLIANFEKPENQPKNRYWDIPCwDHNRVILDSGGGST-SDYIHANWIDGFEDDKKFIATQ 99
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45553601   853 HPMAHTIKDFWQMVWDHNAQTVVLLSSLDDINFA----QFW-PDEATPIESDHYRVKFLNKTNKSDYVSRDFVIQSIQDD 927
Cdd:PHA02747  100 GPFAETCADFWKAVWQEHCSIIVMLTPTKGTNGEekcyQYWcLNEDGNIDMEDFRIETLKTSVRAKYILTLIEITDKILK 179
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45553601   928 YELTVKMLHCPSWPEMSNPNSIYDFI-----VDVHER-------CNDYRNGPIVIVDRYGGAQACTFCAISSLAIEMEYC 995
Cdd:PHA02747  180 DSRKISHFQCSEWFEDETPSDHPDFIkfikiIDINRKksgklfnPKDALLCPIVVHCSDGVGKTGIFCAVDICLNQLVKR 259
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*...
gi 45553601   996 STANVYQYAKLYHNKRPGVWTSSEDIRVI----YNILSFLPGNLNLLK 1039
Cdd:PHA02747  260 KAICLAKTAEKIREQRHAGIMNFDDYLFIqpgyEVLHYFLSKIKAIDK 307
R-PTPc-M-1 cd14633
catalytic domain of receptor-type tyrosine-protein phosphatase M, repeat 1; Receptor-type ...
765-1028 8.55e-24

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: 102.43  E-value: 8.55e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45553601  765 MAEQVEELKNCTPY-LEQQYKNIIQFQ--PKDihiaSAMKQVNSIKNR-GAIFPIEGSRVHLTPKPGEDGSDYINASWLH 840
Cdd:cd14633    2 LLQHITQMKCAEGYgFKEEYESFFEGQsaPWD----SAKKDENRMKNRyGNIIAYDHSRVRLQPIEGETSSDYINGNYID 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45553601  841 GFRRLRDFIVTQHPMAHTIKDFWQMVWDHNAQTVVLLSSLDD---INFAQFWPDEaTPIESDhYRVKFLNKTNKSDYVSR 917
Cdd:cd14633   78 GYHRPNHYIATQGPMQETIYDFWRMVWHENTASIIMVTNLVEvgrVKCCKYWPDD-TEIYKD-IKVTLIETELLAEYVIR 155
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45553601  918 DFVIQSIQDDYELTVKMLHCPSWPEMSNP---NSIYDFIVDVHERcNDYRNGPIVIVDRYGGAQACTFCAISSLAIEMEY 994
Cdd:cd14633  156 TFAVEKRGVHEIREIRQFHFTGWPDHGVPyhaTGLLGFVRQVKSK-SPPNAGPLVVHCSAGAGRTGCFIVIDIMLDMAER 234
                        250       260       270
                 ....*....|....*....|....*....|....
gi 45553601  995 CSTANVYQYAKLYHNKRPGVWTSSEDIRVIYNIL 1028
Cdd:cd14633  235 EGVVDIYNCVRELRSRRVNMVQTEEQYVFIHDAI 268
PTPc-N1_2 cd14545
catalytic domain of tyrosine-protein phosphatase non-receptor type 1 and type 2; ...
818-993 1.76e-23

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: 100.54  E-value: 1.76e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45553601  818 SRVHLTpkpgEDGSDYINASWLHGFRRLRDFIVTQHPMAHTIKDFWQMVWDHNAQTVVLLSSL---DDINFAQFWP---D 891
Cdd:cd14545   15 SRVKLK----QGDNDYINASLVEVEEAKRSYILTQGPLPNTSGHFWQMVWEQNSKAVIMLNKLmekGQIKCAQYWPqgeG 90
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45553601  892 EATPIESDHYRVKFLNKTNKSDYVSRDFVIQSIQDDYELTVKMLHCPSWPEMS---NPNSIYDFIVDVHER-CNDYRNGP 967
Cdd:cd14545   91 NAMIFEDTGLKVTLLSEEDKSYYTVRTLELENLKTQETREVLHFHYTTWPDFGvpeSPAAFLNFLQKVRESgSLSSDVGP 170
                        170       180
                 ....*....|....*....|....*.
gi 45553601  968 IVIVDRYGGAQACTFCAISSLAIEME 993
Cdd:cd14545  171 PVVHCSAGIGRSGTFCLVDTCLVLIE 196
R-PTPc-T-1 cd14630
catalytic domain of receptor-type tyrosine-protein phosphatase T, repeat 1; Receptor-type ...
804-988 2.22e-23

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: 100.49  E-value: 2.22e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45553601  804 NSIKNR-GAIFPIEGSRVHLTPKPGEDGSDYINASWLHGFRRLRDFIVTQHPMAHTIKDFWQMVWDHNAQTVVLLSSLDD 882
Cdd:cd14630    3 NRNKNRyGNIISYDHSRVRLQLLDGDPHSDYINANYIDGYHRPRHYIATQGPMQETVKDFWRMIWQENSASVVMVTNLVE 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45553601  883 ---INFAQFWPDEaTPIESDhYRVKFLNKTNKSDYVSRDFVIQSIQDDYELTVKMLHCPSWPEMSNP---NSIYDFIVDV 956
Cdd:cd14630   83 vgrVKCVRYWPDD-TEVYGD-IKVTLIETEPLAEYVIRTFTVQKKGYHEIREIRQFHFTSWPDHGVPcyaTGLLGFVRQV 160
                        170       180       190
                 ....*....|....*....|....*....|..
gi 45553601  957 hERCNDYRNGPIVIVDRYGGAQACTFCAISSL 988
Cdd:cd14630  161 -KFLNPPDAGPIVVHCSAGAGRTGCFIAIDIM 191
R-PTP-Z-2 cd17669
catalytic domain of receptor-type tyrosine-protein phosphatase Z, repeat 2; Receptor-type ...
548-754 2.86e-23

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: 98.91  E-value: 2.86e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45553601  548 YINANFIDGYQKGHAFIGTQGPLPDTFDCFWRMIWEQRVAIIVMITNLVERGRRKCdMYWP-KDGVETYGVIQVKLIEEE 626
Cdd:cd17669    1 YINASYIMGYYQSNEFIITQHPLLHTIKDFWRMIWDHNAQLIVMLPDGQNMAEDEF-VYWPnKDEPINCETFKVTLIAEE 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45553601  627 VMSTYTVRTLqIKHLKLKKKKQCNTEKLVYQYHYTNWPDhgtPDHPLP----VLNFVKKSSAanpAEAGPIVVHCSAGVG 702
Cdd:cd17669   80 HKCLSNEEKL-IIQDFILEATQDDYVLEVRHFQCPKWPN---PDSPISktfeLISIIKEEAA---NRDGPMIVHDEHGGV 152
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|..
gi 45553601  703 RTGTYIVLDAMLKQIQQKNIVNVFGFLRHIRAQRNFLVQTEEQYIFLHDALV 754
Cdd:cd17669  153 TAGTFCALTTLMHQLEKENSVDVYQVAKMINLMRPGVFTDIEQYQFLYKAIL 204
R5-PTPc-1 cd14549
catalytic domain of R5 subfamily receptor-type tyrosine-protein phosphatases, repeat 1; The R5 ...
833-1011 4.41e-23

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: 98.58  E-value: 4.41e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45553601  833 YINASWLHGFRRLRDFIVTQHPMAHTIKDFWQMVWDHNAQTVVLLSSLDD---INFAQFWPDEATPiESDHYRVKFLNKT 909
Cdd:cd14549    1 YINANYVDGYNKARAYIATQGPLPSTFDDFWRMVWEQNSAIIVMITNLVErgrRKCDQYWPKEGTE-TYGNIQVTLLSTE 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45553601  910 NKSDYVSRDFVIQSIQ------DDYELTVKMLHCPSWPEMSNPNS---IYDFIVDVhERCNDYRNGPIVI-----VDRYG 975
Cdd:cd14549   80 VLATYTVRTFSLKNLKlkkvkgRSSERVVYQYHYTQWPDHGVPDYtlpVLSFVRKS-SAANPPGAGPIVVhcsagVGRTG 158
                        170       180       190
                 ....*....|....*....|....*....|....*.
gi 45553601  976 gaqacTFCAISSLAIEMEYCSTANVYQYAKLYHNKR 1011
Cdd:cd14549  159 -----TYIVIDSMLQQIQDKGTVNVFGFLKHIRTQR 189
R-PTPc-T-2 cd14634
PTP domain of receptor-type tyrosine-protein phosphatase T, repeat 2; Receptor-type ...
833-1027 4.81e-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: 98.55  E-value: 4.81e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45553601  833 YINASWLHGFRRLRDFIVTQHPMAHTIKDFWQMVWDHNAQTVVLLSSLDDINFA-QFWPDEAT----PIEsdhyrVKFLN 907
Cdd:cd14634    1 YINAALMDSHKQPAAFIVTQHPLPNTVADFWRLVFDYNCSSVVMLNEMDAAQLCmQYWPEKTSccygPIQ-----VEFVS 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45553601  908 KTNKSDYVSRDFVIQSI---QDDYELtVKMLHCPSWPEMSNPNSIYDFIVDVHERCN------DYRNGPIVIVDRYGGAQ 978
Cdd:cd14634   76 ADIDEDIISRIFRICNMarpQDGYRI-VQHLQYIGWPAYRDTPPSKRSILKVVRRLEkwqeqyDGREGRTVVHCLNGGGR 154
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*....
gi 45553601  979 ACTFCAISSLAIEMEYCSTANVYQYAKLYHNKRPGVWTSSEDIRVIYNI 1027
Cdd:cd14634  155 SGTFCAICSVCEMIQQQNIIDVFHTVKTLRNNKSNMVETLEQYKFVYEV 203
R-PTPc-D-1 cd14624
catalytic domain of receptor-type tyrosine-protein phosphatase D, repeat 1; Receptor-type ...
765-1011 6.46e-23

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: 100.19  E-value: 6.46e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45553601  765 MAEQVEELK-NCTPYLEQQYKNI---IQFQPKDIHIasamkQVNSIKNRGA-IFPIEGSRVHLTPKPGEDGSDYINASWL 839
Cdd:cd14624    9 LADHIERLKaNDNLKFSQEYESIdpgQQFTWEHSNL-----EVNKPKNRYAnVIAYDHSRVLLSAIEGIPGSDYINANYI 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45553601  840 HGFRRLRDFIVTQHPMAHTIKDFWQMVWDHNAQTVVLLSSLDD---INFAQFWPDEATPIESdHYRVKFLNKTNKSDYVS 916
Cdd:cd14624   84 DGYRKQNAYIATQGALPETFGDFWRMIWEQRSATVVMMTKLEErsrVKCDQYWPSRGTETYG-LIQVTLLDTVELATYCV 162
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45553601  917 RDFVIQSIQDDYELTVKMLHCPSWPEMSNPNSIYDFIVDVH--ERCNDYRNGPIVIVDRYGGAQACTFCAISSLAIEMEY 994
Cdd:cd14624  163 RTFALYKNGSSEKREVRQFQFTAWPDHGVPEHPTPFLAFLRrvKTCNPPDAGPMVVHCSAGVGRTGCFIVIDAMLERIKH 242
                        250
                 ....*....|....*..
gi 45553601  995 CSTANVYQYAKLYHNKR 1011
Cdd:cd14624  243 EKTVDIYGHVTLMRAQR 259
R-PTPc-A-E-1 cd14551
catalytic domain of receptor-type tyrosine-protein phosphatase A and E, repeat 1; ...
833-1012 9.19e-23

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: 97.68  E-value: 9.19e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45553601  833 YINASWLHGFRRLRDFIVTQHPMAHTIKDFWQMVWDHNAQTVVLLSSLDD---INFAQFWPDEATPIESDhYRVKFLNKT 909
Cdd:cd14551    1 YINASYIDGYQEKNKFIAAQGPKDETVNDFWRMIWEQGSATIVMVTNLKErkeKKCSQYWPDQGCWTYGN-LRVRVEDTV 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45553601  910 NKSDYVSRDFVIQSIQDDY----ELTVKMLHCPSWPEMSNPNS---IYDFIVDVhERCNDYRNGPIVIVDRYGGAQACTF 982
Cdd:cd14551   80 VLVDYTTRKFCIQKVNRGIgekrVRLVTQFHFTSWPDFGVPFTpigMLKFLKKV-KSANPPRAGPIVVHCSAGVGRTGTF 158
                        170       180       190
                 ....*....|....*....|....*....|
gi 45553601  983 CAISSLAIEMEYCSTANVYQYAKLYHNKRP 1012
Cdd:cd14551  159 IVIDAMLDMMHAEGKVDVFGFVSRIRQQRS 188
PTPc-N11_6 cd14544
catalytic domain of tyrosine-protein phosphatase non-receptor type 11 and type 6; ...
804-970 1.26e-22

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: 98.69  E-value: 1.26e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45553601  804 NSIKNR-GAIFPIEGSRVHLTPK-PGEDGSDYINASWLH-------GFRRLRDFIVTQHPMAHTIKDFWQMVWDHNAQTV 874
Cdd:cd14544    1 NKGKNRyKNILPFDHTRVILKDRdPNVPGSDYINANYIRnenegptTDENAKTYIATQGCLENTVSDFWSMVWQENSRVI 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45553601  875 VLLSSLDDI---NFAQFWPDEATPIESDHYRVKFLNKTNKSDYVSRDFVIQSI-QDDYELTVKMLHCPSWPEM---SNPN 947
Cdd:cd14544   81 VMTTKEVERgknKCVRYWPDEGMQKQYGPYRVQNVSEHDTTDYTLRELQVSKLdQGDPIREIWHYQYLSWPDHgvpSDPG 160
                        170       180
                 ....*....|....*....|....*
gi 45553601  948 SIYDFIVDVHERcNDYRN--GPIVI 970
Cdd:cd14544  161 GVLNFLEDVNQR-QESLPhaGPIVV 184
R-PTPc-O cd14614
catalytic domain of receptor-type tyrosine-protein phosphatase O; Receptor-type ...
793-988 1.38e-21

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: 95.34  E-value: 1.38e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45553601  793 DIHIASAMKQVNSIKNRGA-IFPIEGSRVHLTPKPGEDGSDYINASWLHGFRRLRDFIVTQHPMAHTIKDFWQMVWDHNA 871
Cdd:cd14614    1 DIPHFAADLPVNRCKNRYTnILPYDFSRVKLVSMHEEEGSDYINANYIPGYNSPQEYIATQGPLPETRNDFWKMVLQQKS 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45553601  872 QTVVLLSSLDD---INFAQFWPDEATPIESDHYRVKFLNKTNKSDYVSRDFVIqSIQDDYElTVKMLHCPSWPEMSNPN- 947
Cdd:cd14614   81 QIIVMLTQCNEkrrVKCDHYWPFTEEPVAYGDITVEMLSEEEQPDWAIREFRV-SYADEVQ-DVMHFNYTAWPDHGVPTa 158
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*
gi 45553601  948 ----SIYDFIVDVHERCNDyRNGPIVIVDRYGGAQACTFCAISSL 988
Cdd:cd14614  159 naaeSILQFVQMVRQQAVK-SKGPMIIHCSAGVGRTGTFIALDRL 202
PTPc-KIM cd14547
catalytic domain of the kinase interaction motif (KIM) family of protein-tyrosine phosphatases; ...
812-986 1.91e-21

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: 94.39  E-value: 1.91e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45553601  812 IFPIEGSRVHLTPKPGEDGSDYINASWLHGFRRLRD-FIVTQHPMAHTIKDFWQMVWDHNAQTVVLLSSLDDIN--FAQF 888
Cdd:cd14547    6 ILPNEHSRVCLPSVDDDPLSSYINANYIRGYDGEEKaYIATQGPLPNTVADFWRMVWQEKTPIIVMITNLTEAKekCAQY 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45553601  889 WPDEaTPIESDHYRVKFLNKTNKSDYVSRDFVIQSIQDDYEltVKMLHCPSWPEMSNPNS---IYDFIVDVHE-RCNDYR 964
Cdd:cd14547   86 WPEE-ENETYGDFEVTVQSVKETDGYTVRKLTLKYGGEKRY--LKHYWYTSWPDHKTPEAaqpLLSLVQEVEEaRQTEPH 162
                        170       180
                 ....*....|....*....|...
gi 45553601  965 NGPIVIVDRYG-GAQACtFCAIS 986
Cdd:cd14547  163 RGPIVVHCSAGiGRTGC-FIATS 184
R-PTPc-Q cd14616
catalytic domain of receptor-type tyrosine-protein phosphatase Q; Receptor-type ...
812-988 5.13e-21

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: 93.05  E-value: 5.13e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45553601  812 IFPIEGSRVHLTPKPGEDGSDYINASWLHGFRRLRDFIVTQHPMAHTIKDFWQMVWDHNAQTVVLLSSLDD---INFAQF 888
Cdd:cd14616    6 IKPYNNNRVKLIADAGVPGSDYINASYISGYLCPNEFIATQGPLPGTVGDFWRMVWETRAKTIVMLTQCFEkgrIRCHQY 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45553601  889 WPDEATPIE--SDHYRVKFLNKTnKSDYVSRDFVIQSiQDDYeLTVKMLHCPSWPEMSNPNSIYDFIVDVH----ERCND 962
Cdd:cd14616   86 WPEDNKPVTvfGDIVITKLMEDV-QIDWTIRDLKIER-HGDY-MMVRQCNFTSWPEHGVPESSAPLIHFVKlvraSRAHD 162
                        170       180
                 ....*....|....*....|....*.
gi 45553601  963 yrNGPIVIVDRYGGAQACTFCAISSL 988
Cdd:cd14616  163 --NTPMIVHCSAGVGRTGVFIALDHL 186
R-PTPc-K-2 cd14636
PTP domain of receptor-type tyrosine-protein phosphatase K, repeat 2; Receptor-type ...
833-1027 1.15e-20

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


Pssm-ID: 350484 [Multi-domain]  Cd Length: 206  Bit Score: 91.63  E-value: 1.15e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45553601  833 YINASWLHGFRRLRDFIVTQHPMAHTIKDFWQMVWDHNAQTVVLLSSLDDIN-FAQFWPDEATpIESDHYRVKFLNKTNK 911
Cdd:cd14636    1 YINAALMDSYRQPAAFIVTQHPLPNTVKDFWRLVYDYGCTSIVMLNEVDLAQgCPQYWPEEGM-LRYGPIQVECMSCSMD 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45553601  912 SDYVSRDFVIQSI---QDDYeLTVKMLHCPSWPEM----SNPNSIYDFIVDV---HERCnDYRNGPIVIVDRYGGAQACT 981
Cdd:cd14636   80 CDVISRIFRICNLtrpQEGY-LMVQQFQYLGWASHrevpGSKRSFLKLILQVekwQEEC-DEGEGRTIIHCLNGGGRSGM 157
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*.
gi 45553601  982 FCAISSLAIEMEYCSTANVYQYAKLYHNKRPGVWTSSEDIRVIYNI 1027
Cdd:cd14636  158 FCAISIVCEMIKRQNVVDVFHAVKTLRNSKPNMVETPEQYRFCYDV 203
PTP_fungal cd18533
fungal protein tyrosine phosphatases; This subfamily contains Saccharomyces cerevisiae ...
833-1031 1.62e-20

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: 91.16  E-value: 1.62e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45553601  833 YINASWLH-GFRRLRDFIVTQHPMAHTIKDFWQMVWDHNAQTVVLLSSLDDINF---AQFWPDEATPIESDHYRVKFLNK 908
Cdd:cd18533    1 YINASYITlPGTSSKRYIATQGPLPATIGDFWKMIWQNNVGVIVMLTPLVENGRekcDQYWPSGEYEGEYGDLTVELVSE 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45553601  909 T--NKSDYVSRDFVIQSiQDDYELTVKMLHCPSWPEMSNPNSIYDF--IVDVHERCND--YRNGPIVI-----VDRYGga 977
Cdd:cd18533   81 EenDDGGFIVREFELSK-EDGKVKKVYHIQYKSWPDFGVPDSPEDLltLIKLKRELNDsaSLDPPIIVhcsagVGRTG-- 157
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....
gi 45553601  978 qacTFCAISSLAIEMEycstanvyqyaklyhNKRPGVWTSSEDIRVIYNILSFL 1031
Cdd:cd18533  158 ---TFIALDSLLDELK---------------RGLSDSQDLEDSEDPVYEIVNQL 193
R-PTPc-U-2 cd14637
PTP domain of receptor-type tyrosine-protein phosphatase U, repeat 2; Receptor-type ...
833-1027 2.00e-20

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: 90.74  E-value: 2.00e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45553601  833 YINASWLHGFRRLRDFIVTQHPMAHTIKDFWQMVWDHNAQTVVLLSSLDDINFA----QFWPDEAT----PIEsdhyrVK 904
Cdd:cd14637    1 YINAALTDSYTRSAAFIVTLHPLQNTTTDFWRLVYDYGCTSVVMLNQLNQSNSAwpclQYWPEPGLqqygPME-----VE 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45553601  905 FLNKTNKSDYVSRDFVIQSIQ--DDYELTVKMLHCPSW-PEMSNPNSIYDF---IVDVHERCNDYRNGPIVIVDRYGGAQ 978
Cdd:cd14637   76 FVSGSADEDIVTRLFRVQNITrlQEGHLMVRHFQFLRWsAYRDTPDSKKAFlhlLASVEKWQRESGEGRTVVHCLNGGGR 155
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|
gi 45553601  979 ACTFCAiSSLAIEMEYC-STANVYQYAKLYHNKRPGVWTSSEDIRVIYNI 1027
Cdd:cd14637  156 SGTYCA-SAMILEMIRChNIVDVFYAVKTLRNYKPNMVETLEQYRFCYEI 204
R-PTP-N-N2 cd14546
PTP-like domain of receptor-type tyrosine-protein phosphatase-like N and N2; Receptor-type ...
833-985 2.64e-20

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: 90.58  E-value: 2.64e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45553601  833 YINASWLHGFR-RLRDFIVTQHPMAHTIKDFWQMVWDHNAQTVVLLSSLDDINFAQ---FWPDEATPIESDhYRVKFLNK 908
Cdd:cd14546    1 YINASTIYDHDpRNPAYIATQGPLPHTIADFWQMIWEQGCVVIVMLTRLQENGVKQcarYWPEEGSEVYHI-YEVHLVSE 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45553601  909 TNKS-DYVSRDFVIQSIQDDYELTVKMLHCPSWPEMS---NPNSIYDFIVDVHeRCNDYRNGPIVIVDRYGGAQACTFCA 984
Cdd:cd14546   80 HIWCdDYLVRSFYLKNLQTSETRTVTQFHFLSWPDEGipaSAKPLLEFRRKVN-KSYRGRSCPIVVHCSDGAGRTGTYIL 158

                 .
gi 45553601  985 I 985
Cdd:cd14546  159 I 159
PTPc-N11 cd14605
catalytic domain of tyrosine-protein phosphatase non-receptor type 11; Tyrosine-protein ...
804-988 2.76e-20

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: 92.00  E-value: 2.76e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45553601  804 NSIKNR-GAIFPIEGSRVHLTP-KPGEDGSDYINASWL--------HGFRRLRDFIVTQHPMAHTIKDFWQMVWDHNAQT 873
Cdd:cd14605    2 NKNKNRyKNILPFDHTRVVLHDgDPNEPVSDYINANIImpefetkcNNSKPKKSYIATQGCLQNTVNDFWRMVFQENSRV 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45553601  874 VVLLS---SLDDINFAQFWPDEATPIESDHYRVKFLNKTNKSDYVSRDFVIQSI-QDDYELTVKMLHCPSWPEM---SNP 946
Cdd:cd14605   82 IVMTTkevERGKSKCVKYWPDEYALKEYGVMRVRNVKESAAHDYILRELKLSKVgQGNTERTVWQYHFRTWPDHgvpSDP 161
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|...
gi 45553601  947 NSIYDFIVDVHERCNDYRN-GPIVIVDRYGGAQACTFCAISSL 988
Cdd:cd14605  162 GGVLDFLEEVHHKQESIMDaGPVVVHCSAGIGRTGTFIVIDIL 204
R-PTPc-G-1 cd17667
catalytic domain of receptor-type tyrosine-protein phosphatase G, repeat 1; Receptor-type ...
766-1028 3.03e-20

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: 92.41  E-value: 3.03e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45553601  766 AEQVEELKNCTPYLE--QQYKNiiqfQPKDIHiasamkqvnsiKNRGA-IFPIEGSRVHLTPKPGEDG--SDYINASWLH 840
Cdd:cd17667    2 SEDFEEVQRCTADMNitAEHSN----HPDNKH-----------KNRYInILAYDHSRVKLRPLPGKDSkhSDYINANYVD 66
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45553601  841 GFRRLRDFIVTQHPMAHTIKDFWQMVWDHNAQTVVLLSSLDDI---NFAQFWPDEatpiESDHYR--VKFLNKTN-KSDY 914
Cdd:cd17667   67 GYNKAKAYIATQGPLKSTFEDFWRMIWEQNTGIIVMITNLVEKgrrKCDQYWPTE----NSEEYGniIVTLKSTKiHACY 142
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45553601  915 VSRDFVIQSIQDDY-----------ELTVKMLHCPSWPEMSNPNSIYDFIVDVhERCNDYRN---GPIVIVDRYGGAQAC 980
Cdd:cd17667  143 TVRRFSIRNTKVKKgqkgnpkgrqnERTVIQYHYTQWPDMGVPEYALPVLTFV-RRSSAARTpemGPVLVHCSAGVGRTG 221
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*...
gi 45553601  981 TFCAISSLAIEMEYCSTANVYQYAKLYHNKRPGVWTSSEDIRVIYNIL 1028
Cdd:cd17667  222 TYIVIDSMLQQIKDKSTVNVLGFLKHIRTQRNYLVQTEEQYIFIHDAL 269
PTPc-N1 cd14608
catalytic domain of tyrosine-protein phosphatase non-receptor type 1; Tyrosine-protein ...
787-1033 3.14e-20

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: 92.40  E-value: 3.14e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45553601  787 IQFQPKDIHIASAMKQVNSIKNR-GAIFPIEGSRVHLTpkpgEDGSDYINASWLHGFRRLRDFIVTQHPMAHTIKDFWQM 865
Cdd:cd14608    8 IRHEASDFPCRVAKLPKNKNRNRyRDVSPFDHSRIKLH----QEDNDYINASLIKMEEAQRSYILTQGPLPNTCGHFWEM 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45553601  866 VWDHNAQTVVLLSSL---DDINFAQFWP---DEATPIESDHYRVKFLNKTNKSDYVSRDFVIQSIQDDYELTVKMLHCPS 939
Cdd:cd14608   84 VWEQKSRGVVMLNRVmekGSLKCAQYWPqkeEKEMIFEDTNLKLTLISEDIKSYYTVRQLELENLTTQETREILHFHYTT 163
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45553601  940 WPEM---SNPNSIYDFIVDVHER-CNDYRNGPIVIVDRYGGAQACTFCAISSLAIEMEY---CSTANVYQYAKLYHNKRP 1012
Cdd:cd14608  164 WPDFgvpESPASFLNFLFKVRESgSLSPEHGPVVVHCSAGIGRSGTFCLADTCLLLMDKrkdPSSVDIKKVLLEMRKFRM 243
                        250       260
                 ....*....|....*....|.
gi 45553601 1013 GVWTSSEDIRVIYniLSFLPG 1033
Cdd:cd14608  244 GLIQTADQLRFSY--LAVIEG 262
R-PTP-G-2 cd17670
PTP-like domain of receptor-type tyrosine-protein phosphatase G, repeat 2; Receptor-type ...
548-754 5.89e-20

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: 89.35  E-value: 5.89e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45553601  548 YINANFIDGYQKGHAFIGTQGPLPDTFDCFWRMIWEQRVAIIVMITNlvERGRRKCD-MYWPKD----GVETYGVIQVK- 621
Cdd:cd17670    1 YINASYIMGYYRSNEFIITQHPLPHTTKDFWRMIWDHNAQIIVMLPD--NQGLAEDEfVYWPSReesmNCEAFTVTLISk 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45553601  622 ----LIEEE--VMSTYTVRTLQIKHLKLKKKKQCnteklvyqyhyTNWPDhgtPDHPLP----VLNFVKKSSAanpAEAG 691
Cdd:cd17670   79 drlcLSNEEqiIIHDFILEATQDDYVLEVRHFQC-----------PKWPN---PDAPISstfeLINVIKEEAL---TRDG 141
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 45553601  692 PIVVHCSAGVGRTGTYIVLDAMLKQIQQKNIVNVFGFLRHIRAQRNFLVQTEEQYIFLHDALV 754
Cdd:cd17670  142 PTIVHDEFGAVSAGTLCALTTLSQQLENENAVDVYQVAKMINLMRPGVFTDIEQYQFLYKAML 204
R-PTPc-M-2 cd14635
PTP domain of receptor-type tyrosine-protein phosphatase M, repeat 2; Receptor-type ...
833-1014 6.17e-20

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: 89.36  E-value: 6.17e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45553601  833 YINASWLHGFRRLRDFIVTQHPMAHTIKDFWQMVWDHNAQTVVLLSSLDDINFA-QFWPDEAT----PIEsdhyrVKFLN 907
Cdd:cd14635    1 YINAALMDSYKQPSAFIVTQHPLPNTVKDFWRLVLDYHCTSIVMLNDVDPAQLCpQYWPENGVhrhgPIQ-----VEFVS 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45553601  908 KTNKSDYVSRDFVIQSI---QDDYELtVKMLHCPSWPEMSN-PNSIYDFI-----VDVHERCNDYRNGPIVIVDRYGGAQ 978
Cdd:cd14635   76 ADLEEDIISRIFRIYNAarpQDGYRM-VQQFQFLGWPMYRDtPVSKRSFLklirqVDKWQEEYNGGEGRTVVHCLNGGGR 154
                        170       180       190
                 ....*....|....*....|....*....|....*.
gi 45553601  979 ACTFCAISSLAIEMEYCSTANVYQYAKLYHNKRPGV 1014
Cdd:cd14635  155 SGTFCAISIVCEMLRHQRAVDVFHAVKTLRNNKPNM 190
R-PTPc-B cd14617
catalytic domain of receptor-type tyrosine-protein phosphatase B; Receptor-type ...
812-1001 7.47e-20

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: 89.98  E-value: 7.47e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45553601  812 IFPIEGSRVHLTPKPGEDGSDYINASWLHGFRRLRDFIVTQHPMAHTIKDFWQMVWDHNAQTVVLLSSLDD---INFAQF 888
Cdd:cd14617    6 ILPYDSTRVKLSNVDDDPCSDYINASYIPGNNFRREYIATQGPLPGTKDDFWKMVWEQNVHNIVMVTQCVEkgrVKCDHY 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45553601  889 WPDEATPIESDHYRVKFLNKTNKSDYVSRDFVIQS-IQDDYELTVKMLHCPSWPEMSNPN---SIYDFIVDVHERCNDYR 964
Cdd:cd14617   86 WPADQDSLYYGDLIVQMLSESVLPEWTIREFKICSeEQLDAPRLVRHFHYTVWPDHGVPEttqSLIQFVRTVRDYINRTP 165
                        170       180       190
                 ....*....|....*....|....*....|....*...
gi 45553601  965 N-GPIVIVDRYGGAQACTFCAISSLAIEMEYCSTANVY 1001
Cdd:cd14617  166 GsGPTVVHCSAGVGRTGTFIALDRILQQLDSKDSVDIY 203
PTPc-N12 cd14604
catalytic domain of tyrosine-protein phosphatase non-receptor type 12; Tyrosine-protein ...
801-985 4.53e-19

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: 89.22  E-value: 4.53e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45553601  801 KQVNSIKNR-GAIFPIEGSRVHLTPKPGEDGSDYINASWLHGFRRLRDFIVTQHPMAHTIKDFWQMVWDHNAQTVVLLS- 878
Cdd:cd14604   54 KEENVKKNRyKDILPFDHSRVKLTLKTSSQDSDYINANFIKGVYGPKAYIATQGPLANTVIDFWRMIWEYNVAIIVMACr 133
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45553601  879 --SLDDINFAQFWPDEA-TPIESDHYRVKFLNKTNKSDYVSRDFVIQSIQDDYELTvkMLHCPSWPEMSNPNSiYDFIVD 955
Cdd:cd14604  134 efEMGRKKCERYWPLYGeEPMTFGPFRISCEAEQARTDYFIRTLLLEFQNETRRLY--QFHYVNWPDHDVPSS-FDSILD 210
                        170       180       190
                 ....*....|....*....|....*....|...
gi 45553601  956 VHERCNDYR---NGPIVIVDRYGGAQACTFCAI 985
Cdd:cd14604  211 MISLMRKYQeheDVPICIHCSAGCGRTGAICAI 243
PTPc-N2 cd14607
catalytic domain of tyrosine-protein phosphatase non-receptor type 2; Tyrosine-protein ...
787-993 5.41e-19

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: 88.10  E-value: 5.41e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45553601  787 IQFQPKDIHIASAMKQVNSIKNR-GAIFPIEGSRVHLTpkpgEDGSDYINASWLHGFRRLRDFIVTQHPMAHTIKDFWQM 865
Cdd:cd14607    7 IRNESHDYPHRVAKYPENRNRNRyRDVSPYDHSRVKLQ----NTENDYINASLVVIEEAQRSYILTQGPLPNTCCHFWLM 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45553601  866 VWDHNAQTVVLLSSL---DDINFAQFWP---DEATPIESDHYRVKFLNKTNKSDYVSRDFVIQSIQDDYELTVKMLHCPS 939
Cdd:cd14607   83 VWQQKTKAVVMLNRIvekDSVKCAQYWPtdeEEVLSFKETGFSVKLLSEDVKSYYTVHLLQLENINSGETRTISHFHYTT 162
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 45553601  940 WPEM---SNPNSIYDFIVDVHE-RCNDYRNGPIVIVDRYGGAQACTFCAISSLAIEME 993
Cdd:cd14607  163 WPDFgvpESPASFLNFLFKVREsGSLSPEHGPAVVHCSAGIGRSGTFSLVDTCLVLME 220
R-PTPc-K-1 cd14631
catalytic domain of receptor-type tyrosine-protein phosphatase K, repeat 1; Receptor-type ...
819-1028 5.71e-19

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: 87.00  E-value: 5.71e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45553601  819 RVHLTPKPGEDGSDYINASWLHGFRRLRDFIVTQHPMAHTIKDFWQMVWDHNAQTVVLLSSLDDINFA---QFWPDEaTP 895
Cdd:cd14631    1 RVILQPVEDDPSSDYINANYIDGYQRPSHYIATQGPVHETVYDFWRMIWQEQSACIVMVTNLVEVGRVkcyKYWPDD-TE 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45553601  896 IESDhYRVKFLNKTNKSDYVSRDFVIQSIQDDYELTVKMLHCPSWPEMSNP---NSIYDFIVDVhERCNDYRNGPIVIVD 972
Cdd:cd14631   80 VYGD-FKVTCVEMEPLAEYVVRTFTLERRGYNEIREVKQFHFTGWPDHGVPyhaTGLLSFIRRV-KLSNPPSAGPIVVHC 157
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 45553601  973 RYGGAQACTFCAISSLAIEMEYCSTANVYQYAKLYHNKRPGVWTSSEDIRVIYNIL 1028
Cdd:cd14631  158 SAGAGRTGCYIVIDIMLDMAEREGVVDIYNCVKALRSRRINMVQTEEQYIFIHDAI 213
PTPc-N18 cd14603
catalytic domain of tyrosine-protein phosphatase non-receptor type 18; Tyrosine-protein ...
766-985 1.24e-18

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: 87.19  E-value: 1.24e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45553601  766 AEQVEELKNCTPYLEQQYKNIIQfqpkdihiASAMKQvNSIKNR-GAIFPIEGSRVHLTPKPGEDGSDYINASWLHGFRR 844
Cdd:cd14603    1 AGEFSEIRACSAAFKADYVCSTV--------AGGRKE-NVKKNRyKDILPYDQTRVILSLLQEEGHSDYINANFIKGVDG 71
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45553601  845 LRDFIVTQHPMAHTIKDFWQMVWDHNAQTVVLlsSLDDINFAQ-----FWPDEATPIESDHYRVKFLnktnKSDYVSRDF 919
Cdd:cd14603   72 SRAYIATQGPLSHTVLDFWRMIWQYGVKVILM--ACREIEMGKkkcerYWAQEQEPLQTGPFTITLV----KEKRLNEEV 145
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 45553601  920 VIQSIQDDY---ELTVKMLHCPSWPEMSNPNSiYDFIVDVHERCNDYRNG---PIVIVDRYGGAQACTFCAI 985
Cdd:cd14603  146 ILRTLKVTFqkeSRSVSHFQYMAWPDHGIPDS-PDCMLAMIELARRLQGSgpePLCVHCSAGCGRTGVICTV 216
PTPc-N22 cd14602
catalytic domain of tyrosine-protein phosphatase non-receptor type 22; Tyrosine-protein ...
807-1031 1.77e-18

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: 86.05  E-value: 1.77e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45553601  807 KNR-GAIFPIEGSRVHLTPKPGEDGSDYINASWLHGFRRLRDFIVTQHPMAHTIKDFWQMVWDHNAQTVVLLS---SLDD 882
Cdd:cd14602    1 KNRyKDILPYDHSRVELSLITSDEDSDYINANFIKGVYGPRAYIATQGPLSTTLLDFWRMIWEYSVLIIVMACmefEMGK 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45553601  883 INFAQFWPDEAT-PIESDHYRVKFLNKTNKSDYVSRDFVIQSIQDDYelTVKMLHCPSWPEMSNPNS---IYDFIVDVhe 958
Cdd:cd14602   81 KKCERYWAEPGEmQLEFGPFSVTCEAEKRKSDYIIRTLKVKFNSETR--TIYQFHYKNWPDHDVPSSidpILELIWDV-- 156
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45553601  959 RC-NDYRNGPIVIVDRYGGAQACTFCAISSL-------AIEMEYcstaNVYQYAKLYHNKRPGVWTSSEDIRVIYNILSF 1030
Cdd:cd14602  157 RCyQEDDSVPICIHCSAGCGRTGVICAIDYTwmllkdgIIPENF----SVFSLIQEMRTQRPSLVQTKEQYELVYNAVIE 232

                 .
gi 45553601 1031 L 1031
Cdd:cd14602  233 L 233
R-PTPc-U-1 cd14632
catalytic domain of receptor-type tyrosine-protein phosphatase U, repeat 1; Receptor-type ...
833-1026 9.13e-18

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: 83.18  E-value: 9.13e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45553601  833 YINASWLHGFRRLRDFIVTQHPMAHTIKDFWQMVWDHNAQTVVLLSSLDD---INFAQFWPDeatpiESDHY---RVKFL 906
Cdd:cd14632    1 YINANYIDGYHRSNHFIATQGPKQEMVYDFWRMVWQEHCSSIVMITKLVEvgrVKCSKYWPD-----DSDTYgdiKITLL 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45553601  907 NKTNKSDYVSRDFVIQSIQDDYELTVKMLHCPSWPEMSNP---NSIYDFIVDVhERCNDYRNGPIVIVDRYGGAQacTFC 983
Cdd:cd14632   76 KTETLAEYSVRTFALERRGYSARHEVKQFHFTSWPEHGVPyhaTGLLAFIRRV-KASTPPDAGPVVVHCSAGAGR--TGC 152
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*
gi 45553601  984 AIS-SLAIEMEYCS-TANVYQYAKLYHNKRPGVWTSSEDIRVIYN 1026
Cdd:cd14632  153 YIVlDVMLDMAECEgVVDIYNCVKTLCSRRINMIQTEEQYIFIHD 197
R-PTPc-R cd14611
catalytic domain of receptor-type tyrosine-protein phosphatase R; Receptor-type ...
807-970 1.07e-17

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: 83.43  E-value: 1.07e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45553601  807 KNR-GAIFPIEGSRVHLTPKPGEDG-SDYINASWLHGFR-RLRDFIVTQHPMAHTIKDFWQMVWDHNAQTVVLLSSLDDI 883
Cdd:cd14611    2 KNRyKTILPNPHSRVCLKPKNSNDSlSTYINANYIRGYGgKEKAFIATQGPMINTVNDFWQMVWQEDSPVIVMITKLKEK 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45553601  884 N--FAQFWPDEatpiESDHYRVKFL-NKTNKSD-YVSRDFVIQsiQDDYELTVKMLHCPSWPEMSNPNS---IYDFIVDV 956
Cdd:cd14611   82 NekCVLYWPEK----RGIYGKVEVLvNSVKECDnYTIRNLTLK--QGSQSRSVKHYWYTSWPDHKTPDSaqpLLQLMLDV 155
                        170
                 ....*....|....*
gi 45553601  957 HE-RCNDYRNGPIVI 970
Cdd:cd14611  156 EEdRLASPGRGPVVV 170
PTPc-N7 cd14612
catalytic domain of tyrosine-protein phosphatase non-receptor type 7; Tyrosine-protein ...
807-970 1.74e-17

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: 83.35  E-value: 1.74e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45553601  807 KNR-GAIFPIEGSRVHL-TPKPGEDGSDYINASWLHGFR-RLRDFIVTQHPMAHTIKDFWQMVWDHNAQTVVLLSSLDDI 883
Cdd:cd14612   18 KDRyKTILPNPQSRVCLrRAGSQEEEGSYINANYIRGYDgKEKAYIATQGPMLNTVSDFWEMVWQEECPIIVMITKLKEK 97
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45553601  884 N--FAQFWPDEatpiESDHYRVKF-LNKTNKSD-YVSRDFVIQSIQDDYEltVKMLHCPSWPEMSNPNS---IYDFIVDV 956
Cdd:cd14612   98 KekCVHYWPEK----EGTYGRFEIrVQDMKECDgYTIRDLTIQLEEESRS--VKHYWFSSWPDHQTPESagpLLRLVAEV 171
                        170
                 ....*....|....*
gi 45553601  957 HERCNDYRN-GPIVI 970
Cdd:cd14612  172 EESRQTAASpGPIVV 186
PHA02746 PHA02746
protein tyrosine phosphatase; Provisional
816-1009 2.36e-17

protein tyrosine phosphatase; Provisional


Pssm-ID: 165113 [Multi-domain]  Cd Length: 323  Bit Score: 84.70  E-value: 2.36e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45553601   816 EGSRVHLTPKpgEDGSDYINASWLHGFRRLRDFIVTQHPMAHTIKDFWQMVWDHNAQTVVLLSSLDD---INFAQFWPDE 892
Cdd:PHA02746   85 DGKKIEVTSE--DNAENYIHANFVDGFKEANKFICAQGPKEDTSEDFFKLISEHESQVIVSLTDIDDddeKCFELWTKEE 162
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45553601   893 ATPIESDHYRVKFLNKTNKSDYVSRDFVIQSIQDDYELTVKMLHCPSWPEMSNPNSIYDFiVDVHERCNDYRN------- 965
Cdd:PHA02746  163 DSELAFGRFVAKILDIIEELSFTKTRLMITDKISDTSREIHHFWFPDWPDNGIPTGMAEF-LELINKVNEEQAelikqad 241
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....
gi 45553601   966 ------GPIVIVDRYGGAQACTFCAI----SSLAIEMEYCSTANVYQYAKLYHN 1009
Cdd:PHA02746  242 ndpqtlGPIVVHCSAGIGRAGTFCAIdnalEQLEKEKEVCLGEIVLKIRKQRHS 295
PTPc-N5 cd14613
catalytic domain of tyrosine-protein phosphatase non-receptor type 5; Tyrosine-protein ...
807-1029 2.47e-17

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: 83.37  E-value: 2.47e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45553601  807 KNR-GAIFPIEGSRVHLTPKPGEDG-SDYINASWLHGF-RRLRDFIVTQHPMAHTIKDFWQMVWDHNAQTVVLLSSLDDI 883
Cdd:cd14613   28 KNRyKTILPNPHSRVCLTSPDQDDPlSSYINANYIRGYgGEEKVYIATQGPTVNTVGDFWRMVWQERSPIIVMITNIEEM 107
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45553601  884 N--FAQFWPDEATPIESDHYRVKflNKTNKSDYVSRDFVIQSiqDDYELTVKMLHCPSWPEMSNPNS---IYDFIVDVHE 958
Cdd:cd14613  108 NekCTEYWPEEQVTYEGIEITVK--QVIHADDYRLRLITLKS--GGEERGLKHYWYTSWPDQKTPDNappLLQLVQEVEE 183
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 45553601  959 --RCNDYRNGPIVIVDRYGGAQACTFCAISSLAIEMEYCSTANVYQYAKLYHNKRPGVWTSSEDIRVIYNILS 1029
Cdd:cd14613  184 arQQAEPNCGPVIVHCSAGIGRTGCFIATSICCKQLRNEGVVDILRTTCQLRLDRGGMIQTCEQYQFVHHVLS 256
R-PTPc-typeIIb-1 cd14555
catalytic domain of type IIb (or R2B) subfamily receptor-type tyrosine-protein phosphatases, ...
833-1011 3.00e-17

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: 81.50  E-value: 3.00e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45553601  833 YINASWLHGFRRLRDFIVTQHPMAHTIKDFWQMVWDHNAQTVVLLSSLDD---INFAQFWPDEaTPIESDhYRVKFLNKT 909
Cdd:cd14555    1 YINANYIDGYHRPNHYIATQGPMQETVYDFWRMVWQENSASIVMVTNLVEvgrVKCSRYWPDD-TEVYGD-IKVTLVETE 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45553601  910 NKSDYVSRDFVIQSIQDDYELTVKMLHCPSWPEMSNP---NSIYDFIVDVHERcNDYRNGPIVIVDRYGGAQACTFCAIS 986
Cdd:cd14555   79 PLAEYVVRTFALERRGYHEIREVRQFHFTGWPDHGVPyhaTGLLGFIRRVKAS-NPPSAGPIVVHCSAGAGRTGCYIVID 157
                        170       180
                 ....*....|....*....|....*
gi 45553601  987 SLAIEMEYCSTANVYQYAKLYHNKR 1011
Cdd:cd14555  158 IMLDMAEREGVVDIYNCVKELRSRR 182
PTPc-N3 cd14600
catalytic domain of tyrosine-protein phosphatase non-receptor type 3; Tyrosine-protein ...
796-953 4.97e-17

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: 82.59  E-value: 4.97e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45553601  796 IASAMKQVNSIKNR-GAIFPIEGSRVHLtpkpgEDGSDYINASWLH----GFRRLRDFIVTQHPMAHTIKDFWQMVWDHN 870
Cdd:cd14600   32 ITCAKLPQNMDKNRyKDVLPYDATRVVL-----QGNEDYINASYVNmeipSANIVNKYIATQGPLPHTCAQFWQVVWEQK 106
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45553601  871 AQTVVLLSSLDD---INFAQFWPDEATPIESDHYRVKFLNKTNKSDYVSRDFVIQSIQDDYELTVKMLHCPSWPEMSNPN 947
Cdd:cd14600  107 LSLIVMLTTLTErgrTKCHQYWPDPPDVMEYGGFRVQCHSEDCTIAYVFREMLLTNTQTGEERTVTHLQYVAWPDHGVPD 186

                 ....*.
gi 45553601  948 SIYDFI 953
Cdd:cd14600  187 DSSDFL 192
PTPc_motif smart00404
Protein tyrosine phosphatase, catalytic domain motif;
931-1028 9.36e-17

Protein tyrosine phosphatase, catalytic domain motif;


Pssm-ID: 214649 [Multi-domain]  Cd Length: 105  Bit Score: 77.01  E-value: 9.36e-17
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45553601     931 TVKMLHCPSWPEMSNP---NSIYDFIVDVHERCND-YRNGPIVIVDRYGGAQACTFCAISSLAIEMEYCS-TANVYQYAK 1005
Cdd:smart00404    1 TVKHYHYTGWPDHGVPespDSILELLRAVKKNLNQsESSGPVVVHCSAGVGRTGTFVAIDILLQQLEAEAgEVDIFDTVK 80
                            90       100
                    ....*....|....*....|...
gi 45553601    1006 LYHNKRPGVWTSSEDIRVIYNIL 1028
Cdd:smart00404   81 ELRSQRPGMVQTEEQYLFLYRAL 103
PTPc_DSPc smart00012
Protein tyrosine phosphatase, catalytic domain, undefined specificity; Protein tyrosine ...
931-1028 9.36e-17

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: 77.01  E-value: 9.36e-17
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45553601     931 TVKMLHCPSWPEMSNP---NSIYDFIVDVHERCND-YRNGPIVIVDRYGGAQACTFCAISSLAIEMEYCS-TANVYQYAK 1005
Cdd:smart00012    1 TVKHYHYTGWPDHGVPespDSILELLRAVKKNLNQsESSGPVVVHCSAGVGRTGTFVAIDILLQQLEAEAgEVDIFDTVK 80
                            90       100
                    ....*....|....*....|...
gi 45553601    1006 LYHNKRPGVWTSSEDIRVIYNIL 1028
Cdd:smart00012   81 ELRSQRPGMVQTEEQYLFLYRAL 103
R-PTPc-Z-1 cd17668
catalytic domain of receptor-type tyrosine-protein phosphatase Z, repeat 1; Receptor-type ...
833-1028 1.67e-16

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: 79.64  E-value: 1.67e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45553601  833 YINASWLHGFRRLRDFIVTQHPMAHTIKDFWQMVWDHNAQTVVLLSSLDDI---NFAQFWPDEATPiESDHYRVKFLNKT 909
Cdd:cd17668    1 YINANYVDGYNKPKAYIAAQGPLKSTAEDFWRMIWEHNVEVIVMITNLVEKgrrKCDQYWPADGSE-EYGNFLVTQKSVQ 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45553601  910 NKSDYVSRDFVIQSIQ--------DDYELTVKMLHCPSWPEMSNPNSIYDFIVDVHERCNDYR--NGPIVIVDRYGGAQA 979
Cdd:cd17668   80 VLAYYTVRNFTLRNTKikkgsqkgRPSGRVVTQYHYTQWPDMGVPEYTLPVLTFVRKASYAKRhaVGPVVVHCSAGVGRT 159
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*....
gi 45553601  980 CTFCAISSLAIEMEYCSTANVYQYAKLYHNKRPGVWTSSEDIRVIYNIL 1028
Cdd:cd17668  160 GTYIVLDSMLQQIQHEGTVNIFGFLKHIRSQRNYLVQTEEQYVFIHDAL 208
PTPc-N3_4 cd14541
catalytic domain of tyrosine-protein phosphatase non-receptor type 21 and type 14; ...
832-967 3.51e-16

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: 78.91  E-value: 3.51e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45553601  832 DYINASWLH----GFRRLRDFIVTQHPMAHTIKDFWQMVWDHNAQTVVLLSSLDD---INFAQFWPDEATPIESDHYRVK 904
Cdd:cd14541    1 DYINANYVNmeipGSGIVNRYIAAQGPLPNTCADFWQMVWEQKSTLIVMLTTLVErgrVKCHQYWPDLGETMQFGNLQIT 80
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 45553601  905 FLNKTNKSDYVSRDFVIQSIQDDYELTVKMLHCPSWPEM---SNPNSIYDFIvdvhERCNDYRNGP 967
Cdd:cd14541   81 CVSEEVTPSFAFREFILTNTNTGEERHITQMQYLAWPDHgvpDDSSDFLDFV----KRVRQNRVGM 142
PHA02740 PHA02740
protein tyrosine phosphatase; Provisional
493-753 3.71e-16

protein tyrosine phosphatase; Provisional


Pssm-ID: 165107 [Multi-domain]  Cd Length: 298  Bit Score: 80.78  E-value: 3.71e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45553601   493 REYEAIQNEciSDDLPCEHSQHPENKRK--NRYLNITAYDHSRVHLHptpGQKKNLDyinANFIDGYQKGHAFIGTQGPL 570
Cdd:PHA02740   29 KEYRAIVPE--HEDEANKACAQAENKAKdeNLALHITRLLHRRIKLF---NDEKVLD---ARFVDGYDFEQKFICIINLC 100
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45553601   571 PDTFDCFWRMIWEQRVAIIVMITNLVErgrRKC-DMYWP-KDG-VETYGVIQVKLIEEEVMSTYTVRTLQIkhlklkkKK 647
Cdd:PHA02740  101 EDACDKFLQALSDNKVQIIVLISRHAD---KKCfNQFWSlKEGcVITSDKFQIETLEIIIKPHFNLTLLSL-------TD 170
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45553601   648 QCNTEKLVYQYHYTNWPDHGTPDHPLPVLNF----------VKKSSAAnpAEAGPIVVHCSAGVGRTGTYIVLDAMLKQI 717
Cdd:PHA02740  171 KFGQAQKISHFQYTAWPADGFSHDPDAFIDFfcniddlcadLEKHKAD--GKIAPIIIDCIDGISSSAVFCVFDICATEF 248
                         250       260       270
                  ....*....|....*....|....*....|....*.
gi 45553601   718 QQKNIVNVFGFLRHIRAQRNFLVQTEEQYIFLHDAL 753
Cdd:PHA02740  249 DKTGMLSIANALKKVRQKKYGCMNCLDDYVFCYHLI 284
R-PTPc-C-1 cd14557
catalytic domain of receptor-type tyrosine-protein phosphatase C, repeat 1; Receptor-type ...
833-1010 5.00e-16

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: 77.95  E-value: 5.00e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45553601  833 YINASWLHGFRRLRDFIVTQHPMAHTIKDFWQMVWDHNAQTVVLLSSLDDIN---FAQFWP--DEATPIESDhYRVKFLN 907
Cdd:cd14557    1 YINASYIDGFKEPRKYIAAQGPKDETVDDFWRMIWEQKSTVIVMVTRCEEGNrnkCAQYWPsmEEGSRAFGD-VVVKINE 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45553601  908 KTNKSDYVSRDFVIQSIQDDY-ELTVKMLHCPSWPEMSNPNSIYdFIVDVHERCNDYRN---GPIVIVDRYGGAQACTFC 983
Cdd:cd14557   80 EKICPDYIIRKLNINNKKEKGsGREVTHIQFTSWPDHGVPEDPH-LLLKLRRRVNAFNNffsGPIVVHCSAGVGRTGTYI 158
                        170       180
                 ....*....|....*....|....*...
gi 45553601  984 AISSLAIEMEYCSTANVYQY-AKLYHNK 1010
Cdd:cd14557  159 GIDAMLEGLEAEGRVDVYGYvVKLRRQR 186
fn3 pfam00041
Fibronectin type III domain;
172-274 6.53e-16

Fibronectin type III domain;


Pssm-ID: 394996 [Multi-domain]  Cd Length: 85  Bit Score: 73.99  E-value: 6.53e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45553601    172 SKPQNLTILDVSANSITMSWHPPKNQNGAIAGYHVFHIHDNQTGVEivkNSRNSVETLIHFELQNLRefnyvfiwglfgv 251
Cdd:pfam00041    1 SAPSNLTVTDVTSTSLTVSWTPPPDGNGPITGYEVEYRPKNSGEPW---NEITVPGTTTSVTLTGLK------------- 64
                           90       100
                   ....*....|....*....|...
gi 45553601    252 kgPYTDYRVIVKAFTTKNEGEPS 274
Cdd:pfam00041   65 --PGTEYEVRVQAVNGGGEGPPS 85
FN3 cd00063
Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein ...
171-281 1.67e-15

Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein fibronectin. Its tenth fibronectin type III repeat contains an RGD cell recognition sequence in a flexible loop between 2 strands. Approximately 2% of all animal proteins contain the FN3 repeat; including extracellular and intracellular proteins, membrane spanning cytokine receptors, growth hormone receptors, tyrosine phosphatase receptors, and adhesion molecules. FN3-like domains are also found in bacterial glycosyl hydrolases.


Pssm-ID: 238020 [Multi-domain]  Cd Length: 93  Bit Score: 72.91  E-value: 1.67e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45553601  171 PSKPQNLTILDVSANSITMSWHPPKNQNGAIAGYHVFHIHDNQTGVEIVKNSRNSVEtliHFELQNLRefnyvfiwglfg 250
Cdd:cd00063    1 PSPPTNLRVTDVTSTSVTLSWTPPEDDGGPITGYVVEYREKGSGDWKEVEVTPGSET---SYTLTGLK------------ 65
                         90       100       110
                 ....*....|....*....|....*....|.
gi 45553601  251 vkgPYTDYRVIVKAFTTKNEGEPSDQIAQRT 281
Cdd:cd00063   66 ---PGTEYEFRVRAVNGGGESPPSESVTVTT 93
PTPc-N13 cd14597
catalytic domain of tyrosine-protein phosphatase non-receptor type 13; Tyrosine-protein ...
804-969 2.01e-15

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: 77.18  E-value: 2.01e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45553601  804 NSIKNR-GAIFPIEGSRVHLtpkpGEDGsDYINASWLHGFRRLRDF--IVTQHPMAHTIKDFWQMVWDHNAQTVVLLSSL 880
Cdd:cd14597    3 NRKKNRyKNILPYDTTRVPL----GDEG-GYINASFIKMPVGDEEFvyIACQGPLPTTVADFWQMVWEQKSTVIAMMTQE 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45553601  881 ---DDINFAQFWPDE--ATPIESDHYRVKFLNKTNKSDYVSRDFVIQSIQDDYELTVKMLHCPSWPEMSNPNSIYDFIVD 955
Cdd:cd14597   78 vegGKIKCQRYWPEIlgKTTMVDNRLQLTLVRMQQLKNFVIRVLELEDIQTREVRHITHLNFTAWPDHDTPSQPEQLLTF 157
                        170
                 ....*....|....
gi 45553601  956 VHERCNDYRNGPIV 969
Cdd:cd14597  158 ISYMRHIHKSGPII 171
PTP-N23 cd14539
PTP-like domain of tyrosine-protein phosphatase non-receptor type 23; Tyrosine-protein ...
833-993 4.16e-15

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: 75.50  E-value: 4.16e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45553601  833 YINASWLHGFRRLR-DFIVTQHPMAHTIKDFWQMVWDHNAQTVVLLSS---LDDINFAQFWPDE-ATPIESDHYRVKFLN 907
Cdd:cd14539    1 YINASLIEDLTPYCpRFIATQAPLPGTAADFWLMVYEQQVSVIVMLVSeqeNEKQKVHRYWPTErGQALVYGAITVSLQS 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45553601  908 KTNKSDYVSRDFVIQSIQDDYELTVKMLHCPSWPEMSNPNSI---YDFIVDVHERCNDYRN--GPIVI-----VDRYGga 977
Cdd:cd14539   81 VRTTPTHVERIISIQHKDTRLSRSVVHLQFTTWPELGLPDSPnplLRFIEEVHSHYLQQRSlqTPIVVhcssgVGRTG-- 158
                        170
                 ....*....|....*.
gi 45553601  978 qacTFCAISSLAIEME 993
Cdd:cd14539  159 ---AFCLLYAAVQEIE 171
PHA02740 PHA02740
protein tyrosine phosphatase; Provisional
781-1039 8.36e-15

protein tyrosine phosphatase; Provisional


Pssm-ID: 165107 [Multi-domain]  Cd Length: 298  Bit Score: 76.54  E-value: 8.36e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45553601   781 QQYKNIIQFQPKDIHIASAmKQVNSIKNRGAIFPIE---GSRVHLTPKpgedgSDYINASWLHGFRRLRDFIVTQHPMAH 857
Cdd:PHA02740   29 KEYRAIVPEHEDEANKACA-QAENKAKDENLALHITrllHRRIKLFND-----EKVLDARFVDGYDFEQKFICIINLCED 102
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45553601   858 TIKDFWQMVWDHNAQTVVLLSSLDDIN-FAQFWP-DEATPIESDHYRVKFLNKTNKSDYVsrdFVIQSIQDDYELTVKML 935
Cdd:PHA02740  103 ACDKFLQALSDNKVQIIVLISRHADKKcFNQFWSlKEGCVITSDKFQIETLEIIIKPHFN---LTLLSLTDKFGQAQKIS 179
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45553601   936 HC--PSWPE---MSNPNSIYDFIVDVHERCNDYRN-------GPIVIVDRYGGAQACTFCAISSLAIEMEYCSTANVYQY 1003
Cdd:PHA02740  180 HFqyTAWPAdgfSHDPDAFIDFFCNIDDLCADLEKhkadgkiAPIIIDCIDGISSSAVFCVFDICATEFDKTGMLSIANA 259
                         250       260       270
                  ....*....|....*....|....*....|....*..
gi 45553601  1004 AKLYHNKRPGVWTSSEDIRVIYNILS-FLPGNLNLLK 1039
Cdd:PHA02740  260 LKKVRQKKYGCMNCLDDYVFCYHLIAaYLKEKFDILK 296
PTPc-N20_13 cd14538
catalytic domain of tyrosine-protein phosphatase non-receptor type 20 and type 13; ...
833-970 1.12e-14

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: 74.33  E-value: 1.12e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45553601  833 YINAS---WLHGFRRLRdFIVTQHPMAHTIKDFWQMVWDHNAQtVVLLSSLD----DINFAQFWPD--EATPIESDHYRV 903
Cdd:cd14538    1 YINAShirIPVGGDTYH-YIACQGPLPNTTGDFWQMVWEQKSE-VIAMVTQDveggKVKCHRYWPDslNKPLICGGRLEV 78
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45553601  904 KFLNKTNKSDYVSRDFVIQSIQDDYELTVKMLHCPSWPEMSNPNS---IYDFIVDVHERCNDyrnGPIVI 970
Cdd:cd14538   79 SLEKYQSLQDFVIRRISLRDKETGEVHHITHLNFTTWPDHGTPQSadpLLRFIRYMRRIHNS---GPIVV 145
PHA02742 PHA02742
protein tyrosine phosphatase; Provisional
767-985 3.33e-14

protein tyrosine phosphatase; Provisional


Pssm-ID: 165109 [Multi-domain]  Cd Length: 303  Bit Score: 75.04  E-value: 3.33e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45553601   767 EQVEELKNCTPYLEQQYKNIIQ-FQPKDIHIASAMKqvNSIKNRGAIFPI-EGSRVHLTPKPGedGSDYINASWLHGFRR 844
Cdd:PHA02742   16 EQLIEESNLAEILKEEHEHIMQeIVAFSCNESLELK--NMKKCRYPDAPCfDRNRVILKIEDG--GDDFINASYVDGHNA 91
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45553601   845 LRDFIVTQHPMAHTIKDFWQMVWDHNAQTVVLLSSLDDINFAQFWPDEATPIESDHYRVKFLNKTNK----SDYVSRDFV 920
Cdd:PHA02742   92 KGRFICTQAPLEETALDFWQAIFQDQVRVIVMITKIMEDGKEACYPYWMPHERGKATHGEFKIKTKKiksfRNYAVTNLC 171
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 45553601   921 IQSIQDDYELTVKMLHCPSWPEMS---NPNSIYDFIVDVHERC----------NDYRNGPIVIVDRYGGAQACTFCAI 985
Cdd:PHA02742  172 LTDTNTGASLDIKHFAYEDWPHGGlprDPNKFLDFVLAVREADlkadvdikgeNIVKEPPILVHCSAGLDRAGAFCAI 249
PTPc-N21_14 cd14540
catalytic domain of tyrosine-protein phosphatase non-receptor type 21 and type 14; ...
833-965 1.47e-13

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: 71.33  E-value: 1.47e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45553601  833 YINASWLHGF--RRLRDFIVTQHPMAHTIKDFWQMVWDHNAQTVVLLSSLDD---INFAQFWPDEAtpIESD-----HYR 902
Cdd:cd14540    1 YINASHITATvgGKQRFYIAAQGPLQNTVGDFWQMVWEQGVYLVVMVTAEEEggrEKCFRYWPTLG--GEHDaltfgEYK 78
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 45553601  903 VKFLNKTNKSDYVSRDFVIQSIQDDYELTVKMLHCPSWPEMSNPNSIYDFIvDVHERCNDYRN 965
Cdd:cd14540   79 VSTKFSVSSGCYTTTGLRVKHTLSGQSRTVWHLQYTDWPDHGCPEDVSGFL-DFLEEINSVRR 140
PTPc-N14 cd14599
catalytic domain of tyrosine-protein phosphatase non-receptor type 14; Tyrosine-protein ...
782-958 1.67e-13

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: 72.72  E-value: 1.67e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45553601  782 QYKNIIQFQPKDIHIASAMKQvNSIKNR-GAIFPIEGSRVHLTPKPgEDGSDYINASWLHGFRRLRD--FIVTQHPMAHT 858
Cdd:cd14599   17 EYEQIPKKKADGVFTTATLPE-NAERNRiREVVPYEENRVELVPTK-ENNTGYINASHIKVTVGGEEwhYIATQGPLPHT 94
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45553601  859 IKDFWQMVWDHNAQTVVLLSSLDDINFAQ---FWPDEATPIESDHY---RVKFLNKTNKSDYVSRDFVIQSIQDDYELTV 932
Cdd:cd14599   95 CHDFWQMVWEQGVNVIAMVTAEEEGGRSKshrYWPKLGSKHSSATYgkfKVTTKFRTDSGCYATTGLKVKHLLSGQERTV 174
                        170       180
                 ....*....|....*....|....*.
gi 45553601  933 KMLHCPSWPEMSNPNSIYDFIVDVHE 958
Cdd:cd14599  175 WHLQYTDWPDHGCPEEVQGFLSYLEE 200
PTP_YopH-like cd14559
YopH and related bacterial protein tyrosine phosphatases; Yersinia outer protein H (YopH) ...
549-746 2.77e-13

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: 70.51  E-value: 2.77e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45553601  549 INANFIDGYQKgHAFIGTQGPLPDTFDCFWRMIWEQRVAIIVMITNLVERGRRKCDMYWPKDGveTYGVIQVKliEEEVM 628
Cdd:cd14559   18 LNANRVQIGNK-NVAIACQYPKNEQLEDHLKMLADNRTPCLVVLASNKDIQRKGLPPYFRQSG--TYGSVTVK--SKKTG 92
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45553601  629 STYTVRTLQIKHLKLKKKKQCNTEKL-VYqyHYTNWPDHGTPD---------------HPLPVLNFVKKSSAANPAEAGP 692
Cdd:cd14559   93 KDELVDGLKADMYNLKITDGNKTITIpVV--HVTNWPDHTAISseglkeladlvnksaEEKRNFYKSKGSSAINDKNKLL 170
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 45553601  693 IVVHCSAGVGRTGTYIVLDAMLKQIqqkNIVNVFGFLRHIRAQRN-FLVQTEEQY 746
Cdd:cd14559  171 PVIHCRAGVGRTGQLAAAMELNKSP---NNLSVEDIVSDMRTSRNgKMVQKDEQL 222
PTPc-N22_18_12 cd14542
catalytic domain of tyrosine-protein phosphatase non-receptor type 22, type 18 and type 12; ...
833-985 3.19e-13

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: 69.76  E-value: 3.19e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45553601  833 YINASWLHGFRRLRDFIVTQHPMAHTIKDFWQMVWDHNAQTVVLLS---SLDDINFAQFWPDEAtpiESDHYRVKFLNKT 909
Cdd:cd14542    1 YINANFIKGVSGSKAYIATQGPLPNTVLDFWRMIWEYNVQVIVMACrefEMGKKKCERYWPEEG---EEQLQFGPFKISL 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45553601  910 NKSDYVSRDFVIQSIQ---DDYELTVKMLHCPSWPEMSNPNSIyDFIVDVHERCNDYRNG---PIVIVDRYGGAQACTFC 983
Cdd:cd14542   78 EKEKRVGPDFLIRTLKvtfQKESRTVYQFHYTAWPDHGVPSSV-DPILDLVRLVRDYQGSedvPICVHCSAGCGRTGTIC 156

                 ..
gi 45553601  984 AI 985
Cdd:cd14542  157 AI 158
PTPc-N6 cd14606
catalytic domain of tyrosine-protein phosphatase non-receptor type 6; Tyrosine-protein ...
800-970 4.55e-13

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: 70.68  E-value: 4.55e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45553601  800 MKQVNSIKNR-GAIFPIEGSRVHLTPK-PGEDGSDYINASWLHGFRRLRD-----FIVTQHPMAHTIKDFWQMVWDHNAQ 872
Cdd:cd14606   14 QRPENKSKNRyKNILPFDHSRVILQGRdSNIPGSDYINANYVKNQLLGPDenaktYIASQGCLEATVNDFWQMAWQENSR 93
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45553601  873 TVVLLSSldDINFAQ-----FWPDEATPIESDHYRVKFLNKTNKSDYVSRDFVIqSIQDDYELTVKMLHCP--SWPEM-- 943
Cdd:cd14606   94 VIVMTTR--EVEKGRnkcvpYWPEVGMQRAYGPYSVTNCGEHDTTEYKLRTLQV-SPLDNGELIREIWHYQylSWPDHgv 170
                        170       180
                 ....*....|....*....|....*....
gi 45553601  944 -SNPNSIYDFIVDVHERCNDYRN-GPIVI 970
Cdd:cd14606  171 pSEPGGVLSFLDQINQRQESLPHaGPIIV 199
PTPc_plant_PTP1 cd17658
protein tyrosine phosphatase 1 from Arabidopsis thaliana and similar plant PTPs; Arabidopsis ...
833-1026 1.52e-12

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: 67.87  E-value: 1.52e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45553601  833 YINASWLH--GFRRLRDFIVTQHPMAHTIKDFWQMVWDHNAQTVVLLSSLDDIN----FAQFWPDEATPiESDHYRVKFL 906
Cdd:cd17658    1 YINASLVEtpASESLPKFIATQGPLPHTFEDFWEMVIQQRCPVIIMLTRLVDNYstakCADYFPAEENE-SREFGRISVT 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45553601  907 NKTNKSDYVS---RDFVIQSIQ-DDYELTVKMLHCPSWPEMSNPNSIYdFIVDVHER--CNDYRNGPIVIVDRYGGAQAC 980
Cdd:cd17658   80 NKKLKHSQHSitlRVLEVQYIEsEEPPLSVLHIQYPEWPDHGVPKDTR-SVRELLKRlyGIPPSAGPIVVHCSAGIGRTG 158
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|.
gi 45553601  981 TFCAISS-----LAIEMeycSTANVYQYAKLYHNKRPGVWTSSEDIRVIYN 1026
Cdd:cd17658  159 AYCTIHNtirriLEGDM---SAVDLSKTVRKFRSQRIGMVQTQDQYIFCYA 206
PTPc-N4 cd14601
catalytic domain of tyrosine-protein phosphatase non-receptor type 4; Tyrosine-protein ...
832-953 3.37e-12

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: 67.28  E-value: 3.37e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45553601  832 DYINASWLH----GFRRLRDFIVTQHPMAHTIKDFWQMVWDHNAQTVVLLSSLDD---INFAQFWPDEATPIESDHYRVK 904
Cdd:cd14601    1 DYINANYINmeipSSSIINRYIACQGPLPNTCSDFWQMTWEQGSSMVVMLTTQVErgrVKCHQYWPEPSGSSSYGGFQVT 80
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*....
gi 45553601  905 FLNKTNKSDYVSRDFVIQSIQDDYELTVKMLHCPSWPEMSNPNSIYDFI 953
Cdd:cd14601   81 CHSEEGNPAYVFREMTLTNLEKNESRPLTQIQYIAWPDHGVPDDSSDFL 129
PTPc-N20 cd14596
catalytic domain of tyrosine-protein phosphatase non-receptor type 20; Tyrosine-protein ...
833-970 7.45e-12

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: 65.92  E-value: 7.45e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45553601  833 YINASWLH---GFRRLRdFIVTQHPMAHTIKDFWQMVWDHNAQTVVLLS---SLDDINFAQFWPDEAT-PIESDHYRVkF 905
Cdd:cd14596    1 YINASYITmpvGEEELF-YIATQGPLPSTIDDFWQMVWENRSDVIAMMTrevERGKVKCHRYWPETLQePMELENYQL-R 78
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45553601  906 LNKTNKSDYvsrdFVIQSIQDDYELT-----VKMLHCPSWPEMSNPNSIYDFIVDVHERCNDYRNGPIVI 970
Cdd:cd14596   79 LENYQALQY----FIIRIIKLVEKETgenrlIKHLQFTTWPDHGTPQSSDQLVKFICYMRKVHNTGPIVV 144
PHA02738 PHA02738
hypothetical protein; Provisional
818-1000 9.75e-12

hypothetical protein; Provisional


Pssm-ID: 222923 [Multi-domain]  Cd Length: 320  Bit Score: 67.64  E-value: 9.75e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45553601   818 SRVHLtPKPGEDGsDYINASWLHGFRRLRDFIVTQHPMAHTIKDFWQMVWDHNAQTVVLLSSLDDINFAQ---FWPD-EA 893
Cdd:PHA02738   64 SRVIL-PAERNRG-DYINANYVDGFEYKKKFICGQAPTRQTCYDFYRMLWMEHVQIIVMLCKKKENGREKcfpYWSDvEQ 141
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45553601   894 TPIESDHYRVKFLNKTNKSDYVSRDFViqsIQDDYELTVKMLH--CPSWPEMSNPNSIYDFI----------VDVHErcN 961
Cdd:PHA02738  142 GSIRFGKFKITTTQVETHPHYVKSTLL---LTDGTSATQTVTHfnFTAWPDHDVPKNTSEFLnfvlevrqcqKELAQ--E 216
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*.
gi 45553601   962 DYRNG-------PIVIVDRYGGAQACTFCAISSLAIEMEYCSTANV 1000
Cdd:PHA02738  217 SLQIGhnrlqppPIVVHCNAGLGRTPCYCVVDISISRFDACATVSI 262
FN3 smart00060
Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, ...
171-271 2.02e-09

Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, fibronectin. The tenth fibronectin type III repeat contains a RGD cell recognition sequence in a flexible loop between 2 strands. Type III modules are present in both extracellular and intracellular proteins.


Pssm-ID: 214495 [Multi-domain]  Cd Length: 83  Bit Score: 55.31  E-value: 2.02e-09
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45553601     171 PSKPQNLTILDVSANSITMSWHPPKNQNGaiAGYHV-FHIHDNQTGVEIVKNSRNSVETliHFELQNLRefnyvfiwglf 249
Cdd:smart00060    1 PSPPSNLRVTDVTSTSVTLSWEPPPDDGI--TGYIVgYRVEYREEGSEWKEVNVTPSST--SYTLTGLK----------- 65
                            90       100
                    ....*....|....*....|..
gi 45553601     250 gvkgPYTDYRVIVKAFTTKNEG 271
Cdd:smart00060   66 ----PGTEYEFRVRAVNGAGEG 83
FN3 COG3401
Fibronectin type 3 domain [General function prediction only];
111-364 4.27e-09

Fibronectin type 3 domain [General function prediction only];


Pssm-ID: 442628 [Multi-domain]  Cd Length: 603  Bit Score: 60.79  E-value: 4.27e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45553601  111 PVLGTVATSIEQQDQPPDVPATTLAFANAFPVPVAGEmgngnGNYNDATPPYAAVDDNYVPSKPQNLTILDVSANSITMS 190
Cdd:COG3401  178 AAVATTSLTVTSTTLVDGGGDIEPGTTYYYRVAATDT-----GGESAPSNEVSVTTPTTPPSAPTGLTATADTPGSVTLS 252
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45553601  191 WHPpkNQNGAIAGYHVFHIHDNQTGVEIVKNSRNSveTLIHFELQNLREFNYVfiwglfgvkgpytdyrviVKAFTT-KN 269
Cdd:COG3401  253 WDP--VTESDATGYRVYRSNSGDGPFTKVATVTTT--SYTDTGLTNGTTYYYR------------------VTAVDAaGN 310
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45553601  270 EGEPSDQIAQRTDVGGPSAPAIVNLTCHSQESITIRWRRPYEfyNTIDFYII--KTRLAGQDThrdiRINASAKelETAM 347
Cdd:COG3401  311 ESAPSNVVSVTTDLTPPAAPSGLTATAVGSSSITLSWTASSD--ADVTGYNVyrSTSGGGTYT----KIAETVT--TTSY 382
                        250
                 ....*....|....*..
gi 45553601  348 ILQNLTTNSYYEVKVAA 364
Cdd:COG3401  383 TDTGLTPGTTYYYKVTA 399
FN3 cd00063
Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein ...
286-364 8.87e-09

Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein fibronectin. Its tenth fibronectin type III repeat contains an RGD cell recognition sequence in a flexible loop between 2 strands. Approximately 2% of all animal proteins contain the FN3 repeat; including extracellular and intracellular proteins, membrane spanning cytokine receptors, growth hormone receptors, tyrosine phosphatase receptors, and adhesion molecules. FN3-like domains are also found in bacterial glycosyl hydrolases.


Pssm-ID: 238020 [Multi-domain]  Cd Length: 93  Bit Score: 54.04  E-value: 8.87e-09
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 45553601  286 PSAPAIVNLTCHSQESITIRWRRPYEFYNTIDFYIIKTRLAGQDTHRDIRINASAkelETAMILQNLTTNSYYEVKVAA 364
Cdd:cd00063    1 PSPPTNLRVTDVTSTSVTLSWTPPEDDGGPITGYVVEYREKGSGDWKEVEVTPGS---ETSYTLTGLKPGTEYEFRVRA 76
PTP_DSP_cys cd14494
cys-based protein tyrosine phosphatase and dual-specificity phosphatase superfamily; This ...
691-751 3.17e-08

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: 53.12  E-value: 3.17e-08
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 45553601  691 GPIVVHCSAGVGRTGTYIVLDAMLKQiqqknIVNVFGFLRHIRAQRNF-LVQTEEQYIFLHD 751
Cdd:cd14494   57 EPVLVHCKAGVGRTGTLVACYLVLLG-----GMSAEEAVRIVRLIRPGgIPQTIEQLDFLIK 113
CDC14 COG2453
Protein-tyrosine phosphatase [Signal transduction mechanisms];
657-751 5.01e-08

Protein-tyrosine phosphatase [Signal transduction mechanisms];


Pssm-ID: 441989 [Multi-domain]  Cd Length: 140  Bit Score: 53.05  E-value: 5.01e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45553601  657 QYHYTNWPDHGTPDHP--LPVLNFVKKSSAANpaeaGPIVVHCSAGVGRTGT----YIVLDAM-LKQIqqknivnvfgfL 729
Cdd:COG2453   49 EYLHLPIPDFGAPDDEqlQEAVDFIDEALREG----KKVLVHCRGGIGRTGTvaaaYLVLLGLsAEEA-----------L 113
                         90       100
                 ....*....|....*....|..
gi 45553601  730 RHIRAQRNFLVQTEEQYIFLHD 751
Cdd:COG2453  114 ARVRAARPGAVETPAQRAFLER 135
PTPc-N21 cd14598
catalytic domain of tyrosine-protein phosphatase non-receptor type 21; Tyrosine-protein ...
833-958 3.16e-07

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: 52.67  E-value: 3.16e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45553601  833 YINAS----------WlhgfrrlrDFIVTQHPMAHTIKDFWQMVWDHNAQTVVLLSSLDDINFAQ---FWP---DEATPI 896
Cdd:cd14598    1 YINAShikvtvggkeW--------DYIATQGPLQNTCQDFWQMVWEQGVAIIAMVTAEEEGGREKsfrYWPrlgSRHNTV 72
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 45553601  897 ESDHYRVKFLNKTNKSDYVSRDFVIQSIQDDYELTVKMLHCPSWPEMSNPNSIYDFIVDVHE 958
Cdd:cd14598   73 TYGRFKITTRFRTDSGCYATTGLKIKHLLTGQERTVWHLQYTDWPEHGCPEDLKGFLSYLEE 134
FN3 smart00060
Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, ...
286-366 1.07e-05

Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, fibronectin. The tenth fibronectin type III repeat contains a RGD cell recognition sequence in a flexible loop between 2 strands. Type III modules are present in both extracellular and intracellular proteins.


Pssm-ID: 214495 [Multi-domain]  Cd Length: 83  Bit Score: 44.91  E-value: 1.07e-05
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45553601     286 PSAPAIVNLTCHSQESITIRWRRPYEfyNTIDFYIIKTRLAGQDTHRDiRINASAKELETAMILQNLTTNSYYEVKVAAA 365
Cdd:smart00060    1 PSPPSNLRVTDVTSTSVTLSWEPPPD--DGITGYIVGYRVEYREEGSE-WKEVNVTPSSTSYTLTGLKPGTEYEFRVRAV 77

                    .
gi 45553601     366 T 366
Cdd:smart00060   78 N 78
DSPc smart00195
Dual specificity phosphatase, catalytic domain;
688-735 2.09e-04

Dual specificity phosphatase, catalytic domain;


Pssm-ID: 214551 [Multi-domain]  Cd Length: 138  Bit Score: 42.65  E-value: 2.09e-04
                            10        20        30        40
                    ....*....|....*....|....*....|....*....|....*...
gi 45553601     688 AEAGPIVVHCSAGVGRTGTYIVldAMLKQIQQKNIVNVFGFLRHIRAQ 735
Cdd:smart00195   76 SKGGKVLVHCQAGVSRSATLII--AYLMKTRNMSLNDAYDFVKDRRPI 121
DUSP23 cd14504
dual specificity phosphatase 23; Dual specificity phosphatase 23 (DUSP23), also known as ...
676-745 2.09e-04

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: 42.65  E-value: 2.09e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 45553601  676 LNFVKKSSAANpaeaGPIVVHCSAGVGRTGT----YIVLDAMLKQIQQknivnvfgfLRHIRAQRNFLVQTEEQ 745
Cdd:cd14504   72 LDIVEEANAKN----EAVLVHCLAGKGRTGTmlacYLVKTGKISAVDA---------INEIRRIRPGSIETSEQ 132
fn3 pfam00041
Fibronectin type III domain;
287-366 2.50e-04

Fibronectin type III domain;


Pssm-ID: 394996 [Multi-domain]  Cd Length: 85  Bit Score: 40.86  E-value: 2.50e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45553601    287 SAPAIVNLTCHSQESITIRWRRPYEFYNTIDFYIIKTRLAG-QDTHRDIRINASakelETAMILQNLTTNSYYEVKVAAA 365
Cdd:pfam00041    1 SAPSNLTVTDVTSTSLTVSWTPPPDGNGPITGYEVEYRPKNsGEPWNEITVPGT----TTSVTLTGLKPGTEYEVRVQAV 76

                   .
gi 45553601    366 T 366
Cdd:pfam00041   77 N 77
PTPLP-like cd14495
Protein tyrosine phosphatase-like domains of phytases and similar domains; This subfamily ...
652-789 6.09e-04

Protein tyrosine phosphatase-like domains of phytases and similar domains; This subfamily contains the tandem protein tyrosine phosphatase (PTP)-like domains of protein tyrosine phosphatase-like phytases (PTPLPs) and similar domains including the PTP domain of Pseudomonas syringae tyrosine-protein phosphatase hopPtoD2. PTPLPs, also known as cysteine phytases, are one of four known classes of phytases, enzymes that degrade phytate (inositol hexakisphosphate [InsP(6)]) to less-phosphorylated myo-inositol derivatives. Phytate is the most abundant cellular inositol phosphate and plays important roles in a broad scope of cellular processes, including DNA repair, RNA processing and export, development, apoptosis, and pathogenicity. PTPLPs adopt a PTP fold, including the active-site signature sequence (CX5R(S/T)) and utilize a classical PTP reaction mechanism. However, these enzymes display no catalytic activity against classical PTP substrates due to several unique structural features that confer specificity for myo-inositol polyphosphates.


Pssm-ID: 350345  Cd Length: 278  Bit Score: 43.13  E-value: 6.09e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45553601  652 EKLVYQ--YHYTNW--PDHGTPDhPLPV---LNFVKkssaANPAEAGpIVVHCSAGVGRTGTYIVLDAMLKqiqqkNIVN 724
Cdd:cd14495  147 EELVKKkgAHYVRIaaTDHVWPD-DEEIdafVAFYR----SLPADAW-LHFHCRAGKGRTTTFMVMYDMLK-----NPKD 215
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 45553601  725 VFgfLRHIrAQRNFLVqteeqyiflhdalveaiasGETNLMAEQVEELKNCTPYLEQQYKNIIQF 789
Cdd:cd14495  216 VS--FDDI-IARQYLI-------------------GGNYLAYEVDKDKNWKRPYYEERAQFLQKF 258
PTP_PTPDC1 cd14506
protein tyrosine phosphatase domain of PTP domain-containing protein 1; protein tyrosine ...
655-751 7.63e-04

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: 42.34  E-value: 7.63e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45553601  655 VYQYHYtNWPDHGTPDhPLPVLNFVKKSSAAnPAEAGPIVVHCSAGVGRTGTYI--VLDAMLKQIQQKNIvnvfgflRHI 732
Cdd:cd14506   77 IYFYNF-GWKDYGVPS-LTTILDIVKVMAFA-LQEGGKVAVHCHAGLGRTGVLIacYLVYALRMSADQAI-------RLV 146
                         90
                 ....*....|....*....
gi 45553601  733 RAQRNFLVQTEEQYIFLHD 751
Cdd:cd14506  147 RSKRPNSIQTRGQVLCVRE 165
CDKN3-like cd14505
cyclin-dependent kinase inhibitor 3 and similar proteins; This family is composed of ...
693-751 1.97e-03

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: 40.32  E-value: 1.97e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 45553601  693 IVVHCSAGVGRTGT-----YIVLDAMLKQIQQKNIVnvfgflrhiRAQRNFLVQTEEQYIFLHD 751
Cdd:cd14505  109 VLIHCKGGLGRTGLiaaclLLELGDTLDPEQAIAAV---------RALRPGAIQTPKQENFLHQ 163
PTPlike_phytase pfam14566
Inositol hexakisphosphate; Inositol hexakisphosphate, often called phytate, is found in ...
656-715 3.39e-03

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: 39.60  E-value: 3.39e-03
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 45553601    656 YQYHYT-------NWPDHGTPDhplPVLNFVKkssaaNPAEAGPIVVHCSAGVGRTGTYIVLDAMLK 715
Cdd:pfam14566   99 PGVDYRripitdeKAPLEEDFD---ALISIVK-----DAPEDTALVFNCQMGRGRTTTAMVIADLVR 157
CDC14_C cd14499
C-terminal dual-specificity phosphatase domain of CDC14 family proteins; The cell division ...
688-713 4.46e-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: 39.36  E-value: 4.46e-03
                         10        20
                 ....*....|....*....|....*.
gi 45553601  688 AEAGPIVVHCSAGVGRTGTYIVLDAM 713
Cdd:cd14499  107 NEKGAIAVHCKAGLGRTGTLIACYLM 132
PTP_PTEN-like cd14497
protein tyrosine phosphatase-like domain of phosphatase and tensin homolog and similar ...
658-709 8.61e-03

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


Pssm-ID: 350347 [Multi-domain]  Cd Length: 160  Bit Score: 38.33  E-value: 8.61e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 45553601  658 YHYtNWPDHgtpdHPLPV---LNFVK------KSSAANPAeagpiVVHCSAGVGRTGTYIV 709
Cdd:cd14497   64 LHY-GFPDH----HPPPLgllLEIVDdidswlSEDPNNVA-----VVHCKAGKGRTGTVIC 114
 
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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