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Conserved domains on  [gi|23172565|gb|AAF56891|]
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protein tyrosine phosphatase 99A, isoform A [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 ...
533-736 3.05e-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: 3.05e-143
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23172565  533 YINANFIDGYQKGHAFIGTQGPLPDTFDCFWRMIWEQRVAIIVMITNLVERGRRKCDMYWPKDGVETYGVIQVKLIEEEV 612
Cdd:cd14549    1 YINANYVDGYNKARAYIATQGPLPSTFDDFWRMVWEQNSAIIVMITNLVERGRRKCDQYWPKEGTETYGNIQVTLLSTEV 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23172565  613 MSTYTVRTLQIKHLKLKKKKQCNTEKLVYQYHYTNWPDHGTPDHPLPVLNFVKKSSAANPAEAGPIVVHCSAGVGRTGTY 692
Cdd:cd14549   81 LATYTVRTFSLKNLKLKKVKGRSSERVVYQYHYTQWPDHGVPDYTLPVLSFVRKSSAANPPGAGPIVVHCSAGVGRTGTY 160
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....
gi 23172565  693 IVLDAMLKQIQQKNIVNVFGFLRHIRAQRNFLVQTEEQYIFLHD 736
Cdd:cd14549  161 IVIDSMLQQIQDKGTVNVFGFLKHIRTQRNYLVQTEEQYIFIHD 204
R5-PTP-2 cd14550
PTP-like domain of R5 subfamily receptor-type tyrosine-protein phosphatases, repeat 2; The R5 ...
818-1011 9.78e-102

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: 9.78e-102
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23172565  818 YINASWLHGFRRLRDFIVTQHPMAHTIKDFWQMVWDHNAQTVVLLSSLD-DINFAQFWPDEATPIESDHYRVKFLNKTNK 896
Cdd:cd14550    1 YINASYLQGYRRSNEFIITQHPLEHTIKDFWQMIWDHNSQTIVMLTDNElNEDEPIYWPTKEKPLECETFKVTLSGEDHS 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23172565  897 S-----DYVSRDFVIQSIQDDYELTVKMLHCPSWPEMSNP-NSIYDFIVDVHERCNDyRNGPIVIVDRYGGAQACTFCAI 970
Cdd:cd14550   81 ClsneiRLIVRDFILESTQDDYVLEVRQFQCPSWPNPCSPiHTVFELINTVQEWAQQ-RDGPIVVHDRYGGVQAATFCAL 159
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|.
gi 23172565  971 SSLAIEMEYCSTANVYQYAKLYHNKRPGVWTSSEDIRVIYN 1011
Cdd:cd14550  160 TTLHQQLEHESSVDVYQVAKLYHLMRPGVFTSKEDYQFLYK 200
fn3 pfam00041
Fibronectin type III domain;
172-259 2.01e-19

Fibronectin type III domain;


:

Pssm-ID: 394996 [Multi-domain]  Cd Length: 85  Bit Score: 84.00  E-value: 2.01e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23172565    172 SKPQNLTILDVSANSITMSWHPPKNQNGAIAGYHVFHIHDNQTGVEivkNSRNSVETLIHFELQNLRPYTDYRVIVKAFT 251
Cdd:pfam00041    1 SAPSNLTVTDVTSTSLTVSWTPPPDGNGPITGYEVEYRPKNSGEPW---NEITVPGTTTSVTLTGLKPGTEYEVRVQAVN 77

                   ....*...
gi 23172565    252 TKNEGEPS 259
Cdd:pfam00041   78 GGGEGPPS 85
FN3 super family cl27307
Fibronectin type 3 domain [General function prediction only];
111-349 2.35e-11

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: 68.11  E-value: 2.35e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23172565  111 PVLGTVATSIEQQDQPPDVPATTLAFANAFPVPVAGEmgngnGNYNDATPPYAAVDDNYVPSKPQNLTILDVSANSITMS 190
Cdd:COG3401  178 AAVATTSLTVTSTTLVDGGGDIEPGTTYYYRVAATDT-----GGESAPSNEVSVTTPTTPPSAPTGLTATADTPGSVTLS 252
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23172565  191 WHPpkNQNGAIAGYHVFHIHDNQTGVEIVKNSRNSvetliHFELQNLRPYTDYRVIVKAFTT-KNEGEPSDQIAQRTDVG 269
Cdd:COG3401  253 WDP--VTESDATGYRVYRSNSGDGPFTKVATVTTT-----SYTDTGLTNGTTYYYRVTAVDAaGNESAPSNVVSVTTDLT 325
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23172565  270 GPSAPAIVNLTCHSQESITIRWRRPYEfyNTIDFYII--KTRLAGQDThrdiRINASAKelETAMILQNLTTNSYYEVKV 347
Cdd:COG3401  326 PPAAPSGLTATAVGSSSITLSWTASSD--ADVTGYNVyrSTSGGGTYT----KIAETVT--TTSYTDTGLTPGTTYYYKV 397

                 ..
gi 23172565  348 AA 349
Cdd:COG3401  398 TA 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 ...
533-736 3.05e-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: 3.05e-143
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23172565  533 YINANFIDGYQKGHAFIGTQGPLPDTFDCFWRMIWEQRVAIIVMITNLVERGRRKCDMYWPKDGVETYGVIQVKLIEEEV 612
Cdd:cd14549    1 YINANYVDGYNKARAYIATQGPLPSTFDDFWRMVWEQNSAIIVMITNLVERGRRKCDQYWPKEGTETYGNIQVTLLSTEV 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23172565  613 MSTYTVRTLQIKHLKLKKKKQCNTEKLVYQYHYTNWPDHGTPDHPLPVLNFVKKSSAANPAEAGPIVVHCSAGVGRTGTY 692
Cdd:cd14549   81 LATYTVRTFSLKNLKLKKVKGRSSERVVYQYHYTQWPDHGVPDYTLPVLSFVRKSSAANPPGAGPIVVHCSAGVGRTGTY 160
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....
gi 23172565  693 IVLDAMLKQIQQKNIVNVFGFLRHIRAQRNFLVQTEEQYIFLHD 736
Cdd:cd14549  161 IVIDSMLQQIQDKGTVNVFGFLKHIRTQRNYLVQTEEQYIFIHD 204
PTPc smart00194
Protein tyrosine phosphatase, catalytic domain;
475-740 4.16e-117

Protein tyrosine phosphatase, catalytic domain;


Pssm-ID: 214550 [Multi-domain]  Cd Length: 259  Bit Score: 364.29  E-value: 4.16e-117
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23172565     475 GFSREYEAIQNECIsDDLPCEHSQHPENKRKNRYLNITAYDHSRVHLHPTPGQkkNLDYINANFIDGYQKGHAFIGTQGP 554
Cdd:smart00194    1 GLEEEFEKLDRLKP-DDESCTVAAFPENRDKNRYKDVLPYDHTRVKLKPPPGE--GSDYINASYIDGPNGPKAYIATQGP 77
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23172565     555 LPDTFDCFWRMIWEQRVAIIVMITNLVERGRRKCDMYWPKDGVE--TYGVIQVKLIEEEVMSTYTVRTLQIKHLklkkkk 632
Cdd:smart00194   78 LPSTVEDFWRMVWEQKVTVIVMLTELVEKGREKCAQYWPDEEGEplTYGDITVTLKSVEKVDDYTIRTLEVTNT------ 151
                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23172565     633 QCNTEKLVYQYHYTNWPDHGTPDHPLPVLNFVKKSSAANPAEAGPIVVHCSAGVGRTGTYIVLDAMLKQIQQKNIVNVFG 712
Cdd:smart00194  152 GCSETRTVTHYHYTNWPDHGVPESPESILDLIRAVRKSQSTSTGPIVVHCSAGVGRTGTFIAIDILLQQLEAGKEVDIFE 231
                           250       260
                    ....*....|....*....|....*...
gi 23172565     713 FLRHIRAQRNFLVQTEEQYIFLHDALVE 740
Cdd:smart00194  232 IVKELRSQRPGMVQTEEQYIFLYRAILE 259
Y_phosphatase pfam00102
Protein-tyrosine phosphatase;
502-740 8.49e-106

Protein-tyrosine phosphatase;


Pssm-ID: 459674 [Multi-domain]  Cd Length: 234  Bit Score: 332.67  E-value: 8.49e-106
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23172565    502 NKRKNRYLNITAYDHSRVHLHPTPGQKknlDYINANFIDGYQKGHAFIGTQGPLPDTFDCFWRMIWEQRVAIIVMITNLV 581
Cdd:pfam00102    1 NLEKNRYKDVLPYDHTRVKLTGDPGPS---DYINASYIDGYKKPKKYIATQGPLPNTVEDFWRMVWEEKVTIIVMLTELE 77
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23172565    582 ERGRRKCDMYWP--KDGVETYGVIQVKLI-EEEVMSTYTVRTLQIkhlklkKKKQCNTEKLVYQYHYTNWPDHGTPDHPL 658
Cdd:pfam00102   78 EKGREKCAQYWPeeEGESLEYGDFTVTLKkEKEDEKDYTVRTLEV------SNGGSEETRTVKHFHYTGWPDHGVPESPN 151
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23172565    659 PVLNFVKK-SSAANPAEAGPIVVHCSAGVGRTGTYIVLDAMLKQIQQKNIVNVFGFLRHIRAQRNFLVQTEEQYIFLHDA 737
Cdd:pfam00102  152 SLLDLLRKvRKSSLDGRSGPIVVHCSAGIGRTGTFIAIDIALQQLEAEGEVDIFQIVKELRSQRPGMVQTLEQYIFLYDA 231

                   ...
gi 23172565    738 LVE 740
Cdd:pfam00102  232 ILE 234
R5-PTP-2 cd14550
PTP-like domain of R5 subfamily receptor-type tyrosine-protein phosphatases, repeat 2; The R5 ...
818-1011 9.78e-102

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: 9.78e-102
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23172565  818 YINASWLHGFRRLRDFIVTQHPMAHTIKDFWQMVWDHNAQTVVLLSSLD-DINFAQFWPDEATPIESDHYRVKFLNKTNK 896
Cdd:cd14550    1 YINASYLQGYRRSNEFIITQHPLEHTIKDFWQMIWDHNSQTIVMLTDNElNEDEPIYWPTKEKPLECETFKVTLSGEDHS 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23172565  897 S-----DYVSRDFVIQSIQDDYELTVKMLHCPSWPEMSNP-NSIYDFIVDVHERCNDyRNGPIVIVDRYGGAQACTFCAI 970
Cdd:cd14550   81 ClsneiRLIVRDFILESTQDDYVLEVRQFQCPSWPNPCSPiHTVFELINTVQEWAQQ-RDGPIVVHDRYGGVQAATFCAL 159
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|.
gi 23172565  971 SSLAIEMEYCSTANVYQYAKLYHNKRPGVWTSSEDIRVIYN 1011
Cdd:cd14550  160 TTLHQQLEHESSVDVYQVAKLYHLMRPGVFTSKEDYQFLYK 200
PTPc smart00194
Protein tyrosine phosphatase, catalytic domain;
764-1015 1.52e-69

Protein tyrosine phosphatase, catalytic domain;


Pssm-ID: 214550 [Multi-domain]  Cd Length: 259  Bit Score: 233.71  E-value: 1.52e-69
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23172565     764 LEQQYKNIIQFQPKDIHIASAMKQVNSIKNR-GAIFPIEGSRVHLTPKPGEdGSDYINASWLHGFRRLRDFIVTQHPMAH 842
Cdd:smart00194    2 LEEEFEKLDRLKPDDESCTVAAFPENRDKNRyKDVLPYDHTRVKLKPPPGE-GSDYINASYIDGPNGPKAYIATQGPLPS 80
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23172565     843 TIKDFWQMVWDHNAQTVVLLSSLDD---INFAQFWPDEA-TPIESDHYRVKFLNKTNKSDYVSRDFVIQSIQDDYELTVK 918
Cdd:smart00194   81 TVEDFWRMVWEQKVTVIVMLTELVEkgrEKCAQYWPDEEgEPLTYGDITVTLKSVEKVDDYTIRTLEVTNTGCSETRTVT 160
                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23172565     919 MLHCPSWPEMSNPNS---IYDFIVDVHERCNDYrNGPIVIVDRYGGAQACTFCAISSLAIEMEYCSTANVYQYAKLYHNK 995
Cdd:smart00194  161 HYHYTNWPDHGVPESpesILDLIRAVRKSQSTS-TGPIVVHCSAGVGRTGTFIAIDILLQQLEAGKEVDIFEIVKELRSQ 239
                           250       260
                    ....*....|....*....|
gi 23172565     996 RPGVWTSSEDIRVIYNILSF 1015
Cdd:smart00194  240 RPGMVQTEEQYIFLYRAILE 259
Y_phosphatase pfam00102
Protein-tyrosine phosphatase;
789-1013 6.51e-68

Protein-tyrosine phosphatase;


Pssm-ID: 459674 [Multi-domain]  Cd Length: 234  Bit Score: 228.28  E-value: 6.51e-68
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23172565    789 NSIKNR-GAIFPIEGSRVHLTPKPGedGSDYINASWLHGFRRLRDFIVTQHPMAHTIKDFWQMVWDHNAQTVVLLSSLDD 867
Cdd:pfam00102    1 NLEKNRyKDVLPYDHTRVKLTGDPG--PSDYINASYIDGYKKPKKYIATQGPLPNTVEDFWRMVWEEKVTIIVMLTELEE 78
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23172565    868 IN---FAQFWPDEA-TPIESDHYRVKFLN-KTNKSDYVSRDFVIQSIQDDYELTVKMLHCPSWPEM---SNPNSIYDFIV 939
Cdd:pfam00102   79 KGrekCAQYWPEEEgESLEYGDFTVTLKKeKEDEKDYTVRTLEVSNGGSEETRTVKHFHYTGWPDHgvpESPNSLLDLLR 158
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 23172565    940 DVHERCNDYRNGPIVIVDRYGGAQACTFCAISSLAIEMEYCSTANVYQYAKLYHNKRPGVWTSSEDIRVIYNIL 1013
Cdd:pfam00102  159 KVRKSSLDGRSGPIVVHCSAGIGRTGTFIAIDIALQQLEAEGEVDIFQIVKELRSQRPGMVQTLEQYIFLYDAI 232
PHA02746 PHA02746
protein tyrosine phosphatase; Provisional
496-759 1.42e-47

protein tyrosine phosphatase; Provisional


Pssm-ID: 165113 [Multi-domain]  Cd Length: 323  Bit Score: 173.29  E-value: 1.42e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23172565   496 HSQHPENKRKNRYLNITAYDHSRVHLHpTPGQKKNLD-------------------YINANFIDGYQKGHAFIGTQGPLP 556
Cdd:PHA02746   45 HFLKKENLKKNRFHDIPCWDHSRVVIN-AHESLKMFDvgdsdgkkievtsednaenYIHANFVDGFKEANKFICAQGPKE 123
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23172565   557 DTFDCFWRMIWEQRVAIIVMITNlVERGRRKCDMYW--PKDGVETYGVIQVKLIEEEVMSTYTVRTLQIKHLKLkkkkqc 634
Cdd:PHA02746  124 DTSEDFFKLISEHESQVIVSLTD-IDDDDEKCFELWtkEEDSELAFGRFVAKILDIIEELSFTKTRLMITDKIS------ 196
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23172565   635 NTEKLVYQYHYTNWPDHGTPDHPLPVLNFV----------KKSSAANPAEAGPIVVHCSAGVGRTGTYIVLDAMLKQIQQ 704
Cdd:PHA02746  197 DTSREIHHFWFPDWPDNGIPTGMAEFLELInkvneeqaelIKQADNDPQTLGPIVVHCSAGIGRAGTFCAIDNALEQLEK 276
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 23172565   705 KNIVNVFGFLRHIRAQRNFLVQTEEQYIFLHDALVEAIasgetnlmaeqVEELKN 759
Cdd:PHA02746  277 EKEVCLGEIVLKIRKQRHSSVFLPEQYAFCYKALKYAI-----------IEEAKK 320
COG5599 COG5599
Protein tyrosine phosphatase [Signal transduction mechanisms];
496-734 1.94e-41

Protein tyrosine phosphatase [Signal transduction mechanisms];


Pssm-ID: 444335 [Multi-domain]  Cd Length: 282  Bit Score: 154.09  E-value: 1.94e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23172565  496 HSQHPENKRKNRYLNITAYDHSRVhlhptpgqKKNLDYINANFIDGYQKgHAFIGTQGPLPDTFDCFWRMIWEQRVAIIV 575
Cdd:COG5599   36 YLQNINGSPLNRFRDIQPYKETAL--------RANLGYLNANYIQVIGN-HRYIATQYPLEEQLEDFFQMLFDNNTPVLV 106
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23172565  576 MITNLVERGRRKCDM--YWPKDGVETYGVIQVKLIEEEVMST-YTVRTLQIKHLklkkkkQCNTEKL-VYQYHYTNWPDH 651
Cdd:COG5599  107 VLASDDEISKPKVKMpvYFRQDGEYGKYEVSSELTESIQLRDgIEARTYVLTIK------GTGQKKIeIPVLHVKNWPDH 180
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23172565  652 GTPD----HPLpvLNFVKKSSAANPAEAGPIVVHCSAGVGRTGTYIVLDAMLKQIQQKNI--VNVFGFLRHIRAQRNF-L 724
Cdd:COG5599  181 GAISaealKNL--ADLIDKKEKIKDPDKLLPVVHCRAGVGRTGTLIACLALSKSINALVQitLSVEEIVIDMRTSRNGgM 258
                        250
                 ....*....|
gi 23172565  725 VQTEEQYIFL 734
Cdd:COG5599  259 VQTSEQLDVL 268
PHA02747 PHA02747
protein tyrosine phosphatase; Provisional
759-1024 7.02e-24

protein tyrosine phosphatase; Provisional


Pssm-ID: 165114 [Multi-domain]  Cd Length: 312  Bit Score: 103.93  E-value: 7.02e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23172565   759 NCTPYLEQQYKNIIqFQPKDIHIASAMKQVNSIKNRGAIFPI-EGSRVHLTPKPGEDgSDYINASWLHGFRRLRDFIVTQ 837
Cdd:PHA02747   22 NCFGIIRDEHHQII-LKPFDGLIANFEKPENQPKNRYWDIPCwDHNRVILDSGGGST-SDYIHANWIDGFEDDKKFIATQ 99
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23172565   838 HPMAHTIKDFWQMVWDHNAQTVVLLSSLDDINFA----QFW-PDEATPIESDHYRVKFLNKTNKSDYVSRDFVIQSIQDD 912
Cdd:PHA02747  100 GPFAETCADFWKAVWQEHCSIIVMLTPTKGTNGEekcyQYWcLNEDGNIDMEDFRIETLKTSVRAKYILTLIEITDKILK 179
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23172565   913 YELTVKMLHCPSWPEMSNPNSIYDFI-----VDVHER-------CNDYRNGPIVIVDRYGGAQACTFCAISSLAIEMEYC 980
Cdd:PHA02747  180 DSRKISHFQCSEWFEDETPSDHPDFIkfikiIDINRKksgklfnPKDALLCPIVVHCSDGVGKTGIFCAVDICLNQLVKR 259
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*...
gi 23172565   981 STANVYQYAKLYHNKRPGVWTSSEDIRVI----YNILSFLPGNLNLLK 1024
Cdd:PHA02747  260 KAICLAKTAEKIREQRHAGIMNFDDYLFIqpgyEVLHYFLSKIKAIDK 307
fn3 pfam00041
Fibronectin type III domain;
172-259 2.01e-19

Fibronectin type III domain;


Pssm-ID: 394996 [Multi-domain]  Cd Length: 85  Bit Score: 84.00  E-value: 2.01e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23172565    172 SKPQNLTILDVSANSITMSWHPPKNQNGAIAGYHVFHIHDNQTGVEivkNSRNSVETLIHFELQNLRPYTDYRVIVKAFT 251
Cdd:pfam00041    1 SAPSNLTVTDVTSTSLTVSWTPPPDGNGPITGYEVEYRPKNSGEPW---NEITVPGTTTSVTLTGLKPGTEYEVRVQAVN 77

                   ....*...
gi 23172565    252 TKNEGEPS 259
Cdd:pfam00041   78 GGGEGPPS 85
FN3 cd00063
Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein ...
171-266 5.12e-19

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: 82.93  E-value: 5.12e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23172565  171 PSKPQNLTILDVSANSITMSWHPPKNQNGAIAGYHVFHIHDNQTGVEIVKNSRNSVEtliHFELQNLRPYTDYRVIVKAF 250
Cdd:cd00063    1 PSPPTNLRVTDVTSTSVTLSWTPPEDDGGPITGYVVEYREKGSGDWKEVEVTPGSET---SYTLTGLKPGTEYEFRVRAV 77
                         90
                 ....*....|....*.
gi 23172565  251 TTKNEGEPSDQIAQRT 266
Cdd:cd00063   78 NGGGESPPSESVTVTT 93
FN3 smart00060
Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, ...
171-256 5.93e-13

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: 65.33  E-value: 5.93e-13
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23172565     171 PSKPQNLTILDVSANSITMSWHPPKNQNGaiAGYHV-FHIHDNQTGVEIVKNSRNSVETliHFELQNLRPYTDYRVIVKA 249
Cdd:smart00060    1 PSPPSNLRVTDVTSTSVTLSWEPPPDDGI--TGYIVgYRVEYREEGSEWKEVNVTPSST--SYTLTGLKPGTEYEFRVRA 76

                    ....*..
gi 23172565     250 FTTKNEG 256
Cdd:smart00060   77 VNGAGEG 83
FN3 COG3401
Fibronectin type 3 domain [General function prediction only];
111-349 2.35e-11

Fibronectin type 3 domain [General function prediction only];


Pssm-ID: 442628 [Multi-domain]  Cd Length: 603  Bit Score: 68.11  E-value: 2.35e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23172565  111 PVLGTVATSIEQQDQPPDVPATTLAFANAFPVPVAGEmgngnGNYNDATPPYAAVDDNYVPSKPQNLTILDVSANSITMS 190
Cdd:COG3401  178 AAVATTSLTVTSTTLVDGGGDIEPGTTYYYRVAATDT-----GGESAPSNEVSVTTPTTPPSAPTGLTATADTPGSVTLS 252
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23172565  191 WHPpkNQNGAIAGYHVFHIHDNQTGVEIVKNSRNSvetliHFELQNLRPYTDYRVIVKAFTT-KNEGEPSDQIAQRTDVG 269
Cdd:COG3401  253 WDP--VTESDATGYRVYRSNSGDGPFTKVATVTTT-----SYTDTGLTNGTTYYYRVTAVDAaGNESAPSNVVSVTTDLT 325
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23172565  270 GPSAPAIVNLTCHSQESITIRWRRPYEfyNTIDFYII--KTRLAGQDThrdiRINASAKelETAMILQNLTTNSYYEVKV 347
Cdd:COG3401  326 PPAAPSGLTATAVGSSSITLSWTASSD--ADVTGYNVyrSTSGGGTYT----KIAETVT--TTSYTDTGLTPGTTYYYKV 397

                 ..
gi 23172565  348 AA 349
Cdd:COG3401  398 TA 399
FN3 cd00063
Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein ...
271-349 8.84e-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: 8.84e-09
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 23172565  271 PSAPAIVNLTCHSQESITIRWRRPYEFYNTIDFYIIKTRLAGQDTHRDIRINASAkelETAMILQNLTTNSYYEVKVAA 349
Cdd:cd00063    1 PSPPTNLRVTDVTSTSVTLSWTPPEDDGGPITGYVVEYREKGSGDWKEVEVTPGS---ETSYTLTGLKPGTEYEFRVRA 76
FN3 smart00060
Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, ...
271-351 1.05e-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: 1.05e-05
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23172565     271 PSAPAIVNLTCHSQESITIRWRRPYEfyNTIDFYIIKTRLAGQDTHRDiRINASAKELETAMILQNLTTNSYYEVKVAAA 350
Cdd:smart00060    1 PSPPSNLRVTDVTSTSVTLSWEPPPD--DGITGYIVGYRVEYREEGSE-WKEVNVTPSSTSYTLTGLKPGTEYEFRVRAV 77

                    .
gi 23172565     351 T 351
Cdd:smart00060   78 N 78
fn3 pfam00041
Fibronectin type III domain;
272-351 2.49e-04

Fibronectin type III domain;


Pssm-ID: 394996 [Multi-domain]  Cd Length: 85  Bit Score: 40.86  E-value: 2.49e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23172565    272 SAPAIVNLTCHSQESITIRWRRPYEFYNTIDFYIIKTRLAG-QDTHRDIRINASakelETAMILQNLTTNSYYEVKVAAA 350
Cdd:pfam00041    1 SAPSNLTVTDVTSTSLTVSWTPPPDGNGPITGYEVEYRPKNsGEPWNEITVPGT----TTSVTLTGLKPGTEYEVRVQAV 76

                   .
gi 23172565    351 T 351
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 ...
533-736 3.05e-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: 3.05e-143
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23172565  533 YINANFIDGYQKGHAFIGTQGPLPDTFDCFWRMIWEQRVAIIVMITNLVERGRRKCDMYWPKDGVETYGVIQVKLIEEEV 612
Cdd:cd14549    1 YINANYVDGYNKARAYIATQGPLPSTFDDFWRMVWEQNSAIIVMITNLVERGRRKCDQYWPKEGTETYGNIQVTLLSTEV 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23172565  613 MSTYTVRTLQIKHLKLKKKKQCNTEKLVYQYHYTNWPDHGTPDHPLPVLNFVKKSSAANPAEAGPIVVHCSAGVGRTGTY 692
Cdd:cd14549   81 LATYTVRTFSLKNLKLKKVKGRSSERVVYQYHYTQWPDHGVPDYTLPVLSFVRKSSAANPPGAGPIVVHCSAGVGRTGTY 160
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....
gi 23172565  693 IVLDAMLKQIQQKNIVNVFGFLRHIRAQRNFLVQTEEQYIFLHD 736
Cdd:cd14549  161 IVIDSMLQQIQDKGTVNVFGFLKHIRTQRNYLVQTEEQYIFIHD 204
R-PTPc-G-1 cd17667
catalytic domain of receptor-type tyrosine-protein phosphatase G, repeat 1; Receptor-type ...
476-742 7.23e-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: 385.54  E-value: 7.23e-125
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23172565  476 FSREYEAIQnECISD-DLPCEHSQHPENKRKNRYLNITAYDHSRVHLHPTPGQ-KKNLDYINANFIDGYQKGHAFIGTQG 553
Cdd:cd17667    1 FSEDFEEVQ-RCTADmNITAEHSNHPDNKHKNRYINILAYDHSRVKLRPLPGKdSKHSDYINANYVDGYNKAKAYIATQG 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23172565  554 PLPDTFDCFWRMIWEQRVAIIVMITNLVERGRRKCDMYWPKDGVETYGVIQVKLIEEEVMSTYTVRTLQIKHLKLKKKKQ 633
Cdd:cd17667   80 PLKSTFEDFWRMIWEQNTGIIVMITNLVEKGRRKCDQYWPTENSEEYGNIIVTLKSTKIHACYTVRRFSIRNTKVKKGQK 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23172565  634 CNT-----EKLVYQYHYTNWPDHGTPDHPLPVLNFVKKSSAANPAEAGPIVVHCSAGVGRTGTYIVLDAMLKQIQQKNIV 708
Cdd:cd17667  160 GNPkgrqnERTVIQYHYTQWPDMGVPEYALPVLTFVRRSSAARTPEMGPVLVHCSAGVGRTGTYIVIDSMLQQIKDKSTV 239
                        250       260       270
                 ....*....|....*....|....*....|....
gi 23172565  709 NVFGFLRHIRAQRNFLVQTEEQYIFLHDALVEAI 742
Cdd:cd17667  240 NVLGFLKHIRTQRNYLVQTEEQYIFIHDALLEAI 273
R-PTPc-LAR-1 cd14553
catalytic domain of LAR family receptor-type tyrosine-protein phosphatases, repeat 1; The LAR ...
502-744 9.56e-118

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: 9.56e-118
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23172565  502 NKRKNRYLNITAYDHSRVHLHPTPGQKKNlDYINANFIDGYQKGHAFIGTQGPLPDTFDCFWRMIWEQRVAIIVMITNLV 581
Cdd:cd14553    3 NKPKNRYANVIAYDHSRVILQPIEGVPGS-DYINANYCDGYRKQNAYIATQGPLPETFGDFWRMVWEQRSATIVMMTKLE 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23172565  582 ERGRRKCDMYWPKDGVETYGVIQVKLIEEEVMSTYTVRTLQIKHLKlkkkkqCNTEKLVYQYHYTNWPDHGTPDHPLPVL 661
Cdd:cd14553   82 ERSRVKCDQYWPTRGTETYGLIQVTLLDTVELATYTVRTFALHKNG------SSEKREVRQFQFTAWPDHGVPEHPTPFL 155
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23172565  662 NFVKKSSAANPAEAGPIVVHCSAGVGRTGTYIVLDAMLKQIQQKNIVNVFGFLRHIRAQRNFLVQTEEQYIFLHDALVEA 741
Cdd:cd14553  156 AFLRRVKACNPPDAGPIVVHCSAGVGRTGCFIVIDSMLERIKHEKTVDIYGHVTCLRAQRNYMVQTEDQYIFIHDALLEA 235

                 ...
gi 23172565  742 IAS 744
Cdd:cd14553  236 VTC 238
PTPc smart00194
Protein tyrosine phosphatase, catalytic domain;
475-740 4.16e-117

Protein tyrosine phosphatase, catalytic domain;


Pssm-ID: 214550 [Multi-domain]  Cd Length: 259  Bit Score: 364.29  E-value: 4.16e-117
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23172565     475 GFSREYEAIQNECIsDDLPCEHSQHPENKRKNRYLNITAYDHSRVHLHPTPGQkkNLDYINANFIDGYQKGHAFIGTQGP 554
Cdd:smart00194    1 GLEEEFEKLDRLKP-DDESCTVAAFPENRDKNRYKDVLPYDHTRVKLKPPPGE--GSDYINASYIDGPNGPKAYIATQGP 77
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23172565     555 LPDTFDCFWRMIWEQRVAIIVMITNLVERGRRKCDMYWPKDGVE--TYGVIQVKLIEEEVMSTYTVRTLQIKHLklkkkk 632
Cdd:smart00194   78 LPSTVEDFWRMVWEQKVTVIVMLTELVEKGREKCAQYWPDEEGEplTYGDITVTLKSVEKVDDYTIRTLEVTNT------ 151
                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23172565     633 QCNTEKLVYQYHYTNWPDHGTPDHPLPVLNFVKKSSAANPAEAGPIVVHCSAGVGRTGTYIVLDAMLKQIQQKNIVNVFG 712
Cdd:smart00194  152 GCSETRTVTHYHYTNWPDHGVPESPESILDLIRAVRKSQSTSTGPIVVHCSAGVGRTGTFIAIDILLQQLEAGKEVDIFE 231
                           250       260
                    ....*....|....*....|....*...
gi 23172565     713 FLRHIRAQRNFLVQTEEQYIFLHDALVE 740
Cdd:smart00194  232 IVKELRSQRPGMVQTEEQYIFLYRAILE 259
Y_phosphatase pfam00102
Protein-tyrosine phosphatase;
502-740 8.49e-106

Protein-tyrosine phosphatase;


Pssm-ID: 459674 [Multi-domain]  Cd Length: 234  Bit Score: 332.67  E-value: 8.49e-106
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23172565    502 NKRKNRYLNITAYDHSRVHLHPTPGQKknlDYINANFIDGYQKGHAFIGTQGPLPDTFDCFWRMIWEQRVAIIVMITNLV 581
Cdd:pfam00102    1 NLEKNRYKDVLPYDHTRVKLTGDPGPS---DYINASYIDGYKKPKKYIATQGPLPNTVEDFWRMVWEEKVTIIVMLTELE 77
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23172565    582 ERGRRKCDMYWP--KDGVETYGVIQVKLI-EEEVMSTYTVRTLQIkhlklkKKKQCNTEKLVYQYHYTNWPDHGTPDHPL 658
Cdd:pfam00102   78 EKGREKCAQYWPeeEGESLEYGDFTVTLKkEKEDEKDYTVRTLEV------SNGGSEETRTVKHFHYTGWPDHGVPESPN 151
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23172565    659 PVLNFVKK-SSAANPAEAGPIVVHCSAGVGRTGTYIVLDAMLKQIQQKNIVNVFGFLRHIRAQRNFLVQTEEQYIFLHDA 737
Cdd:pfam00102  152 SLLDLLRKvRKSSLDGRSGPIVVHCSAGIGRTGTFIAIDIALQQLEAEGEVDIFQIVKELRSQRPGMVQTLEQYIFLYDA 231

                   ...
gi 23172565    738 LVE 740
Cdd:pfam00102  232 ILE 234
R5-PTP-2 cd14550
PTP-like domain of R5 subfamily receptor-type tyrosine-protein phosphatases, repeat 2; The R5 ...
818-1011 9.78e-102

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: 9.78e-102
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23172565  818 YINASWLHGFRRLRDFIVTQHPMAHTIKDFWQMVWDHNAQTVVLLSSLD-DINFAQFWPDEATPIESDHYRVKFLNKTNK 896
Cdd:cd14550    1 YINASYLQGYRRSNEFIITQHPLEHTIKDFWQMIWDHNSQTIVMLTDNElNEDEPIYWPTKEKPLECETFKVTLSGEDHS 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23172565  897 S-----DYVSRDFVIQSIQDDYELTVKMLHCPSWPEMSNP-NSIYDFIVDVHERCNDyRNGPIVIVDRYGGAQACTFCAI 970
Cdd:cd14550   81 ClsneiRLIVRDFILESTQDDYVLEVRQFQCPSWPNPCSPiHTVFELINTVQEWAQQ-RDGPIVVHDRYGGVQAATFCAL 159
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|.
gi 23172565  971 SSLAIEMEYCSTANVYQYAKLYHNKRPGVWTSSEDIRVIYN 1011
Cdd:cd14550  160 TTLHQQLEHESSVDVYQVAKLYHLMRPGVFTSKEDYQFLYK 200
R-PTPc-F-1 cd14626
catalytic domain of receptor-type tyrosine-protein phosphatase F, repeat 1; Receptor-type ...
459-742 6.25e-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: 6.25e-101
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23172565  459 NEFAKHVASLHADGDIGFSREYEAIQNeciSDDLPCEHSQHPENKRKNRYLNITAYDHSRVHLHPTPGQKKNlDYINANF 538
Cdd:cd14626    1 SDLADNIERLKANDGLKFSQEYESIDP---GQQFTWENSNLEVNKPKNRYANVIAYDHSRVILTSVDGVPGS-DYINANY 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23172565  539 IDGYQKGHAFIGTQGPLPDTFDCFWRMIWEQRVAIIVMITNLVERGRRKCDMYWPKDGVETYGVIQVKLIEEEVMSTYTV 618
Cdd:cd14626   77 IDGYRKQNAYIATQGPLPETLSDFWRMVWEQRTATIVMMTRLEEKSRVKCDQYWPIRGTETYGMIQVTLLDTVELATYSV 156
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23172565  619 RTLQIKHLKLkkkkqcNTEKLVYQYHYTNWPDHGTPDHPLPVLNFVKKSSAANPAEAGPIVVHCSAGVGRTGTYIVLDAM 698
Cdd:cd14626  157 RTFALYKNGS------SEKREVRQFQFMAWPDHGVPEYPTPILAFLRRVKACNPPDAGPMVVHCSAGVGRTGCFIVIDAM 230
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....
gi 23172565  699 LKQIQQKNIVNVFGFLRHIRAQRNFLVQTEEQYIFLHDALVEAI 742
Cdd:cd14626  231 LERMKHEKTVDIYGHVTCMRSQRNYMVQTEDQYIFIHEALLEAA 274
R-PTPc-D-1 cd14624
catalytic domain of receptor-type tyrosine-protein phosphatase D, repeat 1; Receptor-type ...
456-745 4.44e-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: 313.98  E-value: 4.44e-98
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23172565  456 VPVNEFAKHVASLHADGDIGFSREYEAIQNeciSDDLPCEHSQHPENKRKNRYLNITAYDHSRVHLHPTPGQKKNlDYIN 535
Cdd:cd14624    4 IPILELADHIERLKANDNLKFSQEYESIDP---GQQFTWEHSNLEVNKPKNRYANVIAYDHSRVLLSAIEGIPGS-DYIN 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23172565  536 ANFIDGYQKGHAFIGTQGPLPDTFDCFWRMIWEQRVAIIVMITNLVERGRRKCDMYWPKDGVETYGVIQVKLIEEEVMST 615
Cdd:cd14624   80 ANYIDGYRKQNAYIATQGALPETFGDFWRMIWEQRSATVVMMTKLEERSRVKCDQYWPSRGTETYGLIQVTLLDTVELAT 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23172565  616 YTVRTLQIKHLKLkkkkqcNTEKLVYQYHYTNWPDHGTPDHPLPVLNFVKKSSAANPAEAGPIVVHCSAGVGRTGTYIVL 695
Cdd:cd14624  160 YCVRTFALYKNGS------SEKREVRQFQFTAWPDHGVPEHPTPFLAFLRRVKTCNPPDAGPMVVHCSAGVGRTGCFIVI 233
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|
gi 23172565  696 DAMLKQIQQKNIVNVFGFLRHIRAQRNFLVQTEEQYIFLHDALVEAIASG 745
Cdd:cd14624  234 DAMLERIKHEKTVDIYGHVTLMRAQRNYMVQTEDQYIFIHDALLEAVTCG 283
R-PTPc-Z-1 cd17668
catalytic domain of receptor-type tyrosine-protein phosphatase Z, repeat 1; Receptor-type ...
533-739 1.59e-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: 309.60  E-value: 1.59e-97
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23172565  533 YINANFIDGYQKGHAFIGTQGPLPDTFDCFWRMIWEQRVAIIVMITNLVERGRRKCDMYWPKDGVETYGVIQVKLIEEEV 612
Cdd:cd17668    1 YINANYVDGYNKPKAYIAAQGPLKSTAEDFWRMIWEHNVEVIVMITNLVEKGRRKCDQYWPADGSEEYGNFLVTQKSVQV 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23172565  613 MSTYTVRTLQIKHLKLKKKKQC--NTEKLVYQYHYTNWPDHGTPDHPLPVLNFVKKSSAANPAEAGPIVVHCSAGVGRTG 690
Cdd:cd17668   81 LAYYTVRNFTLRNTKIKKGSQKgrPSGRVVTQYHYTQWPDMGVPEYTLPVLTFVRKASYAKRHAVGPVVVHCSAGVGRTG 160
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*....
gi 23172565  691 TYIVLDAMLKQIQQKNIVNVFGFLRHIRAQRNFLVQTEEQYIFLHDALV 739
Cdd:cd17668  161 TYIVLDSMLQQIQHEGTVNIFGFLKHIRSQRNYLVQTEEQYVFIHDALV 209
R-PTPc-S-1 cd14625
catalytic domain of receptor-type tyrosine-protein phosphatase S, repeat 1; Receptor-type ...
456-743 6.40e-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: 310.87  E-value: 6.40e-97
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23172565  456 VPVNEFAKHVASLHADGDIGFSREYEAIQNeciSDDLPCEHSQHPENKRKNRYLNITAYDHSRVHLHPTPGQKKNlDYIN 535
Cdd:cd14625    4 IPISELAEHTERLKANDNLKLSQEYESIDP---GQQFTWEHSNLEVNKPKNRYANVIAYDHSRVILQPIEGIMGS-DYIN 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23172565  536 ANFIDGYQKGHAFIGTQGPLPDTFDCFWRMIWEQRVAIIVMITNLVERGRRKCDMYWPKDGVETYGVIQVKLIEEEVMST 615
Cdd:cd14625   80 ANYIDGYRKQNAYIATQGPLPETFGDFWRMVWEQRSATVVMMTKLEEKSRIKCDQYWPSRGTETYGMIQVTLLDTIELAT 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23172565  616 YTVRTLQIKHLKLkkkkqcNTEKLVYQYHYTNWPDHGTPDHPLPVLNFVKKSSAANPAEAGPIVVHCSAGVGRTGTYIVL 695
Cdd:cd14625  160 FCVRTFSLHKNGS------SEKREVRQFQFTAWPDHGVPEYPTPFLAFLRRVKTCNPPDAGPIVVHCSAGVGRTGCFIVI 233
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*...
gi 23172565  696 DAMLKQIQQKNIVNVFGFLRHIRAQRNFLVQTEEQYIFLHDALVEAIA 743
Cdd:cd14625  234 DAMLERIKHEKTVDIYGHVTLMRSQRNYMVQTEDQYSFIHDALLEAVA 281
PTPc cd00047
catalytic domain of protein tyrosine phosphatases; Protein tyrosine phosphatases (PTP, EC 3.1. ...
533-736 2.29e-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: 289.57  E-value: 2.29e-90
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23172565  533 YINANFIDGYQKGHAFIGTQGPLPDTFDCFWRMIWEQRVAIIVMITNLVERGRRKCDMYWPKDGVET--YGVIQVKLIEE 610
Cdd:cd00047    1 YINASYIDGYRGPKEYIATQGPLPNTVEDFWRMVWEQKVSVIVMLTNLVEKGREKCERYWPEEGGKPleYGDITVTLVSE 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23172565  611 EVMSTYTVRTLQIKHLklkkkkQCNTEKLVYQYHYTNWPDHGTPDHPLPVLNFVKKSSAANPAEAGPIVVHCSAGVGRTG 690
Cdd:cd00047   81 EELSDYTIRTLELSPK------GCSESREVTHLHYTGWPDHGVPSSPEDLLALVRRVRKEARKPNGPIVVHCSAGVGRTG 154
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*.
gi 23172565  691 TYIVLDAMLKQIQQKNIVNVFGFLRHIRAQRNFLVQTEEQYIFLHD 736
Cdd:cd00047  155 TFIAIDILLERLEAEGEVDVFEIVKALRKQRPGMVQTLEQYEFIYE 200
R3-PTPc cd14548
catalytic domain of R3 subfamily receptor-type tyrosine-protein phosphatases and similar ...
507-735 3.54e-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: 3.54e-87
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23172565  507 RYLNITAYDHSRVHLHPTPGQKKNlDYINANFIDGYQKGHAFIGTQGPLPDTFDCFWRMIWEQRVAIIVMITNLVERGRR 586
Cdd:cd14548    1 RYTNILPYDHSRVKLIPINEEEGS-DYINANYIPGYNSPREFIATQGPLPGTKDDFWRMVWEQNSHTIVMLTQCMEKGRV 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23172565  587 KCDMYWPKDGVET-YGVIQVKLIEEEVMSTYTVRTLQIkhlklkkkkqCNTEK--LVYQYHYTNWPDHGTPDHPLPVLNF 663
Cdd:cd14548   80 KCDHYWPFDQDPVyYGDITVTMLSESVLPDWTIREFKL----------ERGDEvrSVRQFHFTAWPDHGVPEAPDSLLRF 149
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 23172565  664 VKKSSAANPAEAGPIVVHCSAGVGRTGTYIVLDAMLKQIQQKNIVNVFGFLRHIRAQRNFLVQTEEQYIFLH 735
Cdd:cd14548  150 VRLVRDYIKQEKGPTIVHCSAGVGRTGTFIALDRLLQQIESEDYVDIFGIVYDLRKHRPLMVQTEAQYIFLH 221
PTPc-N9 cd14543
catalytic domain of tyrosine-protein phosphatase non-receptor type 9; Tyrosine-protein ...
475-735 5.43e-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: 5.43e-85
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23172565  475 GFSREYEAIQNECISDDLPCehSQHPENKRKNRYLNITAYDHSRVHLhPTPGQKKNLDYINANFIDGYQKGHAFIGTQGP 554
Cdd:cd14543    4 GIYEEYEDIRREPPAGTFLC--SLAPANQEKNRYGDVLCLDQSRVKL-PKRNGDERTDYINANFMDGYKQKNAYIATQGP 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23172565  555 LPDTFDCFWRMIWEQRVAIIVMITNLVERGRRKCDMYWP--KDGVETYGVIQVKLIEEEVMSTYTVRTLQIkhlklkKKK 632
Cdd:cd14543   81 LPKTYSDFWRMVWEQKVLVIVMTTRVVERGRVKCGQYWPleEGSSLRYGDLTVTNLSVENKEHYKKTTLEI------HNT 154
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23172565  633 QCNTEKLVYQYHYTNWPDHGTPDHPLPVLNF-----------VKKSSAANPAEAG--PIVVHCSAGVGRTGTYIVLDAML 699
Cdd:cd14543  155 ETDESRQVTHFQFTSWPDFGVPSSAAALLDFlgevrqqqalaVKAMGDRWKGHPPgpPIVVHCSAGIGRTGTFCTLDICL 234
                        250       260       270
                 ....*....|....*....|....*....|....*.
gi 23172565  700 KQIQQKNIVNVFGFLRHIRAQRNFLVQTEEQYIFLH 735
Cdd:cd14543  235 SQLEDVGTLNVMQTVRRMRTQRAFSIQTPDQYYFCY 270
R-PTPc-A-1 cd14621
catalytic domain of receptor-type tyrosine-protein phosphatase A, repeat 1; Receptor-type ...
456-749 3.68e-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: 3.68e-83
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23172565  456 VPVNEFAKHVASLHADGDIGFSREYEAIQNECISDDlpCEHSQHPENKRKNRYLNITAYDHSRVHLHPTPGQKKNlDYIN 535
Cdd:cd14621    8 LPVDKLEEEINRRMADDNKLFREEFNALPACPIQAT--CEAASKEENKEKNRYVNILPYDHSRVHLTPVEGVPDS-DYIN 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23172565  536 ANFIDGYQKGHAFIGTQGPLPDTFDCFWRMIWEQRVAIIVMITNLVERGRRKCDMYWPKDGVETYGVIQVKLIEEEVMST 615
Cdd:cd14621   85 ASFINGYQEKNKFIAAQGPKEETVNDFWRMIWEQNTATIVMVTNLKERKECKCAQYWPDQGCWTYGNIRVSVEDVTVLVD 164
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23172565  616 YTVRTLQIKHLKLKKKKQcnTEKLVYQYHYTNWPDHGTPDHPLPVLNFVKKSSAANPAEAGPIVVHCSAGVGRTGTYIVL 695
Cdd:cd14621  165 YTVRKFCIQQVGDVTNKK--PQRLITQFHFTSWPDFGVPFTPIGMLKFLKKVKNCNPQYAGAIVVHCSAGVGRTGTFIVI 242
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....
gi 23172565  696 DAMLKQIQQKNIVNVFGFLRHIRAQRNFLVQTEEQYIFLHDALVEAIASGETNL 749
Cdd:cd14621  243 DAMLDMMHAERKVDVYGFVSRIRAQRCQMVQTDMQYVFIYQALLEHYLYGDTEL 296
R-PTPc-M-1 cd14633
catalytic domain of receptor-type tyrosine-protein phosphatase M, repeat 1; Receptor-type ...
460-741 4.07e-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: 4.07e-79
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23172565  460 EFAKHVASLHADGDIGFSREYEAIQNeciSDDLPCEHSQHPENKRKNRYLNITAYDHSRVHLHPTPGQKkNLDYINANFI 539
Cdd:cd14633    1 DLLQHITQMKCAEGYGFKEEYESFFE---GQSAPWDSAKKDENRMKNRYGNIIAYDHSRVRLQPIEGET-SSDYINGNYI 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23172565  540 DGYQKGHAFIGTQGPLPDTFDCFWRMIWEQRVAIIVMITNLVERGRRKCDMYWPKDgVETYGVIQVKLIEEEVMSTYTVR 619
Cdd:cd14633   77 DGYHRPNHYIATQGPMQETIYDFWRMVWHENTASIIMVTNLVEVGRVKCCKYWPDD-TEIYKDIKVTLIETELLAEYVIR 155
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23172565  620 TLQIKHLKLKKKKQcnteklVYQYHYTNWPDHGTPDHPLPVLNFVKKSSAANPAEAGPIVVHCSAGVGRTGTYIVLDAML 699
Cdd:cd14633  156 TFAVEKRGVHEIRE------IRQFHFTGWPDHGVPYHATGLLGFVRQVKSKSPPNAGPLVVHCSAGAGRTGCFIVIDIML 229
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|..
gi 23172565  700 KQIQQKNIVNVFGFLRHIRAQRNFLVQTEEQYIFLHDALVEA 741
Cdd:cd14633  230 DMAEREGVVDIYNCVRELRSRRVNMVQTEEQYVFIHDAILEA 271
R-PTPc-E-1 cd14620
catalytic domain of receptor-type tyrosine-protein phosphatase E, repeat 1; Receptor-type ...
508-740 7.79e-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: 7.79e-78
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23172565  508 YLNITAYDHSRVHLHPTPGQKKNlDYINANFIDGYQKGHAFIGTQGPLPDTFDCFWRMIWEQRVAIIVMITNLVERGRRK 587
Cdd:cd14620    1 YPNILPYDHSRVILSQLDGIPCS-DYINASYIDGYKEKNKFIAAQGPKQETVNDFWRMVWEQKSATIVMLTNLKERKEEK 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23172565  588 CDMYWPKDGVETYGVIQVKLIEEEVMSTYTVRTLQIKHLKLKKkkqCNTEKLVYQYHYTNWPDHGTPDHPLPVLNFVKKS 667
Cdd:cd14620   80 CYQYWPDQGCWTYGNIRVAVEDCVVLVDYTIRKFCIQPQLPDG---CKAPRLVTQLHFTSWPDFGVPFTPIGMLKFLKKV 156
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 23172565  668 SAANPAEAGPIVVHCSAGVGRTGTYIVLDAMLKQIQQKNIVNVFGFLRHIRAQRNFLVQTEEQYIFLHDALVE 740
Cdd:cd14620  157 KSVNPVHAGPIVVHCSAGVGRTGTFIVIDAMIDMMHAEQKVDVFEFVSRIRNQRPQMVQTDMQYSFIYQALLE 229
R-PTPc-T-1 cd14630
catalytic domain of receptor-type tyrosine-protein phosphatase T, repeat 1; Receptor-type ...
501-741 1.74e-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: 1.74e-77
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23172565  501 ENKRKNRYLNITAYDHSRVHLHPTPGQKKNlDYINANFIDGYQKGHAFIGTQGPLPDTFDCFWRMIWEQRVAIIVMITNL 580
Cdd:cd14630    2 ENRNKNRYGNIISYDHSRVRLQLLDGDPHS-DYINANYIDGYHRPRHYIATQGPMQETVKDFWRMIWQENSASVVMVTNL 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23172565  581 VERGRRKCDMYWPkDGVETYGVIQVKLIEEEVMSTYTVRTLQIKHLKLKKKKQcnteklVYQYHYTNWPDHGTPDHPLPV 660
Cdd:cd14630   81 VEVGRVKCVRYWP-DDTEVYGDIKVTLIETEPLAEYVIRTFTVQKKGYHEIRE------IRQFHFTSWPDHGVPCYATGL 153
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23172565  661 LNFVKKSSAANPAEAGPIVVHCSAGVGRTGTYIVLDAMLKQIQQKNIVNVFGFLRHIRAQRNFLVQTEEQYIFLHDALVE 740
Cdd:cd14630  154 LGFVRQVKFLNPPDAGPIVVHCSAGAGRTGCFIAIDIMLDMAENEGVVDIFNCVRELRAQRVNMVQTEEQYVFVHDAILE 233

                 .
gi 23172565  741 A 741
Cdd:cd14630  234 A 234
R-PTPc-typeIIb-1 cd14555
catalytic domain of type IIb (or R2B) subfamily receptor-type tyrosine-protein phosphatases, ...
533-741 1.12e-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: 1.12e-74
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23172565  533 YINANFIDGYQKGHAFIGTQGPLPDTFDCFWRMIWEQRVAIIVMITNLVERGRRKCDMYWPKDgVETYGVIQVKLIEEEV 612
Cdd:cd14555    1 YINANYIDGYHRPNHYIATQGPMQETVYDFWRMVWQENSASIVMVTNLVEVGRVKCSRYWPDD-TEVYGDIKVTLVETEP 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23172565  613 MSTYTVRTLQIKHLKLKKKKQcnteklVYQYHYTNWPDHGTPDHPLPVLNFVKKSSAANPAEAGPIVVHCSAGVGRTGTY 692
Cdd:cd14555   80 LAEYVVRTFALERRGYHEIRE------VRQFHFTGWPDHGVPYHATGLLGFIRRVKASNPPSAGPIVVHCSAGAGRTGCY 153
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*....
gi 23172565  693 IVLDAMLKQIQQKNIVNVFGFLRHIRAQRNFLVQTEEQYIFLHDALVEA 741
Cdd:cd14555  154 IVIDIMLDMAEREGVVDIYNCVKELRSRRVNMVQTEEQYIFIHDAILEA 202
R-PTPc-A-E-1 cd14551
catalytic domain of receptor-type tyrosine-protein phosphatase A and E, repeat 1; ...
533-735 2.67e-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: 245.21  E-value: 2.67e-74
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23172565  533 YINANFIDGYQKGHAFIGTQGPLPDTFDCFWRMIWEQRVAIIVMITNLVERGRRKCDMYWPKDGVETYGVIQVKLIEEEV 612
Cdd:cd14551    1 YINASYIDGYQEKNKFIAAQGPKDETVNDFWRMIWEQGSATIVMVTNLKERKEKKCSQYWPDQGCWTYGNLRVRVEDTVV 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23172565  613 MSTYTVRTLQIKHLKLKKKkqCNTEKLVYQYHYTNWPDHGTPDHPLPVLNFVKKSSAANPAEAGPIVVHCSAGVGRTGTY 692
Cdd:cd14551   81 LVDYTTRKFCIQKVNRGIG--EKRVRLVTQFHFTSWPDFGVPFTPIGMLKFLKKVKSANPPRAGPIVVHCSAGVGRTGTF 158
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|...
gi 23172565  693 IVLDAMLKQIQQKNIVNVFGFLRHIRAQRNFLVQTEEQYIFLH 735
Cdd:cd14551  159 IVIDAMLDMMHAEGKVDVFGFVSRIRQQRSQMVQTDMQYVFIY 201
R-PTPc-J cd14615
catalytic domain of receptor-type tyrosine-protein phosphatase J; Receptor-type ...
506-734 6.03e-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: 6.03e-72
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23172565  506 NRYLNITAYDHSRVHL----HPTPgqkknlDYINANFIDGYQKGHAFIGTQGPLPDTFDCFWRMIWEQRVAIIVMITNLV 581
Cdd:cd14615    1 NRYNNVLPYDISRVKLsvqsHSTD------DYINANYMPGYNSKKEFIAAQGPLPNTVKDFWRMVWEKNVYAIVMLTKCV 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23172565  582 ERGRRKCDMYWPKDGVETYGVIQVKLIEEEVMSTYTVRTLQIkhlklkKKKQCNTEKLVYQYHYTNWPDHGTPDHPLPVL 661
Cdd:cd14615   75 EQGRTKCEEYWPSKQKKDYGDITVTMTSEIVLPEWTIRDFTV------KNAQTNESRTVRHFHFTSWPDHGVPETTDLLI 148
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 23172565  662 NF---VKKSSAANPAEaGPIVVHCSAGVGRTGTYIVLDAMLKQIQQKNIVNVFGFLRHIRAQRNFLVQTEEQYIFL 734
Cdd:cd14615  149 NFrhlVREYMKQNPPN-SPILVHCSAGVGRTGTFIAIDRLIYQIENENVVDVYGIVYDLRMHRPLMVQTEDQYVFL 223
R-PTPc-U-1 cd14632
catalytic domain of receptor-type tyrosine-protein phosphatase U, repeat 1; Receptor-type ...
533-741 6.21e-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: 6.21e-71
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23172565  533 YINANFIDGYQKGHAFIGTQGPLPDTFDCFWRMIWEQRVAIIVMITNLVERGRRKCDMYWPKDGvETYGVIQVKLIEEEV 612
Cdd:cd14632    1 YINANYIDGYHRSNHFIATQGPKQEMVYDFWRMVWQEHCSSIVMITKLVEVGRVKCSKYWPDDS-DTYGDIKITLLKTET 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23172565  613 MSTYTVRTLQIKHLKLKKKKQcnteklVYQYHYTNWPDHGTPDHPLPVLNFVKKSSAANPAEAGPIVVHCSAGVGRTGTY 692
Cdd:cd14632   80 LAEYSVRTFALERRGYSARHE------VKQFHFTSWPEHGVPYHATGLLAFIRRVKASTPPDAGPVVVHCSAGAGRTGCY 153
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*....
gi 23172565  693 IVLDAMLKQIQQKNIVNVFGFLRHIRAQRNFLVQTEEQYIFLHDALVEA 741
Cdd:cd14632  154 IVLDVMLDMAECEGVVDIYNCVKTLCSRRINMIQTEEQYIFIHDAILEA 202
PTPc-N11_6 cd14544
catalytic domain of tyrosine-protein phosphatase non-receptor type 11 and type 6; ...
502-742 2.77e-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: 2.77e-70
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23172565  502 NKRKNRYLNITAYDHSRVHLHPTPGQKKNLDYINANFI--DGYQKGH-----AFIGTQGPLPDTFDCFWRMIWEQRVAII 574
Cdd:cd14544    1 NKGKNRYKNILPFDHTRVILKDRDPNVPGSDYINANYIrnENEGPTTdenakTYIATQGCLENTVSDFWSMVWQENSRVI 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23172565  575 VMITNLVERGRRKCDMYWPKDG-VETYGVIQVKLIEEEVMSTYTVRTLQIkhlklKKKKQCNTEKLVYQYHYTNWPDHGT 653
Cdd:cd14544   81 VMTTKEVERGKNKCVRYWPDEGmQKQYGPYRVQNVSEHDTTDYTLRELQV-----SKLDQGDPIREIWHYQYLSWPDHGV 155
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23172565  654 PDHPLPVLNFV----KKSSAANpaEAGPIVVHCSAGVGRTGTYIVLDAMLKQIQQKNI---VNVFGFLRHIRAQRNFLVQ 726
Cdd:cd14544  156 PSDPGGVLNFLedvnQRQESLP--HAGPIVVHCSAGIGRTGTFIVIDMLLDQIKRKGLdcdIDIQKTIQMVRSQRSGMVQ 233
                        250
                 ....*....|....*.
gi 23172565  727 TEEQYIFLHDALVEAI 742
Cdd:cd14544  234 TEAQYKFIYVAVAQYI 249
R-PTPc-H cd14619
catalytic domain of receptor-type tyrosine-protein phosphatase H; Receptor-type ...
506-742 2.82e-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: 234.78  E-value: 2.82e-70
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23172565  506 NRYLNITAYDHSRVHLHPTPGQKKNlDYINANFIDGYQKGHAFIGTQGPLPDTFDCFWRMIWEQRVAIIVMITNLVERGR 585
Cdd:cd14619    1 NRFRNVLPYDWSRVPLKPIHEEPGS-DYINANYMPGYWSSQEFIATQGPLPQTVGDFWRMIWEQQSSTIVMLTNCMEAGR 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23172565  586 RKCDMYWPKDGVE-TYGVIQVKLIEEEVMSTYTVRTLQIKHLKLKKKkqcnteKLVYQYHYTNWPDHGTPDHPLPVLNF- 663
Cdd:cd14619   80 VKCEHYWPLDYTPcTYGHLRVTVVSEEVMENWTVREFLLKQVEEQKT------LSVRHFHFTAWPDHGVPSSTDTLLAFr 153
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23172565  664 -VKKSSAANPAEAGPIVVHCSAGVGRTGTYIVLDAMLKQIQQKNIVNVFGFLRHIRAQRNFLVQTEEQYIFLHDALVEAI 742
Cdd:cd14619  154 rLLRQWLDQTMSGGPTVVHCSAGVGRTGTLIALDVLLQQLQSEGLLGPFSFVQKMRENRPLMVQTESQYVFLHQCILDFL 233
PTPc smart00194
Protein tyrosine phosphatase, catalytic domain;
764-1015 1.52e-69

Protein tyrosine phosphatase, catalytic domain;


Pssm-ID: 214550 [Multi-domain]  Cd Length: 259  Bit Score: 233.71  E-value: 1.52e-69
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23172565     764 LEQQYKNIIQFQPKDIHIASAMKQVNSIKNR-GAIFPIEGSRVHLTPKPGEdGSDYINASWLHGFRRLRDFIVTQHPMAH 842
Cdd:smart00194    2 LEEEFEKLDRLKPDDESCTVAAFPENRDKNRyKDVLPYDHTRVKLKPPPGE-GSDYINASYIDGPNGPKAYIATQGPLPS 80
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23172565     843 TIKDFWQMVWDHNAQTVVLLSSLDD---INFAQFWPDEA-TPIESDHYRVKFLNKTNKSDYVSRDFVIQSIQDDYELTVK 918
Cdd:smart00194   81 TVEDFWRMVWEQKVTVIVMLTELVEkgrEKCAQYWPDEEgEPLTYGDITVTLKSVEKVDDYTIRTLEVTNTGCSETRTVT 160
                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23172565     919 MLHCPSWPEMSNPNS---IYDFIVDVHERCNDYrNGPIVIVDRYGGAQACTFCAISSLAIEMEYCSTANVYQYAKLYHNK 995
Cdd:smart00194  161 HYHYTNWPDHGVPESpesILDLIRAVRKSQSTS-TGPIVVHCSAGVGRTGTFIAIDILLQQLEAGKEVDIFEIVKELRSQ 239
                           250       260
                    ....*....|....*....|
gi 23172565     996 RPGVWTSSEDIRVIYNILSF 1015
Cdd:smart00194  240 RPGMVQTEEQYIFLYRAILE 259
R-PTPc-B cd14617
catalytic domain of receptor-type tyrosine-protein phosphatase B; Receptor-type ...
506-735 7.88e-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: 230.58  E-value: 7.88e-69
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23172565  506 NRYLNITAYDHSRVHL---HPTPGQkknlDYINANFIDGYQKGHAFIGTQGPLPDTFDCFWRMIWEQRVAIIVMITNLVE 582
Cdd:cd14617    1 NRYNNILPYDSTRVKLsnvDDDPCS----DYINASYIPGNNFRREYIATQGPLPGTKDDFWKMVWEQNVHNIVMVTQCVE 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23172565  583 RGRRKCDMYWPKDGVET-YGVIQVKLIEEEVMSTYTVRTLQIkhlklKKKKQCNTEKLVYQYHYTNWPDHGTPDHPLPVL 661
Cdd:cd14617   77 KGRVKCDHYWPADQDSLyYGDLIVQMLSESVLPEWTIREFKI-----CSEEQLDAPRLVRHFHYTVWPDHGVPETTQSLI 151
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 23172565  662 NFVK--KSSAANPAEAGPIVVHCSAGVGRTGTYIVLDAMLKQIQQKNIVNVFGFLRHIRAQRNFLVQTEEQYIFLH 735
Cdd:cd14617  152 QFVRtvRDYINRTPGSGPTVVHCSAGVGRTGTFIALDRILQQLDSKDSVDIYGAVHDLRLHRVHMVQTECQYVYLH 227
R-PTPc-K-1 cd14631
catalytic domain of receptor-type tyrosine-protein phosphatase K, repeat 1; Receptor-type ...
518-741 4.29e-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: 4.29e-68
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23172565  518 RVHLHPTPGQKKNlDYINANFIDGYQKGHAFIGTQGPLPDTFDCFWRMIWEQRVAIIVMITNLVERGRRKCDMYWPKDgV 597
Cdd:cd14631    1 RVILQPVEDDPSS-DYINANYIDGYQRPSHYIATQGPVHETVYDFWRMIWQEQSACIVMVTNLVEVGRVKCYKYWPDD-T 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23172565  598 ETYGVIQVKLIEEEVMSTYTVRTLQIKHLKLkkkkqcNTEKLVYQYHYTNWPDHGTPDHPLPVLNFVKKSSAANPAEAGP 677
Cdd:cd14631   79 EVYGDFKVTCVEMEPLAEYVVRTFTLERRGY------NEIREVKQFHFTGWPDHGVPYHATGLLSFIRRVKLSNPPSAGP 152
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 23172565  678 IVVHCSAGVGRTGTYIVLDAMLKQIQQKNIVNVFGFLRHIRAQRNFLVQTEEQYIFLHDALVEA 741
Cdd:cd14631  153 IVVHCSAGAGRTGCYIVIDIMLDMAEREGVVDIYNCVKALRSRRINMVQTEEQYIFIHDAILEA 216
Y_phosphatase pfam00102
Protein-tyrosine phosphatase;
789-1013 6.51e-68

Protein-tyrosine phosphatase;


Pssm-ID: 459674 [Multi-domain]  Cd Length: 234  Bit Score: 228.28  E-value: 6.51e-68
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23172565    789 NSIKNR-GAIFPIEGSRVHLTPKPGedGSDYINASWLHGFRRLRDFIVTQHPMAHTIKDFWQMVWDHNAQTVVLLSSLDD 867
Cdd:pfam00102    1 NLEKNRyKDVLPYDHTRVKLTGDPG--PSDYINASYIDGYKKPKKYIATQGPLPNTVEDFWRMVWEEKVTIIVMLTELEE 78
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23172565    868 IN---FAQFWPDEA-TPIESDHYRVKFLN-KTNKSDYVSRDFVIQSIQDDYELTVKMLHCPSWPEM---SNPNSIYDFIV 939
Cdd:pfam00102   79 KGrekCAQYWPEEEgESLEYGDFTVTLKKeKEDEKDYTVRTLEVSNGGSEETRTVKHFHYTGWPDHgvpESPNSLLDLLR 158
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 23172565    940 DVHERCNDYRNGPIVIVDRYGGAQACTFCAISSLAIEMEYCSTANVYQYAKLYHNKRPGVWTSSEDIRVIYNIL 1013
Cdd:pfam00102  159 KVRKSSLDGRSGPIVVHCSAGIGRTGTFIAIDIALQQLEAEGEVDIFQIVKELRSQRPGMVQTLEQYIFLYDAI 232
PTPc-KIM cd14547
catalytic domain of the kinase interaction motif (KIM) family of protein-tyrosine phosphatases; ...
506-735 1.29e-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: 226.89  E-value: 1.29e-67
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23172565  506 NRYLNITAYDHSRVHLHPTPGQKKnLDYINANFIDGYQ-KGHAFIGTQGPLPDTFDCFWRMIWEQRVAIIVMITNLVERg 584
Cdd:cd14547    1 NRYKTILPNEHSRVCLPSVDDDPL-SSYINANYIRGYDgEEKAYIATQGPLPNTVADFWRMVWQEKTPIIVMITNLTEA- 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23172565  585 RRKCDMYWPKDGVETYGVIQVKLIEEEVMSTYTVRTLQIKhlklkkkkQCNTEKLVYQYHYTNWPDHGTPDHPLPVLNFV 664
Cdd:cd14547   79 KEKCAQYWPEEENETYGDFEVTVQSVKETDGYTVRKLTLK--------YGGEKRYLKHYWYTSWPDHKTPEAAQPLLSLV 150
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 23172565  665 KK--SSAANPAEAGPIVVHCSAGVGRTGTYIVLDAMLKQIQQKNIVNVFGFLRHIRAQRNFLVQTEEQYIFLH 735
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 ...
500-737 4.46e-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: 225.87  E-value: 4.46e-67
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23172565  500 PENKRKNRYLNITAYDHSRVHLHPTPGQKKNlDYINANFIDGYQKGHAFIGTQGPLPDTFDCFWRMIWEQRVAIIVMITN 579
Cdd:cd14554    4 PCNKFKNRLVNILPYESTRVCLQPIRGVEGS-DYINASFIDGYRQRGAYIATQGPLAETTEDFWRMLWEHNSTIIVMLTK 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23172565  580 LVERGRRKCDMYWPKDGVETYGVIQVKLIEEEVMSTYTVRTLQIKHLKLkkkkqcNTEKLVYQYHYTNWPDHGTPDHPLP 659
Cdd:cd14554   83 LREMGREKCHQYWPAERSARYQYFVVDPMAEYNMPQYILREFKVTDARD------GQSRTVRQFQFTDWPEQGVPKSGEG 156
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23172565  660 VLNFVKK--SSAANPAEAGPIVVHCSAGVGRTGTYIVLDAMLKQIQQKNIVNVFGFLRHIRAQRNFLVQTEEQYIFLHDA 737
Cdd:cd14554  157 FIDFIGQvhKTKEQFGQEGPITVHCSAGVGRTGVFITLSIVLERMRYEGVVDVFQTVKLLRTQRPAMVQTEDQYQFCYRA 236
R-PTPc-V cd14618
catalytic domain of receptor-type tyrosine-protein phosphatase V; Receptor-type ...
506-739 1.43e-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: 1.43e-66
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23172565  506 NRYLNITAYDHSRVHLHPTPGQKKNlDYINANFIDGYQKGHAFIGTQGPLPDTFDCFWRMIWEQRVAIIVMITNLVERGR 585
Cdd:cd14618    1 NRYPHVLPYDHSRVRLSQLGGEPHS-DYINANFIPGYTSPQEFIATQGPLKKTIEDFWRLVWEQQVCNIIMLTVGMENGR 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23172565  586 RKCDMYWPKDGVE-TYGVIQVKLIEEEVMSTYTVRTLQIKHLKLkkkkqcNTEKLVYQYHYTNWPDHGTPDHPLPVLNFV 664
Cdd:cd14618   80 VLCDHYWPSESTPvSYGHITVHLLAQSSEDEWTRREFKLWHEDL------RKERRVKHLHYTAWPDHGIPESTSSLMAFR 153
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 23172565  665 K--KSSAANPAEAGPIVVHCSAGVGRTGTYIVLDAMLKQIQQKNIVNVFGFLRHIRAQRNFLVQTEEQYIFLHDALV 739
Cdd:cd14618  154 ElvREHVQATKGKGPTLVHCSAGVGRSGTFIALDRLLRQLKEEKVVDVFNTVYILRMHRYLMIQTLSQYIFLHSCIL 230
R-PTPc-O cd14614
catalytic domain of receptor-type tyrosine-protein phosphatase O; Receptor-type ...
491-735 5.25e-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: 223.23  E-value: 5.25e-66
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23172565  491 DLPCEHSQHPENKRKNRYLNITAYDHSRVHLhPTPGQKKNLDYINANFIDGYQKGHAFIGTQGPLPDTFDCFWRMIWEQR 570
Cdd:cd14614    1 DIPHFAADLPVNRCKNRYTNILPYDFSRVKL-VSMHEEEGSDYINANYIPGYNSPQEYIATQGPLPETRNDFWKMVLQQK 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23172565  571 VAIIVMITNLVERGRRKCDMYWP--KDGVeTYGVIQVKLIEEEVMSTYTVRTLQIkhlKLKKKKQCnteklVYQYHYTNW 648
Cdd:cd14614   80 SQIIVMLTQCNEKRRVKCDHYWPftEEPV-AYGDITVEMLSEEEQPDWAIREFRV---SYADEVQD-----VMHFNYTAW 150
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23172565  649 PDHGTP--DHPLPVLNFVKKSSAANPAEAGPIVVHCSAGVGRTGTYIVLDAMLKQIQQKNIVNVFGFLRHIRAQRNFLVQ 726
Cdd:cd14614  151 PDHGVPtaNAAESILQFVQMVRQQAVKSKGPMIIHCSAGVGRTGTFIALDRLLQHIRDHEFVDILGLVSEMRSYRMSMVQ 230

                 ....*....
gi 23172565  727 TEEQYIFLH 735
Cdd:cd14614  231 TEEQYIFIH 239
PTPc-N11 cd14605
catalytic domain of tyrosine-protein phosphatase non-receptor type 11; Tyrosine-protein ...
501-744 1.50e-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: 1.50e-65
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23172565  501 ENKRKNRYLNITAYDHSRVHLHPTPGQKKNLDYINANFI--------DGYQKGHAFIGTQGPLPDTFDCFWRMIWEQRVA 572
Cdd:cd14605    1 ENKNKNRYKNILPFDHTRVVLHDGDPNEPVSDYINANIImpefetkcNNSKPKKSYIATQGCLQNTVNDFWRMVFQENSR 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23172565  573 IIVMITNLVERGRRKCDMYWPKD-GVETYGVIQVKLIEEEVMSTYTVRTLQIkhlklKKKKQCNTEKLVYQYHYTNWPDH 651
Cdd:cd14605   81 VIVMTTKEVERGKSKCVKYWPDEyALKEYGVMRVRNVKESAAHDYILRELKL-----SKVGQGNTERTVWQYHFRTWPDH 155
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23172565  652 GTPDHPLPVLNFVK--KSSAANPAEAGPIVVHCSAGVGRTGTYIVLDAMLKQIQQKNI---VNVFGFLRHIRAQRNFLVQ 726
Cdd:cd14605  156 GVPSDPGGVLDFLEevHHKQESIMDAGPVVVHCSAGIGRTGTFIVIDILIDIIREKGVdcdIDVPKTIQMVRSQRSGMVQ 235
                        250
                 ....*....|....*...
gi 23172565  727 TEEQYIFLHDALVEAIAS 744
Cdd:cd14605  236 TEAQYRFIYMAVQHYIET 253
PTP_fungal cd18533
fungal protein tyrosine phosphatases; This subfamily contains Saccharomyces cerevisiae ...
533-736 5.85e-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: 5.85e-64
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23172565  533 YINANFID-GYQKGHAFIGTQGPLPDTFDCFWRMIWEQRVAIIVMITNLVERGRRKCDMYWPKDGVET-YGVIQVKLIEE 610
Cdd:cd18533    1 YINASYITlPGTSSKRYIATQGPLPATIGDFWKMIWQNNVGVIVMLTPLVENGREKCDQYWPSGEYEGeYGDLTVELVSE 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23172565  611 EV--MSTYTVRTLQIKHLKlkkkkqcNTEKLVYQYHYTNWPDHGTPDHPLPVLN--FVKKSSAANPAEAGPIVVHCSAGV 686
Cdd:cd18533   81 EEndDGGFIVREFELSKED-------GKVKKVYHIQYKSWPDFGVPDSPEDLLTliKLKRELNDSASLDPPIIVHCSAGV 153
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 23172565  687 GRTGTYIVLDAMLKQIQ-QKNIVN--------VFGFLRHIRAQRNFLVQTEEQYIFLHD 736
Cdd:cd18533  154 GRTGTFIALDSLLDELKrGLSDSQdledsedpVYEIVNQLRKQRMSMVQTLRQYIFLYD 212
R-PTPc-C-1 cd14557
catalytic domain of receptor-type tyrosine-protein phosphatase C, repeat 1; Receptor-type ...
533-735 6.02e-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: 6.02e-63
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23172565  533 YINANFIDGYQKGHAFIGTQGPLPDTFDCFWRMIWEQRVAIIVMITNLVERGRRKCDMYWP--KDGVETYGVIQVKLIEE 610
Cdd:cd14557    1 YINASYIDGFKEPRKYIAAQGPKDETVDDFWRMIWEQKSTVIVMVTRCEEGNRNKCAQYWPsmEEGSRAFGDVVVKINEE 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23172565  611 EVMSTYTVRTLQIKHLKLKKkkqcnTEKLVYQYHYTNWPDHGTPDHPLPVLNFVKKSSAANPAEAGPIVVHCSAGVGRTG 690
Cdd:cd14557   81 KICPDYIIRKLNINNKKEKG-----SGREVTHIQFTSWPDHGVPEDPHLLLKLRRRVNAFNNFFSGPIVVHCSAGVGRTG 155
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*
gi 23172565  691 TYIVLDAMLKQIQQKNIVNVFGFLRHIRAQRNFLVQTEEQYIFLH 735
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; ...
533-735 5.98e-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: 5.98e-62
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23172565  533 YINANFIDGYQKGHAFIGTQGPLPDTFDCFWRMIWEQRVAIIVMITNLVERGRRKCDMYWPKDGVE--TYGVIQVKLIEE 610
Cdd:cd14542    1 YINANFIKGVSGSKAYIATQGPLPNTVLDFWRMIWEYNVQVIVMACREFEMGKKKCERYWPEEGEEqlQFGPFKISLEKE 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23172565  611 EVMST-YTVRTLQIKHLklkkkkqcNTEKLVYQYHYTNWPDHGTPDHPLPVLNFVKKSSAANPAEAGPIVVHCSAGVGRT 689
Cdd:cd14542   81 KRVGPdFLIRTLKVTFQ--------KESRTVYQFHYTAWPDHGVPSSVDPILDLVRLVRDYQGSEDVPICVHCSAGCGRT 152
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|
gi 23172565  690 GTYIVLD----AMLKQIQQKNIvNVFGFLRHIRAQRNFLVQTEEQYIFLH 735
Cdd:cd14542  153 GTICAIDyvwnLLKTGKIPEEF-SLFDLVREMRKQRPAMVQTKEQYELVY 201
PTPc-N1 cd14608
catalytic domain of tyrosine-protein phosphatase non-receptor type 1; Tyrosine-protein ...
480-740 7.96e-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: 7.96e-62
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23172565  480 YEAIQNEciSDDLPCEHSQHPENKRKNRYLNITAYDHSRVHLHptpgQKKNlDYINANFIDGYQKGHAFIGTQGPLPDTF 559
Cdd:cd14608    5 YQDIRHE--ASDFPCRVAKLPKNKNRNRYRDVSPFDHSRIKLH----QEDN-DYINASLIKMEEAQRSYILTQGPLPNTC 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23172565  560 DCFWRMIWEQRVAIIVMITNLVERGRRKCDMYWP----KDGVETYGVIQVKLIEEEVMSTYTVRTLQIKHLKLKKKKQcn 635
Cdd:cd14608   78 GHFWEMVWEQKSRGVVMLNRVMEKGSLKCAQYWPqkeeKEMIFEDTNLKLTLISEDIKSYYTVRQLELENLTTQETRE-- 155
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23172565  636 teklVYQYHYTNWPDHGTPDHPLPVLNF---VKKSSAANPaEAGPIVVHCSAGVGRTGTYIVLDAMLKQIQQK---NIVN 709
Cdd:cd14608  156 ----ILHFHYTTWPDFGVPESPASFLNFlfkVRESGSLSP-EHGPVVVHCSAGIGRSGTFCLADTCLLLMDKRkdpSSVD 230
                        250       260       270
                 ....*....|....*....|....*....|.
gi 23172565  710 VFGFLRHIRAQRNFLVQTEEQYIFLHDALVE 740
Cdd:cd14608  231 IKKVLLEMRKFRMGLIQTADQLRFSYLAVIE 261
R-PTPc-Q cd14616
catalytic domain of receptor-type tyrosine-protein phosphatase Q; Receptor-type ...
506-735 4.06e-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: 4.06e-61
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23172565  506 NRYLNITAYDHSRVHLHPTPGQKKNlDYINANFIDGYQKGHAFIGTQGPLPDTFDCFWRMIWEQRVAIIVMITNLVERGR 585
Cdd:cd14616    1 NRFPNIKPYNNNRVKLIADAGVPGS-DYINASYISGYLCPNEFIATQGPLPGTVGDFWRMVWETRAKTIVMLTQCFEKGR 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23172565  586 RKCDMYWPKDG--VETYGVIQVKLIEEEVMSTYTVRTLQIKHLKLKKkkqcntekLVYQYHYTNWPDHGTPDHPLPVLNF 663
Cdd:cd14616   80 IRCHQYWPEDNkpVTVFGDIVITKLMEDVQIDWTIRDLKIERHGDYM--------MVRQCNFTSWPEHGVPESSAPLIHF 151
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 23172565  664 VKKSSAANPAEAGPIVVHCSAGVGRTGTYIVLDAMLKQIQQKNIVNVFGFLRHIRAQRNFLVQTEEQYIFLH 735
Cdd:cd14616  152 VKLVRASRAHDNTPMIVHCSAGVGRTGVFIALDHLTQHINDHDFVDIYGLVAELRSERMCMVQNLAQYIFLH 223
PTPc-N18 cd14603
catalytic domain of tyrosine-protein phosphatase non-receptor type 18; Tyrosine-protein ...
477-740 1.86e-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: 1.86e-59
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23172565  477 SREYEAIQNECIS----DDLPCEHSQHPENKRKNRYLNITAYDHSRVHLHPTPGQKKNlDYINANFIDGYQKGHAFIGTQ 552
Cdd:cd14603    1 AGEFSEIRACSAAfkadYVCSTVAGGRKENVKKNRYKDILPYDQTRVILSLLQEEGHS-DYINANFIKGVDGSRAYIATQ 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23172565  553 GPLPDTFDCFWRMIWEQRVAIIVMITNLVERGRRKCDMYWP-KDGVETYGVIQVKLIEEEVMSTYTV-RTLQIKHlklkk 630
Cdd:cd14603   80 GPLSHTVLDFWRMIWQYGVKVILMACREIEMGKKKCERYWAqEQEPLQTGPFTITLVKEKRLNEEVIlRTLKVTF----- 154
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23172565  631 kkqCNTEKLVYQYHYTNWPDHGTPDHPLPVLNFVKKSSAANPAEAGPIVVHCSAGVGRTGTYIVLD----AMLKQIQQKN 706
Cdd:cd14603  155 ---QKESRSVSHFQYMAWPDHGIPDSPDCMLAMIELARRLQGSGPEPLCVHCSAGCGRTGVICTVDyvrqLLLTQRIPPD 231
                        250       260       270
                 ....*....|....*....|....*....|....
gi 23172565  707 IvNVFGFLRHIRAQRNFLVQTEEQYIFLHDALVE 740
Cdd:cd14603  232 F-SIFDVVLEMRKQRPAAVQTEEQYEFLYHTVAQ 264
PTPc-N1_2 cd14545
catalytic domain of tyrosine-protein phosphatase non-receptor type 1 and type 2; ...
503-733 4.90e-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: 4.90e-59
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23172565  503 KRKNRYLNITAYDHSRVHLHptpgQKKNlDYINANFIDGYQKGHAFIGTQGPLPDTFDCFWRMIWEQRVAIIVMITNLVE 582
Cdd:cd14545    1 LNRYRDRDPYDHDRSRVKLK----QGDN-DYINASLVEVEEAKRSYILTQGPLPNTSGHFWQMVWEQNSKAVIMLNKLME 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23172565  583 RGRRKCDMYWPKDGVETYGV----IQVKLIEEEVMSTYTVRTLQIKHLKLkkkkqcNTEKLVYQYHYTNWPDHGTPDHPL 658
Cdd:cd14545   76 KGQIKCAQYWPQGEGNAMIFedtgLKVTLLSEEDKSYYTVRTLELENLKT------QETREVLHFHYTTWPDFGVPESPA 149
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23172565  659 PVLNF---VKKSSAANPaEAGPIVVHCSAGVGRTGTYIVLDAMLKQIQQKNI--VNVFGFLRHIRAQRNFLVQTEEQYIF 733
Cdd:cd14545  150 AFLNFlqkVRESGSLSS-DVGPPVVHCSAGIGRSGTFCLVDTCLVLIEKGNPssVDVKKVLLEMRKYRMGLIQTPDQLRF 228
PTPc-N12 cd14604
catalytic domain of tyrosine-protein phosphatase non-receptor type 12; Tyrosine-protein ...
493-740 7.40e-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: 7.40e-59
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23172565  493 PCEHSQHPENKRKNRYLNITAYDHSRVHLH-PTPGQKKnlDYINANFIDGYQKGHAFIGTQGPLPDTFDCFWRMIWEQRV 571
Cdd:cd14604   48 PTATGEKEENVKKNRYKDILPFDHSRVKLTlKTSSQDS--DYINANFIKGVYGPKAYIATQGPLANTVIDFWRMIWEYNV 125
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23172565  572 AIIVMITNLVERGRRKCDMYWPKDGVE--TYGVIQVKLIEEEVMSTYTVRTLQIKHLklkkkkqcNTEKLVYQYHYTNWP 649
Cdd:cd14604  126 AIIVMACREFEMGRKKCERYWPLYGEEpmTFGPFRISCEAEQARTDYFIRTLLLEFQ--------NETRRLYQFHYVNWP 197
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23172565  650 DHGTPDHPLPVLNFVKKSSAANPAEAGPIVVHCSAGVGRTGTYIVLD---AMLKQIQQKNIVNVFGFLRHIRAQRNFLVQ 726
Cdd:cd14604  198 DHDVPSSFDSILDMISLMRKYQEHEDVPICIHCSAGCGRTGAICAIDytwNLLKAGKIPEEFNVFNLIQEMRTQRHSAVQ 277
                        250
                 ....*....|....
gi 23172565  727 TEEQYIFLHDALVE 740
Cdd:cd14604  278 TKEQYELVHRAIAQ 291
PTPc-N6 cd14606
catalytic domain of tyrosine-protein phosphatase non-receptor type 6; Tyrosine-protein ...
498-744 7.40e-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: 203.57  E-value: 7.40e-59
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23172565  498 QHPENKRKNRYLNITAYDHSRVHLHPTPGQKKNLDYINANFIDGYQKG-----HAFIGTQGPLPDTFDCFWRMIWEQRVA 572
Cdd:cd14606   14 QRPENKSKNRYKNILPFDHSRVILQGRDSNIPGSDYINANYVKNQLLGpdenaKTYIASQGCLEATVNDFWQMAWQENSR 93
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23172565  573 IIVMITNLVERGRRKCDMYWPKDGVE-TYGVIQVKLIEEEVMSTYTVRTLQIKHLKlkkkkqcNTEKL--VYQYHYTNWP 649
Cdd:cd14606   94 VIVMTTREVEKGRNKCVPYWPEVGMQrAYGPYSVTNCGEHDTTEYKLRTLQVSPLD-------NGELIreIWHYQYLSWP 166
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23172565  650 DHGTPDHPLPVLNFVKKSSAANPA--EAGPIVVHCSAGVGRTGTYIVLDAMLKQIQQKNI---VNVFGFLRHIRAQRNFL 724
Cdd:cd14606  167 DHGVPSEPGGVLSFLDQINQRQESlpHAGPIIVHCSAGIGRTGTIIVIDMLMENISTKGLdcdIDIQKTIQMVRAQRSGM 246
                        250       260
                 ....*....|....*....|
gi 23172565  725 VQTEEQYIFLHDALVEAIAS 744
Cdd:cd14606  247 VQTEAQYKFIYVAIAQFIET 266
R-PTP-D-2 cd14628
PTP-like domain of receptor-type tyrosine-protein phosphatase D, repeat 2; Receptor-type ...
488-744 1.74e-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: 1.74e-58
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23172565  488 ISDDLPCehsqhpeNKRKNRYLNITAYDHSRVHLHPTPGQKKNlDYINANFIDGYQKGHAFIGTQGPLPDTFDCFWRMIW 567
Cdd:cd14628   45 ISANLPC-------NKFKNRLVNIMPYESTRVCLQPIRGVEGS-DYINASFIDGYRQQKAYIATQGPLAETTEDFWRMLW 116
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23172565  568 EQRVAIIVMITNLVERGRRKCDMYWPKDGVETYGVIQVKLIEEEVMSTYTVRTLQIKHLKLkkkkqcNTEKLVYQYHYTN 647
Cdd:cd14628  117 EHNSTIVVMLTKLREMGREKCHQYWPAERSARYQYFVVDPMAEYNMPQYILREFKVTDARD------GQSRTVRQFQFTD 190
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23172565  648 WPDHGTPDHPLPVLNFVKK--SSAANPAEAGPIVVHCSAGVGRTGTYIVLDAMLKQIQQKNIVNVFGFLRHIRAQRNFLV 725
Cdd:cd14628  191 WPEQGVPKSGEGFIDFIGQvhKTKEQFGQDGPISVHCSAGVGRTGVFITLSIVLERMRYEGVVDIFQTVKMLRTQRPAMV 270
                        250
                 ....*....|....*....
gi 23172565  726 QTEEQYIFLHDALVEAIAS 744
Cdd:cd14628  271 QTEDQYQFCYRAALEYLGS 289
PTPc-N2 cd14607
catalytic domain of tyrosine-protein phosphatase non-receptor type 2; Tyrosine-protein ...
480-738 2.61e-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: 201.73  E-value: 2.61e-58
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23172565  480 YEAIQNEciSDDLPCEHSQHPENKRKNRYLNITAYDHSRVHLhptpgQKKNLDYINANFIDGYQKGHAFIGTQGPLPDTF 559
Cdd:cd14607    4 YLEIRNE--SHDYPHRVAKYPENRNRNRYRDVSPYDHSRVKL-----QNTENDYINASLVVIEEAQRSYILTQGPLPNTC 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23172565  560 DCFWRMIWEQRVAIIVMITNLVERGRRKCDMYWPKDGVETYGV----IQVKLIEEEVMSTYTVRTLQIkhlklkKKKQCN 635
Cdd:cd14607   77 CHFWLMVWQQKTKAVVMLNRIVEKDSVKCAQYWPTDEEEVLSFketgFSVKLLSEDVKSYYTVHLLQL------ENINSG 150
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23172565  636 TEKLVYQYHYTNWPDHGTPDHPLPVLNF---VKKSSAANPaEAGPIVVHCSAGVGRTGTYIVLDAMLKQIQQKN--IVNV 710
Cdd:cd14607  151 ETRTISHFHYTTWPDFGVPESPASFLNFlfkVRESGSLSP-EHGPAVVHCSAGIGRSGTFSLVDTCLVLMEKKDpdSVDI 229
                        250       260
                 ....*....|....*....|....*...
gi 23172565  711 FGFLRHIRAQRNFLVQTEEQYIFLHDAL 738
Cdd:cd14607  230 KQVLLDMRKYRMGLIQTPDQLRFSYMAV 257
R-PTP-S-2 cd14627
PTP-like domain of receptor-type tyrosine-protein phosphatase S, repeat 2; Receptor-type ...
488-744 2.65e-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: 2.65e-58
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23172565  488 ISDDLPCehsqhpeNKRKNRYLNITAYDHSRVHLHPTPGQKKNlDYINANFIDGYQKGHAFIGTQGPLPDTFDCFWRMIW 567
Cdd:cd14627   46 ISANLPC-------NKFKNRLVNIMPYETTRVCLQPIRGVEGS-DYINASFIDGYRQQKAYIATQGPLAETTEDFWRMLW 117
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23172565  568 EQRVAIIVMITNLVERGRRKCDMYWPKDGVETYGVIQVKLIEEEVMSTYTVRTLQIKHLKLkkkkqcNTEKLVYQYHYTN 647
Cdd:cd14627  118 ENNSTIVVMLTKLREMGREKCHQYWPAERSARYQYFVVDPMAEYNMPQYILREFKVTDARD------GQSRTVRQFQFTD 191
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23172565  648 WPDHGTPDHPLPVLNFVKK--SSAANPAEAGPIVVHCSAGVGRTGTYIVLDAMLKQIQQKNIVNVFGFLRHIRAQRNFLV 725
Cdd:cd14627  192 WPEQGVPKSGEGFIDFIGQvhKTKEQFGQDGPISVHCSAGVGRTGVFITLSIVLERMRYEGVVDIFQTVKMLRTQRPAMV 271
                        250
                 ....*....|....*....
gi 23172565  726 QTEEQYIFLHDALVEAIAS 744
Cdd:cd14627  272 QTEDEYQFCYQAALEYLGS 290
PTPc-N22 cd14602
catalytic domain of tyrosine-protein phosphatase non-receptor type 22; Tyrosine-protein ...
505-740 5.76e-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: 5.76e-57
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23172565  505 KNRYLNITAYDHSRVHLHPTPGQKKNlDYINANFIDGYQKGHAFIGTQGPLPDTFDCFWRMIWEQRVAIIVMITNLVERG 584
Cdd:cd14602    1 KNRYKDILPYDHSRVELSLITSDEDS-DYINANFIKGVYGPRAYIATQGPLSTTLLDFWRMIWEYSVLIIVMACMEFEMG 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23172565  585 RRKCDMYWPKDGVET--YGVIQVKLIEEEVMSTYTVRTLQIkhlklkkkkQCNTE-KLVYQYHYTNWPDHGTPDHPLPVL 661
Cdd:cd14602   80 KKKCERYWAEPGEMQleFGPFSVTCEAEKRKSDYIIRTLKV---------KFNSEtRTIYQFHYKNWPDHDVPSSIDPIL 150
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23172565  662 NFVKKSSAANPAEAGPIVVHCSAGVGRTGTYIVLDAMLKQIQQKNI---VNVFGFLRHIRAQRNFLVQTEEQYIFLHDAL 738
Cdd:cd14602  151 ELIWDVRCYQEDDSVPICIHCSAGCGRTGVICAIDYTWMLLKDGIIpenFSVFSLIQEMRTQRPSLVQTKEQYELVYNAV 230

                 ..
gi 23172565  739 VE 740
Cdd:cd14602  231 IE 232
R-PTPc-A-2 cd14623
catalytic domain of receptor-type tyrosine-protein phosphatase A, repeat 2; Receptor-type ...
507-740 1.12e-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: 1.12e-56
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23172565  507 RYLNITAYDHSRVHLhPTPGQKKNLDYINANFIDGYQKGHAFIGTQGPLPDTFDCFWRMIWEQRVAIIVMITNLVERGRR 586
Cdd:cd14623    1 RVLQIIPYEFNRVII-PVKRGEENTDYVNASFIDGYRQKDSYIASQGPLQHTIEDFWRMIWEWKSCSIVMLTELEERGQE 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23172565  587 KCDMYWPKDGVETYGVIQVKLIEEEVMSTYTVRTLQIKHLKLkkkkqcNTEKLVYQYHYTNWPDHGTPDHPLPVLNFVKK 666
Cdd:cd14623   80 KCAQYWPSDGSVSYGDITIELKKEEECESYTVRDLLVTNTRE------NKSRQIRQFHFHGWPEVGIPSDGKGMINIIAA 153
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 23172565  667 SSAANPAEAG-PIVVHCSAGVGRTGTYIVLDAMLKQIQQKNIVNVFGFLRHIRAQRNFLVQTEEQYIFLHDALVE 740
Cdd:cd14623  154 VQKQQQQSGNhPITVHCSAGAGRTGTFCALSTVLERVKAEGILDVFQTVKSLRLQRPHMVQTLEQYEFCYKVVQE 228
R-PTP-F-2 cd14629
PTP-like domain of receptor-type tyrosine-protein phosphatase F, repeat 2; Receptor-type ...
488-744 1.87e-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: 1.87e-56
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23172565  488 ISDDLPCehsqhpeNKRKNRYLNITAYDHSRVHLHPTPGQKKNlDYINANFIDGYQKGHAFIGTQGPLPDTFDCFWRMIW 567
Cdd:cd14629   46 ISANLPC-------NKFKNRLVNIMPYELTRVCLQPIRGVEGS-DYINASFIDGYRQQKAYIATQGPLAETTEDFWRMLW 117
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23172565  568 EQRVAIIVMITNLVERGRRKCDMYWPKDGVETYGVIQVKLIEEEVMSTYTVRTLQIKHLKLkkkkqcNTEKLVYQYHYTN 647
Cdd:cd14629  118 EHNSTIVVMLTKLREMGREKCHQYWPAERSARYQYFVVDPMAEYNMPQYILREFKVTDARD------GQSRTIRQFQFTD 191
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23172565  648 WPDHGTPDHPLPVLNFVKK--SSAANPAEAGPIVVHCSAGVGRTGTYIVLDAMLKQIQQKNIVNVFGFLRHIRAQRNFLV 725
Cdd:cd14629  192 WPEQGVPKTGEGFIDFIGQvhKTKEQFGQDGPITVHCSAGVGRTGVFITLSIVLERMRYEGVVDMFQTVKTLRTQRPAMV 271
                        250
                 ....*....|....*....
gi 23172565  726 QTEEQYIFLHDALVEAIAS 744
Cdd:cd14629  272 QTEDQYQLCYRAALEYLGS 290
R-PTPc-A-E-2 cd14552
catalytic domain of receptor-type tyrosine-protein phosphatase A and E, repeat 2; ...
533-739 4.73e-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: 4.73e-56
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23172565  533 YINANFIDGYQKGHAFIGTQGPLPDTFDCFWRMIWEQRVAIIVMITNLVERGRRKCDMYWPKDGVETYGVIQVKLIEEEV 612
Cdd:cd14552    1 YINASFIDGYRQKDAYIATQGPLDHTVEDFWRMIWEWKSCSIVMLTEIKERSQNKCAQYWPEDGSVSSGDITVELKDQTD 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23172565  613 MSTYTVRTLQIkhlklkKKKQCNTEKLVYQYHYTNWPDHGTPDHPLPVLNFV-----KKSSAANpaeaGPIVVHCSAGVG 687
Cdd:cd14552   81 YEDYTLRDFLV------TKGKGGSTRTVRQFHFHGWPEVGIPDNGKGMIDLIaavqkQQQQSGN----HPITVHCSAGAG 150
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|..
gi 23172565  688 RTGTYIVLDAMLKQIQQKNIVNVFGFLRHIRAQRNFLVQTEEQYIFLHDALV 739
Cdd:cd14552  151 RTGTFCALSTVLERVKAEGVLDVFQVVKSLRLQRPHMVQTLEQYEFCYKVVQ 202
PTPc-N13 cd14597
catalytic domain of tyrosine-protein phosphatase non-receptor type 13; Tyrosine-protein ...
501-733 6.89e-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: 6.89e-56
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23172565  501 ENKRKNRYLNITAYDHSRVHLhptpGQKKnlDYINANFIDGYQKG--HAFIGTQGPLPDTFDCFWRMIWEQRVAIIVMIT 578
Cdd:cd14597    2 ENRKKNRYKNILPYDTTRVPL----GDEG--GYINASFIKMPVGDeeFVYIACQGPLPTTVADFWQMVWEQKSTVIAMMT 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23172565  579 NLVERGRRKCDMYWPKDGVETYGV---IQVKLIEEEVMSTYTVRTLQIKHLklkkkkQCNTEKLVYQYHYTNWPDHGTPD 655
Cdd:cd14597   76 QEVEGGKIKCQRYWPEILGKTTMVdnrLQLTLVRMQQLKNFVIRVLELEDI------QTREVRHITHLNFTAWPDHDTPS 149
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 23172565  656 HPLPVLNFVkkSSAANPAEAGPIVVHCSAGVGRTGTYIVLDAMLKQIQQKNIVNVFGFLRHIRAQRNFLVQTEEQYIF 733
Cdd:cd14597  150 QPEQLLTFI--SYMRHIHKSGPIITHCSAGIGRSGTLICIDVVLGLISKDLDFDISDIVRTMRLQRHGMVQTEDQYIF 225
PTPc-N7 cd14612
catalytic domain of tyrosine-protein phosphatase non-receptor type 7; Tyrosine-protein ...
500-738 8.29e-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: 8.29e-56
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23172565  500 PENKRKNRYLNITAYDHSRVHLHPTPGQKKNLDYINANFIDGYQ-KGHAFIGTQGPLPDTFDCFWRMIWEQRVAIIVMIT 578
Cdd:cd14612   13 PGHASKDRYKTILPNPQSRVCLRRAGSQEEEGSYINANYIRGYDgKEKAYIATQGPMLNTVSDFWEMVWQEECPIIVMIT 92
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23172565  579 NLVERgRRKCDMYWP-KDGveTYGVIQVKLIEEEVMSTYTVRTLQIkhlklkkkkQCNTE-KLVYQYHYTNWPDHGTPDH 656
Cdd:cd14612   93 KLKEK-KEKCVHYWPeKEG--TYGRFEIRVQDMKECDGYTIRDLTI---------QLEEEsRSVKHYWFSSWPDHQTPES 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23172565  657 PLPVLNFVKK-----SSAANPaeaGPIVVHCSAGVGRTGTYIVLDAMLKQIQQKNIVNVFGFLRHIRAQRNFLVQTEEQY 731
Cdd:cd14612  161 AGPLLRLVAEveesrQTAASP---GPIVVHCSAGIGRTGCFIATSIGCQQLKDTGKVDILGIVCQLRLDRGGMIQTSEQY 237

                 ....*..
gi 23172565  732 IFLHDAL 738
Cdd:cd14612  238 QFLHHTL 244
PTPc-N20_13 cd14538
catalytic domain of tyrosine-protein phosphatase non-receptor type 20 and type 13; ...
533-742 1.99e-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: 1.99e-55
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23172565  533 YINANFID---GYQKGHaFIGTQGPLPDTFDCFWRMIWEQRVAIIVMITNLVERGRRKCDMYWPKDGVET---YGVIQVK 606
Cdd:cd14538    1 YINASHIRipvGGDTYH-YIACQGPLPNTTGDFWQMVWEQKSEVIAMVTQDVEGGKVKCHRYWPDSLNKPlicGGRLEVS 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23172565  607 LIEEEVMSTYTVRTLQIKHLklkkkkQCNTEKLVYQYHYTNWPDHGTPDHPLPVLNFVkkSSAANPAEAGPIVVHCSAGV 686
Cdd:cd14538   80 LEKYQSLQDFVIRRISLRDK------ETGEVHHITHLNFTTWPDHGTPQSADPLLRFI--RYMRRIHNSGPIVVHCSAGI 151
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 23172565  687 GRTGTYIVLDAMLKQIQQKNIVNVFGFLRHIRAQRNFLVQTEEQYIFLHDALVEAI 742
Cdd:cd14538  152 GRTGVLITIDVALGLIERDLPFDIQDIVKDLREQRQGMIQTKDQYIFCYKACLEVL 207
R-PTP-N cd14609
PTP-like domain of receptor-type tyrosine-protein phosphatase N; Receptor-type ...
476-742 2.69e-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: 2.69e-54
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23172565  476 FSREYEAIqneCISDDLP--CEHSQHPENKRKNRYLNITAYDHSRVHLHPTPGQKKNlDYINAN-FIDGYQKGHAFIGTQ 552
Cdd:cd14609   17 LAKEWQAL---CAYQAEPntCSTAQGEANVKKNRNPDFVPYDHARIKLKAESNPSRS-DYINASpIIEHDPRMPAYIATQ 92
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23172565  553 GPLPDTFDCFWRMIWEQRVAIIVMITNLVERGRRKCDMYWPKDGVETYGVIQVKLIEEEV-MSTYTVRTLQIkhlklkKK 631
Cdd:cd14609   93 GPLSHTIADFWQMVWENGCTVIVMLTPLVEDGVKQCDRYWPDEGSSLYHIYEVNLVSEHIwCEDFLVRSFYL------KN 166
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23172565  632 KQCNTEKLVYQYHYTNWPDHGTPDHPLPVLNFVKKSSAANPAEAGPIVVHCSAGVGRTGTYIVLDAMLKQIQQ--KNIvN 709
Cdd:cd14609  167 VQTQETRTLTQFHFLSWPAEGIPSSTRPLLDFRRKVNKCYRGRSCPIIVHCSDGAGRTGTYILIDMVLNRMAKgvKEI-D 245
                        250       260       270
                 ....*....|....*....|....*....|...
gi 23172565  710 VFGFLRHIRAQRNFLVQTEEQYIFLHDALVEAI 742
Cdd:cd14609  246 IAATLEHVRDQRPGMVRTKDQFEFALTAVAEEV 278
R-PTP-N2 cd14610
PTP-like domain of receptor-type tyrosine-protein phosphatase N2; Receptor-type ...
478-742 5.01e-54

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


Pssm-ID: 350458 [Multi-domain]  Cd Length: 283  Bit Score: 190.27  E-value: 5.01e-54
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23172565  478 REYEAIqneCISDDLP--CEHSQHPENKRKNRYLNITAYDHSRVHLHPTPGQKKNlDYINANFI-DGYQKGHAFIGTQGP 554
Cdd:cd14610   21 KEWEAL---CAYQAEPnaTNVAQREENVQKNRSLAVLPYDHSRIILKAENSHSHS-DYINASPImDHDPRNPAYIATQGP 96
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23172565  555 LPDTFDCFWRMIWEQRVAIIVMITNLVERGRRKCDMYWPKDGVETYGVIQVKLIEEEV-MSTYTVRTLQIkhlklkKKKQ 633
Cdd:cd14610   97 LPATVADFWQMVWESGCVVIVMLTPLAENGVKQCYHYWPDEGSNLYHIYEVNLVSEHIwCEDFLVRSFYL------KNLQ 170
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23172565  634 CNTEKLVYQYHYTNWPDHGTPDHPLPVLNFVKKSSAANPAEAGPIVVHCSAGVGRTGTYIVLDAML-KQIQQKNIVNVFG 712
Cdd:cd14610  171 TNETRTVTQFHFLSWNDQGVPASTRSLLDFRRKVNKCYRGRSCPIIVHCSDGAGRSGTYILIDMVLnKMAKGAKEIDIAA 250
                        250       260       270
                 ....*....|....*....|....*....|
gi 23172565  713 FLRHIRAQRNFLVQTEEQYIFLHDALVEAI 742
Cdd:cd14610  251 TLEHLRDQRPGMVQTKEQFEFALTAVAEEV 280
R-PTPc-R cd14611
catalytic domain of receptor-type tyrosine-protein phosphatase R; Receptor-type ...
505-735 7.15e-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: 7.15e-53
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23172565  505 KNRYLNITAYDHSRVHLHPTPGQKKNLDYINANFIDGYQ-KGHAFIGTQGPLPDTFDCFWRMIWEQRVAIIVMITNLVER 583
Cdd:cd14611    2 KNRYKTILPNPHSRVCLKPKNSNDSLSTYINANYIRGYGgKEKAFIATQGPMINTVNDFWQMVWQEDSPVIVMITKLKEK 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23172565  584 GRrKCDMYWP-KDGVetYGVIQVKLIEEEVMSTYTVRTLQIKhlklkkkkQCNTEKLVYQYHYTNWPDHGTPDHPLPVLN 662
Cdd:cd14611   82 NE-KCVLYWPeKRGI--YGKVEVLVNSVKECDNYTIRNLTLK--------QGSQSRSVKHYWYTSWPDHKTPDSAQPLLQ 150
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 23172565  663 F---VKKSSAANPAEaGPIVVHCSAGVGRTGTYIVLDAMLKQIQQKNIVNVFGFLRHIRAQRNFLVQTEEQYIFLH 735
Cdd:cd14611  151 LmldVEEDRLASPGR-GPVVVHCSAGIGRTGCFIATTIGCQQLKEEGVVDVLSIVCQLRVDRGGMVQTSEQYEFVH 225
PTPc-N5 cd14613
catalytic domain of tyrosine-protein phosphatase non-receptor type 5; Tyrosine-protein ...
504-738 1.90e-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: 1.90e-52
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23172565  504 RKNRYLNITAYDHSRVHLhPTPGQKKNLD-YINANFIDGY-QKGHAFIGTQGPLPDTFDCFWRMIWEQRVAIIVMITNLV 581
Cdd:cd14613   27 RKNRYKTILPNPHSRVCL-TSPDQDDPLSsYINANYIRGYgGEEKVYIATQGPTVNTVGDFWRMVWQERSPIIVMITNIE 105
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23172565  582 ERGRrKCDMYWPKDGVeTYGVIQVKLIEEEVMSTYTVRTLQIKHLklkkkkqcNTEKLVYQYHYTNWPDHGTPDHPLPVL 661
Cdd:cd14613  106 EMNE-KCTEYWPEEQV-TYEGIEITVKQVIHADDYRLRLITLKSG--------GEERGLKHYWYTSWPDQKTPDNAPPLL 175
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23172565  662 NFVKKSSAAN---PAEAGPIVVHCSAGVGRTGTYIVLDAMLKQIQQKNIVNVFGFLRHIRAQRNFLVQTEEQYIFLHDAL 738
Cdd:cd14613  176 QLVQEVEEARqqaEPNCGPVIVHCSAGIGRTGCFIATSICCKQLRNEGVVDILRTTCQLRLDRGGMIQTCEQYQFVHHVL 255
R-PTP-C-2 cd14558
PTP-like domain of receptor-type tyrosine-protein phosphatase C, repeat 2; Receptor-type ...
533-736 8.35e-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: 8.35e-52
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23172565  533 YINANFIDGYQKGHAFIGTQGPLPDTFDCFWRMIWEQRVAIIVMITNLVERGRRKCDMYWPkDGVETYGVIQVKLIEEEV 612
Cdd:cd14558    1 YINASFIDGYWGPKSLIATQGPLPDTIADFWQMIFQKKVKVIVMLTELKEGDQEQCAQYWG-DEKKTYGDIEVELKDTEK 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23172565  613 MSTYTVRTLQIKHLKLKKKKQcnteklVYQYHYTNWPDHGTPDHPLPVLNF---VKKSSAANPAEAG---PIVVHCSAGV 686
Cdd:cd14558   80 SPTYTVRVFEITHLKRKDSRT------VYQYQYHKWKGEELPEKPKDLVDMiksIKQKLPYKNSKHGrsvPIVVHCSDGS 153
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|
gi 23172565  687 GRTGTYIVLDAMLKQIQQKNIVNVFGFLRHIRAQRNFLVQTEEQYIFLHD 736
Cdd:cd14558  154 SRTGIFCALWNLLESAETEKVVDVFQVVKALRKQRPGMVSTLEQYQFLYD 203
PTPc-N3_4 cd14541
catalytic domain of tyrosine-protein phosphatase non-receptor type 21 and type 14; ...
532-741 1.02e-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: 1.02e-51
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23172565  532 DYINANFIDGYQKGHA----FIGTQGPLPDTFDCFWRMIWEQRVAIIVMITNLVERGRRKCDMYWPK-DGVETYGVIQVK 606
Cdd:cd14541    1 DYINANYVNMEIPGSGivnrYIAAQGPLPNTCADFWQMVWEQKSTLIVMLTTLVERGRVKCHQYWPDlGETMQFGNLQIT 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23172565  607 LIEEEVMSTYTVRTLQIkhlklkKKKQCNTEKLVYQYHYTNWPDHGTPDHPLPVLNFVKKSSAANPAEAGPIVVHCSAGV 686
Cdd:cd14541   81 CVSEEVTPSFAFREFIL------TNTNTGEERHITQMQYLAWPDHGVPDDSSDFLDFVKRVRQNRVGMVEPTVVHCSAGI 154
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 23172565  687 GRTGTYIVLDAMLKQIQQKNIVNVFGFLRHIRAQRNFLVQTEEQYIFLHDALVEA 741
Cdd:cd14541  155 GRTGVLITMETAMCLIEANEPVYPLDIVRTMRDQRAMLIQTPSQYRFVCEAILRV 209
PTPc-N3 cd14600
catalytic domain of tyrosine-protein phosphatase non-receptor type 3; Tyrosine-protein ...
500-739 3.90e-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: 181.59  E-value: 3.90e-51
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23172565  500 PENKRKNRYLNITAYDHSRVHLhptpgqKKNLDYINANFID----GYQKGHAFIGTQGPLPDTFDCFWRMIWEQRVAIIV 575
Cdd:cd14600   38 PQNMDKNRYKDVLPYDATRVVL------QGNEDYINASYVNmeipSANIVNKYIATQGPLPHTCAQFWQVVWEQKLSLIV 111
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23172565  576 MITNLVERGRRKCDMYWPK-DGVETYGVIQVKLIEEEVMSTYTVRTLQIkhlklkKKKQCNTEKLVYQYHYTNWPDHGTP 654
Cdd:cd14600  112 MLTTLTERGRTKCHQYWPDpPDVMEYGGFRVQCHSEDCTIAYVFREMLL------TNTQTGEERTVTHLQYVAWPDHGVP 185
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23172565  655 DHPLPVLNFVkKSSAANPAEAGPIVVHCSAGVGRTGTYIVLDAMLKQIQQKNIVNVFGFLRHIRAQRNFLVQTEEQYIFL 734
Cdd:cd14600  186 DDSSDFLEFV-NYVRSKRVENEPVLVHCSAGIGRTGVLVTMETAMCLTERNQPVYPLDIVRKMRDQRAMMVQTSSQYKFV 264

                 ....*
gi 23172565  735 HDALV 739
Cdd:cd14600  265 CEAIL 269
R-PTP-Z-2 cd17669
catalytic domain of receptor-type tyrosine-protein phosphatase Z, repeat 2; Receptor-type ...
818-1013 8.85e-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: 8.85e-51
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23172565  818 YINASWLHGFRRLRDFIVTQHPMAHTIKDFWQMVWDHNAQTVVLLSslDDINFAQ----FWPDEATPIESDHYRVKFLNK 893
Cdd:cd17669    1 YINASYIMGYYQSNEFIITQHPLLHTIKDFWRMIWDHNAQLIVMLP--DGQNMAEdefvYWPNKDEPINCETFKVTLIAE 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23172565  894 -----TNKSDYVSRDFVIQSIQDDYELTVKMLHCPSWPEMSNPNS-IYDFIVDVHERCNDyRNGPIVIVDRYGGAQACTF 967
Cdd:cd17669   79 ehkclSNEEKLIIQDFILEATQDDYVLEVRHFQCPKWPNPDSPISkTFELISIIKEEAAN-RDGPMIVHDEHGGVTAGTF 157
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*.
gi 23172565  968 CAISSLAIEMEYCSTANVYQYAKLYHNKRPGVWTSSEDIRVIYNIL 1013
Cdd:cd17669  158 CALTTLMHQLEKENSVDVYQVAKMINLMRPGVFTDIEQYQFLYKAI 203
R-PTPc-E-2 cd14622
catalytic domain of receptor-type tyrosine-protein phosphatase E, repeat 2; Receptor-type ...
532-735 2.04e-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: 2.04e-50
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23172565  532 DYINANFIDGYQKGHAFIGTQGPLPDTFDCFWRMIWEQRVAIIVMITNLVERGRRKCDMYWPKDGVETYGVIQVKLIEEE 611
Cdd:cd14622    1 DYINASFIDGYRQKDYFIATQGPLAHTVEDFWRMVWEWKCHTIVMLTELQEREQEKCVQYWPSEGSVTHGEITIEIKNDT 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23172565  612 VMSTYTVRTLQIkhlklkKKKQCNTEKLVYQYHYTNWPDHGTPDHPLPVLNFVKKSSAANPAEAG-PIVVHCSAGVGRTG 690
Cdd:cd14622   81 LLETISIRDFLV------TYNQEKQTRLVRQFHFHGWPEIGIPAEGKGMIDLIAAVQKQQQQTGNhPIVVHCSAGAGRTG 154
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*
gi 23172565  691 TYIVLDAMLKQIQQKNIVNVFGFLRHIRAQRNFLVQTEEQYIFLH 735
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 ...
533-742 1.39e-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: 1.39e-49
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23172565  533 YINANFI-DGYQKGHAFIGTQGPLPDTFDCFWRMIWEQRVAIIVMITNLVERGRRKCDMYWPKDGVETYGVIQVKLIEEE 611
Cdd:cd14546    1 YINASTIyDHDPRNPAYIATQGPLPHTIADFWQMIWEQGCVVIVMLTRLQENGVKQCARYWPEEGSEVYHIYEVHLVSEH 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23172565  612 VMST-YTVRTLQIkhlklkKKKQCNTEKLVYQYHYTNWPDHGTPDHPLPVLNFVKKSSAANPAEAGPIVVHCSAGVGRTG 690
Cdd:cd14546   81 IWCDdYLVRSFYL------KNLQTSETRTVTQFHFLSWPDEGIPASAKPLLEFRRKVNKSYRGRSCPIVVHCSDGAGRTG 154
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....
gi 23172565  691 TYIVLDAMLKQIQQ--KNIvNVFGFLRHIRAQRNFLVQTEEQYIFLHDALVEAI 742
Cdd:cd14546  155 TYILIDMVLNRMAKgaKEI-DIAATLEHLRDQRPGMVKTKDQFEFVLTAVAEEV 207
PTPc-N14 cd14599
catalytic domain of tyrosine-protein phosphatase non-receptor type 14; Tyrosine-protein ...
500-740 1.78e-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: 1.78e-49
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23172565  500 PENKRKNRYLNITAYDHSRVHLHPTpgQKKNLDYINANFIDGYQKGHA--FIGTQGPLPDTFDCFWRMIWEQRVAIIVMI 577
Cdd:cd14599   36 PENAERNRIREVVPYEENRVELVPT--KENNTGYINASHIKVTVGGEEwhYIATQGPLPHTCHDFWQMVWEQGVNVIAMV 113
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23172565  578 TNLVERGRRKCDMYWPKDGV----ETYGVIQVKLIEEEVMSTYTVRTLQIKHLKLkkkkqcNTEKLVYQYHYTNWPDHGT 653
Cdd:cd14599  114 TAEEEGGRSKSHRYWPKLGSkhssATYGKFKVTTKFRTDSGCYATTGLKVKHLLS------GQERTVWHLQYTDWPDHGC 187
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23172565  654 PDHPLPVLNFVKK--------------SSAANPaeagPIVVHCSAGVGRTGTYIVLDAMLKQIQQKNIVNVFGFLRHIRA 719
Cdd:cd14599  188 PEEVQGFLSYLEEiqsvrrhtnsmldsTKNCNP----PIVVHCSAGVGRTGVVILTELMIGCLEHNEKVEVPVMLRHLRE 263
                        250       260
                 ....*....|....*....|.
gi 23172565  720 QRNFLVQTEEQYIFLHDALVE 740
Cdd:cd14599  264 QRMFMIQTIAQYKFVYQVLIQ 284
PTPc-N21_14 cd14540
catalytic domain of tyrosine-protein phosphatase non-receptor type 21 and type 14; ...
533-740 1.17e-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: 1.17e-48
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23172565  533 YINANFIDGYQKGHA--FIGTQGPLPDTFDCFWRMIWEQRVAIIVMITNLVERGRRKCDMYWPKDGVE----TYGVIQVK 606
Cdd:cd14540    1 YINASHITATVGGKQrfYIAAQGPLQNTVGDFWQMVWEQGVYLVVMVTAEEEGGREKCFRYWPTLGGEhdalTFGEYKVS 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23172565  607 LIEEEVMSTYTVRTLQIkhlklkKKKQCNTEKLVYQYHYTNWPDHGTPDHPLPVLNFVKKSSA----ANPAEAG-----P 677
Cdd:cd14540   81 TKFSVSSGCYTTTGLRV------KHTLSGQSRTVWHLQYTDWPDHGCPEDVSGFLDFLEEINSvrrhTNQDVAGhnrnpP 154
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 23172565  678 IVVHCSAGVGRTGTYIVLDAMLKQIQQKNIVNVFGFLRHIRAQRNFLVQTEEQYIFLHDALVE 740
Cdd:cd14540  155 TLVHCSAGVGRTGVVILADLMLYCLDHNEELDIPRVLALLRHQRMLLVQTLAQYKFVYNVLIQ 217
R-PTP-G-2 cd17670
PTP-like domain of receptor-type tyrosine-protein phosphatase G, repeat 2; Receptor-type ...
818-1013 1.59e-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: 1.59e-48
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23172565  818 YINASWLHGFRRLRDFIVTQHPMAHTIKDFWQMVWDHNAQTVVLLSslDDINFAQ----FWPDEATPIESDHYRVKFLNK 893
Cdd:cd17670    1 YINASYIMGYYRSNEFIITQHPLPHTTKDFWRMIWDHNAQIIVMLP--DNQGLAEdefvYWPSREESMNCEAFTVTLISK 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23172565  894 -----TNKSDYVSRDFVIQSIQDDYELTVKMLHCPSWPEMSNP-NSIYDFIVDVHERCNDyRNGPIVIVDRYGGAQACTF 967
Cdd:cd17670   79 drlclSNEEQIIIHDFILEATQDDYVLEVRHFQCPKWPNPDAPiSSTFELINVIKEEALT-RDGPTIVHDEFGAVSAGTL 157
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*.
gi 23172565  968 CAISSLAIEMEYCSTANVYQYAKLYHNKRPGVWTSSEDIRVIYNIL 1013
Cdd:cd17670  158 CALTTLSQQLENENAVDVYQVAKMINLMRPGVFTDIEQYQFLYKAM 203
PHA02746 PHA02746
protein tyrosine phosphatase; Provisional
496-759 1.42e-47

protein tyrosine phosphatase; Provisional


Pssm-ID: 165113 [Multi-domain]  Cd Length: 323  Bit Score: 173.29  E-value: 1.42e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23172565   496 HSQHPENKRKNRYLNITAYDHSRVHLHpTPGQKKNLD-------------------YINANFIDGYQKGHAFIGTQGPLP 556
Cdd:PHA02746   45 HFLKKENLKKNRFHDIPCWDHSRVVIN-AHESLKMFDvgdsdgkkievtsednaenYIHANFVDGFKEANKFICAQGPKE 123
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23172565   557 DTFDCFWRMIWEQRVAIIVMITNlVERGRRKCDMYW--PKDGVETYGVIQVKLIEEEVMSTYTVRTLQIKHLKLkkkkqc 634
Cdd:PHA02746  124 DTSEDFFKLISEHESQVIVSLTD-IDDDDEKCFELWtkEEDSELAFGRFVAKILDIIEELSFTKTRLMITDKIS------ 196
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23172565   635 NTEKLVYQYHYTNWPDHGTPDHPLPVLNFV----------KKSSAANPAEAGPIVVHCSAGVGRTGTYIVLDAMLKQIQQ 704
Cdd:PHA02746  197 DTSREIHHFWFPDWPDNGIPTGMAEFLELInkvneeqaelIKQADNDPQTLGPIVVHCSAGIGRAGTFCAIDNALEQLEK 276
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 23172565   705 KNIVNVFGFLRHIRAQRNFLVQTEEQYIFLHDALVEAIasgetnlmaeqVEELKN 759
Cdd:PHA02746  277 EKEVCLGEIVLKIRKQRHSSVFLPEQYAFCYKALKYAI-----------IEEAKK 320
PTPc-N20 cd14596
catalytic domain of tyrosine-protein phosphatase non-receptor type 20; Tyrosine-protein ...
533-742 6.82e-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: 167.23  E-value: 6.82e-47
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23172565  533 YINANFID---GYQKgHAFIGTQGPLPDTFDCFWRMIWEQRVAIIVMITNLVERGRRKCDMYWPKDGVETYGV--IQVKL 607
Cdd:cd14596    1 YINASYITmpvGEEE-LFYIATQGPLPSTIDDFWQMVWENRSDVIAMMTREVERGKVKCHRYWPETLQEPMELenYQLRL 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23172565  608 IEEEVMSTYTVRTLQIkhlklkKKKQCNTEKLVYQYHYTNWPDHGTPDHPLPVLNFVKKSSAANpaEAGPIVVHCSAGVG 687
Cdd:cd14596   80 ENYQALQYFIIRIIKL------VEKETGENRLIKHLQFTTWPDHGTPQSSDQLVKFICYMRKVH--NTGPIVVHCSAGIG 151
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 23172565  688 RTGTYIVLDAMLKQIQQKNIVNVFGFLRHIRAQRNFLVQTEEQYIFLHDALVEAI 742
Cdd:cd14596  152 RAGVLICVDVLLSLIEKDLSFNIKDIVREMRQQRYGMIQTKDQYLFCYKVVLEVL 206
PTPc-N4 cd14601
catalytic domain of tyrosine-protein phosphatase non-receptor type 4; Tyrosine-protein ...
532-740 8.78e-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: 163.96  E-value: 8.78e-46
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23172565  532 DYINANFID----GYQKGHAFIGTQGPLPDTFDCFWRMIWEQRVAIIVMITNLVERGRRKCDMYWPK-DGVETYGVIQVK 606
Cdd:cd14601    1 DYINANYINmeipSSSIINRYIACQGPLPNTCSDFWQMTWEQGSSMVVMLTTQVERGRVKCHQYWPEpSGSSSYGGFQVT 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23172565  607 LIEEEVMSTYTVRTLQIkhlklkKKKQCNTEKLVYQYHYTNWPDHGTPDHPLPVLNFVKKSSAANPAEAGPIVVHCSAGV 686
Cdd:cd14601   81 CHSEEGNPAYVFREMTL------TNLEKNESRPLTQIQYIAWPDHGVPDDSSDFLDFVCLVRNKRAGKDEPVVVHCSAGI 154
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....
gi 23172565  687 GRTGTYIVLDAMLKQIQQKNIVNVFGFLRHIRAQRNFLVQTEEQYIFLHDALVE 740
Cdd:cd14601  155 GRTGVLITMETAMCLIECNQPVYPLDIVRTMRDQRAMMIQTPSQYRFVCEAILK 208
PHA02747 PHA02747
protein tyrosine phosphatase; Provisional
495-735 6.09e-45

protein tyrosine phosphatase; Provisional


Pssm-ID: 165114 [Multi-domain]  Cd Length: 312  Bit Score: 165.17  E-value: 6.09e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23172565   495 EHSQHPENKRKNRYLNITAYDHSRVHLHPTPGQKKNldYINANFIDGYQKGHAFIGTQGPLPDTFDCFWRMIWEQRVAII 574
Cdd:PHA02747   44 ANFEKPENQPKNRYWDIPCWDHNRVILDSGGGSTSD--YIHANWIDGFEDDKKFIATQGPFAETCADFWKAVWQEHCSII 121
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23172565   575 VMIT-NLVERGRRKCDMYW--PKDGVETYGVIQVKLIEEEVMSTYTVRTLQIKHLKLkkkkqcNTEKLVYQYHYTNWPDH 651
Cdd:PHA02747  122 VMLTpTKGTNGEEKCYQYWclNEDGNIDMEDFRIETLKTSVRAKYILTLIEITDKIL------KDSRKISHFQCSEWFED 195
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23172565   652 GTP-DHP-----LPVLNFVKKSSAA--NPAEA--GPIVVHCSAGVGRTGTYIVLDAMLKQIQQKNIVNVFGFLRHIRAQR 721
Cdd:PHA02747  196 ETPsDHPdfikfIKIIDINRKKSGKlfNPKDAllCPIVVHCSDGVGKTGIFCAVDICLNQLVKRKAICLAKTAEKIREQR 275
                         250
                  ....*....|....
gi 23172565   722 NFLVQTEEQYIFLH 735
Cdd:PHA02747  276 HAGIMNFDDYLFIQ 289
PTP-N23 cd14539
PTP-like domain of tyrosine-protein phosphatase non-receptor type 23; Tyrosine-protein ...
533-736 6.81e-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: 6.81e-45
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23172565  533 YINANFIDGYQKGHA-FIGTQGPLPDTFDCFWRMIWEQRVAIIVMITNLVERGRRKCDMYWPKD-GVE-TYGVIQVKLIE 609
Cdd:cd14539    1 YINASLIEDLTPYCPrFIATQAPLPGTAADFWLMVYEQQVSVIVMLVSEQENEKQKVHRYWPTErGQAlVYGAITVSLQS 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23172565  610 EEVMSTYTVRTLQIkhlklkkkkQCNTEKL---VYQYHYTNWPDHGTPDHPLPVLNFVKKSSA---ANPAEAGPIVVHCS 683
Cdd:cd14539   81 VRTTPTHVERIISI---------QHKDTRLsrsVVHLQFTTWPELGLPDSPNPLLRFIEEVHShylQQRSLQTPIVVHCS 151
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....
gi 23172565  684 AGVGRTGTYIVLDAMLKQIQQKN-IVNVFGFLRHIRAQRNFLVQTEEQYIFLHD 736
Cdd:cd14539  152 SGVGRTGAFCLLYAAVQEIEAGNgIPDLPQLVRKMRQQRKYMLQEKEHLKFCYE 205
R-PTPc-typeIIb-2 cd14556
PTP domain of type IIb (or R2B) subfamily receptor-type tyrosine-protein phosphatases, repeat ...
533-736 2.78e-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: 2.78e-44
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23172565  533 YINANFIDGYQKGHAFIGTQGPLPDTFDCFWRMIWEQRVAIIVMItNLVERGRRKCDMYWPKDGVETYGVIQVKLIEEEV 612
Cdd:cd14556    1 YINAALLDSYKQPAAFIVTQHPLPNTVTDFWRLVYDYGCTSIVML-NQLDPKDQSCPQYWPDEGSGTYGPIQVEFVSTTI 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23172565  613 MSTYTVRTLQIkhlklkkkkqCNTEK------LVYQYHYTNWPDHG----TPDHPLPVLNFVKKSSAAnpAEAGPIVVHC 682
Cdd:cd14556   80 DEDVISRIFRL----------QNTTRpqegyrMVQQFQFLGWPRDRdtppSKRALLKLLSEVEKWQEQ--SGEGPIVVHC 147
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....
gi 23172565  683 SAGVGRTGTYIVLDAMLKQIQQKNIVNVFGFLRHIRAQRNFLVQTEEQYIFLHD 736
Cdd:cd14556  148 LNGVGRSGVFCAISSVCERIKVENVVDVFQAVKTLRNHRPNMVETEEQYKFCYD 201
PHA02738 PHA02738
hypothetical protein; Provisional
477-738 1.28e-43

hypothetical protein; Provisional


Pssm-ID: 222923 [Multi-domain]  Cd Length: 320  Bit Score: 161.63  E-value: 1.28e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23172565   477 SREYEAIqnecISDDLPCEHSQHPENKRKNRYLNITAYDHSRVHLhptPGQKKNLDYINANFIDGYQKGHAFIGTQGPLP 556
Cdd:PHA02738   28 TREHQKV----ISEKVDGTFNAEKKNRKLNRYLDAVCFDHSRVIL---PAERNRGDYINANYVDGFEYKKKFICGQAPTR 100
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23172565   557 DTFDCFWRMIWEQRVAIIVMITNLVERGRRKCDMYWP--KDGVETYGVIQVKLIEEEVMSTYTVRTLQIKHLKLKKkkqc 634
Cdd:PHA02738  101 QTCYDFYRMLWMEHVQIIVMLCKKKENGREKCFPYWSdvEQGSIRFGKFKITTTQVETHPHYVKSTLLLTDGTSAT---- 176
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23172565   635 nteKLVYQYHYTNWPDHGTPDHPLPVLNFV------KKSSAANPAEAG-------PIVVHCSAGVGRTGTYIVLDAMLKQ 701
Cdd:PHA02738  177 ---QTVTHFNFTAWPDHDVPKNTSEFLNFVlevrqcQKELAQESLQIGhnrlqppPIVVHCNAGLGRTPCYCVVDISISR 253
                         250       260       270
                  ....*....|....*....|....*....|....*..
gi 23172565   702 IQQKNIVNVFGFLRHIRAQRNFLVQTEEQYIFLHDAL 738
Cdd:PHA02738  254 FDACATVSIPSIVSSIRNQRYYSLFIPFQYFFCYRAV 290
PTPc cd00047
catalytic domain of protein tyrosine phosphatases; Protein tyrosine phosphatases (PTP, EC 3.1. ...
818-1010 1.59e-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: 1.59e-43
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23172565  818 YINASWLHGFRRLRDFIVTQHPMAHTIKDFWQMVWDHNAQTVVLLSSLDDIN---FAQFWPDE-ATPIESDHYRVKFLNK 893
Cdd:cd00047    1 YINASYIDGYRGPKEYIATQGPLPNTVEDFWRMVWEQKVSVIVMLTNLVEKGrekCERYWPEEgGKPLEYGDITVTLVSE 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23172565  894 TNKSDYVSRDFVIQSIQDDYELTVKMLHCPSWPEMSNPNSIYDFI--VDVHERCNDYRNGPIVIVDRYGGAQACTFCAIS 971
Cdd:cd00047   81 EELSDYTIRTLELSPKGCSESREVTHLHYTGWPDHGVPSSPEDLLalVRRVRKEARKPNGPIVVHCSAGVGRTGTFIAID 160
                        170       180       190
                 ....*....|....*....|....*....|....*....
gi 23172565  972 SLAIEMEYCSTANVYQYAKLYHNKRPGVWTSSEDIRVIY 1010
Cdd:cd00047  161 ILLERLEAEGEVDVFEIVKALRKQRPGMVQTLEQYEFIY 199
PHA02742 PHA02742
protein tyrosine phosphatase; Provisional
459-733 1.82e-43

protein tyrosine phosphatase; Provisional


Pssm-ID: 165109 [Multi-domain]  Cd Length: 303  Bit Score: 160.55  E-value: 1.82e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23172565   459 NEFAKHVASLHADGDIG--FSREYEAIQNECISddLPCEHSQHPENKRKNRYLNITAYDHSRVHLhptPGQKKNLDYINA 536
Cdd:PHA02742    9 NSFAKNCEQLIEESNLAeiLKEEHEHIMQEIVA--FSCNESLELKNMKKCRYPDAPCFDRNRVIL---KIEDGGDDFINA 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23172565   537 NFIDGYQKGHAFIGTQGPLPDTFDCFWRMIWEQRVAIIVMITNLVERGRRKCDMYW--PKDGVETYGVIQVKLIEEEVMS 614
Cdd:PHA02742   84 SYVDGHNAKGRFICTQAPLEETALDFWQAIFQDQVRVIVMITKIMEDGKEACYPYWmpHERGKATHGEFKIKTKKIKSFR 163
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23172565   615 TYTVRTLQIkhlklkkkKQCNTEKL--VYQYHYTNWPDHGTPDHPLPVLNFV-----------KKSSAANPAEAGPIVVH 681
Cdd:PHA02742  164 NYAVTNLCL--------TDTNTGASldIKHFAYEDWPHGGLPRDPNKFLDFVlavreadlkadVDIKGENIVKEPPILVH 235
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|..
gi 23172565   682 CSAGVGRTGTYIVLDAMLKQIQQKNIVNVFGFLRHIRAQRNFLVQTEEQYIF 733
Cdd:PHA02742  236 CSAGLDRAGAFCAIDICISKYNERAIIPLLSIVRDLRKQRHNCLSLPQQYIF 287
PTPc_plant_PTP1 cd17658
protein tyrosine phosphatase 1 from Arabidopsis thaliana and similar plant PTPs; Arabidopsis ...
533-733 2.56e-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: 2.56e-43
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23172565  533 YINANFI--DGYQKGHAFIGTQGPLPDTFDCFWRMIWEQRVAIIVMITNLVERGRR-KCDMYWPKD--GVETYGVIQVKL 607
Cdd:cd17658    1 YINASLVetPASESLPKFIATQGPLPHTFEDFWEMVIQQRCPVIIMLTRLVDNYSTaKCADYFPAEenESREFGRISVTN 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23172565  608 IEEEVMST-YTVRTLQIKHLKLKKKKQCnteklVYQYHYTNWPDHGTPDHPLPVLNFVKKSSAAnPAEAGPIVVHCSAGV 686
Cdd:cd17658   81 KKLKHSQHsITLRVLEVQYIESEEPPLS-----VLHIQYPEWPDHGVPKDTRSVRELLKRLYGI-PPSAGPIVVHCSAGI 154
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*....
gi 23172565  687 GRTGTYIVLDAMLKQIQQKNI--VNVFGFLRHIRAQRNFLVQTEEQYIF 733
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 ...
788-1010 5.36e-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: 5.36e-42
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23172565  788 VNSIKNRGA-IFPIEGSRVHLTPKPGEDGSDYINASWLHGFRRLRDFIVTQHPMAHTIKDFWQMVWDHNAQTVVLLSSLD 866
Cdd:cd14554    5 CNKFKNRLVnILPYESTRVCLQPIRGVEGSDYINASFIDGYRQRGAYIATQGPLAETTEDFWRMLWEHNSTIIVMLTKLR 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23172565  867 DINF---AQFWPDEaTPIESDHYRVKFLNKTNKSDYVSRDFVIQSIQDDYELTVKMLHCPSWPEMSNPNS---IYDFIVD 940
Cdd:cd14554   85 EMGRekcHQYWPAE-RSARYQYFVVDPMAEYNMPQYILREFKVTDARDGQSRTVRQFQFTDWPEQGVPKSgegFIDFIGQ 163
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 23172565  941 VHERCNDY-RNGPIVIVDRYGGAQACTFCAISSLAIEMEYCSTANVYQYAKLYHNKRPGVWTSSEDIRVIY 1010
Cdd:cd14554  164 VHKTKEQFgQEGPITVHCSAGVGRTGVFITLSIVLERMRYEGVVDVFQTVKLLRTQRPAMVQTEDQYQFCY 234
COG5599 COG5599
Protein tyrosine phosphatase [Signal transduction mechanisms];
496-734 1.94e-41

Protein tyrosine phosphatase [Signal transduction mechanisms];


Pssm-ID: 444335 [Multi-domain]  Cd Length: 282  Bit Score: 154.09  E-value: 1.94e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23172565  496 HSQHPENKRKNRYLNITAYDHSRVhlhptpgqKKNLDYINANFIDGYQKgHAFIGTQGPLPDTFDCFWRMIWEQRVAIIV 575
Cdd:COG5599   36 YLQNINGSPLNRFRDIQPYKETAL--------RANLGYLNANYIQVIGN-HRYIATQYPLEEQLEDFFQMLFDNNTPVLV 106
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23172565  576 MITNLVERGRRKCDM--YWPKDGVETYGVIQVKLIEEEVMST-YTVRTLQIKHLklkkkkQCNTEKL-VYQYHYTNWPDH 651
Cdd:COG5599  107 VLASDDEISKPKVKMpvYFRQDGEYGKYEVSSELTESIQLRDgIEARTYVLTIK------GTGQKKIeIPVLHVKNWPDH 180
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23172565  652 GTPD----HPLpvLNFVKKSSAANPAEAGPIVVHCSAGVGRTGTYIVLDAMLKQIQQKNI--VNVFGFLRHIRAQRNF-L 724
Cdd:COG5599  181 GAISaealKNL--ADLIDKKEKIKDPDKLLPVVHCRAGVGRTGTLIACLALSKSINALVQitLSVEEIVIDMRTSRNGgM 258
                        250
                 ....*....|
gi 23172565  725 VQTEEQYIFL 734
Cdd:COG5599  259 VQTSEQLDVL 268
R-PTP-D-2 cd14628
PTP-like domain of receptor-type tyrosine-protein phosphatase D, repeat 2; Receptor-type ...
753-1010 1.13e-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: 1.13e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23172565  753 QVEELKNCTPyLEQQYKNIIQFQPKDIHIASAMKQVNSIKNRGA-IFPIEGSRVHLTPKPGEDGSDYINASWLHGFRRLR 831
Cdd:cd14628   17 QIETGENVTG-MELEFKRLASSKAHTSRFISANLPCNKFKNRLVnIMPYESTRVCLQPIRGVEGSDYINASFIDGYRQQK 95
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23172565  832 DFIVTQHPMAHTIKDFWQMVWDHNAQTVVLLSSLDDINFA---QFWPDEATPiESDHYRVKFLNKTNKSDYVSRDFVIQS 908
Cdd:cd14628   96 AYIATQGPLAETTEDFWRMLWEHNSTIVVMLTKLREMGREkchQYWPAERSA-RYQYFVVDPMAEYNMPQYILREFKVTD 174
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23172565  909 IQDDYELTVKMLHCPSWPEMSNPNS---IYDFIVDVHERCNDY-RNGPIVIVDRYGGAQACTFCAISSLAIEMEYCSTAN 984
Cdd:cd14628  175 ARDGQSRTVRQFQFTDWPEQGVPKSgegFIDFIGQVHKTKEQFgQDGPISVHCSAGVGRTGVFITLSIVLERMRYEGVVD 254
                        250       260
                 ....*....|....*....|....*.
gi 23172565  985 VYQYAKLYHNKRPGVWTSSEDIRVIY 1010
Cdd:cd14628  255 IFQTVKMLRTQRPAMVQTEDQYQFCY 280
PTPc_motif smart00404
Protein tyrosine phosphatase, catalytic domain motif;
640-740 1.16e-37

Protein tyrosine phosphatase, catalytic domain motif;


Pssm-ID: 214649 [Multi-domain]  Cd Length: 105  Bit Score: 136.72  E-value: 1.16e-37
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23172565     640 VYQYHYTNWPDHGTPDHPLPVLNFVKKSSAANPAEA--GPIVVHCSAGVGRTGTYIVLDAMLKQIQQKNI-VNVFGFLRH 716
Cdd:smart00404    2 VKHYHYTGWPDHGVPESPDSILELLRAVKKNLNQSEssGPVVVHCSAGVGRTGTFVAIDILLQQLEAEAGeVDIFDTVKE 81
                            90       100
                    ....*....|....*....|....
gi 23172565     717 IRAQRNFLVQTEEQYIFLHDALVE 740
Cdd:smart00404   82 LRSQRPGMVQTEEQYLFLYRALLE 105
PTPc_DSPc smart00012
Protein tyrosine phosphatase, catalytic domain, undefined specificity; Protein tyrosine ...
640-740 1.16e-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: 1.16e-37
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23172565     640 VYQYHYTNWPDHGTPDHPLPVLNFVKKSSAANPAEA--GPIVVHCSAGVGRTGTYIVLDAMLKQIQQKNI-VNVFGFLRH 716
Cdd:smart00012    2 VKHYHYTGWPDHGVPESPDSILELLRAVKKNLNQSEssGPVVVHCSAGVGRTGTFVAIDILLQQLEAEAGeVDIFDTVKE 81
                            90       100
                    ....*....|....*....|....
gi 23172565     717 IRAQRNFLVQTEEQYIFLHDALVE 740
Cdd:smart00012   82 LRSQRPGMVQTEEQYLFLYRALLE 105
PTPc-N21 cd14598
catalytic domain of tyrosine-protein phosphatase non-receptor type 21; Tyrosine-protein ...
533-740 4.17e-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: 4.17e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23172565  533 YINANFIDGYQKGHA--FIGTQGPLPDTFDCFWRMIWEQRVAIIVMITNLVERGRRKCDMYWPKDGVE----TYGVIQVK 606
Cdd:cd14598    1 YINASHIKVTVGGKEwdYIATQGPLQNTCQDFWQMVWEQGVAIIAMVTAEEEGGREKSFRYWPRLGSRhntvTYGRFKIT 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23172565  607 LIEEEVMSTYTVRTLQIKHLKLkkkkqcNTEKLVYQYHYTNWPDHGTPDHPLPVLNFVKK--------SSAANPAEAG-P 677
Cdd:cd14598   81 TRFRTDSGCYATTGLKIKHLLT------GQERTVWHLQYTDWPEHGCPEDLKGFLSYLEEiqsvrrhtNSTIDPKSPNpP 154
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 23172565  678 IVVHCSAGVGRTGTYIVLDAMLKQIQQKNIVNVFGFLRHIRAQRNFLVQTEEQYIFLHDALVE 740
Cdd:cd14598  155 VLVHCSAGVGRTGVVILSEIMIACLEHNEMLDIPRVLDMLRQQRMMMVQTLSQYTFVYKVLIQ 217
R-PTP-S-2 cd14627
PTP-like domain of receptor-type tyrosine-protein phosphatase S, repeat 2; Receptor-type ...
753-1010 1.63e-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: 1.63e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23172565  753 QVEELKNCTPyLEQQYKNIIQFQPKDIHIASAMKQVNSIKNRGA-IFPIEGSRVHLTPKPGEDGSDYINASWLHGFRRLR 831
Cdd:cd14627   18 QVEVGEHVTG-MELEFKRLANSKAHTSRFISANLPCNKFKNRLVnIMPYETTRVCLQPIRGVEGSDYINASFIDGYRQQK 96
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23172565  832 DFIVTQHPMAHTIKDFWQMVWDHNAQTVVLLSSLDDINFA---QFWPDEATPiESDHYRVKFLNKTNKSDYVSRDFVIQS 908
Cdd:cd14627   97 AYIATQGPLAETTEDFWRMLWENNSTIVVMLTKLREMGREkchQYWPAERSA-RYQYFVVDPMAEYNMPQYILREFKVTD 175
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23172565  909 IQDDYELTVKMLHCPSWPEMSNPNS---IYDFIVDVHERCNDY-RNGPIVIVDRYGGAQACTFCAISSLAIEMEYCSTAN 984
Cdd:cd14627  176 ARDGQSRTVRQFQFTDWPEQGVPKSgegFIDFIGQVHKTKEQFgQDGPISVHCSAGVGRTGVFITLSIVLERMRYEGVVD 255
                        250       260
                 ....*....|....*....|....*.
gi 23172565  985 VYQYAKLYHNKRPGVWTSSEDIRVIY 1010
Cdd:cd14627  256 IFQTVKMLRTQRPAMVQTEDEYQFCY 281
R-PTP-F-2 cd14629
PTP-like domain of receptor-type tyrosine-protein phosphatase F, repeat 2; Receptor-type ...
764-1010 6.44e-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: 6.44e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23172565  764 LEQQYKNIIQFQPKDIHIASAMKQVNSIKNRGA-IFPIEGSRVHLTPKPGEDGSDYINASWLHGFRRLRDFIVTQHPMAH 842
Cdd:cd14629   28 MELEFKLLANSKAHTSRFISANLPCNKFKNRLVnIMPYELTRVCLQPIRGVEGSDYINASFIDGYRQQKAYIATQGPLAE 107
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23172565  843 TIKDFWQMVWDHNAQTVVLLSSLDDINFA---QFWPDEATPiESDHYRVKFLNKTNKSDYVSRDFVIQSIQDDYELTVKM 919
Cdd:cd14629  108 TTEDFWRMLWEHNSTIVVMLTKLREMGREkchQYWPAERSA-RYQYFVVDPMAEYNMPQYILREFKVTDARDGQSRTIRQ 186
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23172565  920 LHCPSWPEMSNPNS---IYDFIVDVHERCNDY-RNGPIVIVDRYGGAQACTFCAISSLAIEMEYCSTANVYQYAKLYHNK 995
Cdd:cd14629  187 FQFTDWPEQGVPKTgegFIDFIGQVHKTKEQFgQDGPITVHCSAGVGRTGVFITLSIVLERMRYEGVVDMFQTVKTLRTQ 266
                        250
                 ....*....|....*
gi 23172565  996 RPGVWTSSEDIRVIY 1010
Cdd:cd14629  267 RPAMVQTEDQYQLCY 281
R-PTPc-T-2 cd14634
PTP domain of receptor-type tyrosine-protein phosphatase T, repeat 2; Receptor-type ...
533-740 1.02e-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: 1.02e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23172565  533 YINANFIDGYQKGHAFIGTQGPLPDTFDCFWRMIWEQRVAIIVMITNLveRGRRKCDMYWPKDGVETYGVIQVKLIEEEV 612
Cdd:cd14634    1 YINAALMDSHKQPAAFIVTQHPLPNTVADFWRLVFDYNCSSVVMLNEM--DAAQLCMQYWPEKTSCCYGPIQVEFVSADI 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23172565  613 MSTYTVRTLQIkhlklkkkkqCNTEK------LVYQYHYTNWPDH-GTPDHPLPVLNFVK---KSSAANPAEAGPIVVHC 682
Cdd:cd14634   79 DEDIISRIFRI----------CNMARpqdgyrIVQHLQYIGWPAYrDTPPSKRSILKVVRrleKWQEQYDGREGRTVVHC 148
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 23172565  683 SAGVGRTGTYIVLDAMLKQIQQKNIVNVFGFLRHIRAQRNFLVQTEEQYIFLHDALVE 740
Cdd:cd14634  149 LNGGGRSGTFCAICSVCEMIQQQNIIDVFHTVKTLRNNKSNMVETLEQYKFVYEVALE 206
R-PTPc-A-2 cd14623
catalytic domain of receptor-type tyrosine-protein phosphatase A, repeat 2; Receptor-type ...
797-1013 1.46e-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: 1.46e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23172565  797 IFPIEGSRVHLTPKPGEDGSDYINASWLHGFRRLRDFIVTQHPMAHTIKDFWQMVWDHNAQTVVLLSSLDDI---NFAQF 873
Cdd:cd14623    5 IIPYEFNRVIIPVKRGEENTDYVNASFIDGYRQKDSYIASQGPLQHTIEDFWRMIWEWKSCSIVMLTELEERgqeKCAQY 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23172565  874 WPDEATPIESDhYRVKFLNKTNKSDYVSRDFVIQSIQDDYELTVKMLHCPSWPEMSNPNS---IYDFIVDVHERCNDYRN 950
Cdd:cd14623   85 WPSDGSVSYGD-ITIELKKEEECESYTVRDLLVTNTRENKSRQIRQFHFHGWPEVGIPSDgkgMINIIAAVQKQQQQSGN 163
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 23172565  951 GPIVIVDRYGGAQACTFCAISSLAIEMEYCSTANVYQYAKLYHNKRPGVWTSSEDIRVIYNIL 1013
Cdd:cd14623  164 HPITVHCSAGAGRTGTFCALSTVLERVKAEGILDVFQTVKSLRLQRPHMVQTLEQYEFCYKVV 226
R-PTPc-typeIIb-2 cd14556
PTP domain of type IIb (or R2B) subfamily receptor-type tyrosine-protein phosphatases, repeat ...
818-1010 2.51e-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: 119.05  E-value: 2.51e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23172565  818 YINASWLHGFRRLRDFIVTQHPMAHTIKDFWQMVWDHNAQTVVLLSSLDDIN--FAQFWPDEAT----PIEsdhyrVKFL 891
Cdd:cd14556    1 YINAALLDSYKQPAAFIVTQHPLPNTVTDFWRLVYDYGCTSIVMLNQLDPKDqsCPQYWPDEGSgtygPIQ-----VEFV 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23172565  892 NKTNKSDYVSRDFVIQSIQDDYE--LTVKMLHCPSWPE-----MSnPNSIYDFIVDVHERCNDYRNGPIVIVDRYGGAQA 964
Cdd:cd14556   76 STTIDEDVISRIFRLQNTTRPQEgyRMVQQFQFLGWPRdrdtpPS-KRALLKLLSEVEKWQEQSGEGPIVVHCLNGVGRS 154
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*.
gi 23172565  965 CTFCAISSLAIEMEYCSTANVYQYAKLYHNKRPGVWTSSEDIRVIY 1010
Cdd:cd14556  155 GVFCAISSVCERIKVENVVDVFQAVKTLRNHRPNMVETEEQYKFCY 200
R-PTPc-A-E-2 cd14552
catalytic domain of receptor-type tyrosine-protein phosphatase A and E, repeat 2; ...
818-1013 1.29e-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: 1.29e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23172565  818 YINASWLHGFRRLRDFIVTQHPMAHTIKDFWQMVWDHNAQTVVLLSSLDDIN---FAQFWPDEATpIESDHYRVKFLNKT 894
Cdd:cd14552    1 YINASFIDGYRQKDAYIATQGPLDHTVEDFWRMIWEWKSCSIVMLTEIKERSqnkCAQYWPEDGS-VSSGDITVELKDQT 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23172565  895 NKSDYVSRDFVIQSIQDDYELTVKMLHCPSWPEM---SNPNSIYDFIVDVHERCNDYRNGPIVIVDRYGGAQACTFCAIS 971
Cdd:cd14552   80 DYEDYTLRDFLVTKGKGGSTRTVRQFHFHGWPEVgipDNGKGMIDLIAAVQKQQQQSGNHPITVHCSAGAGRTGTFCALS 159
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|..
gi 23172565  972 SLAIEMEYCSTANVYQYAKLYHNKRPGVWTSSEDIRVIYNIL 1013
Cdd:cd14552  160 TVLERVKAEGVLDVFQVVKSLRLQRPHMVQTLEQYEFCYKVV 201
R3-PTPc cd14548
catalytic domain of R3 subfamily receptor-type tyrosine-protein phosphatases and similar ...
797-986 4.50e-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: 4.50e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23172565  797 IFPIEGSRVHLTPKPGEDGSDYINASWLHGFRRLRDFIVTQHPMAHTIKDFWQMVWDHNAQTVVLLSSLDD---INFAQF 873
Cdd:cd14548    5 ILPYDHSRVKLIPINEEEGSDYINANYIPGYNSPREFIATQGPLPGTKDDFWRMVWEQNSHTIVMLTQCMEkgrVKCDHY 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23172565  874 WPDEATPIESDHYRVKFLNKTNKSDYVSRDFVIQSIQDdyELTVKMLHCPSWPEMSNPN---SIYDFIVDVHERCNDyRN 950
Cdd:cd14548   85 WPFDQDPVYYGDITVTMLSESVLPDWTIREFKLERGDE--VRSVRQFHFTAWPDHGVPEapdSLLRFVRLVRDYIKQ-EK 161
                        170       180       190
                 ....*....|....*....|....*....|....*.
gi 23172565  951 GPIVIVDRYGGAQACTFCAISSLAIEMEYCSTANVY 986
Cdd:cd14548  162 GPTIVHCSAGVGRTGTFIALDRLLQQIESEDYVDIF 197
R-PTPc-K-2 cd14636
PTP domain of receptor-type tyrosine-protein phosphatase K, repeat 2; Receptor-type ...
533-740 1.44e-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: 1.44e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23172565  533 YINANFIDGYQKGHAFIGTQGPLPDTFDCFWRMIWEQRVAIIVMITNL-VERGrrkCDMYWPKDGVETYGVIQVKLIEEE 611
Cdd:cd14636    1 YINAALMDSYRQPAAFIVTQHPLPNTVKDFWRLVYDYGCTSIVMLNEVdLAQG---CPQYWPEEGMLRYGPIQVECMSCS 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23172565  612 VMSTYTVRTLQIkhlklkkkkqCNTEK------LVYQYHYTNWPDH----GTPDHPLPVLNFVKKSSAANPAEAGPIVVH 681
Cdd:cd14636   78 MDCDVISRIFRI----------CNLTRpqegylMVQQFQYLGWASHrevpGSKRSFLKLILQVEKWQEECDEGEGRTIIH 147
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 23172565  682 CSAGVGRTGTYIVLDAMLKQIQQKNIVNVFGFLRHIRAQRNFLVQTEEQYIFLHDALVE 740
Cdd:cd14636  148 CLNGGGRSGMFCAISIVCEMIKRQNVVDVFHAVKTLRNSKPNMVETPEQYRFCYDVALE 206
R-PTPc-E-2 cd14622
catalytic domain of receptor-type tyrosine-protein phosphatase E, repeat 2; Receptor-type ...
817-1013 1.97e-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: 1.97e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23172565  817 DYINASWLHGFRRLRDFIVTQHPMAHTIKDFWQMVWDHNAQTVVLLSSLDDI---NFAQFWPDEATPIESDhYRVKFLNK 893
Cdd:cd14622    1 DYINASFIDGYRQKDYFIATQGPLAHTVEDFWRMVWEWKCHTIVMLTELQEReqeKCVQYWPSEGSVTHGE-ITIEIKND 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23172565  894 TNKSDYVSRDFVIQSIQDDYELTVKMLHCPSWPEMSNP---NSIYDFIVDVHERCNDYRNGPIVIVDRYGGAQACTFCAI 970
Cdd:cd14622   80 TLLETISIRDFLVTYNQEKQTRLVRQFHFHGWPEIGIPaegKGMIDLIAAVQKQQQQTGNHPIVVHCSAGAGRTGTFIAL 159
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|...
gi 23172565  971 SSLAIEMEYCSTANVYQYAKLYHNKRPGVWTSSEDIRVIYNIL 1013
Cdd:cd14622  160 SNILERVKAEGLLDVFQTVKSLRLQRPHMVQTLEQYEFCYRVV 202
R-PTPc-V cd14618
catalytic domain of receptor-type tyrosine-protein phosphatase V; Receptor-type ...
797-997 3.52e-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: 3.52e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23172565  797 IFPIEGSRVHLTPKPGEDGSDYINASWLHGFRRLRDFIVTQHPMAHTIKDFWQMVWDHNAQTVVLLS-SLDD--INFAQF 873
Cdd:cd14618    6 VLPYDHSRVRLSQLGGEPHSDYINANFIPGYTSPQEFIATQGPLKKTIEDFWRLVWEQQVCNIIMLTvGMENgrVLCDHY 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23172565  874 WPDEATPIESDHYRVKFLNKTNKSDYVSRDFVIQSIQDDYELTVKMLHCPSWPEMS---NPNSIYDFIVDVHERCNDYRN 950
Cdd:cd14618   86 WPSESTPVSYGHITVHLLAQSSEDEWTRREFKLWHEDLRKERRVKHLHYTAWPDHGipeSTSSLMAFRELVREHVQATKG 165
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*...
gi 23172565  951 -GPIVIVDRYGGAQACTFCAISSLAIEMEYCSTANVYQYAKLYHNKRP 997
Cdd:cd14618  166 kGPTLVHCSAGVGRSGTFIALDRLLRQLKEEKVVDVFNTVYILRMHRY 213
R-PTPc-A-1 cd14621
catalytic domain of receptor-type tyrosine-protein phosphatase A, repeat 1; Receptor-type ...
783-996 3.68e-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: 3.68e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23172565  783 SAMKQVNSIKNRGA-IFPIEGSRVHLTPKPGEDGSDYINASWLHGFRRLRDFIVTQHPMAHTIKDFWQMVWDHNAQTVVL 861
Cdd:cd14621   46 AASKEENKEKNRYVnILPYDHSRVHLTPVEGVPDSDYINASFINGYQEKNKFIAAQGPKEETVNDFWRMIWEQNTATIVM 125
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23172565  862 LSSL---DDINFAQFWPDEATPIESDhYRVKFLNKTNKSDYVSRDFVIQSIQD----DYELTVKMLHCPSWPEMS---NP 931
Cdd:cd14621  126 VTNLkerKECKCAQYWPDQGCWTYGN-IRVSVEDVTVLVDYTVRKFCIQQVGDvtnkKPQRLITQFHFTSWPDFGvpfTP 204
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 23172565  932 NSIYDFIVDVhERCNDYRNGPIVIVDRYGGAQACTFCAISSLAIEMEYCSTANVYQYAKLYHNKR 996
Cdd:cd14621  205 IGMLKFLKKV-KNCNPQYAGAIVVHCSAGVGRTGTFIVIDAMLDMMHAERKVDVYGFVSRIRAQR 268
R-PTPc-E-1 cd14620
catalytic domain of receptor-type tyrosine-protein phosphatase E, repeat 1; Receptor-type ...
797-1013 4.16e-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: 4.16e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23172565  797 IFPIEGSRVHLTPKPGEDGSDYINASWLHGFRRLRDFIVTQHPMAHTIKDFWQMVWDHNAQTVVLLSSL---DDINFAQF 873
Cdd:cd14620    4 ILPYDHSRVILSQLDGIPCSDYINASYIDGYKEKNKFIAAQGPKQETVNDFWRMVWEQKSATIVMLTNLkerKEEKCYQY 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23172565  874 WPDEATPIESDhYRVKFLNKTNKSDYVSRDFVIQSIQDDYELT---VKMLHCPSWPEMSNPNS---IYDFIVDVhERCND 947
Cdd:cd14620   84 WPDQGCWTYGN-IRVAVEDCVVLVDYTIRKFCIQPQLPDGCKAprlVTQLHFTSWPDFGVPFTpigMLKFLKKV-KSVNP 161
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 23172565  948 YRNGPIVIVDRYGGAQACTFCAISSLAIEMEYCSTANVYQYAKLYHNKRPGVWTSSEDIRVIYNIL 1013
Cdd:cd14620  162 VHAGPIVVHCSAGVGRTGTFIVIDAMIDMMHAEQKVDVFEFVSRIRNQRPQMVQTDMQYSFIYQAL 227
R-PTPc-F-1 cd14626
catalytic domain of receptor-type tyrosine-protein phosphatase F, repeat 1; Receptor-type ...
750-996 1.35e-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: 1.35e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23172565  750 MAEQVEELK-NCTPYLEQQYKNI---IQFQPKDIHIasamkQVNSIKNRGA-IFPIEGSRVHLTPKPGEDGSDYINASWL 824
Cdd:cd14626    3 LADNIERLKaNDGLKFSQEYESIdpgQQFTWENSNL-----EVNKPKNRYAnVIAYDHSRVILTSVDGVPGSDYINANYI 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23172565  825 HGFRRLRDFIVTQHPMAHTIKDFWQMVWDHNAQTVVLLSSLDD---INFAQFWPDEATPIESdHYRVKFLNKTNKSDYVS 901
Cdd:cd14626   78 DGYRKQNAYIATQGPLPETLSDFWRMVWEQRTATIVMMTRLEEksrVKCDQYWPIRGTETYG-MIQVTLLDTVELATYSV 156
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23172565  902 RDFVIQSIQDDYELTVKMLHCPSWPEM---SNPNSIYDFIVDVhERCNDYRNGPIVIVDRYGGAQACTFCAISSLAIEME 978
Cdd:cd14626  157 RTFALYKNGSSEKREVRQFQFMAWPDHgvpEYPTPILAFLRRV-KACNPPDAGPMVVHCSAGVGRTGCFIVIDAMLERMK 235
                        250
                 ....*....|....*...
gi 23172565  979 YCSTANVYQYAKLYHNKR 996
Cdd:cd14626  236 HEKTVDIYGHVTCMRSQR 253
R-PTPc-LAR-1 cd14553
catalytic domain of LAR family receptor-type tyrosine-protein phosphatases, repeat 1; The LAR ...
787-996 1.88e-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: 1.88e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23172565  787 QVNSIKNRGA-IFPIEGSRVHLTPKPGEDGSDYINASWLHGFRRLRDFIVTQHPMAHTIKDFWQMVWDHNAQTVVLLSSL 865
Cdd:cd14553    1 EVNKPKNRYAnVIAYDHSRVILQPIEGVPGSDYINANYCDGYRKQNAYIATQGPLPETFGDFWRMVWEQRSATIVMMTKL 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23172565  866 DD---INFAQFWPDEATPIESDhYRVKFLNKTNKSDYVSRDFVIQSIQDDYELTVKMLHCPSWPEM---SNPNSIYDFIV 939
Cdd:cd14553   81 EErsrVKCDQYWPTRGTETYGL-IQVTLLDTVELATYTVRTFALHKNGSSEKREVRQFQFTAWPDHgvpEHPTPFLAFLR 159
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 23172565  940 DVhERCNDYRNGPIVIVDRYGGAQACTFCAISSLAIEMEYCSTANVYQYAKLYHNKR 996
Cdd:cd14553  160 RV-KACNPPDAGPIVVHCSAGVGRTGCFIVIDSMLERIKHEKTVDIYGHVTCLRAQR 215
R-PTPc-H cd14619
catalytic domain of receptor-type tyrosine-protein phosphatase H; Receptor-type ...
797-1016 2.97e-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: 108.44  E-value: 2.97e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23172565  797 IFPIEGSRVHLTPKPGEDGSDYINASWLHGFRRLRDFIVTQHPMAHTIKDFWQMVWDHNAQTVVLLSSLDD---INFAQF 873
Cdd:cd14619    6 VLPYDWSRVPLKPIHEEPGSDYINANYMPGYWSSQEFIATQGPLPQTVGDFWRMIWEQQSSTIVMLTNCMEagrVKCEHY 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23172565  874 WPDEATPIESDHYRVKFLNKTNKSDYVSRDFVIQSIQDDYELTVKMLHCPSWPEM---SNPNSIYDFIVDVHERCNDYRN 950
Cdd:cd14619   86 WPLDYTPCTYGHLRVTVVSEEVMENWTVREFLLKQVEEQKTLSVRHFHFTAWPDHgvpSSTDTLLAFRRLLRQWLDQTMS 165
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 23172565  951 -GPIVIVDRYGGAQACTFCAISSLAIEMEYCSTANVYQYAKLYHNKRP-GVWTSSEDIRVIYNILSFL 1016
Cdd:cd14619  166 gGPTVVHCSAGVGRTGTLIALDVLLQQLQSEGLLGPFSFVQKMRENRPlMVQTESQYVFLHQCILDFL 233
R-PTPc-S-1 cd14625
catalytic domain of receptor-type tyrosine-protein phosphatase S, repeat 1; Receptor-type ...
750-1013 6.65e-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: 6.65e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23172565  750 MAEQVEELK-NCTPYLEQQYKNI---IQFQPKDIHIasamkQVNSIKNRGA-IFPIEGSRVHLTPKPGEDGSDYINASWL 824
Cdd:cd14625    9 LAEHTERLKaNDNLKLSQEYESIdpgQQFTWEHSNL-----EVNKPKNRYAnVIAYDHSRVILQPIEGIMGSDYINANYI 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23172565  825 HGFRRLRDFIVTQHPMAHTIKDFWQMVWDHNAQTVVLLSSLDD---INFAQFWPDEATpiesDHY---RVKFLNKTNKSD 898
Cdd:cd14625   84 DGYRKQNAYIATQGPLPETFGDFWRMVWEQRSATVVMMTKLEEksrIKCDQYWPSRGT----ETYgmiQVTLLDTIELAT 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23172565  899 YVSRDFVIQSIQDDYELTVKMLHCPSWPEMSNPNSIYDFIVDVH--ERCNDYRNGPIVIVDRYGGAQACTFCAISSLAIE 976
Cdd:cd14625  160 FCVRTFSLHKNGSSEKREVRQFQFTAWPDHGVPEYPTPFLAFLRrvKTCNPPDAGPIVVHCSAGVGRTGCFIVIDAMLER 239
                        250       260       270
                 ....*....|....*....|....*....|....*..
gi 23172565  977 MEYCSTANVYQYAKLYHNKRPGVWTSSEDIRVIYNIL 1013
Cdd:cd14625  240 IKHEKTVDIYGHVTLMRSQRNYMVQTEDQYSFIHDAL 276
R-PTP-C-2 cd14558
PTP-like domain of receptor-type tyrosine-protein phosphatase C, repeat 2; Receptor-type ...
818-1010 7.90e-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: 7.90e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23172565  818 YINASWLHGFRRLRDFIVTQHPMAHTIKDFWQMVWDHNAQTVVLLSSL---DDINFAQFWPDEATPIESDHYRVKflNKT 894
Cdd:cd14558    1 YINASFIDGYWGPKSLIATQGPLPDTIADFWQMIFQKKVKVIVMLTELkegDQEQCAQYWGDEKKTYGDIEVELK--DTE 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23172565  895 NKSDYVSRDFVIQSIQDDYELTVKMLHCPSW-----PEmsNPNSIYDFIVDVHERCNDY-----RNGPIVIVDRYGGAQA 964
Cdd:cd14558   79 KSPTYTVRVFEITHLKRKDSRTVYQYQYHKWkgeelPE--KPKDLVDMIKSIKQKLPYKnskhgRSVPIVVHCSDGSSRT 156
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*...
gi 23172565  965 CTFCAISSL--AIEMEycSTANVYQYAKLYHNKRPGVWTSSEDIRVIY 1010
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 ...
533-734 1.90e-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: 1.90e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23172565  533 YINANFIDGYQKGHAFIGTQGPLPDTFDCFWRMIWEQRVAIIVMITNLVERGrrKCDMYWPKDG----VETYGVIQV--- 605
Cdd:cd14550    1 YINASYLQGYRRSNEFIITQHPLEHTIKDFWQMIWDHNSQTIVMLTDNELNE--DEPIYWPTKEkpleCETFKVTLSged 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23172565  606 -KLIEEEVMSTYTVRTLQikhlklkkKKQCNTEKLVYQYHYTNWPDHGTPDHplPVLNFVKKSSAANPAEAGPIVVHCSA 684
Cdd:cd14550   79 hSCLSNEIRLIVRDFILE--------STQDDYVLEVRQFQCPSWPNPCSPIH--TVFELINTVQEWAQQRDGPIVVHDRY 148
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|
gi 23172565  685 GVGRTGTYIVLDAMLKQIQQKNIVNVFGFLRHIRAQRNFLVQTEEQYIFL 734
Cdd:cd14550  149 GGVQAATFCALTTLHQQLEHESSVDVYQVAKLYHLMRPGVFTSKEDYQFL 198
R-PTPc-J cd14615
catalytic domain of receptor-type tyrosine-protein phosphatase J; Receptor-type ...
797-986 2.10e-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: 2.10e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23172565  797 IFPIEGSRVHLTpKPGEDGSDYINASWLHGFRRLRDFIVTQHPMAHTIKDFWQMVWDHNAQTVVLLS---SLDDINFAQF 873
Cdd:cd14615    6 VLPYDISRVKLS-VQSHSTDDYINANYMPGYNSKKEFIAAQGPLPNTVKDFWRMVWEKNVYAIVMLTkcvEQGRTKCEEY 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23172565  874 WPDEAtPIESDHYRVKFLNKTNKSDYVSRDFVIQSIQDDYELTVKMLHCPSWPEMSNPNS---IYDFIVDVHERCNDY-R 949
Cdd:cd14615   85 WPSKQ-KKDYGDITVTMTSEIVLPEWTIRDFTVKNAQTNESRTVRHFHFTSWPDHGVPETtdlLINFRHLVREYMKQNpP 163
                        170       180       190
                 ....*....|....*....|....*....|....*..
gi 23172565  950 NGPIVIVDRYGGAQACTFCAISSLAIEMEYCSTANVY 986
Cdd:cd14615  164 NSPILVHCSAGVGRTGTFIAIDRLIYQIENENVVDVY 200
R-PTPc-M-2 cd14635
PTP domain of receptor-type tyrosine-protein phosphatase M, repeat 2; Receptor-type ...
533-740 2.69e-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: 2.69e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23172565  533 YINANFIDGYQKGHAFIGTQGPLPDTFDCFWRMIWEQRVAIIVMITNLveRGRRKCDMYWPKDGVETYGVIQVKLIEEEV 612
Cdd:cd14635    1 YINAALMDSYKQPSAFIVTQHPLPNTVKDFWRLVLDYHCTSIVMLNDV--DPAQLCPQYWPENGVHRHGPIQVEFVSADL 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23172565  613 MSTYTVRTLQIKHLKLKKkkqcNTEKLVYQYHYTNWPDHgtPDHPLPVLNFVK------KSSAANPAEAGPIVVHCSAGV 686
Cdd:cd14635   79 EEDIISRIFRIYNAARPQ----DGYRMVQQFQFLGWPMY--RDTPVSKRSFLKlirqvdKWQEEYNGGEGRTVVHCLNGG 152
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....
gi 23172565  687 GRTGTYIVLDAMLKQIQQKNIVNVFGFLRHIRAQRNFLVQTEEQYIFLHDALVE 740
Cdd:cd14635  153 GRSGTFCAISIVCEMLRHQRAVDVFHAVKTLRNNKPNMVDLLDQYKFCYEVALE 206
R-PTPc-U-2 cd14637
PTP domain of receptor-type tyrosine-protein phosphatase U, repeat 2; Receptor-type ...
533-740 6.73e-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: 6.73e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23172565  533 YINANFIDGYQKGHAFIGTQGPLPDTFDCFWRMIWEQRVAIIVMITNLVERGRR-KCDMYWPKDGVETYGVIQVKLIEEE 611
Cdd:cd14637    1 YINAALTDSYTRSAAFIVTLHPLQNTTTDFWRLVYDYGCTSVVMLNQLNQSNSAwPCLQYWPEPGLQQYGPMEVEFVSGS 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23172565  612 VMSTYTVRTLQIKHLKLKKKKQCntekLVYQYHYTNW-PDHGTPDHP---LPVLNFVKKSSAANpaEAGPIVVHCSAGVG 687
Cdd:cd14637   81 ADEDIVTRLFRVQNITRLQEGHL----MVRHFQFLRWsAYRDTPDSKkafLHLLASVEKWQRES--GEGRTVVHCLNGGG 154
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|...
gi 23172565  688 RTGTYIVLDAMLKQIQQKNIVNVFGFLRHIRAQRNFLVQTEEQYIFLHDALVE 740
Cdd:cd14637  155 RSGTYCASAMILEMIRCHNIVDVFYAVKTLRNYKPNMVETLEQYRFCYEIALE 207
PTPc-N9 cd14543
catalytic domain of tyrosine-protein phosphatase non-receptor type 9; Tyrosine-protein ...
783-996 7.82e-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: 7.82e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23172565  783 SAMKQVNSIKNR-GAIFPIEGSRVHLTPKPGEDGSDYINASWLHGFRRLRDFIVTQHPMAHTIKDFWQMVWDHNAQTVVL 861
Cdd:cd14543   23 CSLAPANQEKNRyGDVLCLDQSRVKLPKRNGDERTDYINANFMDGYKQKNAYIATQGPLPKTYSDFWRMVWEQKVLVIVM 102
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23172565  862 LSSLDD---INFAQFWP-DEATPIESDHYRVKFLNKTNKSDYVSRDFVIQSIQDDYELTVKMLHCPSWPEMSNPNS---I 934
Cdd:cd14543  103 TTRVVErgrVKCGQYWPlEEGSSLRYGDLTVTNLSVENKEHYKKTTLEIHNTETDESRQVTHFQFTSWPDFGVPSSaaaL 182
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 23172565  935 YDFIVDVHERCNDYRNG------------PIVIVDRYGGAQACTFCAISSLAIEMEYCSTANVYQYAKLYHNKR 996
Cdd:cd14543  183 LDFLGEVRQQQALAVKAmgdrwkghppgpPIVVHCSAGIGRTGTFCTLDICLSQLEDVGTLNVMQTVRRMRTQR 256
R-PTP-N cd14609
PTP-like domain of receptor-type tyrosine-protein phosphatase N; Receptor-type ...
749-999 3.56e-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: 3.56e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23172565  749 LMAEQVEELKNcTPYLEQQYKNIIQFQPKDIHIASAMKQVNSIKNRGAIF-PIEGSRVHLTPKPGEDGSDYINASWL--H 825
Cdd:cd14609    3 ILAYMEDHLRN-RDRLAKEWQALCAYQAEPNTCSTAQGEANVKKNRNPDFvPYDHARIKLKAESNPSRSDYINASPIieH 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23172565  826 GfRRLRDFIVTQHPMAHTIKDFWQMVWDHNAQTVVLLSSLDDINFAQ---FWPDEATPIesdhYRVKFLNKTNK----SD 898
Cdd:cd14609   82 D-PRMPAYIATQGPLSHTIADFWQMVWENGCTVIVMLTPLVEDGVKQcdrYWPDEGSSL----YHIYEVNLVSEhiwcED 156
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23172565  899 YVSRDFVIQSIQDDYELTVKMLHCPSWPEMSNPNS---IYDFIVDVHeRCNDYRNGPIVIVDRYGGAQACTFCAISSLAI 975
Cdd:cd14609  157 FLVRSFYLKNVQTQETRTLTQFHFLSWPAEGIPSStrpLLDFRRKVN-KCYRGRSCPIIVHCSDGAGRTGTYILIDMVLN 235
                        250       260
                 ....*....|....*....|....*.
gi 23172565  976 EMEYcSTANVYQYAKLYH--NKRPGV 999
Cdd:cd14609  236 RMAK-GVKEIDIAATLEHvrDQRPGM 260
R-PTP-N2 cd14610
PTP-like domain of receptor-type tyrosine-protein phosphatase N2; Receptor-type ...
755-1004 4.69e-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: 4.69e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23172565  755 EELKNcTPYLEQQYKNIIQFQPKDIHIASAMKQVNSIKNRG-AIFPIEGSRVHLTPKPGEDGSDYINASWL--HGFRRlR 831
Cdd:cd14610   11 DHLKN-KNRLEKEWEALCAYQAEPNATNVAQREENVQKNRSlAVLPYDHSRIILKAENSHSHSDYINASPImdHDPRN-P 88
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23172565  832 DFIVTQHPMAHTIKDFWQMVWDHNAQTVVLLSSLDDINFAQ---FWPDEAtpieSDHYRVKFLNKTNK----SDYVSRDF 904
Cdd:cd14610   89 AYIATQGPLPATVADFWQMVWESGCVVIVMLTPLAENGVKQcyhYWPDEG----SNLYHIYEVNLVSEhiwcEDFLVRSF 164
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23172565  905 VIQSIQDDYELTVKMLHCPSWPEMSNPNS---IYDFIVDVHeRCNDYRNGPIVIVDRYGGAQACTFCAISSLAIEMEYcS 981
Cdd:cd14610  165 YLKNLQTNETRTVTQFHFLSWNDQGVPAStrsLLDFRRKVN-KCYRGRSCPIIVHCSDGAGRSGTYILIDMVLNKMAK-G 242
                        250       260
                 ....*....|....*....|....*
gi 23172565  982 TANVYQYAKLYH--NKRPGVWTSSE 1004
Cdd:cd14610  243 AKEIDIAATLEHlrDQRPGMVQTKE 267
PHA02747 PHA02747
protein tyrosine phosphatase; Provisional
759-1024 7.02e-24

protein tyrosine phosphatase; Provisional


Pssm-ID: 165114 [Multi-domain]  Cd Length: 312  Bit Score: 103.93  E-value: 7.02e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23172565   759 NCTPYLEQQYKNIIqFQPKDIHIASAMKQVNSIKNRGAIFPI-EGSRVHLTPKPGEDgSDYINASWLHGFRRLRDFIVTQ 837
Cdd:PHA02747   22 NCFGIIRDEHHQII-LKPFDGLIANFEKPENQPKNRYWDIPCwDHNRVILDSGGGST-SDYIHANWIDGFEDDKKFIATQ 99
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23172565   838 HPMAHTIKDFWQMVWDHNAQTVVLLSSLDDINFA----QFW-PDEATPIESDHYRVKFLNKTNKSDYVSRDFVIQSIQDD 912
Cdd:PHA02747  100 GPFAETCADFWKAVWQEHCSIIVMLTPTKGTNGEekcyQYWcLNEDGNIDMEDFRIETLKTSVRAKYILTLIEITDKILK 179
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23172565   913 YELTVKMLHCPSWPEMSNPNSIYDFI-----VDVHER-------CNDYRNGPIVIVDRYGGAQACTFCAISSLAIEMEYC 980
Cdd:PHA02747  180 DSRKISHFQCSEWFEDETPSDHPDFIkfikiIDINRKksgklfnPKDALLCPIVVHCSDGVGKTGIFCAVDICLNQLVKR 259
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*...
gi 23172565   981 STANVYQYAKLYHNKRPGVWTSSEDIRVI----YNILSFLPGNLNLLK 1024
Cdd:PHA02747  260 KAICLAKTAEKIREQRHAGIMNFDDYLFIqpgyEVLHYFLSKIKAIDK 307
R-PTPc-M-1 cd14633
catalytic domain of receptor-type tyrosine-protein phosphatase M, repeat 1; Receptor-type ...
750-1013 8.43e-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: 8.43e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23172565  750 MAEQVEELKNCTPY-LEQQYKNIIQFQ--PKDihiaSAMKQVNSIKNR-GAIFPIEGSRVHLTPKPGEDGSDYINASWLH 825
Cdd:cd14633    2 LLQHITQMKCAEGYgFKEEYESFFEGQsaPWD----SAKKDENRMKNRyGNIIAYDHSRVRLQPIEGETSSDYINGNYID 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23172565  826 GFRRLRDFIVTQHPMAHTIKDFWQMVWDHNAQTVVLLSSLDD---INFAQFWPDEaTPIESDhYRVKFLNKTNKSDYVSR 902
Cdd:cd14633   78 GYHRPNHYIATQGPMQETIYDFWRMVWHENTASIIMVTNLVEvgrVKCCKYWPDD-TEIYKD-IKVTLIETELLAEYVIR 155
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23172565  903 DFVIQSIQDDYELTVKMLHCPSWPEMSNP---NSIYDFIVDVHERcNDYRNGPIVIVDRYGGAQACTFCAISSLAIEMEY 979
Cdd:cd14633  156 TFAVEKRGVHEIREIRQFHFTGWPDHGVPyhaTGLLGFVRQVKSK-SPPNAGPLVVHCSAGAGRTGCFIVIDIMLDMAER 234
                        250       260       270
                 ....*....|....*....|....*....|....
gi 23172565  980 CSTANVYQYAKLYHNKRPGVWTSSEDIRVIYNIL 1013
Cdd:cd14633  235 EGVVDIYNCVRELRSRRVNMVQTEEQYVFIHDAI 268
PTPc-N1_2 cd14545
catalytic domain of tyrosine-protein phosphatase non-receptor type 1 and type 2; ...
803-978 1.74e-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: 1.74e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23172565  803 SRVHLTpkpgEDGSDYINASWLHGFRRLRDFIVTQHPMAHTIKDFWQMVWDHNAQTVVLLSSL---DDINFAQFWP---D 876
Cdd:cd14545   15 SRVKLK----QGDNDYINASLVEVEEAKRSYILTQGPLPNTSGHFWQMVWEQNSKAVIMLNKLmekGQIKCAQYWPqgeG 90
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23172565  877 EATPIESDHYRVKFLNKTNKSDYVSRDFVIQSIQDDYELTVKMLHCPSWPEMS---NPNSIYDFIVDVHER-CNDYRNGP 952
Cdd:cd14545   91 NAMIFEDTGLKVTLLSEEDKSYYTVRTLELENLKTQETREVLHFHYTTWPDFGvpeSPAAFLNFLQKVRESgSLSSDVGP 170
                        170       180
                 ....*....|....*....|....*.
gi 23172565  953 IVIVDRYGGAQACTFCAISSLAIEME 978
Cdd:cd14545  171 PVVHCSAGIGRSGTFCLVDTCLVLIE 196
R-PTPc-T-1 cd14630
catalytic domain of receptor-type tyrosine-protein phosphatase T, repeat 1; Receptor-type ...
789-973 2.36e-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: 2.36e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23172565  789 NSIKNR-GAIFPIEGSRVHLTPKPGEDGSDYINASWLHGFRRLRDFIVTQHPMAHTIKDFWQMVWDHNAQTVVLLSSLDD 867
Cdd:cd14630    3 NRNKNRyGNIISYDHSRVRLQLLDGDPHSDYINANYIDGYHRPRHYIATQGPMQETVKDFWRMIWQENSASVVMVTNLVE 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23172565  868 ---INFAQFWPDEaTPIESDhYRVKFLNKTNKSDYVSRDFVIQSIQDDYELTVKMLHCPSWPEMSNP---NSIYDFIVDV 941
Cdd:cd14630   83 vgrVKCVRYWPDD-TEVYGD-IKVTLIETEPLAEYVIRTFTVQKKGYHEIREIRQFHFTSWPDHGVPcyaTGLLGFVRQV 160
                        170       180       190
                 ....*....|....*....|....*....|..
gi 23172565  942 hERCNDYRNGPIVIVDRYGGAQACTFCAISSL 973
Cdd:cd14630  161 -KFLNPPDAGPIVVHCSAGAGRTGCFIAIDIM 191
R-PTP-Z-2 cd17669
catalytic domain of receptor-type tyrosine-protein phosphatase Z, repeat 2; Receptor-type ...
533-739 3.23e-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: 3.23e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23172565  533 YINANFIDGYQKGHAFIGTQGPLPDTFDCFWRMIWEQRVAIIVMITNLVERGRRKCdMYWP-KDGVETYGVIQVKLIEEE 611
Cdd:cd17669    1 YINASYIMGYYQSNEFIITQHPLLHTIKDFWRMIWDHNAQLIVMLPDGQNMAEDEF-VYWPnKDEPINCETFKVTLIAEE 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23172565  612 VMSTYTVRTLqIKHLKLKKKKQCNTEKLVYQYHYTNWPDhgtPDHPLP----VLNFVKKSSAanpAEAGPIVVHCSAGVG 687
Cdd:cd17669   80 HKCLSNEEKL-IIQDFILEATQDDYVLEVRHFQCPKWPN---PDSPISktfeLISIIKEEAA---NRDGPMIVHDEHGGV 152
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|..
gi 23172565  688 RTGTYIVLDAMLKQIQQKNIVNVFGFLRHIRAQRNFLVQTEEQYIFLHDALV 739
Cdd:cd17669  153 TAGTFCALTTLMHQLEKENSVDVYQVAKMINLMRPGVFTDIEQYQFLYKAIL 204
R5-PTPc-1 cd14549
catalytic domain of R5 subfamily receptor-type tyrosine-protein phosphatases, repeat 1; The R5 ...
818-996 4.35e-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: 4.35e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23172565  818 YINASWLHGFRRLRDFIVTQHPMAHTIKDFWQMVWDHNAQTVVLLSSLDD---INFAQFWPDEATPiESDHYRVKFLNKT 894
Cdd:cd14549    1 YINANYVDGYNKARAYIATQGPLPSTFDDFWRMVWEQNSAIIVMITNLVErgrRKCDQYWPKEGTE-TYGNIQVTLLSTE 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23172565  895 NKSDYVSRDFVIQSIQ------DDYELTVKMLHCPSWPEMSNPNS---IYDFIVDVhERCNDYRNGPIVI-----VDRYG 960
Cdd:cd14549   80 VLATYTVRTFSLKNLKlkkvkgRSSERVVYQYHYTQWPDHGVPDYtlpVLSFVRKS-SAANPPGAGPIVVhcsagVGRTG 158
                        170       180       190
                 ....*....|....*....|....*....|....*.
gi 23172565  961 gaqacTFCAISSLAIEMEYCSTANVYQYAKLYHNKR 996
Cdd:cd14549  159 -----TYIVIDSMLQQIQDKGTVNVFGFLKHIRTQR 189
R-PTPc-T-2 cd14634
PTP domain of receptor-type tyrosine-protein phosphatase T, repeat 2; Receptor-type ...
818-1012 4.75e-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: 4.75e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23172565  818 YINASWLHGFRRLRDFIVTQHPMAHTIKDFWQMVWDHNAQTVVLLSSLDDINFA-QFWPDEAT----PIEsdhyrVKFLN 892
Cdd:cd14634    1 YINAALMDSHKQPAAFIVTQHPLPNTVADFWRLVFDYNCSSVVMLNEMDAAQLCmQYWPEKTSccygPIQ-----VEFVS 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23172565  893 KTNKSDYVSRDFVIQSI---QDDYELtVKMLHCPSWPEMSNPNSIYDFIVDVHERCN------DYRNGPIVIVDRYGGAQ 963
Cdd:cd14634   76 ADIDEDIISRIFRICNMarpQDGYRI-VQHLQYIGWPAYRDTPPSKRSILKVVRRLEkwqeqyDGREGRTVVHCLNGGGR 154
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*....
gi 23172565  964 ACTFCAISSLAIEMEYCSTANVYQYAKLYHNKRPGVWTSSEDIRVIYNI 1012
Cdd:cd14634  155 SGTFCAICSVCEMIQQQNIIDVFHTVKTLRNNKSNMVETLEQYKFVYEV 203
R-PTPc-D-1 cd14624
catalytic domain of receptor-type tyrosine-protein phosphatase D, repeat 1; Receptor-type ...
750-996 7.13e-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: 7.13e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23172565  750 MAEQVEELK-NCTPYLEQQYKNI---IQFQPKDIHIasamkQVNSIKNRGA-IFPIEGSRVHLTPKPGEDGSDYINASWL 824
Cdd:cd14624    9 LADHIERLKaNDNLKFSQEYESIdpgQQFTWEHSNL-----EVNKPKNRYAnVIAYDHSRVLLSAIEGIPGSDYINANYI 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23172565  825 HGFRRLRDFIVTQHPMAHTIKDFWQMVWDHNAQTVVLLSSLDD---INFAQFWPDEATPIESdHYRVKFLNKTNKSDYVS 901
Cdd:cd14624   84 DGYRKQNAYIATQGALPETFGDFWRMIWEQRSATVVMMTKLEErsrVKCDQYWPSRGTETYG-LIQVTLLDTVELATYCV 162
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23172565  902 RDFVIQSIQDDYELTVKMLHCPSWPEMSNPNSIYDFIVDVH--ERCNDYRNGPIVIVDRYGGAQACTFCAISSLAIEMEY 979
Cdd:cd14624  163 RTFALYKNGSSEKREVRQFQFTAWPDHGVPEHPTPFLAFLRrvKTCNPPDAGPMVVHCSAGVGRTGCFIVIDAMLERIKH 242
                        250
                 ....*....|....*..
gi 23172565  980 CSTANVYQYAKLYHNKR 996
Cdd:cd14624  243 EKTVDIYGHVTLMRAQR 259
R-PTPc-A-E-1 cd14551
catalytic domain of receptor-type tyrosine-protein phosphatase A and E, repeat 1; ...
818-997 8.16e-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: 8.16e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23172565  818 YINASWLHGFRRLRDFIVTQHPMAHTIKDFWQMVWDHNAQTVVLLSSLDD---INFAQFWPDEATPIESDhYRVKFLNKT 894
Cdd:cd14551    1 YINASYIDGYQEKNKFIAAQGPKDETVNDFWRMIWEQGSATIVMVTNLKErkeKKCSQYWPDQGCWTYGN-LRVRVEDTV 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23172565  895 NKSDYVSRDFVIQSIQDDY----ELTVKMLHCPSWPEMSNPNS---IYDFIVDVhERCNDYRNGPIVIVDRYGGAQACTF 967
Cdd:cd14551   80 VLVDYTTRKFCIQKVNRGIgekrVRLVTQFHFTSWPDFGVPFTpigMLKFLKKV-KSANPPRAGPIVVHCSAGVGRTGTF 158
                        170       180       190
                 ....*....|....*....|....*....|
gi 23172565  968 CAISSLAIEMEYCSTANVYQYAKLYHNKRP 997
Cdd:cd14551  159 IVIDAMLDMMHAEGKVDVFGFVSRIRQQRS 188
PTPc-N11_6 cd14544
catalytic domain of tyrosine-protein phosphatase non-receptor type 11 and type 6; ...
789-955 1.36e-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: 98.30  E-value: 1.36e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23172565  789 NSIKNR-GAIFPIEGSRVHLTPK-PGEDGSDYINASWLH-------GFRRLRDFIVTQHPMAHTIKDFWQMVWDHNAQTV 859
Cdd:cd14544    1 NKGKNRyKNILPFDHTRVILKDRdPNVPGSDYINANYIRnenegptTDENAKTYIATQGCLENTVSDFWSMVWQENSRVI 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23172565  860 VLLSSLDDI---NFAQFWPDEATPIESDHYRVKFLNKTNKSDYVSRDFVIQSI-QDDYELTVKMLHCPSWPEM---SNPN 932
Cdd:cd14544   81 VMTTKEVERgknKCVRYWPDEGMQKQYGPYRVQNVSEHDTTDYTLRELQVSKLdQGDPIREIWHYQYLSWPDHgvpSDPG 160
                        170       180
                 ....*....|....*....|....*
gi 23172565  933 SIYDFIVDVHERcNDYRN--GPIVI 955
Cdd:cd14544  161 GVLNFLEDVNQR-QESLPhaGPIVV 184
R-PTPc-O cd14614
catalytic domain of receptor-type tyrosine-protein phosphatase O; Receptor-type ...
778-973 1.56e-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: 1.56e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23172565  778 DIHIASAMKQVNSIKNRGA-IFPIEGSRVHLTPKPGEDGSDYINASWLHGFRRLRDFIVTQHPMAHTIKDFWQMVWDHNA 856
Cdd:cd14614    1 DIPHFAADLPVNRCKNRYTnILPYDFSRVKLVSMHEEEGSDYINANYIPGYNSPQEYIATQGPLPETRNDFWKMVLQQKS 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23172565  857 QTVVLLSSLDD---INFAQFWPDEATPIESDHYRVKFLNKTNKSDYVSRDFVIqSIQDDYElTVKMLHCPSWPEMSNPN- 932
Cdd:cd14614   81 QIIVMLTQCNEkrrVKCDHYWPFTEEPVAYGDITVEMLSEEEQPDWAIREFRV-SYADEVQ-DVMHFNYTAWPDHGVPTa 158
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*
gi 23172565  933 ----SIYDFIVDVHERCNDyRNGPIVIVDRYGGAQACTFCAISSL 973
Cdd:cd14614  159 naaeSILQFVQMVRQQAVK-SKGPMIIHCSAGVGRTGTFIALDRL 202
PTPc-KIM cd14547
catalytic domain of the kinase interaction motif (KIM) family of protein-tyrosine phosphatases; ...
797-971 2.08e-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: 2.08e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23172565  797 IFPIEGSRVHLTPKPGEDGSDYINASWLHGFRRLRD-FIVTQHPMAHTIKDFWQMVWDHNAQTVVLLSSLDDIN--FAQF 873
Cdd:cd14547    6 ILPNEHSRVCLPSVDDDPLSSYINANYIRGYDGEEKaYIATQGPLPNTVADFWRMVWQEKTPIIVMITNLTEAKekCAQY 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23172565  874 WPDEaTPIESDHYRVKFLNKTNKSDYVSRDFVIQSIQDDYEltVKMLHCPSWPEMSNPNS---IYDFIVDVHE-RCNDYR 949
Cdd:cd14547   86 WPEE-ENETYGDFEVTVQSVKETDGYTVRKLTLKYGGEKRY--LKHYWYTSWPDHKTPEAaqpLLSLVQEVEEaRQTEPH 162
                        170       180
                 ....*....|....*....|...
gi 23172565  950 NGPIVIVDRYG-GAQACtFCAIS 971
Cdd:cd14547  163 RGPIVVHCSAGiGRTGC-FIATS 184
R-PTPc-Q cd14616
catalytic domain of receptor-type tyrosine-protein phosphatase Q; Receptor-type ...
797-973 5.06e-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: 5.06e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23172565  797 IFPIEGSRVHLTPKPGEDGSDYINASWLHGFRRLRDFIVTQHPMAHTIKDFWQMVWDHNAQTVVLLSSLDD---INFAQF 873
Cdd:cd14616    6 IKPYNNNRVKLIADAGVPGSDYINASYISGYLCPNEFIATQGPLPGTVGDFWRMVWETRAKTIVMLTQCFEkgrIRCHQY 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23172565  874 WPDEATPIE--SDHYRVKFLNKTnKSDYVSRDFVIQSiQDDYeLTVKMLHCPSWPEMSNPNSIYDFIVDVH----ERCND 947
Cdd:cd14616   86 WPEDNKPVTvfGDIVITKLMEDV-QIDWTIRDLKIER-HGDY-MMVRQCNFTSWPEHGVPESSAPLIHFVKlvraSRAHD 162
                        170       180
                 ....*....|....*....|....*.
gi 23172565  948 yrNGPIVIVDRYGGAQACTFCAISSL 973
Cdd:cd14616  163 --NTPMIVHCSAGVGRTGVFIALDHL 186
R-PTPc-K-2 cd14636
PTP domain of receptor-type tyrosine-protein phosphatase K, repeat 2; Receptor-type ...
818-1012 1.13e-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: 1.13e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23172565  818 YINASWLHGFRRLRDFIVTQHPMAHTIKDFWQMVWDHNAQTVVLLSSLDDIN-FAQFWPDEATpIESDHYRVKFLNKTNK 896
Cdd:cd14636    1 YINAALMDSYRQPAAFIVTQHPLPNTVKDFWRLVYDYGCTSIVMLNEVDLAQgCPQYWPEEGM-LRYGPIQVECMSCSMD 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23172565  897 SDYVSRDFVIQSI---QDDYeLTVKMLHCPSWPEM----SNPNSIYDFIVDV---HERCnDYRNGPIVIVDRYGGAQACT 966
Cdd:cd14636   80 CDVISRIFRICNLtrpQEGY-LMVQQFQYLGWASHrevpGSKRSFLKLILQVekwQEEC-DEGEGRTIIHCLNGGGRSGM 157
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*.
gi 23172565  967 FCAISSLAIEMEYCSTANVYQYAKLYHNKRPGVWTSSEDIRVIYNI 1012
Cdd:cd14636  158 FCAISIVCEMIKRQNVVDVFHAVKTLRNSKPNMVETPEQYRFCYDV 203
PTP_fungal cd18533
fungal protein tyrosine phosphatases; This subfamily contains Saccharomyces cerevisiae ...
818-1016 1.63e-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: 1.63e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23172565  818 YINASWLH-GFRRLRDFIVTQHPMAHTIKDFWQMVWDHNAQTVVLLSSLDDINF---AQFWPDEATPIESDHYRVKFLNK 893
Cdd:cd18533    1 YINASYITlPGTSSKRYIATQGPLPATIGDFWKMIWQNNVGVIVMLTPLVENGRekcDQYWPSGEYEGEYGDLTVELVSE 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23172565  894 T--NKSDYVSRDFVIQSiQDDYELTVKMLHCPSWPEMSNPNSIYDF--IVDVHERCND--YRNGPIVI-----VDRYGga 962
Cdd:cd18533   81 EenDDGGFIVREFELSK-EDGKVKKVYHIQYKSWPDFGVPDSPEDLltLIKLKRELNDsaSLDPPIIVhcsagVGRTG-- 157
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....
gi 23172565  963 qacTFCAISSLAIEMEycstanvyqyaklyhNKRPGVWTSSEDIRVIYNILSFL 1016
Cdd:cd18533  158 ---TFIALDSLLDELK---------------RGLSDSQDLEDSEDPVYEIVNQL 193
R-PTPc-U-2 cd14637
PTP domain of receptor-type tyrosine-protein phosphatase U, repeat 2; Receptor-type ...
818-1012 2.03e-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: 2.03e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23172565  818 YINASWLHGFRRLRDFIVTQHPMAHTIKDFWQMVWDHNAQTVVLLSSLDDINFA----QFWPDEAT----PIEsdhyrVK 889
Cdd:cd14637    1 YINAALTDSYTRSAAFIVTLHPLQNTTTDFWRLVYDYGCTSVVMLNQLNQSNSAwpclQYWPEPGLqqygPME-----VE 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23172565  890 FLNKTNKSDYVSRDFVIQSIQ--DDYELTVKMLHCPSW-PEMSNPNSIYDF---IVDVHERCNDYRNGPIVIVDRYGGAQ 963
Cdd:cd14637   76 FVSGSADEDIVTRLFRVQNITrlQEGHLMVRHFQFLRWsAYRDTPDSKKAFlhlLASVEKWQRESGEGRTVVHCLNGGGR 155
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|
gi 23172565  964 ACTFCAiSSLAIEMEYC-STANVYQYAKLYHNKRPGVWTSSEDIRVIYNI 1012
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 ...
818-970 2.65e-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: 2.65e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23172565  818 YINASWLHGFR-RLRDFIVTQHPMAHTIKDFWQMVWDHNAQTVVLLSSLDDINFAQ---FWPDEATPIESDhYRVKFLNK 893
Cdd:cd14546    1 YINASTIYDHDpRNPAYIATQGPLPHTIADFWQMIWEQGCVVIVMLTRLQENGVKQcarYWPEEGSEVYHI-YEVHLVSE 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23172565  894 TNKS-DYVSRDFVIQSIQDDYELTVKMLHCPSWPEMS---NPNSIYDFIVDVHeRCNDYRNGPIVIVDRYGGAQACTFCA 969
Cdd:cd14546   80 HIWCdDYLVRSFYLKNLQTSETRTVTQFHFLSWPDEGipaSAKPLLEFRRKVN-KSYRGRSCPIVVHCSDGAGRTGTYIL 158

                 .
gi 23172565  970 I 970
Cdd:cd14546  159 I 159
PTPc-N11 cd14605
catalytic domain of tyrosine-protein phosphatase non-receptor type 11; Tyrosine-protein ...
789-973 2.72e-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: 2.72e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23172565  789 NSIKNR-GAIFPIEGSRVHLTP-KPGEDGSDYINASWL--------HGFRRLRDFIVTQHPMAHTIKDFWQMVWDHNAQT 858
Cdd:cd14605    2 NKNKNRyKNILPFDHTRVVLHDgDPNEPVSDYINANIImpefetkcNNSKPKKSYIATQGCLQNTVNDFWRMVFQENSRV 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23172565  859 VVLLS---SLDDINFAQFWPDEATPIESDHYRVKFLNKTNKSDYVSRDFVIQSI-QDDYELTVKMLHCPSWPEM---SNP 931
Cdd:cd14605   82 IVMTTkevERGKSKCVKYWPDEYALKEYGVMRVRNVKESAAHDYILRELKLSKVgQGNTERTVWQYHFRTWPDHgvpSDP 161
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|...
gi 23172565  932 NSIYDFIVDVHERCNDYRN-GPIVIVDRYGGAQACTFCAISSL 973
Cdd:cd14605  162 GGVLDFLEEVHHKQESIMDaGPVVVHCSAGIGRTGTFIVIDIL 204
PTPc-N1 cd14608
catalytic domain of tyrosine-protein phosphatase non-receptor type 1; Tyrosine-protein ...
772-1018 3.09e-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: 3.09e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23172565  772 IQFQPKDIHIASAMKQVNSIKNR-GAIFPIEGSRVHLTpkpgEDGSDYINASWLHGFRRLRDFIVTQHPMAHTIKDFWQM 850
Cdd:cd14608    8 IRHEASDFPCRVAKLPKNKNRNRyRDVSPFDHSRIKLH----QEDNDYINASLIKMEEAQRSYILTQGPLPNTCGHFWEM 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23172565  851 VWDHNAQTVVLLSSL---DDINFAQFWP---DEATPIESDHYRVKFLNKTNKSDYVSRDFVIQSIQDDYELTVKMLHCPS 924
Cdd:cd14608   84 VWEQKSRGVVMLNRVmekGSLKCAQYWPqkeEKEMIFEDTNLKLTLISEDIKSYYTVRQLELENLTTQETREILHFHYTT 163
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23172565  925 WPEM---SNPNSIYDFIVDVHER-CNDYRNGPIVIVDRYGGAQACTFCAISSLAIEMEY---CSTANVYQYAKLYHNKRP 997
Cdd:cd14608  164 WPDFgvpESPASFLNFLFKVRESgSLSPEHGPVVVHCSAGIGRSGTFCLADTCLLLMDKrkdPSSVDIKKVLLEMRKFRM 243
                        250       260
                 ....*....|....*....|.
gi 23172565  998 GVWTSSEDIRVIYniLSFLPG 1018
Cdd:cd14608  244 GLIQTADQLRFSY--LAVIEG 262
R-PTPc-G-1 cd17667
catalytic domain of receptor-type tyrosine-protein phosphatase G, repeat 1; Receptor-type ...
789-1013 3.67e-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: 92.02  E-value: 3.67e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23172565  789 NSIKNRGA-IFPIEGSRVHLTPKPGEDG--SDYINASWLHGFRRLRDFIVTQHPMAHTIKDFWQMVWDHNAQTVVLLSSL 865
Cdd:cd17667   27 NKHKNRYInILAYDHSRVKLRPLPGKDSkhSDYINANYVDGYNKAKAYIATQGPLKSTFEDFWRMIWEQNTGIIVMITNL 106
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23172565  866 DDI---NFAQFWPDEatpiESDHYR--VKFLNKTN-KSDYVSRDFVIQSIQDDY-----------ELTVKMLHCPSWPEM 928
Cdd:cd17667  107 VEKgrrKCDQYWPTE----NSEEYGniIVTLKSTKiHACYTVRRFSIRNTKVKKgqkgnpkgrqnERTVIQYHYTQWPDM 182
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23172565  929 SNPNSIYDFIVDVhERCNDYRN---GPIVIVDRYGGAQACTFCAISSLAIEMEYCSTANVYQYAKLYHNKRPGVWTSSED 1005
Cdd:cd17667  183 GVPEYALPVLTFV-RRSSAARTpemGPVLVHCSAGVGRTGTYIVIDSMLQQIKDKSTVNVLGFLKHIRTQRNYLVQTEEQ 261

                 ....*...
gi 23172565 1006 IRVIYNIL 1013
Cdd:cd17667  262 YIFIHDAL 269
R-PTPc-M-2 cd14635
PTP domain of receptor-type tyrosine-protein phosphatase M, repeat 2; Receptor-type ...
818-999 6.39e-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: 6.39e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23172565  818 YINASWLHGFRRLRDFIVTQHPMAHTIKDFWQMVWDHNAQTVVLLSSLDDINFA-QFWPDEAT----PIEsdhyrVKFLN 892
Cdd:cd14635    1 YINAALMDSYKQPSAFIVTQHPLPNTVKDFWRLVLDYHCTSIVMLNDVDPAQLCpQYWPENGVhrhgPIQ-----VEFVS 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23172565  893 KTNKSDYVSRDFVIQSI---QDDYELtVKMLHCPSWPEMSN-PNSIYDFI-----VDVHERCNDYRNGPIVIVDRYGGAQ 963
Cdd:cd14635   76 ADLEEDIISRIFRIYNAarpQDGYRM-VQQFQFLGWPMYRDtPVSKRSFLklirqVDKWQEEYNGGEGRTVVHCLNGGGR 154
                        170       180       190
                 ....*....|....*....|....*....|....*.
gi 23172565  964 ACTFCAISSLAIEMEYCSTANVYQYAKLYHNKRPGV 999
Cdd:cd14635  155 SGTFCAISIVCEMLRHQRAVDVFHAVKTLRNNKPNM 190
R-PTP-G-2 cd17670
PTP-like domain of receptor-type tyrosine-protein phosphatase G, repeat 2; Receptor-type ...
533-739 6.65e-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: 6.65e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23172565  533 YINANFIDGYQKGHAFIGTQGPLPDTFDCFWRMIWEQRVAIIVMITNlvERGRRKCD-MYWPKD----GVETYGVIQVK- 606
Cdd:cd17670    1 YINASYIMGYYRSNEFIITQHPLPHTTKDFWRMIWDHNAQIIVMLPD--NQGLAEDEfVYWPSReesmNCEAFTVTLISk 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23172565  607 ----LIEEE--VMSTYTVRTLQIKHLKLKKKKQCnteklvyqyhyTNWPDhgtPDHPLP----VLNFVKKSSAanpAEAG 676
Cdd:cd17670   79 drlcLSNEEqiIIHDFILEATQDDYVLEVRHFQC-----------PKWPN---PDAPISstfeLINVIKEEAL---TRDG 141
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 23172565  677 PIVVHCSAGVGRTGTYIVLDAMLKQIQQKNIVNVFGFLRHIRAQRNFLVQTEEQYIFLHDALV 739
Cdd:cd17670  142 PTIVHDEFGAVSAGTLCALTTLSQQLENENAVDVYQVAKMINLMRPGVFTDIEQYQFLYKAML 204
R-PTPc-B cd14617
catalytic domain of receptor-type tyrosine-protein phosphatase B; Receptor-type ...
797-986 8.26e-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: 89.59  E-value: 8.26e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23172565  797 IFPIEGSRVHLTPKPGEDGSDYINASWLHGFRRLRDFIVTQHPMAHTIKDFWQMVWDHNAQTVVLLSSLDD---INFAQF 873
Cdd:cd14617    6 ILPYDSTRVKLSNVDDDPCSDYINASYIPGNNFRREYIATQGPLPGTKDDFWKMVWEQNVHNIVMVTQCVEkgrVKCDHY 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23172565  874 WPDEATPIESDHYRVKFLNKTNKSDYVSRDFVIQS-IQDDYELTVKMLHCPSWPEMSNPN---SIYDFIVDVHERCNDYR 949
Cdd:cd14617   86 WPADQDSLYYGDLIVQMLSESVLPEWTIREFKICSeEQLDAPRLVRHFHYTVWPDHGVPEttqSLIQFVRTVRDYINRTP 165
                        170       180       190
                 ....*....|....*....|....*....|....*...
gi 23172565  950 N-GPIVIVDRYGGAQACTFCAISSLAIEMEYCSTANVY 986
Cdd:cd14617  166 GsGPTVVHCSAGVGRTGTFIALDRILQQLDSKDSVDIY 203
fn3 pfam00041
Fibronectin type III domain;
172-259 2.01e-19

Fibronectin type III domain;


Pssm-ID: 394996 [Multi-domain]  Cd Length: 85  Bit Score: 84.00  E-value: 2.01e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23172565    172 SKPQNLTILDVSANSITMSWHPPKNQNGAIAGYHVFHIHDNQTGVEivkNSRNSVETLIHFELQNLRPYTDYRVIVKAFT 251
Cdd:pfam00041    1 SAPSNLTVTDVTSTSLTVSWTPPPDGNGPITGYEVEYRPKNSGEPW---NEITVPGTTTSVTLTGLKPGTEYEVRVQAVN 77

                   ....*...
gi 23172565    252 TKNEGEPS 259
Cdd:pfam00041   78 GGGEGPPS 85
PTPc-N12 cd14604
catalytic domain of tyrosine-protein phosphatase non-receptor type 12; Tyrosine-protein ...
786-970 4.46e-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: 4.46e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23172565  786 KQVNSIKNR-GAIFPIEGSRVHLTPKPGEDGSDYINASWLHGFRRLRDFIVTQHPMAHTIKDFWQMVWDHNAQTVVLLS- 863
Cdd:cd14604   54 KEENVKKNRyKDILPFDHSRVKLTLKTSSQDSDYINANFIKGVYGPKAYIATQGPLANTVIDFWRMIWEYNVAIIVMACr 133
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23172565  864 --SLDDINFAQFWPDEA-TPIESDHYRVKFLNKTNKSDYVSRDFVIQSIQDDYELTvkMLHCPSWPEMSNPNSiYDFIVD 940
Cdd:cd14604  134 efEMGRKKCERYWPLYGeEPMTFGPFRISCEAEQARTDYFIRTLLLEFQNETRRLY--QFHYVNWPDHDVPSS-FDSILD 210
                        170       180       190
                 ....*....|....*....|....*....|...
gi 23172565  941 VHERCNDYR---NGPIVIVDRYGGAQACTFCAI 970
Cdd:cd14604  211 MISLMRKYQeheDVPICIHCSAGCGRTGAICAI 243
FN3 cd00063
Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein ...
171-266 5.12e-19

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: 82.93  E-value: 5.12e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23172565  171 PSKPQNLTILDVSANSITMSWHPPKNQNGAIAGYHVFHIHDNQTGVEIVKNSRNSVEtliHFELQNLRPYTDYRVIVKAF 250
Cdd:cd00063    1 PSPPTNLRVTDVTSTSVTLSWTPPEDDGGPITGYVVEYREKGSGDWKEVEVTPGSET---SYTLTGLKPGTEYEFRVRAV 77
                         90
                 ....*....|....*.
gi 23172565  251 TTKNEGEPSDQIAQRT 266
Cdd:cd00063   78 NGGGESPPSESVTVTT 93
R-PTPc-K-1 cd14631
catalytic domain of receptor-type tyrosine-protein phosphatase K, repeat 1; Receptor-type ...
804-1013 5.64e-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: 5.64e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23172565  804 RVHLTPKPGEDGSDYINASWLHGFRRLRDFIVTQHPMAHTIKDFWQMVWDHNAQTVVLLSSLDDINFA---QFWPDEaTP 880
Cdd:cd14631    1 RVILQPVEDDPSSDYINANYIDGYQRPSHYIATQGPVHETVYDFWRMIWQEQSACIVMVTNLVEVGRVkcyKYWPDD-TE 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23172565  881 IESDhYRVKFLNKTNKSDYVSRDFVIQSIQDDYELTVKMLHCPSWPEMSNP---NSIYDFIVDVhERCNDYRNGPIVIVD 957
Cdd:cd14631   80 VYGD-FKVTCVEMEPLAEYVVRTFTLERRGYNEIREVKQFHFTGWPDHGVPyhaTGLLSFIRRV-KLSNPPSAGPIVVHC 157
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 23172565  958 RYGGAQACTFCAISSLAIEMEYCSTANVYQYAKLYHNKRPGVWTSSEDIRVIYNIL 1013
Cdd:cd14631  158 SAGAGRTGCYIVIDIMLDMAEREGVVDIYNCVKALRSRRINMVQTEEQYIFIHDAI 213
PTPc-N2 cd14607
catalytic domain of tyrosine-protein phosphatase non-receptor type 2; Tyrosine-protein ...
772-978 6.09e-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: 6.09e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23172565  772 IQFQPKDIHIASAMKQVNSIKNR-GAIFPIEGSRVHLTpkpgEDGSDYINASWLHGFRRLRDFIVTQHPMAHTIKDFWQM 850
Cdd:cd14607    7 IRNESHDYPHRVAKYPENRNRNRyRDVSPYDHSRVKLQ----NTENDYINASLVVIEEAQRSYILTQGPLPNTCCHFWLM 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23172565  851 VWDHNAQTVVLLSSL---DDINFAQFWP---DEATPIESDHYRVKFLNKTNKSDYVSRDFVIQSIQDDYELTVKMLHCPS 924
Cdd:cd14607   83 VWQQKTKAVVMLNRIvekDSVKCAQYWPtdeEEVLSFKETGFSVKLLSEDVKSYYTVHLLQLENINSGETRTISHFHYTT 162
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 23172565  925 WPEM---SNPNSIYDFIVDVHE-RCNDYRNGPIVIVDRYGGAQACTFCAISSLAIEME 978
Cdd:cd14607  163 WPDFgvpESPASFLNFLFKVREsGSLSPEHGPAVVHCSAGIGRSGTFSLVDTCLVLME 220
PTPc-N18 cd14603
catalytic domain of tyrosine-protein phosphatase non-receptor type 18; Tyrosine-protein ...
751-970 1.22e-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: 1.22e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23172565  751 AEQVEELKNCTPYLEQQYKNIIQfqpkdihiASAMKQvNSIKNR-GAIFPIEGSRVHLTPKPGEDGSDYINASWLHGFRR 829
Cdd:cd14603    1 AGEFSEIRACSAAFKADYVCSTV--------AGGRKE-NVKKNRyKDILPYDQTRVILSLLQEEGHSDYINANFIKGVDG 71
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23172565  830 LRDFIVTQHPMAHTIKDFWQMVWDHNAQTVVLlsSLDDINFAQ-----FWPDEATPIESDHYRVKFLnktnKSDYVSRDF 904
Cdd:cd14603   72 SRAYIATQGPLSHTVLDFWRMIWQYGVKVILM--ACREIEMGKkkcerYWAQEQEPLQTGPFTITLV----KEKRLNEEV 145
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 23172565  905 VIQSIQDDY---ELTVKMLHCPSWPEMSNPNSiYDFIVDVHERCNDYRNG---PIVIVDRYGGAQACTFCAI 970
Cdd:cd14603  146 ILRTLKVTFqkeSRSVSHFQYMAWPDHGIPDS-PDCMLAMIELARRLQGSgpePLCVHCSAGCGRTGVICTV 216
PTPc-N22 cd14602
catalytic domain of tyrosine-protein phosphatase non-receptor type 22; Tyrosine-protein ...
792-1016 1.78e-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: 1.78e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23172565  792 KNR-GAIFPIEGSRVHLTPKPGEDGSDYINASWLHGFRRLRDFIVTQHPMAHTIKDFWQMVWDHNAQTVVLLS---SLDD 867
Cdd:cd14602    1 KNRyKDILPYDHSRVELSLITSDEDSDYINANFIKGVYGPRAYIATQGPLSTTLLDFWRMIWEYSVLIIVMACmefEMGK 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23172565  868 INFAQFWPDEAT-PIESDHYRVKFLNKTNKSDYVSRDFVIQSIQDDYelTVKMLHCPSWPEMSNPNS---IYDFIVDVhe 943
Cdd:cd14602   81 KKCERYWAEPGEmQLEFGPFSVTCEAEKRKSDYIIRTLKVKFNSETR--TIYQFHYKNWPDHDVPSSidpILELIWDV-- 156
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23172565  944 RC-NDYRNGPIVIVDRYGGAQACTFCAISSL-------AIEMEYcstaNVYQYAKLYHNKRPGVWTSSEDIRVIYNILSF 1015
Cdd:cd14602  157 RCyQEDDSVPICIHCSAGCGRTGVICAIDYTwmllkdgIIPENF----SVFSLIQEMRTQRPSLVQTKEQYELVYNAVIE 232

                 .
gi 23172565 1016 L 1016
Cdd:cd14602  233 L 233
R-PTPc-U-1 cd14632
catalytic domain of receptor-type tyrosine-protein phosphatase U, repeat 1; Receptor-type ...
818-1011 9.01e-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: 9.01e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23172565  818 YINASWLHGFRRLRDFIVTQHPMAHTIKDFWQMVWDHNAQTVVLLSSLDD---INFAQFWPDeatpiESDHY---RVKFL 891
Cdd:cd14632    1 YINANYIDGYHRSNHFIATQGPKQEMVYDFWRMVWQEHCSSIVMITKLVEvgrVKCSKYWPD-----DSDTYgdiKITLL 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23172565  892 NKTNKSDYVSRDFVIQSIQDDYELTVKMLHCPSWPEMSNP---NSIYDFIVDVhERCNDYRNGPIVIVDRYGGAQacTFC 968
Cdd:cd14632   76 KTETLAEYSVRTFALERRGYSARHEVKQFHFTSWPEHGVPyhaTGLLAFIRRV-KASTPPDAGPVVVHCSAGAGR--TGC 152
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*
gi 23172565  969 AIS-SLAIEMEYCS-TANVYQYAKLYHNKRPGVWTSSEDIRVIYN 1011
Cdd:cd14632  153 YIVlDVMLDMAECEgVVDIYNCVKTLCSRRINMIQTEEQYIFIHD 197
R-PTPc-R cd14611
catalytic domain of receptor-type tyrosine-protein phosphatase R; Receptor-type ...
792-955 1.05e-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: 1.05e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23172565  792 KNR-GAIFPIEGSRVHLTPKPGEDG-SDYINASWLHGFR-RLRDFIVTQHPMAHTIKDFWQMVWDHNAQTVVLLSSLDDI 868
Cdd:cd14611    2 KNRyKTILPNPHSRVCLKPKNSNDSlSTYINANYIRGYGgKEKAFIATQGPMINTVNDFWQMVWQEDSPVIVMITKLKEK 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23172565  869 N--FAQFWPDEatpiESDHYRVKFL-NKTNKSD-YVSRDFVIQsiQDDYELTVKMLHCPSWPEMSNPNS---IYDFIVDV 941
Cdd:cd14611   82 NekCVLYWPEK----RGIYGKVEVLvNSVKECDnYTIRNLTLK--QGSQSRSVKHYWYTSWPDHKTPDSaqpLLQLMLDV 155
                        170
                 ....*....|....*
gi 23172565  942 HE-RCNDYRNGPIVI 955
Cdd:cd14611  156 EEdRLASPGRGPVVV 170
PTPc-N7 cd14612
catalytic domain of tyrosine-protein phosphatase non-receptor type 7; Tyrosine-protein ...
792-955 1.70e-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: 1.70e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23172565  792 KNR-GAIFPIEGSRVHL-TPKPGEDGSDYINASWLHGFR-RLRDFIVTQHPMAHTIKDFWQMVWDHNAQTVVLLSSLDDI 868
Cdd:cd14612   18 KDRyKTILPNPQSRVCLrRAGSQEEEGSYINANYIRGYDgKEKAYIATQGPMLNTVSDFWEMVWQEECPIIVMITKLKEK 97
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23172565  869 N--FAQFWPDEatpiESDHYRVKF-LNKTNKSD-YVSRDFVIQSIQDDYEltVKMLHCPSWPEMSNPNS---IYDFIVDV 941
Cdd:cd14612   98 KekCVHYWPEK----EGTYGRFEIrVQDMKECDgYTIRDLTIQLEEESRS--VKHYWFSSWPDHQTPESagpLLRLVAEV 171
                        170
                 ....*....|....*
gi 23172565  942 HERCNDYRN-GPIVI 955
Cdd:cd14612  172 EESRQTAASpGPIVV 186
PTPc-N5 cd14613
catalytic domain of tyrosine-protein phosphatase non-receptor type 5; Tyrosine-protein ...
792-1014 2.53e-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: 2.53e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23172565  792 KNR-GAIFPIEGSRVHLTPKPGEDG-SDYINASWLHGF-RRLRDFIVTQHPMAHTIKDFWQMVWDHNAQTVVLLSSLDDI 868
Cdd:cd14613   28 KNRyKTILPNPHSRVCLTSPDQDDPlSSYINANYIRGYgGEEKVYIATQGPTVNTVGDFWRMVWQERSPIIVMITNIEEM 107
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23172565  869 N--FAQFWPDEATPIESDHYRVKflNKTNKSDYVSRDFVIQSiqDDYELTVKMLHCPSWPEMSNPNS---IYDFIVDVHE 943
Cdd:cd14613  108 NekCTEYWPEEQVTYEGIEITVK--QVIHADDYRLRLITLKS--GGEERGLKHYWYTSWPDQKTPDNappLLQLVQEVEE 183
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 23172565  944 --RCNDYRNGPIVIVDRYGGAQACTFCAISSLAIEMEYCSTANVYQYAKLYHNKRPGVWTSSEDIRVIYNILS 1014
Cdd:cd14613  184 arQQAEPNCGPVIVHCSAGIGRTGCFIATSICCKQLRNEGVVDILRTTCQLRLDRGGMIQTCEQYQFVHHVLS 256
PHA02746 PHA02746
protein tyrosine phosphatase; Provisional
801-994 2.55e-17

protein tyrosine phosphatase; Provisional


Pssm-ID: 165113 [Multi-domain]  Cd Length: 323  Bit Score: 84.70  E-value: 2.55e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23172565   801 EGSRVHLTPKpgEDGSDYINASWLHGFRRLRDFIVTQHPMAHTIKDFWQMVWDHNAQTVVLLSSLDD---INFAQFWPDE 877
Cdd:PHA02746   85 DGKKIEVTSE--DNAENYIHANFVDGFKEANKFICAQGPKEDTSEDFFKLISEHESQVIVSLTDIDDddeKCFELWTKEE 162
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23172565   878 ATPIESDHYRVKFLNKTNKSDYVSRDFVIQSIQDDYELTVKMLHCPSWPEMSNPNSIYDFiVDVHERCNDYRN------- 950
Cdd:PHA02746  163 DSELAFGRFVAKILDIIEELSFTKTRLMITDKISDTSREIHHFWFPDWPDNGIPTGMAEF-LELINKVNEEQAelikqad 241
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....
gi 23172565   951 ------GPIVIVDRYGGAQACTFCAI----SSLAIEMEYCSTANVYQYAKLYHN 994
Cdd:PHA02746  242 ndpqtlGPIVVHCSAGIGRAGTFCAIdnalEQLEKEKEVCLGEIVLKIRKQRHS 295
R-PTPc-typeIIb-1 cd14555
catalytic domain of type IIb (or R2B) subfamily receptor-type tyrosine-protein phosphatases, ...
818-996 2.77e-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: 81.89  E-value: 2.77e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23172565  818 YINASWLHGFRRLRDFIVTQHPMAHTIKDFWQMVWDHNAQTVVLLSSLDD---INFAQFWPDEaTPIESDhYRVKFLNKT 894
Cdd:cd14555    1 YINANYIDGYHRPNHYIATQGPMQETVYDFWRMVWQENSASIVMVTNLVEvgrVKCSRYWPDD-TEVYGD-IKVTLVETE 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23172565  895 NKSDYVSRDFVIQSIQDDYELTVKMLHCPSWPEMSNP---NSIYDFIVDVHERcNDYRNGPIVIVDRYGGAQACTFCAIS 971
Cdd:cd14555   79 PLAEYVVRTFALERRGYHEIREVRQFHFTGWPDHGVPyhaTGLLGFIRRVKAS-NPPSAGPIVVHCSAGAGRTGCYIVID 157
                        170       180
                 ....*....|....*....|....*
gi 23172565  972 SLAIEMEYCSTANVYQYAKLYHNKR 996
Cdd:cd14555  158 IMLDMAEREGVVDIYNCVKELRSRR 182
PTPc-N3 cd14600
catalytic domain of tyrosine-protein phosphatase non-receptor type 3; Tyrosine-protein ...
781-938 5.85e-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: 5.85e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23172565  781 IASAMKQVNSIKNR-GAIFPIEGSRVHLtpkpgEDGSDYINASWLH----GFRRLRDFIVTQHPMAHTIKDFWQMVWDHN 855
Cdd:cd14600   32 ITCAKLPQNMDKNRyKDVLPYDATRVVL-----QGNEDYINASYVNmeipSANIVNKYIATQGPLPHTCAQFWQVVWEQK 106
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23172565  856 AQTVVLLSSLDD---INFAQFWPDEATPIESDHYRVKFLNKTNKSDYVSRDFVIQSIQDDYELTVKMLHCPSWPEMSNPN 932
Cdd:cd14600  107 LSLIVMLTTLTErgrTKCHQYWPDPPDVMEYGGFRVQCHSEDCTIAYVFREMLLTNTQTGEERTVTHLQYVAWPDHGVPD 186

                 ....*.
gi 23172565  933 SIYDFI 938
Cdd:cd14600  187 DSSDFL 192
PTPc_motif smart00404
Protein tyrosine phosphatase, catalytic domain motif;
916-1013 9.79e-17

Protein tyrosine phosphatase, catalytic domain motif;


Pssm-ID: 214649 [Multi-domain]  Cd Length: 105  Bit Score: 77.01  E-value: 9.79e-17
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23172565     916 TVKMLHCPSWPEMSNP---NSIYDFIVDVHERCND-YRNGPIVIVDRYGGAQACTFCAISSLAIEMEYCS-TANVYQYAK 990
Cdd:smart00404    1 TVKHYHYTGWPDHGVPespDSILELLRAVKKNLNQsESSGPVVVHCSAGVGRTGTFVAIDILLQQLEAEAgEVDIFDTVK 80
                            90       100
                    ....*....|....*....|...
gi 23172565     991 LYHNKRPGVWTSSEDIRVIYNIL 1013
Cdd:smart00404   81 ELRSQRPGMVQTEEQYLFLYRAL 103
PTPc_DSPc smart00012
Protein tyrosine phosphatase, catalytic domain, undefined specificity; Protein tyrosine ...
916-1013 9.79e-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: 9.79e-17
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23172565     916 TVKMLHCPSWPEMSNP---NSIYDFIVDVHERCND-YRNGPIVIVDRYGGAQACTFCAISSLAIEMEYCS-TANVYQYAK 990
Cdd:smart00012    1 TVKHYHYTGWPDHGVPespDSILELLRAVKKNLNQsESSGPVVVHCSAGVGRTGTFVAIDILLQQLEAEAgEVDIFDTVK 80
                            90       100
                    ....*....|....*....|...
gi 23172565     991 LYHNKRPGVWTSSEDIRVIYNIL 1013
Cdd:smart00012   81 ELRSQRPGMVQTEEQYLFLYRAL 103
R-PTPc-Z-1 cd17668
catalytic domain of receptor-type tyrosine-protein phosphatase Z, repeat 1; Receptor-type ...
818-1013 1.53e-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: 1.53e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23172565  818 YINASWLHGFRRLRDFIVTQHPMAHTIKDFWQMVWDHNAQTVVLLSSLDDI---NFAQFWPDEATPiESDHYRVKFLNKT 894
Cdd:cd17668    1 YINANYVDGYNKPKAYIAAQGPLKSTAEDFWRMIWEHNVEVIVMITNLVEKgrrKCDQYWPADGSE-EYGNFLVTQKSVQ 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23172565  895 NKSDYVSRDFVIQSIQ--------DDYELTVKMLHCPSWPEMSNPNSIYDFIVDVHERCNDYR--NGPIVIVDRYGGAQA 964
Cdd:cd17668   80 VLAYYTVRNFTLRNTKikkgsqkgRPSGRVVTQYHYTQWPDMGVPEYTLPVLTFVRKASYAKRhaVGPVVVHCSAGVGRT 159
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*....
gi 23172565  965 CTFCAISSLAIEMEYCSTANVYQYAKLYHNKRPGVWTSSEDIRVIYNIL 1013
Cdd:cd17668  160 GTYIVLDSMLQQIQHEGTVNIFGFLKHIRSQRNYLVQTEEQYVFIHDAL 208
PTPc-N3_4 cd14541
catalytic domain of tyrosine-protein phosphatase non-receptor type 21 and type 14; ...
817-952 3.60e-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: 78.53  E-value: 3.60e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23172565  817 DYINASWLH----GFRRLRDFIVTQHPMAHTIKDFWQMVWDHNAQTVVLLSSLDD---INFAQFWPDEATPIESDHYRVK 889
Cdd:cd14541    1 DYINANYVNmeipGSGIVNRYIAAQGPLPNTCADFWQMVWEQKSTLIVMLTTLVErgrVKCHQYWPDLGETMQFGNLQIT 80
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 23172565  890 FLNKTNKSDYVSRDFVIQSIQDDYELTVKMLHCPSWPEM---SNPNSIYDFIvdvhERCNDYRNGP 952
Cdd:cd14541   81 CVSEEVTPSFAFREFILTNTNTGEERHITQMQYLAWPDHgvpDDSSDFLDFV----KRVRQNRVGM 142
PHA02740 PHA02740
protein tyrosine phosphatase; Provisional
478-738 3.72e-16

protein tyrosine phosphatase; Provisional


Pssm-ID: 165107 [Multi-domain]  Cd Length: 298  Bit Score: 80.78  E-value: 3.72e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23172565   478 REYEAIQNEciSDDLPCEHSQHPENKRK--NRYLNITAYDHSRVHLHptpGQKKNLDyinANFIDGYQKGHAFIGTQGPL 555
Cdd:PHA02740   29 KEYRAIVPE--HEDEANKACAQAENKAKdeNLALHITRLLHRRIKLF---NDEKVLD---ARFVDGYDFEQKFICIINLC 100
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23172565   556 PDTFDCFWRMIWEQRVAIIVMITNLVErgrRKC-DMYWP-KDG-VETYGVIQVKLIEEEVMSTYTVRTLQIkhlklkkKK 632
Cdd:PHA02740  101 EDACDKFLQALSDNKVQIIVLISRHAD---KKCfNQFWSlKEGcVITSDKFQIETLEIIIKPHFNLTLLSL-------TD 170
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23172565   633 QCNTEKLVYQYHYTNWPDHGTPDHPLPVLNF----------VKKSSAAnpAEAGPIVVHCSAGVGRTGTYIVLDAMLKQI 702
Cdd:PHA02740  171 KFGQAQKISHFQYTAWPADGFSHDPDAFIDFfcniddlcadLEKHKAD--GKIAPIIIDCIDGISSSAVFCVFDICATEF 248
                         250       260       270
                  ....*....|....*....|....*....|....*.
gi 23172565   703 QQKNIVNVFGFLRHIRAQRNFLVQTEEQYIFLHDAL 738
Cdd:PHA02740  249 DKTGMLSIANALKKVRQKKYGCMNCLDDYVFCYHLI 284
R-PTPc-C-1 cd14557
catalytic domain of receptor-type tyrosine-protein phosphatase C, repeat 1; Receptor-type ...
818-995 5.08e-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: 5.08e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23172565  818 YINASWLHGFRRLRDFIVTQHPMAHTIKDFWQMVWDHNAQTVVLLSSLDDIN---FAQFWP--DEATPIESDhYRVKFLN 892
Cdd:cd14557    1 YINASYIDGFKEPRKYIAAQGPKDETVDDFWRMIWEQKSTVIVMVTRCEEGNrnkCAQYWPsmEEGSRAFGD-VVVKINE 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23172565  893 KTNKSDYVSRDFVIQSIQDDY-ELTVKMLHCPSWPEMSNPNSIYdFIVDVHERCNDYRN---GPIVIVDRYGGAQACTFC 968
Cdd:cd14557   80 EKICPDYIIRKLNINNKKEKGsGREVTHIQFTSWPDHGVPEDPH-LLLKLRRRVNAFNNffsGPIVVHCSAGVGRTGTYI 158
                        170       180
                 ....*....|....*....|....*...
gi 23172565  969 AISSLAIEMEYCSTANVYQY-AKLYHNK 995
Cdd:cd14557  159 GIDAMLEGLEAEGRVDVYGYvVKLRRQR 186
PTPc-N13 cd14597
catalytic domain of tyrosine-protein phosphatase non-receptor type 13; Tyrosine-protein ...
789-954 2.07e-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: 2.07e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23172565  789 NSIKNR-GAIFPIEGSRVHLtpkpGEDGsDYINASWLHGFRRLRDF--IVTQHPMAHTIKDFWQMVWDHNAQTVVLLSSL 865
Cdd:cd14597    3 NRKKNRyKNILPYDTTRVPL----GDEG-GYINASFIKMPVGDEEFvyIACQGPLPTTVADFWQMVWEQKSTVIAMMTQE 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23172565  866 ---DDINFAQFWPDE--ATPIESDHYRVKFLNKTNKSDYVSRDFVIQSIQDDYELTVKMLHCPSWPEMSNPNSIYDFIVD 940
Cdd:cd14597   78 vegGKIKCQRYWPEIlgKTTMVDNRLQLTLVRMQQLKNFVIRVLELEDIQTREVRHITHLNFTAWPDHDTPSQPEQLLTF 157
                        170
                 ....*....|....
gi 23172565  941 VHERCNDYRNGPIV 954
Cdd:cd14597  158 ISYMRHIHKSGPII 171
PTP-N23 cd14539
PTP-like domain of tyrosine-protein phosphatase non-receptor type 23; Tyrosine-protein ...
818-978 4.39e-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: 4.39e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23172565  818 YINASWLHGFRRLR-DFIVTQHPMAHTIKDFWQMVWDHNAQTVVLLSS---LDDINFAQFWPDE-ATPIESDHYRVKFLN 892
Cdd:cd14539    1 YINASLIEDLTPYCpRFIATQAPLPGTAADFWLMVYEQQVSVIVMLVSeqeNEKQKVHRYWPTErGQALVYGAITVSLQS 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23172565  893 KTNKSDYVSRDFVIQSIQDDYELTVKMLHCPSWPEMSNPNSI---YDFIVDVHERCNDYRN--GPIVI-----VDRYGga 962
Cdd:cd14539   81 VRTTPTHVERIISIQHKDTRLSRSVVHLQFTTWPELGLPDSPnplLRFIEEVHSHYLQQRSlqTPIVVhcssgVGRTG-- 158
                        170
                 ....*....|....*.
gi 23172565  963 qacTFCAISSLAIEME 978
Cdd:cd14539  159 ---AFCLLYAAVQEIE 171
PHA02740 PHA02740
protein tyrosine phosphatase; Provisional
766-1024 8.47e-15

protein tyrosine phosphatase; Provisional


Pssm-ID: 165107 [Multi-domain]  Cd Length: 298  Bit Score: 76.54  E-value: 8.47e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23172565   766 QQYKNIIQFQPKDIHIASAmKQVNSIKNRGAIFPIE---GSRVHLTPKpgedgSDYINASWLHGFRRLRDFIVTQHPMAH 842
Cdd:PHA02740   29 KEYRAIVPEHEDEANKACA-QAENKAKDENLALHITrllHRRIKLFND-----EKVLDARFVDGYDFEQKFICIINLCED 102
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23172565   843 TIKDFWQMVWDHNAQTVVLLSSLDDIN-FAQFWP-DEATPIESDHYRVKFLNKTNKSDYVsrdFVIQSIQDDYELTVKML 920
Cdd:PHA02740  103 ACDKFLQALSDNKVQIIVLISRHADKKcFNQFWSlKEGCVITSDKFQIETLEIIIKPHFN---LTLLSLTDKFGQAQKIS 179
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23172565   921 HC--PSWPE---MSNPNSIYDFIVDVHERCNDYRN-------GPIVIVDRYGGAQACTFCAISSLAIEMEYCSTANVYQY 988
Cdd:PHA02740  180 HFqyTAWPAdgfSHDPDAFIDFFCNIDDLCADLEKhkadgkiAPIIIDCIDGISSSAVFCVFDICATEFDKTGMLSIANA 259
                         250       260       270
                  ....*....|....*....|....*....|....*..
gi 23172565   989 AKLYHNKRPGVWTSSEDIRVIYNILS-FLPGNLNLLK 1024
Cdd:PHA02740  260 LKKVRQKKYGCMNCLDDYVFCYHLIAaYLKEKFDILK 296
PTPc-N20_13 cd14538
catalytic domain of tyrosine-protein phosphatase non-receptor type 20 and type 13; ...
818-955 1.14e-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: 1.14e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23172565  818 YINAS---WLHGFRRLRdFIVTQHPMAHTIKDFWQMVWDHNAQtVVLLSSLD----DINFAQFWPD--EATPIESDHYRV 888
Cdd:cd14538    1 YINAShirIPVGGDTYH-YIACQGPLPNTTGDFWQMVWEQKSE-VIAMVTQDveggKVKCHRYWPDslNKPLICGGRLEV 78
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23172565  889 KFLNKTNKSDYVSRDFVIQSIQDDYELTVKMLHCPSWPEMSNPNS---IYDFIVDVHERCNDyrnGPIVI 955
Cdd:cd14538   79 SLEKYQSLQDFVIRRISLRDKETGEVHHITHLNFTTWPDHGTPQSadpLLRFIRYMRRIHNS---GPIVV 145
PHA02742 PHA02742
protein tyrosine phosphatase; Provisional
752-970 4.17e-14

protein tyrosine phosphatase; Provisional


Pssm-ID: 165109 [Multi-domain]  Cd Length: 303  Bit Score: 74.65  E-value: 4.17e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23172565   752 EQVEELKNCTPYLEQQYKNIIQ-FQPKDIHIASAMKqvNSIKNRGAIFPI-EGSRVHLTPKPGedGSDYINASWLHGFRR 829
Cdd:PHA02742   16 EQLIEESNLAEILKEEHEHIMQeIVAFSCNESLELK--NMKKCRYPDAPCfDRNRVILKIEDG--GDDFINASYVDGHNA 91
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23172565   830 LRDFIVTQHPMAHTIKDFWQMVWDHNAQTVVLLSSLDDINFAQFWPDEATPIESDHYRVKFLNKTNK----SDYVSRDFV 905
Cdd:PHA02742   92 KGRFICTQAPLEETALDFWQAIFQDQVRVIVMITKIMEDGKEACYPYWMPHERGKATHGEFKIKTKKiksfRNYAVTNLC 171
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 23172565   906 IQSIQDDYELTVKMLHCPSWPEMS---NPNSIYDFIVDVHERC----------NDYRNGPIVIVDRYGGAQACTFCAI 970
Cdd:PHA02742  172 LTDTNTGASLDIKHFAYEDWPHGGlprDPNKFLDFVLAVREADlkadvdikgeNIVKEPPILVHCSAGLDRAGAFCAI 249
PTPc-N21_14 cd14540
catalytic domain of tyrosine-protein phosphatase non-receptor type 21 and type 14; ...
818-950 1.46e-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: 1.46e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23172565  818 YINASWLHGF--RRLRDFIVTQHPMAHTIKDFWQMVWDHNAQTVVLLSSLDD---INFAQFWPDEAtpIESD-----HYR 887
Cdd:cd14540    1 YINASHITATvgGKQRFYIAAQGPLQNTVGDFWQMVWEQGVYLVVMVTAEEEggrEKCFRYWPTLG--GEHDaltfgEYK 78
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 23172565  888 VKFLNKTNKSDYVSRDFVIQSIQDDYELTVKMLHCPSWPEMSNPNSIYDFIvDVHERCNDYRN 950
Cdd:cd14540   79 VSTKFSVSSGCYTTTGLRVKHTLSGQSRTVWHLQYTDWPDHGCPEDVSGFL-DFLEEINSVRR 140
PTPc-N14 cd14599
catalytic domain of tyrosine-protein phosphatase non-receptor type 14; Tyrosine-protein ...
767-943 1.65e-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: 1.65e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23172565  767 QYKNIIQFQPKDIHIASAMKQvNSIKNR-GAIFPIEGSRVHLTPKPgEDGSDYINASWLHGFRRLRD--FIVTQHPMAHT 843
Cdd:cd14599   17 EYEQIPKKKADGVFTTATLPE-NAERNRiREVVPYEENRVELVPTK-ENNTGYINASHIKVTVGGEEwhYIATQGPLPHT 94
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23172565  844 IKDFWQMVWDHNAQTVVLLSSLDDINFAQ---FWPDEATPIESDHY---RVKFLNKTNKSDYVSRDFVIQSIQDDYELTV 917
Cdd:cd14599   95 CHDFWQMVWEQGVNVIAMVTAEEEGGRSKshrYWPKLGSKHSSATYgkfKVTTKFRTDSGCYATTGLKVKHLLSGQERTV 174
                        170       180
                 ....*....|....*....|....*.
gi 23172565  918 KMLHCPSWPEMSNPNSIYDFIVDVHE 943
Cdd:cd14599  175 WHLQYTDWPDHGCPEEVQGFLSYLEE 200
PTPc-N22_18_12 cd14542
catalytic domain of tyrosine-protein phosphatase non-receptor type 22, type 18 and type 12; ...
818-970 3.17e-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: 3.17e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23172565  818 YINASWLHGFRRLRDFIVTQHPMAHTIKDFWQMVWDHNAQTVVLLS---SLDDINFAQFWPDEAtpiESDHYRVKFLNKT 894
Cdd:cd14542    1 YINANFIKGVSGSKAYIATQGPLPNTVLDFWRMIWEYNVQVIVMACrefEMGKKKCERYWPEEG---EEQLQFGPFKISL 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23172565  895 NKSDYVSRDFVIQSIQ---DDYELTVKMLHCPSWPEMSNPNSIyDFIVDVHERCNDYRNG---PIVIVDRYGGAQACTFC 968
Cdd:cd14542   78 EKEKRVGPDFLIRTLKvtfQKESRTVYQFHYTAWPDHGVPSSV-DPILDLVRLVRDYQGSedvPICVHCSAGCGRTGTIC 156

                 ..
gi 23172565  969 AI 970
Cdd:cd14542  157 AI 158
PTP_YopH-like cd14559
YopH and related bacterial protein tyrosine phosphatases; Yersinia outer protein H (YopH) ...
534-731 3.39e-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: 3.39e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23172565  534 INANFIDGYQKgHAFIGTQGPLPDTFDCFWRMIWEQRVAIIVMITNLVERGRRKCDMYWPKDGveTYGVIQVKliEEEVM 613
Cdd:cd14559   18 LNANRVQIGNK-NVAIACQYPKNEQLEDHLKMLADNRTPCLVVLASNKDIQRKGLPPYFRQSG--TYGSVTVK--SKKTG 92
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23172565  614 STYTVRTLQIKHLKLKKKKQCNTEKL-VYqyHYTNWPDHGTPD---------------HPLPVLNFVKKSSAANPAEAGP 677
Cdd:cd14559   93 KDELVDGLKADMYNLKITDGNKTITIpVV--HVTNWPDHTAISseglkeladlvnksaEEKRNFYKSKGSSAINDKNKLL 170
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 23172565  678 IVVHCSAGVGRTGTYIVLDAMLKQIqqkNIVNVFGFLRHIRAQRN-FLVQTEEQY 731
Cdd:cd14559  171 PVIHCRAGVGRTGQLAAAMELNKSP---NNLSVEDIVSDMRTSRNgKMVQKDEQL 222
PTPc-N6 cd14606
catalytic domain of tyrosine-protein phosphatase non-receptor type 6; Tyrosine-protein ...
785-955 4.84e-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: 4.84e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23172565  785 MKQVNSIKNR-GAIFPIEGSRVHLTPK-PGEDGSDYINASWLHGFRRLRD-----FIVTQHPMAHTIKDFWQMVWDHNAQ 857
Cdd:cd14606   14 QRPENKSKNRyKNILPFDHSRVILQGRdSNIPGSDYINANYVKNQLLGPDenaktYIASQGCLEATVNDFWQMAWQENSR 93
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23172565  858 TVVLLSSldDINFAQ-----FWPDEATPIESDHYRVKFLNKTNKSDYVSRDFVIqSIQDDYELTVKMLHCP--SWPEM-- 928
Cdd:cd14606   94 VIVMTTR--EVEKGRnkcvpYWPEVGMQRAYGPYSVTNCGEHDTTEYKLRTLQV-SPLDNGELIREIWHYQylSWPDHgv 170
                        170       180
                 ....*....|....*....|....*....
gi 23172565  929 -SNPNSIYDFIVDVHERCNDYRN-GPIVI 955
Cdd:cd14606  171 pSEPGGVLSFLDQINQRQESLPHaGPIIV 199
FN3 smart00060
Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, ...
171-256 5.93e-13

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: 65.33  E-value: 5.93e-13
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23172565     171 PSKPQNLTILDVSANSITMSWHPPKNQNGaiAGYHV-FHIHDNQTGVEIVKNSRNSVETliHFELQNLRPYTDYRVIVKA 249
Cdd:smart00060    1 PSPPSNLRVTDVTSTSVTLSWEPPPDDGI--TGYIVgYRVEYREEGSEWKEVNVTPSST--SYTLTGLKPGTEYEFRVRA 76

                    ....*..
gi 23172565     250 FTTKNEG 256
Cdd:smart00060   77 VNGAGEG 83
PTPc_plant_PTP1 cd17658
protein tyrosine phosphatase 1 from Arabidopsis thaliana and similar plant PTPs; Arabidopsis ...
818-1011 1.63e-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: 1.63e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23172565  818 YINASWLH--GFRRLRDFIVTQHPMAHTIKDFWQMVWDHNAQTVVLLSSLDDIN----FAQFWPDEATPiESDHYRVKFL 891
Cdd:cd17658    1 YINASLVEtpASESLPKFIATQGPLPHTFEDFWEMVIQQRCPVIIMLTRLVDNYstakCADYFPAEENE-SREFGRISVT 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23172565  892 NKTNKSDYVS---RDFVIQSIQ-DDYELTVKMLHCPSWPEMSNPNSIYdFIVDVHER--CNDYRNGPIVIVDRYGGAQAC 965
Cdd:cd17658   80 NKKLKHSQHSitlRVLEVQYIEsEEPPLSVLHIQYPEWPDHGVPKDTR-SVRELLKRlyGIPPSAGPIVVHCSAGIGRTG 158
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|.
gi 23172565  966 TFCAISS-----LAIEMeycSTANVYQYAKLYHNKRPGVWTSSEDIRVIYN 1011
Cdd:cd17658  159 AYCTIHNtirriLEGDM---SAVDLSKTVRKFRSQRIGMVQTQDQYIFCYA 206
PTPc-N4 cd14601
catalytic domain of tyrosine-protein phosphatase non-receptor type 4; Tyrosine-protein ...
817-938 3.46e-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: 3.46e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23172565  817 DYINASWLH----GFRRLRDFIVTQHPMAHTIKDFWQMVWDHNAQTVVLLSSLDD---INFAQFWPDEATPIESDHYRVK 889
Cdd:cd14601    1 DYINANYINmeipSSSIINRYIACQGPLPNTCSDFWQMTWEQGSSMVVMLTTQVErgrVKCHQYWPEPSGSSSYGGFQVT 80
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*....
gi 23172565  890 FLNKTNKSDYVSRDFVIQSIQDDYELTVKMLHCPSWPEMSNPNSIYDFI 938
Cdd:cd14601   81 CHSEEGNPAYVFREMTLTNLEKNESRPLTQIQYIAWPDHGVPDDSSDFL 129
PTPc-N20 cd14596
catalytic domain of tyrosine-protein phosphatase non-receptor type 20; Tyrosine-protein ...
818-955 7.08e-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: 7.08e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23172565  818 YINASWLH---GFRRLRdFIVTQHPMAHTIKDFWQMVWDHNAQTVVLLS---SLDDINFAQFWPDEAT-PIESDHYRVkF 890
Cdd:cd14596    1 YINASYITmpvGEEELF-YIATQGPLPSTIDDFWQMVWENRSDVIAMMTrevERGKVKCHRYWPETLQePMELENYQL-R 78
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23172565  891 LNKTNKSDYvsrdFVIQSIQDDYELT-----VKMLHCPSWPEMSNPNSIYDFIVDVHERCNDYRNGPIVI 955
Cdd:cd14596   79 LENYQALQY----FIIRIIKLVEKETgenrlIKHLQFTTWPDHGTPQSSDQLVKFICYMRKVHNTGPIVV 144
PHA02738 PHA02738
hypothetical protein; Provisional
803-985 9.70e-12

hypothetical protein; Provisional


Pssm-ID: 222923 [Multi-domain]  Cd Length: 320  Bit Score: 67.64  E-value: 9.70e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23172565   803 SRVHLtPKPGEDGsDYINASWLHGFRRLRDFIVTQHPMAHTIKDFWQMVWDHNAQTVVLLSSLDDINFAQ---FWPD-EA 878
Cdd:PHA02738   64 SRVIL-PAERNRG-DYINANYVDGFEYKKKFICGQAPTRQTCYDFYRMLWMEHVQIIVMLCKKKENGREKcfpYWSDvEQ 141
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23172565   879 TPIESDHYRVKFLNKTNKSDYVSRDFViqsIQDDYELTVKMLH--CPSWPEMSNPNSIYDFI----------VDVHErcN 946
Cdd:PHA02738  142 GSIRFGKFKITTTQVETHPHYVKSTLL---LTDGTSATQTVTHfnFTAWPDHDVPKNTSEFLnfvlevrqcqKELAQ--E 216
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*.
gi 23172565   947 DYRNG-------PIVIVDRYGGAQACTFCAISSLAIEMEYCSTANV 985
Cdd:PHA02738  217 SLQIGhnrlqppPIVVHCNAGLGRTPCYCVVDISISRFDACATVSI 262
FN3 COG3401
Fibronectin type 3 domain [General function prediction only];
111-349 2.35e-11

Fibronectin type 3 domain [General function prediction only];


Pssm-ID: 442628 [Multi-domain]  Cd Length: 603  Bit Score: 68.11  E-value: 2.35e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23172565  111 PVLGTVATSIEQQDQPPDVPATTLAFANAFPVPVAGEmgngnGNYNDATPPYAAVDDNYVPSKPQNLTILDVSANSITMS 190
Cdd:COG3401  178 AAVATTSLTVTSTTLVDGGGDIEPGTTYYYRVAATDT-----GGESAPSNEVSVTTPTTPPSAPTGLTATADTPGSVTLS 252
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23172565  191 WHPpkNQNGAIAGYHVFHIHDNQTGVEIVKNSRNSvetliHFELQNLRPYTDYRVIVKAFTT-KNEGEPSDQIAQRTDVG 269
Cdd:COG3401  253 WDP--VTESDATGYRVYRSNSGDGPFTKVATVTTT-----SYTDTGLTNGTTYYYRVTAVDAaGNESAPSNVVSVTTDLT 325
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23172565  270 GPSAPAIVNLTCHSQESITIRWRRPYEfyNTIDFYII--KTRLAGQDThrdiRINASAKelETAMILQNLTTNSYYEVKV 347
Cdd:COG3401  326 PPAAPSGLTATAVGSSSITLSWTASSD--ADVTGYNVyrSTSGGGTYT----KIAETVT--TTSYTDTGLTPGTTYYYKV 397

                 ..
gi 23172565  348 AA 349
Cdd:COG3401  398 TA 399
FN3 cd00063
Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein ...
271-349 8.84e-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: 8.84e-09
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 23172565  271 PSAPAIVNLTCHSQESITIRWRRPYEFYNTIDFYIIKTRLAGQDTHRDIRINASAkelETAMILQNLTTNSYYEVKVAA 349
Cdd:cd00063    1 PSPPTNLRVTDVTSTSVTLSWTPPEDDGGPITGYVVEYREKGSGDWKEVEVTPGS---ETSYTLTGLKPGTEYEFRVRA 76
PTP_DSP_cys cd14494
cys-based protein tyrosine phosphatase and dual-specificity phosphatase superfamily; This ...
676-736 3.13e-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: 3.13e-08
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 23172565  676 GPIVVHCSAGVGRTGTYIVLDAMLKQiqqknIVNVFGFLRHIRAQRNF-LVQTEEQYIFLHD 736
Cdd:cd14494   57 EPVLVHCKAGVGRTGTLVACYLVLLG-----GMSAEEAVRIVRLIRPGgIPQTIEQLDFLIK 113
CDC14 COG2453
Protein-tyrosine phosphatase [Signal transduction mechanisms];
642-736 4.95e-08

Protein-tyrosine phosphatase [Signal transduction mechanisms];


Pssm-ID: 441989 [Multi-domain]  Cd Length: 140  Bit Score: 53.05  E-value: 4.95e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23172565  642 QYHYTNWPDHGTPDHP--LPVLNFVKKSSAANpaeaGPIVVHCSAGVGRTGT----YIVLDAM-LKQIqqknivnvfgfL 714
Cdd:COG2453   49 EYLHLPIPDFGAPDDEqlQEAVDFIDEALREG----KKVLVHCRGGIGRTGTvaaaYLVLLGLsAEEA-----------L 113
                         90       100
                 ....*....|....*....|..
gi 23172565  715 RHIRAQRNFLVQTEEQYIFLHD 736
Cdd:COG2453  114 ARVRAARPGAVETPAQRAFLER 135
PTPc-N21 cd14598
catalytic domain of tyrosine-protein phosphatase non-receptor type 21; Tyrosine-protein ...
818-943 3.12e-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: 3.12e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23172565  818 YINAS----------WlhgfrrlrDFIVTQHPMAHTIKDFWQMVWDHNAQTVVLLSSLDDINFAQ---FWP---DEATPI 881
Cdd:cd14598    1 YINAShikvtvggkeW--------DYIATQGPLQNTCQDFWQMVWEQGVAIIAMVTAEEEGGREKsfrYWPrlgSRHNTV 72
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 23172565  882 ESDHYRVKFLNKTNKSDYVSRDFVIQSIQDDYELTVKMLHCPSWPEMSNPNSIYDFIVDVHE 943
Cdd:cd14598   73 TYGRFKITTRFRTDSGCYATTGLKIKHLLTGQERTVWHLQYTDWPEHGCPEDLKGFLSYLEE 134
FN3 smart00060
Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, ...
271-351 1.05e-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: 1.05e-05
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23172565     271 PSAPAIVNLTCHSQESITIRWRRPYEfyNTIDFYIIKTRLAGQDTHRDiRINASAKELETAMILQNLTTNSYYEVKVAAA 350
Cdd:smart00060    1 PSPPSNLRVTDVTSTSVTLSWEPPPD--DGITGYIVGYRVEYREEGSE-WKEVNVTPSSTSYTLTGLKPGTEYEFRVRAV 77

                    .
gi 23172565     351 T 351
Cdd:smart00060   78 N 78
DUSP23 cd14504
dual specificity phosphatase 23; Dual specificity phosphatase 23 (DUSP23), also known as ...
661-730 2.04e-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: 2.04e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 23172565  661 LNFVKKSSAANpaeaGPIVVHCSAGVGRTGT----YIVLDAMLKQIQQknivnvfgfLRHIRAQRNFLVQTEEQ 730
Cdd:cd14504   72 LDIVEEANAKN----EAVLVHCLAGKGRTGTmlacYLVKTGKISAVDA---------INEIRRIRPGSIETSEQ 132
DSPc smart00195
Dual specificity phosphatase, catalytic domain;
673-720 2.06e-04

Dual specificity phosphatase, catalytic domain;


Pssm-ID: 214551 [Multi-domain]  Cd Length: 138  Bit Score: 42.65  E-value: 2.06e-04
                            10        20        30        40
                    ....*....|....*....|....*....|....*....|....*...
gi 23172565     673 AEAGPIVVHCSAGVGRTGTYIVldAMLKQIQQKNIVNVFGFLRHIRAQ 720
Cdd:smart00195   76 SKGGKVLVHCQAGVSRSATLII--AYLMKTRNMSLNDAYDFVKDRRPI 121
fn3 pfam00041
Fibronectin type III domain;
272-351 2.49e-04

Fibronectin type III domain;


Pssm-ID: 394996 [Multi-domain]  Cd Length: 85  Bit Score: 40.86  E-value: 2.49e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23172565    272 SAPAIVNLTCHSQESITIRWRRPYEFYNTIDFYIIKTRLAG-QDTHRDIRINASakelETAMILQNLTTNSYYEVKVAAA 350
Cdd:pfam00041    1 SAPSNLTVTDVTSTSLTVSWTPPPDGNGPITGYEVEYRPKNsGEPWNEITVPGT----TTSVTLTGLKPGTEYEVRVQAV 76

                   .
gi 23172565    351 T 351
Cdd:pfam00041   77 N 77
FN3 COG3401
Fibronectin type 3 domain [General function prediction only];
129-349 5.00e-04

Fibronectin type 3 domain [General function prediction only];


Pssm-ID: 442628 [Multi-domain]  Cd Length: 603  Bit Score: 44.22  E-value: 5.00e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23172565  129 VPATTLAFANAFPVPVAGEMG-NGNGNYNDATPPYAAVDDNYVPSKPQNLTILDVSANSITMSWHPPKNQNGAIAGYHVF 207
Cdd:COG3401  106 ATNTGLTSSDEVPSPAVGTATtATAVAGGAATAGTYALGAGLYGVDGANASGTTASSVAGAGVVVSPDTSATAAVATTSL 185
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23172565  208 HIHDNQTGVEIVKNSrnsvetlihfelqnlrPYTDYRVIVKAFTTKNEGEPSDQIAQRTDVGGPSAPAIVNLTCHSQESI 287
Cdd:COG3401  186 TVTSTTLVDGGGDIE----------------PGTTYYYRVAATDTGGESAPSNEVSVTTPTTPPSAPTGLTATADTPGSV 249
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 23172565  288 TIRWRRPYEfyNTIDFYIIKTRLAGQDTHRDIrinASAKELE-TAMILQNLTTNSYyevKVAA 349
Cdd:COG3401  250 TLSWDPVTE--SDATGYRVYRSNSGDGPFTKV---ATVTTTSyTDTGLTNGTTYYY---RVTA 304
PTPLP-like cd14495
Protein tyrosine phosphatase-like domains of phytases and similar domains; This subfamily ...
637-774 6.00e-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: 6.00e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23172565  637 EKLVYQ--YHYTNW--PDHGTPDhPLPV---LNFVKkssaANPAEAGpIVVHCSAGVGRTGTYIVLDAMLKqiqqkNIVN 709
Cdd:cd14495  147 EELVKKkgAHYVRIaaTDHVWPD-DEEIdafVAFYR----SLPADAW-LHFHCRAGKGRTTTFMVMYDMLK-----NPKD 215
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 23172565  710 VFgfLRHIrAQRNFLVqteeqyiflhdalveaiasGETNLMAEQVEELKNCTPYLEQQYKNIIQF 774
Cdd:cd14495  216 VS--FDDI-IARQYLI-------------------GGNYLAYEVDKDKNWKRPYYEERAQFLQKF 258
PTP_PTPDC1 cd14506
protein tyrosine phosphatase domain of PTP domain-containing protein 1; protein tyrosine ...
640-736 7.46e-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: 7.46e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23172565  640 VYQYHYtNWPDHGTPDhPLPVLNFVKKSSAAnPAEAGPIVVHCSAGVGRTGTYI--VLDAMLKQIQQKNIvnvfgflRHI 717
Cdd:cd14506   77 IYFYNF-GWKDYGVPS-LTTILDIVKVMAFA-LQEGGKVAVHCHAGLGRTGVLIacYLVYALRMSADQAI-------RLV 146
                         90
                 ....*....|....*....
gi 23172565  718 RAQRNFLVQTEEQYIFLHD 736
Cdd:cd14506  147 RSKRPNSIQTRGQVLCVRE 165
CDKN3-like cd14505
cyclin-dependent kinase inhibitor 3 and similar proteins; This family is composed of ...
678-736 1.95e-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: 1.95e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 23172565  678 IVVHCSAGVGRTGT-----YIVLDAMLKQIQQKNIVnvfgflrhiRAQRNFLVQTEEQYIFLHD 736
Cdd:cd14505  109 VLIHCKGGLGRTGLiaaclLLELGDTLDPEQAIAAV---------RALRPGAIQTPKQENFLHQ 163
PTPlike_phytase pfam14566
Inositol hexakisphosphate; Inositol hexakisphosphate, often called phytate, is found in ...
641-700 3.34e-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: 3.34e-03
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 23172565    641 YQYHYT-------NWPDHGTPDhplPVLNFVKkssaaNPAEAGPIVVHCSAGVGRTGTYIVLDAMLK 700
Cdd:pfam14566   99 PGVDYRripitdeKAPLEEDFD---ALISIVK-----DAPEDTALVFNCQMGRGRTTTAMVIADLVR 157
CDC14_C cd14499
C-terminal dual-specificity phosphatase domain of CDC14 family proteins; The cell division ...
673-698 4.24e-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: 4.24e-03
                         10        20
                 ....*....|....*....|....*.
gi 23172565  673 AEAGPIVVHCSAGVGRTGTYIVLDAM 698
Cdd:cd14499  107 NEKGAIAVHCKAGLGRTGTLIACYLM 132
PTP_PTEN-like cd14497
protein tyrosine phosphatase-like domain of phosphatase and tensin homolog and similar ...
643-694 8.26e-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: 8.26e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 23172565  643 YHYtNWPDHgtpdHPLPV---LNFVK------KSSAANPAeagpiVVHCSAGVGRTGTYIV 694
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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