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Conserved domains on  [gi|2077601385|ref|XP_042740246|]
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tyrosine-protein phosphatase non-receptor type 22 isoform X2 [Lagopus leucura]

Protein Classification

PTPc-N22 domain-containing protein( domain architecture ID 12998656)

PTPc-N22 domain-containing protein

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
PTPc-N22 cd14602
catalytic domain of tyrosine-protein phosphatase non-receptor type 22; Tyrosine-protein ...
 57-290 0e+00

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: 522.48  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077601385  57 KNRYKDILPYDHSRVELSLITSDTDSHYINANFIKGVYGPRAYIATQGPLPTTVTDFWRMIWEYEVLIVVMACMEFEMGK 136
Cdd:cd14602     1 KNRYKDILPYDHSRVELSLITSDEDSDYINANFIKGVYGPRAYIATQGPLSTTLLDFWRMIWEYSVLIIVMACMEFEMGK 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077601385 137 KKCERYWAEVGDPSLQCGPFSVTCEAEEKKNEYVIRTLKVTLNEAARTIHQFHYQNWPDHDIPSSIDPILELIGEVRCYQ 216
Cdd:cd14602    81 KKCERYWAEPGEMQLEFGPFSVTCEAEKRKSDYIIRTLKVKFNSETRTIYQFHYKNWPDHDVPSSIDPILELIWDVRCYQ 160

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2077601385 217 PDDSIPICIHCSAGCGRTGVVCAIDYTWKLLKDGIVPVNFSIFSLIQEMRTQRPSIVQTKEQYKLVYNAVIELF 290
Cdd:cd14602   161 EDDSVPICIHCSAGCGRTGVICAIDYTWMLLKDGIIPENFSVFSLIQEMRTQRPSLVQTKEQYELVYNAVIELF 234
 
Name Accession Description Interval E-value
PTPc-N22 cd14602
catalytic domain of tyrosine-protein phosphatase non-receptor type 22; Tyrosine-protein ...
 57-290 0e+00

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: 522.48  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077601385  57 KNRYKDILPYDHSRVELSLITSDTDSHYINANFIKGVYGPRAYIATQGPLPTTVTDFWRMIWEYEVLIVVMACMEFEMGK 136
Cdd:cd14602     1 KNRYKDILPYDHSRVELSLITSDEDSDYINANFIKGVYGPRAYIATQGPLSTTLLDFWRMIWEYSVLIIVMACMEFEMGK 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077601385 137 KKCERYWAEVGDPSLQCGPFSVTCEAEEKKNEYVIRTLKVTLNEAARTIHQFHYQNWPDHDIPSSIDPILELIGEVRCYQ 216
Cdd:cd14602    81 KKCERYWAEPGEMQLEFGPFSVTCEAEKRKSDYIIRTLKVKFNSETRTIYQFHYKNWPDHDVPSSIDPILELIWDVRCYQ 160

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2077601385 217 PDDSIPICIHCSAGCGRTGVVCAIDYTWKLLKDGIVPVNFSIFSLIQEMRTQRPSIVQTKEQYKLVYNAVIELF 290
Cdd:cd14602   161 EDDSVPICIHCSAGCGRTGVICAIDYTWMLLKDGIIPENFSVFSLIQEMRTQRPSLVQTKEQYELVYNAVIELF 234
PTPc smart00194
Protein tyrosine phosphatase, catalytic domain;
24-288 2.17e-113

Protein tyrosine phosphatase, catalytic domain;


Pssm-ID: 214550 [Multi-domain]  Cd Length: 259  Bit Score: 344.26  E-value: 2.17e-113
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077601385   24 FADEFLKLKRQSTKYRSdkiypTATAECPENIKKNRYKDILPYDHSRVELSLITSDtDSHYINANFIKGVYGPRAYIATQ 103
Cdd:smart00194   2 LEEEFEKLDRLKPDDES-----CTVAAFPENRDKNRYKDVLPYDHTRVKLKPPPGE-GSDYINASYIDGPNGPKAYIATQ 75

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077601385  104 GPLPTTVTDFWRMIWEYEVLIVVMACMEFEMGKKKCERYWAEVGDPSLQCGPFSVTCEAEEKKNEYVIRTLKVTL--NEA 181
Cdd:smart00194  76 GPLPSTVEDFWRMVWEQKVTVIVMLTELVEKGREKCAQYWPDEEGEPLTYGDITVTLKSVEKVDDYTIRTLEVTNtgCSE 155

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077601385  182 ARTIHQFHYQNWPDHDIPSSIDPILELIGEVRCYQPDDSIPICIHCSAGCGRTGVVCAIDYTWKLLKDGIvpvNFSIFSL 261
Cdd:smart00194 156 TRTVTHYHYTNWPDHGVPESPESILDLIRAVRKSQSTSTGPIVVHCSAGVGRTGTFIAIDILLQQLEAGK---EVDIFEI 232

                          250       260
                   ....*....|....*....|....*..
gi 2077601385  262 IQEMRTQRPSIVQTKEQYKLVYNAVIE 288
Cdd:smart00194 233 VKELRSQRPGMVQTEEQYIFLYRAILE 259
Y_phosphatase pfam00102
Protein-tyrosine phosphatase;
54-288 1.72e-105

Protein-tyrosine phosphatase;


Pssm-ID: 459674 [Multi-domain]  Cd Length: 234  Bit Score: 322.65  E-value: 1.72e-105
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077601385  54 NIKKNRYKDILPYDHSRVELSliTSDTDSHYINANFIKGVYGPRAYIATQGPLPTTVTDFWRMIWEYEVLIVVMACMEFE 133
Cdd:pfam00102   1 NLEKNRYKDVLPYDHTRVKLT--GDPGPSDYINASYIDGYKKPKKYIATQGPLPNTVEDFWRMVWEEKVTIIVMLTELEE 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077601385 134 MGKKKCERYWAEVGDPSLQCGPFSVTCEAEEKKN-EYVIRTLKVTLN--EAARTIHQFHYQNWPDHDIPSSIDPILELIG 210
Cdd:pfam00102  79 KGREKCAQYWPEEEGESLEYGDFTVTLKKEKEDEkDYTVRTLEVSNGgsEETRTVKHFHYTGWPDHGVPESPNSLLDLLR 158

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2077601385 211 EVRCYQPDDSI-PICIHCSAGCGRTGVVCAIDYTWKLLKDGIVpvnFSIFSLIQEMRTQRPSIVQTKEQYKLVYNAVIE 288
Cdd:pfam00102 159 KVRKSSLDGRSgPIVVHCSAGIGRTGTFIAIDIALQQLEAEGE---VDIFQIVKELRSQRPGMVQTLEQYIFLYDAILE 234
COG5599 COG5599
Protein tyrosine phosphatase [Signal transduction mechanisms];
10-297 4.99e-50

Protein tyrosine phosphatase [Signal transduction mechanisms];


Pssm-ID: 444335 [Multi-domain]  Cd Length: 282  Bit Score: 177.21  E-value: 4.99e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077601385  10 NLERAQSKKLNQEAFADEFLKLKRQSTKYRSDKIYPtataECPENIKKNRYKDILPYDHSRVElslitsdTDSHYINANF 89
Cdd:COG5599     2 SPKNPIAIKSEEEKINSRLSTLTNELAPSHNDPQYL----QNINGSPLNRFRDIQPYKETALR-------ANLGYLNANY 70

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077601385  90 IKgVYGPRAYIATQGPLPTTVTDFWRMIWEYEVLIVVM--ACMEFEMGKKKCERYWAEVGDPSLQcgpfsvTCEAEEKKN 167
Cdd:COG5599    71 IQ-VIGNHRYIATQYPLEEQLEDFFQMLFDNNTPVLVVlaSDDEISKPKVKMPVYFRQDGEYGKY------EVSSELTES 143

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077601385 168 EYV-----IRTLKVTLNEAA---RTIHQFHYQNWPDHDIPSS--IDPILELIGEVRCYQPDDSIPICIHCSAGCGRTGVV 237
Cdd:COG5599   144 IQLrdgieARTYVLTIKGTGqkkIEIPVLHVKNWPDHGAISAeaLKNLADLIDKKEKIKDPDKLLPVVHCRAGVGRTGTL 223

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2077601385 238 CAIDYTWKLLKDGIVpVNFSIFSLIQEMRTQR-PSIVQTKEQyklvYNAVIELFKRQIEAL 297
Cdd:COG5599   224 IACLALSKSINALVQ-ITLSVEEIVIDMRTSRnGGMVQTSEQ----LDVLVKLAEQQIRPL 279
PHA02738 PHA02738
hypothetical protein; Provisional
 33-286 1.96e-44

hypothetical protein; Provisional


Pssm-ID: 222923 [Multi-domain]  Cd Length: 320  Bit Score: 162.79  E-value: 1.96e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077601385  33 RQSTKYRSDKIYPTATAEcPENIKKNRYKDILPYDHSRVELSliTSDTDSHYINANFIKGVYGPRAYIATQGPLPTTVTD 112
Cdd:PHA02738   29 REHQKVISEKVDGTFNAE-KKNRKLNRYLDAVCFDHSRVILP--AERNRGDYINANYVDGFEYKKKFICGQAPTRQTCYD 105

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077601385 113 FWRMIWEYEVLIVVMACMEFEMGKKKCERYWAEVGDPSLQCGPFSVTCEAEEKKNEYVIRTLKVTL-NEAARTIHQFHYQ 191
Cdd:PHA02738  106 FYRMLWMEHVQIIVMLCKKKENGREKCFPYWSDVEQGSIRFGKFKITTTQVETHPHYVKSTLLLTDgTSATQTVTHFNFT 185

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077601385 192 NWPDHDIPSSIDPILELIGEVRCYQPD-------------DSIPICIHCSAGCGRTGVVCAIDYTWKLLKDGivpVNFSI 258
Cdd:PHA02738  186 AWPDHDVPKNTSEFLNFVLEVRQCQKElaqeslqighnrlQPPPIVVHCNAGLGRTPCYCVVDISISRFDAC---ATVSI 262

                         250       260
                  ....*....|....*....|....*...
gi 2077601385 259 FSLIQEMRTQRPSIVQTKEQYKLVYNAV 286
Cdd:PHA02738  263 PSIVSSIRNQRYYSLFIPFQYFFCYRAV 290
 
Name Accession Description Interval E-value
PTPc-N22 cd14602
catalytic domain of tyrosine-protein phosphatase non-receptor type 22; Tyrosine-protein ...
 57-290 0e+00

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: 522.48  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077601385  57 KNRYKDILPYDHSRVELSLITSDTDSHYINANFIKGVYGPRAYIATQGPLPTTVTDFWRMIWEYEVLIVVMACMEFEMGK 136
Cdd:cd14602     1 KNRYKDILPYDHSRVELSLITSDEDSDYINANFIKGVYGPRAYIATQGPLSTTLLDFWRMIWEYSVLIIVMACMEFEMGK 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077601385 137 KKCERYWAEVGDPSLQCGPFSVTCEAEEKKNEYVIRTLKVTLNEAARTIHQFHYQNWPDHDIPSSIDPILELIGEVRCYQ 216
Cdd:cd14602    81 KKCERYWAEPGEMQLEFGPFSVTCEAEKRKSDYIIRTLKVKFNSETRTIYQFHYKNWPDHDVPSSIDPILELIWDVRCYQ 160

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2077601385 217 PDDSIPICIHCSAGCGRTGVVCAIDYTWKLLKDGIVPVNFSIFSLIQEMRTQRPSIVQTKEQYKLVYNAVIELF 290
Cdd:cd14602   161 EDDSVPICIHCSAGCGRTGVICAIDYTWMLLKDGIIPENFSVFSLIQEMRTQRPSLVQTKEQYELVYNAVIELF 234
PTPc-N12 cd14604
catalytic domain of tyrosine-protein phosphatase non-receptor type 12; Tyrosine-protein ...
 2-294 1.34e-162

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: 472.49  E-value: 1.34e-162
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077601385   2 DQREILLQNLERAQSKKLN----QEAFADEFLKLKRQSTKYRSDKIYPTATAECPENIKKNRYKDILPYDHSRVELSLIT 77
Cdd:cd14604     1 EQVEILKKFIERVQAMKSTdhngEDNFASDFMRLRRLSTKYRTEKIYPTATGEKEENVKKNRYKDILPFDHSRVKLTLKT 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077601385  78 SDTDSHYINANFIKGVYGPRAYIATQGPLPTTVTDFWRMIWEYEVLIVVMACMEFEMGKKKCERYWAEVGDPSLQCGPFS 157
Cdd:cd14604    81 SSQDSDYINANFIKGVYGPKAYIATQGPLANTVIDFWRMIWEYNVAIIVMACREFEMGRKKCERYWPLYGEEPMTFGPFR 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077601385 158 VTCEAEEKKNEYVIRTLKVTLNEAARTIHQFHYQNWPDHDIPSSIDPILELIGEVRCYQPDDSIPICIHCSAGCGRTGVV 237
Cdd:cd14604   161 ISCEAEQARTDYFIRTLLLEFQNETRRLYQFHYVNWPDHDVPSSFDSILDMISLMRKYQEHEDVPICIHCSAGCGRTGAI 240

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 2077601385 238 CAIDYTWKLLKDGIVPVNFSIFSLIQEMRTQRPSIVQTKEQYKLVYNAVIELFKRQI 294
Cdd:cd14604   241 CAIDYTWNLLKAGKIPEEFNVFNLIQEMRTQRHSAVQTKEQYELVHRAIAQLFEKQL 297
PTPc-N22_18_12 cd14542
catalytic domain of tyrosine-protein phosphatase non-receptor type 22, type 18 and type 12; ...
 84-284 2.58e-130

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: 385.62  E-value: 2.58e-130
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077601385  84 YINANFIKGVYGPRAYIATQGPLPTTVTDFWRMIWEYEVLIVVMACMEFEMGKKKCERYWAEVGDPSLQCGPFSVTCEAE 163
Cdd:cd14542     1 YINANFIKGVSGSKAYIATQGPLPNTVLDFWRMIWEYNVQVIVMACREFEMGKKKCERYWPEEGEEQLQFGPFKISLEKE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077601385 164 EKKNE-YVIRTLKVTLNEAARTIHQFHYQNWPDHDIPSSIDPILELIGEVRCYQPDDSIPICIHCSAGCGRTGVVCAIDY 242
Cdd:cd14542    81 KRVGPdFLIRTLKVTFQKESRTVYQFHYTAWPDHGVPSSVDPILDLVRLVRDYQGSEDVPICVHCSAGCGRTGTICAIDY 160

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|..
gi 2077601385 243 TWKLLKDGIVPVNFSIFSLIQEMRTQRPSIVQTKEQYKLVYN 284
Cdd:cd14542   161 VWNLLKTGKIPEEFSLFDLVREMRKQRPAMVQTKEQYELVYR 202
PTPc-N18 cd14603
catalytic domain of tyrosine-protein phosphatase non-receptor type 18; Tyrosine-protein ...
 25-290 1.25e-125

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: 376.09  E-value: 1.25e-125
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077601385  25 ADEFLKLKRQSTKYRSDKIYPTATAECPENIKKNRYKDILPYDHSRVELSLITSDTDSHYINANFIKGVYGPRAYIATQG 104
Cdd:cd14603     1 AGEFSEIRACSAAFKADYVCSTVAGGRKENVKKNRYKDILPYDQTRVILSLLQEEGHSDYINANFIKGVDGSRAYIATQG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077601385 105 PLPTTVTDFWRMIWEYEVLIVVMACMEFEMGKKKCERYWAEVGDPsLQCGPFSVTCEAEEKKNEYVI-RTLKVTLNEAAR 183
Cdd:cd14603    81 PLSHTVLDFWRMIWQYGVKVILMACREIEMGKKKCERYWAQEQEP-LQTGPFTITLVKEKRLNEEVIlRTLKVTFQKESR 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077601385 184 TIHQFHYQNWPDHDIPSSIDPILELIGEVRCYQPDDSIPICIHCSAGCGRTGVVCAIDYTWKLLKDGIVPVNFSIFSLIQ 263
Cdd:cd14603   160 SVSHFQYMAWPDHGIPDSPDCMLAMIELARRLQGSGPEPLCVHCSAGCGRTGVICTVDYVRQLLLTQRIPPDFSIFDVVL 239

                         250       260
                  ....*....|....*....|....*..
gi 2077601385 264 EMRTQRPSIVQTKEQYKLVYNAVIELF 290
Cdd:cd14603   240 EMRKQRPAAVQTEEQYEFLYHTVAQMF 266
PTPc smart00194
Protein tyrosine phosphatase, catalytic domain;
24-288 2.17e-113

Protein tyrosine phosphatase, catalytic domain;


Pssm-ID: 214550 [Multi-domain]  Cd Length: 259  Bit Score: 344.26  E-value: 2.17e-113
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077601385   24 FADEFLKLKRQSTKYRSdkiypTATAECPENIKKNRYKDILPYDHSRVELSLITSDtDSHYINANFIKGVYGPRAYIATQ 103
Cdd:smart00194   2 LEEEFEKLDRLKPDDES-----CTVAAFPENRDKNRYKDVLPYDHTRVKLKPPPGE-GSDYINASYIDGPNGPKAYIATQ 75

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077601385  104 GPLPTTVTDFWRMIWEYEVLIVVMACMEFEMGKKKCERYWAEVGDPSLQCGPFSVTCEAEEKKNEYVIRTLKVTL--NEA 181
Cdd:smart00194  76 GPLPSTVEDFWRMVWEQKVTVIVMLTELVEKGREKCAQYWPDEEGEPLTYGDITVTLKSVEKVDDYTIRTLEVTNtgCSE 155

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077601385  182 ARTIHQFHYQNWPDHDIPSSIDPILELIGEVRCYQPDDSIPICIHCSAGCGRTGVVCAIDYTWKLLKDGIvpvNFSIFSL 261
Cdd:smart00194 156 TRTVTHYHYTNWPDHGVPESPESILDLIRAVRKSQSTSTGPIVVHCSAGVGRTGTFIAIDILLQQLEAGK---EVDIFEI 232

                          250       260
                   ....*....|....*....|....*..
gi 2077601385  262 IQEMRTQRPSIVQTKEQYKLVYNAVIE 288
Cdd:smart00194 233 VKELRSQRPGMVQTEEQYIFLYRAILE 259
Y_phosphatase pfam00102
Protein-tyrosine phosphatase;
54-288 1.72e-105

Protein-tyrosine phosphatase;


Pssm-ID: 459674 [Multi-domain]  Cd Length: 234  Bit Score: 322.65  E-value: 1.72e-105
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077601385  54 NIKKNRYKDILPYDHSRVELSliTSDTDSHYINANFIKGVYGPRAYIATQGPLPTTVTDFWRMIWEYEVLIVVMACMEFE 133
Cdd:pfam00102   1 NLEKNRYKDVLPYDHTRVKLT--GDPGPSDYINASYIDGYKKPKKYIATQGPLPNTVEDFWRMVWEEKVTIIVMLTELEE 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077601385 134 MGKKKCERYWAEVGDPSLQCGPFSVTCEAEEKKN-EYVIRTLKVTLN--EAARTIHQFHYQNWPDHDIPSSIDPILELIG 210
Cdd:pfam00102  79 KGREKCAQYWPEEEGESLEYGDFTVTLKKEKEDEkDYTVRTLEVSNGgsEETRTVKHFHYTGWPDHGVPESPNSLLDLLR 158

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2077601385 211 EVRCYQPDDSI-PICIHCSAGCGRTGVVCAIDYTWKLLKDGIVpvnFSIFSLIQEMRTQRPSIVQTKEQYKLVYNAVIE 288
Cdd:pfam00102 159 KVRKSSLDGRSgPIVVHCSAGIGRTGTFIAIDIALQQLEAEGE---VDIFQIVKELRSQRPGMVQTLEQYIFLYDAILE 234
PTPc cd00047
catalytic domain of protein tyrosine phosphatases; Protein tyrosine phosphatases (PTP, EC 3.1. ...
 84-283 2.30e-92

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: 287.26  E-value: 2.30e-92
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077601385  84 YINANFIKGVYGPRAYIATQGPLPTTVTDFWRMIWEYEVLIVVMACMEFEMGKKKCERYWAEVGDPSLQCGPFSVTCEAE 163
Cdd:cd00047     1 YINASYIDGYRGPKEYIATQGPLPNTVEDFWRMVWEQKVSVIVMLTNLVEKGREKCERYWPEEGGKPLEYGDITVTLVSE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077601385 164 EKKNEYVIRTLKVTL--NEAARTIHQFHYQNWPDHDIPSSIDPILELIGEVRCYQPDDSIPICIHCSAGCGRTGVVCAID 241
Cdd:cd00047    81 EELSDYTIRTLELSPkgCSESREVTHLHYTGWPDHGVPSSPEDLLALVRRVRKEARKPNGPIVVHCSAGVGRTGTFIAID 160

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|..
gi 2077601385 242 YTWKLLKDGIVPvnfSIFSLIQEMRTQRPSIVQTKEQYKLVY 283
Cdd:cd00047   161 ILLERLEAEGEV---DVFEIVKALRKQRPGMVQTLEQYEFIY 199
R3-PTPc cd14548
catalytic domain of R3 subfamily receptor-type tyrosine-protein phosphatases and similar ...
 59-279 9.98e-75

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: 241.87  E-value: 9.98e-75
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077601385  59 RYKDILPYDHSRVELSLITSDTDSHYINANFIKGVYGPRAYIATQGPLPTTVTDFWRMIWEYEVLIVVMACMEFEMGKKK 138
Cdd:cd14548     1 RYTNILPYDHSRVKLIPINEEEGSDYINANYIPGYNSPREFIATQGPLPGTKDDFWRMVWEQNSHTIVMLTQCMEKGRVK 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077601385 139 CERYWAEVGDPsLQCGPFSVTCEAEEKKNEYVIRTLKVTLNEAARTIHQFHYQNWPDHDIPSSIDPILELIGEVRCYQPD 218
Cdd:cd14548    81 CDHYWPFDQDP-VYYGDITVTMLSESVLPDWTIREFKLERGDEVRSVRQFHFTAWPDHGVPEAPDSLLRFVRLVRDYIKQ 159

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2077601385 219 DSIPICIHCSAGCGRTGVVCAIDY-TWKLLKDGIVpvnfSIFSLIQEMRTQRPSIVQTKEQY 279
Cdd:cd14548   160 EKGPTIVHCSAGVGRTGTFIALDRlLQQIESEDYV----DIFGIVYDLRKHRPLMVQTEAQY 217
PTPc-N9 cd14543
catalytic domain of tyrosine-protein phosphatase non-receptor type 9; Tyrosine-protein ...
 45-283 1.67e-71

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: 234.95  E-value: 1.67e-71
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077601385  45 PTATAEC---PENIKKNRYKDILPYDHSRVELSLITSDTDSHYINANFIKGVYGPRAYIATQGPLPTTVTDFWRMIWEYE 121
Cdd:cd14543    17 PAGTFLCslaPANQEKNRYGDVLCLDQSRVKLPKRNGDERTDYINANFMDGYKQKNAYIATQGPLPKTYSDFWRMVWEQK 96

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077601385 122 VLIVVMACMEFEMGKKKCERYWAEVGDPSLQCGPFSVTCEAEEKKNEYVIRTLKVTLNEA--ARTIHQFHYQNWPDHDIP 199
Cdd:cd14543    97 VLVIVMTTRVVERGRVKCGQYWPLEEGSSLRYGDLTVTNLSVENKEHYKKTTLEIHNTETdeSRQVTHFQFTSWPDFGVP 176

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077601385 200 SSIDPILELIGEVRCYQpDDSI--------------PICIHCSAGCGRTGVVCAIDYTWKLLKDgIVPVNfsIFSLIQEM 265
Cdd:cd14543   177 SSAAALLDFLGEVRQQQ-ALAVkamgdrwkghppgpPIVVHCSAGIGRTGTFCTLDICLSQLED-VGTLN--VMQTVRRM 252

                         250
                  ....*....|....*...
gi 2077601385 266 RTQRPSIVQTKEQYKLVY 283
Cdd:cd14543   253 RTQRAFSIQTPDQYYFCY 270
PTP_fungal cd18533
fungal protein tyrosine phosphatases; This subfamily contains Saccharomyces cerevisiae ...
 84-283 3.35e-65

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: 3.35e-65
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077601385  84 YINANFIK-GVYGPRAYIATQGPLPTTVTDFWRMIWEYEVLIVVMACMEFEMGKKKCERYWAEVGDPSLQcGPFSVTC-- 160
Cdd:cd18533     1 YINASYITlPGTSSKRYIATQGPLPATIGDFWKMIWQNNVGVIVMLTPLVENGREKCDQYWPSGEYEGEY-GDLTVELvs 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077601385 161 EAEEKKNEYVIRTLKVTL-NEAARTIHQFHYQNWPDHDIPSSIDPILELIGEVR--CYQPDDSIPICIHCSAGCGRTGVV 237
Cdd:cd18533    80 EEENDDGGFIVREFELSKeDGKVKKVYHIQYKSWPDFGVPDSPEDLLTLIKLKRelNDSASLDPPIIVHCSAGVGRTGTF 159

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 2077601385 238 CAIDYTWKLLKDGI---VPVNFS---IFSLIQEMRTQRPSIVQTKEQYKLVY 283
Cdd:cd18533   160 IALDSLLDELKRGLsdsQDLEDSedpVYEIVNQLRKQRMSMVQTLRQYIFLY 211
PTPc-N11_6 cd14544
catalytic domain of tyrosine-protein phosphatase non-receptor type 11 and type 6; ...
 54-286 5.46e-65

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: 216.95  E-value: 5.46e-65
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077601385  54 NIKKNRYKDILPYDHSRVELSLITSDTD-SHYINANFIKGVY-GPRA------YIATQGPLPTTVTDFWRMIWEYEVLIV 125
Cdd:cd14544     1 NKGKNRYKNILPFDHTRVILKDRDPNVPgSDYINANYIRNENeGPTTdenaktYIATQGCLENTVSDFWSMVWQENSRVI 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077601385 126 VMACMEFEMGKKKCERYWAEVGDpSLQCGPFSVTCEAEEKKNEYVIRTLKVT---LNEAARTIHQFHYQNWPDHDIPSSI 202
Cdd:cd14544    81 VMTTKEVERGKNKCVRYWPDEGM-QKQYGPYRVQNVSEHDTTDYTLRELQVSkldQGDPIREIWHYQYLSWPDHGVPSDP 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077601385 203 DPILELIGEVRCYQP--DDSIPICIHCSAGCGRTGVVCAIDYTWKLLKDGIVPVNFSIFSLIQEMRTQRPSIVQTKEQYK 280
Cdd:cd14544   160 GGVLNFLEDVNQRQEslPHAGPIVVHCSAGIGRTGTFIVIDMLLDQIKRKGLDCDIDIQKTIQMVRSQRSGMVQTEAQYK 239


                  ....*.
gi 2077601385 281 LVYNAV 286
Cdd:cd14544   240 FIYVAV 245
R-PTPc-LAR-1 cd14553
catalytic domain of LAR family receptor-type tyrosine-protein phosphatases, repeat 1; The LAR ...
 54-288 5.66e-65

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: 216.11  E-value: 5.66e-65
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077601385  54 NIKKNRYKDILPYDHSRVELSLITSDTDSHYINANFIKGVYGPRAYIATQGPLPTTVTDFWRMIWEYEVLIVVMACMEFE 133
Cdd:cd14553     3 NKPKNRYANVIAYDHSRVILQPIEGVPGSDYINANYCDGYRKQNAYIATQGPLPETFGDFWRMVWEQRSATIVMMTKLEE 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077601385 134 MGKKKCERYWAEVGdpSLQCGPFSVTCEAEEKKNEYVIRTLKVTLNEAA--RTIHQFHYQNWPDHDIPSSIDPILELIGE 211
Cdd:cd14553    83 RSRVKCDQYWPTRG--TETYGLIQVTLLDTVELATYTVRTFALHKNGSSekREVRQFQFTAWPDHGVPEHPTPFLAFLRR 160

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2077601385 212 VRCYQPDDSIPICIHCSAGCGRTGVVCAIDYTWKLLKDGivpVNFSIFSLIQEMRTQRPSIVQTKEQYKLVYNAVIE 288
Cdd:cd14553   161 VKACNPPDAGPIVVHCSAGVGRTGCFIVIDSMLERIKHE---KTVDIYGHVTCLRAQRNYMVQTEDQYIFIHDALLE 234
R-PTPc-T-1 cd14630
catalytic domain of receptor-type tyrosine-protein phosphatase T, repeat 1; Receptor-type ...
 53-288 5.31e-64

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: 213.73  E-value: 5.31e-64
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077601385  53 ENIKKNRYKDILPYDHSRVELSLITSDTDSHYINANFIKGVYGPRAYIATQGPLPTTVTDFWRMIWEYEVLIVVMACMEF 132
Cdd:cd14630     2 ENRNKNRYGNIISYDHSRVRLQLLDGDPHSDYINANYIDGYHRPRHYIATQGPMQETVKDFWRMIWQENSASVVMVTNLV 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077601385 133 EMGKKKCERYWAevgDPSLQCGPFSVTCEAEEKKNEYVIRTLKVTL--NEAARTIHQFHYQNWPDHDIPSSIDPILELIG 210
Cdd:cd14630    82 EVGRVKCVRYWP---DDTEVYGDIKVTLIETEPLAEYVIRTFTVQKkgYHEIREIRQFHFTSWPDHGVPCYATGLLGFVR 158

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2077601385 211 EVRCYQPDDSIPICIHCSAGCGRTGVVCAIDYTWKLLK-DGIVpvnfSIFSLIQEMRTQRPSIVQTKEQYKLVYNAVIE 288
Cdd:cd14630   159 QVKFLNPPDAGPIVVHCSAGAGRTGCFIAIDIMLDMAEnEGVV----DIFNCVRELRAQRVNMVQTEEQYVFVHDAILE 233
R-PTPc-H cd14619
catalytic domain of receptor-type tyrosine-protein phosphatase H; Receptor-type ...
 58-289 2.19e-63

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


Pssm-ID: 350467 [Multi-domain]  Cd Length: 233  Bit Score: 211.67  E-value: 2.19e-63
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077601385  58 NRYKDILPYDHSRVELSLITSDTDSHYINANFIKGVYGPRAYIATQGPLPTTVTDFWRMIWEYEVLIVVMACMEFEMGKK 137
Cdd:cd14619     1 NRFRNVLPYDWSRVPLKPIHEEPGSDYINANYMPGYWSSQEFIATQGPLPQTVGDFWRMIWEQQSSTIVMLTNCMEAGRV 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077601385 138 KCERYWAEVGDPSLQcGPFSVTCEAEEKKNEYVIR--TLKVTLNEAARTIHQFHYQNWPDHDIPSSIDPILELIGEVRCY 215
Cdd:cd14619    81 KCEHYWPLDYTPCTY-GHLRVTVVSEEVMENWTVRefLLKQVEEQKTLSVRHFHFTAWPDHGVPSSTDTLLAFRRLLRQW 159

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2077601385 216 --QPDDSIPICIHCSAGCGRTGVVCAIDYTW-KLLKDGIVpvnfSIFSLIQEMRTQRPSIVQTKEQYKLVYNAVIEL 289
Cdd:cd14619   160 ldQTMSGGPTVVHCSAGVGRTGTLIALDVLLqQLQSEGLL----GPFSFVQKMRENRPLMVQTESQYVFLHQCILDF 232
PTPc-N6 cd14606
catalytic domain of tyrosine-protein phosphatase non-receptor type 6; Tyrosine-protein ...
 52-288 3.88e-62

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: 209.74  E-value: 3.88e-62
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077601385  52 PENIKKNRYKDILPYDHSRVELSLITSDT-DSHYINANFIKG-VYG----PRAYIATQGPLPTTVTDFWRMIWEYEVLIV 125
Cdd:cd14606    16 PENKSKNRYKNILPFDHSRVILQGRDSNIpGSDYINANYVKNqLLGpdenAKTYIASQGCLEATVNDFWQMAWQENSRVI 95

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077601385 126 VMACMEFEMGKKKCERYWAEVGDPSlQCGPFSVTCEAEEKKNEYVIRTLKVTL---NEAARTIHQFHYQNWPDHDIPSSI 202
Cdd:cd14606    96 VMTTREVEKGRNKCVPYWPEVGMQR-AYGPYSVTNCGEHDTTEYKLRTLQVSPldnGELIREIWHYQYLSWPDHGVPSEP 174

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077601385 203 DPILELIGEVRCYQPD--DSIPICIHCSAGCGRTGVVCAIDYTWKLLKDGIVPVNFSIFSLIQEMRTQRPSIVQTKEQYK 280
Cdd:cd14606   175 GGVLSFLDQINQRQESlpHAGPIIVHCSAGIGRTGTIIVIDMLMENISTKGLDCDIDIQKTIQMVRAQRSGMVQTEAQYK 254


                  ....*...
gi 2077601385 281 LVYNAVIE 288
Cdd:cd14606   255 FIYVAIAQ 262
R-PTP-LAR-2 cd14554
PTP-like domain of the LAR family receptor-type tyrosine-protein phosphatases, repeat 2; The ...
 49-285 6.58e-62

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


Pssm-ID: 350402 [Multi-domain]  Cd Length: 238  Bit Score: 208.15  E-value: 6.58e-62
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077601385  49 AECPENIKKNRYKDILPYDHSRVELSLITSDTDSHYINANFIKGVYGPRAYIATQGPLPTTVTDFWRMIWEYEVLIVVMA 128
Cdd:cd14554     1 ANLPCNKFKNRLVNILPYESTRVCLQPIRGVEGSDYINASFIDGYRQRGAYIATQGPLAETTEDFWRMLWEHNSTIIVML 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077601385 129 CMEFEMGKKKCERYWAEvgDPSLQCGPFSVTCEAEEKKNEYVIRTLKVT--LNEAARTIHQFHYQNWPDHDIPSSIDPIL 206
Cdd:cd14554    81 TKLREMGREKCHQYWPA--ERSARYQYFVVDPMAEYNMPQYILREFKVTdaRDGQSRTVRQFQFTDWPEQGVPKSGEGFI 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077601385 207 ELIGEV-RCY-QPDDSIPICIHCSAGCGRTGVVCAIDYTWKLLK-DGIVpvnfSIFSLIQEMRTQRPSIVQTKEQYKLVY 283
Cdd:cd14554   159 DFIGQVhKTKeQFGQEGPITVHCSAGVGRTGVFITLSIVLERMRyEGVV----DVFQTVKLLRTQRPAMVQTEDQYQFCY 234


                  ..
gi 2077601385 284 NA 285
Cdd:cd14554   235 RA 236
PTPc-KIM cd14547
catalytic domain of the kinase interaction motif (KIM) family of protein-tyrosine phosphatases; ...
 58-283 4.15e-61

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


Pssm-ID: 350395 [Multi-domain]  Cd Length: 224  Bit Score: 205.32  E-value: 4.15e-61
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077601385  58 NRYKDILPYDHSRVELSLITSDTDSHYINANFIKGVYG-PRAYIATQGPLPTTVTDFWRMIWEYEVLIVVMACMEFEMgK 136
Cdd:cd14547     1 NRYKTILPNEHSRVCLPSVDDDPLSSYINANYIRGYDGeEKAYIATQGPLPNTVADFWRMVWQEKTPIIVMITNLTEA-K 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077601385 137 KKCERYWAEVGDpsLQCGPFSVTCEAEEKKNEYVIRTLKVTLNEAARTIHQFHYQNWPDHDIPSSIDPILELIGEVRCY- 215
Cdd:cd14547    80 EKCAQYWPEEEN--ETYGDFEVTVQSVKETDGYTVRKLTLKYGGEKRYLKHYWYTSWPDHKTPEAAQPLLSLVQEVEEAr 157

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077601385 216 -QPDDSIPICIHCSAGCGRTGVVCAIDY-TWKLLKDGIVPVnfsiFSLIQEMRTQRPSIVQTKEQYKLVY 283
Cdd:cd14547   158 qTEPHRGPIVVHCSAGIGRTGCFIATSIgCQQLREEGVVDV----LGIVCQLRLDRGGMVQTAEQYEFVH 223
R5-PTPc-1 cd14549
catalytic domain of R5 subfamily receptor-type tyrosine-protein phosphatases, repeat 1; The R5 ...
 84-279 1.78e-60

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: 202.97  E-value: 1.78e-60
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077601385  84 YINANFIKGVYGPRAYIATQGPLPTTVTDFWRMIWEYEVLIVVMACMEFEMGKKKCERYWAEVGdpSLQCGPFSVTCEAE 163
Cdd:cd14549     1 YINANYVDGYNKARAYIATQGPLPSTFDDFWRMVWEQNSAIIVMITNLVERGRRKCDQYWPKEG--TETYGNIQVTLLST 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077601385 164 EKKNEYVIRTL--------KVTLNEAARTIHQFHYQNWPDHDIPSSIDPILELIGEVRCYQPDDSIPICIHCSAGCGRTG 235
Cdd:cd14549    79 EVLATYTVRTFslknlklkKVKGRSSERVVYQYHYTQWPDHGVPDYTLPVLSFVRKSSAANPPGAGPIVVHCSAGVGRTG 158

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*
gi 2077601385 236 VVCAIDYTWKLLKD-GIVpvnfSIFSLIQEMRTQRPSIVQTKEQY 279
Cdd:cd14549   159 TYIVIDSMLQQIQDkGTV----NVFGFLKHIRTQRNYLVQTEEQY 199
R-PTPc-O cd14614
catalytic domain of receptor-type tyrosine-protein phosphatase O; Receptor-type ...
 45-286 4.52e-58

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: 197.80  E-value: 4.52e-58
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077601385  45 PTATAECPENIKKNRYKDILPYDHSRVELSLITSDTDSHYINANFIKGVYGPRAYIATQGPLPTTVTDFWRMIWEYEVLI 124
Cdd:cd14614     3 PHFAADLPVNRCKNRYTNILPYDFSRVKLVSMHEEEGSDYINANYIPGYNSPQEYIATQGPLPETRNDFWKMVLQQKSQI 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077601385 125 VVMACMEFEMGKKKCERYWAEVGDPsLQCGPFSVTCEAEEKKNEYVIRTLKVTLNEAARTIHQFHYQNWPDHDIPS--SI 202
Cdd:cd14614    83 IVMLTQCNEKRRVKCDHYWPFTEEP-VAYGDITVEMLSEEEQPDWAIREFRVSYADEVQDVMHFNYTAWPDHGVPTanAA 161

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077601385 203 DPILELIGEVRCYQPDDSIPICIHCSAGCGRTGVVCAIDYTWKLLKDGIVpvnFSIFSLIQEMRTQRPSIVQTKEQYKLV 282
Cdd:cd14614   162 ESILQFVQMVRQQAVKSKGPMIIHCSAGVGRTGTFIALDRLLQHIRDHEF---VDILGLVSEMRSYRMSMVQTEEQYIFI 238


                  ....
gi 2077601385 283 YNAV 286
Cdd:cd14614   239 HQCV 242
R-PTPc-J cd14615
catalytic domain of receptor-type tyrosine-protein phosphatase J; Receptor-type ...
 58-279 6.04e-58

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


Pssm-ID: 350463 [Multi-domain]  Cd Length: 229  Bit Score: 196.96  E-value: 6.04e-58
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077601385  58 NRYKDILPYDHSRVELSLITSDTDShYINANFIKGVYGPRAYIATQGPLPTTVTDFWRMIWEYEVLIVVMACMEFEMGKK 137
Cdd:cd14615     1 NRYNNVLPYDISRVKLSVQSHSTDD-YINANYMPGYNSKKEFIAAQGPLPNTVKDFWRMVWEKNVYAIVMLTKCVEQGRT 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077601385 138 KCERYWAEvgDPSLQCGPFSVTCEAEEKKNEYVIRTLKVTLNEAA--RTIHQFHYQNWPDHDIPSSIDPILELIGEVRCY 215
Cdd:cd14615    80 KCEEYWPS--KQKKDYGDITVTMTSEIVLPEWTIRDFTVKNAQTNesRTVRHFHFTSWPDHGVPETTDLLINFRHLVREY 157

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2077601385 216 ---QPDDSiPICIHCSAGCGRTGVVCAIDY-TWKLLKDGIVpvnfSIFSLIQEMRTQRPSIVQTKEQY 279
Cdd:cd14615   158 mkqNPPNS-PILVHCSAGVGRTGTFIAIDRlIYQIENENVV----DVYGIVYDLRMHRPLMVQTEDQY 220
PTPc-N20_13 cd14538
catalytic domain of tyrosine-protein phosphatase non-receptor type 20 and type 13; ...
 84-288 4.84e-57

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: 193.74  E-value: 4.84e-57
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077601385  84 YINANFIKGVYG--PRAYIATQGPLPTTVTDFWRMIWEYEVLIVVMACMEFEMGKKKCERYWAE-VGDPSLQCGPFSVTC 160
Cdd:cd14538     1 YINASHIRIPVGgdTYHYIACQGPLPNTTGDFWQMVWEQKSEVIAMVTQDVEGGKVKCHRYWPDsLNKPLICGGRLEVSL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077601385 161 EAEEKKNEYVIRTLKVTLNEAARTIHQFH--YQNWPDHDIPSSIDPILELIGEVRCYQpdDSIPICIHCSAGCGRTGVVC 238
Cdd:cd14538    81 EKYQSLQDFVIRRISLRDKETGEVHHITHlnFTTWPDHGTPQSADPLLRFIRYMRRIH--NSGPIVVHCSAGIGRTGVLI 158

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|
gi 2077601385 239 AIDYTWKLLKDGIvpvNFSIFSLIQEMRTQRPSIVQTKEQYKLVYNAVIE 288
Cdd:cd14538   159 TIDVALGLIERDL---PFDIQDIVKDLREQRQGMIQTKDQYIFCYKACLE 205
PTPc-N13 cd14597
catalytic domain of tyrosine-protein phosphatase non-receptor type 13; Tyrosine-protein ...
 53-287 1.42e-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: 193.51  E-value: 1.42e-56
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077601385  53 ENIKKNRYKDILPYDHSRVELSlitsdTDSHYINANFIKGVYGPR--AYIATQGPLPTTVTDFWRMIWEYEVLIVVMACM 130
Cdd:cd14597     2 ENRKKNRYKNILPYDTTRVPLG-----DEGGYINASFIKMPVGDEefVYIACQGPLPTTVADFWQMVWEQKSTVIAMMTQ 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077601385 131 EFEMGKKKCERYWAEV-GDPSLQCGPFSVTCEAEEKKNEYVIRTLK---VTLNEaARTIHQFHYQNWPDHDIPSSIDPIL 206
Cdd:cd14597    77 EVEGGKIKCQRYWPEIlGKTTMVDNRLQLTLVRMQQLKNFVIRVLEledIQTRE-VRHITHLNFTAWPDHDTPSQPEQLL 155

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077601385 207 ELIGEVRcyQPDDSIPICIHCSAGCGRTGVVCAIDYTWKLL-KDgivpVNFSIFSLIQEMRTQRPSIVQTKEQYKLVYNA 285
Cdd:cd14597   156 TFISYMR--HIHKSGPIITHCSAGIGRSGTLICIDVVLGLIsKD----LDFDISDIVRTMRLQRHGMVQTEDQYIFCYQV 229


                  ..
gi 2077601385 286 VI 287
Cdd:cd14597   230 IL 231
R-PTPc-M-1 cd14633
catalytic domain of receptor-type tyrosine-protein phosphatase M, repeat 1; Receptor-type ...
 45-288 6.87e-56

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: 192.95  E-value: 6.87e-56
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077601385  45 PTATAECPENIKKNRYKDILPYDHSRVELSLITSDTDSHYINANFIKGVYGPRAYIATQGPLPTTVTDFWRMIWEYEVLI 124
Cdd:cd14633    31 PWDSAKKDENRMKNRYGNIIAYDHSRVRLQPIEGETSSDYINGNYIDGYHRPNHYIATQGPMQETIYDFWRMVWHENTAS 110

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077601385 125 VVMACMEFEMGKKKCERYWAevgDPSLQCGPFSVTCEAEEKKNEYVIRTLKVTLNEA--ARTIHQFHYQNWPDHDIPSSI 202
Cdd:cd14633   111 IIMVTNLVEVGRVKCCKYWP---DDTEIYKDIKVTLIETELLAEYVIRTFAVEKRGVheIREIRQFHFTGWPDHGVPYHA 187

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077601385 203 DPILELIGEVRCYQPDDSIPICIHCSAGCGRTGVVCAIDYTWKLL-KDGIVpvnfSIFSLIQEMRTQRPSIVQTKEQYKL 281
Cdd:cd14633   188 TGLLGFVRQVKSKSPPNAGPLVVHCSAGAGRTGCFIVIDIMLDMAeREGVV----DIYNCVRELRSRRVNMVQTEEQYVF 263


                  ....*..
gi 2077601385 282 VYNAVIE 288
Cdd:cd14633   264 IHDAILE 270
R-PTP-N cd14609
PTP-like domain of receptor-type tyrosine-protein phosphatase N; Receptor-type ...
 47-288 1.06e-55

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


Pssm-ID: 350457 [Multi-domain]  Cd Length: 281  Bit Score: 192.56  E-value: 1.06e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077601385  47 ATAECPENIKKNRYKDILPYDHSRVELSLITSDTDSHYINANFIKGvYGPR--AYIATQGPLPTTVTDFWRMIWEYEVLI 124
Cdd:cd14609    35 STAQGEANVKKNRNPDFVPYDHARIKLKAESNPSRSDYINASPIIE-HDPRmpAYIATQGPLSHTIADFWQMVWENGCTV 113

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077601385 125 VVMACMEFEMGKKKCERYWAEVGDPSLQCgpFSVTCEAEEKKNE-YVIRT--LKVTLNEAARTIHQFHYQNWPDHDIPSS 201
Cdd:cd14609   114 IVMLTPLVEDGVKQCDRYWPDEGSSLYHI--YEVNLVSEHIWCEdFLVRSfyLKNVQTQETRTLTQFHFLSWPAEGIPSS 191

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077601385 202 IDPILELIGEV-RCYQpDDSIPICIHCSAGCGRTGVVCAIDYTWKLLKDGIVPVNfsIFSLIQEMRTQRPSIVQTKEQYK 280
Cdd:cd14609   192 TRPLLDFRRKVnKCYR-GRSCPIIVHCSDGAGRTGTYILIDMVLNRMAKGVKEID--IAATLEHVRDQRPGMVRTKDQFE 268


                  ....*...
gi 2077601385 281 LVYNAVIE 288
Cdd:cd14609   269 FALTAVAE 276
PTPc-N11 cd14605
catalytic domain of tyrosine-protein phosphatase non-receptor type 11; Tyrosine-protein ...
 53-286 3.26e-55

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: 190.23  E-value: 3.26e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077601385  53 ENIKKNRYKDILPYDHSRVELSlitsDTD-----SHYINANFIKGVYG--------PRAYIATQGPLPTTVTDFWRMIWE 119
Cdd:cd14605     1 ENKNKNRYKNILPFDHTRVVLH----DGDpnepvSDYINANIIMPEFEtkcnnskpKKSYIATQGCLQNTVNDFWRMVFQ 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077601385 120 YEVLIVVMACMEFEMGKKKCERYWAEVGdpSL-QCGPFSVTCEAEEKKNEYVIRTLK---VTLNEAARTIHQFHYQNWPD 195
Cdd:cd14605    77 ENSRVIVMTTKEVERGKSKCVKYWPDEY--ALkEYGVMRVRNVKESAAHDYILRELKlskVGQGNTERTVWQYHFRTWPD 154

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077601385 196 HDIPSSIDPILELIGEVRCYQPD--DSIPICIHCSAGCGRTGVVCAIDYTWKLLKDGIVPVNFSIFSLIQEMRTQRPSIV 273
Cdd:cd14605   155 HGVPSDPGGVLDFLEEVHHKQESimDAGPVVVHCSAGIGRTGTFIVIDILIDIIREKGVDCDIDVPKTIQMVRSQRSGMV 234

                         250
                  ....*....|...
gi 2077601385 274 QTKEQYKLVYNAV 286
Cdd:cd14605   235 QTEAQYRFIYMAV 247
R-PTPc-G-1 cd17667
catalytic domain of receptor-type tyrosine-protein phosphatase G, repeat 1; Receptor-type ...
 24-288 4.53e-55

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: 190.63  E-value: 4.53e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077601385  24 FADEFLKLKRQStkyrSDKIYPTATAECPENIKKNRYKDILPYDHSRVELSLITSDTDSH--YINANFIKGVYGPRAYIA 101
Cdd:cd17667     1 FSEDFEEVQRCT----ADMNITAEHSNHPDNKHKNRYINILAYDHSRVKLRPLPGKDSKHsdYINANYVDGYNKAKAYIA 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077601385 102 TQGPLPTTVTDFWRMIWEYEVLIVVMACMEFEMGKKKCERYWAEvgDPSLQCGPFSVTCEAEEKKNEYVIRTLKVTLN-- 179
Cdd:cd17667    77 TQGPLKSTFEDFWRMIWEQNTGIIVMITNLVEKGRRKCDQYWPT--ENSEEYGNIIVTLKSTKIHACYTVRRFSIRNTkv 154

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077601385 180 -----------EAARTIHQFHYQNWPDHDIPSSIDPILELIGEVRCYQPDDSIPICIHCSAGCGRTGVVCAIDYTWKLLK 248
Cdd:cd17667   155 kkgqkgnpkgrQNERTVIQYHYTQWPDMGVPEYALPVLTFVRRSSAARTPEMGPVLVHCSAGVGRTGTYIVIDSMLQQIK 234

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|
gi 2077601385 249 DGIVpVNfsIFSLIQEMRTQRPSIVQTKEQYKLVYNAVIE 288
Cdd:cd17667   235 DKST-VN--VLGFLKHIRTQRNYLVQTEEQYIFIHDALLE 271
R-PTPc-F-1 cd14626
catalytic domain of receptor-type tyrosine-protein phosphatase F, repeat 1; Receptor-type ...
 54-288 5.43e-55

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: 190.63  E-value: 5.43e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077601385  54 NIKKNRYKDILPYDHSRVELSLITSDTDSHYINANFIKGVYGPRAYIATQGPLPTTVTDFWRMIWEYEVLIVVMACMEFE 133
Cdd:cd14626    41 NKPKNRYANVIAYDHSRVILTSVDGVPGSDYINANYIDGYRKQNAYIATQGPLPETLSDFWRMVWEQRTATIVMMTRLEE 120

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077601385 134 MGKKKCERYWAEVGDPSlqCGPFSVTCEAEEKKNEYVIRTLKVTLNEAA--RTIHQFHYQNWPDHDIPSSIDPILELIGE 211
Cdd:cd14626   121 KSRVKCDQYWPIRGTET--YGMIQVTLLDTVELATYSVRTFALYKNGSSekREVRQFQFMAWPDHGVPEYPTPILAFLRR 198

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2077601385 212 VRCYQPDDSIPICIHCSAGCGRTGVVCAIDYTWKLLKdgiVPVNFSIFSLIQEMRTQRPSIVQTKEQYKLVYNAVIE 288
Cdd:cd14626   199 VKACNPPDAGPMVVHCSAGVGRTGCFIVIDAMLERMK---HEKTVDIYGHVTCMRSQRNYMVQTEDQYIFIHEALLE 272
PTPc-N3 cd14600
catalytic domain of tyrosine-protein phosphatase non-receptor type 3; Tyrosine-protein ...
 38-291 8.29e-55

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: 190.06  E-value: 8.29e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077601385  38 YRSDKIYPTATAECPENIKKNRYKDILPYDHSRVELslitsDTDSHYINANFIK----GVYGPRAYIATQGPLPTTVTDF 113
Cdd:cd14600    24 YRKKPGLAITCAKLPQNMDKNRYKDVLPYDATRVVL-----QGNEDYINASYVNmeipSANIVNKYIATQGPLPHTCAQF 98

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077601385 114 WRMIWEYEVLIVVMACMEFEMGKKKCERYWAEVGDpSLQCGPFSVTCEAEEKKNEYVIRTLKVTLNEAA--RTIHQFHYQ 191
Cdd:cd14600    99 WQVVWEQKLSLIVMLTTLTERGRTKCHQYWPDPPD-VMEYGGFRVQCHSEDCTIAYVFREMLLTNTQTGeeRTVTHLQYV 177

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077601385 192 NWPDHDIPSSIDPILELIGEVRCYQPdDSIPICIHCSAGCGRTGVVCAIDYTWKLLKDgivpvNFSIFSL--IQEMRTQR 269
Cdd:cd14600   178 AWPDHGVPDDSSDFLEFVNYVRSKRV-ENEPVLVHCSAGIGRTGVLVTMETAMCLTER-----NQPVYPLdiVRKMRDQR 251

                         250       260
                  ....*....|....*....|..
gi 2077601385 270 PSIVQTKEQYKLVYNAVIELFK 291
Cdd:cd14600   252 AMMVQTSSQYKFVCEAILRVYE 273
R-PTPc-Q cd14616
catalytic domain of receptor-type tyrosine-protein phosphatase Q; Receptor-type ...
 58-279 1.08e-54

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: 187.81  E-value: 1.08e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077601385  58 NRYKDILPYDHSRVELSLITSDTDSHYINANFIKGVYGPRAYIATQGPLPTTVTDFWRMIWEYEVLIVVMACMEFEMGKK 137
Cdd:cd14616     1 NRFPNIKPYNNNRVKLIADAGVPGSDYINASYISGYLCPNEFIATQGPLPGTVGDFWRMVWETRAKTIVMLTQCFEKGRI 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077601385 138 KCERYWAEVGDPSLQCGPFSVTCEAEEKKNEYVIRTLKVTLNEAARTIHQFHYQNWPDHDIPSSIDPILELIGEVRCYQP 217
Cdd:cd14616    81 RCHQYWPEDNKPVTVFGDIVITKLMEDVQIDWTIRDLKIERHGDYMMVRQCNFTSWPEHGVPESSAPLIHFVKLVRASRA 160

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2077601385 218 DDSIPICIHCSAGCGRTGVVCAIDYTWKLLKDGivpvNF-SIFSLIQEMRTQRPSIVQTKEQY 279
Cdd:cd14616   161 HDNTPMIVHCSAGVGRTGVFIALDHLTQHINDH----DFvDIYGLVAELRSERMCMVQNLAQY 219
R-PTP-D-2 cd14628
PTP-like domain of receptor-type tyrosine-protein phosphatase D, repeat 2; Receptor-type ...
 5-288 1.81e-54

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: 189.94  E-value: 1.81e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077601385   5 EILLQNLeRAQSKKLNQEAFADEFLKLKRQSTKYRSDKIYPT--ATAECPENIKKNRYKDILPYDHSRVELSLITSDTDS 82
Cdd:cd14628     2 EVPARNL-YAYIQKLTQIETGENVTGMELEFKRLASSKAHTSrfISANLPCNKFKNRLVNIMPYESTRVCLQPIRGVEGS 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077601385  83 HYINANFIKGVYGPRAYIATQGPLPTTVTDFWRMIWEYEVLIVVMACMEFEMGKKKCERYWAevGDPSLQCGPFSVTCEA 162
Cdd:cd14628    81 DYINASFIDGYRQQKAYIATQGPLAETTEDFWRMLWEHNSTIVVMLTKLREMGREKCHQYWP--AERSARYQYFVVDPMA 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077601385 163 EEKKNEYVIRTLKVT--LNEAARTIHQFHYQNWPDHDIPSSIDPILELIGEVRCY--QPDDSIPICIHCSAGCGRTGVVC 238
Cdd:cd14628   159 EYNMPQYILREFKVTdaRDGQSRTVRQFQFTDWPEQGVPKSGEGFIDFIGQVHKTkeQFGQDGPISVHCSAGVGRTGVFI 238

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|.
gi 2077601385 239 AIDYTWKLLK-DGIVpvnfSIFSLIQEMRTQRPSIVQTKEQYKLVYNAVIE 288
Cdd:cd14628   239 TLSIVLERMRyEGVV----DIFQTVKMLRTQRPAMVQTEDQYQFCYRAALE 285
R-PTPc-B cd14617
catalytic domain of receptor-type tyrosine-protein phosphatase B; Receptor-type ...
 58-283 4.34e-54

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: 186.28  E-value: 4.34e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077601385  58 NRYKDILPYDHSRVELSLITSDTDSHYINANFIKGVYGPRAYIATQGPLPTTVTDFWRMIWEYEVLIVVMACMEFEMGKK 137
Cdd:cd14617     1 NRYNNILPYDSTRVKLSNVDDDPCSDYINASYIPGNNFRREYIATQGPLPGTKDDFWKMVWEQNVHNIVMVTQCVEKGRV 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077601385 138 KCERYWAEVGDPsLQCGPFSVTCEAEEKKNEYVIRTLKVTLNE---AARTIHQFHYQNWPDHDIPSSIDPILELIGEVRC 214
Cdd:cd14617    81 KCDHYWPADQDS-LYYGDLIVQMLSESVLPEWTIREFKICSEEqldAPRLVRHFHYTVWPDHGVPETTQSLIQFVRTVRD 159

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2077601385 215 Y--QPDDSIPICIHCSAGCGRTGVVCAIDYTWKLL--KDGIvpvnfSIFSLIQEMRTQRPSIVQTKEQYKLVY 283
Cdd:cd14617   160 YinRTPGSGPTVVHCSAGVGRTGTFIALDRILQQLdsKDSV-----DIYGAVHDLRLHRVHMVQTECQYVYLH 227
PTPc-N3_4 cd14541
catalytic domain of tyrosine-protein phosphatase non-receptor type 21 and type 14; ...
 84-291 1.64e-53

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: 184.07  E-value: 1.64e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077601385  84 YINANF----IKGVYGPRAYIATQGPLPTTVTDFWRMIWEYEVLIVVMACMEFEMGKKKCERYWAEVGDpSLQCGPFSVT 159
Cdd:cd14541     2 YINANYvnmeIPGSGIVNRYIAAQGPLPNTCADFWQMVWEQKSTLIVMLTTLVERGRVKCHQYWPDLGE-TMQFGNLQIT 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077601385 160 CEAEEKKNEYVIRTLKVTLNEAA--RTIHQFHYQNWPDHDIPSSIDPILELIGEVRCYQPDDSIPICIHCSAGCGRTGVV 237
Cdd:cd14541    81 CVSEEVTPSFAFREFILTNTNTGeeRHITQMQYLAWPDHGVPDDSSDFLDFVKRVRQNRVGMVEPTVVHCSAGIGRTGVL 160

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....
gi 2077601385 238 CAIDyTWKLLKDGIVPVNfsIFSLIQEMRTQRPSIVQTKEQYKLVYNAVIELFK 291
Cdd:cd14541   161 ITME-TAMCLIEANEPVY--PLDIVRTMRDQRAMLIQTPSQYRFVCEAILRVYE 211
PTPc-N7 cd14612
catalytic domain of tyrosine-protein phosphatase non-receptor type 7; Tyrosine-protein ...
 50-283 1.95e-53

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


Pssm-ID: 350460 [Multi-domain]  Cd Length: 247  Bit Score: 185.42  E-value: 1.95e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077601385  50 ECPENIKKNRYKDILPYDHSRVEL-SLITSDTDSHYINANFIKGVYG-PRAYIATQGPLPTTVTDFWRMIWEYEVLIVVM 127
Cdd:cd14612    11 DIPGHASKDRYKTILPNPQSRVCLrRAGSQEEEGSYINANYIRGYDGkEKAYIATQGPMLNTVSDFWEMVWQEECPIIVM 90

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077601385 128 aCMEFEMGKKKCERYWAEvgdPSLQCGPFSVTCEAEEKKNEYVIRTLKVTLNEAARTIHQFHYQNWPDHDIPSSIDPILE 207
Cdd:cd14612    91 -ITKLKEKKEKCVHYWPE---KEGTYGRFEIRVQDMKECDGYTIRDLTIQLEEESRSVKHYWFSSWPDHQTPESAGPLLR 166

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077601385 208 LIGEV---RCYQPDDSiPICIHCSAGCGRTGVVCAIDYTWKLLKD-GIVpvnfSIFSLIQEMRTQRPSIVQTKEQYKLVY 283
Cdd:cd14612   167 LVAEVeesRQTAASPG-PIVVHCSAGIGRTGCFIATSIGCQQLKDtGKV----DILGIVCQLRLDRGGMIQTSEQYQFLH 241
R-PTPc-A-E-2 cd14552
catalytic domain of receptor-type tyrosine-protein phosphatase A and E, repeat 2; ...
 84-286 4.06e-53

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: 182.85  E-value: 4.06e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077601385  84 YINANFIKGVYGPRAYIATQGPLPTTVTDFWRMIWEYEVLIVVMACMEFEMGKKKCERYWAEvgDPSLQCGPFSVTCEAE 163
Cdd:cd14552     1 YINASFIDGYRQKDAYIATQGPLDHTVEDFWRMIWEWKSCSIVMLTEIKERSQNKCAQYWPE--DGSVSSGDITVELKDQ 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077601385 164 EKKNEYVIRTLKVTLN--EAARTIHQFHYQNWPDHDIPSSIDPILELIGEV-RCYQPDDSIPICIHCSAGCGRTGVVCAI 240
Cdd:cd14552    79 TDYEDYTLRDFLVTKGkgGSTRTVRQFHFHGWPEVGIPDNGKGMIDLIAAVqKQQQQSGNHPITVHCSAGAGRTGTFCAL 158

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*..
gi 2077601385 241 DYTWKLLK-DGIVPVnfsiFSLIQEMRTQRPSIVQTKEQYKLVYNAV 286
Cdd:cd14552   159 STVLERVKaEGVLDV----FQVVKSLRLQRPHMVQTLEQYEFCYKVV 201
R-PTP-S-2 cd14627
PTP-like domain of receptor-type tyrosine-protein phosphatase S, repeat 2; Receptor-type ...
 48-288 5.41e-53

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: 185.71  E-value: 5.41e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077601385  48 TAECPENIKKNRYKDILPYDHSRVELSLITSDTDSHYINANFIKGVYGPRAYIATQGPLPTTVTDFWRMIWEYEVLIVVM 127
Cdd:cd14627    47 SANLPCNKFKNRLVNIMPYETTRVCLQPIRGVEGSDYINASFIDGYRQQKAYIATQGPLAETTEDFWRMLWENNSTIVVM 126

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077601385 128 ACMEFEMGKKKCERYWAevGDPSLQCGPFSVTCEAEEKKNEYVIRTLKVT--LNEAARTIHQFHYQNWPDHDIPSSIDPI 205
Cdd:cd14627   127 LTKLREMGREKCHQYWP--AERSARYQYFVVDPMAEYNMPQYILREFKVTdaRDGQSRTVRQFQFTDWPEQGVPKSGEGF 204

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077601385 206 LELIGEVRCY--QPDDSIPICIHCSAGCGRTGVVCAIDYTWKLLK-DGIVpvnfSIFSLIQEMRTQRPSIVQTKEQYKLV 282
Cdd:cd14627   205 IDFIGQVHKTkeQFGQDGPISVHCSAGVGRTGVFITLSIVLERMRyEGVV----DIFQTVKMLRTQRPAMVQTEDEYQFC 280


                  ....*.
gi 2077601385 283 YNAVIE 288
Cdd:cd14627   281 YQAALE 286
PTPc-N1_2 cd14545
catalytic domain of tyrosine-protein phosphatase non-receptor type 1 and type 2; ...
 57-283 1.18e-52

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: 182.59  E-value: 1.18e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077601385  57 KNRYKDILPYDHSRVELSLITSDTDshYINANFIKGVYGPRAYIATQGPLPTTVTDFWRMIWEYEVLIVVMACMEFEMGK 136
Cdd:cd14545     1 LNRYRDRDPYDHDRSRVKLKQGDND--YINASLVEVEEAKRSYILTQGPLPNTSGHFWQMVWEQNSKAVIMLNKLMEKGQ 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077601385 137 KKCERYWAEVGDPSLQC--GPFSVTCEAEEKKNEYVIRTLKVT--LNEAARTIHQFHYQNWPDHDIPSSIDPILELIGEV 212
Cdd:cd14545    79 IKCAQYWPQGEGNAMIFedTGLKVTLLSEEDKSYYTVRTLELEnlKTQETREVLHFHYTTWPDFGVPESPAAFLNFLQKV 158

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2077601385 213 R---CYQPDDSiPICIHCSAGCGRTGVVCAIDyTWKLLKDGIVPVNFSIFSLIQEMRTQRPSIVQTKEQYKLVY 283
Cdd:cd14545   159 ResgSLSSDVG-PPVVHCSAGIGRSGTFCLVD-TCLVLIEKGNPSSVDVKKVLLEMRKYRMGLIQTPDQLRFSY 230
R-PTP-F-2 cd14629
PTP-like domain of receptor-type tyrosine-protein phosphatase F, repeat 2; Receptor-type ...
 48-288 2.38e-52

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: 183.77  E-value: 2.38e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077601385  48 TAECPENIKKNRYKDILPYDHSRVELSLITSDTDSHYINANFIKGVYGPRAYIATQGPLPTTVTDFWRMIWEYEVLIVVM 127
Cdd:cd14629    47 SANLPCNKFKNRLVNIMPYELTRVCLQPIRGVEGSDYINASFIDGYRQQKAYIATQGPLAETTEDFWRMLWEHNSTIVVM 126

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077601385 128 ACMEFEMGKKKCERYWAevGDPSLQCGPFSVTCEAEEKKNEYVIRTLKVT--LNEAARTIHQFHYQNWPDHDIPSSIDPI 205
Cdd:cd14629   127 LTKLREMGREKCHQYWP--AERSARYQYFVVDPMAEYNMPQYILREFKVTdaRDGQSRTIRQFQFTDWPEQGVPKTGEGF 204

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077601385 206 LELIGEVRCY--QPDDSIPICIHCSAGCGRTGVVCAIDYTWKLLK-DGIVpvnfSIFSLIQEMRTQRPSIVQTKEQYKLV 282
Cdd:cd14629   205 IDFIGQVHKTkeQFGQDGPITVHCSAGVGRTGVFITLSIVLERMRyEGVV----DMFQTVKTLRTQRPAMVQTEDQYQLC 280


                  ....*.
gi 2077601385 283 YNAVIE 288
Cdd:cd14629   281 YRAALE 286
R-PTPc-typeIIb-1 cd14555
catalytic domain of type IIb (or R2B) subfamily receptor-type tyrosine-protein phosphatases, ...
 84-288 2.74e-52

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: 180.50  E-value: 2.74e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077601385  84 YINANFIKGVYGPRAYIATQGPLPTTVTDFWRMIWEYEVLIVVMACMEFEMGKKKCERYWAevgDPSLQCGPFSVTCEAE 163
Cdd:cd14555     1 YINANYIDGYHRPNHYIATQGPMQETVYDFWRMVWQENSASIVMVTNLVEVGRVKCSRYWP---DDTEVYGDIKVTLVET 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077601385 164 EKKNEYVIRTLKVTLN--EAARTIHQFHYQNWPDHDIPSSIDPILELIGEVRCYQPDDSIPICIHCSAGCGRTGVVCAID 241
Cdd:cd14555    78 EPLAEYVVRTFALERRgyHEIREVRQFHFTGWPDHGVPYHATGLLGFIRRVKASNPPSAGPIVVHCSAGAGRTGCYIVID 157

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*...
gi 2077601385 242 YTWKLL-KDGIVpvnfSIFSLIQEMRTQRPSIVQTKEQYKLVYNAVIE 288
Cdd:cd14555   158 IMLDMAeREGVV----DIYNCVKELRSRRVNMVQTEEQYIFIHDAILE 201
R-PTP-N-N2 cd14546
PTP-like domain of receptor-type tyrosine-protein phosphatase-like N and N2; Receptor-type ...
 84-288 3.41e-52

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: 180.33  E-value: 3.41e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077601385  84 YINANFIKGvYGPR--AYIATQGPLPTTVTDFWRMIWEYEVLIVVMACMEFEMGKKKCERYWAEVGdpSLQCGPFSVTCE 161
Cdd:cd14546     1 YINASTIYD-HDPRnpAYIATQGPLPHTIADFWQMIWEQGCVVIVMLTRLQENGVKQCARYWPEEG--SEVYHIYEVHLV 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077601385 162 AEEKKNE-YVIRT--LKVTLNEAARTIHQFHYQNWPDHDIPSSIDPILELIGEV-RCYQpDDSIPICIHCSAGCGRTGVV 237
Cdd:cd14546    78 SEHIWCDdYLVRSfyLKNLQTSETRTVTQFHFLSWPDEGIPASAKPLLEFRRKVnKSYR-GRSCPIVVHCSDGAGRTGTY 156

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|.
gi 2077601385 238 CAIDYTWKLLKDGIVPVNfsIFSLIQEMRTQRPSIVQTKEQYKLVYNAVIE 288
Cdd:cd14546   157 ILIDMVLNRMAKGAKEID--IAATLEHLRDQRPGMVKTKDQFEFVLTAVAE 205
PTPc-N1 cd14608
catalytic domain of tyrosine-protein phosphatase non-receptor type 1; Tyrosine-protein ...
 44-288 6.98e-52

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


Pssm-ID: 350456 [Multi-domain]  Cd Length: 277  Bit Score: 182.15  E-value: 6.98e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077601385  44 YPTATAECPENIKKNRYKDILPYDHSRVELSLitsdTDSHYINANFIKGVYGPRAYIATQGPLPTTVTDFWRMIWEYEVL 123
Cdd:cd14608    15 FPCRVAKLPKNKNRNRYRDVSPFDHSRIKLHQ----EDNDYINASLIKMEEAQRSYILTQGPLPNTCGHFWEMVWEQKSR 90

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077601385 124 IVVMACMEFEMGKKKCERYWAEVGDPSL--QCGPFSVTCEAEEKKNEYVIRTLKVT--LNEAARTIHQFHYQNWPDHDIP 199
Cdd:cd14608    91 GVVMLNRVMEKGSLKCAQYWPQKEEKEMifEDTNLKLTLISEDIKSYYTVRQLELEnlTTQETREILHFHYTTWPDFGVP 170

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077601385 200 SSIDPILELIGEVR---CYQPDDSiPICIHCSAGCGRTGVVCAIDYTWKLLKDGIVPVNFSIFSLIQEMRTQRPSIVQTK 276
Cdd:cd14608   171 ESPASFLNFLFKVResgSLSPEHG-PVVVHCSAGIGRSGTFCLADTCLLLMDKRKDPSSVDIKKVLLEMRKFRMGLIQTA 249

                         250
                  ....*....|..
gi 2077601385 277 EQYKLVYNAVIE 288
Cdd:cd14608   250 DQLRFSYLAVIE 261
R-PTPc-V cd14618
catalytic domain of receptor-type tyrosine-protein phosphatase V; Receptor-type ...
 58-287 1.09e-51

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: 179.75  E-value: 1.09e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077601385  58 NRYKDILPYDHSRVELSLITSDTDSHYINANFIKGVYGPRAYIATQGPLPTTVTDFWRMIWEYEVLIVVMACMEFEMGKK 137
Cdd:cd14618     1 NRYPHVLPYDHSRVRLSQLGGEPHSDYINANFIPGYTSPQEFIATQGPLKKTIEDFWRLVWEQQVCNIIMLTVGMENGRV 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077601385 138 KCERYWAEVGDPsLQCGPFSVTCEAEEKKNEYVIRTLKVTLN--EAARTIHQFHYQNWPDHDIPSSIDPIL---ELI-GE 211
Cdd:cd14618    81 LCDHYWPSESTP-VSYGHITVHLLAQSSEDEWTRREFKLWHEdlRKERRVKHLHYTAWPDHGIPESTSSLMafrELVrEH 159

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2077601385 212 VRCYQpdDSIPICIHCSAGCGRTGVVCAIDYTWKLLKDGIVpvnFSIFSLIQEMRTQRPSIVQTKEQYKLVYNAVI 287
Cdd:cd14618   160 VQATK--GKGPTLVHCSAGVGRSGTFIALDRLLRQLKEEKV---VDVFNTVYILRMHRYLMIQTLSQYIFLHSCIL 230
R-PTPc-A-2 cd14623
catalytic domain of receptor-type tyrosine-protein phosphatase A, repeat 2; Receptor-type ...
 59-288 1.38e-51

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: 179.47  E-value: 1.38e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077601385  59 RYKDILPYDHSRVELSLITSDTDSHYINANFIKGVYGPRAYIATQGPLPTTVTDFWRMIWEYEVLIVVMACMEFEMGKKK 138
Cdd:cd14623     1 RVLQIIPYEFNRVIIPVKRGEENTDYVNASFIDGYRQKDSYIASQGPLQHTIEDFWRMIWEWKSCSIVMLTELEERGQEK 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077601385 139 CERYWAEvgDPSLQCGPFSVTCEAEEKKNEYVIRTLKVTLNE--AARTIHQFHYQNWPDHDIPSSIDPILELIGEV-RCY 215
Cdd:cd14623    81 CAQYWPS--DGSVSYGDITIELKKEEECESYTVRDLLVTNTRenKSRQIRQFHFHGWPEVGIPSDGKGMINIIAAVqKQQ 158

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2077601385 216 QPDDSIPICIHCSAGCGRTGVVCAIDYTWKLLK-DGIVPVnfsiFSLIQEMRTQRPSIVQTKEQYKLVYNAVIE 288
Cdd:cd14623   159 QQSGNHPITVHCSAGAGRTGTFCALSTVLERVKaEGILDV----FQTVKSLRLQRPHMVQTLEQYEFCYKVVQE 228
PTPc-N14 cd14599
catalytic domain of tyrosine-protein phosphatase non-receptor type 14; Tyrosine-protein ...
 17-291 1.41e-50

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: 178.65  E-value: 1.41e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077601385  17 KKLNQEAFADEFlklkRQSTKYRSDKIYPTATaeCPENIKKNRYKDILPYDHSRVELsLITSDTDSHYINANFIKGVYGP 96
Cdd:cd14599     7 RKLEEGMVFTEY----EQIPKKKADGVFTTAT--LPENAERNRIREVVPYEENRVEL-VPTKENNTGYINASHIKVTVGG 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077601385  97 RA--YIATQGPLPTTVTDFWRMIWEYEVLIVVMACMEFEMGKKKCERYWAEVGDP--SLQCGPFSVTCEAEEKKNEYVIR 172
Cdd:cd14599    80 EEwhYIATQGPLPHTCHDFWQMVWEQGVNVIAMVTAEEEGGRSKSHRYWPKLGSKhsSATYGKFKVTTKFRTDSGCYATT 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077601385 173 TLKVT--LNEAARTIHQFHYQNWPDHDIPSSIDPILELIGEVRCYQ----------PDDSIPICIHCSAGCGRTGVVCAI 240
Cdd:cd14599   160 GLKVKhlLSGQERTVWHLQYTDWPDHGCPEEVQGFLSYLEEIQSVRrhtnsmldstKNCNPPIVVHCSAGVGRTGVVILT 239

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|.
gi 2077601385 241 DYTWKLLKDGivpVNFSIFSLIQEMRTQRPSIVQTKEQYKLVYNAVIELFK 291
Cdd:cd14599   240 ELMIGCLEHN---EKVEVPVMLRHLREQRMFMIQTIAQYKFVYQVLIQFLK 287
R-PTP-N2 cd14610
PTP-like domain of receptor-type tyrosine-protein phosphatase N2; Receptor-type ...
 46-288 1.77e-50

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: 178.33  E-value: 1.77e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077601385  46 TATAECPENIKKNRYKDILPYDHSRVELSLITSDTDSHYINANFIKGvYGPR--AYIATQGPLPTTVTDFWRMIWEYEVL 123
Cdd:cd14610    36 TNVAQREENVQKNRSLAVLPYDHSRIILKAENSHSHSDYINASPIMD-HDPRnpAYIATQGPLPATVADFWQMVWESGCV 114

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077601385 124 IVVMACMEFEMGKKKCERYWAEVGDPSLQCgpFSVTCEAEEKK-NEYVIRT--LKVTLNEAARTIHQFHYQNWPDHDIPS 200
Cdd:cd14610   115 VIVMLTPLAENGVKQCYHYWPDEGSNLYHI--YEVNLVSEHIWcEDFLVRSfyLKNLQTNETRTVTQFHFLSWNDQGVPA 192

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077601385 201 SIDPILELIGEV-RCYQpDDSIPICIHCSAGCGRTGVVCAIDYTWKLLKDGIVPVNfsIFSLIQEMRTQRPSIVQTKEQY 279
Cdd:cd14610   193 STRSLLDFRRKVnKCYR-GRSCPIIVHCSDGAGRSGTYILIDMVLNKMAKGAKEID--IAATLEHLRDQRPGMVQTKEQF 269


                  ....*....
gi 2077601385 280 KLVYNAVIE 288
Cdd:cd14610   270 EFALTAVAE 278
R-PTPc-K-1 cd14631
catalytic domain of receptor-type tyrosine-protein phosphatase K, repeat 1; Receptor-type ...
 70-288 2.52e-50

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


Pssm-ID: 350479 [Multi-domain]  Cd Length: 218  Bit Score: 175.59  E-value: 2.52e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077601385  70 RVELSLITSDTDSHYINANFIKGVYGPRAYIATQGPLPTTVTDFWRMIWEYEVLIVVMACMEFEMGKKKCERYWAEvgDP 149
Cdd:cd14631     1 RVILQPVEDDPSSDYINANYIDGYQRPSHYIATQGPVHETVYDFWRMIWQEQSACIVMVTNLVEVGRVKCYKYWPD--DT 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077601385 150 SLQcGPFSVTCEAEEKKNEYVIRTLKVTLN--EAARTIHQFHYQNWPDHDIPSSIDPILELIGEVRCYQPDDSIPICIHC 227
Cdd:cd14631    79 EVY-GDFKVTCVEMEPLAEYVVRTFTLERRgyNEIREVKQFHFTGWPDHGVPYHATGLLSFIRRVKLSNPPSAGPIVVHC 157

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2077601385 228 SAGCGRTGVVCAIDYTWKLL-KDGIVpvnfSIFSLIQEMRTQRPSIVQTKEQYKLVYNAVIE 288
Cdd:cd14631   158 SAGAGRTGCYIVIDIMLDMAeREGVV----DIYNCVKALRSRRINMVQTEEQYIFIHDAILE 215
PTPc-N21_14 cd14540
catalytic domain of tyrosine-protein phosphatase non-receptor type 21 and type 14; ...
 84-288 4.78e-50

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: 174.95  E-value: 4.78e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077601385  84 YINANFIKGVYG--PRAYIATQGPLPTTVTDFWRMIWEYEVLIVVMACMEFEMGKKKCERYWAEVGD--PSLQCGPFSVT 159
Cdd:cd14540     1 YINASHITATVGgkQRFYIAAQGPLQNTVGDFWQMVWEQGVYLVVMVTAEEEGGREKCFRYWPTLGGehDALTFGEYKVS 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077601385 160 CEAEEKKNEYVIRTLKV--TLNEAARTIHQFHYQNWPDHDIPSSIDPILELIGEV-----RCYQPDD----SIPICIHCS 228
Cdd:cd14540    81 TKFSVSSGCYTTTGLRVkhTLSGQSRTVWHLQYTDWPDHGCPEDVSGFLDFLEEInsvrrHTNQDVAghnrNPPTLVHCS 160

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077601385 229 AGCGRTGVVCAIDYTWKLLKDGiVPVNfsIFSLIQEMRTQRPSIVQTKEQYKLVYNAVIE 288
Cdd:cd14540   161 AGVGRTGVVILADLMLYCLDHN-EELD--IPRVLALLRHQRMLLVQTLAQYKFVYNVLIQ 217
COG5599 COG5599
Protein tyrosine phosphatase [Signal transduction mechanisms];
10-297 4.99e-50

Protein tyrosine phosphatase [Signal transduction mechanisms];


Pssm-ID: 444335 [Multi-domain]  Cd Length: 282  Bit Score: 177.21  E-value: 4.99e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077601385  10 NLERAQSKKLNQEAFADEFLKLKRQSTKYRSDKIYPtataECPENIKKNRYKDILPYDHSRVElslitsdTDSHYINANF 89
Cdd:COG5599     2 SPKNPIAIKSEEEKINSRLSTLTNELAPSHNDPQYL----QNINGSPLNRFRDIQPYKETALR-------ANLGYLNANY 70

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077601385  90 IKgVYGPRAYIATQGPLPTTVTDFWRMIWEYEVLIVVM--ACMEFEMGKKKCERYWAEVGDPSLQcgpfsvTCEAEEKKN 167
Cdd:COG5599    71 IQ-VIGNHRYIATQYPLEEQLEDFFQMLFDNNTPVLVVlaSDDEISKPKVKMPVYFRQDGEYGKY------EVSSELTES 143

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077601385 168 EYV-----IRTLKVTLNEAA---RTIHQFHYQNWPDHDIPSS--IDPILELIGEVRCYQPDDSIPICIHCSAGCGRTGVV 237
Cdd:COG5599   144 IQLrdgieARTYVLTIKGTGqkkIEIPVLHVKNWPDHGAISAeaLKNLADLIDKKEKIKDPDKLLPVVHCRAGVGRTGTL 223

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2077601385 238 CAIDYTWKLLKDGIVpVNFSIFSLIQEMRTQR-PSIVQTKEQyklvYNAVIELFKRQIEAL 297
Cdd:COG5599   224 IACLALSKSINALVQ-ITLSVEEIVIDMRTSRnGGMVQTSEQ----LDVLVKLAEQQIRPL 279
PTPc-N5 cd14613
catalytic domain of tyrosine-protein phosphatase non-receptor type 5; Tyrosine-protein ...
 50-286 4.39e-49

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: 173.51  E-value: 4.39e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077601385  50 ECPENIKKNRYKDILPYDHSRVelSLITSDTD---SHYINANFIKGvYG--PRAYIATQGPLPTTVTDFWRMIWEYEVLI 124
Cdd:cd14613    21 DIPGLVRKNRYKTILPNPHSRV--CLTSPDQDdplSSYINANYIRG-YGgeEKVYIATQGPTVNTVGDFWRMVWQERSPI 97

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077601385 125 VVMACMEFEMgKKKCERYWAEvgdPSLQCGPFSVTCEAEEKKNEYVIRTLKVTLNEAARTIHQFHYQNWPDHDIPSSIDP 204
Cdd:cd14613    98 IVMITNIEEM-NEKCTEYWPE---EQVTYEGIEITVKQVIHADDYRLRLITLKSGGEERGLKHYWYTSWPDQKTPDNAPP 173

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077601385 205 ILELIGEV---RCYQPDDSIPICIHCSAGCGRTGVVCAIDYTWKLLKDGIVpvnFSIFSLIQEMRTQRPSIVQTKEQYKL 281
Cdd:cd14613   174 LLQLVQEVeeaRQQAEPNCGPVIVHCSAGIGRTGCFIATSICCKQLRNEGV---VDILRTTCQLRLDRGGMIQTCEQYQF 250


                  ....*
gi 2077601385 282 VYNAV 286
Cdd:cd14613   251 VHHVL 255
R-PTPc-S-1 cd14625
catalytic domain of receptor-type tyrosine-protein phosphatase S, repeat 1; Receptor-type ...
 25-288 9.68e-49

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: 173.74  E-value: 9.68e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077601385  25 ADEFLKLKRQSTKYRSDKIYPTATAECPENIKKNRYKDILPYDHSRVELSLITSDTDSHYINANFIKGVYGPRAYIATQG 104
Cdd:cd14625    18 ANDNLKLSQEYESIDPGQQFTWEHSNLEVNKPKNRYANVIAYDHSRVILQPIEGIMGSDYINANYIDGYRKQNAYIATQG 97

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077601385 105 PLPTTVTDFWRMIWEYEVLIVVMACMEFEMGKKKCERYWAEVGDPSLqcGPFSVTCEAEEKKNEYVIRTLKVTLNEAA-- 182
Cdd:cd14625    98 PLPETFGDFWRMVWEQRSATVVMMTKLEEKSRIKCDQYWPSRGTETY--GMIQVTLLDTIELATFCVRTFSLHKNGSSek 175

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077601385 183 RTIHQFHYQNWPDHDIPSSIDPILELIGEVRCYQPDDSIPICIHCSAGCGRTGVVCAIDYTWKLLKDgivPVNFSIFSLI 262
Cdd:cd14625   176 REVRQFQFTAWPDHGVPEYPTPFLAFLRRVKTCNPPDAGPIVVHCSAGVGRTGCFIVIDAMLERIKH---EKTVDIYGHV 252

                         250       260
                  ....*....|....*....|....*.
gi 2077601385 263 QEMRTQRPSIVQTKEQYKLVYNAVIE 288
Cdd:cd14625   253 TLMRSQRNYMVQTEDQYSFIHDALLE 278
R-PTPc-D-1 cd14624
catalytic domain of receptor-type tyrosine-protein phosphatase D, repeat 1; Receptor-type ...
 54-288 1.07e-48

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: 173.38  E-value: 1.07e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077601385  54 NIKKNRYKDILPYDHSRVELSLITSDTDSHYINANFIKGVYGPRAYIATQGPLPTTVTDFWRMIWEYEVLIVVMACMEFE 133
Cdd:cd14624    47 NKPKNRYANVIAYDHSRVLLSAIEGIPGSDYINANYIDGYRKQNAYIATQGALPETFGDFWRMIWEQRSATVVMMTKLEE 126

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077601385 134 MGKKKCERYWAEVGDPSLqcGPFSVTCEAEEKKNEYVIRTLKVTLNEAA--RTIHQFHYQNWPDHDIPSSIDPILELIGE 211
Cdd:cd14624   127 RSRVKCDQYWPSRGTETY--GLIQVTLLDTVELATYCVRTFALYKNGSSekREVRQFQFTAWPDHGVPEHPTPFLAFLRR 204

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2077601385 212 VRCYQPDDSIPICIHCSAGCGRTGVVCAIDYTWKLLKDgivPVNFSIFSLIQEMRTQRPSIVQTKEQYKLVYNAVIE 288
Cdd:cd14624   205 VKTCNPPDAGPMVVHCSAGVGRTGCFIVIDAMLERIKH---EKTVDIYGHVTLMRAQRNYMVQTEDQYIFIHDALLE 278
PTPc-N20 cd14596
catalytic domain of tyrosine-protein phosphatase non-receptor type 20; Tyrosine-protein ...
 84-291 8.13e-48

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: 168.39  E-value: 8.13e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077601385  84 YINANFIKGVYG--PRAYIATQGPLPTTVTDFWRMIWEYEVLIVVMACMEFEMGKKKCERYWAEVGDPSLQCGPFSVTCE 161
Cdd:cd14596     1 YINASYITMPVGeeELFYIATQGPLPSTIDDFWQMVWENRSDVIAMMTREVERGKVKCHRYWPETLQEPMELENYQLRLE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077601385 162 AEEKKNEYVIRTLKVTLNEA--ARTIHQFHYQNWPDHDIPSSIDPILELIgevrCY--QPDDSIPICIHCSAGCGRTGVV 237
Cdd:cd14596    81 NYQALQYFIIRIIKLVEKETgeNRLIKHLQFTTWPDHGTPQSSDQLVKFI----CYmrKVHNTGPIVVHCSAGIGRAGVL 156

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....
gi 2077601385 238 CAIDYTWKLLKDGIvpvNFSIFSLIQEMRTQRPSIVQTKEQYKLVYNAVIELFK 291
Cdd:cd14596   157 ICVDVLLSLIEKDL---SFNIKDIVREMRQQRYGMIQTKDQYLFCYKVVLEVLQ 207
PTPc-N2 cd14607
catalytic domain of tyrosine-protein phosphatase non-receptor type 2; Tyrosine-protein ...
 44-286 2.27e-47

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: 168.99  E-value: 2.27e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077601385  44 YPTATAECPENIKKNRYKDILPYDHSRVELSlitsDTDSHYINANFIKGVYGPRAYIATQGPLPTTVTDFWRMIWEYEVL 123
Cdd:cd14607    14 YPHRVAKYPENRNRNRYRDVSPYDHSRVKLQ----NTENDYINASLVVIEEAQRSYILTQGPLPNTCCHFWLMVWQQKTK 89

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077601385 124 IVVMACMEFEMGKKKCERYWAEVGDPSL---QCGpFSVTCEAEEKKNEYVIRTLKV-TLNEA-ARTIHQFHYQNWPDHDI 198
Cdd:cd14607    90 AVVMLNRIVEKDSVKCAQYWPTDEEEVLsfkETG-FSVKLLSEDVKSYYTVHLLQLeNINSGeTRTISHFHYTTWPDFGV 168

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077601385 199 PSSIDPILELIGEVR---CYQPDDSiPICIHCSAGCGRTGVVCAIDyTWKLLKDGIVPVNFSIFSLIQEMRTQRPSIVQT 275
Cdd:cd14607   169 PESPASFLNFLFKVResgSLSPEHG-PAVVHCSAGIGRSGTFSLVD-TCLVLMEKKDPDSVDIKQVLLDMRKYRMGLIQT 246

                         250
                  ....*....|.
gi 2077601385 276 KEQYKLVYNAV 286
Cdd:cd14607   247 PDQLRFSYMAV 257
R-PTPc-Z-1 cd17668
catalytic domain of receptor-type tyrosine-protein phosphatase Z, repeat 1; Receptor-type ...
 84-287 4.56e-47

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: 166.31  E-value: 4.56e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077601385  84 YINANFIKGVYGPRAYIATQGPLPTTVTDFWRMIWEYEVLIVVMACMEFEMGKKKCERYWAevGDPSLQCGPFSVTCEAE 163
Cdd:cd17668     1 YINANYVDGYNKPKAYIAAQGPLKSTAEDFWRMIWEHNVEVIVMITNLVEKGRRKCDQYWP--ADGSEEYGNFLVTQKSV 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077601385 164 EKKNEYVIRTLKVTLNE----------AARTIHQFHYQNWPDHDIPSSIDPILELIGEVRCYQPDDSIPICIHCSAGCGR 233
Cdd:cd17668    79 QVLAYYTVRNFTLRNTKikkgsqkgrpSGRVVTQYHYTQWPDMGVPEYTLPVLTFVRKASYAKRHAVGPVVVHCSAGVGR 158

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 2077601385 234 TGVVCAIDYTWKLLK-DGIVpvnfSIFSLIQEMRTQRPSIVQTKEQYKLVYNAVI 287
Cdd:cd17668   159 TGTYIVLDSMLQQIQhEGTV----NIFGFLKHIRSQRNYLVQTEEQYVFIHDALV 209
R-PTPc-E-1 cd14620
catalytic domain of receptor-type tyrosine-protein phosphatase E, repeat 1; Receptor-type ...
 60-288 1.56e-46

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: 165.50  E-value: 1.56e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077601385  60 YKDILPYDHSRVELSLITSDTDSHYINANFIKGVYGPRAYIATQGPLPTTVTDFWRMIWEYEVLIVVMACMEFEMGKKKC 139
Cdd:cd14620     1 YPNILPYDHSRVILSQLDGIPCSDYINASYIDGYKEKNKFIAAQGPKQETVNDFWRMVWEQKSATIVMLTNLKERKEEKC 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077601385 140 ERYWAEVGdpslqC---GPFSVTCEAEEKKNEYVIRTLKVT-----LNEAARTIHQFHYQNWPDHDIPSSIDPILELIGE 211
Cdd:cd14620    81 YQYWPDQG-----CwtyGNIRVAVEDCVVLVDYTIRKFCIQpqlpdGCKAPRLVTQLHFTSWPDFGVPFTPIGMLKFLKK 155

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2077601385 212 VRCYQPDDSIPICIHCSAGCGRTGVVCAIDYTWKLLKDgivPVNFSIFSLIQEMRTQRPSIVQTKEQYKLVYNAVIE 288
Cdd:cd14620   156 VKSVNPVHAGPIVVHCSAGVGRTGTFIVIDAMIDMMHA---EQKVDVFEFVSRIRNQRPQMVQTDMQYSFIYQALLE 229
R-PTP-C-2 cd14558
PTP-like domain of receptor-type tyrosine-protein phosphatase C, repeat 2; Receptor-type ...
 84-283 3.76e-46

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: 163.33  E-value: 3.76e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077601385  84 YINANFIKGVYGPRAYIATQGPLPTTVTDFWRMIWEYEVLIVVMACMEFEMGKKKCERYWaevGDPSLQCGPFSVTCEAE 163
Cdd:cd14558     1 YINASFIDGYWGPKSLIATQGPLPDTIADFWQMIFQKKVKVIVMLTELKEGDQEQCAQYW---GDEKKTYGDIEVELKDT 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077601385 164 EKKNEYVIRTLKVTL--NEAARTIHQFHYQNWPDHDIPSSIDPILELIGEVRCYQPDD------SIPICIHCSAGCGRTG 235
Cdd:cd14558    78 EKSPTYTVRVFEITHlkRKDSRTVYQYQYHKWKGEELPEKPKDLVDMIKSIKQKLPYKnskhgrSVPIVVHCSDGSSRTG 157

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 2077601385 236 VVCAIdytWKLL----KDGIVPVnfsiFSLIQEMRTQRPSIVQTKEQYKLVY 283
Cdd:cd14558   158 IFCAL---WNLLesaeTEKVVDV----FQVVKALRKQRPGMVSTLEQYQFLY 202
PTP-N23 cd14539
PTP-like domain of tyrosine-protein phosphatase non-receptor type 23; Tyrosine-protein ...
 84-283 6.29e-46

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: 162.94  E-value: 6.29e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077601385  84 YINANFIKGV--YGPRaYIATQGPLPTTVTDFWRMIWEYEVLIVVMACMEFEMGKKKCERYW-AEVGDPsLQCGPFSVTC 160
Cdd:cd14539     1 YINASLIEDLtpYCPR-FIATQAPLPGTAADFWLMVYEQQVSVIVMLVSEQENEKQKVHRYWpTERGQA-LVYGAITVSL 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077601385 161 EAEEKKNEYVIRTLKVTLNEA--ARTIHQFHYQNWPDHDIPSSIDPILELIGEVRCY---QPDDSIPICIHCSAGCGRTG 235
Cdd:cd14539    79 QSVRTTPTHVERIISIQHKDTrlSRSVVHLQFTTWPELGLPDSPNPLLRFIEEVHSHylqQRSLQTPIVVHCSSGVGRTG 158

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 2077601385 236 VVCaidytwkLLKDGIVPVN-----FSIFSLIQEMRTQRPSIVQTKEQYKLVY 283
Cdd:cd14539   159 AFC-------LLYAAVQEIEagngiPDLPQLVRKMRQQRKYMLQEKEHLKFCY 204
R-PTPc-A-1 cd14621
catalytic domain of receptor-type tyrosine-protein phosphatase A, repeat 1; Receptor-type ...
 53-288 1.03e-45

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: 165.58  E-value: 1.03e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077601385  53 ENIKKNRYKDILPYDHSRVELSLITSDTDSHYINANFIKGVYGPRAYIATQGPLPTTVTDFWRMIWEYEVLIVVMACMEF 132
Cdd:cd14621    51 ENKEKNRYVNILPYDHSRVHLTPVEGVPDSDYINASFINGYQEKNKFIAAQGPKEETVNDFWRMIWEQNTATIVMVTNLK 130

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077601385 133 EMGKKKCERYWAEVGdpSLQCGPFSVTCEAEEKKNEYVIRTL------KVTLNEAARTIHQFHYQNWPDHDIPSSIDPIL 206
Cdd:cd14621   131 ERKECKCAQYWPDQG--CWTYGNIRVSVEDVTVLVDYTVRKFciqqvgDVTNKKPQRLITQFHFTSWPDFGVPFTPIGML 208

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077601385 207 ELIGEVRCYQPDDSIPICIHCSAGCGRTGVVCAIDYTWKLLKdgiVPVNFSIFSLIQEMRTQRPSIVQTKEQYKLVYNAV 286
Cdd:cd14621   209 KFLKKVKNCNPQYAGAIVVHCSAGVGRTGTFIVIDAMLDMMH---AERKVDVYGFVSRIRAQRCQMVQTDMQYVFIYQAL 285


                  ..
gi 2077601385 287 IE 288
Cdd:cd14621   286 LE 287
R-PTPc-U-1 cd14632
catalytic domain of receptor-type tyrosine-protein phosphatase U, repeat 1; Receptor-type ...
 84-288 5.79e-45

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: 160.22  E-value: 5.79e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077601385  84 YINANFIKGVYGPRAYIATQGPLPTTVTDFWRMIWEYEVLIVVMACMEFEMGKKKCERYWAEVGDpslQCGPFSVTCEAE 163
Cdd:cd14632     1 YINANYIDGYHRSNHFIATQGPKQEMVYDFWRMVWQEHCSSIVMITKLVEVGRVKCSKYWPDDSD---TYGDIKITLLKT 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077601385 164 EKKNEYVIRTLKVTLN--EAARTIHQFHYQNWPDHDIPSSIDPILELIGEVRCYQPDDSIPICIHCSAGCGRTGVVCAID 241
Cdd:cd14632    78 ETLAEYSVRTFALERRgySARHEVKQFHFTSWPEHGVPYHATGLLAFIRRVKASTPPDAGPVVVHCSAGAGRTGCYIVLD 157

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*...
gi 2077601385 242 YTWKLLK-DGIVpvnfSIFSLIQEMRTQRPSIVQTKEQYKLVYNAVIE 288
Cdd:cd14632   158 VMLDMAEcEGVV----DIYNCVKTLCSRRINMIQTEEQYIFIHDAILE 201
PHA02738 PHA02738
hypothetical protein; Provisional
 33-286 1.96e-44

hypothetical protein; Provisional


Pssm-ID: 222923 [Multi-domain]  Cd Length: 320  Bit Score: 162.79  E-value: 1.96e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077601385  33 RQSTKYRSDKIYPTATAEcPENIKKNRYKDILPYDHSRVELSliTSDTDSHYINANFIKGVYGPRAYIATQGPLPTTVTD 112
Cdd:PHA02738   29 REHQKVISEKVDGTFNAE-KKNRKLNRYLDAVCFDHSRVILP--AERNRGDYINANYVDGFEYKKKFICGQAPTRQTCYD 105

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077601385 113 FWRMIWEYEVLIVVMACMEFEMGKKKCERYWAEVGDPSLQCGPFSVTCEAEEKKNEYVIRTLKVTL-NEAARTIHQFHYQ 191
Cdd:PHA02738  106 FYRMLWMEHVQIIVMLCKKKENGREKCFPYWSDVEQGSIRFGKFKITTTQVETHPHYVKSTLLLTDgTSATQTVTHFNFT 185

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077601385 192 NWPDHDIPSSIDPILELIGEVRCYQPD-------------DSIPICIHCSAGCGRTGVVCAIDYTWKLLKDGivpVNFSI 258
Cdd:PHA02738  186 AWPDHDVPKNTSEFLNFVLEVRQCQKElaqeslqighnrlQPPPIVVHCNAGLGRTPCYCVVDISISRFDAC---ATVSI 262

                         250       260
                  ....*....|....*....|....*...
gi 2077601385 259 FSLIQEMRTQRPSIVQTKEQYKLVYNAV 286
Cdd:PHA02738  263 PSIVSSIRNQRYYSLFIPFQYFFCYRAV 290
PTPc-N4 cd14601
catalytic domain of tyrosine-protein phosphatase non-receptor type 4; Tyrosine-protein ...
 84-291 3.49e-44

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: 158.57  E-value: 3.49e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077601385  84 YINANFI------KGVYgpRAYIATQGPLPTTVTDFWRMIWEYEVLIVVMACMEFEMGKKKCERYWAEVGDPSlQCGPFS 157
Cdd:cd14601     2 YINANYInmeipsSSII--NRYIACQGPLPNTCSDFWQMTWEQGSSMVVMLTTQVERGRVKCHQYWPEPSGSS-SYGGFQ 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077601385 158 VTCEAEEKKNEYVIRTLKVT--LNEAARTIHQFHYQNWPDHDIPSSIDPILELIGEVRCYQPDDSIPICIHCSAGCGRTG 235
Cdd:cd14601    79 VTCHSEEGNPAYVFREMTLTnlEKNESRPLTQIQYIAWPDHGVPDDSSDFLDFVCLVRNKRAGKDEPVVVHCSAGIGRTG 158

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 2077601385 236 VVCAIDYTWKLLKdgivpVNFSIFSL--IQEMRTQRPSIVQTKEQYKLVYNAVIELFK 291
Cdd:cd14601   159 VLITMETAMCLIE-----CNQPVYPLdiVRTMRDQRAMMIQTPSQYRFVCEAILKVYE 211
R-PTPc-R cd14611
catalytic domain of receptor-type tyrosine-protein phosphatase R; Receptor-type ...
 57-284 4.63e-44

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


Pssm-ID: 350459 [Multi-domain]  Cd Length: 226  Bit Score: 158.54  E-value: 4.63e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077601385  57 KNRYKDILPYDHSRVELSLITS-DTDSHYINANFIKGVYG-PRAYIATQGPLPTTVTDFWRMIWEYEVLIVVMaCMEFEM 134
Cdd:cd14611     2 KNRYKTILPNPHSRVCLKPKNSnDSLSTYINANYIRGYGGkEKAFIATQGPMINTVNDFWQMVWQEDSPVIVM-ITKLKE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077601385 135 GKKKCERYWAEVGDPSlqcGPFSVTCEAEEKKNEYVIRTLKVTLNEAARTIHQFHYQNWPDHDIPSSIDPILELIGEV-- 212
Cdd:cd14611    81 KNEKCVLYWPEKRGIY---GKVEVLVNSVKECDNYTIRNLTLKQGSQSRSVKHYWYTSWPDHKTPDSAQPLLQLMLDVee 157

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2077601385 213 -RCYQPDDSiPICIHCSAGCGRTGvvCAIDYT---WKLLKDGIVpvnfSIFSLIQEMRTQRPSIVQTKEQYKLVYN 284
Cdd:cd14611   158 dRLASPGRG-PVVVHCSAGIGRTG--CFIATTigcQQLKEEGVV----DVLSIVCQLRVDRGGMVQTSEQYEFVHH 226
R-PTPc-typeIIb-2 cd14556
PTP domain of type IIb (or R2B) subfamily receptor-type tyrosine-protein phosphatases, repeat ...
 84-283 1.23e-43

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: 156.41  E-value: 1.23e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077601385  84 YINANFIKGVYGPRAYIATQGPLPTTVTDFWRMIWEYEVLIVVMaCMEFEMGKKKCERYWAEVGdpSLQCGPFSVTCEAE 163
Cdd:cd14556     1 YINAALLDSYKQPAAFIVTQHPLPNTVTDFWRLVYDYGCTSIVM-LNQLDPKDQSCPQYWPDEG--SGTYGPIQVEFVST 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077601385 164 EKKNEYVIRTLKVT----LNEAARTIHQFHYQNWPDH-DIPSSIDPILELIGEVRCYQPD-DSIPICIHCSAGCGRTGVV 237
Cdd:cd14556    78 TIDEDVISRIFRLQnttrPQEGYRMVQQFQFLGWPRDrDTPPSKRALLKLLSEVEKWQEQsGEGPIVVHCLNGVGRSGVF 157

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*..
gi 2077601385 238 CAIDYTWKLLK-DGIVPVnfsiFSLIQEMRTQRPSIVQTKEQYKLVY 283
Cdd:cd14556   158 CAISSVCERIKvENVVDV----FQAVKTLRNHRPNMVETEEQYKFCY 200
R-PTPc-E-2 cd14622
catalytic domain of receptor-type tyrosine-protein phosphatase E, repeat 2; Receptor-type ...
 84-286 2.07e-42

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


Pssm-ID: 350470 [Multi-domain]  Cd Length: 205  Bit Score: 153.24  E-value: 2.07e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077601385  84 YINANFIKGVYGPRAYIATQGPLPTTVTDFWRMIWEYEVLIVVMACMEFEMGKKKCERYWAEVGdpSLQCGPFSVTCEAE 163
Cdd:cd14622     2 YINASFIDGYRQKDYFIATQGPLAHTVEDFWRMVWEWKCHTIVMLTELQEREQEKCVQYWPSEG--SVTHGEITIEIKND 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077601385 164 EKKNEYVIRTLKVTLN--EAARTIHQFHYQNWPDHDIPSSIDPILELIGEV-RCYQPDDSIPICIHCSAGCGRTGVVCAI 240
Cdd:cd14622    80 TLLETISIRDFLVTYNqeKQTRLVRQFHFHGWPEIGIPAEGKGMIDLIAAVqKQQQQTGNHPIVVHCSAGAGRTGTFIAL 159

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*..
gi 2077601385 241 DYTWKLLK-DGIVPVnfsiFSLIQEMRTQRPSIVQTKEQYKLVYNAV 286
Cdd:cd14622   160 SNILERVKaEGLLDV----FQTVKSLRLQRPHMVQTLEQYEFCYRVV 202
R-PTPc-C-1 cd14557
catalytic domain of receptor-type tyrosine-protein phosphatase C, repeat 1; Receptor-type ...
 84-283 2.21e-41

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: 149.98  E-value: 2.21e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077601385  84 YINANFIKGVYGPRAYIATQGPLPTTVTDFWRMIWEYEVLIVVMACMEFEMGKKKCERYWAEVGDPSLQCGPFSVTCEAE 163
Cdd:cd14557     1 YINASYIDGFKEPRKYIAAQGPKDETVDDFWRMIWEQKSTVIVMVTRCEEGNRNKCAQYWPSMEEGSRAFGDVVVKINEE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077601385 164 EKKNEYVIRTLKVTLNE---AARTIHQFHYQNWPDHDIPSSIDPILELIGEVRCYQPDDSIPICIHCSAGCGRTGVVCAI 240
Cdd:cd14557    81 KICPDYIIRKLNINNKKekgSGREVTHIQFTSWPDHGVPEDPHLLLKLRRRVNAFNNFFSGPIVVHCSAGVGRTGTYIGI 160

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....
gi 2077601385 241 DYTWKLLK-DGIVPVnfsiFSLIQEMRTQRPSIVQTKEQYKLVY 283
Cdd:cd14557   161 DAMLEGLEaEGRVDV----YGYVVKLRRQRCLMVQVEAQYILIH 200
PHA02746 PHA02746
protein tyrosine phosphatase; Provisional
 52-297 5.40e-40

protein tyrosine phosphatase; Provisional


Pssm-ID: 165113 [Multi-domain]  Cd Length: 323  Bit Score: 150.18  E-value: 5.40e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077601385  52 PENIKKNRYKDILPYDHSRVELS------------------LITS-DTDSHYINANFIKGVYGPRAYIATQGPLPTTVTD 112
Cdd:PHA02746   49 KENLKKNRFHDIPCWDHSRVVINaheslkmfdvgdsdgkkiEVTSeDNAENYIHANFVDGFKEANKFICAQGPKEDTSED 128

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077601385 113 FWRMIWEYEVLIVVmACMEFEMGKKKCERYWAEVGDPSLQCGPFSVTCEAEEKKNEYVIRTLKVT--LNEAARTIHQFHY 190
Cdd:PHA02746  129 FFKLISEHESQVIV-SLTDIDDDDEKCFELWTKEEDSELAFGRFVAKILDIIEELSFTKTRLMITdkISDTSREIHHFWF 207

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077601385 191 QNWPDHDIPSSIDPILELIGEVRCYQ----------PDDSIPICIHCSAGCGRTGVVCAIDYTW-KLLKDGIVpvnfSIF 259
Cdd:PHA02746  208 PDWPDNGIPTGMAEFLELINKVNEEQaelikqadndPQTLGPIVVHCSAGIGRAGTFCAIDNALeQLEKEKEV----CLG 283

                         250       260       270
                  ....*....|....*....|....*....|....*...
gi 2077601385 260 SLIQEMRTQRPSIVQTKEQYKLVYNAVIELFKRQIEAL 297
Cdd:PHA02746  284 EIVLKIRKQRHSSVFLPEQYAFCYKALKYAIIEEAKKK 321
PHA02747 PHA02747
protein tyrosine phosphatase; Provisional
 47-282 3.36e-39

protein tyrosine phosphatase; Provisional


Pssm-ID: 165114 [Multi-domain]  Cd Length: 312  Bit Score: 147.46  E-value: 3.36e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077601385  47 ATAECPENIKKNRYKDILPYDHSRVELSlITSDTDSHYINANFIKGVYGPRAYIATQGPLPTTVTDFWRMIWEYEVLIVV 126
Cdd:PHA02747   44 ANFEKPENQPKNRYWDIPCWDHNRVILD-SGGGSTSDYIHANWIDGFEDDKKFIATQGPFAETCADFWKAVWQEHCSIIV 122

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077601385 127 MAC-MEFEMGKKKCERYWAEVGDPSLQCGPFSVTCEAEEKKNEYVIRTLKVT--LNEAARTIHQFHYQNWPDHDIPSSID 203
Cdd:PHA02747  123 MLTpTKGTNGEEKCYQYWCLNEDGNIDMEDFRIETLKTSVRAKYILTLIEITdkILKDSRKISHFQCSEWFEDETPSDHP 202

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077601385 204 PILELIGEV--------RCYQPDDSI--PICIHCSAGCGRTGVVCAIDYTWKLLkdgIVPVNFSIFSLIQEMRTQRPSIV 273
Cdd:PHA02747  203 DFIKFIKIIdinrkksgKLFNPKDALlcPIVVHCSDGVGKTGIFCAVDICLNQL---VKRKAICLAKTAEKIREQRHAGI 279


                  ....*....
gi 2077601385 274 QTKEQYKLV 282
Cdd:PHA02747  280 MNFDDYLFI 288
R-PTPc-A-E-1 cd14551
catalytic domain of receptor-type tyrosine-protein phosphatase A and E, repeat 1; ...
 84-283 5.94e-39

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: 143.13  E-value: 5.94e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077601385  84 YINANFIKGVYGPRAYIATQGPLPTTVTDFWRMIWEYEVLIVVMACMEFEMGKKKCERYWAEVGDPSLqcGPFSVTCEAE 163
Cdd:cd14551     1 YINASYIDGYQEKNKFIAAQGPKDETVNDFWRMIWEQGSATIVMVTNLKERKEKKCSQYWPDQGCWTY--GNLRVRVEDT 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077601385 164 EKKNEYVIRTL------KVTLNEAARTIHQFHYQNWPDHDIPSSIDPILELIGEVRCYQPDDSIPICIHCSAGCGRTGVV 237
Cdd:cd14551    79 VVLVDYTTRKFciqkvnRGIGEKRVRLVTQFHFTSWPDFGVPFTPIGMLKFLKKVKSANPPRAGPIVVHCSAGVGRTGTF 158

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*..
gi 2077601385 238 CAIDYTWKLLK-DGIVPVnfsiFSLIQEMRTQRPSIVQTKEQYKLVY 283
Cdd:cd14551   159 IVIDAMLDMMHaEGKVDV----FGFVSRIRQQRSQMVQTDMQYVFIY 201
PTPc_plant_PTP1 cd17658
protein tyrosine phosphatase 1 from Arabidopsis thaliana and similar plant PTPs; Arabidopsis ...
 84-284 2.33e-36

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: 136.05  E-value: 2.33e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077601385  84 YINANFIKG---VYGPRaYIATQGPLPTTVTDFWRMIWEYEVLIVVMACMEFEMGKK-KCERYWAEVGDPSLQCGPFSVT 159
Cdd:cd17658     1 YINASLVETpasESLPK-FIATQGPLPHTFEDFWEMVIQQRCPVIIMLTRLVDNYSTaKCADYFPAEENESREFGRISVT 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077601385 160 CEAEE-KKNEYVIRTLKVTLNE---AARTIHQFHYQNWPDHDIPSSIDPILELIGevRCYQ-PDDSIPICIHCSAGCGRT 234
Cdd:cd17658    80 NKKLKhSQHSITLRVLEVQYIEseePPLSVLHIQYPEWPDHGVPKDTRSVRELLK--RLYGiPPSAGPIVVHCSAGIGRT 157

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|.
gi 2077601385 235 GVVCAIDYTW-KLLKDGIVPVNFSifSLIQEMRTQRPSIVQTKEQYKLVYN 284
Cdd:cd17658   158 GAYCTIHNTIrRILEGDMSAVDLS--KTVRKFRSQRIGMVQTQDQYIFCYA 206
PTPc-N21 cd14598
catalytic domain of tyrosine-protein phosphatase non-receptor type 21; Tyrosine-protein ...
 84-291 3.34e-36

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: 136.26  E-value: 3.34e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077601385  84 YINANFIKGVYGPRA--YIATQGPLPTTVTDFWRMIWEYEVLIVVMACMEFEMGKKKCERYWAEVGD--PSLQCGPFSVT 159
Cdd:cd14598     1 YINASHIKVTVGGKEwdYIATQGPLQNTCQDFWQMVWEQGVAIIAMVTAEEEGGREKSFRYWPRLGSrhNTVTYGRFKIT 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077601385 160 CEAEEKKNEYVIRTLKVT--LNEAARTIHQFHYQNWPDHDIPSSIDPILELIGEVRCYQ--------PDDS-IPICIHCS 228
Cdd:cd14598    81 TRFRTDSGCYATTGLKIKhlLTGQERTVWHLQYTDWPEHGCPEDLKGFLSYLEEIQSVRrhtnstidPKSPnPPVLVHCS 160

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2077601385 229 AGCGRTGVVCAIDYTWKLLKDGIVpvnFSIFSLIQEMRTQRPSIVQTKEQYKLVYNAVIELFK 291
Cdd:cd14598   161 AGVGRTGVVILSEIMIACLEHNEM---LDIPRVLDMLRQQRMMMVQTLSQYTFVYKVLIQFLK 220
PHA02742 PHA02742
protein tyrosine phosphatase; Provisional
 53-291 1.72e-34

protein tyrosine phosphatase; Provisional


Pssm-ID: 165109 [Multi-domain]  Cd Length: 303  Bit Score: 133.97  E-value: 1.72e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077601385  53 ENIKKNRYKDILPYDHSRVELSliTSDTDSHYINANFIKGVYGPRAYIATQGPLPTTVTDFWRMIWEYEVLIVVMACMEF 132
Cdd:PHA02742   51 KNMKKCRYPDAPCFDRNRVILK--IEDGGDDFINASYVDGHNAKGRFICTQAPLEETALDFWQAIFQDQVRVIVMITKIM 128

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077601385 133 EMGKKKCERYWAEVGDPSLQCGPFSVTCEAEEKKNEYVIRTLKVTLNE--AARTIHQFHYQNWPDHDIPSSIDPILELIG 210
Cdd:PHA02742  129 EDGKEACYPYWMPHERGKATHGEFKIKTKKIKSFRNYAVTNLCLTDTNtgASLDIKHFAYEDWPHGGLPRDPNKFLDFVL 208

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077601385 211 EVRCYQPDDSI-----------PICIHCSAGCGRTGVVCAIDYTWKLLKDGIVpvnFSIFSLIQEMRTQRPSIVQTKEQY 279
Cdd:PHA02742  209 AVREADLKADVdikgenivkepPILVHCSAGLDRAGAFCAIDICISKYNERAI---IPLLSIVRDLRKQRHNCLSLPQQY 285

                         250
                  ....*....|..
gi 2077601385 280 KLVYNAVIELFK 291
Cdd:PHA02742  286 IFCYFIVLIFAK 297
PTPc_motif smart00404
Protein tyrosine phosphatase, catalytic domain motif;
184-288 1.78e-34

Protein tyrosine phosphatase, catalytic domain motif;


Pssm-ID: 214649 [Multi-domain]  Cd Length: 105  Bit Score: 127.09  E-value: 1.78e-34
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077601385  184 TIHQFHYQNWPDHDIPSSIDPILELIGEVR--CYQPDDSIPICIHCSAGCGRTGVVCAIDYTWKLLKDGIVPVNfsIFSL 261
Cdd:smart00404   1 TVKHYHYTGWPDHGVPESPDSILELLRAVKknLNQSESSGPVVVHCSAGVGRTGTFVAIDILLQQLEAEAGEVD--IFDT 78

                           90       100
                   ....*....|....*....|....*..
gi 2077601385  262 IQEMRTQRPSIVQTKEQYKLVYNAVIE 288
Cdd:smart00404  79 VKELRSQRPGMVQTEEQYLFLYRALLE 105
PTPc_DSPc smart00012
Protein tyrosine phosphatase, catalytic domain, undefined specificity; Protein tyrosine ...
 184-288 1.78e-34

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: 127.09  E-value: 1.78e-34
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077601385  184 TIHQFHYQNWPDHDIPSSIDPILELIGEVR--CYQPDDSIPICIHCSAGCGRTGVVCAIDYTWKLLKDGIVPVNfsIFSL 261
Cdd:smart00012   1 TVKHYHYTGWPDHGVPESPDSILELLRAVKknLNQSESSGPVVVHCSAGVGRTGTFVAIDILLQQLEAEAGEVD--IFDT 78

                           90       100
                   ....*....|....*....|....*..
gi 2077601385  262 IQEMRTQRPSIVQTKEQYKLVYNAVIE 288
Cdd:smart00012  79 VKELRSQRPGMVQTEEQYLFLYRALLE 105
R-PTPc-K-2 cd14636
PTP domain of receptor-type tyrosine-protein phosphatase K, repeat 2; Receptor-type ...
 84-288 2.35e-29

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: 115.89  E-value: 2.35e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077601385  84 YINANFIKGVYGPRAYIATQGPLPTTVTDFWRMIWEYEVLIVVMaCMEFEMgKKKCERYWAEVGdpSLQCGPFSVTCEAE 163
Cdd:cd14636     1 YINAALMDSYRQPAAFIVTQHPLPNTVKDFWRLVYDYGCTSIVM-LNEVDL-AQGCPQYWPEEG--MLRYGPIQVECMSC 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077601385 164 EKKNEYVIRTLKVT----LNEAARTIHQFHYQNWPDH-DIPSSIDPILELIGEVRCYQPD----DSIPIcIHCSAGCGRT 234
Cdd:cd14636    77 SMDCDVISRIFRICnltrPQEGYLMVQQFQYLGWASHrEVPGSKRSFLKLILQVEKWQEEcdegEGRTI-IHCLNGGGRS 155

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....
gi 2077601385 235 GVVCAIDYTWKLLKDGIVpvnFSIFSLIQEMRTQRPSIVQTKEQYKLVYNAVIE 288
Cdd:cd14636   156 GMFCAISIVCEMIKRQNV---VDVFHAVKTLRNSKPNMVETPEQYRFCYDVALE 206
R-PTPc-T-2 cd14634
PTP domain of receptor-type tyrosine-protein phosphatase T, repeat 2; Receptor-type ...
 84-288 7.82e-25

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: 102.79  E-value: 7.82e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077601385  84 YINANFIKGVYGPRAYIATQGPLPTTVTDFWRMIWEYEVLIVVMACmefEMGKKK-CERYWAEvgDPSLQCGPFSVTCEA 162
Cdd:cd14634     1 YINAALMDSHKQPAAFIVTQHPLPNTVADFWRLVFDYNCSSVVMLN---EMDAAQlCMQYWPE--KTSCCYGPIQVEFVS 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077601385 163 EEKKNEYVIRTLKVT----LNEAARTIHQFHYQNWPDH-DIPSSIDPILELIGEVRCYQPD---DSIPICIHCSAGCGRT 234
Cdd:cd14634    76 ADIDEDIISRIFRICnmarPQDGYRIVQHLQYIGWPAYrDTPPSKRSILKVVRRLEKWQEQydgREGRTVVHCLNGGGRS 155

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....
gi 2077601385 235 GVVCAIDYTWKLLKDGIVpvnFSIFSLIQEMRTQRPSIVQTKEQYKLVYNAVIE 288
Cdd:cd14634   156 GTFCAICSVCEMIQQQNI---IDVFHTVKTLRNNKSNMVETLEQYKFVYEVALE 206
R-PTPc-M-2 cd14635
PTP domain of receptor-type tyrosine-protein phosphatase M, repeat 2; Receptor-type ...
 84-288 1.03e-23

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: 99.76  E-value: 1.03e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077601385  84 YINANFIKGVYGPRAYIATQGPLPTTVTDFWRMIWEYEVLIVVMacMEFEMGKKKCERYWAEVGdpSLQCGPFSVTCEAE 163
Cdd:cd14635     1 YINAALMDSYKQPSAFIVTQHPLPNTVKDFWRLVLDYHCTSIVM--LNDVDPAQLCPQYWPENG--VHRHGPIQVEFVSA 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077601385 164 EKKNEYVIRTLKV----TLNEAARTIHQFHYQNWPDH-DIPSSIDPILELIGEVRCYQPD---DSIPICIHCSAGCGRTG 235
Cdd:cd14635    77 DLEEDIISRIFRIynaaRPQDGYRMVQQFQFLGWPMYrDTPVSKRSFLKLIRQVDKWQEEyngGEGRTVVHCLNGGGRSG 156

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 2077601385 236 VVCAIDYTWKLLKDgivPVNFSIFSLIQEMRTQRPSIVQTKEQYKLVYNAVIE 288
Cdd:cd14635   157 TFCAISIVCEMLRH---QRAVDVFHAVKTLRNNKPNMVDLLDQYKFCYEVALE 206
R5-PTP-2 cd14550
PTP-like domain of R5 subfamily receptor-type tyrosine-protein phosphatases, repeat 2; The R5 ...
 84-284 4.59e-23

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: 97.78  E-value: 4.59e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077601385  84 YINANFIKGVYGPRAYIATQGPLPTTVTDFWRMIWEYEVLIVVMaCMEFEMGKKKCErYWAEVGDPsLQCGPFSVT-CEA 162
Cdd:cd14550     1 YINASYLQGYRRSNEFIITQHPLEHTIKDFWQMIWDHNSQTIVM-LTDNELNEDEPI-YWPTKEKP-LECETFKVTlSGE 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077601385 163 EEKKNEYVIR------TLKVTLNEAARTIHQFHYQNWPDHDIPssIDPILELIGEVRCYQPDDSIPICIHCSAGCGRTGV 236
Cdd:cd14550    78 DHSCLSNEIRlivrdfILESTQDDYVLEVRQFQCPSWPNPCSP--IHTVFELINTVQEWAQQRDGPIVVHDRYGGVQAAT 155

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|
gi 2077601385 237 VCAIdYTWK--LLKDGIVPVnFSIFSLIQEMrtqRPSIVQTKEQYKLVYN 284
Cdd:cd14550   156 FCAL-TTLHqqLEHESSVDV-YQVAKLYHLM---RPGVFTSKEDYQFLYK 200
R-PTP-Z-2 cd17669
catalytic domain of receptor-type tyrosine-protein phosphatase Z, repeat 2; Receptor-type ...
 84-287 9.98e-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: 96.99  E-value: 9.98e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077601385  84 YINANFIKGVYGPRAYIATQGPLPTTVTDFWRMIWEYEVLIVVMACMEFEMGKKKCErYWAEVGDPsLQCGPFSVTCEAE 163
Cdd:cd17669     1 YINASYIMGYYQSNEFIITQHPLLHTIKDFWRMIWDHNAQLIVMLPDGQNMAEDEFV-YWPNKDEP-INCETFKVTLIAE 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077601385 164 EKK---NE--YVIR--TLKVTLNEAARTIHQFHYQNWPDHDIPssIDPILELIGEVRCYQPDDSIPICIHCSAGCGRTGV 236
Cdd:cd17669    79 EHKclsNEekLIIQdfILEATQDDYVLEVRHFQCPKWPNPDSP--ISKTFELISIIKEEAANRDGPMIVHDEHGGVTAGT 156

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 2077601385 237 VCAI-DYTWKLLKDGIVPVnFSIFSLIQEMrtqRPSIVQTKEQYKLVYNAVI 287
Cdd:cd17669   157 FCALtTLMHQLEKENSVDV-YQVAKMINLM---RPGVFTDIEQYQFLYKAIL 204
R-PTP-G-2 cd17670
PTP-like domain of receptor-type tyrosine-protein phosphatase G, repeat 2; Receptor-type ...
 84-287 4.48e-22

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: 95.13  E-value: 4.48e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077601385  84 YINANFIKGVYGPRAYIATQGPLPTTVTDFWRMIWEYEVLIVVMacMEFEMGKKKCERYWAEVGDPSLQCGPFSVTCEAE 163
Cdd:cd17670     1 YINASYIMGYYRSNEFIITQHPLPHTTKDFWRMIWDHNAQIIVM--LPDNQGLAEDEFVYWPSREESMNCEAFTVTLISK 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077601385 164 EK---KNEYVI----RTLKVTLNEAARTIHQFHYQNWPDHDIPssIDPILELIGEVRCYQPDDSIPICIHCSAGCGRTGV 236
Cdd:cd17670    79 DRlclSNEEQIiihdFILEATQDDYVLEVRHFQCPKWPNPDAP--ISSTFELINVIKEEALTRDGPTIVHDEFGAVSAGT 156

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|.
gi 2077601385 237 VCAIDYTWKLLKDGIVPVNFSIFSLIQEMrtqRPSIVQTKEQYKLVYNAVI 287
Cdd:cd17670   157 LCALTTLSQQLENENAVDVYQVAKMINLM---RPGVFTDIEQYQFLYKAML 204
R-PTPc-U-2 cd14637
PTP domain of receptor-type tyrosine-protein phosphatase U, repeat 2; Receptor-type ...
 84-288 1.31e-21

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


Pssm-ID: 350485 [Multi-domain]  Cd Length: 207  Bit Score: 93.82  E-value: 1.31e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077601385  84 YINANFIKGVYGPRAYIATQGPLPTTVTDFWRMIWEYEVLIVVMACMEFEMGKK-KCERYWAEVGdpSLQCGPFSV---T 159
Cdd:cd14637     1 YINAALTDSYTRSAAFIVTLHPLQNTTTDFWRLVYDYGCTSVVMLNQLNQSNSAwPCLQYWPEPG--LQQYGPMEVefvS 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077601385 160 CEAEEKKNEYVIRTLKVT-LNEAARTIHQFHYQNW-PDHDIPSSIDPILELIGEVRCYQPDDSI-PICIHCSAGCGRTGV 236
Cdd:cd14637    79 GSADEDIVTRLFRVQNITrLQEGHLMVRHFQFLRWsAYRDTPDSKKAFLHLLASVEKWQRESGEgRTVVHCLNGGGRSGT 158

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 2077601385 237 VCAIDYTWKLLKDGIVpvnFSIFSLIQEMRTQRPSIVQTKEQYKLVYNAVIE 288
Cdd:cd14637   159 YCASAMILEMIRCHNI---VDVFYAVKTLRNYKPNMVETLEQYRFCYEIALE 207
PTP_YopH-like cd14559
YopH and related bacterial protein tyrosine phosphatases; Yersinia outer protein H (YopH) ...
 58-281 8.61e-17

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: 80.14  E-value: 8.61e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077601385  58 NRYKDIlpydHSRVELSlitsdtDSHYINANFIKgVYGPRAYIATQGPLPTTVTDFWRMIWEYEVLIVVMACMEFEMGKK 137
Cdd:cd14559     1 NRFTNI----QTRVSTP------VGKNLNANRVQ-IGNKNVAIACQYPKNEQLEDHLKMLADNRTPCLVVLASNKDIQRK 69

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077601385 138 KCERYWAevgdPSLQCGPFSVTCEaEEKKNEYVIRT------LKVTLNEAARTIHQFHYQNWPDHD-IPS---------- 200
Cdd:cd14559    70 GLPPYFR----QSGTYGSVTVKSK-KTGKDELVDGLkadmynLKITDGNKTITIPVVHVTNWPDHTaISSeglkeladlv 144

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077601385 201 --SID---PILELIGEVRCYQPDDSIPIcIHCSAGCGRTGVVCAidyTWKLLKDgivPVNFSIFSLIQEMRTQRPS-IVQ 274
Cdd:cd14559   145 nkSAEekrNFYKSKGSSAINDKNKLLPV-IHCRAGVGRTGQLAA---AMELNKS---PNNLSVEDIVSDMRTSRNGkMVQ 217


                  ....*..
gi 2077601385 275 TKEQYKL 281
Cdd:cd14559   218 KDEQLDT 224
PHA02740 PHA02740
protein tyrosine phosphatase; Provisional
 47-284 9.60e-10

protein tyrosine phosphatase; Provisional


Pssm-ID: 165107 [Multi-domain]  Cd Length: 298  Bit Score: 60.75  E-value: 9.60e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077601385  47 ATAECPENIkkNRYKD------ILPYDHSRVELSlitsdTDSHYINANFIKGVYGPRAYIATQGPLPTTVTDFWRMIWEY 120
Cdd:PHA02740   42 ANKACAQAE--NKAKDenlalhITRLLHRRIKLF-----NDEKVLDARFVDGYDFEQKFICIINLCEDACDKFLQALSDN 114

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077601385 121 EVLIVVMACmefEMGKKKC-ERYWAEVGDPSLQCGPFSVTCEAEEKKNEYVIRTLKVTLNEA-ARTIHQFHYQNWP---- 194
Cdd:PHA02740  115 KVQIIVLIS---RHADKKCfNQFWSLKEGCVITSDKFQIETLEIIIKPHFNLTLLSLTDKFGqAQKISHFQYTAWPadgf 191

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077601385 195 DHDIPSSID---PILELIGEVRCYQPDDSI-PICIHCSAGCGRTGVVCAIDYTW-KLLKDGIVpvnfSIFSLIQEMRTQR 269
Cdd:PHA02740  192 SHDPDAFIDffcNIDDLCADLEKHKADGKIaPIIIDCIDGISSSAVFCVFDICAtEFDKTGML----SIANALKKVRQKK 267

                         250
                  ....*....|....*
gi 2077601385 270 PSIVQTKEQYKLVYN 284
Cdd:PHA02740  268 YGCMNCLDDYVFCYH 282
PTP_DSP_cys cd14494
cys-based protein tyrosine phosphatase and dual-specificity phosphatase superfamily; This ...
 202-284 1.30e-09

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


Pssm-ID: 350344 [Multi-domain]  Cd Length: 113  Bit Score: 56.20  E-value: 1.30e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077601385 202 IDPILELIGEvrcyQPDDSIPICIHCSAGCGRTGVVCAIDytwkLLKDGivpvNFSIFSLIQEMRTQRPS-IVQTKEQYK 280
Cdd:cd14494    42 VDRFLEVLDQ----AEKPGEPVLVHCKAGVGRTGTLVACY----LVLLG----GMSAEEAVRIVRLIRPGgIPQTIEQLD 109


                  ....
gi 2077601385 281 LVYN 284
Cdd:cd14494   110 FLIK 113
CDC14 COG2453
Protein-tyrosine phosphatase [Signal transduction mechanisms];
187-283 1.76e-06

Protein-tyrosine phosphatase [Signal transduction mechanisms];


Pssm-ID: 441989 [Multi-domain]  Cd Length: 140  Bit Score: 48.04  E-value: 1.76e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077601385 187 QFHYQNWPDHDIPS--SIDPILELIgeVRCYQPDDsiPICIHCSAGCGRTGVVCAidyTWkLLKDGIvpvnfsifSL--- 261
Cdd:COG2453    49 EYLHLPIPDFGAPDdeQLQEAVDFI--DEALREGK--KVLVHCRGGIGRTGTVAA---AY-LVLLGL--------SAeea 112

                          90       100
                  ....*....|....*....|..
gi 2077601385 262 IQEMRTQRPSIVQTKEQYKLVY 283
Cdd:COG2453   113 LARVRAARPGAVETPAQRAFLE 134
DUSP23 cd14504
dual specificity phosphatase 23; Dual specificity phosphatase 23 (DUSP23), also known as ...
 171-282 3.49e-06

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: 47.27  E-value: 3.49e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077601385 171 IRTLkVTLNEAARTIHQFHYQNWPDHDIPS------SIDPILELIGEVRcYQPDDSIPICIHCSAGCGRTGVV--CAIDY 242
Cdd:cd14504    29 IRHV-VTLTEEPPPEHSDTCPGLRYHHIPIedytppTLEQIDEFLDIVE-EANAKNEAVLVHCLAGKGRTGTMlaCYLVK 106

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 2077601385 243 TWKLlkDGIvpvnfsifSLIQEMRTQRPSIVQTKEQYKLV 282
Cdd:cd14504   107 TGKI--SAV--------DAINEIRRIRPGSIETSEQEKFV 136
CDKN3-like cd14505
cyclin-dependent kinase inhibitor 3 and similar proteins; This family is composed of ...
 158-283 3.63e-04

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: 41.87  E-value: 3.63e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077601385 158 VTCEAEEkkneyvIRTLKV-TLNEAART--IHQFHYQnWPDHDIPSSIDPILELIGEVR-CYQPDDSIpiCIHCSAGCGR 233
Cdd:cd14505    49 TLCTDGE------LEELGVpDLLEQYQQagITWHHLP-IPDGGVPSDIAQWQELLEELLsALENGKKV--LIHCKGGLGR 119

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 2077601385 234 TGVVCAidyTWKLLKDGIVPVNfsifSLIQEMRTQRPSIVQTKEQYKLVY 283
Cdd:cd14505   120 TGLIAA---CLLLELGDTLDPE----QAIAAVRALRPGAIQTPKQENFLH 162
PTP_PTPDC1 cd14506
protein tyrosine phosphatase domain of PTP domain-containing protein 1; protein tyrosine ...
 223-282 2.51e-03

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: 40.02  E-value: 2.51e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2077601385 223 ICIHCSAGCGRTGVV--CAIDYTWKLLKDgivpvnfsifSLIQEMRTQRPSIVQTKEQYKLV 282
Cdd:cd14506   112 VAVHCHAGLGRTGVLiaCYLVYALRMSAD----------QAIRLVRSKRPNSIQTRGQVLCV 163
PTP_PTEN-like cd14497
protein tyrosine phosphatase-like domain of phosphatase and tensin homolog and similar ...
 186-239 2.72e-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: 39.10  E-value: 2.72e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 2077601385 186 HQFHYQNWPDHDIPSsIDPILELIGEVRCY-QPDDSIPICIHCSAGCGRTGVVCA 239
Cdd:cd14497    61 GRVLHYGFPDHHPPP-LGLLLEIVDDIDSWlSEDPNNVAVVHCKAGKGRTGTVIC 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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