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Conserved domains on  [gi|17544644|ref|NP_502200|]
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Tyrosine-protein phosphatase domain-containing protein [Caenorhabditis elegans]

Protein Classification

protein tyrosine phosphatase family protein( domain architecture ID 12193126)

cys-based protein tyrosine phosphatase (PTP) family protein, such as tyrosine-protein phosphatase that catalyzes the dephosphorylation of phosphotyrosine groups in phosphoproteins

CATH:  3.90.190.10
EC:  3.1.3.-
Gene Ontology:  GO:0004721|GO:0006470
PubMed:  27514797|17057753

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
PTPc smart00194
Protein tyrosine phosphatase, catalytic domain;
146-386 3.82e-58

Protein tyrosine phosphatase, catalytic domain;


:

Pssm-ID: 214550 [Multi-domain]  Cd Length: 259  Bit Score: 191.33  E-value: 3.82e-58
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17544644    146 CPNRCKMWQSHSSRNRHTDYKCYDHNRIIVQMCK---DDYINGSKINVPHFTPSIYLVQLPKmdsVDAVEEFWRVVFHEQ 222
Cdd:smart00194  17 ESCTVAAFPENRDKNRYKDVLPYDHTRVKLKPPPgegSDYINASYIDGPNGPKAYIATQGPL---PSTVEDFWRMVWEQK 93

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17544644    223 CQTVHIIARPEELTNPAIDKLFCQESGAWLYANGFFVNTRKVEKKENAKADMFVVEllPEGCSNAVMCSVYLHTYWKPLF 302
Cdd:smart00194  94 VTVIVMLTELVEKGREKCAQYWPDEEGEPLTYGDITVTLKSVEKVDDYTIRTLEVT--NTGCSETRTVTHYHYTNWPDHG 171

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17544644    303 GPD---RFGAQIRAAHQIAKNENGnsPTVIASVNGSGRNAALLTLAVVEDQLTRGKEPKISEIVRTIREQRPQSVDSYIQ 379
Cdd:smart00194 172 VPEspeSILDLIRAVRKSQSTSTG--PIVVHCSAGVGRTGTFIAIDILLQQLEAGKEVDIFEIVKELRSQRPGMVQTEEQ 249


                   ....*..
gi 17544644    380 YVSLYMA 386
Cdd:smart00194 250 YIFLYRA 256
 
Name Accession Description Interval E-value
PTPc smart00194
Protein tyrosine phosphatase, catalytic domain;
146-386 3.82e-58

Protein tyrosine phosphatase, catalytic domain;


Pssm-ID: 214550 [Multi-domain]  Cd Length: 259  Bit Score: 191.33  E-value: 3.82e-58
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17544644    146 CPNRCKMWQSHSSRNRHTDYKCYDHNRIIVQMCK---DDYINGSKINVPHFTPSIYLVQLPKmdsVDAVEEFWRVVFHEQ 222
Cdd:smart00194  17 ESCTVAAFPENRDKNRYKDVLPYDHTRVKLKPPPgegSDYINASYIDGPNGPKAYIATQGPL---PSTVEDFWRMVWEQK 93

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17544644    223 CQTVHIIARPEELTNPAIDKLFCQESGAWLYANGFFVNTRKVEKKENAKADMFVVEllPEGCSNAVMCSVYLHTYWKPLF 302
Cdd:smart00194  94 VTVIVMLTELVEKGREKCAQYWPDEEGEPLTYGDITVTLKSVEKVDDYTIRTLEVT--NTGCSETRTVTHYHYTNWPDHG 171

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17544644    303 GPD---RFGAQIRAAHQIAKNENGnsPTVIASVNGSGRNAALLTLAVVEDQLTRGKEPKISEIVRTIREQRPQSVDSYIQ 379
Cdd:smart00194 172 VPEspeSILDLIRAVRKSQSTSTG--PIVVHCSAGVGRTGTFIAIDILLQQLEAGKEVDIFEIVKELRSQRPGMVQTEEQ 249


                   ....*..
gi 17544644    380 YVSLYMA 386
Cdd:smart00194 250 YIFLYRA 256
Y_phosphatase pfam00102
Protein-tyrosine phosphatase;
156-386 8.23e-54

Protein-tyrosine phosphatase;


Pssm-ID: 459674 [Multi-domain]  Cd Length: 234  Bit Score: 178.97  E-value: 8.23e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17544644   156 HSSRNRHTDYKCYDHNRIIVQMCKD--DYINGSKINVPHFTPSIYLVQLPKMDSVdavEEFWRVVFHEQCQTVHIIARPE 233
Cdd:pfam00102   1 NLEKNRYKDVLPYDHTRVKLTGDPGpsDYINASYIDGYKKPKKYIATQGPLPNTV---EDFWRMVWEEKVTIIVMLTELE 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17544644   234 ELTNPAIDKLFCQESGAWLYANGFFVNTRKveKKENAKADMFVVELLPEGCSNAVMC-SVYLHTYWKPLFGPDRFGAQIR 312
Cdd:pfam00102  78 EKGREKCAQYWPEEEGESLEYGDFTVTLKK--EKEDEKDYTVRTLEVSNGGSEETRTvKHFHYTGWPDHGVPESPNSLLD 155

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 17544644   313 AAHQI--AKNENGNSPTVIASVNGSGRNAALLTLAVVEDQLTRGKEPKISEIVRTIREQRPQSVDSYIQYVSLYMA 386
Cdd:pfam00102 156 LLRKVrkSSLDGRSGPIVVHCSAGIGRTGTFIAIDIALQQLEAEGEVDIFQIVKELRSQRPGMVQTLEQYIFLYDA 231
PTPc cd00047
catalytic domain of protein tyrosine phosphatases; Protein tyrosine phosphatases (PTP, EC 3.1. ...
 182-385 1.26e-41

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: 145.89  E-value: 1.26e-41
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17544644 182 YINGSKINVPHFTPSIYLVQLPKMDSVdavEEFWRVVFHEQCQTVHIIARPEELTNPAIDKLFCQESGAWLYANGFFVNT 261
Cdd:cd00047   1 YINASYIDGYRGPKEYIATQGPLPNTV---EDFWRMVWEQKVSVIVMLTNLVEKGREKCERYWPEEGGKPLEYGDITVTL 77

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17544644 262 RKVEKKENAkaDMFVVELLPEGCSNAVMCSVYLHTYWKPLFGPDRFGAQIRAAHQIAK-NENGNSPTVIASVNGSGRNAA 340
Cdd:cd00047  78 VSEEELSDY--TIRTLELSPKGCSESREVTHLHYTGWPDHGVPSSPEDLLALVRRVRKeARKPNGPIVVHCSAGVGRTGT 155

                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*
gi 17544644 341 LLTLAVVEDQLTRGKEPKISEIVRTIREQRPQSVDSYIQYVSLYM 385
Cdd:cd00047 156 FIAIDILLERLEAEGEVDVFEIVKALRKQRPGMVQTLEQYEFIYE 200
PHA02747 PHA02747
protein tyrosine phosphatase; Provisional
 151-383 5.32e-08

protein tyrosine phosphatase; Provisional


Pssm-ID: 165114 [Multi-domain]  Cd Length: 312  Bit Score: 54.24  E-value: 5.32e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17544644  151 KMWQS-----HSSRNRHTDYKCYDHNRIIVQM---CKDDYINGSKINVPHFTPSIYLVQLPKMDSVDaveEFWRVVFHEQ 222
Cdd:PHA02747  41 GLIANfekpeNQPKNRYWDIPCWDHNRVILDSgggSTSDYIHANWIDGFEDDKKFIATQGPFAETCA---DFWKAVWQEH 117

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17544644  223 CQTVhIIARPEELTN--PAIDKLFCQESGAWLYANGFFVNTRKVEKKenAKADMFVVELLPEGCSNAVMCSVYLHTYW-- 298
Cdd:PHA02747 118 CSII-VMLTPTKGTNgeEKCYQYWCLNEDGNIDMEDFRIETLKTSVR--AKYILTLIEITDKILKDSRKISHFQCSEWfe 194

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17544644  299 --KPLFGPD--RFGAQIRAAHQIA-KNENGN----SPTVIASVNGSGRNAALLTLAVVEDQLTRGKEPKISEIVRTIREQ 369
Cdd:PHA02747 195 deTPSDHPDfiKFIKIIDINRKKSgKLFNPKdallCPIVVHCSDGVGKTGIFCAVDICLNQLVKRKAICLAKTAEKIREQ 274

                        250
                 ....*....|....
gi 17544644  370 RPQSVDSYIQYVSL 383
Cdd:PHA02747 275 RHAGIMNFDDYLFI 288
 
Name Accession Description Interval E-value
PTPc smart00194
Protein tyrosine phosphatase, catalytic domain;
146-386 3.82e-58

Protein tyrosine phosphatase, catalytic domain;


Pssm-ID: 214550 [Multi-domain]  Cd Length: 259  Bit Score: 191.33  E-value: 3.82e-58
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17544644    146 CPNRCKMWQSHSSRNRHTDYKCYDHNRIIVQMCK---DDYINGSKINVPHFTPSIYLVQLPKmdsVDAVEEFWRVVFHEQ 222
Cdd:smart00194  17 ESCTVAAFPENRDKNRYKDVLPYDHTRVKLKPPPgegSDYINASYIDGPNGPKAYIATQGPL---PSTVEDFWRMVWEQK 93

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17544644    223 CQTVHIIARPEELTNPAIDKLFCQESGAWLYANGFFVNTRKVEKKENAKADMFVVEllPEGCSNAVMCSVYLHTYWKPLF 302
Cdd:smart00194  94 VTVIVMLTELVEKGREKCAQYWPDEEGEPLTYGDITVTLKSVEKVDDYTIRTLEVT--NTGCSETRTVTHYHYTNWPDHG 171

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17544644    303 GPD---RFGAQIRAAHQIAKNENGnsPTVIASVNGSGRNAALLTLAVVEDQLTRGKEPKISEIVRTIREQRPQSVDSYIQ 379
Cdd:smart00194 172 VPEspeSILDLIRAVRKSQSTSTG--PIVVHCSAGVGRTGTFIAIDILLQQLEAGKEVDIFEIVKELRSQRPGMVQTEEQ 249


                   ....*..
gi 17544644    380 YVSLYMA 386
Cdd:smart00194 250 YIFLYRA 256
Y_phosphatase pfam00102
Protein-tyrosine phosphatase;
156-386 8.23e-54

Protein-tyrosine phosphatase;


Pssm-ID: 459674 [Multi-domain]  Cd Length: 234  Bit Score: 178.97  E-value: 8.23e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17544644   156 HSSRNRHTDYKCYDHNRIIVQMCKD--DYINGSKINVPHFTPSIYLVQLPKMDSVdavEEFWRVVFHEQCQTVHIIARPE 233
Cdd:pfam00102   1 NLEKNRYKDVLPYDHTRVKLTGDPGpsDYINASYIDGYKKPKKYIATQGPLPNTV---EDFWRMVWEEKVTIIVMLTELE 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17544644   234 ELTNPAIDKLFCQESGAWLYANGFFVNTRKveKKENAKADMFVVELLPEGCSNAVMC-SVYLHTYWKPLFGPDRFGAQIR 312
Cdd:pfam00102  78 EKGREKCAQYWPEEEGESLEYGDFTVTLKK--EKEDEKDYTVRTLEVSNGGSEETRTvKHFHYTGWPDHGVPESPNSLLD 155

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 17544644   313 AAHQI--AKNENGNSPTVIASVNGSGRNAALLTLAVVEDQLTRGKEPKISEIVRTIREQRPQSVDSYIQYVSLYMA 386
Cdd:pfam00102 156 LLRKVrkSSLDGRSGPIVVHCSAGIGRTGTFIAIDIALQQLEAEGEVDIFQIVKELRSQRPGMVQTLEQYIFLYDA 231
PTPc cd00047
catalytic domain of protein tyrosine phosphatases; Protein tyrosine phosphatases (PTP, EC 3.1. ...
 182-385 1.26e-41

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: 145.89  E-value: 1.26e-41
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17544644 182 YINGSKINVPHFTPSIYLVQLPKMDSVdavEEFWRVVFHEQCQTVHIIARPEELTNPAIDKLFCQESGAWLYANGFFVNT 261
Cdd:cd00047   1 YINASYIDGYRGPKEYIATQGPLPNTV---EDFWRMVWEQKVSVIVMLTNLVEKGREKCERYWPEEGGKPLEYGDITVTL 77

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17544644 262 RKVEKKENAkaDMFVVELLPEGCSNAVMCSVYLHTYWKPLFGPDRFGAQIRAAHQIAK-NENGNSPTVIASVNGSGRNAA 340
Cdd:cd00047  78 VSEEELSDY--TIRTLELSPKGCSESREVTHLHYTGWPDHGVPSSPEDLLALVRRVRKeARKPNGPIVVHCSAGVGRTGT 155

                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*
gi 17544644 341 LLTLAVVEDQLTRGKEPKISEIVRTIREQRPQSVDSYIQYVSLYM 385
Cdd:cd00047 156 FIAIDILLERLEAEGEVDVFEIVKALRKQRPGMVQTLEQYEFIYE 200
PTPc_motif smart00404
Protein tyrosine phosphatase, catalytic domain motif;
289-386 2.10e-17

Protein tyrosine phosphatase, catalytic domain motif;


Pssm-ID: 214649 [Multi-domain]  Cd Length: 105  Bit Score: 77.40  E-value: 2.10e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17544644    289 MCSVYLHTYWKPLFGPDRFGAQIRAAHQIAKNEN---GNSPTVIASVNGSGRNAALLTLAVVEDQLTRG-KEPKISEIVR 364
Cdd:smart00404   1 TVKHYHYTGWPDHGVPESPDSILELLRAVKKNLNqseSSGPVVVHCSAGVGRTGTFVAIDILLQQLEAEaGEVDIFDTVK 80

                           90       100
                   ....*....|....*....|..
gi 17544644    365 TIREQRPQSVDSYIQYVSLYMA 386
Cdd:smart00404  81 ELRSQRPGMVQTEEQYLFLYRA 102
PTPc_DSPc smart00012
Protein tyrosine phosphatase, catalytic domain, undefined specificity; Protein tyrosine ...
 289-386 2.10e-17

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


Pssm-ID: 214469 [Multi-domain]  Cd Length: 105  Bit Score: 77.40  E-value: 2.10e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17544644    289 MCSVYLHTYWKPLFGPDRFGAQIRAAHQIAKNEN---GNSPTVIASVNGSGRNAALLTLAVVEDQLTRG-KEPKISEIVR 364
Cdd:smart00012   1 TVKHYHYTGWPDHGVPESPDSILELLRAVKKNLNqseSSGPVVVHCSAGVGRTGTFVAIDILLQQLEAEaGEVDIFDTVK 80

                           90       100
                   ....*....|....*....|..
gi 17544644    365 TIREQRPQSVDSYIQYVSLYMA 386
Cdd:smart00012  81 ELRSQRPGMVQTEEQYLFLYRA 102
R-PTPc-E-1 cd14620
catalytic domain of receptor-type tyrosine-protein phosphatase E, repeat 1; Receptor-type ...
 168-386 6.84e-10

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: 58.80  E-value: 6.84e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17544644 168 YDHNRIIVQ-----MCKDdYINGSKINVPHFTPSIYLVQLPKMDSVDaveEFWRVVFHEQCQTVHIIARPEELTNPAIDK 242
Cdd:cd14620   7 YDHSRVILSqldgiPCSD-YINASYIDGYKEKNKFIAAQGPKQETVN---DFWRMVWEQKSATIVMLTNLKERKEEKCYQ 82

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17544644 243 lFCQESGAWLYANgFFVNTRKVEKKENAKADMFVVE-LLPEGCSNAVMCSVYLHTYWkPLFGPD-------RFGAQIRAA 314
Cdd:cd14620  83 -YWPDQGCWTYGN-IRVAVEDCVVLVDYTIRKFCIQpQLPDGCKAPRLVTQLHFTSW-PDFGVPftpigmlKFLKKVKSV 159

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 17544644 315 hqiakNENGNSPTVIASVNGSGRNAALLTLAVVEDQLTRGKEPKISEIVRTIREQRPQSVDSYIQYVSLYMA 386
Cdd:cd14620 160 -----NPVHAGPIVVHCSAGVGRTGTFIVIDAMIDMMHAEQKVDVFEFVSRIRNQRPQMVQTDMQYSFIYQA 226
R-PTP-N cd14609
PTP-like domain of receptor-type tyrosine-protein phosphatase N; Receptor-type ...
 140-380 9.11e-10

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: 59.28  E-value: 9.11e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17544644 140 RDTEASC-----PNRCKMWQSHSS--RNRHTDYKCYDHNRIIVQM----CKDDYINGSKInVPH--FTPSIYLVQLPKMD 206
Cdd:cd14609  19 KEWQALCayqaePNTCSTAQGEANvkKNRNPDFVPYDHARIKLKAesnpSRSDYINASPI-IEHdpRMPAYIATQGPLSH 97

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17544644 207 SvdaVEEFWRVVFHEQCQTVHIIARPEELTNPAIDKLFCQEsGAWLY-------------ANGFFVNT---RKVEKKENA 270
Cdd:cd14609  98 T---IADFWQMVWENGCTVIVMLTPLVEDGVKQCDRYWPDE-GSSLYhiyevnlvsehiwCEDFLVRSfylKNVQTQETR 173

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17544644 271 KADMFVVELLP-EGCSNAVmcsvylhtywKPLFGPDRfgaqiraahQIAKNENGNS-PTVIASVNGSGRNAALLTLAVVE 348
Cdd:cd14609 174 TLTQFHFLSWPaEGIPSST----------RPLLDFRR---------KVNKCYRGRScPIIVHCSDGAGRTGTYILIDMVL 234

                       250       260       270
                ....*....|....*....|....*....|...
gi 17544644 349 DQLTRG-KEPKISEIVRTIREQRPQSVDSYIQY 380
Cdd:cd14609 235 NRMAKGvKEIDIAATLEHVRDQRPGMVRTKDQF 267
R3-PTPc cd14548
catalytic domain of R3 subfamily receptor-type tyrosine-protein phosphatases and similar ...
 161-384 1.01e-08

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: 55.44  E-value: 1.01e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17544644 161 RHTDYKCYDHNRI-IVQMCKD---DYINGSKINVPHFTPSIYLVQLPKMDSVDaveEFWRVVFHEQCQTvhIIArpeeLT 236
Cdd:cd14548   1 RYTNILPYDHSRVkLIPINEEegsDYINANYIPGYNSPREFIATQGPLPGTKD---DFWRMVWEQNSHT--IVM----LT 71

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17544644 237 NpaidklfCQESGA------WLYAN--GFFVNTRKVEKKENAKADMFVVELLPEGcSNAVMCSVYLH-TYWkPLFG---- 303
Cdd:cd14548  72 Q-------CMEKGRvkcdhyWPFDQdpVYYGDITVTMLSESVLPDWTIREFKLER-GDEVRSVRQFHfTAW-PDHGvpea 142

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17544644 304 PDRFGAQIRAAHQIAKNENGnsPTVIASVNGSGRNAALLTLAVVEDQLTRGKEPKISEIVRTIREQRPQSVDSYIQYVSL 383
Cdd:cd14548 143 PDSLLRFVRLVRDYIKQEKG--PTIVHCSAGVGRTGTFIALDRLLQQIESEDYVDIFGIVYDLRKHRPLMVQTEAQYIFL 220


                .
gi 17544644 384 Y 384
Cdd:cd14548 221 H 221
PTPc-N18 cd14603
catalytic domain of tyrosine-protein phosphatase non-receptor type 18; Tyrosine-protein ...
 159-386 3.19e-08

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: 54.45  E-value: 3.19e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17544644 159 RNRHTDYKCYDHNRIIVQMCKD----DYINGSKINVPHFTPSIYLVQLPKMDSVdavEEFWRVVFHEQCQTVHIIARPEE 234
Cdd:cd14603  33 KNRYKDILPYDQTRVILSLLQEeghsDYINANFIKGVDGSRAYIATQGPLSHTV---LDFWRMIWQYGVKVILMACREIE 109

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17544644 235 LTNPAIDKLFCQESGAWLYanGFFVNTrKVEKKEnAKADMFVVELLPEGCSNAVMCSVYLHTYWkPLFG----PDRFGAQ 310
Cdd:cd14603 110 MGKKKCERYWAQEQEPLQT--GPFTIT-LVKEKR-LNEEVILRTLKVTFQKESRSVSHFQYMAW-PDHGipdsPDCMLAM 184

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 17544644 311 IRAAHQiaKNENGNSPTVIASVNGSGRNAALLTLAVVEDQLTRGKEP---KISEIVRTIREQRPQSVDSYIQYVSLYMA 386
Cdd:cd14603 185 IELARR--LQGSGPEPLCVHCSAGCGRTGVICTVDYVRQLLLTQRIPpdfSIFDVVLEMRKQRPAAVQTEEQYEFLYHT 261
PHA02747 PHA02747
protein tyrosine phosphatase; Provisional
 151-383 5.32e-08

protein tyrosine phosphatase; Provisional


Pssm-ID: 165114 [Multi-domain]  Cd Length: 312  Bit Score: 54.24  E-value: 5.32e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17544644  151 KMWQS-----HSSRNRHTDYKCYDHNRIIVQM---CKDDYINGSKINVPHFTPSIYLVQLPKMDSVDaveEFWRVVFHEQ 222
Cdd:PHA02747  41 GLIANfekpeNQPKNRYWDIPCWDHNRVILDSgggSTSDYIHANWIDGFEDDKKFIATQGPFAETCA---DFWKAVWQEH 117

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17544644  223 CQTVhIIARPEELTN--PAIDKLFCQESGAWLYANGFFVNTRKVEKKenAKADMFVVELLPEGCSNAVMCSVYLHTYW-- 298
Cdd:PHA02747 118 CSII-VMLTPTKGTNgeEKCYQYWCLNEDGNIDMEDFRIETLKTSVR--AKYILTLIEITDKILKDSRKISHFQCSEWfe 194

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17544644  299 --KPLFGPD--RFGAQIRAAHQIA-KNENGN----SPTVIASVNGSGRNAALLTLAVVEDQLTRGKEPKISEIVRTIREQ 369
Cdd:PHA02747 195 deTPSDHPDfiKFIKIIDINRKKSgKLFNPKdallCPIVVHCSDGVGKTGIFCAVDICLNQLVKRKAICLAKTAEKIREQ 274

                        250
                 ....*....|....
gi 17544644  370 RPQSVDSYIQYVSL 383
Cdd:PHA02747 275 RHAGIMNFDDYLFI 288
R-PTPc-A-1 cd14621
catalytic domain of receptor-type tyrosine-protein phosphatase A, repeat 1; Receptor-type ...
 143-386 2.44e-07

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: 51.95  E-value: 2.44e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17544644 143 EASCPNRCKmwQSHSSRNRHTDYKCYDHNRI----IVQMCKDDYINGSKINVPHFTPSIYLVQLPKMDSVDaveEFWRVV 218
Cdd:cd14621  41 QATCEAASK--EENKEKNRYVNILPYDHSRVhltpVEGVPDSDYINASFINGYQEKNKFIAAQGPKEETVN---DFWRMI 115

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17544644 219 FHEQCQTVHIIARPEELTNPAIDKlFCQESGAWLYANgFFVNTRKVEKKENAKADMFVVELLPE--GCSNAVMCSVYLHT 296
Cdd:cd14621 116 WEQNTATIVMVTNLKERKECKCAQ-YWPDQGCWTYGN-IRVSVEDVTVLVDYTVRKFCIQQVGDvtNKKPQRLITQFHFT 193

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17544644 297 YWkPLFGPD-------RFGAQIRAAhqiakNENGNSPTVIASVNGSGRNAALLTLAVVEDQLTRGKEPKISEIVRTIREQ 369
Cdd:cd14621 194 SW-PDFGVPftpigmlKFLKKVKNC-----NPQYAGAIVVHCSAGVGRTGTFIVIDAMLDMMHAERKVDVYGFVSRIRAQ 267

                       250
                ....*....|....*..
gi 17544644 370 RPQSVDSYIQYVSLYMA 386
Cdd:cd14621 268 RCQMVQTDMQYVFIYQA 284
PTP_fungal cd18533
fungal protein tyrosine phosphatases; This subfamily contains Saccharomyces cerevisiae ...
 182-384 2.99e-07

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: 50.71  E-value: 2.99e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17544644 182 YINGSKINVPHFTPSIYL-VQLPKMDSVDaveEFWRVVFHEQCQTVHIIARPEELtnpAIDKlfC----QESGAWLYANG 256
Cdd:cd18533   1 YINASYITLPGTSSKRYIaTQGPLPATIG---DFWKMIWQNNVGVIVMLTPLVEN---GREK--CdqywPSGEYEGEYGD 72

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17544644 257 FFVNTRKVEKKENAKADMFVVELLPEGCSnavMCSVYlHTYWK--PLFG----PDRFGAQIRAAHQIAKNENGNSPTVIA 330
Cdd:cd18533  73 LTVELVSEEENDDGGFIVREFELSKEDGK---VKKVY-HIQYKswPDFGvpdsPEDLLTLIKLKRELNDSASLDPPIIVH 148

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 17544644 331 SVNGSGRNAALLTLAVVEDQLTRGKEPK---------ISEIVRTIREQRPQSVDSYIQYVSLY 384
Cdd:cd18533 149 CSAGVGRTGTFIALDSLLDELKRGLSDSqdledsedpVYEIVNQLRKQRMSMVQTLRQYIFLY 211
PTPc-N2 cd14607
catalytic domain of tyrosine-protein phosphatase non-receptor type 2; Tyrosine-protein ...
 140-231 3.08e-07

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: 51.51  E-value: 3.08e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17544644 140 RDTEASCPNRCKMWQSHSSRNRHTDYKCYDHNRIIVQMCKDDYINGSKINVPHFTPSIYLVQLPKMDSVDaveEFWRVVF 219
Cdd:cd14607   8 RNESHDYPHRVAKYPENRNRNRYRDVSPYDHSRVKLQNTENDYINASLVVIEEAQRSYILTQGPLPNTCC---HFWLMVW 84

                        90
                ....*....|..
gi 17544644 220 HEQCQTVHIIAR 231
Cdd:cd14607  85 QQKTKAVVMLNR 96
PTPc-N1 cd14608
catalytic domain of tyrosine-protein phosphatase non-receptor type 1; Tyrosine-protein ...
 140-231 2.24e-06

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: 48.87  E-value: 2.24e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17544644 140 RDTEASCPNRCKMWQSHSSRNRHTDYKCYDHNRIIVQMCKDDYINGSKINVPHFTPSIYLVQLPKMDSVDaveEFWRVVF 219
Cdd:cd14608   9 RHEASDFPCRVAKLPKNKNRNRYRDVSPFDHSRIKLHQEDNDYINASLIKMEEAQRSYILTQGPLPNTCG---HFWEMVW 85

                        90
                ....*....|..
gi 17544644 220 HEQCQTVHIIAR 231
Cdd:cd14608  86 EQKSRGVVMLNR 97
R-PTPc-A-2 cd14623
catalytic domain of receptor-type tyrosine-protein phosphatase A, repeat 2; Receptor-type ...
 168-384 2.91e-06

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: 48.12  E-value: 2.91e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17544644 168 YDHNRIIVQMCK----DDYINGSKINVPHFTPSIYLVQLPKMDSVdavEEFWRVVFHEQCQTVHIIARPEELTNPAIDKl 243
Cdd:cd14623   8 YEFNRVIIPVKRgeenTDYVNASFIDGYRQKDSYIASQGPLQHTI---EDFWRMIWEWKSCSIVMLTELEERGQEKCAQ- 83

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17544644 244 FCQESGAWLYANgFFVNTRKVEKKENAKADMFVVELLPEGCSNAVMcsvYLHTYWKPLFGPDRFGA---QIRAAHQIAKN 320
Cdd:cd14623  84 YWPSDGSVSYGD-ITIELKKEEECESYTVRDLLVTNTRENKSRQIR---QFHFHGWPEVGIPSDGKgmiNIIAAVQKQQQ 159

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 17544644 321 ENGNSPTVIASVNGSGRNAALLTLAVVEDQLTRGKEPKISEIVRTIREQRPQSVDSYIQYVSLY 384
Cdd:cd14623 160 QSGNHPITVHCSAGAGRTGTFCALSTVLERVKAEGILDVFQTVKSLRLQRPHMVQTLEQYEFCY 223
PHA02742 PHA02742
protein tyrosine phosphatase; Provisional
 158-385 3.31e-06

protein tyrosine phosphatase; Provisional


Pssm-ID: 165109 [Multi-domain]  Cd Length: 303  Bit Score: 48.46  E-value: 3.31e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17544644  158 SRNRHTDYKCYDHNRIIVQMCK--DDYINGSKINVPHFTPSIYLVQLPKMDSVDaveEFWRVVFHEQCQTVHIIARPEEL 235
Cdd:PHA02742  54 KKCRYPDAPCFDRNRVILKIEDggDDFINASYVDGHNAKGRFICTQAPLEETAL---DFWQAIFQDQVRVIVMITKIMED 130

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17544644  236 TNPAIDKLF-CQESGAWLYANgFFVNTRKVEKKENAKADMFVVELLPEGCSNAVMCSVYlhTYWkPLFGPDR-------F 307
Cdd:PHA02742 131 GKEACYPYWmPHERGKATHGE-FKIKTKKIKSFRNYAVTNLCLTDTNTGASLDIKHFAY--EDW-PHGGLPRdpnkfldF 206

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17544644  308 GAQIRAAHQIA------KNENGNSPTVIASVNGSGRNAALLTLAVVEDQLTRGKEPKISEIVRTIREQRPQSVDSYIQYV 381
Cdd:PHA02742 207 VLAVREADLKAdvdikgENIVKEPPILVHCSAGLDRAGAFCAIDICISKYNERAIIPLLSIVRDLRKQRHNCLSLPQQYI 286


                 ....
gi 17544644  382 SLYM 385
Cdd:PHA02742 287 FCYF 290
R-PTPc-H cd14619
catalytic domain of receptor-type tyrosine-protein phosphatase H; Receptor-type ...
 160-384 1.45e-05

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: 46.04  E-value: 1.45e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17544644 160 NRHTDYKCYDHNRIIVQMCKD----DYINGSkinvphFTPSIYLVQ--------LPKmdsvdAVEEFWRVVFHEQCQTVH 227
Cdd:cd14619   1 NRFRNVLPYDWSRVPLKPIHEepgsDYINAN------YMPGYWSSQefiatqgpLPQ-----TVGDFWRMIWEQQSSTIV 69

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17544644 228 IiarpeeLTNpaidklfCQESGA------WL--YANGFFVNTRKVEKKENAKADMFVVELLPEGCSNAVMCSV--YLHTY 297
Cdd:cd14619  70 M------LTN-------CMEAGRvkcehyWPldYTPCTYGHLRVTVVSEEVMENWTVREFLLKQVEEQKTLSVrhFHFTA 136

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17544644 298 WkPLFG----PDRFGAQIRAAHQIAKNENGNSPTVIASVNGSGRNAALLTLAVVEDQLTRGKEPKISEIVRTIREQRPQS 373
Cdd:cd14619 137 W-PDHGvpssTDTLLAFRRLLRQWLDQTMSGGPTVVHCSAGVGRTGTLIALDVLLQQLQSEGLLGPFSFVQKMRENRPLM 215

                       250
                ....*....|.
gi 17544644 374 VDSYIQYVSLY 384
Cdd:cd14619 216 VQTESQYVFLH 226
R-PTPc-A-E-2 cd14552
catalytic domain of receptor-type tyrosine-protein phosphatase A and E, repeat 2; ...
 182-386 1.78e-05

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: 45.34  E-value: 1.78e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17544644 182 YINGSKINVPHFTPSIYLVQLPKMDSVdavEEFWRVVFHEQCQTVHIIARPEELTNpaiDK--LFCQESGAWLYANgFFV 259
Cdd:cd14552   1 YINASFIDGYRQKDAYIATQGPLDHTV---EDFWRMIWEWKSCSIVMLTEIKERSQ---NKcaQYWPEDGSVSSGD-ITV 73

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17544644 260 NTRKVEKKENAKADMFVVELLPEGCSNAVMcSVYLHTyWKPLFGPDRFGAQIR--AAHQIAKNENGNSPTVIASVNGSGR 337
Cdd:cd14552  74 ELKDQTDYEDYTLRDFLVTKGKGGSTRTVR-QFHFHG-WPEVGIPDNGKGMIDliAAVQKQQQQSGNHPITVHCSAGAGR 151

                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*....
gi 17544644 338 NAALLTLAVVEDQLTRGKEPKISEIVRTIREQRPQSVDSYIQYVSLYMA 386
Cdd:cd14552 152 TGTFCALSTVLERVKAEGVLDVFQVVKSLRLQRPHMVQTLEQYEFCYKV 200
R-PTPc-F-1 cd14626
catalytic domain of receptor-type tyrosine-protein phosphatase F, repeat 1; Receptor-type ...
 129-386 2.06e-05

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: 45.80  E-value: 2.06e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17544644 129 LRFNQseggvrrDTEASCPNRCKMWQS-----HSSRNRHTDYKCYDHNRIIVQMCK----DDYINGSKINVPHFTPSIYL 199
Cdd:cd14626  16 LKFSQ-------EYESIDPGQQFTWENsnlevNKPKNRYANVIAYDHSRVILTSVDgvpgSDYINANYIDGYRKQNAYIA 88

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17544644 200 VQLPKMDSVDaveEFWRVVFHEQCQTVHIIARPEELTNPAIDKlFCQESGAWLYAngfFVNTRKVEKKENAKADMFVVEL 279
Cdd:cd14626  89 TQGPLPETLS---DFWRMVWEQRTATIVMMTRLEEKSRVKCDQ-YWPIRGTETYG---MIQVTLLDTVELATYSVRTFAL 161

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17544644 280 LPEGCSNAVMCSVYLHTYWkPLFGPDRFGAQIRAAHQIAK--NENGNSPTVIASVNGSGRNAALLtlaVVEDQLTRGKEP 357
Cdd:cd14626 162 YKNGSSEKREVRQFQFMAW-PDHGVPEYPTPILAFLRRVKacNPPDAGPMVVHCSAGVGRTGCFI---VIDAMLERMKHE 237

                       250       260       270
                ....*....|....*....|....*....|..
gi 17544644 358 KISEI---VRTIREQRPQSVDSYIQYVSLYMA 386
Cdd:cd14626 238 KTVDIyghVTCMRSQRNYMVQTEDQYIFIHEA 269
R-PTPc-M-1 cd14633
catalytic domain of receptor-type tyrosine-protein phosphatase M, repeat 1; Receptor-type ...
 159-386 3.14e-05

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: 45.42  E-value: 3.14e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17544644 159 RNRHTDYKCYDHNRIIVQMCK----DDYINGSKINVPHfTPSIYLVQLPKMDsvDAVEEFWRVVFHEQCQTVHIIARPEE 234
Cdd:cd14633  43 KNRYGNIIAYDHSRVRLQPIEgetsSDYINGNYIDGYH-RPNHYIATQGPMQ--ETIYDFWRMVWHENTASIIMVTNLVE 119

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17544644 235 LTNPAIDKLFCQESGAWLYANGFFVNTRKVEKkenAKADMFVVEllPEGCSNAVMCSVYLHTYWKPLFGPDRFGAQIRAA 314
Cdd:cd14633 120 VGRVKCCKYWPDDTEIYKDIKVTLIETELLAE---YVIRTFAVE--KRGVHEIREIRQFHFTGWPDHGVPYHATGLLGFV 194

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 17544644 315 HQI-AKNENGNSPTVIASVNGSGRNAALLTLAVVEDQLTRGKEPKISEIVRTIREQRPQSVDSYIQYVSLYMA 386
Cdd:cd14633 195 RQVkSKSPPNAGPLVVHCSAGAGRTGCFIVIDIMLDMAEREGVVDIYNCVRELRSRRVNMVQTEEQYVFIHDA 267
R-PTPc-S-1 cd14625
catalytic domain of receptor-type tyrosine-protein phosphatase S, repeat 1; Receptor-type ...
 159-386 3.28e-05

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: 45.47  E-value: 3.28e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17544644 159 RNRHTDYKCYDHNRIIVQ----MCKDDYINGSKINVPHFTPSIYLVQLPKMDSVDaveEFWRVVFHEQCQTVHIIARPEE 234
Cdd:cd14625  50 KNRYANVIAYDHSRVILQpiegIMGSDYINANYIDGYRKQNAYIATQGPLPETFG---DFWRMVWEQRSATVVMMTKLEE 126

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17544644 235 LTNPAIDKlFCQESGAWLYAngfFVNTRKVEKKENAKADMFVVELLPEGCSNAVMCSVYLHTYWkPLFG----PDRFGAQ 310
Cdd:cd14625 127 KSRIKCDQ-YWPSRGTETYG---MIQVTLLDTIELATFCVRTFSLHKNGSSEKREVRQFQFTAW-PDHGvpeyPTPFLAF 201

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 17544644 311 IRAAHQIAKNENGnsPTVIASVNGSGRNAALLtlaVVEDQLTRGKEPKISEI---VRTIREQRPQSVDSYIQYVSLYMA 386
Cdd:cd14625 202 LRRVKTCNPPDAG--PIVVHCSAGVGRTGCFI---VIDAMLERIKHEKTVDIyghVTLMRSQRNYMVQTEDQYSFIHDA 275
R-PTPc-E-2 cd14622
catalytic domain of receptor-type tyrosine-protein phosphatase E, repeat 2; Receptor-type ...
 181-384 3.45e-05

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: 44.61  E-value: 3.45e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17544644 181 DYINGSKINVPHFTPSIYLVQLPKMDSVdavEEFWRVVFHEQCQTVHIIArpeELTNPAIDKLFcqesGAWLYANGFFVN 260
Cdd:cd14622   1 DYINASFIDGYRQKDYFIATQGPLAHTV---EDFWRMVWEWKCHTIVMLT---ELQEREQEKCV----QYWPSEGSVTHG 70

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17544644 261 TRKVEKKENAKADMFVVE--LLPEGCSNAVMCSVYLHTYWKPLFGPDRFGA---QIRAAHQIAKNENGNSPTVIASVNGS 335
Cdd:cd14622  71 EITIEIKNDTLLETISIRdfLVTYNQEKQTRLVRQFHFHGWPEIGIPAEGKgmiDLIAAVQKQQQQTGNHPIVVHCSAGA 150

                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*....
gi 17544644 336 GRNAALLTLAVVEDQLTRGKEPKISEIVRTIREQRPQSVDSYIQYVSLY 384
Cdd:cd14622 151 GRTGTFIALSNILERVKAEGLLDVFQTVKSLRLQRPHMVQTLEQYEFCY 199
PHA02738 PHA02738
hypothetical protein; Provisional
 160-386 5.01e-05

hypothetical protein; Provisional


Pssm-ID: 222923 [Multi-domain]  Cd Length: 320  Bit Score: 44.92  E-value: 5.01e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17544644  160 NRHTDYKCYDHNRIIVQMCKD--DYINGSKINVPHFTPSIYLVQLPKMDSvdaVEEFWRVVFHEQCQTVHIIARPEELTN 237
Cdd:PHA02738  53 NRYLDAVCFDHSRVILPAERNrgDYINANYVDGFEYKKKFICGQAPTRQT---CYDFYRMLWMEHVQIIVMLCKKKENGR 129

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17544644  238 PAIDKLFCQESGAWLYANGFFVNTRKVEKKENAKADMFvveLLPEGCSNAVMCSVYLHTYWKPLFGPD------RFGAQI 311
Cdd:PHA02738 130 EKCFPYWSDVEQGSIRFGKFKITTTQVETHPHYVKSTL---LLTDGTSATQTVTHFNFTAWPDHDVPKntseflNFVLEV 206

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17544644  312 RAAH--------QIAKNENGNSPTVIASVNGSGRNAALLTLAVVEDQLTRGKEPKISEIVRTIREQRPQSVDSYIQYVSL 383
Cdd:PHA02738 207 RQCQkelaqeslQIGHNRLQPPPIVVHCNAGLGRTPCYCVVDISISRFDACATVSIPSIVSSIRNQRYYSLFIPFQYFFC 286


                 ...
gi 17544644  384 YMA 386
Cdd:PHA02738 287 YRA 289
PTPc-N20_13 cd14538
catalytic domain of tyrosine-protein phosphatase non-receptor type 20 and type 13; ...
 182-386 6.44e-05

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: 43.90  E-value: 6.44e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17544644 182 YINGSKINVP-HFTPSIYLV-QLPKMDSVDaveEFWRVVFHEQCQTVHIIARPEEltnpaIDKLFCQ-------ESGAWL 252
Cdd:cd14538   1 YINASHIRIPvGGDTYHYIAcQGPLPNTTG---DFWQMVWEQKSEVIAMVTQDVE-----GGKVKCHrywpdslNKPLIC 72

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17544644 253 YaNGFFVNTRKVEKKENAKADMFVVELLPEGCSNAVMCSVYlhTYWK----PLFGPD--RFGAQIRAAHQIAknengnsP 326
Cdd:cd14538  73 G-GRLEVSLEKYQSLQDFVIRRISLRDKETGEVHHITHLNF--TTWPdhgtPQSADPllRFIRYMRRIHNSG-------P 142

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|
gi 17544644 327 TVIASVNGSGRNAALLTLAVVEDQLTRGKEPKISEIVRTIREQRPQSVDSYIQYVSLYMA 386
Cdd:cd14538 143 IVVHCSAGIGRTGVLITIDVALGLIERDLPFDIQDIVKDLREQRQGMIQTKDQYIFCYKA 202
R-PTPc-typeIIb-2 cd14556
PTP domain of type IIb (or R2B) subfamily receptor-type tyrosine-protein phosphatases, repeat ...
 182-384 1.93e-04

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: 42.39  E-value: 1.93e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17544644 182 YINGSKINvPHFTPSIYLVQ---LPkmdsvDAVEEFWRVVFHEQCQTVHIIARPEELTNPAIDKLFCQESGAWLYANGFF 258
Cdd:cd14556   1 YINAALLD-SYKQPAAFIVTqhpLP-----NTVTDFWRLVYDYGCTSIVMLNQLDPKDQSCPQYWPDEGSGTYGPIQVEF 74

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17544644 259 VNTrkvEKKENAKADMFVVELLPEGCSNAVMCSVYLHTYWkPLFG--PDRFGAQIRAAHQIAK--NENGNSPTVIASVNG 334
Cdd:cd14556  75 VST---TIDEDVISRIFRLQNTTRPQEGYRMVQQFQFLGW-PRDRdtPPSKRALLKLLSEVEKwqEQSGEGPIVVHCLNG 150

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|
gi 17544644 335 SGRNAALLTLAVVEDQLTRGKEPKISEIVRTIREQRPQSVDSYIQYVSLY 384
Cdd:cd14556 151 VGRSGVFCAISSVCERIKVENVVDVFQAVKTLRNHRPNMVETEEQYKFCY 200
PTPc-N1_2 cd14545
catalytic domain of tyrosine-protein phosphatase non-receptor type 1 and type 2; ...
 159-226 2.60e-04

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: 42.38  E-value: 2.60e-04
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17544644 159 RNRHTDYKCYDHNRIIVQMCK--DDYINGSKINVPHFTPSIYLVQLPKMDSVDaveEFWRVVFHEQCQTV 226
Cdd:cd14545   1 LNRYRDRDPYDHDRSRVKLKQgdNDYINASLVEVEEAKRSYILTQGPLPNTSG---HFWQMVWEQNSKAV 67
R-PTPc-T-1 cd14630
catalytic domain of receptor-type tyrosine-protein phosphatase T, repeat 1; Receptor-type ...
 158-386 4.23e-04

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: 41.55  E-value: 4.23e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17544644 158 SRNRHTDYKCYDHNRIIVQMCKD----DYINGSKINVPHfTPSIYLVQLPKMDsvDAVEEFWRVVFHEQCQTVHIIARPE 233
Cdd:cd14630   5 NKNRYGNIISYDHSRVRLQLLDGdphsDYINANYIDGYH-RPRHYIATQGPMQ--ETVKDFWRMIWQENSASVVMVTNLV 81

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17544644 234 ELTNPAIDKLFCQESGawLYANgffVNTRKVEKKENAKADMFVVELLPEGCSNAVMCSVYLHTYWK----PLFGPDRFGA 309
Cdd:cd14630  82 EVGRVKCVRYWPDDTE--VYGD---IKVTLIETEPLAEYVIRTFTVQKKGYHEIREIRQFHFTSWPdhgvPCYATGLLGF 156

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 17544644 310 qIRAAHQIAKNENGnsPTVIASVNGSGRNAALLTLAVVEDQLTRGKEPKISEIVRTIREQRPQSVDSYIQYVSLYMA 386
Cdd:cd14630 157 -VRQVKFLNPPDAG--PIVVHCSAGAGRTGCFIAIDIMLDMAENEGVVDIFNCVRELRAQRVNMVQTEEQYVFVHDA 230
PTPc-N12 cd14604
catalytic domain of tyrosine-protein phosphatase non-receptor type 12; Tyrosine-protein ...
 159-395 4.32e-04

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: 41.84  E-value: 4.32e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17544644 159 RNRHTDYKCYDHNRIIVQM----CKDDYINGSKINVPHFTPSIYLVQLPKMDSVdavEEFWRVVFHEQCQTVHIIARPEE 234
Cdd:cd14604  60 KNRYKDILPFDHSRVKLTLktssQDSDYINANFIKGVYGPKAYIATQGPLANTV---IDFWRMIWEYNVAIIVMACREFE 136

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17544644 235 LTNPAIDKLFCQESGAWLYANGFFVNTrkveKKENAKADMFVVELLPEGCSNAVMCSVYLHTYWKPLFGPDRFGAQIRAA 314
Cdd:cd14604 137 MGRKKCERYWPLYGEEPMTFGPFRISC----EAEQARTDYFIRTLLLEFQNETRRLYQFHYVNWPDHDVPSSFDSILDMI 212

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17544644 315 HQIAK-NENGNSPTVIASVNGSGRNAALLTLAVVEDQLTRGKEPK---ISEIVRTIREQRPQSVDSYIQYVSLYMATNWL 390
Cdd:cd14604 213 SLMRKyQEHEDVPICIHCSAGCGRTGAICAIDYTWNLLKAGKIPEefnVFNLIQEMRTQRHSAVQTKEQYELVHRAIAQL 292


                ....*
gi 17544644 391 IKTKL 395
Cdd:cd14604 293 FEKQL 297
R-PTPc-D-1 cd14624
catalytic domain of receptor-type tyrosine-protein phosphatase D, repeat 1; Receptor-type ...
 129-386 4.66e-04

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: 42.03  E-value: 4.66e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17544644 129 LRFNQseggvrrDTEASCPNRCKMWQsHSS------RNRHTDYKCYDHNRIIVQMCK----DDYINGSKINVPHFTPSIY 198
Cdd:cd14624  22 LKFSQ-------EYESIDPGQQFTWE-HSNlevnkpKNRYANVIAYDHSRVLLSAIEgipgSDYINANYIDGYRKQNAYI 93

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17544644 199 LVQ--LPkmdsvDAVEEFWRVVFHEQCQTVHIIARPEELTNPAIDKlFCQESGAWLYAngfFVNTRKVEKKENAKADMFV 276
Cdd:cd14624  94 ATQgaLP-----ETFGDFWRMIWEQRSATVVMMTKLEERSRVKCDQ-YWPSRGTETYG---LIQVTLLDTVELATYCVRT 164

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17544644 277 VELLPEGCSNAVMCSVYLHTYWkPLFG----PDRFGAQIRAAHQIAKNENGnsPTVIASVNGSGRNAALLTLAVVEDQLT 352
Cdd:cd14624 165 FALYKNGSSEKREVRQFQFTAW-PDHGvpehPTPFLAFLRRVKTCNPPDAG--PMVVHCSAGVGRTGCFIVIDAMLERIK 241

                       250       260       270
                ....*....|....*....|....*....|....
gi 17544644 353 RGKEPKISEIVRTIREQRPQSVDSYIQYVSLYMA 386
Cdd:cd14624 242 HEKTVDIYGHVTLMRAQRNYMVQTEDQYIFIHDA 275
PTPc-N13 cd14597
catalytic domain of tyrosine-protein phosphatase non-receptor type 13; Tyrosine-protein ...
 154-384 8.98e-04

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: 40.58  E-value: 8.98e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17544644 154 QSHSSRNRHTDYKCYDHNRIIVQMcKDDYINGSKINVP-HFTPSIYLV---QLPKmdsvdAVEEFWRVVFHEQCQTVHII 229
Cdd:cd14597   1 KENRKKNRYKNILPYDTTRVPLGD-EGGYINASFIKMPvGDEEFVYIAcqgPLPT-----TVADFWQMVWEQKSTVIAMM 74

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17544644 230 ARPEELtnpaiDKLFCQESGAWLYANGFFVNTR-KVEKKENAKADMFVVEL--LPEGCSNAVMCSVYLH-TYWKPLFGPD 305
Cdd:cd14597  75 TQEVEG-----GKIKCQRYWPEILGKTTMVDNRlQLTLVRMQQLKNFVIRVleLEDIQTREVRHITHLNfTAWPDHDTPS 149

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17544644 306 R------FGAQIRAAHQiaknengNSPTVIASVNGSGRNAALLTLAVVEDQLTRGKEPKISEIVRTIREQRPQSVDSYIQ 379
Cdd:cd14597 150 QpeqlltFISYMRHIHK-------SGPIITHCSAGIGRSGTLICIDVVLGLISKDLDFDISDIVRTMRLQRHGMVQTEDQ 222


                ....*
gi 17544644 380 YVSLY 384
Cdd:cd14597 223 YIFCY 227
 
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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