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Conserved domains on  [gi|71991025|ref|NP_501764|]
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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;
111-434 2.02e-69

Protein tyrosine phosphatase, catalytic domain;


:

Pssm-ID: 214550 [Multi-domain]  Cd Length: 259  Bit Score: 221.76  E-value: 2.02e-69
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71991025    111 LSTYFDEHLAGYTPP-NFTSVEWEKSLSKNRSKNHKLNDNTRVILSPENTEnsrtdpPDTYINASHIKFDNSQKEFIVTQ 189
Cdd:smart00194   2 LEEEFEKLDRLKPDDeSCTVAAFPENRDKNRYKDVLPYDHTRVKLKPPPGE------GSDYINASYIDGPNGPKAYIATQ 75

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71991025    190 YPLPDTVRDFWRMVSIMKVTQIVTIFEPqtdeaIEEFRnptltlaapaptstmttiggfpvpigqiahnrdqiqgqsIRC 269
Cdd:smart00194  76 GPLPSTVEDFWRMVWEQKVTVIVMLTEL-----VEKGR---------------------------------------EKC 111

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71991025    270 ESnvhrssFFPLETDHYMNLKGWLINTRRVTvdhrNKGWMNKYTVEVVAEGCSEATFAKVYNCTTWPWKKYPDDEKKVLA 349
Cdd:smart00194 112 AQ------YWPDEEGEPLTYGDITVTLKSVE----KVDDYTIRTLEVTNTGCSETRTVTHYHYTNWPDHGVPESPESILD 181

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71991025    350 LVRAPYKDTSTSLianleklAPIVVMCDLGLDRSATVVLTSIIIDQIIAGKTPDCDALFKKMRDQRAGVFTMSIFYTYAI 429
Cdd:smart00194 182 LIRAVRKSQSTST-------GPIVVHCSAGVGRTGTFIAIDILLQQLEAGKEVDIFEIVKELRSQRPGMVQTEEQYIFLY 254


                   ....*
gi 71991025    430 RAALF 434
Cdd:smart00194 255 RAILE 259
 
Name Accession Description Interval E-value
PTPc smart00194
Protein tyrosine phosphatase, catalytic domain;
111-434 2.02e-69

Protein tyrosine phosphatase, catalytic domain;


Pssm-ID: 214550 [Multi-domain]  Cd Length: 259  Bit Score: 221.76  E-value: 2.02e-69
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71991025    111 LSTYFDEHLAGYTPP-NFTSVEWEKSLSKNRSKNHKLNDNTRVILSPENTEnsrtdpPDTYINASHIKFDNSQKEFIVTQ 189
Cdd:smart00194   2 LEEEFEKLDRLKPDDeSCTVAAFPENRDKNRYKDVLPYDHTRVKLKPPPGE------GSDYINASYIDGPNGPKAYIATQ 75

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71991025    190 YPLPDTVRDFWRMVSIMKVTQIVTIFEPqtdeaIEEFRnptltlaapaptstmttiggfpvpigqiahnrdqiqgqsIRC 269
Cdd:smart00194  76 GPLPSTVEDFWRMVWEQKVTVIVMLTEL-----VEKGR---------------------------------------EKC 111

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71991025    270 ESnvhrssFFPLETDHYMNLKGWLINTRRVTvdhrNKGWMNKYTVEVVAEGCSEATFAKVYNCTTWPWKKYPDDEKKVLA 349
Cdd:smart00194 112 AQ------YWPDEEGEPLTYGDITVTLKSVE----KVDDYTIRTLEVTNTGCSETRTVTHYHYTNWPDHGVPESPESILD 181

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71991025    350 LVRAPYKDTSTSLianleklAPIVVMCDLGLDRSATVVLTSIIIDQIIAGKTPDCDALFKKMRDQRAGVFTMSIFYTYAI 429
Cdd:smart00194 182 LIRAVRKSQSTST-------GPIVVHCSAGVGRTGTFIAIDILLQQLEAGKEVDIFEIVKELRSQRPGMVQTEEQYIFLY 254


                   ....*
gi 71991025    430 RAALF 434
Cdd:smart00194 255 RAILE 259
Y_phosphatase pfam00102
Protein-tyrosine phosphatase;
136-433 3.90e-36

Protein-tyrosine phosphatase;


Pssm-ID: 459674 [Multi-domain]  Cd Length: 234  Bit Score: 133.52  E-value: 3.90e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71991025   136 LSKNRSKNHKLNDNTRVILSPEntensrtDPPDTYINASHIKFDNSQKEFIVTQYPLPDTVRDFWRMVSIMKVTQIVtif 215
Cdd:pfam00102   2 LEKNRYKDVLPYDHTRVKLTGD-------PGPSDYINASYIDGYKKPKKYIATQGPLPNTVEDFWRMVWEEKVTIIV--- 71

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71991025   216 epqtdeaieefrnptltlaapaptstMTTiggfpvpigqiahnrDQIQGQSIRCEsnvhrsSFFPLETDHYMNLKGWLIN 295
Cdd:pfam00102  72 --------------------------MLT---------------ELEEKGREKCA------QYWPEEEGESLEYGDFTVT 104

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71991025   296 TRRVTVDhrNKGWMnKYTVEVVAEGCSEATFAKVYNCTTWPWKKYPDDEKKVLALVRAPYKDTSTSlianleKLAPIVVM 375
Cdd:pfam00102 105 LKKEKED--EKDYT-VRTLEVSNGGSEETRTVKHFHYTGWPDHGVPESPNSLLDLLRKVRKSSLDG------RSGPIVVH 175

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 71991025   376 CDLGLDRSATVVLTSIIIDQIIAGKTPDCDALFKKMRDQRAGVFTMSIFYTYAIRAAL 433
Cdd:pfam00102 176 CSAGIGRTGTFIAIDIALQQLEAEGEVDIFQIVKELRSQRPGMVQTLEQYIFLYDAIL 233
PTPc cd00047
catalytic domain of protein tyrosine phosphatases; Protein tyrosine phosphatases (PTP, EC 3.1. ...
 170-427 2.80e-31

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: 119.31  E-value: 2.80e-31
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71991025 170 YINASHIKFDNSQKEFIVTQYPLPDTVRDFWRMVSIMKVTQIVtifepqtdeaieefrnptltlaapaptstMTTiggfp 249
Cdd:cd00047   1 YINASYIDGYRGPKEYIATQGPLPNTVEDFWRMVWEQKVSVIV-----------------------------MLT----- 46

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71991025 250 vpigqiahnrDQIQGQSIRCESnvhrssFFPLETDHYMNLKGWLINTRRVtvdHRNKGWMnKYTVEVVAEGCSEATFAKV 329
Cdd:cd00047  47 ----------NLVEKGREKCER------YWPEEGGKPLEYGDITVTLVSE---EELSDYT-IRTLELSPKGCSESREVTH 106

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71991025 330 YNCTTWPWKKYPDDEKKVLALVRApykdtstSLIANLEKLAPIVVMCDLGLDRSATVVLTSIIIDQIIAGKTPDCDALFK 409
Cdd:cd00047 107 LHYTGWPDHGVPSSPEDLLALVRR-------VRKEARKPNGPIVVHCSAGVGRTGTFIAIDILLERLEAEGEVDVFEIVK 179

                       250
                ....*....|....*...
gi 71991025 410 KMRDQRAGVFTMSIFYTY 427
Cdd:cd00047 180 ALRKQRPGMVQTLEQYEF 197
PHA02742 PHA02742
protein tyrosine phosphatase; Provisional
 134-438 1.31e-12

protein tyrosine phosphatase; Provisional


Pssm-ID: 165109 [Multi-domain]  Cd Length: 303  Bit Score: 68.49  E-value: 1.31e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71991025  134 KSLSKNRSKNHKLNDNTRVILSPEntensrtDPPDTYINASHIKFDNSQKEFIVTQYPLPDTVRDFWRMVSIMKVTQIVT 213
Cdd:PHA02742  51 KNMKKCRYPDAPCFDRNRVILKIE-------DGGDDFINASYVDGHNAKGRFICTQAPLEETALDFWQAIFQDQVRVIVM 123

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71991025  214 IfepqtDEAIEEFRNPTLTLAAPAPTSTMTtiggfpvpigqiaHNRDQIQGQSIRcesnvhrsSFfpletdhymnlKGWL 293
Cdd:PHA02742 124 I-----TKIMEDGKEACYPYWMPHERGKAT-------------HGEFKIKTKKIK--------SF-----------RNYA 166

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71991025  294 INTRRVTvdHRNKGwmnkYTVEVvaegcseatfaKVYNCTTWPWKKYPDDEKKVLALVRAPYKDTSTSLI----ANLEKL 369
Cdd:PHA02742 167 VTNLCLT--DTNTG----ASLDI-----------KHFAYEDWPHGGLPRDPNKFLDFVLAVREADLKADVdikgENIVKE 229

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 71991025  370 APIVVMCDLGLDRSATVVLTSIIIDQIIAGKTPDCDALFKKMRDQRAGVFTMSIFYTYAIRAALFYMKI 438
Cdd:PHA02742 230 PPILVHCSAGLDRAGAFCAIDICISKYNERAIIPLLSIVRDLRKQRHNCLSLPQQYIFCYFIVLIFAKL 298
COG5599 COG5599
Protein tyrosine phosphatase [Signal transduction mechanisms];
128-419 1.25e-04

Protein tyrosine phosphatase [Signal transduction mechanisms];


Pssm-ID: 444335 [Multi-domain]  Cd Length: 282  Bit Score: 43.93  E-value: 1.25e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71991025 128 TSVEWEKsLSKNRSKNHKLNDNTRVILS-----PENTENSRTdPPDTYINASHIKFDNSQKeFIVTQYPLPDTVRDFWRM 202
Cdd:COG5599  20 LSTLTNE-LAPSHNDPQYLQNINGSPLNrfrdiQPYKETALR-ANLGYLNANYIQVIGNHR-YIATQYPLEEQLEDFFQM 96

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71991025 203 VsimkvtqivtifepqtdeaieeFRNPTLTLAAPAPTSTMTT-IGGFPVPIGQiahnrdqiQGQSIRCESNVHRSSFFPL 281
Cdd:COG5599  97 L----------------------FDNNTPVLVVLASDDEISKpKVKMPVYFRQ--------DGEYGKYEVSSELTESIQL 146

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71991025 282 ETDhymnlkgwlintrrVTVDhrnkgwmnkyTVEVVAEGCSEATFA-KVYNCTTWPWKKYPDDE--KKVLALVRAPYKdt 358
Cdd:COG5599 147 RDG--------------IEAR----------TYVLTIKGTGQKKIEiPVLHVKNWPDHGAISAEalKNLADLIDKKEK-- 200

                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 71991025 359 stslIANLEKLaPIVVMCDLGLDRSATVVLTSIIIDQIIAGKTPDCDA--LFKKMRDQRAGVF 419
Cdd:COG5599 201 ----IKDPDKL-LPVVHCRAGVGRTGTLIACLALSKSINALVQITLSVeeIVIDMRTSRNGGM 258
 
Name Accession Description Interval E-value
PTPc smart00194
Protein tyrosine phosphatase, catalytic domain;
111-434 2.02e-69

Protein tyrosine phosphatase, catalytic domain;


Pssm-ID: 214550 [Multi-domain]  Cd Length: 259  Bit Score: 221.76  E-value: 2.02e-69
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71991025    111 LSTYFDEHLAGYTPP-NFTSVEWEKSLSKNRSKNHKLNDNTRVILSPENTEnsrtdpPDTYINASHIKFDNSQKEFIVTQ 189
Cdd:smart00194   2 LEEEFEKLDRLKPDDeSCTVAAFPENRDKNRYKDVLPYDHTRVKLKPPPGE------GSDYINASYIDGPNGPKAYIATQ 75

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71991025    190 YPLPDTVRDFWRMVSIMKVTQIVTIFEPqtdeaIEEFRnptltlaapaptstmttiggfpvpigqiahnrdqiqgqsIRC 269
Cdd:smart00194  76 GPLPSTVEDFWRMVWEQKVTVIVMLTEL-----VEKGR---------------------------------------EKC 111

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71991025    270 ESnvhrssFFPLETDHYMNLKGWLINTRRVTvdhrNKGWMNKYTVEVVAEGCSEATFAKVYNCTTWPWKKYPDDEKKVLA 349
Cdd:smart00194 112 AQ------YWPDEEGEPLTYGDITVTLKSVE----KVDDYTIRTLEVTNTGCSETRTVTHYHYTNWPDHGVPESPESILD 181

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71991025    350 LVRAPYKDTSTSLianleklAPIVVMCDLGLDRSATVVLTSIIIDQIIAGKTPDCDALFKKMRDQRAGVFTMSIFYTYAI 429
Cdd:smart00194 182 LIRAVRKSQSTST-------GPIVVHCSAGVGRTGTFIAIDILLQQLEAGKEVDIFEIVKELRSQRPGMVQTEEQYIFLY 254


                   ....*
gi 71991025    430 RAALF 434
Cdd:smart00194 255 RAILE 259
Y_phosphatase pfam00102
Protein-tyrosine phosphatase;
136-433 3.90e-36

Protein-tyrosine phosphatase;


Pssm-ID: 459674 [Multi-domain]  Cd Length: 234  Bit Score: 133.52  E-value: 3.90e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71991025   136 LSKNRSKNHKLNDNTRVILSPEntensrtDPPDTYINASHIKFDNSQKEFIVTQYPLPDTVRDFWRMVSIMKVTQIVtif 215
Cdd:pfam00102   2 LEKNRYKDVLPYDHTRVKLTGD-------PGPSDYINASYIDGYKKPKKYIATQGPLPNTVEDFWRMVWEEKVTIIV--- 71

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71991025   216 epqtdeaieefrnptltlaapaptstMTTiggfpvpigqiahnrDQIQGQSIRCEsnvhrsSFFPLETDHYMNLKGWLIN 295
Cdd:pfam00102  72 --------------------------MLT---------------ELEEKGREKCA------QYWPEEEGESLEYGDFTVT 104

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71991025   296 TRRVTVDhrNKGWMnKYTVEVVAEGCSEATFAKVYNCTTWPWKKYPDDEKKVLALVRAPYKDTSTSlianleKLAPIVVM 375
Cdd:pfam00102 105 LKKEKED--EKDYT-VRTLEVSNGGSEETRTVKHFHYTGWPDHGVPESPNSLLDLLRKVRKSSLDG------RSGPIVVH 175

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 71991025   376 CDLGLDRSATVVLTSIIIDQIIAGKTPDCDALFKKMRDQRAGVFTMSIFYTYAIRAAL 433
Cdd:pfam00102 176 CSAGIGRTGTFIAIDIALQQLEAEGEVDIFQIVKELRSQRPGMVQTLEQYIFLYDAIL 233
PTPc cd00047
catalytic domain of protein tyrosine phosphatases; Protein tyrosine phosphatases (PTP, EC 3.1. ...
 170-427 2.80e-31

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: 119.31  E-value: 2.80e-31
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71991025 170 YINASHIKFDNSQKEFIVTQYPLPDTVRDFWRMVSIMKVTQIVtifepqtdeaieefrnptltlaapaptstMTTiggfp 249
Cdd:cd00047   1 YINASYIDGYRGPKEYIATQGPLPNTVEDFWRMVWEQKVSVIV-----------------------------MLT----- 46

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71991025 250 vpigqiahnrDQIQGQSIRCESnvhrssFFPLETDHYMNLKGWLINTRRVtvdHRNKGWMnKYTVEVVAEGCSEATFAKV 329
Cdd:cd00047  47 ----------NLVEKGREKCER------YWPEEGGKPLEYGDITVTLVSE---EELSDYT-IRTLELSPKGCSESREVTH 106

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71991025 330 YNCTTWPWKKYPDDEKKVLALVRApykdtstSLIANLEKLAPIVVMCDLGLDRSATVVLTSIIIDQIIAGKTPDCDALFK 409
Cdd:cd00047 107 LHYTGWPDHGVPSSPEDLLALVRR-------VRKEARKPNGPIVVHCSAGVGRTGTFIAIDILLERLEAEGEVDVFEIVK 179

                       250
                ....*....|....*...
gi 71991025 410 KMRDQRAGVFTMSIFYTY 427
Cdd:cd00047 180 ALRKQRPGMVQTLEQYEF 197
PTPc-KIM cd14547
catalytic domain of the kinase interaction motif (KIM) family of protein-tyrosine phosphatases; ...
 139-417 1.56e-19

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: 87.07  E-value: 1.56e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71991025 139 NRSKNHKLNDNTRVILsPENTEnsrtDPPDTYINASHIK-FDNSQKEFIVTQYPLPDTVRDFWRMVSIMKVTQIVTIfeP 217
Cdd:cd14547   1 NRYKTILPNEHSRVCL-PSVDD----DPLSSYINANYIRgYDGEEKAYIATQGPLPNTVADFWRMVWQEKTPIIVMI--T 73

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71991025 218 QTDEAIEEfrnptltLAAPAPTSTMTTIGGFpvpigqiahnrdQIQGQSIRcesnvhrssffplETDHYmnlkgwliNTR 297
Cdd:cd14547  74 NLTEAKEK-------CAQYWPEEENETYGDF------------EVTVQSVK-------------ETDGY--------TVR 113

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71991025 298 RVTVDHrnkgwmnkytvevvaegCSEATFAKVYNCTTWPWKKYPDDEKKVLALVRapykdTSTSLIANLEKLAPIVVMCD 377
Cdd:cd14547 114 KLTLKY-----------------GGEKRYLKHYWYTSWPDHKTPEAAQPLLSLVQ-----EVEEARQTEPHRGPIVVHCS 171

                       250       260       270       280
                ....*....|....*....|....*....|....*....|
gi 71991025 378 LGLDRSATVVLTSIIIDQIIAGKTPDCDALFKKMRDQRAG 417
Cdd:cd14547 172 AGIGRTGCFIATSIGCQQLREEGVVDVLGIVCQLRLDRGG 211
PTPc_DSPc smart00012
Protein tyrosine phosphatase, catalytic domain, undefined specificity; Protein tyrosine ...
 328-434 6.16e-18

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: 78.94  E-value: 6.16e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71991025    328 KVYNCTTWPWKKYPDDEKKVLALVRApykdtSTSLIANLEKLAPIVVMCDLGLDRSATVVLTSIIIDQIIAG-KTPDCDA 406
Cdd:smart00012   3 KHYHYTGWPDHGVPESPDSILELLRA-----VKKNLNQSESSGPVVVHCSAGVGRTGTFVAIDILLQQLEAEaGEVDIFD 77

                           90       100
                   ....*....|....*....|....*...
gi 71991025    407 LFKKMRDQRAGVFTMSIFYTYAIRAALF 434
Cdd:smart00012  78 TVKELRSQRPGMVQTEEQYLFLYRALLE 105
PTPc_motif smart00404
Protein tyrosine phosphatase, catalytic domain motif;
328-434 6.16e-18

Protein tyrosine phosphatase, catalytic domain motif;


Pssm-ID: 214649 [Multi-domain]  Cd Length: 105  Bit Score: 78.94  E-value: 6.16e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71991025    328 KVYNCTTWPWKKYPDDEKKVLALVRApykdtSTSLIANLEKLAPIVVMCDLGLDRSATVVLTSIIIDQIIAG-KTPDCDA 406
Cdd:smart00404   3 KHYHYTGWPDHGVPESPDSILELLRA-----VKKNLNQSESSGPVVVHCSAGVGRTGTFVAIDILLQQLEAEaGEVDIFD 77

                           90       100
                   ....*....|....*....|....*...
gi 71991025    407 LFKKMRDQRAGVFTMSIFYTYAIRAALF 434
Cdd:smart00404  78 TVKELRSQRPGMVQTEEQYLFLYRALLE 105
R3-PTPc cd14548
catalytic domain of R3 subfamily receptor-type tyrosine-protein phosphatases and similar ...
 148-415 6.89e-16

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: 76.62  E-value: 6.89e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71991025 148 DNTRVILSPENTensrtDPPDTYINASHIKFDNSQKEFIVTQYPLPDTVRDFWRMVSIMKVTQIVtifepqtdeaieefr 227
Cdd:cd14548   9 DHSRVKLIPINE-----EEGSDYINANYIPGYNSPREFIATQGPLPGTKDDFWRMVWEQNSHTIV--------------- 68

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71991025 228 nptltlaapaptstMTTIGgfpvpigqiahnrdqIQGQSIRCEsnvhrsSFFPLETD--HYMNLkgwlintrrvTVDHRN 305
Cdd:cd14548  69 --------------MLTQC---------------MEKGRVKCD------HYWPFDQDpvYYGDI----------TVTMLS 103

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71991025 306 KGWMNKYTV-EVVAEGCSEATFAKVYNCTTWPWKKYPDDEKKVLALVRApYKDTstslIANLEKlaPIVVMCDLGLDRSA 384
Cdd:cd14548 104 ESVLPDWTIrEFKLERGDEVRSVRQFHFTAWPDHGVPEAPDSLLRFVRL-VRDY----IKQEKG--PTIVHCSAGVGRTG 176

                       250       260       270
                ....*....|....*....|....*....|.
gi 71991025 385 TVVLTSIIIDQIIAGKTPDCDALFKKMRDQR 415
Cdd:cd14548 177 TFIALDRLLQQIESEDYVDIFGIVYDLRKHR 207
PTPc-N7 cd14612
catalytic domain of tyrosine-protein phosphatase non-receptor type 7; Tyrosine-protein ...
 124-427 3.78e-14

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: 72.18  E-value: 3.78e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71991025 124 PPNFTS---VEWEKSLSKNRSKNHKLNDNTRVILSPENTENSRTDppdtYINASHIK-FDNSQKEFIVTQYPLPDTVRDF 199
Cdd:cd14612   1 PPNFVSpeeLDIPGHASKDRYKTILPNPQSRVCLRRAGSQEEEGS----YINANYIRgYDGKEKAYIATQGPMLNTVSDF 76

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71991025 200 WRMVSIMKVTQIVTIFEPQTdeaieefRNPTLTLAAPAPTSTmttiggfpvpigqiaHNRDQIQGQSIRcesnvhrssff 279
Cdd:cd14612  77 WEMVWQEECPIIVMITKLKE-------KKEKCVHYWPEKEGT---------------YGRFEIRVQDMK----------- 123

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71991025 280 plETDHYMnlkgwlinTRRVTVDHRnkgwmnkytvevvaegcSEATFAKVYNCTTWPWKKYPDDEKKVLALVR--APYKD 357
Cdd:cd14612 124 --ECDGYT--------IRDLTIQLE-----------------EESRSVKHYWFSSWPDHQTPESAGPLLRLVAevEESRQ 176

                       250       260       270       280       290       300       310
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71991025 358 TSTSlianlekLAPIVVMCDLGLDRSATVVLTSIIIDQIIAGKTPDCDALFKKMRDQRAGVFTMSIFYTY 427
Cdd:cd14612 177 TAAS-------PGPIVVHCSAGIGRTGCFIATSIGCQQLKDTGKVDILGIVCQLRLDRGGMIQTSEQYQF 239
R-PTP-N2 cd14610
PTP-like domain of receptor-type tyrosine-protein phosphatase N2; Receptor-type ...
 117-431 7.30e-14

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: 72.01  E-value: 7.30e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71991025 117 EHLAGY-TPPNFTSV-EWEKSLSKNRSKNHKLNDNTRVILSPENTEnSRTDppdtYINASHI-KFDNSQKEFIVTQYPLP 193
Cdd:cd14610  24 EALCAYqAEPNATNVaQREENVQKNRSLAVLPYDHSRIILKAENSH-SHSD----YINASPImDHDPRNPAYIATQGPLP 98

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71991025 194 DTVRDFWRMVSIMKVTQIVtIFEPQTDEAIEEFRNptltlAAPAPTSTMTTIggFPVpigqiahnrdQIQGQSIRCESNV 273
Cdd:cd14610  99 ATVADFWQMVWESGCVVIV-MLTPLAENGVKQCYH-----YWPDEGSNLYHI--YEV----------NLVSEHIWCEDFL 160

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71991025 274 HRSSFFP-LETDHymnlkgwlinTRRVTVDHrnkgwmnkytvevvaegcseatfakvynCTTWPWKKYPDDEKKVLAL-- 350
Cdd:cd14610 161 VRSFYLKnLQTNE----------TRTVTQFH----------------------------FLSWNDQGVPASTRSLLDFrr 202

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71991025 351 -VRAPYKDTStslianleklAPIVVMCDLGLDRSATVVLTSIIIDQIIAG-KTPDCDALFKKMRDQRAGVFTMSIFYTYA 428
Cdd:cd14610 203 kVNKCYRGRS----------CPIIVHCSDGAGRSGTYILIDMVLNKMAKGaKEIDIAATLEHLRDQRPGMVQTKEQFEFA 272


                ...
gi 71991025 429 IRA 431
Cdd:cd14610 273 LTA 275
R5-PTP-2 cd14550
PTP-like domain of R5 subfamily receptor-type tyrosine-protein phosphatases, repeat 2; The R5 ...
 170-226 1.35e-13

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: 69.27  E-value: 1.35e-13
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....*..
gi 71991025 170 YINASHIKFDNSQKEFIVTQYPLPDTVRDFWRMVSIMKVTQIVTIFEPQTDEAIEEF 226
Cdd:cd14550   1 YINASYLQGYRRSNEFIITQHPLEHTIKDFWQMIWDHNSQTIVMLTDNELNEDEPIY 57
PTPc-N11 cd14605
catalytic domain of tyrosine-protein phosphatase non-receptor type 11; Tyrosine-protein ...
 137-437 1.99e-13

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: 70.05  E-value: 1.99e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71991025 137 SKNRSKNHKLNDNTRVILspenTENSRTDPPDTYINASHI------KFDNSQ--KEFIVTQYPLPDTVRDFWRMVSIMKV 208
Cdd:cd14605   4 NKNRYKNILPFDHTRVVL----HDGDPNEPVSDYINANIImpefetKCNNSKpkKSYIATQGCLQNTVNDFWRMVFQENS 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71991025 209 TQIVtifepqtdeaieefrnptltlaapaptstMTTiggfpvpigqiahnRDQIQGQSiRCesnvhrSSFFPLEtdhyMN 288
Cdd:cd14605  80 RVIV-----------------------------MTT--------------KEVERGKS-KC------VKYWPDE----YA 105

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71991025 289 LKGW-LINTRRVTVDHRNKGWMNKYTVEVVAEGCSEATFAKvYNCTTWPWKKYPDDEKKVLA-LVRAPYKDTSTSlianl 366
Cdd:cd14605 106 LKEYgVMRVRNVKESAAHDYILRELKLSKVGQGNTERTVWQ-YHFRTWPDHGVPSDPGGVLDfLEEVHHKQESIM----- 179

                       250       260       270       280       290       300       310
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 71991025 367 eKLAPIVVMCDLGLDRSATVVLTSIIIDqIIAGKTPDCDALFKK----MRDQRAGVFTMSIFYTYAIRAALFYMK 437
Cdd:cd14605 180 -DAGPVVVHCSAGIGRTGTFIVIDILID-IIREKGVDCDIDVPKtiqmVRSQRSGMVQTEAQYRFIYMAVQHYIE 252
PHA02742 PHA02742
protein tyrosine phosphatase; Provisional
 134-438 1.31e-12

protein tyrosine phosphatase; Provisional


Pssm-ID: 165109 [Multi-domain]  Cd Length: 303  Bit Score: 68.49  E-value: 1.31e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71991025  134 KSLSKNRSKNHKLNDNTRVILSPEntensrtDPPDTYINASHIKFDNSQKEFIVTQYPLPDTVRDFWRMVSIMKVTQIVT 213
Cdd:PHA02742  51 KNMKKCRYPDAPCFDRNRVILKIE-------DGGDDFINASYVDGHNAKGRFICTQAPLEETALDFWQAIFQDQVRVIVM 123

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71991025  214 IfepqtDEAIEEFRNPTLTLAAPAPTSTMTtiggfpvpigqiaHNRDQIQGQSIRcesnvhrsSFfpletdhymnlKGWL 293
Cdd:PHA02742 124 I-----TKIMEDGKEACYPYWMPHERGKAT-------------HGEFKIKTKKIK--------SF-----------RNYA 166

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71991025  294 INTRRVTvdHRNKGwmnkYTVEVvaegcseatfaKVYNCTTWPWKKYPDDEKKVLALVRAPYKDTSTSLI----ANLEKL 369
Cdd:PHA02742 167 VTNLCLT--DTNTG----ASLDI-----------KHFAYEDWPHGGLPRDPNKFLDFVLAVREADLKADVdikgENIVKE 229

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 71991025  370 APIVVMCDLGLDRSATVVLTSIIIDQIIAGKTPDCDALFKKMRDQRAGVFTMSIFYTYAIRAALFYMKI 438
Cdd:PHA02742 230 PPILVHCSAGLDRAGAFCAIDICISKYNERAIIPLLSIVRDLRKQRHNCLSLPQQYIFCYFIVLIFAKL 298
R5-PTPc-1 cd14549
catalytic domain of R5 subfamily receptor-type tyrosine-protein phosphatases, repeat 1; The R5 ...
 170-415 1.49e-12

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: 66.61  E-value: 1.49e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71991025 170 YINASHIKFDNSQKEFIVTQYPLPDTVRDFWRMVSIMKVTQIVTI-------------FEPQtdEAIEEFRNPTLTLaap 236
Cdd:cd14549   1 YINANYVDGYNKARAYIATQGPLPSTFDDFWRMVWEQNSAIIVMItnlvergrrkcdqYWPK--EGTETYGNIQVTL--- 75

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71991025 237 aptstmttiggfpvpigqiahnrdqiqgqsircESNVHRSSFfpletdhymnlkgwliNTRRVTVDHRNKGWMNkytvev 316
Cdd:cd14549  76 ---------------------------------LSTEVLATY----------------TVRTFSLKNLKLKKVK------ 100

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71991025 317 vaeGCSEATFAKVYNCTTWPWKKYPDDEKKVLALVRapykdtsTSLIANLEKLAPIVVMCDLGLDRSATVVLTSIIIDQI 396
Cdd:cd14549 101 ---GRSSERVVYQYHYTQWPDHGVPDYTLPVLSFVR-------KSSAANPPGAGPIVVHCSAGVGRTGTYIVIDSMLQQI 170

                       250
                ....*....|....*....
gi 71991025 397 IAGKTPDCDALFKKMRDQR 415
Cdd:cd14549 171 QDKGTVNVFGFLKHIRTQR 189
PTPc-N5 cd14613
catalytic domain of tyrosine-protein phosphatase non-receptor type 5; Tyrosine-protein ...
 138-418 3.14e-12

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: 66.42  E-value: 3.14e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71991025 138 KNRSKNHKLNDNTRVILSPENTEnsrtDPPDTYINASHIK-FDNSQKEFIVTQYPLPDTVRDFWRMVSIMKVTQIVTIFE 216
Cdd:cd14613  28 KNRYKTILPNPHSRVCLTSPDQD----DPLSSYINANYIRgYGGEEKVYIATQGPTVNTVGDFWRMVWQERSPIIVMITN 103

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71991025 217 pqtdeaIEEfRNPTLTLAAPAptsTMTTIGGFPVPIGQIAHNRDqiqgqsircesnvHRSSFFPLETDhymnlkgwlint 296
Cdd:cd14613 104 ------IEE-MNEKCTEYWPE---EQVTYEGIEITVKQVIHADD-------------YRLRLITLKSG------------ 148

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71991025 297 rrvtvdhrnkgwmnkytvevvaegcSEATFAKVYNCTTWPWKKYPDDEKKVLALVRapykDTSTSLIANLEKLAPIVVMC 376
Cdd:cd14613 149 -------------------------GEERGLKHYWYTSWPDQKTPDNAPPLLQLVQ----EVEEARQQAEPNCGPVIVHC 199

                       250       260       270       280
                ....*....|....*....|....*....|....*....|..
gi 71991025 377 DLGLDRSATVVLTSIIIDQIIAGKTPDCDALFKKMRDQRAGV 418
Cdd:cd14613 200 SAGIGRTGCFIATSICCKQLRNEGVVDILRTTCQLRLDRGGM 241
PTPc-N11_6 cd14544
catalytic domain of tyrosine-protein phosphatase non-receptor type 11 and type 6; ...
 138-437 3.36e-12

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: 66.33  E-value: 3.36e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71991025 138 KNRSKNHKLNDNTRVILspenTENSRTDPPDTYINASHIKFDNSQ-------KEFIVTQYPLPDTVRDFWRMVSIMKVTQ 210
Cdd:cd14544   4 KNRYKNILPFDHTRVIL----KDRDPNVPGSDYINANYIRNENEGpttdenaKTYIATQGCLENTVSDFWSMVWQENSRV 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71991025 211 IVTifepqTDEAIEEFRNPTltlaapaptstmttiggfpVPIGQIAHNRDQIQGQSIRCESNVHRSSFfpletdhymnlk 290
Cdd:cd14544  80 IVM-----TTKEVERGKNKC-------------------VRYWPDEGMQKQYGPYRVQNVSEHDTTDY------------ 123

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71991025 291 gwlinTRRvtvdhrnkgwmnKYTVEVVAEGCSEATFAKvYNCTTWPWKKYPDDEKKVLALVRAPYKDTSTslianLEKLA 370
Cdd:cd14544 124 -----TLR------------ELQVSKLDQGDPIREIWH-YQYLSWPDHGVPSDPGGVLNFLEDVNQRQES-----LPHAG 180

                       250       260       270       280       290       300       310
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 71991025 371 PIVVMCDLGLDRSATVVLTSIIIDQIIAgKTPDCDALFKKM----RDQRAGVFTMSIFYTYAIRAALFYMK 437
Cdd:cd14544 181 PIVVHCSAGIGRTGTFIVIDMLLDQIKR-KGLDCDIDIQKTiqmvRSQRSGMVQTEAQYKFIYVAVAQYIE 250
PTPc-N14 cd14599
catalytic domain of tyrosine-protein phosphatase non-receptor type 14; Tyrosine-protein ...
 127-437 3.59e-12

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: 66.94  E-value: 3.59e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71991025 127 FTSVEWEKSLSKNRSKNHKLNDNTRVILSPeNTENsrtdpPDTYINASHIKFDNSQKE--FIVTQYPLPDTVRDFWRMVS 204
Cdd:cd14599  30 FTTATLPENAERNRIREVVPYEENRVELVP-TKEN-----NTGYINASHIKVTVGGEEwhYIATQGPLPHTCHDFWQMVW 103

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71991025 205 IMKVTQIVTIfepqtdEAIEEFRNPTLTLAAPAPTS--TMTTIGGFPVPigqiahnrdqiqgQSIRCESNVHRSSffPLE 282
Cdd:cd14599 104 EQGVNVIAMV------TAEEEGGRSKSHRYWPKLGSkhSSATYGKFKVT-------------TKFRTDSGCYATT--GLK 162

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71991025 283 TDHymnlkgwLINTRRVTVdhrnkgWMNKYtvevvaegcseatfakvyncTTWPWKKYPDDEKKVLAL---VRAPYKDTS 359
Cdd:cd14599 163 VKH-------LLSGQERTV------WHLQY--------------------TDWPDHGCPEEVQGFLSYleeIQSVRRHTN 209

                       250       260       270       280       290       300       310
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 71991025 360 TSLIANLEKLAPIVVMCDLGLDRSATVVLTSIIIDQIIAGKTPDCDALFKKMRDQRAGVFTMSIFYTYAIRAALFYMK 437
Cdd:cd14599 210 SMLDSTKNCNPPIVVHCSAGVGRTGVVILTELMIGCLEHNEKVEVPVMLRHLREQRMFMIQTIAQYKFVYQVLIQFLK 287
PTPc-N13 cd14597
catalytic domain of tyrosine-protein phosphatase non-receptor type 13; Tyrosine-protein ...
 138-434 3.60e-12

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: 66.01  E-value: 3.60e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71991025 138 KNRSKNHKLNDNTRVILSPENTensrtdppdtYINASHIKFDNSQKEF--IVTQYPLPDTVRDFWRMVSIMKVTQIVTIF 215
Cdd:cd14597   6 KNRYKNILPYDTTRVPLGDEGG----------YINASFIKMPVGDEEFvyIACQGPLPTTVADFWQMVWEQKSTVIAMMT 75

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71991025 216 EPQTDEAIEEFRNptltlaapaptstmttiggFPVPIGQIAHNRDQIQgqsircesnvhrssffpLETDHYMNLKGWLIn 295
Cdd:cd14597  76 QEVEGGKIKCQRY-------------------WPEILGKTTMVDNRLQ-----------------LTLVRMQQLKNFVI- 118

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71991025 296 tRRVTVDHRNKGwmnkytvevvaegcsEATFAKVYNCTTWPWKKYPDDEKKVLALVrapykdtstSLIANLEKLAPIVVM 375
Cdd:cd14597 119 -RVLELEDIQTR---------------EVRHITHLNFTAWPDHDTPSQPEQLLTFI---------SYMRHIHKSGPIITH 173

                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|....*....
gi 71991025 376 CDLGLDRSATVVLTSIIIDQIIAGKTPDCDALFKKMRDQRAGVFTMSIFYTYAIRAALF 434
Cdd:cd14597 174 CSAGIGRSGTLICIDVVLGLISKDLDFDISDIVRTMRLQRHGMVQTEDQYIFCYQVILY 232
R-PTPc-B cd14617
catalytic domain of receptor-type tyrosine-protein phosphatase B; Receptor-type ...
 139-212 7.03e-12

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: 64.94  E-value: 7.03e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71991025 139 NRSKNHKLNDNTRVILSpenteNSRTDPPDTYINASHIKFDNSQKEFIVTQYPLPDTVRDFWRMV------SIMKVTQIV 212
Cdd:cd14617   1 NRYNNILPYDSTRVKLS-----NVDDDPCSDYINASYIPGNNFRREYIATQGPLPGTKDDFWKMVweqnvhNIVMVTQCV 75
PTPc-N21_14 cd14540
catalytic domain of tyrosine-protein phosphatase non-receptor type 21 and type 14; ...
 170-428 7.36e-12

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: 64.79  E-value: 7.36e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71991025 170 YINASHIKFD--NSQKEFIVTQYPLPDTVRDFWRMVSIMKVTQIVTIFEPQTDEAIEEFRN-PTLTLAAPAptstmTTIG 246
Cdd:cd14540   1 YINASHITATvgGKQRFYIAAQGPLQNTVGDFWQMVWEQGVYLVVMVTAEEEGGREKCFRYwPTLGGEHDA-----LTFG 75

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71991025 247 GFPVpigqiahnrdqiqgqsircesnvhrSSFFPLETDHYMnlkgwlinTRRVTVDHrnkgwmnkytvevVAEGCSEATF 326
Cdd:cd14540  76 EYKV-------------------------STKFSVSSGCYT--------TTGLRVKH-------------TLSGQSRTVW 109

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71991025 327 AKVYncTTWPWKKYPDDEKKVLAL------VRApykdTSTSLIANLEKLAPIVVMCDLGLDRSATVVLTSIIIDQIIAGK 400
Cdd:cd14540 110 HLQY--TDWPDHGCPEDVSGFLDFleeinsVRR----HTNQDVAGHNRNPPTLVHCSAGVGRTGVVILADLMLYCLDHNE 183

                       250       260
                ....*....|....*....|....*...
gi 71991025 401 TPDCDALFKKMRDQRagvftMSIFYTYA 428
Cdd:cd14540 184 ELDIPRVLALLRHQR-----MLLVQTLA 206
PTPc-N18 cd14603
catalytic domain of tyrosine-protein phosphatase non-receptor type 18; Tyrosine-protein ...
 133-212 7.46e-12

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: 65.62  E-value: 7.46e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71991025 133 EKSLSKNRSKNHKLNDNTRVILSPEnTENSRTDppdtYINASHIKFDNSQKEFIVTQYPLPDTVRDFWRMVSIMKVTQIV 212
Cdd:cd14603  28 KENVKKNRYKDILPYDQTRVILSLL-QEEGHSD----YINANFIKGVDGSRAYIATQGPLSHTVLDFWRMIWQYGVKVIL 102
PTP-N23 cd14539
PTP-like domain of tyrosine-protein phosphatase non-receptor type 23; Tyrosine-protein ...
 170-415 1.01e-11

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: 63.94  E-value: 1.01e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71991025 170 YINASHIK-FDNSQKEFIVTQYPLPDTVRDFWRMVSIMKVTQIVtifepqtdeaieefrnptlTLAAPAPTSTMTTIGGF 248
Cdd:cd14539   1 YINASLIEdLTPYCPRFIATQAPLPGTAADFWLMVYEQQVSVIV-------------------MLVSEQENEKQKVHRYW 61

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71991025 249 PVPIGQiahnrDQIQGQSIRCESNVhRSSFFPLEtdhymnlkgwlintRRVTVDHRNKGWMNKYTvevvaegcsEATFak 328
Cdd:cd14539  62 PTERGQ-----ALVYGAITVSLQSV-RTTPTHVE--------------RIISIQHKDTRLSRSVV---------HLQF-- 110

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71991025 329 vyncTTWPWKKYPDDEKKVLALVrapyKDTSTSLIANLEKLAPIVVMCDLGLDRSATVVLTSIIIDQIIAGK-TPDCDAL 407
Cdd:cd14539 111 ----TTWPELGLPDSPNPLLRFI----EEVHSHYLQQRSLQTPIVVHCSSGVGRTGAFCLLYAAVQEIEAGNgIPDLPQL 182


                ....*...
gi 71991025 408 FKKMRDQR 415
Cdd:cd14539 183 VRKMRQQR 190
PTPc-N20_13 cd14538
catalytic domain of tyrosine-protein phosphatase non-receptor type 20 and type 13; ...
 170-417 1.02e-11

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: 63.93  E-value: 1.02e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71991025 170 YINASHIKFDNSQKEF--IVTQYPLPDTVRDFWRMVSIMKVTQIVTIFEPQTDEAIEEFRNptltlaapAPTSTMTTIgg 247
Cdd:cd14538   1 YINASHIRIPVGGDTYhyIACQGPLPNTTGDFWQMVWEQKSEVIAMVTQDVEGGKVKCHRY--------WPDSLNKPL-- 70

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71991025 248 fpvpigqIAHNRDQIQGQSircesnvhrssffpletdhYMNLKGWLIntRRVTVDHRNKGwmnkyTVEVVAEgcseatfa 327
Cdd:cd14538  71 -------ICGGRLEVSLEK-------------------YQSLQDFVI--RRISLRDKETG-----EVHHITH-------- 109

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71991025 328 kvYNCTTWPWKKYPddeKKVLALVRApykdtsTSLIANLEKLAPIVVMCDLGLDRSATVVLTSIIIDQIIAGKTPDCDAL 407
Cdd:cd14538 110 --LNFTTWPDHGTP---QSADPLLRF------IRYMRRIHNSGPIVVHCSAGIGRTGVLITIDVALGLIERDLPFDIQDI 178

                       250
                ....*....|
gi 71991025 408 FKKMRDQRAG 417
Cdd:cd14538 179 VKDLREQRQG 188
R-PTPc-H cd14619
catalytic domain of receptor-type tyrosine-protein phosphatase H; Receptor-type ...
 139-415 1.13e-11

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: 64.52  E-value: 1.13e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71991025 139 NRSKNHKLNDNTRVILSPentenSRTDPPDTYINASHIKFDNSQKEFIVTQYPLPDTVRDFWRMVSIMKVTQIVTIfepq 218
Cdd:cd14619   1 NRFRNVLPYDWSRVPLKP-----IHEEPGSDYINANYMPGYWSSQEFIATQGPLPQTVGDFWRMIWEQQSSTIVML---- 71

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71991025 219 tdeaieefrnptltlaapapTSTMttiggfpvpigqiahnrdqiQGQSIRCEsnvhrsSFFPLETD--HYMNLkgwlint 296
Cdd:cd14619  72 --------------------TNCM--------------------EAGRVKCE------HYWPLDYTpcTYGHL------- 98

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71991025 297 rRVTVDHRNK--GW-MNKYTVEVVAEgcSEATFAKVYNCTTWPWKKYPDDEKKVLA---LVRAPYKDTSTSlianleklA 370
Cdd:cd14619  99 -RVTVVSEEVmeNWtVREFLLKQVEE--QKTLSVRHFHFTAWPDHGVPSSTDTLLAfrrLLRQWLDQTMSG--------G 167

                       250       260       270       280
                ....*....|....*....|....*....|....*....|....*
gi 71991025 371 PIVVMCDLGLDRSATVVLTSIIIDQIIAGKTPDCDALFKKMRDQR 415
Cdd:cd14619 168 PTVVHCSAGVGRTGTLIALDVLLQQLQSEGLLGPFSFVQKMRENR 212
R-PTPc-J cd14615
catalytic domain of receptor-type tyrosine-protein phosphatase J; Receptor-type ...
 139-212 1.19e-11

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: 64.45  E-value: 1.19e-11
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 71991025 139 NRSKNHKLNDNTRVILSPENTensrtdPPDTYINASHIKFDNSQKEFIVTQYPLPDTVRDFWRMVSIMKVTQIV 212
Cdd:cd14615   1 NRYNNVLPYDISRVKLSVQSH------STDDYINANYMPGYNSKKEFIAAQGPLPNTVKDFWRMVWEKNVYAIV 68
PTPc-N9 cd14543
catalytic domain of tyrosine-protein phosphatase non-receptor type 9; Tyrosine-protein ...
 124-212 1.49e-11

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: 64.69  E-value: 1.49e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71991025 124 PP--NFTSVEWEKSLSKNRSKNHKLNDNTRVILSPENtENSRTDppdtYINASHIKFDNSQKEFIVTQYPLPDTVRDFWR 201
Cdd:cd14543  16 PPagTFLCSLAPANQEKNRYGDVLCLDQSRVKLPKRN-GDERTD----YINANFMDGYKQKNAYIATQGPLPKTYSDFWR 90

                        90
                ....*....|.
gi 71991025 202 MVSIMKVTQIV 212
Cdd:cd14543  91 MVWEQKVLVIV 101
R-PTPc-F-1 cd14626
catalytic domain of receptor-type tyrosine-protein phosphatase F, repeat 1; Receptor-type ...
 132-415 3.19e-11

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: 63.90  E-value: 3.19e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71991025 132 WEKS-LSKNRSKNHKLN----DNTRVILSPENTEnsrtdPPDTYINASHIKFDNSQKEFIVTQYPLPDTVRDFWRMVSIM 206
Cdd:cd14626  33 WENSnLEVNKPKNRYANviayDHSRVILTSVDGV-----PGSDYINANYIDGYRKQNAYIATQGPLPETLSDFWRMVWEQ 107

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71991025 207 KVTQIVTIFEpqtdeaIEEfrnptltlaapaptstmttiggfpvpigqiahnrdqiqgqsircESNVHRSSFFPLE-TDH 285
Cdd:cd14626 108 RTATIVMMTR------LEE--------------------------------------------KSRVKCDQYWPIRgTET 137

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71991025 286 YMNLKGWLINTRRVTVdhrnkgwmnkYTVEVVA---EGCSEATFAKVYNCTTWPWKKYPDDEKKVLALVRAPYKdtstsl 362
Cdd:cd14626 138 YGMIQVTLLDTVELAT----------YSVRTFAlykNGSSEKREVRQFQFMAWPDHGVPEYPTPILAFLRRVKA------ 201

                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|...
gi 71991025 363 iANLEKLAPIVVMCDLGLDRSATVVLTSIIIDQIIAGKTPDCDALFKKMRDQR 415
Cdd:cd14626 202 -CNPPDAGPMVVHCSAGVGRTGCFIVIDAMLERMKHEKTVDIYGHVTCMRSQR 253
PTPc-N6 cd14606
catalytic domain of tyrosine-protein phosphatase non-receptor type 6; Tyrosine-protein ...
 137-437 5.04e-11

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: 62.98  E-value: 5.04e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71991025 137 SKNRSKNHKLNDNTRVILspENTENSRtdPPDTYINASHIK-----FDNSQKEFIVTQYPLPDTVRDFWRMVSIMKVTQI 211
Cdd:cd14606  20 SKNRYKNILPFDHSRVIL--QGRDSNI--PGSDYINANYVKnqllgPDENAKTYIASQGCLEATVNDFWQMAWQENSRVI 95

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71991025 212 VtifepQTDEAIEEFRNPTLTLaapaptstmttiggFPVPIGQIAHNRdqiqgqsircesnvhrssfFPLETDHYMNLKG 291
Cdd:cd14606  96 V-----MTTREVEKGRNKCVPY--------------WPEVGMQRAYGP-------------------YSVTNCGEHDTTE 137

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71991025 292 WLINTRRVTVDHRNKG----WMNKYtvevvaegcseatfakvyncTTWPWKKYPDDEKKVLALVrapykDTSTSLIANLE 367
Cdd:cd14606 138 YKLRTLQVSPLDNGELireiWHYQY--------------------LSWPDHGVPSEPGGVLSFL-----DQINQRQESLP 192

                       250       260       270       280       290       300       310
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 71991025 368 KLAPIVVMCDLGLDRSATVVLTSIIIDQIIAgKTPDCDALFKK----MRDQRAGVFTMSIFYTYAIRAALFYMK 437
Cdd:cd14606 193 HAGPIIVHCSAGIGRTGTIIVIDMLMENIST-KGLDCDIDIQKtiqmVRAQRSGMVQTEAQYKFIYVAIAQFIE 265
R-PTPc-G-1 cd17667
catalytic domain of receptor-type tyrosine-protein phosphatase G, repeat 1; Receptor-type ...
 139-415 5.30e-11

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: 63.13  E-value: 5.30e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71991025 139 NRSKNHKLN----DNTRVILSPENTENSRTDppdTYINASHIKFDNSQKEFIVTQYPLPDTVRDFWRMV------SIMKV 208
Cdd:cd17667  27 NKHKNRYINilayDHSRVKLRPLPGKDSKHS---DYINANYVDGYNKAKAYIATQGPLKSTFEDFWRMIweqntgIIVMI 103

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71991025 209 TQIVTIFEPQTD-----EAIEEFRNPTLTLAAPAPTSTMTtiggfpvpigqiahnrdqIQGQSIRcesnvhrssffplet 283
Cdd:cd17667 104 TNLVEKGRRKCDqywptENSEEYGNIIVTLKSTKIHACYT------------------VRRFSIR--------------- 150

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71991025 284 dhymnlkgwliNTRRVTVDHRN-KGWMNKYTVevvaegcseatfaKVYNCTTWPWKKYPDDEKKVLALVRapykdtsTSL 362
Cdd:cd17667 151 -----------NTKVKKGQKGNpKGRQNERTV-------------IQYHYTQWPDMGVPEYALPVLTFVR-------RSS 199

                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|...
gi 71991025 363 IANLEKLAPIVVMCDLGLDRSATVVLTSIIIDQIIAGKTPDCDALFKKMRDQR 415
Cdd:cd17667 200 AARTPEMGPVLVHCSAGVGRTGTYIVIDSMLQQIKDKSTVNVLGFLKHIRTQR 252
R-PTPc-LAR-1 cd14553
catalytic domain of LAR family receptor-type tyrosine-protein phosphatases, repeat 1; The LAR ...
 133-212 7.05e-11

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: 62.03  E-value: 7.05e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71991025 133 EKSLSKNRSKNHKLNDNTRVILSP-ENTENSrtdppdTYINASHIKFDNSQKEFIVTQYPLPDTVRDFWRMVSIMKVTQI 211
Cdd:cd14553   1 EVNKPKNRYANVIAYDHSRVILQPiEGVPGS------DYINANYCDGYRKQNAYIATQGPLPETFGDFWRMVWEQRSATI 74


                .
gi 71991025 212 V 212
Cdd:cd14553  75 V 75
R-PTP-N cd14609
PTP-like domain of receptor-type tyrosine-protein phosphatase N; Receptor-type ...
 124-431 3.28e-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: 60.82  E-value: 3.28e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71991025 124 PPNFTSVEWEKSLSKNRSKNHKLNDNTRVILSPEnTENSRTDppdtYINASHI-KFDNSQKEFIVTQYPLPDTVRDFWRM 202
Cdd:cd14609  31 PNTCSTAQGEANVKKNRNPDFVPYDHARIKLKAE-SNPSRSD----YINASPIiEHDPRMPAYIATQGPLSHTIADFWQM 105

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71991025 203 VSIMKVTQIVtIFEPQTDEAIEEFRNptltlAAPAPTSTMTTIggFPVpigqiahnrdQIQGQSIRCESNVHRSSFFPle 282
Cdd:cd14609 106 VWENGCTVIV-MLTPLVEDGVKQCDR-----YWPDEGSSLYHI--YEV----------NLVSEHIWCEDFLVRSFYLK-- 165

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71991025 283 tdhymNLKGWliNTRRVTVDHrnkgwmnkytvevvaegcseatfakvynCTTWPWKKYPDDEKKVLAL---VRAPYKDTS 359
Cdd:cd14609 166 -----NVQTQ--ETRTLTQFH----------------------------FLSWPAEGIPSSTRPLLDFrrkVNKCYRGRS 210

                       250       260       270       280       290       300       310
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 71991025 360 tslianleklAPIVVMCDLGLDRSATVVLTSIIIDQIIAG-KTPDCDALFKKMRDQRAGVFTMSIFYTYAIRA 431
Cdd:cd14609 211 ----------CPIIVHCSDGAGRTGTYILIDMVLNRMAKGvKEIDIAATLEHVRDQRPGMVRTKDQFEFALTA 273
PTP_fungal cd18533
fungal protein tyrosine phosphatases; This subfamily contains Saccharomyces cerevisiae ...
 170-212 4.01e-10

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: 59.57  E-value: 4.01e-10
                        10        20        30        40
                ....*....|....*....|....*....|....*....|....
gi 71991025 170 YINASHIKFDN-SQKEFIVTQYPLPDTVRDFWRMVSIMKVTQIV 212
Cdd:cd18533   1 YINASYITLPGtSSKRYIATQGPLPATIGDFWKMIWQNNVGVIV 44
R-PTPc-O cd14614
catalytic domain of receptor-type tyrosine-protein phosphatase O; Receptor-type ...
 136-214 4.37e-10

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: 59.90  E-value: 4.37e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71991025 136 LSKNRSKNHKLN----DNTRV-ILSPENTENSrtdppdTYINASHIKFDNSQKEFIVTQYPLPDTVRDFWRMVSIMKVTQ 210
Cdd:cd14614   9 LPVNRCKNRYTNilpyDFSRVkLVSMHEEEGS------DYINANYIPGYNSPQEYIATQGPLPETRNDFWKMVLQQKSQI 82


                ....
gi 71991025 211 IVTI 214
Cdd:cd14614  83 IVML 86
R-PTPc-typeIIb-2 cd14556
PTP domain of type IIb (or R2B) subfamily receptor-type tyrosine-protein phosphatases, repeat ...
 170-212 4.39e-10

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: 59.34  E-value: 4.39e-10
                        10        20        30        40
                ....*....|....*....|....*....|....*....|...
gi 71991025 170 YINASHIKFDNSQKEFIVTQYPLPDTVRDFWRMVSIMKVTQIV 212
Cdd:cd14556   1 YINAALLDSYKQPAAFIVTQHPLPNTVTDFWRLVYDYGCTSIV 43
R-PTPc-U-1 cd14632
catalytic domain of receptor-type tyrosine-protein phosphatase U, repeat 1; Receptor-type ...
 170-394 6.16e-10

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: 58.91  E-value: 6.16e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71991025 170 YINASHIKFDNSQKEFIVTQYPLPDTVRDFWRMVSIMKVTQIVTIfepqtdeaieefrnptltlaapaptSTMTTIGgfp 249
Cdd:cd14632   1 YINANYIDGYHRSNHFIATQGPKQEMVYDFWRMVWQEHCSSIVMI-------------------------TKLVEVG--- 52

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71991025 250 vpigqiahnrdqiqgqSIRCesnvhrSSFFPLETDHYMNLKGWLINTRRVTvdhrnkgwmnKYTVEVVA---EGCSEATF 326
Cdd:cd14632  53 ----------------RVKC------SKYWPDDSDTYGDIKITLLKTETLA----------EYSVRTFAlerRGYSARHE 100

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 71991025 327 AKVYNCTTWPWKKYPDDEKKVLALVRApyKDTSTSLIAnleklAPIVVMCDLGLDRSATVVLTSIIID 394
Cdd:cd14632 101 VKQFHFTSWPEHGVPYHATGLLAFIRR--VKASTPPDA-----GPVVVHCSAGAGRTGCYIVLDVMLD 161
R-PTP-LAR-2 cd14554
PTP-like domain of the LAR family receptor-type tyrosine-protein phosphatases, repeat 2; The ...
 135-203 6.35e-10

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: 59.46  E-value: 6.35e-10
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 71991025 135 SLSKNRSKNHKLN----DNTRVILSP-ENTENSrtdppdTYINASHIKFDNSQKEFIVTQYPLPDTVRDFWRMV 203
Cdd:cd14554   2 NLPCNKFKNRLVNilpyESTRVCLQPiRGVEGS------DYINASFIDGYRQRGAYIATQGPLAETTEDFWRML 69
R-PTPc-S-1 cd14625
catalytic domain of receptor-type tyrosine-protein phosphatase S, repeat 1; Receptor-type ...
 132-415 9.84e-10

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: 59.34  E-value: 9.84e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71991025 132 WEKS-LSKNRSKNHKLN----DNTRVILSP-ENTENSrtdppdTYINASHIKFDNSQKEFIVTQYPLPDTVRDFWRMVSi 205
Cdd:cd14625  39 WEHSnLEVNKPKNRYANviayDHSRVILQPiEGIMGS------DYINANYIDGYRKQNAYIATQGPLPETFGDFWRMVW- 111

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71991025 206 mkvtqivtifepqtdeaieEFRNPTLTLaapaptstMTTIGgfpvpigqiahnrdqiQGQSIRCEsnvhrsSFFPLE-TD 284
Cdd:cd14625 112 -------------------EQRSATVVM--------MTKLE----------------EKSRIKCD------QYWPSRgTE 142

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71991025 285 HYMNLKGWLINTRRVTVdhrnkgwMNKYTVEVVAEGCSEATFAKVYNCTTWPWKKYPDDEKKVLALVRapykdtsTSLIA 364
Cdd:cd14625 143 TYGMIQVTLLDTIELAT-------FCVRTFSLHKNGSSEKREVRQFQFTAWPDHGVPEYPTPFLAFLR-------RVKTC 208

                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|.
gi 71991025 365 NLEKLAPIVVMCDLGLDRSATVVLTSIIIDQIIAGKTPDCDALFKKMRDQR 415
Cdd:cd14625 209 NPPDAGPIVVHCSAGVGRTGCFIVIDAMLERIKHEKTVDIYGHVTLMRSQR 259
PTPc-N12 cd14604
catalytic domain of tyrosine-protein phosphatase non-receptor type 12; Tyrosine-protein ...
 131-212 1.11e-09

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: 59.56  E-value: 1.11e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71991025 131 EWEKSLSKNRSKNHKLNDNTRVILSPEnTENSRTDppdtYINASHIKFDNSQKEFIVTQYPLPDTVRDFWRMVSIMKVTQ 210
Cdd:cd14604  53 EKEENVKKNRYKDILPFDHSRVKLTLK-TSSQDSD----YINANFIKGVYGPKAYIATQGPLANTVIDFWRMIWEYNVAI 127


                ..
gi 71991025 211 IV 212
Cdd:cd14604 128 IV 129
R-PTP-D-2 cd14628
PTP-like domain of receptor-type tyrosine-protein phosphatase D, repeat 2; Receptor-type ...
 138-436 2.76e-09

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: 58.20  E-value: 2.76e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71991025 138 KNRSKNHKLNDNTRVILSP-ENTENSrtdppdTYINASHIKFDNSQKEFIVTQYPLPDTVRDFWRMVSIMKVTQIVTIFE 216
Cdd:cd14628  55 KNRLVNIMPYESTRVCLQPiRGVEGS------DYINASFIDGYRQQKAYIATQGPLAETTEDFWRMLWEHNSTIVVMLTK 128

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71991025 217 pqtdeaIEEFRNPTLTLAAPAPTSTmttiggfpvpigqiahnrdqiqgqsircesnvhRSSFFPLETDHYMNLKGWLINT 296
Cdd:cd14628 129 ------LREMGREKCHQYWPAERSA---------------------------------RYQYFVVDPMAEYNMPQYILRE 169

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71991025 297 RRVTvDHRNkgwmnkytvevvaegcSEATFAKVYNCTTWPWKKYPDDEKKVLALVRAPYKDTStsliaNLEKLAPIVVMC 376
Cdd:cd14628 170 FKVT-DARD----------------GQSRTVRQFQFTDWPEQGVPKSGEGFIDFIGQVHKTKE-----QFGQDGPISVHC 227

                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|
gi 71991025 377 DLGLDRSATVVLTSIIIDQIIAGKTPDCDALFKKMRDQRAGVFTMSIFYTYAIRAALFYM 436
Cdd:cd14628 228 SAGVGRTGVFITLSIVLERMRYEGVVDIFQTVKMLRTQRPAMVQTEDQYQFCYRAALEYL 287
R-PTPc-E-1 cd14620
catalytic domain of receptor-type tyrosine-protein phosphatase E, repeat 1; Receptor-type ...
 147-433 3.02e-09

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: 57.26  E-value: 3.02e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71991025 147 NDNTRVILSPENTensrtDPPDTYINASHIKFDNSQKEFIVTQYPLPDTVRDFWRMVSIMKVTQIV--TIFEPQTDEAIE 224
Cdd:cd14620   7 YDHSRVILSQLDG-----IPCSDYINASYIDGYKEKNKFIAAQGPKQETVNDFWRMVWEQKSATIVmlTNLKERKEEKCY 81

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71991025 225 EFrnptltlaapAPTSTMTTIGGFPVPIGQIAhnrdqiqgqsircesnvhrssffpletdhymnlkgwlintrrVTVDHR 304
Cdd:cd14620  82 QY----------WPDQGCWTYGNIRVAVEDCV------------------------------------------VLVDYT 109

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71991025 305 nkgwMNKYTVEVVA-EGCSEATFAKVYNCTTWPWKKYPDDEKKVLALVRapyKDTSTsliaNLEKLAPIVVMCDLGLDRS 383
Cdd:cd14620 110 ----IRKFCIQPQLpDGCKAPRLVTQLHFTSWPDFGVPFTPIGMLKFLK---KVKSV----NPVHAGPIVVHCSAGVGRT 178

                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|
gi 71991025 384 ATVVLTSIIIDQIIAGKTPDCDALFKKMRDQRAGVFTMSIFYTYAIRAAL 433
Cdd:cd14620 179 GTFIVIDAMIDMMHAEQKVDVFEFVSRIRNQRPQMVQTDMQYSFIYQALL 228
R-PTP-C-2 cd14558
PTP-like domain of receptor-type tyrosine-protein phosphatase C, repeat 2; Receptor-type ...
 170-218 3.79e-09

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: 56.63  E-value: 3.79e-09
                        10        20        30        40
                ....*....|....*....|....*....|....*....|....*....
gi 71991025 170 YINASHIKFDNSQKEFIVTQYPLPDTVRDFWRMVSIMKVTQIVTIFEPQ 218
Cdd:cd14558   1 YINASFIDGYWGPKSLIATQGPLPDTIADFWQMIFQKKVKVIVMLTELK 49
PTPc-N1 cd14608
catalytic domain of tyrosine-protein phosphatase non-receptor type 1; Tyrosine-protein ...
 136-436 7.75e-09

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: 56.57  E-value: 7.75e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71991025 136 LSKNRSKNHKLN----DNTRVILSPENTEnsrtdppdtYINASHIKFDNSQKEFIVTQYPLPDTVRDFWRMVsimkvtqi 211
Cdd:cd14608  22 LPKNKNRNRYRDvspfDHSRIKLHQEDND---------YINASLIKMEEAQRSYILTQGPLPNTCGHFWEMV-------- 84

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71991025 212 vtiFEPQTdeaieefrnptltlaapaptstmttiggfpvpIGQIAHNRdQIQGQSIRCesnvhrSSFFPLETDHYMNLKG 291
Cdd:cd14608  85 ---WEQKS--------------------------------RGVVMLNR-VMEKGSLKC------AQYWPQKEEKEMIFED 122

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71991025 292 wlINTRRVTVDHRNKGWmnkYTV-EVVAEGCSEATFAKV--YNCTTWPWKKYPDDEKKVLALVRAPYKDTSTSlianlEK 368
Cdd:cd14608 123 --TNLKLTLISEDIKSY---YTVrQLELENLTTQETREIlhFHYTTWPDFGVPESPASFLNFLFKVRESGSLS-----PE 192

                       250       260       270       280       290       300       310
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 71991025 369 LAPIVVMCDLGLDRSATVVLTS---IIIDQIIAGKTPDCDALFKKMRDQRAGVF----TMSIFYTYAIRAALFYM 436
Cdd:cd14608 193 HGPVVVHCSAGIGRSGTFCLADtclLLMDKRKDPSSVDIKKVLLEMRKFRMGLIqtadQLRFSYLAVIEGAKFIM 267
R-PTPc-Q cd14616
catalytic domain of receptor-type tyrosine-protein phosphatase Q; Receptor-type ...
 139-203 1.02e-08

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: 55.68  E-value: 1.02e-08
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 71991025 139 NRSKNHKLNDNTRVILSPENTEnsrtdPPDTYINASHIKFDNSQKEFIVTQYPLPDTVRDFWRMV 203
Cdd:cd14616   1 NRFPNIKPYNNNRVKLIADAGV-----PGSDYINASYISGYLCPNEFIATQGPLPGTVGDFWRMV 60
PTPc-N1_2 cd14545
catalytic domain of tyrosine-protein phosphatase non-receptor type 1 and type 2; ...
 138-203 1.15e-08

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: 55.48  E-value: 1.15e-08
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 71991025 138 KNRSKNHKLNDNTRVILSPENTENSrtdppdtYINASHIKFDNSQKEFIVTQYPLPDTVRDFWRMV 203
Cdd:cd14545   1 LNRYRDRDPYDHDRSRVKLKQGDND-------YINASLVEVEEAKRSYILTQGPLPNTSGHFWQMV 59
R-PTP-S-2 cd14627
PTP-like domain of receptor-type tyrosine-protein phosphatase S, repeat 2; Receptor-type ...
 138-436 1.66e-08

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: 55.89  E-value: 1.66e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71991025 138 KNRSKNHKLNDNTRVILSP-ENTENSrtdppdTYINASHIKFDNSQKEFIVTQYPLPDTVRDFWRMVSIMKVTQIVTIFE 216
Cdd:cd14627  56 KNRLVNIMPYETTRVCLQPiRGVEGS------DYINASFIDGYRQQKAYIATQGPLAETTEDFWRMLWENNSTIVVMLTK 129

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71991025 217 pqtdeaIEEFRNPTLTLAAPAPTSTmttiggfpvpigqiahnrdqiqgqsircesnvhRSSFFPLETDHYMNLKGWLINT 296
Cdd:cd14627 130 ------LREMGREKCHQYWPAERSA---------------------------------RYQYFVVDPMAEYNMPQYILRE 170

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71991025 297 RRVTvDHRNkgwmnkytvevvaegcSEATFAKVYNCTTWPWKKYPDDEKKVLALVRAPYKDTStsliaNLEKLAPIVVMC 376
Cdd:cd14627 171 FKVT-DARD----------------GQSRTVRQFQFTDWPEQGVPKSGEGFIDFIGQVHKTKE-----QFGQDGPISVHC 228

                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|
gi 71991025 377 DLGLDRSATVVLTSIIIDQIIAGKTPDCDALFKKMRDQRAGVFTMSIFYTYAIRAALFYM 436
Cdd:cd14627 229 SAGVGRTGVFITLSIVLERMRYEGVVDIFQTVKMLRTQRPAMVQTEDEYQFCYQAALEYL 288
R-PTPc-T-1 cd14630
catalytic domain of receptor-type tyrosine-protein phosphatase T, repeat 1; Receptor-type ...
 138-433 1.78e-08

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: 55.03  E-value: 1.78e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71991025 138 KNRSKNHKLN----DNTRVILspentENSRTDPPDTYINASHIKFDNSQKEFIVTQYPLPDTVRDFWRMV------SIMK 207
Cdd:cd14630   2 ENRNKNRYGNiisyDHSRVRL-----QLLDGDPHSDYINANYIDGYHRPRHYIATQGPMQETVKDFWRMIwqensaSVVM 76

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71991025 208 VTQIVTIfepqtdeaieefrnptltlaapaptstmttiggfpvpigqiahnrdqiqgQSIRCesnvhrSSFFPLETDHYM 287
Cdd:cd14630  77 VTNLVEV--------------------------------------------------GRVKC------VRYWPDDTEVYG 100

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71991025 288 NLKGWLINTRRVTvdhrnKGWMNKYTVEvvAEGCSEATFAKVYNCTTWPWKKYPDDEKKVLALVRapykdtsTSLIANLE 367
Cdd:cd14630 101 DIKVTLIETEPLA-----EYVIRTFTVQ--KKGYHEIREIRQFHFTSWPDHGVPCYATGLLGFVR-------QVKFLNPP 166

                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 71991025 368 KLAPIVVMCDLGLDRSATVVLTSIIIDQIIAGKTPDCDALFKKMRDQRAGVFTMSIFYTYAIRAAL 433
Cdd:cd14630 167 DAGPIVVHCSAGAGRTGCFIAIDIMLDMAENEGVVDIFNCVRELRAQRVNMVQTEEQYVFVHDAIL 232
PHA02738 PHA02738
hypothetical protein; Provisional
 138-436 1.92e-08

hypothetical protein; Provisional


Pssm-ID: 222923 [Multi-domain]  Cd Length: 320  Bit Score: 55.70  E-value: 1.92e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71991025  138 KNRSKNHKLN----DNTRVILSpenTENSRTDppdtYINASHIKFDNSQKEFIVTQYPLPDTVRDFWRMVsIMKVTQIVT 213
Cdd:PHA02738  48 KNRKLNRYLDavcfDHSRVILP---AERNRGD----YINANYVDGFEYKKKFICGQAPTRQTCYDFYRML-WMEHVQIIV 119

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71991025  214 IfepqtdeaieefrnptltlaapaptstmttiggfpvpigqIAHNRDQIQGQSIRCESNVHRSSffpletdhyMNLKGWL 293
Cdd:PHA02738 120 M----------------------------------------LCKKKENGREKCFPYWSDVEQGS---------IRFGKFK 150

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71991025  294 INTRRV-TVDHRNKgwmnkyTVEVVAEGCSEATFAKVYNCTTWPWKKYPDDEKKVLAL---VRAPYKDTSTSLIANLEKL 369
Cdd:PHA02738 151 ITTTQVeTHPHYVK------STLLLTDGTSATQTVTHFNFTAWPDHDVPKNTSEFLNFvleVRQCQKELAQESLQIGHNR 224

                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71991025  370 A---PIVVMCDLGLDRSATVVLTSIIIDQIIAGKTPDCDALFKKMRDQRAGVFTMSIFYTYAIRAALFYM 436
Cdd:PHA02738 225 LqppPIVVHCNAGLGRTPCYCVVDISISRFDACATVSIPSIVSSIRNQRYYSLFIPFQYFFCYRAVKRYV 294
PTPc-N20 cd14596
catalytic domain of tyrosine-protein phosphatase non-receptor type 20; Tyrosine-protein ...
 170-417 2.85e-08

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: 53.98  E-value: 2.85e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71991025 170 YINASHIKFDNSQKE--FIVTQYPLPDTVRDFWRMVsimkvtqivtiFEPQTDeaieefrnptltlaapaptstmttigg 247
Cdd:cd14596   1 YINASYITMPVGEEElfYIATQGPLPSTIDDFWQMV-----------WENRSD--------------------------- 42

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71991025 248 fpvpigQIAHNRDQIQGQSIRCesnvHRssFFPLETDHYMNLKGWlintrRVTVDHRNK-GWMNKYTVEVVAEGCSEATF 326
Cdd:cd14596  43 ------VIAMMTREVERGKVKC----HR--YWPETLQEPMELENY-----QLRLENYQAlQYFIIRIIKLVEKETGENRL 105

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71991025 327 AKVYNCTTWPWKKYPDDEKKVLALVRAPYKDTSTslianleklAPIVVMCDLGLDRSATVVLTSIIIDQIIAGKTPDCDA 406
Cdd:cd14596 106 IKHLQFTTWPDHGTPQSSDQLVKFICYMRKVHNT---------GPIVVHCSAGIGRAGVLICVDVLLSLIEKDLSFNIKD 176

                       250
                ....*....|.
gi 71991025 407 LFKKMRDQRAG 417
Cdd:cd14596 177 IVREMRQQRYG 187
PHA02747 PHA02747
protein tyrosine phosphatase; Provisional
 116-436 3.02e-08

protein tyrosine phosphatase; Provisional


Pssm-ID: 165114 [Multi-domain]  Cd Length: 312  Bit Score: 55.01  E-value: 3.02e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71991025  116 DEHLAGYTPP---NFTSVEWEKSLSKNRSKNHKLNDNTRVILspenteNSRTDPPDTYINASHIKFDNSQKEFIVTQYPL 192
Cdd:PHA02747  29 DEHHQIILKPfdgLIANFEKPENQPKNRYWDIPCWDHNRVIL------DSGGGSTSDYIHANWIDGFEDDKKFIATQGPF 102

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71991025  193 PDTVRDFWRMVSIMKVTQIVTIfepqtdeaieefrnptltlaapapTSTMTTIGgfpvpigqiahnrdqiqgqsircESN 272
Cdd:PHA02747 103 AETCADFWKAVWQEHCSIIVML------------------------TPTKGTNG-----------------------EEK 135

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71991025  273 VHRssFFPLETDHYMNLKGWLINTRRVTVdhrnKGWMNKYTVEVVAEGCSEATFAKVYNCTTWPWKKYPDDEK---KVLA 349
Cdd:PHA02747 136 CYQ--YWCLNEDGNIDMEDFRIETLKTSV----RAKYILTLIEITDKILKDSRKISHFQCSEWFEDETPSDHPdfiKFIK 209

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71991025  350 LVRAPYKDTSTSLIANLEKLAPIVVMCDLGLDRSATVVLTSIIIDQIIAGKTPDCDALFKKMRDQRAGvfTMSIFYTYAI 429
Cdd:PHA02747 210 IIDINRKKSGKLFNPKDALLCPIVVHCSDGVGKTGIFCAVDICLNQLVKRKAICLAKTAEKIREQRHA--GIMNFDDYLF 287


                 ....*..
gi 71991025  430 RAALFYM 436
Cdd:PHA02747 288 IQPGYEV 294
R-PTPc-E-2 cd14622
catalytic domain of receptor-type tyrosine-protein phosphatase E, repeat 2; Receptor-type ...
 170-415 3.44e-08

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: 53.86  E-value: 3.44e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71991025 170 YINASHIKFDNSQKEFIVTQYPLPDTVRDFWRMVSIMKVTQIVTIFEPQTDEAIEEFRNptltlaapAPTSTMTTIGGFP 249
Cdd:cd14622   2 YINASFIDGYRQKDYFIATQGPLAHTVEDFWRMVWEWKCHTIVMLTELQEREQEKCVQY--------WPSEGSVTHGEIT 73

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71991025 250 VPIgqiahNRDQIqgqsirCESnvhrssffpletdhymnlkgwlINTRRVTVDHRNKgwmnkytvevvaegcSEATFAKV 329
Cdd:cd14622  74 IEI-----KNDTL------LET----------------------ISIRDFLVTYNQE---------------KQTRLVRQ 105

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71991025 330 YNCTTWPWKKYPDDEKKVLALVRAPYKDTSTSliANleklAPIVVMCDLGLDRSATVVLTSIIIDQIIAGKTPDCDALFK 409
Cdd:cd14622 106 FHFHGWPEIGIPAEGKGMIDLIAAVQKQQQQT--GN----HPIVVHCSAGAGRTGTFIALSNILERVKAEGLLDVFQTVK 179


                ....*.
gi 71991025 410 KMRDQR 415
Cdd:cd14622 180 SLRLQR 185
R-PTPc-V cd14618
catalytic domain of receptor-type tyrosine-protein phosphatase V; Receptor-type ...
 148-214 6.57e-08

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: 53.41  E-value: 6.57e-08
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 71991025 148 DNTRVILSPENTEnsrtdPPDTYINASHIKFDNSQKEFIVTQYPLPDTVRDFWRMVSIMKVTQIVTI 214
Cdd:cd14618  10 DHSRVRLSQLGGE-----PHSDYINANFIPGYTSPQEFIATQGPLKKTIEDFWRLVWEQQVCNIIML 71
R-PTP-G-2 cd17670
PTP-like domain of receptor-type tyrosine-protein phosphatase G, repeat 2; Receptor-type ...
 170-203 7.06e-08

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: 52.76  E-value: 7.06e-08
                        10        20        30
                ....*....|....*....|....*....|....
gi 71991025 170 YINASHIKFDNSQKEFIVTQYPLPDTVRDFWRMV 203
Cdd:cd17670   1 YINASYIMGYYRSNEFIITQHPLPHTTKDFWRMI 34
PTPc-N2 cd14607
catalytic domain of tyrosine-protein phosphatase non-receptor type 2; Tyrosine-protein ...
 137-214 7.81e-08

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: 53.43  E-value: 7.81e-08
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 71991025 137 SKNRSKNHKLNDNTRVILspENTENSrtdppdtYINASHIKFDNSQKEFIVTQYPLPDTVRDFWRMVSIMKVTQIVTI 214
Cdd:cd14607  26 NRNRYRDVSPYDHSRVKL--QNTEND-------YINASLVVIEEAQRSYILTQGPLPNTCCHFWLMVWQQKTKAVVML 94
R-PTPc-Z-1 cd17668
catalytic domain of receptor-type tyrosine-protein phosphatase Z, repeat 1; Receptor-type ...
 170-415 8.43e-08

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: 52.67  E-value: 8.43e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71991025 170 YINASHIKFDNSQKEFIVTQYPLPDTVRDFWRMVSIMKVTQIVTIfepqtDEAIEEFRNptltlaapaptstmttiggfp 249
Cdd:cd17668   1 YINANYVDGYNKPKAYIAAQGPLKSTAEDFWRMIWEHNVEVIVMI-----TNLVEKGRR--------------------- 54

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71991025 250 vpigqiahnrdqiqgqsiRCEsnvhrsSFFPLE-TDHYMNlkgWLINTRRVTV----DHRNKGWMNKYTVEVVAEGCSEA 324
Cdd:cd17668  55 ------------------KCD------QYWPADgSEEYGN---FLVTQKSVQVlayyTVRNFTLRNTKIKKGSQKGRPSG 107

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71991025 325 TFAKVYNCTTWPWKKYPDDEKKVLALVRapykdtsTSLIANLEKLAPIVVMCDLGLDRSATVVLTSIIIDQIIAGKTPDC 404
Cdd:cd17668 108 RVVTQYHYTQWPDMGVPEYTLPVLTFVR-------KASYAKRHAVGPVVVHCSAGVGRTGTYIVLDSMLQQIQHEGTVNI 180

                       250
                ....*....|.
gi 71991025 405 DALFKKMRDQR 415
Cdd:cd17668 181 FGFLKHIRSQR 191
PTPc-N21 cd14598
catalytic domain of tyrosine-protein phosphatase non-receptor type 21; Tyrosine-protein ...
 170-437 1.50e-07

catalytic domain of tyrosine-protein phosphatase non-receptor type 21; Tyrosine-protein phosphatase non-receptor type 21 (PTPN21), also called protein-tyrosine phosphatase D1, belongs to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. PTPN21 is a component of a multivalent scaffold complex nucleated by focal adhesion kinase (FAK) at specific intracellular sites. It promotes cytoskeleton events that induce cell adhesion and migration by modulating Src-FAK signaling. It can also selectively associate with and stimulate Tec family kinases and modulate Stat3 activation. Human PTPN21 may also play a pathologic role in gastrointestinal tract tumorigenesis. PTPN21 contains an N-terminal FERM domain and a C-terminal catalytic PTP domain, separated by a long intervening sequence.


Pssm-ID: 350446 [Multi-domain]  Cd Length: 220  Bit Score: 51.90  E-value: 1.50e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71991025 170 YINASHIKFDNSQKE--FIVTQYPLPDTVRDFWRMVSIMKVTQIVTIFEPQTDEAIEEFRN-PTLtlaapAPTSTMTTIG 246
Cdd:cd14598   1 YINASHIKVTVGGKEwdYIATQGPLQNTCQDFWQMVWEQGVAIIAMVTAEEEGGREKSFRYwPRL-----GSRHNTVTYG 75

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71991025 247 GFPVPIgqiahnrdqiqgqSIRCESNVHRSSffPLETDHymnlkgwLINTRRVTVdhrnkgWMNKYtvevvaegcseatf 326
Cdd:cd14598  76 RFKITT-------------RFRTDSGCYATT--GLKIKH-------LLTGQERTV------WHLQY-------------- 113

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71991025 327 akvyncTTWPWKKYPDDEKKVLAL------VRAPYKDTSTSLIANLeklaPIVVMCDLGLDRSATVVLTSIIIDQIIAGK 400
Cdd:cd14598 114 ------TDWPEHGCPEDLKGFLSYleeiqsVRRHTNSTIDPKSPNP----PVLVHCSAGVGRTGVVILSEIMIACLEHNE 183

                       250       260       270
                ....*....|....*....|....*....|....*..
gi 71991025 401 TPDCDALFKKMRDQRAGVFTMSIFYTYAIRAALFYMK 437
Cdd:cd14598 184 MLDIPRVLDMLRQQRMMMVQTLSQYTFVYKVLIQFLK 220
R-PTP-F-2 cd14629
PTP-like domain of receptor-type tyrosine-protein phosphatase F, repeat 2; Receptor-type ...
 138-436 1.53e-07

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: 52.81  E-value: 1.53e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71991025 138 KNRSKNHKLNDNTRVILSP-ENTENSrtdppdTYINASHIKFDNSQKEFIVTQYPLPDTVRDFWRMVSIMKVTQIVTIFE 216
Cdd:cd14629  56 KNRLVNIMPYELTRVCLQPiRGVEGS------DYINASFIDGYRQQKAYIATQGPLAETTEDFWRMLWEHNSTIVVMLTK 129

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71991025 217 pqtdeaIEEFRNPTLTLAAPAPTSTmttiggfpvpigqiahnrdqiqgqsircesnvhRSSFFPLETDHYMNLKGWLINT 296
Cdd:cd14629 130 ------LREMGREKCHQYWPAERSA---------------------------------RYQYFVVDPMAEYNMPQYILRE 170

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71991025 297 RRVTvDHRNkgwmnkytvevvaegcSEATFAKVYNCTTWPWKKYPDDEKKVLALVRAPYKDTStsliaNLEKLAPIVVMC 376
Cdd:cd14629 171 FKVT-DARD----------------GQSRTIRQFQFTDWPEQGVPKTGEGFIDFIGQVHKTKE-----QFGQDGPITVHC 228

                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|
gi 71991025 377 DLGLDRSATVVLTSIIIDQIIAGKTPDCDALFKKMRDQRAGVFTMSIFYTYAIRAALFYM 436
Cdd:cd14629 229 SAGVGRTGVFITLSIVLERMRYEGVVDMFQTVKTLRTQRPAMVQTEDQYQLCYRAALEYL 288
R-PTPc-A-E-2 cd14552
catalytic domain of receptor-type tyrosine-protein phosphatase A and E, repeat 2; ...
 170-415 1.68e-07

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: 51.50  E-value: 1.68e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71991025 170 YINASHIKFDNSQKEFIVTQYPLPDTVRDFWRMVSIMKVTQIVTIFEPQTDEAIEefrnptltLAAPAPTSTMTTIGGFP 249
Cdd:cd14552   1 YINASFIDGYRQKDAYIATQGPLDHTVEDFWRMIWEWKSCSIVMLTEIKERSQNK--------CAQYWPEDGSVSSGDIT 72

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71991025 250 VPIgqiahnRDQIQGQSIRcesnvhrssffpletdhymnlkgwlINTRRVTVDHRNKgwmnkytVEVVAEgcseatfakv 329
Cdd:cd14552  73 VEL------KDQTDYEDYT-------------------------LRDFLVTKGKGGS-------TRTVRQ---------- 104

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71991025 330 YNCTTWPWKKYPDDEKKVLALVRAPYKDTSTSliANleklAPIVVMCDLGLDRSATVVLTSIIIDQIIAGKTPDCDALFK 409
Cdd:cd14552 105 FHFHGWPEVGIPDNGKGMIDLIAAVQKQQQQS--GN----HPITVHCSAGAGRTGTFCALSTVLERVKAEGVLDVFQVVK 178


                ....*.
gi 71991025 410 KMRDQR 415
Cdd:cd14552 179 SLRLQR 184
R-PTP-Z-2 cd17669
catalytic domain of receptor-type tyrosine-protein phosphatase Z, repeat 2; Receptor-type ...
 170-226 1.73e-07

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: 51.53  E-value: 1.73e-07
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....*..
gi 71991025 170 YINASHIKFDNSQKEFIVTQYPLPDTVRDFWRMVSIMKVTQIVTIFEPQtDEAIEEF 226
Cdd:cd17669   1 YINASYIMGYYQSNEFIITQHPLLHTIKDFWRMIWDHNAQLIVMLPDGQ-NMAEDEF 56
R-PTPc-K-1 cd14631
catalytic domain of receptor-type tyrosine-protein phosphatase K, repeat 1; Receptor-type ...
 151-415 2.15e-07

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: 51.56  E-value: 2.15e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71991025 151 RVILSPenTENsrtDPPDTYINASHIKFDNSQKEFIVTQYPLPDTVRDFWRMVSIMKVTQIVTIfepqtdeaieefrnpt 230
Cdd:cd14631   1 RVILQP--VED---DPSSDYINANYIDGYQRPSHYIATQGPVHETVYDFWRMIWQEQSACIVMV---------------- 59

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71991025 231 ltlaapaptSTMTTIGgfpvpigqiahnrdqiqgqSIRCesnvhrSSFFPLETDHYMNLKgwlinTRRVTVDHRNKGWMN 310
Cdd:cd14631  60 ---------TNLVEVG-------------------RVKC------YKYWPDDTEVYGDFK-----VTCVEMEPLAEYVVR 100

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71991025 311 KYTVEvvAEGCSEATFAKVYNCTTWPWKKYPDDEKKVLALVRapykdtsTSLIANLEKLAPIVVMCDLGLDRSATVVLTS 390
Cdd:cd14631 101 TFTLE--RRGYNEIREVKQFHFTGWPDHGVPYHATGLLSFIR-------RVKLSNPPSAGPIVVHCSAGAGRTGCYIVID 171

                       250       260
                ....*....|....*....|....*
gi 71991025 391 IIIDQIIAGKTPDCDALFKKMRDQR 415
Cdd:cd14631 172 IMLDMAEREGVVDIYNCVKALRSRR 196
R-PTPc-D-1 cd14624
catalytic domain of receptor-type tyrosine-protein phosphatase D, repeat 1; Receptor-type ...
 132-415 3.27e-07

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: 51.66  E-value: 3.27e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71991025 132 WEKS-LSKNRSKNHKLN----DNTRVILSPentenSRTDPPDTYINASHIKFDNSQKEFIVTQYPLPDTVRDFWRMvsim 206
Cdd:cd14624  39 WEHSnLEVNKPKNRYANviayDHSRVLLSA-----IEGIPGSDYINANYIDGYRKQNAYIATQGALPETFGDFWRM---- 109

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71991025 207 kvtqivtifepqtdeaIEEFRNPTLTLaapaptstMTTIGgfpvpigqiahnrdqiQGQSIRCEsnvhrsSFFPLE-TDH 285
Cdd:cd14624 110 ----------------IWEQRSATVVM--------MTKLE----------------ERSRVKCD------QYWPSRgTET 143

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71991025 286 YMNLKGWLINTRRVTVdhrnkgwmnkYTVEVVA---EGCSEATFAKVYNCTTWPWKKYPDDEKKVLALVRapykdtsTSL 362
Cdd:cd14624 144 YGLIQVTLLDTVELAT----------YCVRTFAlykNGSSEKREVRQFQFTAWPDHGVPEHPTPFLAFLR-------RVK 206

                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|...
gi 71991025 363 IANLEKLAPIVVMCDLGLDRSATVVLTSIIIDQIIAGKTPDCDALFKKMRDQR 415
Cdd:cd14624 207 TCNPPDAGPMVVHCSAGVGRTGCFIVIDAMLERIKHEKTVDIYGHVTLMRAQR 259
PTPc-N22 cd14602
catalytic domain of tyrosine-protein phosphatase non-receptor type 22; Tyrosine-protein ...
 138-212 5.27e-07

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: 50.61  E-value: 5.27e-07
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 71991025 138 KNRSKNHKLNDNTRVILSPENTENSrtdppDTYINASHIKFDNSQKEFIVTQYPLPDTVRDFWRMVSIMKVTQIV 212
Cdd:cd14602   1 KNRYKDILPYDHSRVELSLITSDED-----SDYINANFIKGVYGPRAYIATQGPLSTTLLDFWRMIWEYSVLIIV 70
R-PTPc-K-2 cd14636
PTP domain of receptor-type tyrosine-protein phosphatase K, repeat 2; Receptor-type ...
 170-216 5.34e-07

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: 50.02  E-value: 5.34e-07
                        10        20        30        40
                ....*....|....*....|....*....|....*....|....*..
gi 71991025 170 YINASHIKFDNSQKEFIVTQYPLPDTVRDFWRMVSIMKVTQIVTIFE 216
Cdd:cd14636   1 YINAALMDSYRQPAAFIVTQHPLPNTVKDFWRLVYDYGCTSIVMLNE 47
R-PTPc-typeIIb-1 cd14555
catalytic domain of type IIb (or R2B) subfamily receptor-type tyrosine-protein phosphatases, ...
 170-415 7.87e-07

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: 49.53  E-value: 7.87e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71991025 170 YINASHIKFDNSQKEFIVTQYPLPDTVRDFWRMV------SIMKVTQIVTIfepqtdeaieefrnptltlaapaptstmt 243
Cdd:cd14555   1 YINANYIDGYHRPNHYIATQGPMQETVYDFWRMVwqensaSIVMVTNLVEV----------------------------- 51

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71991025 244 tiggfpvpigqiahnrdqiqgQSIRCesnvhrSSFFPLETDHYMNLKGWLINTRRVTvdhrnkgwmnKYTVEVVA---EG 320
Cdd:cd14555  52 ---------------------GRVKC------SRYWPDDTEVYGDIKVTLVETEPLA----------EYVVRTFAlerRG 94

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71991025 321 CSEATFAKVYNCTTWPWKKYPDDEKKVLALVRAPYKDTSTSlianlekLAPIVVMCDLGLDRSATVVLTSIIIDQIIAGK 400
Cdd:cd14555  95 YHEIREVRQFHFTGWPDHGVPYHATGLLGFIRRVKASNPPS-------AGPIVVHCSAGAGRTGCYIVIDIMLDMAEREG 167

                       250
                ....*....|....*
gi 71991025 401 TPDCDALFKKMRDQR 415
Cdd:cd14555 168 VVDIYNCVKELRSRR 182
PTPc-N22_18_12 cd14542
catalytic domain of tyrosine-protein phosphatase non-receptor type 22, type 18 and type 12; ...
 170-203 1.05e-06

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: 49.34  E-value: 1.05e-06
                        10        20        30
                ....*....|....*....|....*....|....
gi 71991025 170 YINASHIKFDNSQKEFIVTQYPLPDTVRDFWRMV 203
Cdd:cd14542   1 YINANFIKGVSGSKAYIATQGPLPNTVLDFWRMI 34
PTPc_plant_PTP1 cd17658
protein tyrosine phosphatase 1 from Arabidopsis thaliana and similar plant PTPs; Arabidopsis ...
 170-417 1.21e-06

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: 49.00  E-value: 1.21e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71991025 170 YINASHIKFDNSQK--EFIVTQYPLPDTVRDFWRMV------SIMKVTQIVTIFE--------PQTDEAIEEFRNPTLTL 233
Cdd:cd17658   1 YINASLVETPASESlpKFIATQGPLPHTFEDFWEMViqqrcpVIIMLTRLVDNYStakcadyfPAEENESREFGRISVTN 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71991025 234 AAPAPTSTMTTIGGFPVpigqiAHNRDQIQgqsircesnvhrssffPLETDHYMNLKgwlintrrvtvdhrnkgwmnkyt 313
Cdd:cd17658  81 KKLKHSQHSITLRVLEV-----QYIESEEP----------------PLSVLHIQYPE----------------------- 116

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71991025 314 vevvaegcseatfakvyncttWPWKKYPDDEKKVLALVRAPYkdtstsLIAnlEKLAPIVVMCDLGLDRSATVVLTSIII 393
Cdd:cd17658 117 ---------------------WPDHGVPKDTRSVRELLKRLY------GIP--PSAGPIVVHCSAGIGRTGAYCTIHNTI 167

                       250       260
                ....*....|....*....|....*....
gi 71991025 394 DQIIAGktpDCDAL-----FKKMRDQRAG 417
Cdd:cd17658 168 RRILEG---DMSAVdlsktVRKFRSQRIG 193
R-PTPc-M-1 cd14633
catalytic domain of receptor-type tyrosine-protein phosphatase M, repeat 1; Receptor-type ...
 115-433 1.37e-06

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: 49.66  E-value: 1.37e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71991025 115 FDEHLAGYTPPnFTSVEWEKSLSKNRSKNHKLNDNTRVILSP-ENTENSrtdppdTYINASHIKFDNSQKEFIVTQYPLP 193
Cdd:cd14633  21 YESFFEGQSAP-WDSAKKDENRMKNRYGNIIAYDHSRVRLQPiEGETSS------DYINGNYIDGYHRPNHYIATQGPMQ 93

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71991025 194 DTVRDFWRMVSIMKVTQIVTIfepqtdeaieefrnptltlaapaptSTMTTIGgfpvpigqiahnrdqiqgqSIRCesnv 273
Cdd:cd14633  94 ETIYDFWRMVWHENTASIIMV-------------------------TNLVEVG-------------------RVKC---- 125

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71991025 274 hrSSFFPLETDHYMNLKGWLINTRrvtvdhrnkgWMNKYTVEVVA---EGCSEATFAKVYNCTTWPWKKYPDDEKKVLAL 350
Cdd:cd14633 126 --CKYWPDDTEIYKDIKVTLIETE----------LLAEYVIRTFAvekRGVHEIREIRQFHFTGWPDHGVPYHATGLLGF 193

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71991025 351 VRAPYKDTSTSlianlekLAPIVVMCDLGLDRSATVVLTSIIIDQIIAGKTPDCDALFKKMRDQRAGVFTMSIFYTYAIR 430
Cdd:cd14633 194 VRQVKSKSPPN-------AGPLVVHCSAGAGRTGCFIVIDIMLDMAEREGVVDIYNCVRELRSRRVNMVQTEEQYVFIHD 266


                ...
gi 71991025 431 AAL 433
Cdd:cd14633 267 AIL 269
R-PTPc-T-2 cd14634
PTP domain of receptor-type tyrosine-protein phosphatase T, repeat 2; Receptor-type ...
 170-216 1.41e-06

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: 48.86  E-value: 1.41e-06
                        10        20        30        40
                ....*....|....*....|....*....|....*....|....*..
gi 71991025 170 YINASHIKFDNSQKEFIVTQYPLPDTVRDFWRMVSIMKVTQIVTIFE 216
Cdd:cd14634   1 YINAALMDSHKQPAAFIVTQHPLPNTVADFWRLVFDYNCSSVVMLNE 47
R-PTPc-M-2 cd14635
PTP domain of receptor-type tyrosine-protein phosphatase M, repeat 2; Receptor-type ...
 170-214 2.16e-06

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: 48.53  E-value: 2.16e-06
                        10        20        30        40
                ....*....|....*....|....*....|....*....|....*
gi 71991025 170 YINASHIKFDNSQKEFIVTQYPLPDTVRDFWRMVSIMKVTQIVTI 214
Cdd:cd14635   1 YINAALMDSYKQPSAFIVTQHPLPNTVKDFWRLVLDYHCTSIVML 45
PTPc-N3 cd14600
catalytic domain of tyrosine-protein phosphatase non-receptor type 3; Tyrosine-protein ...
 134-212 2.22e-06

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: 49.08  E-value: 2.22e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71991025 134 KSLSKNRSKNHKLNDNTRVILSPEntensrtdppDTYINASHIKFD----NSQKEFIVTQYPLPDTVRDFWRMVSIMKVT 209
Cdd:cd14600  39 QNMDKNRYKDVLPYDATRVVLQGN----------EDYINASYVNMEipsaNIVNKYIATQGPLPHTCAQFWQVVWEQKLS 108


                ...
gi 71991025 210 QIV 212
Cdd:cd14600 109 LIV 111
PHA02746 PHA02746
protein tyrosine phosphatase; Provisional
 134-221 4.96e-06

protein tyrosine phosphatase; Provisional


Pssm-ID: 165113 [Multi-domain]  Cd Length: 323  Bit Score: 48.49  E-value: 4.96e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71991025  134 KSLSKNRSKNHKLNDNTRVILS--------------PENTENSRTDPPDTYINASHIKFDNSQKEFIVTQYPLPDTVRDF 199
Cdd:PHA02746  50 ENLKKNRFHDIPCWDHSRVVINaheslkmfdvgdsdGKKIEVTSEDNAENYIHANFVDGFKEANKFICAQGPKEDTSEDF 129

                         90       100
                 ....*....|....*....|..
gi 71991025  200 WRMVSIMKVTQIVTIFEPQTDE 221
Cdd:PHA02746 130 FKLISEHESQVIVSLTDIDDDD 151
R-PTPc-C-1 cd14557
catalytic domain of receptor-type tyrosine-protein phosphatase C, repeat 1; Receptor-type ...
 170-415 5.74e-06

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: 47.13  E-value: 5.74e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71991025 170 YINASHIKFDNSQKEFIVTQYPLPDTVRDFWRMVSIMKVTQIVTIFEpqtdeaIEEFRNPTLTLAAPAPTSTMTTIGGFP 249
Cdd:cd14557   1 YINASYIDGFKEPRKYIAAQGPKDETVDDFWRMIWEQKSTVIVMVTR------CEEGNRNKCAQYWPSMEEGSRAFGDVV 74

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71991025 250 VPIGQIAHNRDQIqgqsircesnvhrssffpletdhymnlkgwlinTRRVTVDHRNKGWMNKYTVEVvaegcseatfakv 329
Cdd:cd14557  75 VKINEEKICPDYI---------------------------------IRKLNINNKKEKGSGREVTHI------------- 108

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71991025 330 yNCTTWPWKKYPDDEKKVLALVRapykdtSTSLIANLEKlAPIVVMCDLGLDRSATVVLTSIIIDQIIAGKTPDCDALFK 409
Cdd:cd14557 109 -QFTSWPDHGVPEDPHLLLKLRR------RVNAFNNFFS-GPIVVHCSAGVGRTGTYIGIDAMLEGLEAEGRVDVYGYVV 180


                ....*.
gi 71991025 410 KMRDQR 415
Cdd:cd14557 181 KLRRQR 186
R-PTP-N-N2 cd14546
PTP-like domain of receptor-type tyrosine-protein phosphatase-like N and N2; Receptor-type ...
 170-418 8.02e-06

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: 46.67  E-value: 8.02e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71991025 170 YINASHIKFDN-SQKEFIVTQYPLPDTVRDFWRMVSIMKVTQIVTIFEPQTDEAIEEFRNptltlaapAPTSTMTTIGGF 248
Cdd:cd14546   1 YINASTIYDHDpRNPAYIATQGPLPHTIADFWQMIWEQGCVVIVMLTRLQENGVKQCARY--------WPEEGSEVYHIY 72

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71991025 249 PVpigqiahnrdQIQGQSIRCESNVHRSsfFPLEtdhymNLKGWliNTRRVTVDHRnkgwmnkytvevvaegcseatfak 328
Cdd:cd14546  73 EV----------HLVSEHIWCDDYLVRS--FYLK-----NLQTS--ETRTVTQFHF------------------------ 109

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71991025 329 vyncTTWPWKKYPDDEKKVLALVRAPYKDTSTslianleKLAPIVVMCDLGLDRSATVVLTSIIIDQIIAG-KTPDCDAL 407
Cdd:cd14546 110 ----LSWPDEGIPASAKPLLEFRRKVNKSYRG-------RSCPIVVHCSDGAGRTGTYILIDMVLNRMAKGaKEIDIAAT 178

                       250
                ....*....|.
gi 71991025 408 FKKMRDQRAGV 418
Cdd:cd14546 179 LEHLRDQRPGM 189
R-PTPc-A-1 cd14621
catalytic domain of receptor-type tyrosine-protein phosphatase A, repeat 1; Receptor-type ...
 133-214 1.17e-05

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: 46.94  E-value: 1.17e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71991025 133 EKSLSKNRSKNHKLNDNTRVILSPentenSRTDPPDTYINASHIKFDNSQKEFIVTQYPLPDTVRDFWRMVSIMKVTQIV 212
Cdd:cd14621  50 EENKEKNRYVNILPYDHSRVHLTP-----VEGVPDSDYINASFINGYQEKNKFIAAQGPKEETVNDFWRMIWEQNTATIV 124


                ..
gi 71991025 213 TI 214
Cdd:cd14621 125 MV 126
R-PTPc-A-E-1 cd14551
catalytic domain of receptor-type tyrosine-protein phosphatase A and E, repeat 1; ...
 170-214 6.56e-05

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: 43.75  E-value: 6.56e-05
                        10        20        30        40
                ....*....|....*....|....*....|....*....|....*
gi 71991025 170 YINASHIKFDNSQKEFIVTQYPLPDTVRDFWRMVSIMKVTQIVTI 214
Cdd:cd14551   1 YINASYIDGYQEKNKFIAAQGPKDETVNDFWRMIWEQGSATIVMV 45
COG5599 COG5599
Protein tyrosine phosphatase [Signal transduction mechanisms];
128-419 1.25e-04

Protein tyrosine phosphatase [Signal transduction mechanisms];


Pssm-ID: 444335 [Multi-domain]  Cd Length: 282  Bit Score: 43.93  E-value: 1.25e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71991025 128 TSVEWEKsLSKNRSKNHKLNDNTRVILS-----PENTENSRTdPPDTYINASHIKFDNSQKeFIVTQYPLPDTVRDFWRM 202
Cdd:COG5599  20 LSTLTNE-LAPSHNDPQYLQNINGSPLNrfrdiQPYKETALR-ANLGYLNANYIQVIGNHR-YIATQYPLEEQLEDFFQM 96

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71991025 203 VsimkvtqivtifepqtdeaieeFRNPTLTLAAPAPTSTMTT-IGGFPVPIGQiahnrdqiQGQSIRCESNVHRSSFFPL 281
Cdd:COG5599  97 L----------------------FDNNTPVLVVLASDDEISKpKVKMPVYFRQ--------DGEYGKYEVSSELTESIQL 146

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71991025 282 ETDhymnlkgwlintrrVTVDhrnkgwmnkyTVEVVAEGCSEATFA-KVYNCTTWPWKKYPDDE--KKVLALVRAPYKdt 358
Cdd:COG5599 147 RDG--------------IEAR----------TYVLTIKGTGQKKIEiPVLHVKNWPDHGAISAEalKNLADLIDKKEK-- 200

                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 71991025 359 stslIANLEKLaPIVVMCDLGLDRSATVVLTSIIIDQIIAGKTPDCDA--LFKKMRDQRAGVF 419
Cdd:COG5599 201 ----IKDPDKL-LPVVHCRAGVGRTGTLIACLALSKSINALVQITLSVeeIVIDMRTSRNGGM 258
PTPc-N3_4 cd14541
catalytic domain of tyrosine-protein phosphatase non-receptor type 21 and type 14; ...
 170-212 1.79e-04

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: 42.70  E-value: 1.79e-04
                        10        20        30        40
                ....*....|....*....|....*....|....*....|....*..
gi 71991025 170 YINASHIKFDNSQKE----FIVTQYPLPDTVRDFWRMVSIMKVTQIV 212
Cdd:cd14541   2 YINANYVNMEIPGSGivnrYIAAQGPLPNTCADFWQMVWEQKSTLIV 48
R-PTPc-A-2 cd14623
catalytic domain of receptor-type tyrosine-protein phosphatase A, repeat 2; Receptor-type ...
 151-415 5.61e-04

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: 41.57  E-value: 5.61e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71991025 151 RVILSPENTENSrTDppdtYINASHIKFDNSQKEFIVTQYPLPDTVRDFWRMVSIMKVTQIVTIFEpqTDEAIEEfrnpt 230
Cdd:cd14623  12 RVIIPVKRGEEN-TD----YVNASFIDGYRQKDSYIASQGPLQHTIEDFWRMIWEWKSCSIVMLTE--LEERGQE----- 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71991025 231 lTLAAPAPTSTMTTIGGFPVPIgqiahNRDQiqgqsiRCESNVHRSSFfpletdhymnlkgwLINTRRvtvdhrnkgwmn 310
Cdd:cd14623  80 -KCAQYWPSDGSVSYGDITIEL-----KKEE------ECESYTVRDLL--------------VTNTRE------------ 121

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71991025 311 kytvevvaegcSEATFAKVYNCTTWPWKKYPDDEKKVLALVRAPYKDTSTSliANleklAPIVVMCDLGLDRSATVVLTS 390
Cdd:cd14623 122 -----------NKSRQIRQFHFHGWPEVGIPSDGKGMINIIAAVQKQQQQS--GN----HPITVHCSAGAGRTGTFCALS 184

                       250       260
                ....*....|....*....|....*
gi 71991025 391 IIIDQIIAGKTPDCDALFKKMRDQR 415
Cdd:cd14623 185 TVLERVKAEGILDVFQTVKSLRLQR 209
R-PTPc-U-2 cd14637
PTP domain of receptor-type tyrosine-protein phosphatase U, repeat 2; Receptor-type ...
 170-214 7.32e-04

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: 40.66  E-value: 7.32e-04
                        10        20        30        40
                ....*....|....*....|....*....|....*....|....*
gi 71991025 170 YINASHIKFDNSQKEFIVTQYPLPDTVRDFWRMVSIMKVTQIVTI 214
Cdd:cd14637   1 YINAALTDSYTRSAAFIVTLHPLQNTTTDFWRLVYDYGCTSVVML 45
 
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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