NCBI Conserved Domain Search

PTP-like domain of R5 subfamily receptor-type tyrosine-protein phosphatases, repeat 2; The R5 ...

1386-1586

4.55e-122

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: 380.51 E-value: 4.55e-122

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658117657 1386 YINASYIMGYQQSNEFIITQNPLPSTMKDFWKMIWDHSTQVVIALPDGlDLAEDECIYWPTKSQPIRFDTFTVTFMGEDH 1465
Cdd:cd14550      1 YINASYLQGYRRSNEFIITQHPLEHTIKDFWQMIWDHNSQTIVMLTDN-ELNEDEPIYWPTKEKPLECETFKVTLSGEDH 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658117657 1466 MCLSNEDMLIVQDFILEATQDDYVLEVRQYRAPRWPNPDGPISNTFELINIIKEESVSRDGPIVVHDKRGGNIAGTFCAL 1545
Cdd:cd14550     80 SCLSNEIRLIVRDFILESTQDDYVLEVRQFQCPSWPNPCSPIHTVFELINTVQEWAQQRDGPIVVHDRYGGVQAATFCAL 159

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|.
gi 1658117657 1546 MTLLHQLEMESSFDVYWVAKMINLMRPGIFTDIDQYQFLYK 1586
Cdd:cd14550    160 TTLHQQLEHESSVDVYQVAKLYHLMRPGVFTSKEDYQFLYK 200

fn3

pfam00041

Fibronectin type III domain;

73-155

1.17e-10

Fibronectin type III domain;

Pssm-ID: 394996 [Multi-domain] Cd Length: 85 Bit Score: 59.35 E-value: 1.17e-10

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658117657   73 SEPENVEADPYNYTSLLVTWERPRAVYDVgIERYLVSYQPVGDEDlPKNEYLTDGDQDvGAIIQDLSANTSYVVQVVAVC 152
Cdd:pfam00041    1 SAPSNLTVTDVTSTSLTVSWTPPPDGNGP-ITGYEVEYRPKNSGE-PWNEITVPGTTT-SVTLTGLKPGTEYEVRVQAVN 77


                   ...
gi 1658117657  153 ING 155
Cdd:pfam00041   78 GGG 80

alpha_CA super family

cl00012

Carbonic anhydrase alpha (vertebrate-like) group. Carbonic anhydrases (CAs) are ...

19-58

1.03e-06

Carbonic anhydrase alpha (vertebrate-like) group. Carbonic anhydrases (CAs) are zinc-containing enzymes that catalyze the reversible hydration of carbon dioxide in a two-step mechanism: a nucleophilic attack of a zinc-bound hydroxide ion on carbon dioxide, followed by the regeneration of the active site by ionization of the zinc-bound water molecule and removal of a proton from the active site. They are ubiquitous enzymes involved in fundamental processes like photosynthesis, respiration, pH homeostasis and ion transport. There are three evolutionary distinct groups - alpha, beta and gamma carbonic anhydrases - which show no significant sequence identity or structural similarity. Most alpha CAs are monomeric enzymes. The zinc ion is complexed by three histidine residues and a fourth conserved histidine plays a potential role in proton transfer.

The actual alignment was detected with superfamily member cd03122:

Pssm-ID: 469577 [Multi-domain] Cd Length: 253 Bit Score: 51.97 E-value: 1.03e-06

                           10        20        30        40
                   ....*....|....*....|....*....|....*....|
gi 1658117657   19 QLETFCEVMTMQQAGyVMLMDYLQNNFREQQLKFVGQVFS 58
Cdd:cd03122    215 QLEAFRELLTRRQDG-VMSGDYLPNNGRPQQPLGSRTVFS 253

Name

Accession

Description

Interval

E-value

R-PTPc-G-1

cd17667

catalytic domain of receptor-type tyrosine-protein phosphatase G, repeat 1; Receptor-type ...

1035-1303

9.73e-158

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: 480.30 E-value: 9.73e-158

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658117657 1035 ECYEEIQACTVDLGITADSSIHPENKNKNRYINILAYDHSRVKLSSSSDRNGWSADYINANYVDGFTQPKAYIATQGPLK 1114
Cdd:cd17667      3 EDFEEVQRCTADMNITAEHSNHPDNKHKNRYINILAYDHSRVKLRPLPGKDSKHSDYINANYVDGYNKAKAYIATQGPLK 82

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658117657 1115 SSMEDFWRMVWEQNASVIVMITNLVEKGRRKCDQYWPLDSQEEYGSFLVTLRSTKVLAYYTQRTFTLKNTRAKKGSQ--- 1191
Cdd:cd17667     83 STFEDFWRMIWEQNTGIIVMITNLVEKGRRKCDQYWPTENSEEYGNIIVTLKSTKIHACYTVRRFSIRNTKVKKGQKgnp 162

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658117657 1192 KEQTHERTVVQYHYTQWPDMGVPEYTLPVLTFVRKSSQANLGNMGPVVVHCSAGVGRTGTYIVLDSMLRQIKEQGTVNIL 1271
Cdd:cd17667    163 KGRQNERTVIQYHYTQWPDMGVPEYALPVLTFVRRSSAARTPEMGPVLVHCSAGVGRTGTYIVIDSMLQQIKDKSTVNVL 242

                          250       260       270
                   ....*....|....*....|....*....|..
gi 1658117657 1272 GFLKHIRTQRNYLVQTEEQYIFIHDALVEAIL 1303
Cdd:cd17667    243 GFLKHIRTQRNYLVQTEEQYIFIHDALLEAIL 274

R5-PTP-2

PTP-like domain of R5 subfamily receptor-type tyrosine-protein phosphatases, repeat 2; The R5 ...

1386-1586

4.55e-122

Pssm-ID: 350398 [Multi-domain] Cd Length: 200 Bit Score: 380.51 E-value: 4.55e-122

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658117657 1386 YINASYIMGYQQSNEFIITQNPLPSTMKDFWKMIWDHSTQVVIALPDGlDLAEDECIYWPTKSQPIRFDTFTVTFMGEDH 1465
Cdd:cd14550      1 YINASYLQGYRRSNEFIITQHPLEHTIKDFWQMIWDHNSQTIVMLTDN-ELNEDEPIYWPTKEKPLECETFKVTLSGEDH 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658117657 1466 MCLSNEDMLIVQDFILEATQDDYVLEVRQYRAPRWPNPDGPISNTFELINIIKEESVSRDGPIVVHDKRGGNIAGTFCAL 1545
Cdd:cd14550     80 SCLSNEIRLIVRDFILESTQDDYVLEVRQFQCPSWPNPCSPIHTVFELINTVQEWAQQRDGPIVVHDRYGGVQAATFCAL 159

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|.
gi 1658117657 1546 MTLLHQLEMESSFDVYWVAKMINLMRPGIFTDIDQYQFLYK 1586
Cdd:cd14550    160 TTLHQQLEHESSVDVYQVAKLYHLMRPGVFTSKEDYQFLYK 200

PTPc

Protein tyrosine phosphatase, catalytic domain;

1026-1300

3.65e-115

Protein tyrosine phosphatase, catalytic domain;

Pssm-ID: 214550 [Multi-domain] Cd Length: 259 Bit Score: 363.90 E-value: 3.65e-115

                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658117657  1026 FSQEFEILKECYEEIQACTVdlgitadsSIHPENKNKNRYINILAYDHSRVKLSsssDRNGWSADYINANYVDGFTQPKA 1105
Cdd:smart00194    2 LEEEFEKLDRLKPDDESCTV--------AAFPENRDKNRYKDVLPYDHTRVKLK---PPPGEGSDYINASYIDGPNGPKA 70

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658117657  1106 YIATQGPLKSSMEDFWRMVWEQNASVIVMITNLVEKGRRKCDQYWPLDSQE--EYGSFLVTLRSTKVLAYYTQRTFTLKN 1183
Cdd:smart00194   71 YIATQGPLPSTVEDFWRMVWEQKVTVIVMLTELVEKGREKCAQYWPDEEGEplTYGDITVTLKSVEKVDDYTIRTLEVTN 150

                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658117657  1184 TrakkgsqkEQTHERTVVQYHYTQWPDMGVPEYTLPVLTFVRKSSQANLGNMGPVVVHCSAGVGRTGTYIVLDSMLRQIK 1263
Cdd:smart00194  151 T--------GCSETRTVTHYHYTNWPDHGVPESPESILDLIRAVRKSQSTSTGPIVVHCSAGVGRTGTFIAIDILLQQLE 222

                           250       260       270
                    ....*....|....*....|....*....|....*..
gi 1658117657  1264 EQGTVNILGFLKHIRTQRNYLVQTEEQYIFIHDALVE 1300
Cdd:smart00194  223 AGKEVDIFEIVKELRSQRPGMVQTEEQYIFLYRAILE 259

Y_phosphatase

Protein-tyrosine phosphatase;

1059-1300

3.23e-111

Protein-tyrosine phosphatase;

Pssm-ID: 459674 [Multi-domain] Cd Length: 234 Bit Score: 351.93 E-value: 3.23e-111

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658117657 1059 NKNKNRYINILAYDHSRVKLSSSSDRNgwsaDYINANYVDGFTQPKAYIATQGPLKSSMEDFWRMVWEQNASVIVMITNL 1138
Cdd:pfam00102    1 NLEKNRYKDVLPYDHTRVKLTGDPGPS----DYINASYIDGYKKPKKYIATQGPLPNTVEDFWRMVWEEKVTIIVMLTEL 76

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658117657 1139 VEKGRRKCDQYWPLDSQE--EYGSFLVTLRSTK-VLAYYTQRTFTLKNTRAKkgsqkeqtHERTVVQYHYTQWPDMGVPE 1215
Cdd:pfam00102   77 EEKGREKCAQYWPEEEGEslEYGDFTVTLKKEKeDEKDYTVRTLEVSNGGSE--------ETRTVKHFHYTGWPDHGVPE 148

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658117657 1216 YTLPVLTFVRK-SSQANLGNMGPVVVHCSAGVGRTGTYIVLDSMLRQIKEQGTVNILGFLKHIRTQRNYLVQTEEQYIFI 1294
Cdd:pfam00102  149 SPNSLLDLLRKvRKSSLDGRSGPIVVHCSAGIGRTGTFIAIDIALQQLEAEGEVDIFQIVKELRSQRPGMVQTLEQYIFL 228


                   ....*.
gi 1658117657 1295 HDALVE 1300
Cdd:pfam00102  229 YDAILE 234

PTPc

Protein tyrosine phosphatase, catalytic domain;

1332-1589

5.08e-71

Protein tyrosine phosphatase, catalytic domain;

Pssm-ID: 214550 [Multi-domain] Cd Length: 259 Bit Score: 238.71 E-value: 5.08e-71

                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658117657  1332 LEKQFKMITQSNAKQCDYSAALKQCNRDKNRNSSLLPVERSRVHLSTTAGEISDYINASYIMGYQQSNEFIITQNPLPST 1411
Cdd:smart00194    2 LEEEFEKLDRLKPDDESCTVAAFPENRDKNRYKDVLPYDHTRVKLKPPPGEGSDYINASYIDGPNGPKAYIATQGPLPST 81

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658117657  1412 MKDFWKMIWDHSTQVVIALPDGLDL-AEDECIYWPTK-SQPIRFDTFTVTFMGEDHMclsneDMLIVQDFILEATQDDYV 1489
Cdd:smart00194   82 VEDFWRMVWEQKVTVIVMLTELVEKgREKCAQYWPDEeGEPLTYGDITVTLKSVEKV-----DDYTIRTLEVTNTGCSET 156

                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658117657  1490 LEVRQYRAPRWP---NPDGPISnTFELINIIKEESVSRDGPIVVHDKRGGNIAGTFCALMTLLHQLEMESSFDVYWVAKM 1566
Cdd:smart00194  157 RTVTHYHYTNWPdhgVPESPES-ILDLIRAVRKSQSTSTGPIVVHCSAGVGRTGTFIAIDILLQQLEAGKEVDIFEIVKE 235

                           250       260
                    ....*....|....*....|...
gi 1658117657  1567 INLMRPGIFTDIDQYQFLYKVIM 1589
Cdd:smart00194  236 LRSQRPGMVQTEEQYIFLYRAIL 258

Y_phosphatase

Protein-tyrosine phosphatase;

1357-1589

3.74e-64

Protein-tyrosine phosphatase;

Pssm-ID: 459674 [Multi-domain] Cd Length: 234 Bit Score: 217.88 E-value: 3.74e-64

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658117657 1357 NRDKNRNSSLLPVERSRVHLSTTAGEiSDYINASYIMGYQQSNEFIITQNPLPSTMKDFWKMIWDHSTQVVIALPDGLDL 1436
Cdd:pfam00102    1 NLEKNRYKDVLPYDHTRVKLTGDPGP-SDYINASYIDGYKKPKKYIATQGPLPNTVEDFWRMVWEEKVTIIVMLTELEEK 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658117657 1437 AEDEC-IYWPTKS-QPIRFDTFTVTFMGEDhmclSNEDMLIVQDFILEATQDDYVLEVRQYRAPRWPNPDGP--ISNTFE 1512
Cdd:pfam00102   80 GREKCaQYWPEEEgESLEYGDFTVTLKKEK----EDEKDYTVRTLEVSNGGSEETRTVKHFHYTGWPDHGVPesPNSLLD 155

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1658117657 1513 LINIIKEESV-SRDGPIVVHDKRGGNIAGTFCALMTLLHQLEMESSFDVYWVAKMINLMRPGIFTDIDQYQFLYKVIM 1589
Cdd:pfam00102  156 LLRKVRKSSLdGRSGPIVVHCSAGIGRTGTFIAIDIALQQLEAEGEVDIFQIVKELRSQRPGMVQTLEQYIFLYDAIL 233

PHA02738

hypothetical protein; Provisional

1031-1298

8.76e-53

hypothetical protein; Provisional

Pssm-ID: 222923 [Multi-domain] Cd Length: 320 Bit Score: 188.60 E-value: 8.76e-53

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658117657 1031 EILKECYEEIQACTVDLGITADSsihpENKNKNRYINILAYDHSRVKLSSSSDRngwsADYINANYVDGFTQPKAYIATQ 1110
Cdd:PHA02738    25 EVITREHQKVISEKVDGTFNAEK----KNRKLNRYLDAVCFDHSRVILPAERNR----GDYINANYVDGFEYKKKFICGQ 96

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658117657 1111 GPLKSSMEDFWRMVWEQNASVIVMITNLVEKGRRKCDQYWPLDSQEE--YGSFLVTLRSTKVLAYYTQRTFTLKNtrakk 1188
Cdd:PHA02738    97 APTRQTCYDFYRMLWMEHVQIIVMLCKKKENGREKCFPYWSDVEQGSirFGKFKITTTQVETHPHYVKSTLLLTD----- 171

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658117657 1189 GSQKEQtherTVVQYHYTQWPDMGVPEYTLPVLTFVRKSSQA-------------NLGNMGPVVVHCSAGVGRTGTYIVL 1255
Cdd:PHA02738   172 GTSATQ----TVTHFNFTAWPDHDVPKNTSEFLNFVLEVRQCqkelaqeslqighNRLQPPPIVVHCNAGLGRTPCYCVV 247

                          250       260       270       280
                   ....*....|....*....|....*....|....*....|...
gi 1658117657 1256 DSMLRQIKEQGTVNILGFLKHIRTQRNYLVQTEEQYIFIHDAL 1298
Cdd:PHA02738   248 DISISRFDACATVSIPSIVSSIRNQRYYSLFIPFQYFFCYRAV 290

COG5599

Protein tyrosine phosphatase [Signal transduction mechanisms];

1057-1294

1.11e-43

Protein tyrosine phosphatase [Signal transduction mechanisms];

Pssm-ID: 444335 [Multi-domain] Cd Length: 282 Bit Score: 161.03 E-value: 1.11e-43

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658117657 1057 PENKNKNRYINILAYDHSRVklsSSSDRngwsadYINANYVDGfTQPKAYIATQGPLKSSMEDFWRMVWEQNASVIVMIT 1136
Cdd:COG5599     40 INGSPLNRFRDIQPYKETAL---RANLG------YLNANYIQV-IGNHRYIATQYPLEEQLEDFFQMLFDNNTPVLVVLA 109

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658117657 1137 NLVE--KGRRKCDQYWPLDsqEEYGSFLVTLRSTKVLAYYTQ---RTFTLKntraKKGSQKEQtheRTVVQYHYTQWPDM 1211
Cdd:COG5599    110 SDDEisKPKVKMPVYFRQD--GEYGKYEVSSELTESIQLRDGieaRTYVLT----IKGTGQKK---IEIPVLHVKNWPDH 180

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658117657 1212 GVP--EYTLPVLTFVRKSSQANLGNMGPVVVHCSAGVGRTGTYIVLDSMLRQIKE--QGTVNILGFLKHIRTQRNY-LVQ 1286
Cdd:COG5599    181 GAIsaEALKNLADLIDKKEKIKDPDKLLPVVHCRAGVGRTGTLIACLALSKSINAlvQITLSVEEIVIDMRTSRNGgMVQ 260


                   ....*...
gi 1658117657 1287 TEEQYIFI 1294
Cdd:COG5599    261 TSEQLDVL 268

PHA02746

protein tyrosine phosphatase; Provisional

1350-1588

4.58e-26

protein tyrosine phosphatase; Provisional

Pssm-ID: 165113 [Multi-domain] Cd Length: 323 Bit Score: 110.89 E-value: 4.58e-26

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658117657 1350 SAALKQCNRDKNRNSSLLPVERSRVHLS--------------------TTAGEISDYINASYIMGYQQSNEFIITQNPLP 1409
Cdd:PHA02746    44 NHFLKKENLKKNRFHDIPCWDHSRVVINaheslkmfdvgdsdgkkievTSEDNAENYIHANFVDGFKEANKFICAQGPKE 123

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658117657 1410 STMKDFWKMIWDHSTQVVIALPDGLDLAEDECIYWPT-KSQPIRFDTFTVTFMGEDHMCLSNEDMLIVQDFILEATQddy 1488
Cdd:PHA02746   124 DTSEDFFKLISEHESQVIVSLTDIDDDDEKCFELWTKeEDSELAFGRFVAKILDIIEELSFTKTRLMITDKISDTSR--- 200

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658117657 1489 vlEVRQYRAPRWP---NPDGPiSNTFELINIIKEESV----------SRDGPIVVHDKRGGNIAGTFCALMTLLHQLEME 1555
Cdd:PHA02746   201 --EIHHFWFPDWPdngIPTGM-AEFLELINKVNEEQAelikqadndpQTLGPIVVHCSAGIGRAGTFCAIDNALEQLEKE 277

                          250       260       270
                   ....*....|....*....|....*....|...
gi 1658117657 1556 SSFDVYWVAKMINLMRPGIFTDIDQYQFLYKVI 1588
Cdd:PHA02746   278 KEVCLGEIVLKIRKQRHSSVFLPEQYAFCYKAL 310

fn3

pfam00041

Fibronectin type III domain;

73-155

1.17e-10

Fibronectin type III domain;

Pssm-ID: 394996 [Multi-domain] Cd Length: 85 Bit Score: 59.35 E-value: 1.17e-10

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658117657   73 SEPENVEADPYNYTSLLVTWERPRAVYDVgIERYLVSYQPVGDEDlPKNEYLTDGDQDvGAIIQDLSANTSYVVQVVAVC 152
Cdd:pfam00041    1 SAPSNLTVTDVTSTSLTVSWTPPPDGNGP-ITGYEVEYRPKNSGE-PWNEITVPGTTT-SVTLTGLKPGTEYEVRVQAVN 77


                   ...
gi 1658117657  153 ING 155
Cdd:pfam00041   78 GGG 80

FN3

smart00060

Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, ...

73-155

2.97e-08

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

Pssm-ID: 214495 [Multi-domain] Cd Length: 83 Bit Score: 52.62 E-value: 2.97e-08

                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658117657    73 SEPENVEADPYNYTSLLVTWERPRavyDVGIERYLVSYQPVGDEDLPKNEYLTDGDQDVGAIIQDLSANTSYVVQVVAVC 152
Cdd:smart00060    2 SPPSNLRVTDVTSTSVTLSWEPPP---DDGITGYIVGYRVEYREEGSEWKEVNVTPSSTSYTLTGLKPGTEYEFRVRAVN 78


                    ...
gi 1658117657   153 ING 155
Cdd:smart00060   79 GAG 81

FN3

cd00063

Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein ...

73-155

2.45e-07

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

Pssm-ID: 238020 [Multi-domain] Cd Length: 93 Bit Score: 50.19 E-value: 2.45e-07

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658117657   73 SEPENVEADPYNYTSLLVTWERPRAvYDVGIERYLVSYQPVGDEDLpkNEYLTDGDQDVGAIIQDLSANTSYVVQVVAVC 152
Cdd:cd00063      2 SPPTNLRVTDVTSTSVTLSWTPPED-DGGPITGYVVEYREKGSGDW--KEVEVTPGSETSYTLTGLKPGTEYEFRVRAVN 78


                   ...
gi 1658117657  153 ING 155
Cdd:cd00063     79 GGG 81

alpha_CARP_receptor_like

cd03122

Carbonic anhydrase alpha related protein, receptor_like subfamily. Carbonic anhydrase related ...

19-58

1.03e-06

Carbonic anhydrase alpha related protein, receptor_like subfamily. Carbonic anhydrase related proteins (CARPs) are sequence similar to carbonic anhydrases. Carbonic anhydrases are zinc-containing enzymes that catalyze the reversible hydration of carbon dioxide in a two-step mechanism. CARPs have lost conserved histidines involved in zinc binding and consequently their catalytic activity. This sub-family of carbonic anhydrase-related domains found in tyrosine phosphatase receptors may play a role in cell adhesion.

Pssm-ID: 239396 [Multi-domain] Cd Length: 253 Bit Score: 51.97 E-value: 1.03e-06

                           10        20        30        40
                   ....*....|....*....|....*....|....*....|
gi 1658117657   19 QLETFCEVMTMQQAGyVMLMDYLQNNFREQQLKFVGQVFS 58
Cdd:cd03122    215 QLEAFRELLTRRQDG-VMSGDYLPNNGRPQQPLGSRTVFS 253

Name

Accession

Description

Interval

E-value

R-PTPc-G-1

cd17667

catalytic domain of receptor-type tyrosine-protein phosphatase G, repeat 1; Receptor-type ...

1035-1303

9.73e-158

Pssm-ID: 350505 [Multi-domain] Cd Length: 274 Bit Score: 480.30 E-value: 9.73e-158

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658117657 1035 ECYEEIQACTVDLGITADSSIHPENKNKNRYINILAYDHSRVKLSSSSDRNGWSADYINANYVDGFTQPKAYIATQGPLK 1114
Cdd:cd17667      3 EDFEEVQRCTADMNITAEHSNHPDNKHKNRYINILAYDHSRVKLRPLPGKDSKHSDYINANYVDGYNKAKAYIATQGPLK 82

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658117657 1115 SSMEDFWRMVWEQNASVIVMITNLVEKGRRKCDQYWPLDSQEEYGSFLVTLRSTKVLAYYTQRTFTLKNTRAKKGSQ--- 1191
Cdd:cd17667     83 STFEDFWRMIWEQNTGIIVMITNLVEKGRRKCDQYWPTENSEEYGNIIVTLKSTKIHACYTVRRFSIRNTKVKKGQKgnp 162

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658117657 1192 KEQTHERTVVQYHYTQWPDMGVPEYTLPVLTFVRKSSQANLGNMGPVVVHCSAGVGRTGTYIVLDSMLRQIKEQGTVNIL 1271
Cdd:cd17667    163 KGRQNERTVIQYHYTQWPDMGVPEYALPVLTFVRRSSAARTPEMGPVLVHCSAGVGRTGTYIVIDSMLQQIKDKSTVNVL 242

                          250       260       270
                   ....*....|....*....|....*....|..
gi 1658117657 1272 GFLKHIRTQRNYLVQTEEQYIFIHDALVEAIL 1303
Cdd:cd17667    243 GFLKHIRTQRNYLVQTEEQYIFIHDALLEAIL 274

R-PTPc-Z-1

cd17668

catalytic domain of receptor-type tyrosine-protein phosphatase Z, repeat 1; Receptor-type ...

1091-1299

1.58e-138

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: 425.93 E-value: 1.58e-138

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658117657 1091 YINANYVDGFTQPKAYIATQGPLKSSMEDFWRMVWEQNASVIVMITNLVEKGRRKCDQYWPLDSQEEYGSFLVTLRSTKV 1170
Cdd:cd17668      1 YINANYVDGYNKPKAYIAAQGPLKSTAEDFWRMIWEHNVEVIVMITNLVEKGRRKCDQYWPADGSEEYGNFLVTQKSVQV 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658117657 1171 LAYYTQRTFTLKNTRAKKGSQKEQTHERTVVQYHYTQWPDMGVPEYTLPVLTFVRKSSQANLGNMGPVVVHCSAGVGRTG 1250
Cdd:cd17668     81 LAYYTVRNFTLRNTKIKKGSQKGRPSGRVVTQYHYTQWPDMGVPEYTLPVLTFVRKASYAKRHAVGPVVVHCSAGVGRTG 160

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*....
gi 1658117657 1251 TYIVLDSMLRQIKEQGTVNILGFLKHIRTQRNYLVQTEEQYIFIHDALV 1299
Cdd:cd17668    161 TYIVLDSMLQQIQHEGTVNIFGFLKHIRSQRNYLVQTEEQYVFIHDALV 209

R5-PTPc-1

cd14549

catalytic domain of R5 subfamily receptor-type tyrosine-protein phosphatases, repeat 1; The R5 ...

1091-1296

2.86e-137

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: 422.14 E-value: 2.86e-137

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658117657 1091 YINANYVDGFTQPKAYIATQGPLKSSMEDFWRMVWEQNASVIVMITNLVEKGRRKCDQYWPLDSQEEYGSFLVTLRSTKV 1170
Cdd:cd14549      1 YINANYVDGYNKARAYIATQGPLPSTFDDFWRMVWEQNSAIIVMITNLVERGRRKCDQYWPKEGTETYGNIQVTLLSTEV 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658117657 1171 LAYYTQRTFTLKNTRAKKGsqKEQTHERTVVQYHYTQWPDMGVPEYTLPVLTFVRKSSQANLGNMGPVVVHCSAGVGRTG 1250
Cdd:cd14549     81 LATYTVRTFSLKNLKLKKV--KGRSSERVVYQYHYTQWPDHGVPDYTLPVLSFVRKSSAANPPGAGPIVVHCSAGVGRTG 158

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*.
gi 1658117657 1251 TYIVLDSMLRQIKEQGTVNILGFLKHIRTQRNYLVQTEEQYIFIHD 1296
Cdd:cd14549    159 TYIVIDSMLQQIQDKGTVNVFGFLKHIRTQRNYLVQTEEQYIFIHD 204

R5-PTP-2

PTP-like domain of R5 subfamily receptor-type tyrosine-protein phosphatases, repeat 2; The R5 ...

1386-1586

4.55e-122

Pssm-ID: 350398 [Multi-domain] Cd Length: 200 Bit Score: 380.51 E-value: 4.55e-122

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658117657 1386 YINASYIMGYQQSNEFIITQNPLPSTMKDFWKMIWDHSTQVVIALPDGlDLAEDECIYWPTKSQPIRFDTFTVTFMGEDH 1465
Cdd:cd14550      1 YINASYLQGYRRSNEFIITQHPLEHTIKDFWQMIWDHNSQTIVMLTDN-ELNEDEPIYWPTKEKPLECETFKVTLSGEDH 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658117657 1466 MCLSNEDMLIVQDFILEATQDDYVLEVRQYRAPRWPNPDGPISNTFELINIIKEESVSRDGPIVVHDKRGGNIAGTFCAL 1545
Cdd:cd14550     80 SCLSNEIRLIVRDFILESTQDDYVLEVRQFQCPSWPNPCSPIHTVFELINTVQEWAQQRDGPIVVHDRYGGVQAATFCAL 159

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|.
gi 1658117657 1546 MTLLHQLEMESSFDVYWVAKMINLMRPGIFTDIDQYQFLYK 1586
Cdd:cd14550    160 TTLHQQLEHESSVDVYQVAKLYHLMRPGVFTSKEDYQFLYK 200

R-PTP-Z-2

cd17669

catalytic domain of receptor-type tyrosine-protein phosphatase Z, repeat 2; Receptor-type ...

1386-1589

1.76e-120

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: 376.26 E-value: 1.76e-120

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658117657 1386 YINASYIMGYQQSNEFIITQNPLPSTMKDFWKMIWDHSTQVVIALPDGLDLAEDECIYWPTKSQPIRFDTFTVTFMGEDH 1465
Cdd:cd17669      1 YINASYIMGYYQSNEFIITQHPLLHTIKDFWRMIWDHNAQLIVMLPDGQNMAEDEFVYWPNKDEPINCETFKVTLIAEEH 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658117657 1466 MCLSNEDMLIVQDFILEATQDDYVLEVRQYRAPRWPNPDGPISNTFELINIIKEESVSRDGPIVVHDKRGGNIAGTFCAL 1545
Cdd:cd17669     81 KCLSNEEKLIIQDFILEATQDDYVLEVRHFQCPKWPNPDSPISKTFELISIIKEEAANRDGPMIVHDEHGGVTAGTFCAL 160

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....
gi 1658117657 1546 MTLLHQLEMESSFDVYWVAKMINLMRPGIFTDIDQYQFLYKVIM 1589
Cdd:cd17669    161 TTLMHQLEKENSVDVYQVAKMINLMRPGVFTDIEQYQFLYKAIL 204

PTPc

Protein tyrosine phosphatase, catalytic domain;

1026-1300

3.65e-115

Protein tyrosine phosphatase, catalytic domain;

Pssm-ID: 214550 [Multi-domain] Cd Length: 259 Bit Score: 363.90 E-value: 3.65e-115

                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658117657  1026 FSQEFEILKECYEEIQACTVdlgitadsSIHPENKNKNRYINILAYDHSRVKLSsssDRNGWSADYINANYVDGFTQPKA 1105
Cdd:smart00194    2 LEEEFEKLDRLKPDDESCTV--------AAFPENRDKNRYKDVLPYDHTRVKLK---PPPGEGSDYINASYIDGPNGPKA 70

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658117657  1106 YIATQGPLKSSMEDFWRMVWEQNASVIVMITNLVEKGRRKCDQYWPLDSQE--EYGSFLVTLRSTKVLAYYTQRTFTLKN 1183
Cdd:smart00194   71 YIATQGPLPSTVEDFWRMVWEQKVTVIVMLTELVEKGREKCAQYWPDEEGEplTYGDITVTLKSVEKVDDYTIRTLEVTN 150

                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658117657  1184 TrakkgsqkEQTHERTVVQYHYTQWPDMGVPEYTLPVLTFVRKSSQANLGNMGPVVVHCSAGVGRTGTYIVLDSMLRQIK 1263
Cdd:smart00194  151 T--------GCSETRTVTHYHYTNWPDHGVPESPESILDLIRAVRKSQSTSTGPIVVHCSAGVGRTGTFIAIDILLQQLE 222

                           250       260       270
                    ....*....|....*....|....*....|....*..
gi 1658117657  1264 EQGTVNILGFLKHIRTQRNYLVQTEEQYIFIHDALVE 1300
Cdd:smart00194  223 AGKEVDIFEIVKELRSQRPGMVQTEEQYIFLYRAILE 259

Y_phosphatase

Protein-tyrosine phosphatase;

1059-1300

3.23e-111

Protein-tyrosine phosphatase;

Pssm-ID: 459674 [Multi-domain] Cd Length: 234 Bit Score: 351.93 E-value: 3.23e-111

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658117657 1059 NKNKNRYINILAYDHSRVKLSSSSDRNgwsaDYINANYVDGFTQPKAYIATQGPLKSSMEDFWRMVWEQNASVIVMITNL 1138
Cdd:pfam00102    1 NLEKNRYKDVLPYDHTRVKLTGDPGPS----DYINASYIDGYKKPKKYIATQGPLPNTVEDFWRMVWEEKVTIIVMLTEL 76

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658117657 1139 VEKGRRKCDQYWPLDSQE--EYGSFLVTLRSTK-VLAYYTQRTFTLKNTRAKkgsqkeqtHERTVVQYHYTQWPDMGVPE 1215
Cdd:pfam00102   77 EEKGREKCAQYWPEEEGEslEYGDFTVTLKKEKeDEKDYTVRTLEVSNGGSE--------ETRTVKHFHYTGWPDHGVPE 148

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658117657 1216 YTLPVLTFVRK-SSQANLGNMGPVVVHCSAGVGRTGTYIVLDSMLRQIKEQGTVNILGFLKHIRTQRNYLVQTEEQYIFI 1294
Cdd:pfam00102  149 SPNSLLDLLRKvRKSSLDGRSGPIVVHCSAGIGRTGTFIAIDIALQQLEAEGEVDIFQIVKELRSQRPGMVQTLEQYIFL 228


                   ....*.
gi 1658117657 1295 HDALVE 1300
Cdd:pfam00102  229 YDAILE 234

R-PTP-G-2

cd17670

PTP-like domain of receptor-type tyrosine-protein phosphatase G, repeat 2; Receptor-type ...

1386-1590

2.15e-109

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: 345.51 E-value: 2.15e-109

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658117657 1386 YINASYIMGYQQSNEFIITQNPLPSTMKDFWKMIWDHSTQVVIALPDGLDLAEDECIYWPTKSQPIRFDTFTVTFMGEDH 1465
Cdd:cd17670      1 YINASYIMGYYRSNEFIITQHPLPHTTKDFWRMIWDHNAQIIVMLPDNQGLAEDEFVYWPSREESMNCEAFTVTLISKDR 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658117657 1466 MCLSNEDMLIVQDFILEATQDDYVLEVRQYRAPRWPNPDGPISNTFELINIIKEESVSRDGPIVVHDKRGGNIAGTFCAL 1545
Cdd:cd17670     81 LCLSNEEQIIIHDFILEATQDDYVLEVRHFQCPKWPNPDAPISSTFELINVIKEEALTRDGPTIVHDEFGAVSAGTLCAL 160

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*
gi 1658117657 1546 MTLLHQLEMESSFDVYWVAKMINLMRPGIFTDIDQYQFLYKVIMS 1590
Cdd:cd17670    161 TTLSQQLENENAVDVYQVAKMINLMRPGVFTDIEQYQFLYKAMLS 205

R-PTPc-LAR-1

cd14553

catalytic domain of LAR family receptor-type tyrosine-protein phosphatases, repeat 1; The LAR ...

1059-1304

2.28e-109

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: 347.08 E-value: 2.28e-109

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658117657 1059 NKNKNRYINILAYDHSRVKLSSSSDRNGwsADYINANYVDGFTQPKAYIATQGPLKSSMEDFWRMVWEQNASVIVMITNL 1138
Cdd:cd14553      3 NKPKNRYANVIAYDHSRVILQPIEGVPG--SDYINANYCDGYRKQNAYIATQGPLPETFGDFWRMVWEQRSATIVMMTKL 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658117657 1139 VEKGRRKCDQYWPLDSQEEYGSFLVTLRSTKVLAYYTQRTFTLKntraKKGSqkeqTHERTVVQYHYTQWPDMGVPEYTL 1218
Cdd:cd14553     81 EERSRVKCDQYWPTRGTETYGLIQVTLLDTVELATYTVRTFALH----KNGS----SEKREVRQFQFTAWPDHGVPEHPT 152

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658117657 1219 PVLTFVRKSSQANLGNMGPVVVHCSAGVGRTGTYIVLDSMLRQIKEQGTVNILGFLKHIRTQRNYLVQTEEQYIFIHDAL 1298
Cdd:cd14553    153 PFLAFLRRVKACNPPDAGPIVVHCSAGVGRTGCFIVIDSMLERIKHEKTVDIYGHVTCLRAQRNYMVQTEDQYIFIHDAL 232


                   ....*.
gi 1658117657 1299 VEAILS 1304
Cdd:cd14553    233 LEAVTC 238

PTPc

cd00047

catalytic domain of protein tyrosine phosphatases; Protein tyrosine phosphatases (PTP, EC 3.1. ...

1091-1296

2.80e-95

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: 305.75 E-value: 2.80e-95

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658117657 1091 YINANYVDGFTQPKAYIATQGPLKSSMEDFWRMVWEQNASVIVMITNLVEKGRRKCDQYWPLDSQE--EYGSFLVTLRST 1168
Cdd:cd00047      1 YINASYIDGYRGPKEYIATQGPLPNTVEDFWRMVWEQKVSVIVMLTNLVEKGREKCERYWPEEGGKplEYGDITVTLVSE 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658117657 1169 KVLAYYTQRTFTLKNTRAKKgsqkeqthERTVVQYHYTQWPDMGVPEYTLPVLTFVRKSSQANLGNMGPVVVHCSAGVGR 1248
Cdd:cd00047     81 EELSDYTIRTLELSPKGCSE--------SREVTHLHYTGWPDHGVPSSPEDLLALVRRVRKEARKPNGPIVVHCSAGVGR 152

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*...
gi 1658117657 1249 TGTYIVLDSMLRQIKEQGTVNILGFLKHIRTQRNYLVQTEEQYIFIHD 1296
Cdd:cd00047    153 TGTFIAIDILLERLEAEGEVDVFEIVKALRKQRPGMVQTLEQYEFIYE 200

R-PTPc-F-1

cd14626

catalytic domain of receptor-type tyrosine-protein phosphatase F, repeat 1; Receptor-type ...

1021-1302

1.60e-93

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: 303.88 E-value: 1.60e-93

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658117657 1021 HDSNTFSQEFEilkecyeeiqacTVDLG--ITADSSIHPENKNKNRYINILAYDHSRVKLSSSSDRNGwsADYINANYVD 1098
Cdd:cd14626     13 NDGLKFSQEYE------------SIDPGqqFTWENSNLEVNKPKNRYANVIAYDHSRVILTSVDGVPG--SDYINANYID 78

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658117657 1099 GFTQPKAYIATQGPLKSSMEDFWRMVWEQNASVIVMITNLVEKGRRKCDQYWPLDSQEEYGSFLVTLRSTKVLAYYTQRT 1178
Cdd:cd14626     79 GYRKQNAYIATQGPLPETLSDFWRMVWEQRTATIVMMTRLEEKSRVKCDQYWPIRGTETYGMIQVTLLDTVELATYSVRT 158

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658117657 1179 FTLKntraKKGSqkeqTHERTVVQYHYTQWPDMGVPEYTLPVLTFVRKSSQANLGNMGPVVVHCSAGVGRTGTYIVLDSM 1258
Cdd:cd14626    159 FALY----KNGS----SEKREVRQFQFMAWPDHGVPEYPTPILAFLRRVKACNPPDAGPMVVHCSAGVGRTGCFIVIDAM 230

                          250       260       270       280
                   ....*....|....*....|....*....|....*....|....
gi 1658117657 1259 LRQIKEQGTVNILGFLKHIRTQRNYLVQTEEQYIFIHDALVEAI 1302
Cdd:cd14626    231 LERMKHEKTVDIYGHVTCMRSQRNYMVQTEDQYIFIHEALLEAA 274

R3-PTPc

cd14548

catalytic domain of R3 subfamily receptor-type tyrosine-protein phosphatases and similar ...

1064-1295

8.56e-90

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: 290.80 E-value: 8.56e-90

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658117657 1064 RYINILAYDHSRVKLSSSSDRNGwsADYINANYVDGFTQPKAYIATQGPLKSSMEDFWRMVWEQNASVIVMITNLVEKGR 1143
Cdd:cd14548      1 RYTNILPYDHSRVKLIPINEEEG--SDYINANYIPGYNSPREFIATQGPLPGTKDDFWRMVWEQNSHTIVMLTQCMEKGR 78

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658117657 1144 RKCDQYWPLDSQE-EYGSFLVTLRSTKVLAYYTQRTFTLKNTRAkkgsqkeqthERTVVQYHYTQWPDMGVPEYTLPVLT 1222
Cdd:cd14548     79 VKCDHYWPFDQDPvYYGDITVTMLSESVLPDWTIREFKLERGDE----------VRSVRQFHFTAWPDHGVPEAPDSLLR 148

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1658117657 1223 FVRKSSQANLGNMGPVVVHCSAGVGRTGTYIVLDSMLRQIKEQGTVNILGFLKHIRTQRNYLVQTEEQYIFIH 1295
Cdd:cd14548    149 FVRLVRDYIKQEKGPTIVHCSAGVGRTGTFIALDRLLQQIESEDYVDIFGIVYDLRKHRPLMVQTEAQYIFLH 221

PTPc-N9

cd14543

catalytic domain of tyrosine-protein phosphatase non-receptor type 9; Tyrosine-protein ...

1032-1295

1.13e-89

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: 292.73 E-value: 1.13e-89

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658117657 1032 ILKEcYEEIQACTVdlGITADSSIHPENKNKNRYINILAYDHSRVKLSS-SSDRNgwsADYINANYVDGFTQPKAYIATQ 1110
Cdd:cd14543      5 IYEE-YEDIRREPP--AGTFLCSLAPANQEKNRYGDVLCLDQSRVKLPKrNGDER---TDYINANFMDGYKQKNAYIATQ 78

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658117657 1111 GPLKSSMEDFWRMVWEQNASVIVMITNLVEKGRRKCDQYWPLD--SQEEYGSFLVTLRSTKVLAYYTQRTFTLKNTrakk 1188
Cdd:cd14543     79 GPLPKTYSDFWRMVWEQKVLVIVMTTRVVERGRVKCGQYWPLEegSSLRYGDLTVTNLSVENKEHYKKTTLEIHNT---- 154

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658117657 1189 gsqkeQTHE-RTVVQYHYTQWPDMGVPEYTLPVLTF---VRKSSQANLGNMG----------PVVVHCSAGVGRTGTYIV 1254
Cdd:cd14543    155 -----ETDEsRQVTHFQFTSWPDFGVPSSAAALLDFlgeVRQQQALAVKAMGdrwkghppgpPIVVHCSAGIGRTGTFCT 229

                          250       260       270       280
                   ....*....|....*....|....*....|....*....|.
gi 1658117657 1255 LDSMLRQIKEQGTVNILGFLKHIRTQRNYLVQTEEQYIFIH 1295
Cdd:cd14543    230 LDICLSQLEDVGTLNVMQTVRRMRTQRAFSIQTPDQYYFCY 270

R-PTPc-S-1

cd14625

catalytic domain of receptor-type tyrosine-protein phosphatase S, repeat 1; Receptor-type ...

1005-1302

1.41e-86

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: 284.29 E-value: 1.41e-86

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658117657 1005 HEALPIKQFVKHVAEL--HDSNTFSQEFEilkecyeeiqacTVDLG--ITADSSIHPENKNKNRYINILAYDHSRVKLSS 1080
Cdd:cd14625      1 HPPIPISELAEHTERLkaNDNLKLSQEYE------------SIDPGqqFTWEHSNLEVNKPKNRYANVIAYDHSRVILQP 68

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658117657 1081 SSDRNGwsADYINANYVDGFTQPKAYIATQGPLKSSMEDFWRMVWEQNASVIVMITNLVEKGRRKCDQYWPLDSQEEYGS 1160
Cdd:cd14625     69 IEGIMG--SDYINANYIDGYRKQNAYIATQGPLPETFGDFWRMVWEQRSATVVMMTKLEEKSRIKCDQYWPSRGTETYGM 146

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658117657 1161 FLVTLRSTKVLAYYTQRTFTLKntraKKGSqkeqTHERTVVQYHYTQWPDMGVPEYTLPVLTFVRKSSQANLGNMGPVVV 1240
Cdd:cd14625    147 IQVTLLDTIELATFCVRTFSLH----KNGS----SEKREVRQFQFTAWPDHGVPEYPTPFLAFLRRVKTCNPPDAGPIVV 218

                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1658117657 1241 HCSAGVGRTGTYIVLDSMLRQIKEQGTVNILGFLKHIRTQRNYLVQTEEQYIFIHDALVEAI 1302
Cdd:cd14625    219 HCSAGVGRTGCFIVIDAMLERIKHEKTVDIYGHVTLMRSQRNYMVQTEDQYSFIHDALLEAV 280

R-PTPc-D-1

cd14624

catalytic domain of receptor-type tyrosine-protein phosphatase D, repeat 1; Receptor-type ...

1005-1302

5.82e-86

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: 282.78 E-value: 5.82e-86

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658117657 1005 HEALPIKQFVKHVAEL--HDSNTFSQEFEilkecyeeiqacTVDLG--ITADSSIHPENKNKNRYINILAYDHSRVKLSS 1080
Cdd:cd14624      1 HPPIPILELADHIERLkaNDNLKFSQEYE------------SIDPGqqFTWEHSNLEVNKPKNRYANVIAYDHSRVLLSA 68

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658117657 1081 SSDRNGwsADYINANYVDGFTQPKAYIATQGPLKSSMEDFWRMVWEQNASVIVMITNLVEKGRRKCDQYWPLDSQEEYGS 1160
Cdd:cd14624     69 IEGIPG--SDYINANYIDGYRKQNAYIATQGALPETFGDFWRMIWEQRSATVVMMTKLEERSRVKCDQYWPSRGTETYGL 146

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658117657 1161 FLVTLRSTKVLAYYTQRTFTLkntrAKKGSqkeqTHERTVVQYHYTQWPDMGVPEYTLPVLTFVRKSSQANLGNMGPVVV 1240
Cdd:cd14624    147 IQVTLLDTVELATYCVRTFAL----YKNGS----SEKREVRQFQFTAWPDHGVPEHPTPFLAFLRRVKTCNPPDAGPMVV 218

                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1658117657 1241 HCSAGVGRTGTYIVLDSMLRQIKEQGTVNILGFLKHIRTQRNYLVQTEEQYIFIHDALVEAI 1302
Cdd:cd14624    219 HCSAGVGRTGCFIVIDAMLERIKHEKTVDIYGHVTLMRAQRNYMVQTEDQYIFIHDALLEAV 280

R-PTPc-T-1

cd14630

catalytic domain of receptor-type tyrosine-protein phosphatase T, repeat 1; Receptor-type ...

1058-1303

7.87e-83

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: 271.90 E-value: 7.87e-83

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658117657 1058 ENKNKNRYINILAYDHSRVKLSSSSDRNgwSADYINANYVDGFTQPKAYIATQGPLKSSMEDFWRMVWEQNASVIVMITN 1137
Cdd:cd14630      2 ENRNKNRYGNIISYDHSRVRLQLLDGDP--HSDYINANYIDGYHRPRHYIATQGPMQETVKDFWRMIWQENSASVVMVTN 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658117657 1138 LVEKGRRKCDQYWPlDSQEEYGSFLVTLRSTKVLAYYTQRTFTLkntrakkgsQKEQTHE-RTVVQYHYTQWPDMGVPEY 1216
Cdd:cd14630     80 LVEVGRVKCVRYWP-DDTEVYGDIKVTLIETEPLAEYVIRTFTV---------QKKGYHEiREIRQFHFTSWPDHGVPCY 149

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658117657 1217 TLPVLTFVRKSSQANLGNMGPVVVHCSAGVGRTGTYIVLDSMLRQIKEQGTVNILGFLKHIRTQRNYLVQTEEQYIFIHD 1296
Cdd:cd14630    150 ATGLLGFVRQVKFLNPPDAGPIVVHCSAGAGRTGCFIAIDIMLDMAENEGVVDIFNCVRELRAQRVNMVQTEEQYVFVHD 229


                   ....*..
gi 1658117657 1297 ALVEAIL 1303
Cdd:cd14630    230 AILEACL 236

R-PTPc-J

cd14615

catalytic domain of receptor-type tyrosine-protein phosphatase J; Receptor-type ...

1063-1294

1.40e-77

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: 256.28 E-value: 1.40e-77

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658117657 1063 NRYINILAYDHSRVKLSSSSDRngwSADYINANYVDGFTQPKAYIATQGPLKSSMEDFWRMVWEQNASVIVMITNLVEKG 1142
Cdd:cd14615      1 NRYNNVLPYDISRVKLSVQSHS---TDDYINANYMPGYNSKKEFIAAQGPLPNTVKDFWRMVWEKNVYAIVMLTKCVEQG 77

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658117657 1143 RRKCDQYWPLDSQEEYGSFLVTLRSTKVLAYYTQRTFTLKNTrakkgsqkeQTHE-RTVVQYHYTQWPDMGVPEYTLPVL 1221
Cdd:cd14615     78 RTKCEEYWPSKQKKDYGDITVTMTSEIVLPEWTIRDFTVKNA---------QTNEsRTVRHFHFTSWPDHGVPETTDLLI 148

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1658117657 1222 TF---VRKSSQANLGNmGPVVVHCSAGVGRTGTYIVLDSMLRQIKEQGTVNILGFLKHIRTQRNYLVQTEEQYIFI 1294
Cdd:cd14615    149 NFrhlVREYMKQNPPN-SPILVHCSAGVGRTGTFIAIDRLIYQIENENVVDVYGIVYDLRMHRPLMVQTEDQYVFL 223

R-PTPc-M-1

cd14633

catalytic domain of receptor-type tyrosine-protein phosphatase M, repeat 1; Receptor-type ...

1052-1303

2.28e-77

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: 257.66 E-value: 2.28e-77

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658117657 1052 DSSIHPENKNKNRYINILAYDHSRVKLSSSSDRNGwsADYINANYVDGFTQPKAYIATQGPLKSSMEDFWRMVWEQNASV 1131
Cdd:cd14633     33 DSAKKDENRMKNRYGNIIAYDHSRVRLQPIEGETS--SDYINGNYIDGYHRPNHYIATQGPMQETIYDFWRMVWHENTAS 110

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658117657 1132 IVMITNLVEKGRRKCDQYWPlDSQEEYGSFLVTLRSTKVLAYYTQRTFTLkntrakkgsQKEQTHE-RTVVQYHYTQWPD 1210
Cdd:cd14633    111 IIMVTNLVEVGRVKCCKYWP-DDTEIYKDIKVTLIETELLAEYVIRTFAV---------EKRGVHEiREIRQFHFTGWPD 180

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658117657 1211 MGVPEYTLPVLTFVRKSSQANLGNMGPVVVHCSAGVGRTGTYIVLDSMLRQIKEQGTVNILGFLKHIRTQRNYLVQTEEQ 1290
Cdd:cd14633    181 HGVPYHATGLLGFVRQVKSKSPPNAGPLVVHCSAGAGRTGCFIVIDIMLDMAEREGVVDIYNCVRELRSRRVNMVQTEEQ 260

                          250
                   ....*....|...
gi 1658117657 1291 YIFIHDALVEAIL 1303
Cdd:cd14633    261 YVFIHDAILEACL 273

R-PTPc-typeIIb-1

cd14555

catalytic domain of type IIb (or R2B) subfamily receptor-type tyrosine-protein phosphatases, ...

1091-1303

2.72e-76

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: 251.76 E-value: 2.72e-76

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658117657 1091 YINANYVDGFTQPKAYIATQGPLKSSMEDFWRMVWEQNASVIVMITNLVEKGRRKCDQYWPLDSqEEYGSFLVTLRSTKV 1170
Cdd:cd14555      1 YINANYIDGYHRPNHYIATQGPMQETVYDFWRMVWQENSASIVMVTNLVEVGRVKCSRYWPDDT-EVYGDIKVTLVETEP 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658117657 1171 LAYYTQRTFTLkntrakkgsQKEQTHE-RTVVQYHYTQWPDMGVPEYTLPVLTFVRKSSQANLGNMGPVVVHCSAGVGRT 1249
Cdd:cd14555     80 LAEYVVRTFAL---------ERRGYHEiREVRQFHFTGWPDHGVPYHATGLLGFIRRVKASNPPSAGPIVVHCSAGAGRT 150

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....
gi 1658117657 1250 GTYIVLDSMLRQIKEQGTVNILGFLKHIRTQRNYLVQTEEQYIFIHDALVEAIL 1303
Cdd:cd14555    151 GCYIVIDIMLDMAEREGVVDIYNCVKELRSRRVNMVQTEEQYIFIHDAILEACL 204

R-PTPc-A-1

cd14621

catalytic domain of receptor-type tyrosine-protein phosphatase A, repeat 1; Receptor-type ...

1022-1309

3.38e-76

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: 255.33 E-value: 3.38e-76

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658117657 1022 DSNTFSQEFEILKECyeEIQActvdlgiTADSSIHPENKNKNRYINILAYDHSRVKLSSSSDRNgwSADYINANYVDGFT 1101
Cdd:cd14621     24 DNKLFREEFNALPAC--PIQA-------TCEAASKEENKEKNRYVNILPYDHSRVHLTPVEGVP--DSDYINASFINGYQ 92

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658117657 1102 QPKAYIATQGPLKSSMEDFWRMVWEQNASVIVMITNLVEKGRRKCDQYWPLDSQEEYGSFLVTLRSTKVLAYYTQRTFTL 1181
Cdd:cd14621     93 EKNKFIAAQGPKEETVNDFWRMIWEQNTATIVMVTNLKERKECKCAQYWPDQGCWTYGNIRVSVEDVTVLVDYTVRKFCI 172

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658117657 1182 KNTrakkGSQKEQTHERTVVQYHYTQWPDMGVPEYTLPVLTFVRKSSQANLGNMGPVVVHCSAGVGRTGTYIVLDSMLRQ 1261
Cdd:cd14621    173 QQV----GDVTNKKPQRLITQFHFTSWPDFGVPFTPIGMLKFLKKVKNCNPQYAGAIVVHCSAGVGRTGTFIVIDAMLDM 248

                          250       260       270       280
                   ....*....|....*....|....*....|....*....|....*...
gi 1658117657 1262 IKEQGTVNILGFLKHIRTQRNYLVQTEEQYIFIHDALVEAILSKETEV 1309
Cdd:cd14621    249 MHAERKVDVYGFVSRIRAQRCQMVQTDMQYVFIYQALLEHYLYGDTEL 296

R-PTPc-B

cd14617

catalytic domain of receptor-type tyrosine-protein phosphatase B; Receptor-type ...

1063-1295

7.83e-76

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: 251.38 E-value: 7.83e-76

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658117657 1063 NRYINILAYDHSRVKLSSSSDRNGwsADYINANYVDGFTQPKAYIATQGPLKSSMEDFWRMVWEQNASVIVMITNLVEKG 1142
Cdd:cd14617      1 NRYNNILPYDSTRVKLSNVDDDPC--SDYINASYIPGNNFRREYIATQGPLPGTKDDFWKMVWEQNVHNIVMVTQCVEKG 78

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658117657 1143 RRKCDQYWPLDSQE-EYGSFLVTLRSTKVLAYYTQRTFtlkntraKKGSQKEQTHERTVVQYHYTQWPDMGVPEYTLPVL 1221
Cdd:cd14617     79 RVKCDHYWPADQDSlYYGDLIVQMLSESVLPEWTIREF-------KICSEEQLDAPRLVRHFHYTVWPDHGVPETTQSLI 151

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1658117657 1222 TFVR--KSSQANLGNMGPVVVHCSAGVGRTGTYIVLDSMLRQIKEQGTVNILGFLKHIRTQRNYLVQTEEQYIFIH 1295
Cdd:cd14617    152 QFVRtvRDYINRTPGSGPTVVHCSAGVGRTGTFIALDRILQQLDSKDSVDIYGAVHDLRLHRVHMVQTECQYVYLH 227

R-PTPc-H

cd14619

catalytic domain of receptor-type tyrosine-protein phosphatase H; Receptor-type ...

1063-1302

4.27e-75

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: 249.42 E-value: 4.27e-75

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658117657 1063 NRYINILAYDHSRVKLSSSSDRNGwsADYINANYVDGFTQPKAYIATQGPLKSSMEDFWRMVWEQNASVIVMITNLVEKG 1142
Cdd:cd14619      1 NRFRNVLPYDWSRVPLKPIHEEPG--SDYINANYMPGYWSSQEFIATQGPLPQTVGDFWRMIWEQQSSTIVMLTNCMEAG 78

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658117657 1143 RRKCDQYWPLDSQE-EYGSFLVTLRSTKVLAYYTQRTFTLKNtrakkgsqKEQTHERTVVQYHYTQWPDMGVPEYTLPVL 1221
Cdd:cd14619     79 RVKCEHYWPLDYTPcTYGHLRVTVVSEEVMENWTVREFLLKQ--------VEEQKTLSVRHFHFTAWPDHGVPSSTDTLL 150

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658117657 1222 TFVRKSSQANLGNM--GPVVVHCSAGVGRTGTYIVLDSMLRQIKEQGTVNILGFLKHIRTQRNYLVQTEEQYIFIHDALV 1299
Cdd:cd14619    151 AFRRLLRQWLDQTMsgGPTVVHCSAGVGRTGTLIALDVLLQQLQSEGLLGPFSFVQKMRENRPLMVQTESQYVFLHQCIL 230


                   ...
gi 1658117657 1300 EAI 1302
Cdd:cd14619    231 DFL 233

PTPc-N11_6

cd14544

catalytic domain of tyrosine-protein phosphatase non-receptor type 11 and type 6; ...

1059-1302

3.15e-74

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: 247.76 E-value: 3.15e-74

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658117657 1059 NKNKNRYINILAYDHSRVKLSSSsDRNGWSADYINANYV-------DGFTQPKAYIATQGPLKSSMEDFWRMVWEQNASV 1131
Cdd:cd14544      1 NKGKNRYKNILPFDHTRVILKDR-DPNVPGSDYINANYIrnenegpTTDENAKTYIATQGCLENTVSDFWSMVWQENSRV 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658117657 1132 IVMITNLVEKGRRKCDQYWP-LDSQEEYGSFLVTLRSTKVLAYYTQRTFTLKNTrakkgsqKEQTHERTVVQYHYTQWPD 1210
Cdd:cd14544     80 IVMTTKEVERGKNKCVRYWPdEGMQKQYGPYRVQNVSEHDTTDYTLRELQVSKL-------DQGDPIREIWHYQYLSWPD 152

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658117657 1211 MGVPEYTLPVLTFVRK--SSQANLGNMGPVVVHCSAGVGRTGTYIVLDSMLRQIKEQG---TVNILGFLKHIRTQRNYLV 1285
Cdd:cd14544    153 HGVPSDPGGVLNFLEDvnQRQESLPHAGPIVVHCSAGIGRTGTFIVIDMLLDQIKRKGldcDIDIQKTIQMVRSQRSGMV 232

                          250
                   ....*....|....*..
gi 1658117657 1286 QTEEQYIFIHDALVEAI 1302
Cdd:cd14544    233 QTEAQYKFIYVAVAQYI 249

PTPc-KIM

cd14547

catalytic domain of the kinase interaction motif (KIM) family of protein-tyrosine phosphatases; ...

1063-1295

1.52e-73

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: 244.61 E-value: 1.52e-73

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658117657 1063 NRYINILAYDHSRVKLSSSSdrNGWSADYINANYVDGFT-QPKAYIATQGPLKSSMEDFWRMVWEQNASVIVMITNLVEK 1141
Cdd:cd14547      1 NRYKTILPNEHSRVCLPSVD--DDPLSSYINANYIRGYDgEEKAYIATQGPLPNTVADFWRMVWQEKTPIIVMITNLTEA 78

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658117657 1142 gRRKCDQYWPLDSQEEYGSFLVTLRSTKVLAYYTQRTFTLKNtrakkgsqkeQTHERTVVQYHYTQWPDMGVPEYTLPVL 1221
Cdd:cd14547     79 -KEKCAQYWPEEENETYGDFEVTVQSVKETDGYTVRKLTLKY----------GGEKRYLKHYWYTSWPDHKTPEAAQPLL 147

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1658117657 1222 TFVRKSSQA--NLGNMGPVVVHCSAGVGRTGTYIVLDSMLRQIKEQGTVNILGFLKHIRTQRNYLVQTEEQYIFIH 1295
Cdd:cd14547    148 SLVQEVEEArqTEPHRGPIVVHCSAGIGRTGCFIATSIGCQQLREEGVVDVLGIVCQLRLDRGGMVQTAEQYEFVH 223

R-PTPc-O

cd14614

catalytic domain of receptor-type tyrosine-protein phosphatase O; Receptor-type ...

1057-1295

3.70e-72

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: 241.33 E-value: 3.70e-72

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658117657 1057 PENKNKNRYINILAYDHSRVKLSSSSDRNGwsADYINANYVDGFTQPKAYIATQGPLKSSMEDFWRMVWEQNASVIVMIT 1136
Cdd:cd14614     10 PVNRCKNRYTNILPYDFSRVKLVSMHEEEG--SDYINANYIPGYNSPQEYIATQGPLPETRNDFWKMVLQQKSQIIVMLT 87

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658117657 1137 NLVEKGRRKCDQYWPLDSQE-EYGSFLVTLRSTKVLAYYTQRTFTLkntrakkgSQKEQTHErtVVQYHYTQWPDMGVPE 1215
Cdd:cd14614     88 QCNEKRRVKCDHYWPFTEEPvAYGDITVEMLSEEEQPDWAIREFRV--------SYADEVQD--VMHFNYTAWPDHGVPT 157

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658117657 1216 YTL--PVLTFVRKSSQANLGNMGPVVVHCSAGVGRTGTYIVLDSMLRQIKEQGTVNILGFLKHIRTQRNYLVQTEEQYIF 1293
Cdd:cd14614    158 ANAaeSILQFVQMVRQQAVKSKGPMIIHCSAGVGRTGTFIALDRLLQHIRDHEFVDILGLVSEMRSYRMSMVQTEEQYIF 237


                   ..
gi 1658117657 1294 IH 1295
Cdd:cd14614    238 IH 239

R-PTPc-K-1

cd14631

catalytic domain of receptor-type tyrosine-protein phosphatase K, repeat 1; Receptor-type ...

1088-1303

1.01e-71

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: 239.15 E-value: 1.01e-71

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658117657 1088 SADYINANYVDGFTQPKAYIATQGPLKSSMEDFWRMVWEQNASVIVMITNLVEKGRRKCDQYWPlDSQEEYGSFLVTLRS 1167
Cdd:cd14631     12 SSDYINANYIDGYQRPSHYIATQGPVHETVYDFWRMIWQEQSACIVMVTNLVEVGRVKCYKYWP-DDTEVYGDFKVTCVE 90

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658117657 1168 TKVLAYYTQRTFTLKntraKKGSQKEqtheRTVVQYHYTQWPDMGVPEYTLPVLTFVRKSSQANLGNMGPVVVHCSAGVG 1247
Cdd:cd14631     91 MEPLAEYVVRTFTLE----RRGYNEI----REVKQFHFTGWPDHGVPYHATGLLSFIRRVKLSNPPSAGPIVVHCSAGAG 162

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 1658117657 1248 RTGTYIVLDSMLRQIKEQGTVNILGFLKHIRTQRNYLVQTEEQYIFIHDALVEAIL 1303
Cdd:cd14631    163 RTGCYIVIDIMLDMAEREGVVDIYNCVKALRSRRINMVQTEEQYIFIHDAILEACL 218

PTPc

Protein tyrosine phosphatase, catalytic domain;

1332-1589

5.08e-71

Protein tyrosine phosphatase, catalytic domain;

Pssm-ID: 214550 [Multi-domain] Cd Length: 259 Bit Score: 238.71 E-value: 5.08e-71

                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658117657  1332 LEKQFKMITQSNAKQCDYSAALKQCNRDKNRNSSLLPVERSRVHLSTTAGEISDYINASYIMGYQQSNEFIITQNPLPST 1411
Cdd:smart00194    2 LEEEFEKLDRLKPDDESCTVAAFPENRDKNRYKDVLPYDHTRVKLKPPPGEGSDYINASYIDGPNGPKAYIATQGPLPST 81

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658117657  1412 MKDFWKMIWDHSTQVVIALPDGLDL-AEDECIYWPTK-SQPIRFDTFTVTFMGEDHMclsneDMLIVQDFILEATQDDYV 1489
Cdd:smart00194   82 VEDFWRMVWEQKVTVIVMLTELVEKgREKCAQYWPDEeGEPLTYGDITVTLKSVEKV-----DDYTIRTLEVTNTGCSET 156

                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658117657  1490 LEVRQYRAPRWP---NPDGPISnTFELINIIKEESVSRDGPIVVHDKRGGNIAGTFCALMTLLHQLEMESSFDVYWVAKM 1566
Cdd:smart00194  157 RTVTHYHYTNWPdhgVPESPES-ILDLIRAVRKSQSTSTGPIVVHCSAGVGRTGTFIAIDILLQQLEAGKEVDIFEIVKE 235

                           250       260
                    ....*....|....*....|...
gi 1658117657  1567 INLMRPGIFTDIDQYQFLYKVIM 1589
Cdd:smart00194  236 LRSQRPGMVQTEEQYIFLYRAIL 258

R-PTPc-E-1

cd14620

catalytic domain of receptor-type tyrosine-protein phosphatase E, repeat 1; Receptor-type ...

1065-1300

4.67e-70

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: 234.84 E-value: 4.67e-70

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658117657 1065 YINILAYDHSRVKLSSSSdrNGWSADYINANYVDGFTQPKAYIATQGPLKSSMEDFWRMVWEQNASVIVMITNLVEKGRR 1144
Cdd:cd14620      1 YPNILPYDHSRVILSQLD--GIPCSDYINASYIDGYKEKNKFIAAQGPKQETVNDFWRMVWEQKSATIVMLTNLKERKEE 78

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658117657 1145 KCDQYWPLDSQEEYGSFLVTLRSTKVLAYYTQRTFTLKnTRAKKGSQKEqtheRTVVQYHYTQWPDMGVPEYTLPVLTFV 1224
Cdd:cd14620     79 KCYQYWPDQGCWTYGNIRVAVEDCVVLVDYTIRKFCIQ-PQLPDGCKAP----RLVTQLHFTSWPDFGVPFTPIGMLKFL 153

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1658117657 1225 RKSSQANLGNMGPVVVHCSAGVGRTGTYIVLDSMLRQIKEQGTVNILGFLKHIRTQRNYLVQTEEQYIFIHDALVE 1300
Cdd:cd14620    154 KKVKSVNPVHAGPIVVHCSAGVGRTGTFIVIDAMIDMMHAEQKVDVFEFVSRIRNQRPQMVQTDMQYSFIYQALLE 229

R-PTPc-U-1

cd14632

catalytic domain of receptor-type tyrosine-protein phosphatase U, repeat 1; Receptor-type ...

1091-1303

4.76e-70

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: 233.79 E-value: 4.76e-70

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658117657 1091 YINANYVDGFTQPKAYIATQGPLKSSMEDFWRMVWEQNASVIVMITNLVEKGRRKCDQYWPlDSQEEYGSFLVTLRSTKV 1170
Cdd:cd14632      1 YINANYIDGYHRSNHFIATQGPKQEMVYDFWRMVWQEHCSSIVMITKLVEVGRVKCSKYWP-DDSDTYGDIKITLLKTET 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658117657 1171 LAYYTQRTFTLKntraKKGSQKEqtHErtVVQYHYTQWPDMGVPEYTLPVLTFVRKSSQANLGNMGPVVVHCSAGVGRTG 1250
Cdd:cd14632     80 LAEYSVRTFALE----RRGYSAR--HE--VKQFHFTSWPEHGVPYHATGLLAFIRRVKASTPPDAGPVVVHCSAGAGRTG 151

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|...
gi 1658117657 1251 TYIVLDSMLRQIKEQGTVNILGFLKHIRTQRNYLVQTEEQYIFIHDALVEAIL 1303
Cdd:cd14632    152 CYIVLDVMLDMAECEGVVDIYNCVKTLCSRRINMIQTEEQYIFIHDAILEACL 204

R-PTPc-V

cd14618

catalytic domain of receptor-type tyrosine-protein phosphatase V; Receptor-type ...

1063-1299

1.14e-69

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: 233.68 E-value: 1.14e-69

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658117657 1063 NRYINILAYDHSRVKLSSSSDRNgwSADYINANYVDGFTQPKAYIATQGPLKSSMEDFWRMVWEQNASVIVMITNLVEKG 1142
Cdd:cd14618      1 NRYPHVLPYDHSRVRLSQLGGEP--HSDYINANFIPGYTSPQEFIATQGPLKKTIEDFWRLVWEQQVCNIIMLTVGMENG 78

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658117657 1143 RRKCDQYWPLDSQE-EYGSFLVTLRSTKVLAYYTQRTFTLKNTRAKKgsqkeqthERTVVQYHYTQWPDMGVPEYTLPVL 1221
Cdd:cd14618     79 RVLCDHYWPSESTPvSYGHITVHLLAQSSEDEWTRREFKLWHEDLRK--------ERRVKHLHYTAWPDHGIPESTSSLM 150

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658117657 1222 TF---VRKSSQANLGNmGPVVVHCSAGVGRTGTYIVLDSMLRQIKEQGTVNILGFLKHIRTQRNYLVQTEEQYIFIHDAL 1298
Cdd:cd14618    151 AFrelVREHVQATKGK-GPTLVHCSAGVGRSGTFIALDRLLRQLKEEKVVDVFNTVYILRMHRYLMIQTLSQYIFLHSCI 229


                   .
gi 1658117657 1299 V 1299
Cdd:cd14618    230 L 230

R-PTP-LAR-2

cd14554

PTP-like domain of the LAR family receptor-type tyrosine-protein phosphatases, repeat 2; The ...

1057-1297

6.31e-69

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: 232.03 E-value: 6.31e-69

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658117657 1057 PENKNKNRYINILAYDHSRVKLSSSSDRNGwsADYINANYVDGFTQPKAYIATQGPLKSSMEDFWRMVWEQNASVIVMIT 1136
Cdd:cd14554      4 PCNKFKNRLVNILPYESTRVCLQPIRGVEG--SDYINASFIDGYRQRGAYIATQGPLAETTEDFWRMLWEHNSTIIVMLT 81

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658117657 1137 NLVEKGRRKCDQYWPLDSQEEYGSFLVTLRSTKVLAYYTQRTFtlKNTRAKKGSQkeqtheRTVVQYHYTQWPDMGVPEY 1216
Cdd:cd14554     82 KLREMGREKCHQYWPAERSARYQYFVVDPMAEYNMPQYILREF--KVTDARDGQS------RTVRQFQFTDWPEQGVPKS 153

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658117657 1217 TLPVLTFVRK--SSQANLGNMGPVVVHCSAGVGRTGTYIVLDSMLRQIKEQGTVNILGFLKHIRTQRNYLVQTEEQYIFI 1294
Cdd:cd14554    154 GEGFIDFIGQvhKTKEQFGQEGPITVHCSAGVGRTGVFITLSIVLERMRYEGVVDVFQTVKLLRTQRPAMVQTEDQYQFC 233


                   ...
gi 1658117657 1295 HDA 1297
Cdd:cd14554    234 YRA 236

PTP_fungal

cd18533

fungal protein tyrosine phosphatases; This subfamily contains Saccharomyces cerevisiae ...

1091-1296

9.96e-69

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: 230.21 E-value: 9.96e-69

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658117657 1091 YINANYVD-GFTQPKAYIATQGPLKSSMEDFWRMVWEQNASVIVMITNLVEKGRRKCDQYWPLDS-QEEYGSFLVTLRST 1168
Cdd:cd18533      1 YINASYITlPGTSSKRYIATQGPLPATIGDFWKMIWQNNVGVIVMLTPLVENGREKCDQYWPSGEyEGEYGDLTVELVSE 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658117657 1169 KVL--AYYTQRTFTLKntrakkgsqKEQTHERTVVQYHYTQWPDMGVPEYTLPVLTFVR--KSSQANLGNMGPVVVHCSA 1244
Cdd:cd18533     81 EENddGGFIVREFELS---------KEDGKVKKVYHIQYKSWPDFGVPDSPEDLLTLIKlkRELNDSASLDPPIIVHCSA 151

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1658117657 1245 GVGRTGTYIVLDSMLRQIKEQGTVN---------ILGFLKHIRTQRNYLVQTEEQYIFIHD 1296
Cdd:cd18533    152 GVGRTGTFIALDSLLDELKRGLSDSqdledsedpVYEIVNQLRKQRMSMVQTLRQYIFLYD 212

R-PTPc-A-E-1

cd14551

catalytic domain of receptor-type tyrosine-protein phosphatase A and E, repeat 1; ...

1091-1295

6.26e-67

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: 224.79 E-value: 6.26e-67

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658117657 1091 YINANYVDGFTQPKAYIATQGPLKSSMEDFWRMVWEQNASVIVMITNLVEKGRRKCDQYWPLDSQEEYGSFLVTLRSTKV 1170
Cdd:cd14551      1 YINASYIDGYQEKNKFIAAQGPKDETVNDFWRMIWEQGSATIVMVTNLKERKEKKCSQYWPDQGCWTYGNLRVRVEDTVV 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658117657 1171 LAYYTQRTFTLKNTRAKKGSQKEqtheRTVVQYHYTQWPDMGVPEYTLPVLTFVRKSSQANLGNMGPVVVHCSAGVGRTG 1250
Cdd:cd14551     81 LVDYTTRKFCIQKVNRGIGEKRV----RLVTQFHFTSWPDFGVPFTPIGMLKFLKKVKSANPPRAGPIVVHCSAGVGRTG 156

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*
gi 1658117657 1251 TYIVLDSMLRQIKEQGTVNILGFLKHIRTQRNYLVQTEEQYIFIH 1295
Cdd:cd14551    157 TFIVIDAMLDMMHAEGKVDVFGFVSRIRQQRSQMVQTDMQYVFIY 201

R-PTPc-C-1

cd14557

catalytic domain of receptor-type tyrosine-protein phosphatase C, repeat 1; Receptor-type ...

1091-1295

1.26e-65

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: 220.85 E-value: 1.26e-65

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658117657 1091 YINANYVDGFTQPKAYIATQGPLKSSMEDFWRMVWEQNASVIVMITNLVEKGRRKCDQYWPL--DSQEEYGSFLVTLRST 1168
Cdd:cd14557      1 YINASYIDGFKEPRKYIAAQGPKDETVDDFWRMIWEQKSTVIVMVTRCEEGNRNKCAQYWPSmeEGSRAFGDVVVKINEE 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658117657 1169 KVLAYYTQRTFTLKNTRaKKGSQKEQTHertvVQYhyTQWPDMGVPEYTLPVLTFVRKSSQANLGNMGPVVVHCSAGVGR 1248
Cdd:cd14557     81 KICPDYIIRKLNINNKK-EKGSGREVTH----IQF--TSWPDHGVPEDPHLLLKLRRRVNAFNNFFSGPIVVHCSAGVGR 153

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*..
gi 1658117657 1249 TGTYIVLDSMLRQIKEQGTVNILGFLKHIRTQRNYLVQTEEQYIFIH 1295
Cdd:cd14557    154 TGTYIGIDAMLEGLEAEGRVDVYGYVVKLRRQRCLMVQVEAQYILIH 200

Y_phosphatase

Protein-tyrosine phosphatase;

1357-1589

3.74e-64

Protein-tyrosine phosphatase;

Pssm-ID: 459674 [Multi-domain] Cd Length: 234 Bit Score: 217.88 E-value: 3.74e-64

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658117657 1357 NRDKNRNSSLLPVERSRVHLSTTAGEiSDYINASYIMGYQQSNEFIITQNPLPSTMKDFWKMIWDHSTQVVIALPDGLDL 1436
Cdd:pfam00102    1 NLEKNRYKDVLPYDHTRVKLTGDPGP-SDYINASYIDGYKKPKKYIATQGPLPNTVEDFWRMVWEEKVTIIVMLTELEEK 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658117657 1437 AEDEC-IYWPTKS-QPIRFDTFTVTFMGEDhmclSNEDMLIVQDFILEATQDDYVLEVRQYRAPRWPNPDGP--ISNTFE 1512
Cdd:pfam00102   80 GREKCaQYWPEEEgESLEYGDFTVTLKKEK----EDEKDYTVRTLEVSNGGSEETRTVKHFHYTGWPDHGVPesPNSLLD 155

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1658117657 1513 LINIIKEESV-SRDGPIVVHDKRGGNIAGTFCALMTLLHQLEMESSFDVYWVAKMINLMRPGIFTDIDQYQFLYKVIM 1589
Cdd:pfam00102  156 LLRKVRKSSLdGRSGPIVVHCSAGIGRTGTFIAIDIALQQLEAEGEVDIFQIVKELRSQRPGMVQTLEQYIFLYDAIL 233

PTPc-N11

cd14605

catalytic domain of tyrosine-protein phosphatase non-receptor type 11; Tyrosine-protein ...

1058-1298

5.47e-64

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: 218.35 E-value: 5.47e-64

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658117657 1058 ENKNKNRYINILAYDHSRVKLSSSsDRNGWSADYINANYV--------DGFTQPKAYIATQGPLKSSMEDFWRMVWEQNA 1129
Cdd:cd14605      1 ENKNKNRYKNILPFDHTRVVLHDG-DPNEPVSDYINANIImpefetkcNNSKPKKSYIATQGCLQNTVNDFWRMVFQENS 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658117657 1130 SVIVMITNLVEKGRRKCDQYWPLD-SQEEYGSFLVtlRSTKVLAYYTQRTFTLKNTRAKKGSQkeqthERTVVQYHYTQW 1208
Cdd:cd14605     80 RVIVMTTKEVERGKSKCVKYWPDEyALKEYGVMRV--RNVKESAAHDYILRELKLSKVGQGNT-----ERTVWQYHFRTW 152

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658117657 1209 PDMGVPEYTLPVLTFVR--KSSQANLGNMGPVVVHCSAGVGRTGTYIVLDSMLRQIKEQGT---VNILGFLKHIRTQRNY 1283
Cdd:cd14605    153 PDHGVPSDPGGVLDFLEevHHKQESIMDAGPVVVHCSAGIGRTGTFIVIDILIDIIREKGVdcdIDVPKTIQMVRSQRSG 232

                          250
                   ....*....|....*
gi 1658117657 1284 LVQTEEQYIFIHDAL 1298
Cdd:cd14605    233 MVQTEAQYRFIYMAV 247

R-PTP-D-2

cd14628

PTP-like domain of receptor-type tyrosine-protein phosphatase D, repeat 2; Receptor-type ...

1057-1304

6.17e-64

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: 219.60 E-value: 6.17e-64

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658117657 1057 PENKNKNRYINILAYDHSRVKLSSSSDRNGwsADYINANYVDGFTQPKAYIATQGPLKSSMEDFWRMVWEQNASVIVMIT 1136
Cdd:cd14628     50 PCNKFKNRLVNIMPYESTRVCLQPIRGVEG--SDYINASFIDGYRQQKAYIATQGPLAETTEDFWRMLWEHNSTIVVMLT 127

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658117657 1137 NLVEKGRRKCDQYWPLDSQEEYGSFLVTLRSTKVLAYYTQRTFtlKNTRAKKGsqkeqtHERTVVQYHYTQWPDMGVPEY 1216
Cdd:cd14628    128 KLREMGREKCHQYWPAERSARYQYFVVDPMAEYNMPQYILREF--KVTDARDG------QSRTVRQFQFTDWPEQGVPKS 199

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658117657 1217 TLPVLTFVRK--SSQANLGNMGPVVVHCSAGVGRTGTYIVLDSMLRQIKEQGTVNILGFLKHIRTQRNYLVQTEEQYIFI 1294
Cdd:cd14628    200 GEGFIDFIGQvhKTKEQFGQDGPISVHCSAGVGRTGVFITLSIVLERMRYEGVVDIFQTVKMLRTQRPAMVQTEDQYQFC 279

                          250
                   ....*....|
gi 1658117657 1295 HDALVEAILS 1304
Cdd:cd14628    280 YRAALEYLGS 289

R-PTP-S-2

cd14627

PTP-like domain of receptor-type tyrosine-protein phosphatase S, repeat 2; Receptor-type ...

1057-1304

6.33e-64

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: 219.60 E-value: 6.33e-64

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658117657 1057 PENKNKNRYINILAYDHSRVKLSSSSDRNGwsADYINANYVDGFTQPKAYIATQGPLKSSMEDFWRMVWEQNASVIVMIT 1136
Cdd:cd14627     51 PCNKFKNRLVNIMPYETTRVCLQPIRGVEG--SDYINASFIDGYRQQKAYIATQGPLAETTEDFWRMLWENNSTIVVMLT 128

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658117657 1137 NLVEKGRRKCDQYWPLDSQEEYGSFLVTLRSTKVLAYYTQRTFtlKNTRAKKGsqkeqtHERTVVQYHYTQWPDMGVPEY 1216
Cdd:cd14627    129 KLREMGREKCHQYWPAERSARYQYFVVDPMAEYNMPQYILREF--KVTDARDG------QSRTVRQFQFTDWPEQGVPKS 200

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658117657 1217 TLPVLTFVRK--SSQANLGNMGPVVVHCSAGVGRTGTYIVLDSMLRQIKEQGTVNILGFLKHIRTQRNYLVQTEEQYIFI 1294
Cdd:cd14627    201 GEGFIDFIGQvhKTKEQFGQDGPISVHCSAGVGRTGVFITLSIVLERMRYEGVVDIFQTVKMLRTQRPAMVQTEDEYQFC 280

                          250
                   ....*....|
gi 1658117657 1295 HDALVEAILS 1304
Cdd:cd14627    281 YQAALEYLGS 290

PTPc-N6

cd14606

catalytic domain of tyrosine-protein phosphatase non-receptor type 6; Tyrosine-protein ...

1057-1304

6.54e-64

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: 218.60 E-value: 6.54e-64

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658117657 1057 PENKNKNRYINILAYDHSRVKLSSSsDRNGWSADYINANYVD----GFTQP-KAYIATQGPLKSSMEDFWRMVWEQNASV 1131
Cdd:cd14606     16 PENKSKNRYKNILPFDHSRVILQGR-DSNIPGSDYINANYVKnqllGPDENaKTYIASQGCLEATVNDFWQMAWQENSRV 94

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658117657 1132 IVMITNLVEKGRRKCDQYWP-LDSQEEYGSFLVTLRSTKVLAYYTQRTFTL---KNTRAKkgsqkeqtheRTVVQYHYTQ 1207
Cdd:cd14606     95 IVMTTREVEKGRNKCVPYWPeVGMQRAYGPYSVTNCGEHDTTEYKLRTLQVsplDNGELI----------REIWHYQYLS 164

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658117657 1208 WPDMGVPEYTLPVLTFVRK--SSQANLGNMGPVVVHCSAGVGRTGTYIVLDSMLRQIKEQGT---VNILGFLKHIRTQRN 1282
Cdd:cd14606    165 WPDHGVPSEPGGVLSFLDQinQRQESLPHAGPIIVHCSAGIGRTGTIIVIDMLMENISTKGLdcdIDIQKTIQMVRAQRS 244

                          250       260
                   ....*....|....*....|..
gi 1658117657 1283 YLVQTEEQYIFIHDALVEAILS 1304
Cdd:cd14606    245 GMVQTEAQYKFIYVAIAQFIET 266

PTPc-N1_2

cd14545

catalytic domain of tyrosine-protein phosphatase non-receptor type 1 and type 2; ...

1060-1293

7.96e-64

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: 216.87 E-value: 7.96e-64

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658117657 1060 KNKNRYINILAYDHSRVKLssssdrNGWSADYINANYVDGFTQPKAYIATQGPLKSSMEDFWRMVWEQNASVIVMITNLV 1139
Cdd:cd14545      1 LNRYRDRDPYDHDRSRVKL------KQGDNDYINASLVEVEEAKRSYILTQGPLPNTSGHFWQMVWEQNSKAVIMLNKLM 74

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658117657 1140 EKGRRKCDQYWPLDSQE----EYGSFLVTLRSTKVLAYYTQRTFTLKNtraKKGSQkeqthERTVVQYHYTQWPDMGVPE 1215
Cdd:cd14545     75 EKGQIKCAQYWPQGEGNamifEDTGLKVTLLSEEDKSYYTVRTLELEN---LKTQE-----TREVLHFHYTTWPDFGVPE 146

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658117657 1216 YTLPVLTFVRKSSQANL--GNMGPVVVHCSAGVGRTGTYIVLDSMLRQIKEQGT--VNILGFLKHIRTQRNYLVQTEEQY 1291
Cdd:cd14545    147 SPAAFLNFLQKVRESGSlsSDVGPPVVHCSAGIGRSGTFCLVDTCLVLIEKGNPssVDVKKVLLEMRKYRMGLIQTPDQL 226


                   ..
gi 1658117657 1292 IF 1293
Cdd:cd14545    227 RF 228

R-PTP-F-2

cd14629

PTP-like domain of receptor-type tyrosine-protein phosphatase F, repeat 2; Receptor-type ...

1038-1300

1.67e-63

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: 218.44 E-value: 1.67e-63

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658117657 1038 EEIQACTVDLGITADSSIH---------PENKNKNRYINILAYDHSRVKLSSSSDRNGwsADYINANYVDGFTQPKAYIA 1108
Cdd:cd14629     23 ESVTAMELEFKLLANSKAHtsrfisanlPCNKFKNRLVNIMPYELTRVCLQPIRGVEG--SDYINASFIDGYRQQKAYIA 100

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658117657 1109 TQGPLKSSMEDFWRMVWEQNASVIVMITNLVEKGRRKCDQYWPLDSQEEYGSFLVTLRSTKVLAYYTQRTFtlKNTRAKK 1188
Cdd:cd14629    101 TQGPLAETTEDFWRMLWEHNSTIVVMLTKLREMGREKCHQYWPAERSARYQYFVVDPMAEYNMPQYILREF--KVTDARD 178

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658117657 1189 GsqkeqtHERTVVQYHYTQWPDMGVPEYTLPVLTFVRK--SSQANLGNMGPVVVHCSAGVGRTGTYIVLDSMLRQIKEQG 1266
Cdd:cd14629    179 G------QSRTIRQFQFTDWPEQGVPKTGEGFIDFIGQvhKTKEQFGQDGPITVHCSAGVGRTGVFITLSIVLERMRYEG 252

                          250       260       270
                   ....*....|....*....|....*....|....
gi 1658117657 1267 TVNILGFLKHIRTQRNYLVQTEEQYIFIHDALVE 1300
Cdd:cd14629    253 VVDMFQTVKTLRTQRPAMVQTEDQYQLCYRAALE 286

R-PTP-N

cd14609

PTP-like domain of receptor-type tyrosine-protein phosphatase N; Receptor-type ...

1020-1302

1.38e-60

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: 209.51 E-value: 1.38e-60

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658117657 1020 LHDSNTFSQEFEILKECYEEIQACTVDLGITadssihpeNKNKNRYINILAYDHSRVKLSSssDRNGWSADYINAN-YVD 1098
Cdd:cd14609     11 LRNRDRLAKEWQALCAYQAEPNTCSTAQGEA--------NVKKNRNPDFVPYDHARIKLKA--ESNPSRSDYINASpIIE 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658117657 1099 GFTQPKAYIATQGPLKSSMEDFWRMVWEQNASVIVMITNLVEKGRRKCDQYWPLDSQEEYGSFLVTLRSTKVLAY-YTQR 1177
Cdd:cd14609     81 HDPRMPAYIATQGPLSHTIADFWQMVWENGCTVIVMLTPLVEDGVKQCDRYWPDEGSSLYHIYEVNLVSEHIWCEdFLVR 160

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658117657 1178 TFTLKNTrakkgsqkeQTHE-RTVVQYHYTQWPDMGVPEYTLPVLTFVRKSSQANLGNMGPVVVHCSAGVGRTGTYIVLD 1256
Cdd:cd14609    161 SFYLKNV---------QTQEtRTLTQFHFLSWPAEGIPSSTRPLLDFRRKVNKCYRGRSCPIIVHCSDGAGRTGTYILID 231

                          250       260       270       280
                   ....*....|....*....|....*....|....*....|....*..
gi 1658117657 1257 SML-RQIKEQGTVNILGFLKHIRTQRNYLVQTEEQYIFIHDALVEAI 1302
Cdd:cd14609    232 MVLnRMAKGVKEIDIAATLEHVRDQRPGMVRTKDQFEFALTAVAEEV 278

R-PTP-N2

cd14610

PTP-like domain of receptor-type tyrosine-protein phosphatase N2; Receptor-type ...

1020-1302

2.30e-60

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: 209.14 E-value: 2.30e-60

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658117657 1020 LHDSNTFSQEFEILKECYEEIQACTVdlgitadsSIHPENKNKNRYINILAYDHSRVKLSSSSDRNgwSADYINANYV-D 1098
Cdd:cd14610     13 LKNKNRLEKEWEALCAYQAEPNATNV--------AQREENVQKNRSLAVLPYDHSRIILKAENSHS--HSDYINASPImD 82

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658117657 1099 GFTQPKAYIATQGPLKSSMEDFWRMVWEQNASVIVMITNLVEKGRRKCDQYWPLDSQEEYGSFLVTLRSTKVLAY-YTQR 1177
Cdd:cd14610     83 HDPRNPAYIATQGPLPATVADFWQMVWESGCVVIVMLTPLAENGVKQCYHYWPDEGSNLYHIYEVNLVSEHIWCEdFLVR 162

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658117657 1178 TFTLKNTrakkgsqkeQTHE-RTVVQYHYTQWPDMGVPEYTLPVLTFVRKSSQANLGNMGPVVVHCSAGVGRTGTYIVLD 1256
Cdd:cd14610    163 SFYLKNL---------QTNEtRTVTQFHFLSWNDQGVPASTRSLLDFRRKVNKCYRGRSCPIIVHCSDGAGRSGTYILID 233

                          250       260       270       280
                   ....*....|....*....|....*....|....*....|....*..
gi 1658117657 1257 SMLRQI-KEQGTVNILGFLKHIRTQRNYLVQTEEQYIFIHDALVEAI 1302
Cdd:cd14610    234 MVLNKMaKGAKEIDIAATLEHLRDQRPGMVQTKEQFEFALTAVAEEV 280

PTPc-N3_4

cd14541

catalytic domain of tyrosine-protein phosphatase non-receptor type 21 and type 14; ...

1090-1304

6.73e-60

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: 204.87 E-value: 6.73e-60

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658117657 1090 DYINANYVDGFTqPKA-----YIATQGPLKSSMEDFWRMVWEQNASVIVMITNLVEKGRRKCDQYWP-LDSQEEYGSFLV 1163
Cdd:cd14541      1 DYINANYVNMEI-PGSgivnrYIAAQGPLPNTCADFWQMVWEQKSTLIVMLTTLVERGRVKCHQYWPdLGETMQFGNLQI 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658117657 1164 TLRSTKVLAYYTQRTFTLKNTrakkgsqkEQTHERTVVQYHYTQWPDMGVPEYTLPVLTFVRKSSQANLGNMGPVVVHCS 1243
Cdd:cd14541     80 TCVSEEVTPSFAFREFILTNT--------NTGEERHITQMQYLAWPDHGVPDDSSDFLDFVKRVRQNRVGMVEPTVVHCS 151

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1658117657 1244 AGVGRTGTYIVLDSMLRQIKEQGTVNILGFLKHIRTQRNYLVQTEEQYIFIhdalVEAILS 1304
Cdd:cd14541    152 AGIGRTGVLITMETAMCLIEANEPVYPLDIVRTMRDQRAMLIQTPSQYRFV----CEAILR 208

PTPc-N7

cd14612

catalytic domain of tyrosine-protein phosphatase non-receptor type 7; Tyrosine-protein ...

1057-1298

1.25e-59

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: 205.45 E-value: 1.25e-59

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658117657 1057 PENKNKNRYINILAYDHSRVKLSSSSDRNGwSADYINANYVDGFT-QPKAYIATQGPLKSSMEDFWRMVWEQNASVIVMI 1135
Cdd:cd14612     13 PGHASKDRYKTILPNPQSRVCLRRAGSQEE-EGSYINANYIRGYDgKEKAYIATQGPMLNTVSDFWEMVWQEECPIIVMI 91

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658117657 1136 TNLVEKgRRKCDQYWPlDSQEEYGSFLVTLRSTKVLAYYTQRTFTLKNtrakkgsqkeQTHERTVVQYHYTQWPDMGVPE 1215
Cdd:cd14612     92 TKLKEK-KEKCVHYWP-EKEGTYGRFEIRVQDMKECDGYTIRDLTIQL----------EEESRSVKHYWFSSWPDHQTPE 159

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658117657 1216 YTLPVLTFVRK--SSQANLGNMGPVVVHCSAGVGRTGTYIVLDSMLRQIKEQGTVNILGFLKHIRTQRNYLVQTEEQYIF 1293
Cdd:cd14612    160 SAGPLLRLVAEveESRQTAASPGPIVVHCSAGIGRTGCFIATSIGCQQLKDTGKVDILGIVCQLRLDRGGMIQTSEQYQF 239


                   ....*
gi 1658117657 1294 IHDAL 1298
Cdd:cd14612    240 LHHTL 244

R-PTPc-A-E-2

cd14552

catalytic domain of receptor-type tyrosine-protein phosphatase A and E, repeat 2; ...

1091-1299

2.51e-59

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: 202.88 E-value: 2.51e-59

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658117657 1091 YINANYVDGFTQPKAYIATQGPLKSSMEDFWRMVWEQNASVIVMITNLVEKGRRKCDQYWPLDSQEEYGSFLVTLRSTKV 1170
Cdd:cd14552      1 YINASFIDGYRQKDAYIATQGPLDHTVEDFWRMIWEWKSCSIVMLTEIKERSQNKCAQYWPEDGSVSSGDITVELKDQTD 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658117657 1171 LAYYTQRTFTLKNTRAKKgsqkeqthERTVVQYHYTQWPDMGVPEY---TLPVLTFVRKSSQANlGNmGPVVVHCSAGVG 1247
Cdd:cd14552     81 YEDYTLRDFLVTKGKGGS--------TRTVRQFHFHGWPEVGIPDNgkgMIDLIAAVQKQQQQS-GN-HPITVHCSAGAG 150

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|..
gi 1658117657 1248 RTGTYIVLDSMLRQIKEQGTVNILGFLKHIRTQRNYLVQTEEQYIFIHDALV 1299
Cdd:cd14552    151 RTGTFCALSTVLERVKAEGVLDVFQVVKSLRLQRPHMVQTLEQYEFCYKVVQ 202

PTPc-N20_13

cd14538

catalytic domain of tyrosine-protein phosphatase non-receptor type 20 and type 13; ...

1091-1302

3.55e-59

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: 202.60 E-value: 3.55e-59

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658117657 1091 YINANYV--DGFTQPKAYIATQGPLKSSMEDFWRMVWEQNASVIVMITNLVEKGRRKCDQYWPLDSQE---EYGSFLVTL 1165
Cdd:cd14538      1 YINASHIriPVGGDTYHYIACQGPLPNTTGDFWQMVWEQKSEVIAMVTQDVEGGKVKCHRYWPDSLNKpliCGGRLEVSL 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658117657 1166 RSTKVLAYYTQRTFTLKntrakkgsQKEQTHERTVVQYHYTQWPDMGVPEYTLPVLTFVRKSSQanLGNMGPVVVHCSAG 1245
Cdd:cd14538     81 EKYQSLQDFVIRRISLR--------DKETGEVHHITHLNFTTWPDHGTPQSADPLLRFIRYMRR--IHNSGPIVVHCSAG 150

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 1658117657 1246 VGRTGTYIVLDSMLRQIKEQGTVNILGFLKHIRTQRNYLVQTEEQYIFIHDALVEAI 1302
Cdd:cd14538    151 IGRTGVLITIDVALGLIERDLPFDIQDIVKDLREQRQGMIQTKDQYIFCYKACLEVL 207

PTPc-N18

cd14603

catalytic domain of tyrosine-protein phosphatase non-receptor type 18; Tyrosine-protein ...

1037-1300

3.85e-59

catalytic domain of tyrosine-protein phosphatase non-receptor type 18; Tyrosine-protein phosphatase non-receptor type 18 (PTPN18), also called brain-derived phosphatase, belongs to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. PTPN18 regulates HER2-mediated cellular functions through defining both its phosphorylation and ubiquitination states. The N-terminal catalytic PTP domain of PTPN18 blocks lysosomal routing and delays the degradation of HER2 by dephosphorylation, and its C-terminal PEST domain promotes K48-linked HER2 ubiquitination and its destruction via the proteasome pathway.

Pssm-ID: 350451 [Multi-domain] Cd Length: 266 Bit Score: 205.06 E-value: 3.85e-59

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658117657 1037 YEEIQACTV----DLGITADSSIHPENKNKNRYINILAYDHSRVKLSSSSDRNGwsADYINANYVDGFTQPKAYIATQGP 1112
Cdd:cd14603      4 FSEIRACSAafkaDYVCSTVAGGRKENVKKNRYKDILPYDQTRVILSLLQEEGH--SDYINANFIKGVDGSRAYIATQGP 81

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658117657 1113 LKSSMEDFWRMVWEQNASVIVMITNLVEKGRRKCDQYWPLDSQE-EYGSFLVT-LRSTKVLAYYTQRTFTLKntrakkgS 1190
Cdd:cd14603     82 LSHTVLDFWRMIWQYGVKVILMACREIEMGKKKCERYWAQEQEPlQTGPFTITlVKEKRLNEEVILRTLKVT-------F 154

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658117657 1191 QKEqthERTVVQYHYTQWPDMGVPEYTLPVLTFVRKSSQANLGNMGPVVVHCSAGVGRTGTYIVLD---SMLRQIKEQGT 1267
Cdd:cd14603    155 QKE---SRSVSHFQYMAWPDHGIPDSPDCMLAMIELARRLQGSGPEPLCVHCSAGCGRTGVICTVDyvrQLLLTQRIPPD 231

                          250       260       270
                   ....*....|....*....|....*....|...
gi 1658117657 1268 VNILGFLKHIRTQRNYLVQTEEQYIFIHDALVE 1300
Cdd:cd14603    232 FSIFDVVLEMRKQRPAAVQTEEQYEFLYHTVAQ 264

PTPc-N12

cd14604

catalytic domain of tyrosine-protein phosphatase non-receptor type 12; Tyrosine-protein ...

1010-1300

6.61e-59

catalytic domain of tyrosine-protein phosphatase non-receptor type 12; Tyrosine-protein phosphatase non-receptor type 12 (PTPN12), also called PTP-PEST or protein-tyrosine phosphatase G1 (PTPG1), belongs to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. PTPN12 is characterized as a tumor suppressor and a pivotal regulator of EGFR/HER2 signaling. It regulates various physiological processes, including cell migration, immune response, and neuronal activity, by dephosphorylating multiple substrates including HER2, FAK, PYK2, PSTPIP, WASP, p130Cas, paxillin, Shc, catenin, c-Abl, ArgBP2, p190RhoGAP, RhoGDI, cell adhesion kinase beta, and Rho GTPase.

Pssm-ID: 350452 [Multi-domain] Cd Length: 297 Bit Score: 205.55 E-value: 6.61e-59

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658117657 1010 IKQFVKHVAELHDS-----NTFSQEFEILKECYEEIQACTVDLGITADSSihpENKNKNRYINILAYDHSRVKLS---SS 1081
Cdd:cd14604      6 LKKFIERVQAMKSTdhngeDNFASDFMRLRRLSTKYRTEKIYPTATGEKE---ENVKKNRYKDILPFDHSRVKLTlktSS 82

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658117657 1082 SDrngwsADYINANYVDGFTQPKAYIATQGPLKSSMEDFWRMVWEQNASVIVMITNLVEKGRRKCDQYWPLDSQE--EYG 1159
Cdd:cd14604     83 QD-----SDYINANFIKGVYGPKAYIATQGPLANTVIDFWRMIWEYNVAIIVMACREFEMGRKKCERYWPLYGEEpmTFG 157

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658117657 1160 SFLVTLRSTKVLAYYTQRTFTLKNtrakkgsqkeQTHERTVVQYHYTQWPDMGVP---EYTLPVLTFVRKSSQAnlgNMG 1236
Cdd:cd14604    158 PFRISCEAEQARTDYFIRTLLLEF----------QNETRRLYQFHYVNWPDHDVPssfDSILDMISLMRKYQEH---EDV 224

                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1658117657 1237 PVVVHCSAGVGRTGTYIVLD---SMLRQIKEQGTVNILGFLKHIRTQRNYLVQTEEQYIFIHDALVE 1300
Cdd:cd14604    225 PICIHCSAGCGRTGAICAIDytwNLLKAGKIPEEFNVFNLIQEMRTQRHSAVQTKEQYELVHRAIAQ 291

R-PTPc-Q

cd14616

catalytic domain of receptor-type tyrosine-protein phosphatase Q; Receptor-type ...

1063-1295

7.15e-59

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: 202.44 E-value: 7.15e-59

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658117657 1063 NRYINILAYDHSRVKLSSSSDRNGwsADYINANYVDGFTQPKAYIATQGPLKSSMEDFWRMVWEQNASVIVMITNLVEKG 1142
Cdd:cd14616      1 NRFPNIKPYNNNRVKLIADAGVPG--SDYINASYISGYLCPNEFIATQGPLPGTVGDFWRMVWETRAKTIVMLTQCFEKG 78

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658117657 1143 RRKCDQYWPLDSQ--EEYGSFLVTLRSTKVLAYYTQRTFTLKntraKKGsqkeqtHERTVVQYHYTQWPDMGVPEYTLPV 1220
Cdd:cd14616     79 RIRCHQYWPEDNKpvTVFGDIVITKLMEDVQIDWTIRDLKIE----RHG------DYMMVRQCNFTSWPEHGVPESSAPL 148

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1658117657 1221 LTFVRKSSQANLGNMGPVVVHCSAGVGRTGTYIVLDSMLRQIKEQGTVNILGFLKHIRTQRNYLVQTEEQYIFIH 1295
Cdd:cd14616    149 IHFVKLVRASRAHDNTPMIVHCSAGVGRTGVFIALDHLTQHINDHDFVDIYGLVAELRSERMCMVQNLAQYIFLH 223

PTPc-N22

cd14602

catalytic domain of tyrosine-protein phosphatase non-receptor type 22; Tyrosine-protein ...

1062-1300

9.44e-59

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: 202.38 E-value: 9.44e-59

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658117657 1062 KNRYINILAYDHSRVKLS-SSSDRNgwsADYINANYVDGFTQPKAYIATQGPLKSSMEDFWRMVWEQNASVIVMITNLVE 1140
Cdd:cd14602      1 KNRYKDILPYDHSRVELSlITSDED---SDYINANFIKGVYGPRAYIATQGPLSTTLLDFWRMIWEYSVLIIVMACMEFE 77

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658117657 1141 KGRRKCDQYW--PLDSQEEYGSFLVTLRSTKVLAYYTQRTFtlkntRAKKGSQKeqtheRTVVQYHYTQWPDMGVPEYTL 1218
Cdd:cd14602     78 MGKKKCERYWaePGEMQLEFGPFSVTCEAEKRKSDYIIRTL-----KVKFNSET-----RTIYQFHYKNWPDHDVPSSID 147

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658117657 1219 PVLTFVRKSSQANLGNMGPVVVHCSAGVGRTGTYIVLDSMLRQIKEqGTV----NILGFLKHIRTQRNYLVQTEEQYIFI 1294
Cdd:cd14602    148 PILELIWDVRCYQEDDSVPICIHCSAGCGRTGVICAIDYTWMLLKD-GIIpenfSVFSLIQEMRTQRPSLVQTKEQYELV 226


                   ....*.
gi 1658117657 1295 HDALVE 1300
Cdd:cd14602    227 YNAVIE 232

PTPc-N2

cd14607

catalytic domain of tyrosine-protein phosphatase non-receptor type 2; Tyrosine-protein ...

1056-1298

4.54e-58

catalytic domain of tyrosine-protein phosphatase non-receptor type 2; Tyrosine-protein phosphatase non-receptor type 2 (PTPN2), also called T-cell protein-tyrosine phosphatase (TCPTP), belongs to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. PTPN2, a tumor suppressor, dephosphorylates and inactivates EGFRs, Src family kinases, Janus-activated kinases (JAKs)-1 and -3, and signal transducer and activators of transcription (STATs)-1, -3 and -5, in a cell type and context-dependent manner. It is deleted in 6% of all T-cell acute lymphoblastic leukemias and is associated with constitutive JAK1/STAT5 signaling and tumorigenesis.

Pssm-ID: 350455 [Multi-domain] Cd Length: 257 Bit Score: 201.35 E-value: 4.54e-58

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658117657 1056 HPENKNKNRYINILAYDHSRVKLSSSSDrngwsaDYINANYVDGFTQPKAYIATQGPLKSSMEDFWRMVWEQNASVIVMI 1135
Cdd:cd14607     21 YPENRNRNRYRDVSPYDHSRVKLQNTEN------DYINASLVVIEEAQRSYILTQGPLPNTCCHFWLMVWQQKTKAVVML 94

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658117657 1136 TNLVEKGRRKCDQYWPLDSQEEYG----SFLVTLRSTKVLAYYTQRTFTLKNtrAKKGSQKEQTHertvvqYHYTQWPDM 1211
Cdd:cd14607     95 NRIVEKDSVKCAQYWPTDEEEVLSfketGFSVKLLSEDVKSYYTVHLLQLEN--INSGETRTISH------FHYTTWPDF 166

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658117657 1212 GVPEYTLPVLTF---VRKSSQANLGNmGPVVVHCSAGVGRTGTYIVLDS--MLRQIKEQGTVNILGFLKHIRTQRNYLVQ 1286
Cdd:cd14607    167 GVPESPASFLNFlfkVRESGSLSPEH-GPAVVHCSAGIGRSGTFSLVDTclVLMEKKDPDSVDIKQVLLDMRKYRMGLIQ 245

                          250
                   ....*....|..
gi 1658117657 1287 TEEQYIFIHDAL 1298
Cdd:cd14607    246 TPDQLRFSYMAV 257

R-PTPc-R

cd14611

catalytic domain of receptor-type tyrosine-protein phosphatase R; Receptor-type ...

1062-1295

9.41e-58

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

Pssm-ID: 350459 [Multi-domain] Cd Length: 226 Bit Score: 199.37 E-value: 9.41e-58

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658117657 1062 KNRYINILAYDHSRVKLSSSSDRNGWSAdYINANYVDGFT-QPKAYIATQGPLKSSMEDFWRMVWEQNASVIVMITNLVE 1140
Cdd:cd14611      2 KNRYKTILPNPHSRVCLKPKNSNDSLST-YINANYIRGYGgKEKAFIATQGPMINTVNDFWQMVWQEDSPVIVMITKLKE 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658117657 1141 KGRrKCDQYWPlDSQEEYGSFLVTLRSTKVLAYYTQRTFTLKNtrakkGSQKeqtheRTVVQYHYTQWPDMGVPEYTLPV 1220
Cdd:cd14611     81 KNE-KCVLYWP-EKRGIYGKVEVLVNSVKECDNYTIRNLTLKQ-----GSQS-----RSVKHYWYTSWPDHKTPDSAQPL 148

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1658117657 1221 LTF---VRKSSQANLGNmGPVVVHCSAGVGRTGTYIVLDSMLRQIKEQGTVNILGFLKHIRTQRNYLVQTEEQYIFIH 1295
Cdd:cd14611    149 LQLmldVEEDRLASPGR-GPVVVHCSAGIGRTGCFIATTIGCQQLKEEGVVDVLSIVCQLRVDRGGMVQTSEQYEFVH 225

R-PTP-N-N2

cd14546

PTP-like domain of receptor-type tyrosine-protein phosphatase-like N and N2; Receptor-type ...

1091-1302

9.43e-58

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: 198.44 E-value: 9.43e-58

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658117657 1091 YINANYV-DGFTQPKAYIATQGPLKSSMEDFWRMVWEQNASVIVMITNLVEKGRRKCDQYWPLDSQEEYGSFLVTLRSTK 1169
Cdd:cd14546      1 YINASTIyDHDPRNPAYIATQGPLPHTIADFWQMIWEQGCVVIVMLTRLQENGVKQCARYWPEEGSEVYHIYEVHLVSEH 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658117657 1170 VL-AYYTQRTFTLKNTrakkgsqkeQTHE-RTVVQYHYTQWPDMGVPEYTLPVLTFVRKSSQANLGNMGPVVVHCSAGVG 1247
Cdd:cd14546     81 IWcDDYLVRSFYLKNL---------QTSEtRTVTQFHFLSWPDEGIPASAKPLLEFRRKVNKSYRGRSCPIVVHCSDGAG 151

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 1658117657 1248 RTGTYIVLD----SMLRQIKEqgtVNILGFLKHIRTQRNYLVQTEEQYIFIHDALVEAI 1302
Cdd:cd14546    152 RTGTYILIDmvlnRMAKGAKE---IDIAATLEHLRDQRPGMVKTKDQFEFVLTAVAEEV 207

PTPc-N3

cd14600

catalytic domain of tyrosine-protein phosphatase non-receptor type 3; Tyrosine-protein ...

1057-1303

1.27e-57

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: 200.85 E-value: 1.27e-57

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658117657 1057 PENKNKNRYINILAYDHSRVKLSSSSDrngwsadYINANYVDgfTQPKA------YIATQGPLKSSMEDFWRMVWEQNAS 1130
Cdd:cd14600     38 PQNMDKNRYKDVLPYDATRVVLQGNED-------YINASYVN--MEIPSanivnkYIATQGPLPHTCAQFWQVVWEQKLS 108

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658117657 1131 VIVMITNLVEKGRRKCDQYWPlDSQE--EYGSFLVTLRSTKVLAYYTQRTFTLKNTrakkgsqkEQTHERTVVQYHYTQW 1208
Cdd:cd14600    109 LIVMLTTLTERGRTKCHQYWP-DPPDvmEYGGFRVQCHSEDCTIAYVFREMLLTNT--------QTGEERTVTHLQYVAW 179

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658117657 1209 PDMGVPEYTLPVLTFVRKSSQANLGNMgPVVVHCSAGVGRTGTYIVLDSMLRQIKEQGTVNILGFLKHIRTQRNYLVQTE 1288
Cdd:cd14600    180 PDHGVPDDSSDFLEFVNYVRSKRVENE-PVLVHCSAGIGRTGVLVTMETAMCLTERNQPVYPLDIVRKMRDQRAMMVQTS 258

                          250
                   ....*....|....*
gi 1658117657 1289 EQYIFIhdalVEAIL 1303
Cdd:cd14600    259 SQYKFV----CEAIL 269

PTPc-N1

cd14608

catalytic domain of tyrosine-protein phosphatase non-receptor type 1; Tyrosine-protein ...

1037-1300

4.22e-57

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: 199.48 E-value: 4.22e-57

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658117657 1037 YEEIQACTVDLgiTADSSIHPENKNKNRYINILAYDHSRVKLSSSSDrngwsaDYINANYVDGFTQPKAYIATQGPLKSS 1116
Cdd:cd14608      5 YQDIRHEASDF--PCRVAKLPKNKNRNRYRDVSPFDHSRIKLHQEDN------DYINASLIKMEEAQRSYILTQGPLPNT 76

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658117657 1117 MEDFWRMVWEQNASVIVMITNLVEKGRRKCDQYWPLDSQEEY----GSFLVTLRSTKVLAYYTQRTFTLKNTRAKKgsqk 1192
Cdd:cd14608     77 CGHFWEMVWEQKSRGVVMLNRVMEKGSLKCAQYWPQKEEKEMifedTNLKLTLISEDIKSYYTVRQLELENLTTQE---- 152

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658117657 1193 eqthERTVVQYHYTQWPDMGVPEYTLPVLTF---VRKSSQANlGNMGPVVVHCSAGVGRTGTYIVLDS---MLRQIKEQG 1266
Cdd:cd14608    153 ----TREILHFHYTTWPDFGVPESPASFLNFlfkVRESGSLS-PEHGPVVVHCSAGIGRSGTFCLADTcllLMDKRKDPS 227

                          250       260       270
                   ....*....|....*....|....*....|....
gi 1658117657 1267 TVNILGFLKHIRTQRNYLVQTEEQYIFIHDALVE 1300
Cdd:cd14608    228 SVDIKKVLLEMRKFRMGLIQTADQLRFSYLAVIE 261

PTPc-N5

cd14613

catalytic domain of tyrosine-protein phosphatase non-receptor type 5; Tyrosine-protein ...

1062-1298

6.23e-57

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: 198.16 E-value: 6.23e-57

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658117657 1062 KNRYINILAYDHSRVKLSSSSDRNGWSAdYINANYVDGF-TQPKAYIATQGPLKSSMEDFWRMVWEQNASVIVMITNLVE 1140
Cdd:cd14613     28 KNRYKTILPNPHSRVCLTSPDQDDPLSS-YINANYIRGYgGEEKVYIATQGPTVNTVGDFWRMVWQERSPIIVMITNIEE 106

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658117657 1141 KGRrKCDQYWPlDSQEEYGSFLVTLRSTKVLAYYTQRTFTLKNtrakkgsqkeQTHERTVVQYHYTQWPDMGVPEYTLPV 1220
Cdd:cd14613    107 MNE-KCTEYWP-EEQVTYEGIEITVKQVIHADDYRLRLITLKS----------GGEERGLKHYWYTSWPDQKTPDNAPPL 174

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658117657 1221 LTFVRK---SSQANLGNMGPVVVHCSAGVGRTGTYIVLDSMLRQIKEQGTVNILGFLKHIRTQRNYLVQTEEQYIFIHDA 1297
Cdd:cd14613    175 LQLVQEveeARQQAEPNCGPVIVHCSAGIGRTGCFIATSICCKQLRNEGVVDILRTTCQLRLDRGGMIQTCEQYQFVHHV 254


                   .
gi 1658117657 1298 L 1298
Cdd:cd14613    255 L 255

R-PTPc-A-2

cd14623

catalytic domain of receptor-type tyrosine-protein phosphatase A, repeat 2; Receptor-type ...

1064-1300

3.57e-56

catalytic domain of receptor-type tyrosine-protein phosphatase A, repeat 2; Receptor-type tyrosine-protein phosphatase A (PTPRA), also known as receptor-type tyrosine-protein phosphatase alpha (R-PTP-alpha), belongs to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. PTPRA is a positive regulator of Src and Src family kinases via dephosphorylation of the Src-inhibitory tyrosine 527. Thus, it affects transformation and tumorigenesis, inhibition of proliferation, cell cycle arrest, integrin signaling, neuronal differentiation and outgrowth, and ion channel activity. It is also involved in interleukin-1 signaling in fibroblasts through its interaction with the focal adhesion targeting domain of focal adhesion kinase. PTPRA comprises a small extracellular domain, a transmembrane segment, and an intracellular region containing two tandem catalytic PTP domains. This model represents the second PTP domain (repeat 2).

Pssm-ID: 350471 [Multi-domain] Cd Length: 228 Bit Score: 194.88 E-value: 3.57e-56

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658117657 1064 RYINILAYDHSRVKLSSSsdRNGWSADYINANYVDGFTQPKAYIATQGPLKSSMEDFWRMVWEQNASVIVMITNLVEKGR 1143
Cdd:cd14623      1 RVLQIIPYEFNRVIIPVK--RGEENTDYVNASFIDGYRQKDSYIASQGPLQHTIEDFWRMIWEWKSCSIVMLTELEERGQ 78

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658117657 1144 RKCDQYWPLDSQEEYGSFLVTLRSTKVLAYYTQRTFTLKNTRAKKgsqkeqthERTVVQYHYTQWPDMGVP---EYTLPV 1220
Cdd:cd14623     79 EKCAQYWPSDGSVSYGDITIELKKEEECESYTVRDLLVTNTRENK--------SRQIRQFHFHGWPEVGIPsdgKGMINI 150

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658117657 1221 LTFVRKSSQANlGNMgPVVVHCSAGVGRTGTYIVLDSMLRQIKEQGTVNILGFLKHIRTQRNYLVQTEEQYIFIHDALVE 1300
Cdd:cd14623    151 IAAVQKQQQQS-GNH-PITVHCSAGAGRTGTFCALSTVLERVKAEGILDVFQTVKSLRLQRPHMVQTLEQYEFCYKVVQE 228

PTPc-N22_18_12

cd14542

catalytic domain of tyrosine-protein phosphatase non-receptor type 22, type 18 and type 12; ...

1091-1295

9.63e-56

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: 192.64 E-value: 9.63e-56

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658117657 1091 YINANYVDGFTQPKAYIATQGPLKSSMEDFWRMVWEQNASVIVMITNLVEKGRRKCDQYWPlDSQEE---YGSFLVTLRS 1167
Cdd:cd14542      1 YINANFIKGVSGSKAYIATQGPLPNTVLDFWRMIWEYNVQVIVMACREFEMGKKKCERYWP-EEGEEqlqFGPFKISLEK 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658117657 1168 TKVLAY-YTQRtfTLKNTRakkgsQKEqthERTVVQYHYTQWPDMGVPEYTLPVLTFVRKSSQANLGNMGPVVVHCSAGV 1246
Cdd:cd14542     80 EKRVGPdFLIR--TLKVTF-----QKE---SRTVYQFHYTAWPDHGVPSSVDPILDLVRLVRDYQGSEDVPICVHCSAGC 149

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|..
gi 1658117657 1247 GRTGTYIVLD---SMLRQIKEQGTVNILGFLKHIRTQRNYLVQTEEQYIFIH 1295
Cdd:cd14542    150 GRTGTICAIDyvwNLLKTGKIPEEFSLFDLVREMRKQRPAMVQTKEQYELVY 201

PTPc-N13

cd14597

catalytic domain of tyrosine-protein phosphatase non-receptor type 13; Tyrosine-protein ...

1058-1293

1.98e-53

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: 187.34 E-value: 1.98e-53

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658117657 1058 ENKNKNRYINILAYDHSRVKLssssdrnGWSADYINANYVD---GFTQpKAYIATQGPLKSSMEDFWRMVWEQNASVIVM 1134
Cdd:cd14597      2 ENRKKNRYKNILPYDTTRVPL-------GDEGGYINASFIKmpvGDEE-FVYIACQGPLPTTVADFWQMVWEQKSTVIAM 73

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658117657 1135 ITNLVEKGRRKCDQYWPldsqEEYGSFL-------VTLRSTKVLAYYTQRTFTLKNTrakkgsqkeQTHE-RTVVQYHYT 1206
Cdd:cd14597     74 MTQEVEGGKIKCQRYWP----EILGKTTmvdnrlqLTLVRMQQLKNFVIRVLELEDI---------QTREvRHITHLNFT 140

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658117657 1207 QWPDMGVPEYTLPVLTFVrkSSQANLGNMGPVVVHCSAGVGRTGTYIVLDSMLRQIKEQGTVNILGFLKHIRTQRNYLVQ 1286
Cdd:cd14597    141 AWPDHDTPSQPEQLLTFI--SYMRHIHKSGPIITHCSAGIGRSGTLICIDVVLGLISKDLDFDISDIVRTMRLQRHGMVQ 218


                   ....*..
gi 1658117657 1287 TEEQYIF 1293
Cdd:cd14597    219 TEDQYIF 225

R-PTPc-E-2

cd14622

catalytic domain of receptor-type tyrosine-protein phosphatase E, repeat 2; Receptor-type ...

1090-1295

2.00e-53

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: 185.98 E-value: 2.00e-53

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658117657 1090 DYINANYVDGFTQPKAYIATQGPLKSSMEDFWRMVWEQNASVIVMITNLVEKGRRKCDQYWPLDSQEEYGSFLVTLRSTK 1169
Cdd:cd14622      1 DYINASFIDGYRQKDYFIATQGPLAHTVEDFWRMVWEWKCHTIVMLTELQEREQEKCVQYWPSEGSVTHGEITIEIKNDT 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658117657 1170 VLAYYTQRTFTLKNtrakkgSQKEQTheRTVVQYHYTQWPDMGVP---EYTLPVLTFVRKSSQANlGNmGPVVVHCSAGV 1246
Cdd:cd14622     81 LLETISIRDFLVTY------NQEKQT--RLVRQFHFHGWPEIGIPaegKGMIDLIAAVQKQQQQT-GN-HPIVVHCSAGA 150

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*....
gi 1658117657 1247 GRTGTYIVLDSMLRQIKEQGTVNILGFLKHIRTQRNYLVQTEEQYIFIH 1295
Cdd:cd14622    151 GRTGTFIALSNILERVKAEGLLDVFQTVKSLRLQRPHMVQTLEQYEFCY 199

PTPc

cd00047

catalytic domain of protein tyrosine phosphatases; Protein tyrosine phosphatases (PTP, EC 3.1. ...

1386-1586

2.01e-53

Pssm-ID: 350343 [Multi-domain] Cd Length: 200 Bit Score: 185.95 E-value: 2.01e-53

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658117657 1386 YINASYIMGYQQSNEFIITQNPLPSTMKDFWKMIWDHSTQVVIALPDGLDLAEDECI-YWPTK-SQPIRFDTFTVTFMGE 1463
Cdd:cd00047      1 YINASYIDGYRGPKEYIATQGPLPNTVEDFWRMVWEQKVSVIVMLTNLVEKGREKCErYWPEEgGKPLEYGDITVTLVSE 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658117657 1464 DHMclsneDMLIVQDFILEATQDDYVLEVRQYRAPRWPNPDGP--ISNTFELINIIKEESVSRDGPIVVHDKRGGNIAGT 1541
Cdd:cd00047     81 EEL-----SDYTIRTLELSPKGCSESREVTHLHYTGWPDHGVPssPEDLLALVRRVRKEARKPNGPIVVHCSAGVGRTGT 155

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*
gi 1658117657 1542 FCALMTLLHQLEMESSFDVYWVAKMINLMRPGIFTDIDQYQFLYK 1586
Cdd:cd00047    156 FIAIDILLERLEAEGEVDVFEIVKALRKQRPGMVQTLEQYEFIYE 200

PHA02738

hypothetical protein; Provisional

1031-1298

8.76e-53

hypothetical protein; Provisional

Pssm-ID: 222923 [Multi-domain] Cd Length: 320 Bit Score: 188.60 E-value: 8.76e-53

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658117657 1031 EILKECYEEIQACTVDLGITADSsihpENKNKNRYINILAYDHSRVKLSSSSDRngwsADYINANYVDGFTQPKAYIATQ 1110
Cdd:PHA02738    25 EVITREHQKVISEKVDGTFNAEK----KNRKLNRYLDAVCFDHSRVILPAERNR----GDYINANYVDGFEYKKKFICGQ 96

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658117657 1111 GPLKSSMEDFWRMVWEQNASVIVMITNLVEKGRRKCDQYWPLDSQEE--YGSFLVTLRSTKVLAYYTQRTFTLKNtrakk 1188
Cdd:PHA02738    97 APTRQTCYDFYRMLWMEHVQIIVMLCKKKENGREKCFPYWSDVEQGSirFGKFKITTTQVETHPHYVKSTLLLTD----- 171

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658117657 1189 GSQKEQtherTVVQYHYTQWPDMGVPEYTLPVLTFVRKSSQA-------------NLGNMGPVVVHCSAGVGRTGTYIVL 1255
Cdd:PHA02738   172 GTSATQ----TVTHFNFTAWPDHDVPKNTSEFLNFVLEVRQCqkelaqeslqighNRLQPPPIVVHCNAGLGRTPCYCVV 247

                          250       260       270       280
                   ....*....|....*....|....*....|....*....|...
gi 1658117657 1256 DSMLRQIKEQGTVNILGFLKHIRTQRNYLVQTEEQYIFIHDAL 1298
Cdd:PHA02738   248 DISISRFDACATVSIPSIVSSIRNQRYYSLFIPFQYFFCYRAV 290

PTP-N23

cd14539

PTP-like domain of tyrosine-protein phosphatase non-receptor type 23; Tyrosine-protein ...

1091-1296

1.97e-52

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: 183.35 E-value: 1.97e-52

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658117657 1091 YINANYVDGFTQPKA-YIATQGPLKSSMEDFWRMVWEQNASVIVMITNLVEKGRRKCDQYWPLD--SQEEYGSFLVTLRS 1167
Cdd:cd14539      1 YINASLIEDLTPYCPrFIATQAPLPGTAADFWLMVYEQQVSVIVMLVSEQENEKQKVHRYWPTErgQALVYGAITVSLQS 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658117657 1168 TKVLAYYTQRTFTLKNtrakkgsqKEQTHERTVVQYHYTQWPDMGVPEYTLPVLTF---VRKSSQANLGNMGPVVVHCSA 1244
Cdd:cd14539     81 VRTTPTHVERIISIQH--------KDTRLSRSVVHLQFTTWPELGLPDSPNPLLRFieeVHSHYLQQRSLQTPIVVHCSS 152

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|...
gi 1658117657 1245 GVGRTGTYIVLDSMLRQIKE-QGTVNILGFLKHIRTQRNYLVQTEEQYIFIHD 1296
Cdd:cd14539    153 GVGRTGAFCLLYAAVQEIEAgNGIPDLPQLVRKMRQQRKYMLQEKEHLKFCYE 205

PTPc-N21_14

cd14540

catalytic domain of tyrosine-protein phosphatase non-receptor type 21 and type 14; ...

1091-1300

2.16e-52

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: 183.81 E-value: 2.16e-52

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658117657 1091 YINANYVDGFTQPKA--YIATQGPLKSSMEDFWRMVWEQNASVIVMITNLVEKGRRKCDQYWPLDSQEE----YGSFLVT 1164
Cdd:cd14540      1 YINASHITATVGGKQrfYIAAQGPLQNTVGDFWQMVWEQGVYLVVMVTAEEEGGREKCFRYWPTLGGEHdaltFGEYKVS 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658117657 1165 LRSTKVLAYYTQRTFTLKNTRAKKgsqkeqthERTVVQYHYTQWPDMGVPEYTLPVLTFVRKSSQANLGNMG-------- 1236
Cdd:cd14540     81 TKFSVSSGCYTTTGLRVKHTLSGQ--------SRTVWHLQYTDWPDHGCPEDVSGFLDFLEEINSVRRHTNQdvaghnrn 152

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1658117657 1237 -PVVVHCSAGVGRTGTYIVLDSMLRQIKEQGTVNILGFLKHIRTQRNYLVQTEEQYIFIHDALVE 1300
Cdd:cd14540    153 pPTLVHCSAGVGRTGVVILADLMLYCLDHNEELDIPRVLALLRHQRMLLVQTLAQYKFVYNVLIQ 217

PHA02747

protein tyrosine phosphatase; Provisional

1050-1295

2.14e-50

protein tyrosine phosphatase; Provisional

Pssm-ID: 165114 [Multi-domain] Cd Length: 312 Bit Score: 181.35 E-value: 2.14e-50

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658117657 1050 TADSSIHPENKNKNRYINILAYDHSRVKLSSSSdrnGWSADYINANYVDGFTQPKAYIATQGPLKSSMEDFWRMVWEQNA 1129
Cdd:PHA02747    42 LIANFEKPENQPKNRYWDIPCWDHNRVILDSGG---GSTSDYIHANWIDGFEDDKKFIATQGPFAETCADFWKAVWQEHC 118

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658117657 1130 SVIVMIT-NLVEKGRRKCDQYWPL--DSQEEYGSFLVTLRSTKVLAYYTQRTFTLKNtrakkgsqKEQTHERTVVQYHYT 1206
Cdd:PHA02747   119 SIIVMLTpTKGTNGEEKCYQYWCLneDGNIDMEDFRIETLKTSVRAKYILTLIEITD--------KILKDSRKISHFQCS 190

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658117657 1207 QWPDMGVPEYTLPVLTF------VRKSSQANLGN----MGPVVVHCSAGVGRTGTYIVLDSMLRQIKEQGTVNILGFLKH 1276
Cdd:PHA02747   191 EWFEDETPSDHPDFIKFikiidiNRKKSGKLFNPkdalLCPIVVHCSDGVGKTGIFCAVDICLNQLVKRKAICLAKTAEK 270

                          250
                   ....*....|....*....
gi 1658117657 1277 IRTQRNYLVQTEEQYIFIH 1295
Cdd:PHA02747   271 IREQRHAGIMNFDDYLFIQ 289

PHA02746

protein tyrosine phosphatase; Provisional

1038-1303

1.68e-49

protein tyrosine phosphatase; Provisional

Pssm-ID: 165113 [Multi-domain] Cd Length: 323 Bit Score: 179.07 E-value: 1.68e-49

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658117657 1038 EEIQACTVDLGITADSSIHPENKNKNRYINILAYDHSRVKLSS-----SSDRNGW------------SADYINANYVDGF 1100
Cdd:PHA02746    30 EHAEVMDIPIRGTTNHFLKKENLKKNRFHDIPCWDHSRVVINAheslkMFDVGDSdgkkievtsednAENYIHANFVDGF 109

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658117657 1101 TQPKAYIATQGPLKSSMEDFWRMVWEQNASVIVMITNlVEKGRRKCDQYW--PLDSQEEYGSFLVtlrstKVLAYYTQRT 1178
Cdd:PHA02746   110 KEANKFICAQGPKEDTSEDFFKLISEHESQVIVSLTD-IDDDDEKCFELWtkEEDSELAFGRFVA-----KILDIIEELS 183

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658117657 1179 FTlkNTRAKKGSQKEQThERTVVQYHYTQWPDMGVPEYTLPVLTFV----------RKSSQANLGNMGPVVVHCSAGVGR 1248
Cdd:PHA02746   184 FT--KTRLMITDKISDT-SREIHHFWFPDWPDNGIPTGMAEFLELInkvneeqaelIKQADNDPQTLGPIVVHCSAGIGR 260

                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1658117657 1249 TGTYIVLDSMLRQIKEQGTVNILGFLKHIRTQRNYLVQTEEQYIFIHDALVEAIL 1303
Cdd:PHA02746   261 AGTFCAIDNALEQLEKEKEVCLGEIVLKIRKQRHSSVFLPEQYAFCYKALKYAII 315

PTPc-N20

cd14596

catalytic domain of tyrosine-protein phosphatase non-receptor type 20; Tyrosine-protein ...

1091-1302

8.77e-49

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: 173.01 E-value: 8.77e-49

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658117657 1091 YINANYVdgfTQPKA-----YIATQGPLKSSMEDFWRMVWEQNASVIVMITNLVEKGRRKCDQYWPLDSQE--EYGSFLV 1163
Cdd:cd14596      1 YINASYI---TMPVGeeelfYIATQGPLPSTIDDFWQMVWENRSDVIAMMTREVERGKVKCHRYWPETLQEpmELENYQL 77

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658117657 1164 TLRSTKVLAYYTQRTFTLkntrakkgSQKEQTHERTVVQYHYTQWPDMGVPEYTLPVLTFVRKSSQANlgNMGPVVVHCS 1243
Cdd:cd14596     78 RLENYQALQYFIIRIIKL--------VEKETGENRLIKHLQFTTWPDHGTPQSSDQLVKFICYMRKVH--NTGPIVVHCS 147

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 1658117657 1244 AGVGRTGTYIVLDSMLRQIKEQGTVNILGFLKHIRTQRNYLVQTEEQYIFIHDALVEAI 1302
Cdd:cd14596    148 AGIGRAGVLICVDVLLSLIEKDLSFNIKDIVREMRQQRYGMIQTKDQYLFCYKVVLEVL 206

PTPc-N14

cd14599

catalytic domain of tyrosine-protein phosphatase non-receptor type 14; Tyrosine-protein ...

1037-1300

1.41e-48

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: 175.19 E-value: 1.41e-48

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658117657 1037 YEEIQACTVDlGITADSSIhPENKNKNRYINILAYDHSRVKLSSSSDRNgwsADYINANYVDGFTQPKA--YIATQGPLK 1114
Cdd:cd14599     18 YEQIPKKKAD-GVFTTATL-PENAERNRIREVVPYEENRVELVPTKENN---TGYINASHIKVTVGGEEwhYIATQGPLP 92

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658117657 1115 SSMEDFWRMVWEQNASVIVMITNLVEKGRRKCDQYWP----LDSQEEYGSFLVTLRSTKVLAYYTQRTFTLKNTRAKKgs 1190
Cdd:cd14599     93 HTCHDFWQMVWEQGVNVIAMVTAEEEGGRSKSHRYWPklgsKHSSATYGKFKVTTKFRTDSGCYATTGLKVKHLLSGQ-- 170

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658117657 1191 qkeqthERTVVQYHYTQWPDMGVPEYTLPVLTF------VRKSSQANLGNMG----PVVVHCSAGVGRTGTYIVLDSMLR 1260
Cdd:cd14599    171 ------ERTVWHLQYTDWPDHGCPEEVQGFLSYleeiqsVRRHTNSMLDSTKncnpPIVVHCSAGVGRTGVVILTELMIG 244

                          250       260       270       280
                   ....*....|....*....|....*....|....*....|
gi 1658117657 1261 QIKEQGTVNILGFLKHIRTQRNYLVQTEEQYIFIHDALVE 1300
Cdd:cd14599    245 CLEHNEKVEVPVMLRHLREQRMFMIQTIAQYKFVYQVLIQ 284

PTPc-N4

cd14601

catalytic domain of tyrosine-protein phosphatase non-receptor type 4; Tyrosine-protein ...

1090-1303

1.76e-48

catalytic domain of tyrosine-protein phosphatase non-receptor type 4; Tyrosine-protein phosphatase non-receptor type 4 (PTPN4), also called protein-tyrosine phosphatase MEG1, belongs to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. PTPN4 functions in TCR cell signaling, apoptosis, cerebellar synaptic plasticity, and innate immune responses. It specifically inhibits the TRIF-dependent TLR4 pathway by suppressing tyrosine phosphorylation of TRAM. It is a large modular protein containing an N-terminal FERM domain, a PDZ domain and a C-terminal catalytic PTP domain; the PDZ domain regulates the catalytic activity of PTPN4.

Pssm-ID: 350449 [Multi-domain] Cd Length: 212 Bit Score: 172.05 E-value: 1.76e-48

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658117657 1090 DYINANYVD----GFTQPKAYIATQGPLKSSMEDFWRMVWEQNASVIVMITNLVEKGRRKCDQYWPLDS-QEEYGSFLVT 1164
Cdd:cd14601      1 DYINANYINmeipSSSIINRYIACQGPLPNTCSDFWQMTWEQGSSMVVMLTTQVERGRVKCHQYWPEPSgSSSYGGFQVT 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658117657 1165 LRSTKVLAYYTQRTFTLKNTrakkgsqkEQTHERTVVQYHYTQWPDMGVPEYTLPVLTFVRKSSQANLGNMGPVVVHCSA 1244
Cdd:cd14601     81 CHSEEGNPAYVFREMTLTNL--------EKNESRPLTQIQYIAWPDHGVPDDSSDFLDFVCLVRNKRAGKDEPVVVHCSA 152

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 1658117657 1245 GVGRTGTYIVLDSMLRQIKEQGTVNILGFLKHIRTQRNYLVQTEEQYIFIhdalVEAIL 1303
Cdd:cd14601    153 GIGRTGVLITMETAMCLIECNQPVYPLDIVRTMRDQRAMMIQTPSQYRFV----CEAIL 207

R-PTP-C-2

cd14558

PTP-like domain of receptor-type tyrosine-protein phosphatase C, repeat 2; Receptor-type ...

1091-1296

2.63e-48

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: 171.42 E-value: 2.63e-48

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658117657 1091 YINANYVDGFTQPKAYIATQGPLKSSMEDFWRMVWEQNASVIVMITNLVEKGRRKCDQYWPlDSQEEYGSFLVTLRSTKV 1170
Cdd:cd14558      1 YINASFIDGYWGPKSLIATQGPLPDTIADFWQMIFQKKVKVIVMLTELKEGDQEQCAQYWG-DEKKTYGDIEVELKDTEK 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658117657 1171 LAYYTQRTFTLKNTRAKKgsqkeqthERTVVQYHYTQWPDMGVPEYTLPVLTFVR------KSSQANLGNMGPVVVHCSA 1244
Cdd:cd14558     80 SPTYTVRVFEITHLKRKD--------SRTVYQYQYHKWKGEELPEKPKDLVDMIKsikqklPYKNSKHGRSVPIVVHCSD 151

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|..
gi 1658117657 1245 GVGRTGTYIVLDSMLRQIKEQGTVNILGFLKHIRTQRNYLVQTEEQYIFIHD 1296
Cdd:cd14558    152 GSSRTGIFCALWNLLESAETEKVVDVFQVVKALRKQRPGMVSTLEQYQFLYD 203

PTPc_plant_PTP1

cd17658

protein tyrosine phosphatase 1 from Arabidopsis thaliana and similar plant PTPs; Arabidopsis ...

1091-1295

1.30e-47

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: 169.57 E-value: 1.30e-47

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658117657 1091 YINANYV--DGFTQPKAYIATQGPLKSSMEDFWRMVWEQNASVIVMITNLVEKGRR-KCDQYWPLD--SQEEYGSFLVTL 1165
Cdd:cd17658      1 YINASLVetPASESLPKFIATQGPLPHTFEDFWEMVIQQRCPVIIMLTRLVDNYSTaKCADYFPAEenESREFGRISVTN 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658117657 1166 RSTKvlayYTQRTFTLKNTRAKKGSQKEQTheRTVVQYHYTQWPDMGVPEYTLPVLTFVRKSSQANlGNMGPVVVHCSAG 1245
Cdd:cd17658     81 KKLK----HSQHSITLRVLEVQYIESEEPP--LSVLHIQYPEWPDHGVPKDTRSVRELLKRLYGIP-PSAGPIVVHCSAG 153

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|..
gi 1658117657 1246 VGRTGTYIVLDSMLRQIKE--QGTVNILGFLKHIRTQRNYLVQTEEQYIFIH 1295
Cdd:cd17658    154 IGRTGAYCTIHNTIRRILEgdMSAVDLSKTVRKFRSQRIGMVQTQDQYIFCY 205

R-PTP-D-2

cd14628

PTP-like domain of receptor-type tyrosine-protein phosphatase D, repeat 2; Receptor-type ...

1307-1589

1.77e-44

Pssm-ID: 350476 [Multi-domain] Cd Length: 292 Bit Score: 163.75 E-value: 1.77e-44

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658117657 1307 TEVHSSHIHTYVNELL-IPGPSGQTPLEKQFKMITQSNAKQCDYSAALKQCNRDKNRNSSLLPVERSRVHLSTTAG-EIS 1384
Cdd:cd14628      1 TEVPARNLYAYIQKLTqIETGENVTGMELEFKRLASSKAHTSRFISANLPCNKFKNRLVNIMPYESTRVCLQPIRGvEGS 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658117657 1385 DYINASYIMGYQQSNEFIITQNPLPSTMKDFWKMIWDHSTQVVIALPDGLDLAEDEC-IYWPTKsQPIRFDTFTVTFMGE 1463
Cdd:cd14628     81 DYINASFIDGYRQQKAYIATQGPLAETTEDFWRMLWEHNSTIVVMLTKLREMGREKChQYWPAE-RSARYQYFVVDPMAE 159

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658117657 1464 DHMclsneDMLIVQDFILEATQDDYVLEVRQYRAPRWPNPDGPISNTfELINIIKE-----ESVSRDGPIVVHDKRGGNI 1538
Cdd:cd14628    160 YNM-----PQYILREFKVTDARDGQSRTVRQFQFTDWPEQGVPKSGE-GFIDFIGQvhktkEQFGQDGPISVHCSAGVGR 233

                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|.
gi 1658117657 1539 AGTFCALMTLLHQLEMESSFDVYWVAKMINLMRPGIFTDIDQYQFLYKVIM 1589
Cdd:cd14628    234 TGVFITLSIVLERMRYEGVVDIFQTVKMLRTQRPAMVQTEDQYQFCYRAAL 284

R-PTPc-typeIIb-2

cd14556

PTP domain of type IIb (or R2B) subfamily receptor-type tyrosine-protein phosphatases, repeat ...

1091-1296

7.54e-44

PTP domain of type IIb (or R2B) subfamily receptor-type tyrosine-protein phosphatases, repeat 2; The type IIb (or R2B) subfamily of receptor protein tyrosine phosphatases (RPTPs) include the prototypical member PTPmu (or PTPRM), PCP-2 (or PTPRU), PTPrho (or PTPRT), and PTPkappa (or PTPRK). They belong to the larger family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. Type IIb RPTPs mediate cell-cell adhesion though homophilic interactions; their ligand is an identical molecule on an adjacent cell. No heterophilic interactions between the subfamily members have been observed. They also commonly function as tumor suppressors. They contain an extracellular region with an Meprin-A5 (neuropilin)-mu (MAM) domain, an immunoglobulin (Ig) domain, and four fibronectin type III (FN3) repeats, a transmembrane domain, and an intracellular segment with a juxtamembrane domain similar to the cytoplasmic domain of classical cadherins and two tandem PTP domains. This model represents the second (repeat 2) PTP domain.

Pssm-ID: 350404 [Multi-domain] Cd Length: 201 Bit Score: 158.34 E-value: 7.54e-44

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658117657 1091 YINANYVDGFTQPKAYIATQGPLKSSMEDFWRMVWEQNASVIVMItNLVEKGRRKCDQYWPLDSQEEYGSFLVTLRSTKV 1170
Cdd:cd14556      1 YINAALLDSYKQPAAFIVTQHPLPNTVTDFWRLVYDYGCTSIVML-NQLDPKDQSCPQYWPDEGSGTYGPIQVEFVSTTI 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658117657 1171 LAYYTQRTFTLKNTRakkgsqKEQTHERTVVQYHYTQWPDMG----VPEYTLPVLTFVRKsSQANLGNmGPVVVHCSAGV 1246
Cdd:cd14556     80 DEDVISRIFRLQNTT------RPQEGYRMVQQFQFLGWPRDRdtppSKRALLKLLSEVEK-WQEQSGE-GPIVVHCLNGV 151

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|
gi 1658117657 1247 GRTGTYIVLDSMLRQIKEQGTVNILGFLKHIRTQRNYLVQTEEQYIFIHD 1296
Cdd:cd14556    152 GRSGVFCAISSVCERIKVENVVDVFQAVKTLRNHRPNMVETEEQYKFCYD 201

COG5599

Protein tyrosine phosphatase [Signal transduction mechanisms];

1057-1294

1.11e-43

Protein tyrosine phosphatase [Signal transduction mechanisms];

Pssm-ID: 444335 [Multi-domain] Cd Length: 282 Bit Score: 161.03 E-value: 1.11e-43

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658117657 1057 PENKNKNRYINILAYDHSRVklsSSSDRngwsadYINANYVDGfTQPKAYIATQGPLKSSMEDFWRMVWEQNASVIVMIT 1136
Cdd:COG5599     40 INGSPLNRFRDIQPYKETAL---RANLG------YLNANYIQV-IGNHRYIATQYPLEEQLEDFFQMLFDNNTPVLVVLA 109

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658117657 1137 NLVE--KGRRKCDQYWPLDsqEEYGSFLVTLRSTKVLAYYTQ---RTFTLKntraKKGSQKEQtheRTVVQYHYTQWPDM 1211
Cdd:COG5599    110 SDDEisKPKVKMPVYFRQD--GEYGKYEVSSELTESIQLRDGieaRTYVLT----IKGTGQKK---IEIPVLHVKNWPDH 180

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658117657 1212 GVP--EYTLPVLTFVRKSSQANLGNMGPVVVHCSAGVGRTGTYIVLDSMLRQIKE--QGTVNILGFLKHIRTQRNY-LVQ 1286
Cdd:COG5599    181 GAIsaEALKNLADLIDKKEKIKDPDKLLPVVHCRAGVGRTGTLIACLALSKSINAlvQITLSVEEIVIDMRTSRNGgMVQ 260


                   ....*...
gi 1658117657 1287 TEEQYIFI 1294
Cdd:COG5599    261 TSEQLDVL 268

PHA02742

protein tyrosine phosphatase; Provisional

1031-1293

3.06e-43

protein tyrosine phosphatase; Provisional

Pssm-ID: 165109 [Multi-domain] Cd Length: 303 Bit Score: 160.55 E-value: 3.06e-43

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658117657 1031 EILKECYEEIQACTVdlGITADSSIHPENKNKNRYINILAYDHSRVKLSSssdRNGWSaDYINANYVDGFTQPKAYIATQ 1110
Cdd:PHA02742    26 EILKEEHEHIMQEIV--AFSCNESLELKNMKKCRYPDAPCFDRNRVILKI---EDGGD-DFINASYVDGHNAKGRFICTQ 99

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658117657 1111 GPLKSSMEDFWRMVWEQNASVIVMITNLVEKGRRKCDQYWPLD--SQEEYGSFLVTLRSTKVLAYYTQRTFTLKNTRAkk 1188
Cdd:PHA02742   100 APLEETALDFWQAIFQDQVRVIVMITKIMEDGKEACYPYWMPHerGKATHGEFKIKTKKIKSFRNYAVTNLCLTDTNT-- 177

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658117657 1189 GSQKEQTHertvvqYHYTQWPDMGVPEYTLPVLTFVRKSSQA-----------NLGNMGPVVVHCSAGVGRTGTYIVLDS 1257
Cdd:PHA02742   178 GASLDIKH------FAYEDWPHGGLPRDPNKFLDFVLAVREAdlkadvdikgeNIVKEPPILVHCSAGLDRAGAFCAIDI 251

                          250       260       270
                   ....*....|....*....|....*....|....*.
gi 1658117657 1258 MLRQIKEQGTVNILGFLKHIRTQRNYLVQTEEQYIF 1293
Cdd:PHA02742   252 CISKYNERAIIPLLSIVRDLRKQRHNCLSLPQQYIF 287

R-PTP-S-2

cd14627

PTP-like domain of receptor-type tyrosine-protein phosphatase S, repeat 2; Receptor-type ...

1307-1589

3.31e-43

Pssm-ID: 350475 [Multi-domain] Cd Length: 290 Bit Score: 159.90 E-value: 3.31e-43

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658117657 1307 TEVHSSHIHTYVNELLIPGPSGQ-TPLEKQFKMITQSNAKQCDYSAALKQCNRDKNRNSSLLPVERSRVHLSTTAG-EIS 1384
Cdd:cd14627      2 TEVPARNLYSYIQKLAQVEVGEHvTGMELEFKRLANSKAHTSRFISANLPCNKFKNRLVNIMPYETTRVCLQPIRGvEGS 81

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658117657 1385 DYINASYIMGYQQSNEFIITQNPLPSTMKDFWKMIWDHSTQVVIALPDGLDLAEDEC-IYWPTKsQPIRFDTFTVTFMGE 1463
Cdd:cd14627     82 DYINASFIDGYRQQKAYIATQGPLAETTEDFWRMLWENNSTIVVMLTKLREMGREKChQYWPAE-RSARYQYFVVDPMAE 160

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658117657 1464 DHMclsneDMLIVQDFILEATQDDYVLEVRQYRAPRWPNPDGPISNTfELINIIKE-----ESVSRDGPIVVHDKRGGNI 1538
Cdd:cd14627    161 YNM-----PQYILREFKVTDARDGQSRTVRQFQFTDWPEQGVPKSGE-GFIDFIGQvhktkEQFGQDGPISVHCSAGVGR 234

                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|.
gi 1658117657 1539 AGTFCALMTLLHQLEMESSFDVYWVAKMINLMRPGIFTDIDQYQFLYKVIM 1589
Cdd:cd14627    235 TGVFITLSIVLERMRYEGVVDIFQTVKMLRTQRPAMVQTEDEYQFCYQAAL 285

R-PTP-LAR-2

cd14554

PTP-like domain of the LAR family receptor-type tyrosine-protein phosphatases, repeat 2; The ...

1356-1586

5.38e-43

Pssm-ID: 350402 [Multi-domain] Cd Length: 238 Bit Score: 157.30 E-value: 5.38e-43

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658117657 1356 CNRDKNRNSSLLPVERSRVHLSTTAG-EISDYINASYIMGYQQSNEFIITQNPLPSTMKDFWKMIWDHSTQVVIALPDGL 1434
Cdd:cd14554      5 CNKFKNRLVNILPYESTRVCLQPIRGvEGSDYINASFIDGYRQRGAYIATQGPLAETTEDFWRMLWEHNSTIIVMLTKLR 84

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658117657 1435 DLAEDECI-YWPTKsQPIRFDTFTVTFMGEDHMclsneDMLIVQDFILEATQDDYVLEVRQYRAPRWPNPDGPISNTfEL 1513
Cdd:cd14554     85 EMGREKCHqYWPAE-RSARYQYFVVDPMAEYNM-----PQYILREFKVTDARDGQSRTVRQFQFTDWPEQGVPKSGE-GF 157

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1658117657 1514 INIIKE-----ESVSRDGPIVVHDKRGGNIAGTFCALMTLLHQLEMESSFDVYWVAKMINLMRPGIFTDIDQYQFLYK 1586
Cdd:cd14554    158 IDFIGQvhktkEQFGQEGPITVHCSAGVGRTGVFITLSIVLERMRYEGVVDVFQTVKLLRTQRPAMVQTEDQYQFCYR 235

R-PTP-F-2

cd14629

PTP-like domain of receptor-type tyrosine-protein phosphatase F, repeat 2; Receptor-type ...

1307-1589

8.97e-42

Pssm-ID: 350477 [Multi-domain] Cd Length: 291 Bit Score: 155.65 E-value: 8.97e-42

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658117657 1307 TEVHSSHIHTYVNEL-LIPGPSGQTPLEKQFKMITQSNAKQCDYSAALKQCNRDKNRNSSLLPVERSRVHLSTTAG-EIS 1384
Cdd:cd14629      2 TEVPARNLYAHIQKLtQVPPGESVTAMELEFKLLANSKAHTSRFISANLPCNKFKNRLVNIMPYELTRVCLQPIRGvEGS 81

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658117657 1385 DYINASYIMGYQQSNEFIITQNPLPSTMKDFWKMIWDHSTQVVIALPDGLDLAEDEC-IYWPTKsQPIRFDTFTVTFMGE 1463
Cdd:cd14629     82 DYINASFIDGYRQQKAYIATQGPLAETTEDFWRMLWEHNSTIVVMLTKLREMGREKChQYWPAE-RSARYQYFVVDPMAE 160

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658117657 1464 DHMclsneDMLIVQDFILEATQDDYVLEVRQYRAPRWPNPDGPISNTfELINIIKE-----ESVSRDGPIVVHDKRGGNI 1538
Cdd:cd14629    161 YNM-----PQYILREFKVTDARDGQSRTIRQFQFTDWPEQGVPKTGE-GFIDFIGQvhktkEQFGQDGPITVHCSAGVGR 234

                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|.
gi 1658117657 1539 AGTFCALMTLLHQLEMESSFDVYWVAKMINLMRPGIFTDIDQYQFLYKVIM 1589
Cdd:cd14629    235 TGVFITLSIVLERMRYEGVVDMFQTVKTLRTQRPAMVQTEDQYQLCYRAAL 285

PTPc-N21

cd14598

catalytic domain of tyrosine-protein phosphatase non-receptor type 21; Tyrosine-protein ...

1091-1300

3.59e-40

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: 148.58 E-value: 3.59e-40

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658117657 1091 YINANYVDGFTQPKA--YIATQGPLKSSMEDFWRMVWEQNASVIVMITNLVEKGRRKCDQYWP-LDSQEE---YGSFLVT 1164
Cdd:cd14598      1 YINASHIKVTVGGKEwdYIATQGPLQNTCQDFWQMVWEQGVAIIAMVTAEEEGGREKSFRYWPrLGSRHNtvtYGRFKIT 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658117657 1165 LRSTKVLAYYTQRTFTLKNTRAKKgsqkeqthERTVVQYHYTQWPDMGVPEYTLPVLTF------VRKSSQANLGNMG-- 1236
Cdd:cd14598     81 TRFRTDSGCYATTGLKIKHLLTGQ--------ERTVWHLQYTDWPEHGCPEDLKGFLSYleeiqsVRRHTNSTIDPKSpn 152

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1658117657 1237 -PVVVHCSAGVGRTGTYIVLDSMLRQIKEQGTVNILGFLKHIRTQRNYLVQTEEQYIFIHDALVE 1300
Cdd:cd14598    153 pPVLVHCSAGVGRTGVVILSEIMIACLEHNEMLDIPRVLDMLRQQRMMMVQTLSQYTFVYKVLIQ 217

R3-PTPc

cd14548

catalytic domain of R3 subfamily receptor-type tyrosine-protein phosphatases and similar ...

1362-1586

3.75e-40

Pssm-ID: 350396 [Multi-domain] Cd Length: 222 Bit Score: 148.66 E-value: 3.75e-40

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658117657 1362 RNSSLLPVERSRVHLSTTAGEI-SDYINASYIMGYQQSNEFIITQNPLPSTMKDFWKMIWDHSTQVVIALPDGLDLAEDE 1440
Cdd:cd14548      1 RYTNILPYDHSRVKLIPINEEEgSDYINANYIPGYNSPREFIATQGPLPGTKDDFWRMVWEQNSHTIVMLTQCMEKGRVK 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658117657 1441 CI-YWPTKSQPIRFDTFTVTFMGEDHMclsneDMLIVQDFILEatQDDYVLEVRQYRAPRWPN---PDGPISntfeLINI 1516
Cdd:cd14548     81 CDhYWPFDQDPVYYGDITVTMLSESVL-----PDWTIREFKLE--RGDEVRSVRQFHFTAWPDhgvPEAPDS----LLRF 149

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1658117657 1517 IK---EESVSRDGPIVVHDKRGGNIAGTFCALMTLLHQLEMESSFDVYWVAKMINLMRPGIFTDIDQYQFLYK 1586
Cdd:cd14548    150 VRlvrDYIKQEKGPTIVHCSAGVGRTGTFIALDRLLQQIESEDYVDIFGIVYDLRKHRPLMVQTEAQYIFLHQ 222

PTPc_DSPc

smart00012

Protein tyrosine phosphatase, catalytic domain, undefined specificity; Protein tyrosine ...

1199-1300

1.05e-39

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: 142.88 E-value: 1.05e-39

                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658117657  1199 TVVQYHYTQWPDMGVPEYTLPVLTFVR--KSSQANLGNMGPVVVHCSAGVGRTGTYIVLDSMLRQI-KEQGTVNILGFLK 1275
Cdd:smart00012    1 TVKHYHYTGWPDHGVPESPDSILELLRavKKNLNQSESSGPVVVHCSAGVGRTGTFVAIDILLQQLeAEAGEVDIFDTVK 80

                            90       100
                    ....*....|....*....|....*
gi 1658117657  1276 HIRTQRNYLVQTEEQYIFIHDALVE 1300
Cdd:smart00012   81 ELRSQRPGMVQTEEQYLFLYRALLE 105

PTPc_motif

smart00404

Protein tyrosine phosphatase, catalytic domain motif;

1199-1300

1.05e-39

Protein tyrosine phosphatase, catalytic domain motif;

Pssm-ID: 214649 [Multi-domain] Cd Length: 105 Bit Score: 142.88 E-value: 1.05e-39

                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658117657  1199 TVVQYHYTQWPDMGVPEYTLPVLTFVR--KSSQANLGNMGPVVVHCSAGVGRTGTYIVLDSMLRQI-KEQGTVNILGFLK 1275
Cdd:smart00404    1 TVKHYHYTGWPDHGVPESPDSILELLRavKKNLNQSESSGPVVVHCSAGVGRTGTFVAIDILLQQLeAEAGEVDIFDTVK 80

                            90       100
                    ....*....|....*....|....*
gi 1658117657  1276 HIRTQRNYLVQTEEQYIFIHDALVE 1300
Cdd:smart00404   81 ELRSQRPGMVQTEEQYLFLYRALLE 105

R-PTPc-A-E-2

cd14552

catalytic domain of receptor-type tyrosine-protein phosphatase A and E, repeat 2; ...

1386-1588

3.40e-38

Pssm-ID: 350400 [Multi-domain] Cd Length: 202 Bit Score: 142.41 E-value: 3.40e-38

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658117657 1386 YINASYIMGYQQSNEFIITQNPLPSTMKDFWKMIWDHSTQVVIALPDGLDLAEDEC-IYWPTKSQpIRFDTFTVTFMGEd 1464
Cdd:cd14552      1 YINASFIDGYRQKDAYIATQGPLDHTVEDFWRMIWEWKSCSIVMLTEIKERSQNKCaQYWPEDGS-VSSGDITVELKDQ- 78

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658117657 1465 hmclSNEDMLIVQDFILEATQDDYVLEVRQYRAPRWPNPDGPiSNTFELINII----KEESVSRDGPIVVHDKRGGNIAG 1540
Cdd:cd14552     79 ----TDYEDYTLRDFLVTKGKGGSTRTVRQFHFHGWPEVGIP-DNGKGMIDLIaavqKQQQQSGNHPITVHCSAGAGRTG 153

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*...
gi 1658117657 1541 TFCALMTLLHQLEMESSFDVYWVAKMINLMRPGIFTDIDQYQFLYKVI 1588
Cdd:cd14552    154 TFCALSTVLERVKAEGVLDVFQVVKSLRLQRPHMVQTLEQYEFCYKVV 201

R-PTPc-J

cd14615

catalytic domain of receptor-type tyrosine-protein phosphatase J; Receptor-type ...

1361-1589

4.96e-38

Pssm-ID: 350463 [Multi-domain] Cd Length: 229 Bit Score: 142.65 E-value: 4.96e-38

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658117657 1361 NRNSSLLPVERSRVHLSTTAGEISDYINASYIMGYQQSNEFIITQNPLPSTMKDFWKMIWDHSTQVVIALPDGLDLAEDE 1440
Cdd:cd14615      1 NRYNNVLPYDISRVKLSVQSHSTDDYINANYMPGYNSKKEFIAAQGPLPNTVKDFWRMVWEKNVYAIVMLTKCVEQGRTK 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658117657 1441 C-IYWPTKsQPIRFDTFTVTfmgedhmcLSNEDML---IVQDFILEATQDDYVLEVRQYRAPRWpnPDGPISNTFELI-- 1514
Cdd:cd14615     81 CeEYWPSK-QKKDYGDITVT--------MTSEIVLpewTIRDFTVKNAQTNESRTVRHFHFTSW--PDHGVPETTDLLin 149

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1658117657 1515 --NIIKE--ESVSRDGPIVVHDKRGGNIAGTFCALMTLLHQLEMESSFDVYWVAKMINLMRPGIFTDIDQYQFLYKVIM 1589
Cdd:cd14615    150 frHLVREymKQNPPNSPILVHCSAGVGRTGTFIAIDRLIYQIENENVVDVYGIVYDLRMHRPLMVQTEDQYVFLNQCAL 228

R-PTP-C-2

cd14558

PTP-like domain of receptor-type tyrosine-protein phosphatase C, repeat 2; Receptor-type ...

1386-1585

8.17e-38

Pssm-ID: 350406 [Multi-domain] Cd Length: 203 Bit Score: 141.38 E-value: 8.17e-38

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658117657 1386 YINASYIMGYQQSNEFIITQNPLPSTMKDFWKMIWDHSTQVVIALPDGLDLAEDECI-YWPTKSQpirfdtftvTFmGED 1464
Cdd:cd14558      1 YINASFIDGYWGPKSLIATQGPLPDTIADFWQMIFQKKVKVIVMLTELKEGDQEQCAqYWGDEKK---------TY-GDI 70

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658117657 1465 HMCLSNEDM---LIVQDFILEATQDDYVLEVRQYRAPRWpNPDGPISNTFELINIIKE---------ESVSRDGPIVVHD 1532
Cdd:cd14558     71 EVELKDTEKsptYTVRVFEITHLKRKDSRTVYQYQYHKW-KGEELPEKPKDLVDMIKSikqklpyknSKHGRSVPIVVHC 149

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|...
gi 1658117657 1533 KRGGNIAGTFCALMTLLHQLEMESSFDVYWVAKMINLMRPGIFTDIDQYQFLY 1585
Cdd:cd14558    150 SDGSSRTGIFCALWNLLESAETEKVVDVFQVVKALRKQRPGMVSTLEQYQFLY 202

R-PTPc-H

cd14619

catalytic domain of receptor-type tyrosine-protein phosphatase H; Receptor-type ...

1361-1592

9.15e-38

Pssm-ID: 350467 [Multi-domain] Cd Length: 233 Bit Score: 142.34 E-value: 9.15e-38

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658117657 1361 NRNSSLLPVERSRVHLSTT-AGEISDYINASYIMGYQQSNEFIITQNPLPSTMKDFWKMIWDHSTQVVIALPDGLDLAED 1439
Cdd:cd14619      1 NRFRNVLPYDWSRVPLKPIhEEPGSDYINANYMPGYWSSQEFIATQGPLPQTVGDFWRMIWEQQSSTIVMLTNCMEAGRV 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658117657 1440 EC-IYWPTKSQPIRFDTFTVTFMGEDHMclsneDMLIVQDFILEATQDDYVLEVRQYRAPRWPNPDGPiSNTFELI---N 1515
Cdd:cd14619     81 KCeHYWPLDYTPCTYGHLRVTVVSEEVM-----ENWTVREFLLKQVEEQKTLSVRHFHFTAWPDHGVP-SSTDTLLafrR 154

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1658117657 1516 IIKE--ESVSRDGPIVVHDKRGGNIAGTFCALMTLLHQLEMESSFDVYWVAKMINLMRPGIFTDIDQYQFLYKVIMSLV 1592
Cdd:cd14619    155 LLRQwlDQTMSGGPTVVHCSAGVGRTGTLIALDVLLQQLQSEGLLGPFSFVQKMRENRPLMVQTESQYVFLHQCILDFL 233

R-PTPc-V

cd14618

catalytic domain of receptor-type tyrosine-protein phosphatase V; Receptor-type ...

1361-1589

2.10e-37

Pssm-ID: 350466 [Multi-domain] Cd Length: 230 Bit Score: 141.23 E-value: 2.10e-37

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658117657 1361 NRNSSLLPVERSRVHLSTTAGEI-SDYINASYIMGYQQSNEFIITQNPLPSTMKDFWKMIWDHSTQVVIALPDGLDLAED 1439
Cdd:cd14618      1 NRYPHVLPYDHSRVRLSQLGGEPhSDYINANFIPGYTSPQEFIATQGPLKKTIEDFWRLVWEQQVCNIIMLTVGMENGRV 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658117657 1440 ECI-YWPTKSQPIRFDTFTVTFMGEdhmclSNEDMLIVQDFILEATQDDYVLEVRQYRAPRWPN---PDGPiSNTFELIN 1515
Cdd:cd14618     81 LCDhYWPSESTPVSYGHITVHLLAQ-----SSEDEWTRREFKLWHEDLRKERRVKHLHYTAWPDhgiPEST-SSLMAFRE 154

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1658117657 1516 IIKEE--SVSRDGPIVVHDKRGGNIAGTFCALMTLLHQLEMESSFDVYWVAKMINLMRPGIFTDIDQYQFLYKVIM 1589
Cdd:cd14618    155 LVREHvqATKGKGPTLVHCSAGVGRSGTFIALDRLLRQLKEEKVVDVFNTVYILRMHRYLMIQTLSQYIFLHSCIL 230

R-PTPc-E-2

cd14622

catalytic domain of receptor-type tyrosine-protein phosphatase E, repeat 2; Receptor-type ...

1385-1588

5.27e-37

Pssm-ID: 350470 [Multi-domain] Cd Length: 205 Bit Score: 138.98 E-value: 5.27e-37

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658117657 1385 DYINASYIMGYQQSNEFIITQNPLPSTMKDFWKMIWDHSTQVVIALPDGLDLAEDECI-YWPTKSqpirfdtfTVTFmGE 1463
Cdd:cd14622      1 DYINASFIDGYRQKDYFIATQGPLAHTVEDFWRMVWEWKCHTIVMLTELQEREQEKCVqYWPSEG--------SVTH-GE 71

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658117657 1464 DHMCLSNE---DMLIVQDFILEATQDDYVLEVRQYRAPRWPNPDGPiSNTFELINII----KEESVSRDGPIVVHDKRGG 1536
Cdd:cd14622     72 ITIEIKNDtllETISIRDFLVTYNQEKQTRLVRQFHFHGWPEIGIP-AEGKGMIDLIaavqKQQQQTGNHPIVVHCSAGA 150

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|..
gi 1658117657 1537 NIAGTFCALMTLLHQLEMESSFDVYWVAKMINLMRPGIFTDIDQYQFLYKVI 1588
Cdd:cd14622    151 GRTGTFIALSNILERVKAEGLLDVFQTVKSLRLQRPHMVQTLEQYEFCYRVV 202

R-PTPc-A-2

cd14623

catalytic domain of receptor-type tyrosine-protein phosphatase A, repeat 2; Receptor-type ...

1366-1588

1.04e-35

Pssm-ID: 350471 [Multi-domain] Cd Length: 228 Bit Score: 135.94 E-value: 1.04e-35

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658117657 1366 LLPVERSRVHLSTTAGEI-SDYINASYIMGYQQSNEFIITQNPLPSTMKDFWKMIWDHSTQVVIALPDGLDLAEDECI-Y 1443
Cdd:cd14623      5 IIPYEFNRVIIPVKRGEEnTDYVNASFIDGYRQKDSYIASQGPLQHTIEDFWRMIWEWKSCSIVMLTELEERGQEKCAqY 84

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658117657 1444 WPTKSQpIRFDTFTVTFMGEDHmCLSnedmLIVQDFILEATQDDYVLEVRQYRAPRWPNPDGPiSNTFELINII----KE 1519
Cdd:cd14623     85 WPSDGS-VSYGDITIELKKEEE-CES----YTVRDLLVTNTRENKSRQIRQFHFHGWPEVGIP-SDGKGMINIIaavqKQ 157

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1658117657 1520 ESVSRDGPIVVHDKRGGNIAGTFCALMTLLHQLEMESSFDVYWVAKMINLMRPGIFTDIDQYQFLYKVI 1588
Cdd:cd14623    158 QQQSGNHPITVHCSAGAGRTGTFCALSTVLERVKAEGILDVFQTVKSLRLQRPHMVQTLEQYEFCYKVV 226

R-PTPc-typeIIb-2

cd14556

PTP domain of type IIb (or R2B) subfamily receptor-type tyrosine-protein phosphatases, repeat ...

1386-1585

1.13e-35

Pssm-ID: 350404 [Multi-domain] Cd Length: 201 Bit Score: 134.84 E-value: 1.13e-35

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658117657 1386 YINASYIMGYQQSNEFIITQNPLPSTMKDFWKMIWDHSTQVVIALPDgLDLAEDECI-YWPTKSQPiRFDTFTVTFMGED 1464
Cdd:cd14556      1 YINAALLDSYKQPAAFIVTQHPLPNTVTDFWRLVYDYGCTSIVMLNQ-LDPKDQSCPqYWPDEGSG-TYGPIQVEFVSTT 78

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658117657 1465 hmclsNEDMLIVQDFILEAT---QDDYVLeVRQYRAPRWP-NPDGPIS--NTFELINII-KEESVSRDGPIVVHDKRGGN 1537
Cdd:cd14556     79 -----IDEDVISRIFRLQNTtrpQEGYRM-VQQFQFLGWPrDRDTPPSkrALLKLLSEVeKWQEQSGEGPIVVHCLNGVG 152

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*...
gi 1658117657 1538 IAGTFCALMTLLHQLEMESSFDVYWVAKMINLMRPGIFTDIDQYQFLY 1585
Cdd:cd14556    153 RSGVFCAISSVCERIKVENVVDVFQAVKTLRNHRPNMVETEEQYKFCY 200

PTPc-N18

cd14603

catalytic domain of tyrosine-protein phosphatase non-receptor type 18; Tyrosine-protein ...

1334-1591

3.17e-33

Pssm-ID: 350451 [Multi-domain] Cd Length: 266 Bit Score: 130.33 E-value: 3.17e-33

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658117657 1334 KQFKMI-TQSNAKQCDYS----AALKQCNRDKNRNSSLLPVERSRVHLSTTAGEI-SDYINASYIMGYQQSNEFIITQNP 1407
Cdd:cd14603      2 GEFSEIrACSAAFKADYVcstvAGGRKENVKKNRYKDILPYDQTRVILSLLQEEGhSDYINANFIKGVDGSRAYIATQGP 81

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658117657 1408 LPSTMKDFWKMIWDHSTQVVIALPDGLDLAEDEC-IYWPTKSQPIRFDTFTVTFMGEDHMclsNEDmLIVQDFILEATQD 1486
Cdd:cd14603     82 LSHTVLDFWRMIWQYGVKVILMACREIEMGKKKCeRYWAQEQEPLQTGPFTITLVKEKRL---NEE-VILRTLKVTFQKE 157

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658117657 1487 DYVLEVRQYRAprWPN---PDGPiSNTFELINIIKEESVSRDGPIVVHDKRGGNIAGTFCAL---MTLLHQLEMESSFDV 1560
Cdd:cd14603    158 SRSVSHFQYMA--WPDhgiPDSP-DCMLAMIELARRLQGSGPEPLCVHCSAGCGRTGVICTVdyvRQLLLTQRIPPDFSI 234

                          250       260       270
                   ....*....|....*....|....*....|.
gi 1658117657 1561 YWVAKMINLMRPGIFTDIDQYQFLYKVIMSL 1591
Cdd:cd14603    235 FDVVLEMRKQRPAAVQTEEQYEFLYHTVAQM 265

R5-PTP-2