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Conserved domains on  [gi|2499757|sp|Q64612|]
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RecName: Full=Receptor-type tyrosine-protein phosphatase V; Short=R-PTP-V; AltName: Full=Embryonic stem cell protein-tyrosine phosphatase; Short=ES cell phosphatase; AltName: Full=Osteotesticular protein-tyrosine phosphatase; Short=OST-PTP; Flags: Precursor

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
PTP_DSP_cys super family cl28904
cys-based protein tyrosine phosphatase and dual-specificity phosphatase superfamily; This ...
 1178-1407 2.05e-156

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


The actual alignment was detected with superfamily member cd14618:

Pssm-ID: 475123 [Multi-domain]  Cd Length: 230  Bit Score: 475.97  E-value: 2.05e-156
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2499757  1178 NRYPHVLPYDHSRVRLTQLPGEPHSDYINANFIPGYSHTQEIIATQGPLKKTLEDFWRLVWEQQVHVIIMLTVGMENGRV 1257
Cdd:cd14618    1 NRYPHVLPYDHSRVRLSQLGGEPHSDYINANFIPGYTSPQEFIATQGPLKKTIEDFWRLVWEQQVCNIIMLTVGMENGRV 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2499757  1258 LCEHYWPANSTPVTHGHITIHLLAEEPEDEWTRREFQLQHGTEQKQRRVKQLQFTTWPDHSVPEAPSSLLAFVELVQEQV 1337
Cdd:cd14618   81 LCDHYWPSESTPVSYGHITVHLLAQSSEDEWTRREFKLWHEDLRKERRVKHLHYTAWPDHGIPESTSSLMAFRELVREHV 160

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2499757  1338 QATQGKGPILVHCSAGVGRTGTFVALLRLLRQLEEEKVADVFNTVYILRLHRPLMIQTLSQYIFLHSCLL 1407
Cdd:cd14618  161 QATKGKGPTLVHCSAGVGRSGTFIALDRLLRQLKEEKVVDVFNTVYILRMHRYLMIQTLSQYIFLHSCIL 230
PTP_tm pfam18861
TM proximal of protein tyrosine phosphatase, receptor type J; Protein tyrosine phosphatases ...
 950-1069 2.47e-43

TM proximal of protein tyrosine phosphatase, receptor type J; Protein tyrosine phosphatases (PTPs) are known to be signaling molecules that regulate a variety of cellular processes, including cell growth, differentiation, mitotic cycle, and oncogenic transformation. PTP receptor type J possesses an extracellular region containing five fibronectin type III repeats, the transmembrane region included in this Pfam entry, and a intracytoplasmic catalytic domain. This entry probably contains part of a Fn3 domain at the N-terminus.


:

Pssm-ID: 465889  Cd Length: 126  Bit Score: 153.92  E-value: 2.47e-43
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2499757     950 RGMFGKDDGQIQWYGIIATINMTLAQPSREAINYTWYDHYYRGCESFLALLFPNPFYPePWAGPRSWTVPVGTEDCdnTQ 1029
Cdd:pfam18861    3 FSLFNSSNGPIKAYGVIVTTNDSLNRPLKEYLNKTYYDWKYKKTDSYLATVTPNPFTS-PRSSSRSLTVPVGTGSK--WQ 79

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*..
gi 2499757    1030 EICNGRLKSGFQYRFSVVAFSRL-------NTPETILAFSAFSEPRA 1069
Cdd:pfam18861   80 GYCNGPLKPLGSYRFSVAAFTRLefddgliDGEESYVSFTPFSEPIA 126
PTP_DSP_cys super family cl28904
cys-based protein tyrosine phosphatase and dual-specificity phosphatase superfamily; This ...
 1477-1693 6.80e-24

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


The actual alignment was detected with superfamily member cd14618:

Pssm-ID: 475123 [Multi-domain]  Cd Length: 230  Bit Score: 101.94  E-value: 6.80e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2499757  1477 HSQEQFALVEECPEDSMLEASLFPGGPSGCDHVVltgSAGP-----KELWEMVWEHDAHVLVSL--GLPDTKEKPPDIWP 1549
Cdd:cd14618   11 HSRVRLSQLGGEPHSDYINANFIPGYTSPQEFIA---TQGPlkktiEDFWRLVWEQQVCNIIMLtvGMENGRVLCDHYWP 87

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2499757  1550 VEMQPIVTDMVTVHRVSESNTTTgWPSTLFRVIHGESGKERQVQCLQFPC-SESGCELPANTLLTFLDAVGQCCFRGKSK 1628
Cdd:cd14618   88 SESTPVSYGHITVHLLAQSSEDE-WTRREFKLWHEDLRKERRVKHLHYTAwPDHGIPESTSSLMAFRELVREHVQATKGK 166

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2499757  1629 KPgtLLSHSSKNTNQLGTFLAMEQLLQQAGTERTVDVFNVALKQSQACGLMTPTLEQYIYLYNCL 1693
Cdd:cd14618  167 GP--TLVHCSAGVGRSGTFIALDRLLRQLKEEKVVDVFNTVYILRMHRYLMIQTLSQYIFLHSCI 229
FN3 super family cl27307
Fibronectin type 3 domain [General function prediction only];
377-749 5.66e-09

Fibronectin type 3 domain [General function prediction only];


The actual alignment was detected with superfamily member COG3401:

Pssm-ID: 442628 [Multi-domain]  Cd Length: 603  Bit Score: 60.79  E-value: 5.66e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2499757   377 PYDAWVEGSTWLAESAALPREVPGARLWLDGLEASKQPGRRALlYSDDAPGSLGNISVPSGATHViFCGLVPGAHYRVDI 456
Cdd:COG3401   44 LSVTTKESPGTLLVAAGLSSGGGLGTGGRAGTTSGVAAVAVAA-APPTATGLTTLTGSGSVGGAT-NTGLTSSDEVPSPA 121

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2499757   457 ASSTGDISQSISGYTSPLPPQSLEVISRSSPSDLTIAWGPAPGQLEGYKVTWHqDGSQRSPGDLVDLGPDTLSLTLKSLV 536
Cdd:COG3401  122 VGTATTATAVAGGAATAGTYALGAGLYGVDGANASGTTASSVAGAGVVVSPDT-SATAAVATTSLTVTSTTLVDGGGDIE 200

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2499757   537 PGSCYT--VSAWAWAGNLDSDSQ--KIHSCTRPAPPTNLSlGFAHQPAALKASWyHPPGGRDAFHLRLYRlrpltlesek 612
Cdd:COG3401  201 PGTTYYyrVAATDTGGESAPSNEvsVTTPTTPPSAPTGLT-ATADTPGSVTLSW-DPVTESDATGYRVYR---------- 268

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2499757   613 vlpREAQNFSWAQLTAGCE---------------FQVQLSTLWG--SERSSSANAT-GWTPPSAPTLVNVTSDAPTQLQV 674
Cdd:COG3401  269 ---SNSGDGPFTKVATVTTtsytdtgltngttyyYRVTAVDAAGneSAPSNVVSVTtDLTPPAAPSGLTATAVGSSSITL 345

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2499757   675 SWAHVPGGR-SRYQVtLYQESTRTATSIMGPKEDGTSFL--GLTPGTKYKVEVISW--AGPLYTAAANVSAWTYPLIPNE 749
Cdd:COG3401  346 SWTASSDADvTGYNV-YRSTSGGGTYTKIAETVTTTSYTdtGLTPGTTYYYKVTAVdaAGNESAPSEEVSATTASAASGE 424
fn3 pfam00041
Fibronectin type III domain;
148-201 8.99e-05

Fibronectin type III domain;


:

Pssm-ID: 394996 [Multi-domain]  Cd Length: 85  Bit Score: 42.79  E-value: 8.99e-05
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 2499757     148 SWS---DAPGDQDSYQLLLYHLESQTLACNVSVSPDTLSYSFGDLLPGTQYVLEVIT 201
Cdd:pfam00041   19 SWTpppDGNGPITGYEVEYRPKNSGEPWNEITVPGTTTSVTLTGLKPGTEYEVRVQA 75
FN3 smart00060
Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, ...
 49-110 3.74e-03

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: 37.98  E-value: 3.74e-03
                            10        20        30        40        50        60
                    ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2499757       49 STSLFLSWVAAELGGFD-YALSLRSVNSSGSPEGQQLQAHTNESGFEFHGLVPGSRYQLKLTV 110
Cdd:smart00060   14 STSVTLSWEPPPDDGITgYIVGYRVEYREEGSEWKEVNVTPSSTSYTLTGLKPGTEYEFRVRA 76
 
Name Accession Description Interval E-value
R-PTPc-V cd14618
catalytic domain of receptor-type tyrosine-protein phosphatase V; Receptor-type ...
 1178-1407 2.05e-156

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: 475.97  E-value: 2.05e-156
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2499757  1178 NRYPHVLPYDHSRVRLTQLPGEPHSDYINANFIPGYSHTQEIIATQGPLKKTLEDFWRLVWEQQVHVIIMLTVGMENGRV 1257
Cdd:cd14618    1 NRYPHVLPYDHSRVRLSQLGGEPHSDYINANFIPGYTSPQEFIATQGPLKKTIEDFWRLVWEQQVCNIIMLTVGMENGRV 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2499757  1258 LCEHYWPANSTPVTHGHITIHLLAEEPEDEWTRREFQLQHGTEQKQRRVKQLQFTTWPDHSVPEAPSSLLAFVELVQEQV 1337
Cdd:cd14618   81 LCDHYWPSESTPVSYGHITVHLLAQSSEDEWTRREFKLWHEDLRKERRVKHLHYTAWPDHGIPESTSSLMAFRELVREHV 160

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2499757  1338 QATQGKGPILVHCSAGVGRTGTFVALLRLLRQLEEEKVADVFNTVYILRLHRPLMIQTLSQYIFLHSCLL 1407
Cdd:cd14618  161 QATKGKGPTLVHCSAGVGRSGTFIALDRLLRQLKEEKVVDVFNTVYILRMHRYLMIQTLSQYIFLHSCIL 230
PTPc smart00194
Protein tyrosine phosphatase, catalytic domain;
1150-1408 3.85e-106

Protein tyrosine phosphatase, catalytic domain;


Pssm-ID: 214550 [Multi-domain]  Cd Length: 259  Bit Score: 339.25  E-value: 3.85e-106
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2499757     1150 FFQEFEELKEVGK-DQPRLEAEHPDNIIKNRYPHVLPYDHSRVRLTQLPGEPhSDYINANFIPGYSHTQEIIATQGPLKK 1228
Cdd:smart00194    2 LEEEFEKLDRLKPdDESCTVAAFPENRDKNRYKDVLPYDHTRVKLKPPPGEG-SDYINASYIDGPNGPKAYIATQGPLPS 80

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2499757     1229 TLEDFWRLVWEQQVHVIIMLTVGMENGRVLCEHYWPAN-STPVTHGHITIHLLAEEPEDEWTRREFQLQHGTEQKQRRVK 1307
Cdd:smart00194   81 TVEDFWRMVWEQKVTVIVMLTELVEKGREKCAQYWPDEeGEPLTYGDITVTLKSVEKVDDYTIRTLEVTNTGCSETRTVT 160

                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2499757     1308 QLQFTTWPDHSVPEAPSSLLAFVELVqEQVQATQgKGPILVHCSAGVGRTGTFVALLRLLRQLEEEKVADVFNTVYILRL 1387
Cdd:smart00194  161 HYHYTNWPDHGVPESPESILDLIRAV-RKSQSTS-TGPIVVHCSAGVGRTGTFIAIDILLQQLEAGKEVDIFEIVKELRS 238

                           250       260
                    ....*....|....*....|.
gi 2499757     1388 HRPLMIQTLSQYIFLHSCLLN 1408
Cdd:smart00194  239 QRPGMVQTEEQYIFLYRAILE 259
Y_phosphatase pfam00102
Protein-tyrosine phosphatase;
1174-1408 1.56e-100

Protein-tyrosine phosphatase;


Pssm-ID: 459674 [Multi-domain]  Cd Length: 234  Bit Score: 322.27  E-value: 1.56e-100
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2499757    1174 NIIKNRYPHVLPYDHSRVRLTQLPGepHSDYINANFIPGYSHTQEIIATQGPLKKTLEDFWRLVWEQQVHVIIMLTVGME 1253
Cdd:pfam00102    1 NLEKNRYKDVLPYDHTRVKLTGDPG--PSDYINASYIDGYKKPKKYIATQGPLPNTVEDFWRMVWEEKVTIIVMLTELEE 78

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2499757    1254 NGRVLCEHYWP-ANSTPVTHGHITIHLLAEEP-EDEWTRREFQLQHGTEQKQRRVKQLQFTTWPDHSVPEAPSSLLAFVE 1331
Cdd:pfam00102   79 KGREKCAQYWPeEEGESLEYGDFTVTLKKEKEdEKDYTVRTLEVSNGGSEETRTVKHFHYTGWPDHGVPESPNSLLDLLR 158

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2499757    1332 LVqEQVQATQGKGPILVHCSAGVGRTGTFVALLRLLRQLEEEKVADVFNTVYILRLHRPLMIQTLSQYIFLHSCLLN 1408
Cdd:pfam00102  159 KV-RKSSLDGRSGPIVVHCSAGIGRTGTFIAIDIALQQLEAEGEVDIFQIVKELRSQRPGMVQTLEQYIFLYDAILE 234
PTP_tm pfam18861
TM proximal of protein tyrosine phosphatase, receptor type J; Protein tyrosine phosphatases ...
 950-1069 2.47e-43

TM proximal of protein tyrosine phosphatase, receptor type J; Protein tyrosine phosphatases (PTPs) are known to be signaling molecules that regulate a variety of cellular processes, including cell growth, differentiation, mitotic cycle, and oncogenic transformation. PTP receptor type J possesses an extracellular region containing five fibronectin type III repeats, the transmembrane region included in this Pfam entry, and a intracytoplasmic catalytic domain. This entry probably contains part of a Fn3 domain at the N-terminus.


Pssm-ID: 465889  Cd Length: 126  Bit Score: 153.92  E-value: 2.47e-43
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2499757     950 RGMFGKDDGQIQWYGIIATINMTLAQPSREAINYTWYDHYYRGCESFLALLFPNPFYPePWAGPRSWTVPVGTEDCdnTQ 1029
Cdd:pfam18861    3 FSLFNSSNGPIKAYGVIVTTNDSLNRPLKEYLNKTYYDWKYKKTDSYLATVTPNPFTS-PRSSSRSLTVPVGTGSK--WQ 79

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*..
gi 2499757    1030 EICNGRLKSGFQYRFSVVAFSRL-------NTPETILAFSAFSEPRA 1069
Cdd:pfam18861   80 GYCNGPLKPLGSYRFSVAAFTRLefddgliDGEESYVSFTPFSEPIA 126
PHA02738 PHA02738
hypothetical protein; Provisional
 1153-1401 1.77e-40

hypothetical protein; Provisional


Pssm-ID: 222923 [Multi-domain]  Cd Length: 320  Bit Score: 153.16  E-value: 1.77e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2499757   1153 EFEELkeVGKDQPRLEAEHPD--------NIIKNRYPHVLPYDHSRVrltQLPGEPH-SDYINANFIPGYSHTQEIIATQ 1223
Cdd:PHA02738   22 DCEEV--ITREHQKVISEKVDgtfnaekkNRKLNRYLDAVCFDHSRV---ILPAERNrGDYINANYVDGFEYKKKFICGQ 96

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2499757   1224 GPLKKTLEDFWRLVWEQQVHVIIMLTVGMENGRVLCEHYWP-ANSTPVTHGHITIHLLAEEPEDEWTRREFQLQHGTEQK 1302
Cdd:PHA02738   97 APTRQTCYDFYRMLWMEHVQIIVMLCKKKENGREKCFPYWSdVEQGSIRFGKFKITTTQVETHPHYVKSTLLLTDGTSAT 176

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2499757   1303 QrRVKQLQFTTWPDHSVPEAPSSLLAFV--------ELVQEQVQATQGKG---PILVHCSAGVGRTGTFVALLRLLRQLE 1371
Cdd:PHA02738  177 Q-TVTHFNFTAWPDHDVPKNTSEFLNFVlevrqcqkELAQESLQIGHNRLqppPIVVHCNAGLGRTPCYCVVDISISRFD 255

                         250       260       270
                  ....*....|....*....|....*....|
gi 2499757   1372 EEKVADVFNTVYILRLHRPLMIQTLSQYIF 1401
Cdd:PHA02738  256 ACATVSIPSIVSSIRNQRYYSLFIPFQYFF 285
COG5599 COG5599
Protein tyrosine phosphatase [Signal transduction mechanisms];
1128-1402 1.34e-35

Protein tyrosine phosphatase [Signal transduction mechanisms];


Pssm-ID: 444335 [Multi-domain]  Cd Length: 282  Bit Score: 137.53  E-value: 1.34e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2499757  1128 RPIPIHSFRQSYEAKSAHahqtffqEFEELKEVGKDqPRLEaEHPDNIIKNRYPHVLPYDHSRVRltqlpgePHSDYINA 1207
Cdd:COG5599    5 NPIAIKSEEEKINSRLST-------LTNELAPSHND-PQYL-QNINGSPLNRFRDIQPYKETALR-------ANLGYLNA 68

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2499757  1208 NFIPGYSHTQEIiATQGPLKKTLEDFWRLVWEQQVHVIIMLT--VGMENGRVLCEHYWPANSTpvtHGHITIHLLAEEPE 1285
Cdd:COG5599   69 NYIQVIGNHRYI-ATQYPLEEQLEDFFQMLFDNNTPVLVVLAsdDEISKPKVKMPVYFRQDGE---YGKYEVSSELTESI 144

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2499757  1286 ---DEWTRREFQL-QHGTEQKQRRVKQLQFTTWPDHSVPEApSSLLAFVELV-QEQVQATQGKGPILVHCSAGVGRTGTF 1360
Cdd:COG5599  145 qlrDGIEARTYVLtIKGTGQKKIEIPVLHVKNWPDHGAISA-EALKNLADLIdKKEKIKDPDKLLPVVHCRAGVGRTGTL 223

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*
gi 2499757  1361 VALLRLLRQLEEEKVADV-FNTVYI-LRLHR-PLMIQTLSQYIFL 1402
Cdd:COG5599  224 IACLALSKSINALVQITLsVEEIVIdMRTSRnGGMVQTSEQLDVL 268
R-PTPc-V cd14618
catalytic domain of receptor-type tyrosine-protein phosphatase V; Receptor-type ...
 1477-1693 6.80e-24

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: 101.94  E-value: 6.80e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2499757  1477 HSQEQFALVEECPEDSMLEASLFPGGPSGCDHVVltgSAGP-----KELWEMVWEHDAHVLVSL--GLPDTKEKPPDIWP 1549
Cdd:cd14618   11 HSRVRLSQLGGEPHSDYINANFIPGYTSPQEFIA---TQGPlkktiEDFWRLVWEQQVCNIIMLtvGMENGRVLCDHYWP 87

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2499757  1550 VEMQPIVTDMVTVHRVSESNTTTgWPSTLFRVIHGESGKERQVQCLQFPC-SESGCELPANTLLTFLDAVGQCCFRGKSK 1628
Cdd:cd14618   88 SESTPVSYGHITVHLLAQSSEDE-WTRREFKLWHEDLRKERRVKHLHYTAwPDHGIPESTSSLMAFRELVREHVQATKGK 166

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2499757  1629 KPgtLLSHSSKNTNQLGTFLAMEQLLQQAGTERTVDVFNVALKQSQACGLMTPTLEQYIYLYNCL 1693
Cdd:cd14618  167 GP--TLVHCSAGVGRSGTFIALDRLLRQLKEEKVVDVFNTVYILRMHRYLMIQTLSQYIFLHSCI 229
Y_phosphatase pfam00102
Protein-tyrosine phosphatase;
1518-1693 1.86e-18

Protein-tyrosine phosphatase;


Pssm-ID: 459674 [Multi-domain]  Cd Length: 234  Bit Score: 86.53  E-value: 1.86e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2499757    1518 KELWEMVWEHDAHVLVSLGLPD--TKEKPPDIWPVEM-QPIVTDMVTVHRVSESNTTTGWPSTLFRVIHGESGKERQVQC 1594
Cdd:pfam00102   56 EDFWRMVWEEKVTIIVMLTELEekGREKCAQYWPEEEgESLEYGDFTVTLKKEKEDEKDYTVRTLEVSNGGSEETRTVKH 135

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2499757    1595 LQFPC-SESGCELPANTLLTFLDAVGQCCFRGKSkkpGTLLSHSSKNTNQLGTFLAMEQLLQQAGTERTVDVFNVALK-Q 1672
Cdd:pfam00102  136 FHYTGwPDHGVPESPNSLLDLLRKVRKSSLDGRS---GPIVVHCSAGIGRTGTFIAIDIALQQLEAEGEVDIFQIVKElR 212

                          170       180
                   ....*....|....*....|.
gi 2499757    1673 SQACGLMTpTLEQYIYLYNCL 1693
Cdd:pfam00102  213 SQRPGMVQ-TLEQYIFLYDAI 232
PTPc smart00194
Protein tyrosine phosphatase, catalytic domain;
1521-1693 5.96e-17

Protein tyrosine phosphatase, catalytic domain;


Pssm-ID: 214550 [Multi-domain]  Cd Length: 259  Bit Score: 82.71  E-value: 5.96e-17
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2499757     1521 WEMVWEHDAHVLVSLGLPD--TKEKPPDIWPVEM-QPIVTDMVTVHRVSEsNTTTGWPSTLFRVIHGESGKERQVQCLQF 1597
Cdd:smart00194   86 WRMVWEQKVTVIVMLTELVekGREKCAQYWPDEEgEPLTYGDITVTLKSV-EKVDDYTIRTLEVTNTGCSETRTVTHYHY 164

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2499757     1598 ---PcsESGCELPANTLLTFLDAVGQCcfrgKSKKPGTLLSHSSKNTNQLGTFLAMEQLLQQAGTERTVDVFNVALK-QS 1673
Cdd:smart00194  165 tnwP--DHGVPESPESILDLIRAVRKS----QSTSTGPIVVHCSAGVGRTGTFIAIDILLQQLEAGKEVDIFEIVKElRS 238

                           170       180
                    ....*....|....*....|
gi 2499757     1674 QACGlMTPTLEQYIYLYNCL 1693
Cdd:smart00194  239 QRPG-MVQTEEQYIFLYRAI 257
FN3 COG3401
Fibronectin type 3 domain [General function prediction only];
377-749 5.66e-09

Fibronectin type 3 domain [General function prediction only];


Pssm-ID: 442628 [Multi-domain]  Cd Length: 603  Bit Score: 60.79  E-value: 5.66e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2499757   377 PYDAWVEGSTWLAESAALPREVPGARLWLDGLEASKQPGRRALlYSDDAPGSLGNISVPSGATHViFCGLVPGAHYRVDI 456
Cdd:COG3401   44 LSVTTKESPGTLLVAAGLSSGGGLGTGGRAGTTSGVAAVAVAA-APPTATGLTTLTGSGSVGGAT-NTGLTSSDEVPSPA 121

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2499757   457 ASSTGDISQSISGYTSPLPPQSLEVISRSSPSDLTIAWGPAPGQLEGYKVTWHqDGSQRSPGDLVDLGPDTLSLTLKSLV 536
Cdd:COG3401  122 VGTATTATAVAGGAATAGTYALGAGLYGVDGANASGTTASSVAGAGVVVSPDT-SATAAVATTSLTVTSTTLVDGGGDIE 200

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2499757   537 PGSCYT--VSAWAWAGNLDSDSQ--KIHSCTRPAPPTNLSlGFAHQPAALKASWyHPPGGRDAFHLRLYRlrpltlesek 612
Cdd:COG3401  201 PGTTYYyrVAATDTGGESAPSNEvsVTTPTTPPSAPTGLT-ATADTPGSVTLSW-DPVTESDATGYRVYR---------- 268

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2499757   613 vlpREAQNFSWAQLTAGCE---------------FQVQLSTLWG--SERSSSANAT-GWTPPSAPTLVNVTSDAPTQLQV 674
Cdd:COG3401  269 ---SNSGDGPFTKVATVTTtsytdtgltngttyyYRVTAVDAAGneSAPSNVVSVTtDLTPPAAPSGLTATAVGSSSITL 345

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2499757   675 SWAHVPGGR-SRYQVtLYQESTRTATSIMGPKEDGTSFL--GLTPGTKYKVEVISW--AGPLYTAAANVSAWTYPLIPNE 749
Cdd:COG3401  346 SWTASSDADvTGYNV-YRSTSGGGTYTKIAETVTTTSYTdtGLTPGTTYYYKVTAVdaAGNESAPSEEVSATTASAASGE 424
FN3 cd00063
Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein ...
 656-725 1.82e-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: 50.57  E-value: 1.82e-07
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2499757   656 PSAPTLVNVTSDAPTQLQVSWAHVPGGRSR---YQVTLYQESTRTATSIMGPKEDGTSFL--GLTPGTKYKVEVI 725
Cdd:cd00063    1 PSPPTNLRVTDVTSTSVTLSWTPPEDDGGPitgYVVEYREKGSGDWKEVEVTPGSETSYTltGLKPGTEYEFRVR 75
PHA02746 PHA02746
protein tyrosine phosphatase; Provisional
 1516-1698 6.70e-07

protein tyrosine phosphatase; Provisional


Pssm-ID: 165113 [Multi-domain]  Cd Length: 323  Bit Score: 53.11  E-value: 6.70e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2499757   1516 GPKE-----LWEMVWEHDAHVLVSLG-LPDTKEKPPDIWPVEMQPIVTDMVTVHRVSESNTTTGWPSTLFRVIHGESGKE 1589
Cdd:PHA02746  120 GPKEdtsedFFKLISEHESQVIVSLTdIDDDDEKCFELWTKEEDSELAFGRFVAKILDIIEELSFTKTRLMITDKISDTS 199

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2499757   1590 RQVQCLQFP-CSESGCELPANTLLTFLDAVGQCCFRGK------SKKPGTLLSHSSKNTNQLGTFLAMEQLLQQAGTERT 1662
Cdd:PHA02746  200 REIHHFWFPdWPDNGIPTGMAEFLELINKVNEEQAELIkqadndPQTLGPIVVHCSAGIGRAGTFCAIDNALEQLEKEKE 279

                         170       180       190
                  ....*....|....*....|....*....|....*...
gi 2499757   1663 VDVFNVALK--QSQACGLMTPtlEQYIYLYNCLNSALL 1698
Cdd:PHA02746  280 VCLGEIVLKirKQRHSSVFLP--EQYAFCYKALKYAII 315
fn3 pfam00041
Fibronectin type III domain;
657-726 9.67e-06

Fibronectin type III domain;


Pssm-ID: 394996 [Multi-domain]  Cd Length: 85  Bit Score: 45.48  E-value: 9.67e-06
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2499757     657 SAPTLVNVTSDAPTQLQVSWAHVPGGRS---RYQVTLYQE-STRTATSIMGPK-EDGTSFLGLTPGTKYKVEVIS 726
Cdd:pfam00041    1 SAPSNLTVTDVTSTSLTVSWTPPPDGNGpitGYEVEYRPKnSGEPWNEITVPGtTTSVTLTGLKPGTEYEVRVQA 75
FN3 smart00060
Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, ...
 473-547 9.72e-06

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: 45.30  E-value: 9.72e-06
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2499757      473 PLPPQSLEVISRSSPSdLTIAW-GPAPGQLEGYKVTWH-QDGSQRSPGDLVDLGPDTLSLTLKSLVPGSCYTVSAWA 547
Cdd:smart00060    1 PSPPSNLRVTDVTSTS-VTLSWePPPDDGITGYIVGYRvEYREEGSEWKEVNVTPSSTSYTLTGLKPGTEYEFRVRA 76
fn3 pfam00041
Fibronectin type III domain;
148-201 8.99e-05

Fibronectin type III domain;


Pssm-ID: 394996 [Multi-domain]  Cd Length: 85  Bit Score: 42.79  E-value: 8.99e-05
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 2499757     148 SWS---DAPGDQDSYQLLLYHLESQTLACNVSVSPDTLSYSFGDLLPGTQYVLEVIT 201
Cdd:pfam00041   19 SWTpppDGNGPITGYEVEYRPKNSGEPWNEITVPGTTTSVTLTGLKPGTEYEVRVQA 75
FN3 smart00060
Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, ...
 49-110 3.74e-03

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: 37.98  E-value: 3.74e-03
                            10        20        30        40        50        60
                    ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2499757       49 STSLFLSWVAAELGGFD-YALSLRSVNSSGSPEGQQLQAHTNESGFEFHGLVPGSRYQLKLTV 110
Cdd:smart00060   14 STSVTLSWEPPPDDGITgYIVGYRVEYREEGSEWKEVNVTPSSTSYTLTGLKPGTEYEFRVRA 76
fn3 pfam00041
Fibronectin type III domain;
49-109 5.99e-03

Fibronectin type III domain;


Pssm-ID: 394996 [Multi-domain]  Cd Length: 85  Bit Score: 37.39  E-value: 5.99e-03
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2499757      49 STSLFLSWVAAELGG---FDYALSLRSVNSSGSPegQQLQAHTNESGFEFHGLVPGSRYQLKLT 109
Cdd:pfam00041   13 STSLTVSWTPPPDGNgpiTGYEVEYRPKNSGEPW--NEITVPGTTTSVTLTGLKPGTEYEVRVQ 74
 
Name Accession Description Interval E-value
R-PTPc-V cd14618
catalytic domain of receptor-type tyrosine-protein phosphatase V; Receptor-type ...
 1178-1407 2.05e-156

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: 475.97  E-value: 2.05e-156
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2499757  1178 NRYPHVLPYDHSRVRLTQLPGEPHSDYINANFIPGYSHTQEIIATQGPLKKTLEDFWRLVWEQQVHVIIMLTVGMENGRV 1257
Cdd:cd14618    1 NRYPHVLPYDHSRVRLSQLGGEPHSDYINANFIPGYTSPQEFIATQGPLKKTIEDFWRLVWEQQVCNIIMLTVGMENGRV 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2499757  1258 LCEHYWPANSTPVTHGHITIHLLAEEPEDEWTRREFQLQHGTEQKQRRVKQLQFTTWPDHSVPEAPSSLLAFVELVQEQV 1337
Cdd:cd14618   81 LCDHYWPSESTPVSYGHITVHLLAQSSEDEWTRREFKLWHEDLRKERRVKHLHYTAWPDHGIPESTSSLMAFRELVREHV 160

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2499757  1338 QATQGKGPILVHCSAGVGRTGTFVALLRLLRQLEEEKVADVFNTVYILRLHRPLMIQTLSQYIFLHSCLL 1407
Cdd:cd14618  161 QATKGKGPTLVHCSAGVGRSGTFIALDRLLRQLKEEKVVDVFNTVYILRMHRYLMIQTLSQYIFLHSCIL 230
R3-PTPc cd14548
catalytic domain of R3 subfamily receptor-type tyrosine-protein phosphatases and similar ...
 1179-1404 2.89e-123

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: 385.55  E-value: 2.89e-123
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2499757  1179 RYPHVLPYDHSRVRLTQLPGEPHSDYINANFIPGYSHTQEIIATQGPLKKTLEDFWRLVWEQQVHVIIMLTVGMENGRVL 1258
Cdd:cd14548    1 RYTNILPYDHSRVKLIPINEEEGSDYINANYIPGYNSPREFIATQGPLPGTKDDFWRMVWEQNSHTIVMLTQCMEKGRVK 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2499757  1259 CEHYWPANSTPVTHGHITIHLLAEEPEDEWTRREFQLQHGteQKQRRVKQLQFTTWPDHSVPEAPSSLLAFVELVQEQVQ 1338
Cdd:cd14548   81 CDHYWPFDQDPVYYGDITVTMLSESVLPDWTIREFKLERG--DEVRSVRQFHFTAWPDHGVPEAPDSLLRFVRLVRDYIK 158

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2499757  1339 atQGKGPILVHCSAGVGRTGTFVALLRLLRQLEEEKVADVFNTVYILRLHRPLMIQTLSQYIFLHS 1404
Cdd:cd14548  159 --QEKGPTIVHCSAGVGRTGTFIALDRLLQQIESEDYVDIFGIVYDLRKHRPLMVQTEAQYIFLHQ 222
PTPc smart00194
Protein tyrosine phosphatase, catalytic domain;
1150-1408 3.85e-106

Protein tyrosine phosphatase, catalytic domain;


Pssm-ID: 214550 [Multi-domain]  Cd Length: 259  Bit Score: 339.25  E-value: 3.85e-106
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2499757     1150 FFQEFEELKEVGK-DQPRLEAEHPDNIIKNRYPHVLPYDHSRVRLTQLPGEPhSDYINANFIPGYSHTQEIIATQGPLKK 1228
Cdd:smart00194    2 LEEEFEKLDRLKPdDESCTVAAFPENRDKNRYKDVLPYDHTRVKLKPPPGEG-SDYINASYIDGPNGPKAYIATQGPLPS 80

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2499757     1229 TLEDFWRLVWEQQVHVIIMLTVGMENGRVLCEHYWPAN-STPVTHGHITIHLLAEEPEDEWTRREFQLQHGTEQKQRRVK 1307
Cdd:smart00194   81 TVEDFWRMVWEQKVTVIVMLTELVEKGREKCAQYWPDEeGEPLTYGDITVTLKSVEKVDDYTIRTLEVTNTGCSETRTVT 160

                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2499757     1308 QLQFTTWPDHSVPEAPSSLLAFVELVqEQVQATQgKGPILVHCSAGVGRTGTFVALLRLLRQLEEEKVADVFNTVYILRL 1387
Cdd:smart00194  161 HYHYTNWPDHGVPESPESILDLIRAV-RKSQSTS-TGPIVVHCSAGVGRTGTFIAIDILLQQLEAGKEVDIFEIVKELRS 238

                           250       260
                    ....*....|....*....|.
gi 2499757     1388 HRPLMIQTLSQYIFLHSCLLN 1408
Cdd:smart00194  239 QRPGMVQTEEQYIFLYRAILE 259
Y_phosphatase pfam00102
Protein-tyrosine phosphatase;
1174-1408 1.56e-100

Protein-tyrosine phosphatase;


Pssm-ID: 459674 [Multi-domain]  Cd Length: 234  Bit Score: 322.27  E-value: 1.56e-100
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2499757    1174 NIIKNRYPHVLPYDHSRVRLTQLPGepHSDYINANFIPGYSHTQEIIATQGPLKKTLEDFWRLVWEQQVHVIIMLTVGME 1253
Cdd:pfam00102    1 NLEKNRYKDVLPYDHTRVKLTGDPG--PSDYINASYIDGYKKPKKYIATQGPLPNTVEDFWRMVWEEKVTIIVMLTELEE 78

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2499757    1254 NGRVLCEHYWP-ANSTPVTHGHITIHLLAEEP-EDEWTRREFQLQHGTEQKQRRVKQLQFTTWPDHSVPEAPSSLLAFVE 1331
Cdd:pfam00102   79 KGREKCAQYWPeEEGESLEYGDFTVTLKKEKEdEKDYTVRTLEVSNGGSEETRTVKHFHYTGWPDHGVPESPNSLLDLLR 158

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2499757    1332 LVqEQVQATQGKGPILVHCSAGVGRTGTFVALLRLLRQLEEEKVADVFNTVYILRLHRPLMIQTLSQYIFLHSCLLN 1408
Cdd:pfam00102  159 KV-RKSSLDGRSGPIVVHCSAGIGRTGTFIAIDIALQQLEAEGEVDIFQIVKELRSQRPGMVQTLEQYIFLYDAILE 234
R-PTPc-H cd14619
catalytic domain of receptor-type tyrosine-protein phosphatase H; Receptor-type ...
 1178-1410 1.40e-91

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: 296.80  E-value: 1.40e-91
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2499757  1178 NRYPHVLPYDHSRVRLTQLPGEPHSDYINANFIPGYSHTQEIIATQGPLKKTLEDFWRLVWEQQVHVIIMLTVGMENGRV 1257
Cdd:cd14619    1 NRFRNVLPYDWSRVPLKPIHEEPGSDYINANYMPGYWSSQEFIATQGPLPQTVGDFWRMIWEQQSSTIVMLTNCMEAGRV 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2499757  1258 LCEHYWPANSTPVTHGHITIHLLAEEPEDEWTRREFQLQHGTEQKQRRVKQLQFTTWPDHSVPEAPSSLLAFVELVQEQV 1337
Cdd:cd14619   81 KCEHYWPLDYTPCTYGHLRVTVVSEEVMENWTVREFLLKQVEEQKTLSVRHFHFTAWPDHGVPSSTDTLLAFRRLLRQWL 160

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2499757  1338 QATQGKGPILVHCSAGVGRTGTFVALLRLLRQLEEEKVADVFNTVYILRLHRPLMIQTLSQYIFLHSCLLNKI 1410
Cdd:cd14619  161 DQTMSGGPTVVHCSAGVGRTGTLIALDVLLQQLQSEGLLGPFSFVQKMRENRPLMVQTESQYVFLHQCILDFL 233
R-PTPc-J cd14615
catalytic domain of receptor-type tyrosine-protein phosphatase J; Receptor-type ...
 1178-1408 2.68e-89

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: 290.18  E-value: 2.68e-89
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2499757  1178 NRYPHVLPYDHSRVRLTqLPGEPHSDYINANFIPGYSHTQEIIATQGPLKKTLEDFWRLVWEQQVHVIIMLTVGMENGRV 1257
Cdd:cd14615    1 NRYNNVLPYDISRVKLS-VQSHSTDDYINANYMPGYNSKKEFIAAQGPLPNTVKDFWRMVWEKNVYAIVMLTKCVEQGRT 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2499757  1258 LCEHYWPAnSTPVTHGHITIHLLAEEPEDEWTRREFQLQHGTEQKQRRVKQLQFTTWPDHSVPEAPSSLLAFVELVQEQV 1337
Cdd:cd14615   80 KCEEYWPS-KQKKDYGDITVTMTSEIVLPEWTIRDFTVKNAQTNESRTVRHFHFTSWPDHGVPETTDLLINFRHLVREYM 158

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2499757  1338 QATQGKGPILVHCSAGVGRTGTFVALLRLLRQLEEEKVADVFNTVYILRLHRPLMIQTLSQYIFLHSCLLN 1408
Cdd:cd14615  159 KQNPPNSPILVHCSAGVGRTGTFIAIDRLIYQIENENVVDVYGIVYDLRMHRPLMVQTEDQYVFLNQCALD 229
R-PTPc-O cd14614
catalytic domain of receptor-type tyrosine-protein phosphatase O; Receptor-type ...
 1163-1407 7.29e-83

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: 272.15  E-value: 7.29e-83
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2499757  1163 DQPRLEAEHPDNIIKNRYPHVLPYDHSRVRLTQLPGEPHSDYINANFIPGYSHTQEIIATQGPLKKTLEDFWRLVWEQQV 1242
Cdd:cd14614    1 DIPHFAADLPVNRCKNRYTNILPYDFSRVKLVSMHEEEGSDYINANYIPGYNSPQEYIATQGPLPETRNDFWKMVLQQKS 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2499757  1243 HVIIMLTVGMENGRVLCEHYWPANSTPVTHGHITIHLLAEEPEDEWTRREFQLQHGTEQKqrRVKQLQFTTWPDHSVP-- 1320
Cdd:cd14614   81 QIIVMLTQCNEKRRVKCDHYWPFTEEPVAYGDITVEMLSEEEQPDWAIREFRVSYADEVQ--DVMHFNYTAWPDHGVPta 158

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2499757  1321 EAPSSLLAFVELVQEqvQATQGKGPILVHCSAGVGRTGTFVALLRLLRQLEEEKVADVFNTVYILRLHRPLMIQTLSQYI 1400
Cdd:cd14614  159 NAAESILQFVQMVRQ--QAVKSKGPMIIHCSAGVGRTGTFIALDRLLQHIRDHEFVDILGLVSEMRSYRMSMVQTEEQYI 236


                 ....*..
gi 2499757  1401 FLHSCLL 1407
Cdd:cd14614  237 FIHQCVQ 243
PTPc cd00047
catalytic domain of protein tyrosine phosphatases; Protein tyrosine phosphatases (PTP, EC 3.1. ...
 1204-1403 1.85e-81

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: 266.46  E-value: 1.85e-81
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2499757  1204 YINANFIPGYSHTQEIIATQGPLKKTLEDFWRLVWEQQVHVIIMLTVGMENGRVLCEHYWPAN-STPVTHGHITIHLLAE 1282
Cdd:cd00047    1 YINASYIDGYRGPKEYIATQGPLPNTVEDFWRMVWEQKVSVIVMLTNLVEKGREKCERYWPEEgGKPLEYGDITVTLVSE 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2499757  1283 EPEDEWTRREFQLQHGTEQKQRRVKQLQFTTWPDHSVPEAPSSLLAFVELVQEqvQATQGKGPILVHCSAGVGRTGTFVA 1362
Cdd:cd00047   81 EELSDYTIRTLELSPKGCSESREVTHLHYTGWPDHGVPSSPEDLLALVRRVRK--EARKPNGPIVVHCSAGVGRTGTFIA 158

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|.
gi 2499757  1363 LLRLLRQLEEEKVADVFNTVYILRLHRPLMIQTLSQYIFLH 1403
Cdd:cd00047  159 IDILLERLEAEGEVDVFEIVKALRKQRPGMVQTLEQYEFIY 199
R-PTPc-B cd14617
catalytic domain of receptor-type tyrosine-protein phosphatase B; Receptor-type ...
 1178-1403 4.68e-80

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: 263.32  E-value: 4.68e-80
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2499757  1178 NRYPHVLPYDHSRVRLTQLPGEPHSDYINANFIPGYSHTQEIIATQGPLKKTLEDFWRLVWEQQVHVIIMLTVGMENGRV 1257
Cdd:cd14617    1 NRYNNILPYDSTRVKLSNVDDDPCSDYINASYIPGNNFRREYIATQGPLPGTKDDFWKMVWEQNVHNIVMVTQCVEKGRV 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2499757  1258 LCEHYWPANSTPVTHGHITIHLLAEEPEDEWTRREFQLQhGTEQ--KQRRVKQLQFTTWPDHSVPEAPSSLLAFVELVQE 1335
Cdd:cd14617   81 KCDHYWPADQDSLYYGDLIVQMLSESVLPEWTIREFKIC-SEEQldAPRLVRHFHYTVWPDHGVPETTQSLIQFVRTVRD 159

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2499757  1336 QVQATQGKGPILVHCSAGVGRTGTFVALLRLLRQLEEEKVADVFNTVYILRLHRPLMIQTLSQYIFLH 1403
Cdd:cd14617  160 YINRTPGSGPTVVHCSAGVGRTGTFIALDRILQQLDSKDSVDIYGAVHDLRLHRVHMVQTECQYVYLH 227
R-PTPc-LAR-1 cd14553
catalytic domain of LAR family receptor-type tyrosine-protein phosphatases, repeat 1; The LAR ...
 1174-1410 4.92e-80

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: 263.87  E-value: 4.92e-80
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2499757  1174 NIIKNRYPHVLPYDHSRVRLTQLPGEPHSDYINANFIPGYSHTQEIIATQGPLKKTLEDFWRLVWEQQVHVIIMLTVGME 1253
Cdd:cd14553    3 NKPKNRYANVIAYDHSRVILQPIEGVPGSDYINANYCDGYRKQNAYIATQGPLPETFGDFWRMVWEQRSATIVMMTKLEE 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2499757  1254 NGRVLCEHYWPANSTPvTHGHITIHLLAEEPEDEWTRREFQLQHGTEQKQRRVKQLQFTTWPDHSVPEAPSSLLAFVELV 1333
Cdd:cd14553   83 RSRVKCDQYWPTRGTE-TYGLIQVTLLDTVELATYTVRTFALHKNGSSEKREVRQFQFTAWPDHGVPEHPTPFLAFLRRV 161

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2499757  1334 QEQVQATqgKGPILVHCSAGVGRTGTFVALLRLLRQLEEEKVADVFNTVYILRLHRPLMIQTLSQYIFLHSCLLNKI 1410
Cdd:cd14553  162 KACNPPD--AGPIVVHCSAGVGRTGCFIVIDSMLERIKHEKTVDIYGHVTCLRAQRNYMVQTEDQYIFIHDALLEAV 236
PTPc-N9 cd14543
catalytic domain of tyrosine-protein phosphatase non-receptor type 9; Tyrosine-protein ...
 1154-1404 2.75e-74

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: 248.82  E-value: 2.75e-74
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2499757  1154 FEELKEVGKDQPR---LEAEHPDNIIKNRYPHVLPYDHSRVRLTQLPGEPHSDYINANFIPGYSHTQEIIATQGPLKKTL 1230
Cdd:cd14543    6 YEEYEDIRREPPAgtfLCSLAPANQEKNRYGDVLCLDQSRVKLPKRNGDERTDYINANFMDGYKQKNAYIATQGPLPKTY 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2499757  1231 EDFWRLVWEQQVHVIIMLTVGMENGRVLCEHYWP--ANSTPVtHGHITI-HLLAEEPEDeWTRREFQLQHGTEQKQRRVK 1307
Cdd:cd14543   86 SDFWRMVWEQKVLVIVMTTRVVERGRVKCGQYWPleEGSSLR-YGDLTVtNLSVENKEH-YKKTTLEIHNTETDESRQVT 163

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2499757  1308 QLQFTTWPDHSVPEAPSSLLAFVELV-QEQVQATQGKG----------PILVHCSAGVGRTGTFVALLRLLRQLEEEKVA 1376
Cdd:cd14543  164 HFQFTSWPDFGVPSSAAALLDFLGEVrQQQALAVKAMGdrwkghppgpPIVVHCSAGIGRTGTFCTLDICLSQLEDVGTL 243

                        250       260
                 ....*....|....*....|....*...
gi 2499757  1377 DVFNTVYILRLHRPLMIQTLSQYIFLHS 1404
Cdd:cd14543  244 NVMQTVRRMRTQRAFSIQTPDQYYFCYK 271
R-PTPc-F-1 cd14626
catalytic domain of receptor-type tyrosine-protein phosphatase F, repeat 1; Receptor-type ...
 1150-1407 1.52e-68

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: 232.62  E-value: 1.52e-68
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2499757  1150 FFQEFEEL---KEVGKDQPRLEAEHPdniiKNRYPHVLPYDHSRVRLTQLPGEPHSDYINANFIPGYSHTQEIIATQGPL 1226
Cdd:cd14626   18 FSQEYESIdpgQQFTWENSNLEVNKP----KNRYANVIAYDHSRVILTSVDGVPGSDYINANYIDGYRKQNAYIATQGPL 93

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2499757  1227 KKTLEDFWRLVWEQQVHVIIMLTVGMENGRVLCEHYWPANSTPvTHGHITIHLLAEEPEDEWTRREFQLQHGTEQKQRRV 1306
Cdd:cd14626   94 PETLSDFWRMVWEQRTATIVMMTRLEEKSRVKCDQYWPIRGTE-TYGMIQVTLLDTVELATYSVRTFALYKNGSSEKREV 172

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2499757  1307 KQLQFTTWPDHSVPEAPSSLLAFVELVQEQVQATqgKGPILVHCSAGVGRTGTFVALLRLLRQLEEEKVADVFNTVYILR 1386
Cdd:cd14626  173 RQFQFMAWPDHGVPEYPTPILAFLRRVKACNPPD--AGPMVVHCSAGVGRTGCFIVIDAMLERMKHEKTVDIYGHVTCMR 250

                        250       260
                 ....*....|....*....|.
gi 2499757  1387 LHRPLMIQTLSQYIFLHSCLL 1407
Cdd:cd14626  251 SQRNYMVQTEDQYIFIHEALL 271
PTPc-KIM cd14547
catalytic domain of the kinase interaction motif (KIM) family of protein-tyrosine phosphatases; ...
 1178-1403 1.51e-67

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


Pssm-ID: 350395 [Multi-domain]  Cd Length: 224  Bit Score: 227.28  E-value: 1.51e-67
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2499757  1178 NRYPHVLPYDHSRVRLTQLPGEPHSDYINANFIPGYSHTQEI-IATQGPLKKTLEDFWRLVWEQQVHVIIMLTvGMENGR 1256
Cdd:cd14547    1 NRYKTILPNEHSRVCLPSVDDDPLSSYINANYIRGYDGEEKAyIATQGPLPNTVADFWRMVWQEKTPIIVMIT-NLTEAK 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2499757  1257 VLCEHYWPaNSTPVTHGHITIHLLAEEPEDEWTRREFQLQHGTEQkqRRVKQLQFTTWPDHSVPEAPSSLLAFVELVQEQ 1336
Cdd:cd14547   80 EKCAQYWP-EEENETYGDFEVTVQSVKETDGYTVRKLTLKYGGEK--RYLKHYWYTSWPDHKTPEAAQPLLSLVQEVEEA 156

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2499757  1337 VQATQGKGPILVHCSAGVGRTGTFVALLRLLRQLEEEKVADVFNTVYILRLHRPLMIQTLSQYIFLH 1403
Cdd:cd14547  157 RQTEPHRGPIVVHCSAGIGRTGCFIATSIGCQQLREEGVVDVLGIVCQLRLDRGGMVQTAEQYEFVH 223
R-PTPc-D-1 cd14624
catalytic domain of receptor-type tyrosine-protein phosphatase D, repeat 1; Receptor-type ...
 1127-1413 5.01e-67

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: 228.46  E-value: 5.01e-67
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2499757  1127 HRPIPIHSFRQSYEAKSAHAHQTFFQEFEEL---KEVGKDQPRLEAEHPdniiKNRYPHVLPYDHSRVRLTQLPGEPHSD 1203
Cdd:cd14624    1 HPPIPILELADHIERLKANDNLKFSQEYESIdpgQQFTWEHSNLEVNKP----KNRYANVIAYDHSRVLLSAIEGIPGSD 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2499757  1204 YINANFIPGYSHTQEIIATQGPLKKTLEDFWRLVWEQQVHVIIMLTVGMENGRVLCEHYWPANSTPvTHGHITIHLLAEE 1283
Cdd:cd14624   77 YINANYIDGYRKQNAYIATQGALPETFGDFWRMIWEQRSATVVMMTKLEERSRVKCDQYWPSRGTE-TYGLIQVTLLDTV 155

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2499757  1284 PEDEWTRREFQLQHGTEQKQRRVKQLQFTTWPDHSVPEAPSSLLAFVELVqeQVQATQGKGPILVHCSAGVGRTGTFVAL 1363
Cdd:cd14624  156 ELATYCVRTFALYKNGSSEKREVRQFQFTAWPDHGVPEHPTPFLAFLRRV--KTCNPPDAGPMVVHCSAGVGRTGCFIVI 233

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|
gi 2499757  1364 LRLLRQLEEEKVADVFNTVYILRLHRPLMIQTLSQYIFLHSCLLNKILEG 1413
Cdd:cd14624  234 DAMLERIKHEKTVDIYGHVTLMRAQRNYMVQTEDQYIFIHDALLEAVTCG 283
R-PTPc-T-1 cd14630
catalytic domain of receptor-type tyrosine-protein phosphatase T, repeat 1; Receptor-type ...
 1173-1411 8.55e-66

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: 222.98  E-value: 8.55e-66
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2499757  1173 DNIIKNRYPHVLPYDHSRVRLTQLPGEPHSDYINANFIPGYSHTQEIIATQGPLKKTLEDFWRLVWEQQVHVIIMLTVGM 1252
Cdd:cd14630    2 ENRNKNRYGNIISYDHSRVRLQLLDGDPHSDYINANYIDGYHRPRHYIATQGPMQETVKDFWRMIWQENSASVVMVTNLV 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2499757  1253 ENGRVLCEHYWPANSTpvTHGHITIHLLAEEPEDEWTRREFQLQHGTEQKQRRVKQLQFTTWPDHSVPEAPSSLLAFVEl 1332
Cdd:cd14630   82 EVGRVKCVRYWPDDTE--VYGDIKVTLIETEPLAEYVIRTFTVQKKGYHEIREIRQFHFTSWPDHGVPCYATGLLGFVR- 158

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2499757  1333 vQEQVQATQGKGPILVHCSAGVGRTGTFVALLRLLRQLEEEKVADVFNTVYILRLHRPLMIQTLSQYIFLHSCLLNKIL 1411
Cdd:cd14630  159 -QVKFLNPPDAGPIVVHCSAGAGRTGCFIAIDIMLDMAENEGVVDIFNCVRELRAQRVNMVQTEEQYVFVHDAILEACL 236
R-PTPc-G-1 cd17667
catalytic domain of receptor-type tyrosine-protein phosphatase G, repeat 1; Receptor-type ...
 1150-1411 9.68e-66

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: 224.14  E-value: 9.68e-66
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2499757  1150 FFQEFEELKEVGKDQpRLEAEH---PDNIIKNRYPHVLPYDHSRVRLTQLPGE--PHSDYINANFIPGYSHTQEIIATQG 1224
Cdd:cd17667    1 FSEDFEEVQRCTADM-NITAEHsnhPDNKHKNRYINILAYDHSRVKLRPLPGKdsKHSDYINANYVDGYNKAKAYIATQG 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2499757  1225 PLKKTLEDFWRLVWEQQVHVIIMLTVGMENGRVLCEHYWPANSTPvTHGHITIHLLAEEPEDEWTRREFQLQH-----GT 1299
Cdd:cd17667   80 PLKSTFEDFWRMIWEQNTGIIVMITNLVEKGRRKCDQYWPTENSE-EYGNIIVTLKSTKIHACYTVRRFSIRNtkvkkGQ 158

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2499757  1300 E------QKQRRVKQLQFTTWPDHSVPEAPSSLLAFVElvQEQVQATQGKGPILVHCSAGVGRTGTFVALLRLLRQLEEE 1373
Cdd:cd17667  159 KgnpkgrQNERTVIQYHYTQWPDMGVPEYALPVLTFVR--RSSAARTPEMGPVLVHCSAGVGRTGTYIVIDSMLQQIKDK 236

                        250       260       270
                 ....*....|....*....|....*....|....*...
gi 2499757  1374 KVADVFNTVYILRLHRPLMIQTLSQYIFLHSCLLNKIL 1411
Cdd:cd17667  237 STVNVLGFLKHIRTQRNYLVQTEEQYIFIHDALLEAIL 274
R5-PTPc-1 cd14549
catalytic domain of R5 subfamily receptor-type tyrosine-protein phosphatases, repeat 1; The R5 ...
 1204-1403 2.07e-65

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: 220.30  E-value: 2.07e-65
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2499757  1204 YINANFIPGYSHTQEIIATQGPLKKTLEDFWRLVWEQQVHVIIMLTVGMENGRVLCEHYWPANSTPvTHGHITIHLLAEE 1283
Cdd:cd14549    1 YINANYVDGYNKARAYIATQGPLPSTFDDFWRMVWEQNSAIIVMITNLVERGRRKCDQYWPKEGTE-TYGNIQVTLLSTE 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2499757  1284 PEDEWTRREFQLQHGTEQK------QRRVKQLQFTTWPDHSVPEAPSSLLAFvelVQEQVQAT-QGKGPILVHCSAGVGR 1356
Cdd:cd14549   80 VLATYTVRTFSLKNLKLKKvkgrssERVVYQYHYTQWPDHGVPDYTLPVLSF---VRKSSAANpPGAGPIVVHCSAGVGR 156

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*..
gi 2499757  1357 TGTFVALLRLLRQLEEEKVADVFNTVYILRLHRPLMIQTLSQYIFLH 1403
Cdd:cd14549  157 TGTYIVIDSMLQQIQDKGTVNVFGFLKHIRTQRNYLVQTEEQYIFIH 203
R-PTPc-S-1 cd14625
catalytic domain of receptor-type tyrosine-protein phosphatase S, repeat 1; Receptor-type ...
 1127-1410 1.49e-64

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: 221.12  E-value: 1.49e-64
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2499757  1127 HRPIPIHSFRQSYEAKSAHAHQTFFQEFEEL---KEVGKDQPRLEAEHPdniiKNRYPHVLPYDHSRVRLTQLPGEPHSD 1203
Cdd:cd14625    1 HPPIPISELAEHTERLKANDNLKLSQEYESIdpgQQFTWEHSNLEVNKP----KNRYANVIAYDHSRVILQPIEGIMGSD 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2499757  1204 YINANFIPGYSHTQEIIATQGPLKKTLEDFWRLVWEQQVHVIIMLTVGMENGRVLCEHYWPANSTPvTHGHITIHLLAEE 1283
Cdd:cd14625   77 YINANYIDGYRKQNAYIATQGPLPETFGDFWRMVWEQRSATVVMMTKLEEKSRIKCDQYWPSRGTE-TYGMIQVTLLDTI 155

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2499757  1284 PEDEWTRREFQLQHGTEQKQRRVKQLQFTTWPDHSVPEAPSSLLAFVELVqeQVQATQGKGPILVHCSAGVGRTGTFVAL 1363
Cdd:cd14625  156 ELATFCVRTFSLHKNGSSEKREVRQFQFTAWPDHGVPEYPTPFLAFLRRV--KTCNPPDAGPIVVHCSAGVGRTGCFIVI 233

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*..
gi 2499757  1364 LRLLRQLEEEKVADVFNTVYILRLHRPLMIQTLSQYIFLHSCLLNKI 1410
Cdd:cd14625  234 DAMLERIKHEKTVDIYGHVTLMRSQRNYMVQTEDQYSFIHDALLEAV 280
R-PTP-LAR-2 cd14554
PTP-like domain of the LAR family receptor-type tyrosine-protein phosphatases, repeat 2; The ...
 1169-1403 1.96e-64

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: 218.93  E-value: 1.96e-64
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2499757  1169 AEHPDNIIKNRYPHVLPYDHSRVRLTQLPGEPHSDYINANFIPGYSHTQEIIATQGPLKKTLEDFWRLVWEQQVHVIIML 1248
Cdd:cd14554    1 ANLPCNKFKNRLVNILPYESTRVCLQPIRGVEGSDYINASFIDGYRQRGAYIATQGPLAETTEDFWRMLWEHNSTIIVML 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2499757  1249 TVGMENGRVLCEHYWPANsTPVTHGHITIHLLAEEPEDEWTRREFQLQHGTEQKQRRVKQLQFTTWPDHSVPEAPSSLLA 1328
Cdd:cd14554   81 TKLREMGREKCHQYWPAE-RSARYQYFVVDPMAEYNMPQYILREFKVTDARDGQSRTVRQFQFTDWPEQGVPKSGEGFID 159

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2499757  1329 FVELVQEQVQATQGKGPILVHCSAGVGRTGTFVALLRLLRQLEEEKVADVFNTVYILRLHRPLMIQTLSQYIFLH 1403
Cdd:cd14554  160 FIGQVHKTKEQFGQEGPITVHCSAGVGRTGVFITLSIVLERMRYEGVVDVFQTVKLLRTQRPAMVQTEDQYQFCY 234
R-PTPc-Q cd14616
catalytic domain of receptor-type tyrosine-protein phosphatase Q; Receptor-type ...
 1178-1403 3.62e-64

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: 217.85  E-value: 3.62e-64
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2499757  1178 NRYPHVLPYDHSRVRLTQLPGEPHSDYINANFIPGYSHTQEIIATQGPLKKTLEDFWRLVWEQQVHVIIMLTVGMENGRV 1257
Cdd:cd14616    1 NRFPNIKPYNNNRVKLIADAGVPGSDYINASYISGYLCPNEFIATQGPLPGTVGDFWRMVWETRAKTIVMLTQCFEKGRI 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2499757  1258 LCEHYWPANSTPVT-HGHITIHLLAEEPEDEWTRREFQLQ-HGteqKQRRVKQLQFTTWPDHSVPEAPSSLLAFVELVqe 1335
Cdd:cd14616   81 RCHQYWPEDNKPVTvFGDIVITKLMEDVQIDWTIRDLKIErHG---DYMMVRQCNFTSWPEHGVPESSAPLIHFVKLV-- 155

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2499757  1336 QVQATQGKGPILVHCSAGVGRTGTFVALLRLLRQLEEEKVADVFNTVYILRLHRPLMIQTLSQYIFLH 1403
Cdd:cd14616  156 RASRAHDNTPMIVHCSAGVGRTGVFIALDHLTQHINDHDFVDIYGLVAELRSERMCMVQNLAQYIFLH 223
PTPc-N18 cd14603
catalytic domain of tyrosine-protein phosphatase non-receptor type 18; Tyrosine-protein ...
 1172-1403 4.25e-63

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: 216.23  E-value: 4.25e-63
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2499757  1172 PDNIIKNRYPHVLPYDHSRVRLTQLPGEPHSDYINANFIPGYSHTQEIIATQGPLKKTLEDFWRLVWEQQVHVIIMLTVG 1251
Cdd:cd14603   28 KENVKKNRYKDILPYDQTRVILSLLQEEGHSDYINANFIKGVDGSRAYIATQGPLSHTVLDFWRMIWQYGVKVILMACRE 107

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2499757  1252 MENGRVLCEHYWPANSTPVTHGHITIHLLAEE-PEDEWTRREFQLQHgtEQKQRRVKQLQFTTWPDHSVPEAPSSLLAFV 1330
Cdd:cd14603  108 IEMGKKKCERYWAQEQEPLQTGPFTITLVKEKrLNEEVILRTLKVTF--QKESRSVSHFQYMAWPDHGIPDSPDCMLAMI 185

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2499757  1331 ELVQEQVQatQGKGPILVHCSAGVGRTGTFVALLRLLRQLEEEKVAD---VFNTVYILRLHRPLMIQTLSQYIFLH 1403
Cdd:cd14603  186 ELARRLQG--SGPEPLCVHCSAGCGRTGVICTVDYVRQLLLTQRIPPdfsIFDVVLEMRKQRPAAVQTEEQYEFLY 259
PTP_fungal cd18533
fungal protein tyrosine phosphatases; This subfamily contains Saccharomyces cerevisiae ...
 1204-1403 1.69e-62

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: 212.49  E-value: 1.69e-62
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2499757  1204 YINANFI-PGYSHTQEIIATQGPLKKTLEDFWRLVWEQQVHVIIMLTVGMENGRVLCEHYWPANSTPVTHGHITIHLLAE 1282
Cdd:cd18533    1 YINASYItLPGTSSKRYIATQGPLPATIGDFWKMIWQNNVGVIVMLTPLVENGREKCDQYWPSGEYEGEYGDLTVELVSE 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2499757  1283 E--PEDEWTRREFQLQHGTEQKqRRVKQLQFTTWPDHSVPEAPSSLLAFVELVQEQVQATQGKGPILVHCSAGVGRTGTF 1360
Cdd:cd18533   81 EenDDGGFIVREFELSKEDGKV-KKVYHIQYKSWPDFGVPDSPEDLLTLIKLKRELNDSASLDPPIIVHCSAGVGRTGTF 159

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|..
gi 2499757  1361 VA--------LLRLLRQLEEEKVAD-VFNTVYILRLHRPLMIQTLSQYIFLH 1403
Cdd:cd18533  160 IAldslldelKRGLSDSQDLEDSEDpVYEIVNQLRKQRMSMVQTLRQYIFLY 211
R-PTPc-M-1 cd14633
catalytic domain of receptor-type tyrosine-protein phosphatase M, repeat 1; Receptor-type ...
 1150-1411 2.09e-60

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: 208.74  E-value: 2.09e-60
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2499757  1150 FFQEFEELKEvGKDQPRLEAEHPDNIIKNRYPHVLPYDHSRVRLTQLPGEPHSDYINANFIPGYSHTQEIIATQGPLKKT 1229
Cdd:cd14633   17 FKEEYESFFE-GQSAPWDSAKKDENRMKNRYGNIIAYDHSRVRLQPIEGETSSDYINGNYIDGYHRPNHYIATQGPMQET 95

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2499757  1230 LEDFWRLVWEQQVHVIIMLTVGMENGRVLCEHYWPANSTpvTHGHITIHLLAEEPEDEWTRREFQLQHGTEQKQRRVKQL 1309
Cdd:cd14633   96 IYDFWRMVWHENTASIIMVTNLVEVGRVKCCKYWPDDTE--IYKDIKVTLIETELLAEYVIRTFAVEKRGVHEIREIRQF 173

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2499757  1310 QFTTWPDHSVPEAPSSLLAFVELVQEQVQATqgKGPILVHCSAGVGRTGTFVALLRLLRQLEEEKVADVFNTVYILRLHR 1389
Cdd:cd14633  174 HFTGWPDHGVPYHATGLLGFVRQVKSKSPPN--AGPLVVHCSAGAGRTGCFIVIDIMLDMAEREGVVDIYNCVRELRSRR 251

                        250       260
                 ....*....|....*....|..
gi 2499757  1390 PLMIQTLSQYIFLHSCLLNKIL 1411
Cdd:cd14633  252 VNMVQTEEQYVFIHDAILEACL 273
PTPc-N11_6 cd14544
catalytic domain of tyrosine-protein phosphatase non-receptor type 11 and type 6; ...
 1174-1403 2.46e-59

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: 205.00  E-value: 2.46e-59
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2499757  1174 NIIKNRYPHVLPYDHSRVRLTQL-PGEPHSDYINANFI-------PGYSHTQEIIATQGPLKKTLEDFWRLVWEQQVHVI 1245
Cdd:cd14544    1 NKGKNRYKNILPFDHTRVILKDRdPNVPGSDYINANYIrnenegpTTDENAKTYIATQGCLENTVSDFWSMVWQENSRVI 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2499757  1246 IMLTVGMENGRVLCEHYWPANSTPVTHGHITIHLLAEEPEDEWTRREFQLQHGTEQK-QRRVKQLQFTTWPDHSVPEAPS 1324
Cdd:cd14544   81 VMTTKEVERGKNKCVRYWPDEGMQKQYGPYRVQNVSEHDTTDYTLRELQVSKLDQGDpIREIWHYQYLSWPDHGVPSDPG 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2499757  1325 SLLAFVELVQEQVQATQGKGPILVHCSAGVGRTGTFVALLRLLRQLEEEKVA---DVFNTVYILRLHRPLMIQTLSQYIF 1401
Cdd:cd14544  161 GVLNFLEDVNQRQESLPHAGPIVVHCSAGIGRTGTFIVIDMLLDQIKRKGLDcdiDIQKTIQMVRSQRSGMVQTEAQYKF 240


                 ..
gi 2499757  1402 LH 1403
Cdd:cd14544  241 IY 242
R-PTPc-A-1 cd14621
catalytic domain of receptor-type tyrosine-protein phosphatase A, repeat 1; Receptor-type ...
 1125-1413 2.47e-59

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: 206.80  E-value: 2.47e-59
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2499757  1125 RTHRPIPIHSFRQSYEAKSAHAHQTFFQEFEELKEVGKDQPRLEAEHPDNIIKNRYPHVLPYDHSRVRLTQLPGEPHSDY 1204
Cdd:cd14621    3 RKYPPLPVDKLEEEINRRMADDNKLFREEFNALPACPIQATCEAASKEENKEKNRYVNILPYDHSRVHLTPVEGVPDSDY 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2499757  1205 INANFIPGYSHTQEIIATQGPLKKTLEDFWRLVWEQQVHVIIMLTVGMENGRVLCEHYWPANSTpVTHGHITIHLLAEEP 1284
Cdd:cd14621   83 INASFINGYQEKNKFIAAQGPKEETVNDFWRMIWEQNTATIVMVTNLKERKECKCAQYWPDQGC-WTYGNIRVSVEDVTV 161

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2499757  1285 EDEWTRREFQLQH----GTEQKQRRVKQLQFTTWPDHSVPEAPSSLLAFVELVQEqvQATQGKGPILVHCSAGVGRTGTF 1360
Cdd:cd14621  162 LVDYTVRKFCIQQvgdvTNKKPQRLITQFHFTSWPDFGVPFTPIGMLKFLKKVKN--CNPQYAGAIVVHCSAGVGRTGTF 239

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|...
gi 2499757  1361 VALLRLLRQLEEEKVADVFNTVYILRLHRPLMIQTLSQYIFLHSCLLNKILEG 1413
Cdd:cd14621  240 IVIDAMLDMMHAERKVDVYGFVSRIRAQRCQMVQTDMQYVFIYQALLEHYLYG 292
R-PTPc-A-E-2 cd14552
catalytic domain of receptor-type tyrosine-protein phosphatase A and E, repeat 2; ...
 1204-1401 3.58e-58

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: 199.80  E-value: 3.58e-58
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2499757  1204 YINANFIPGYSHTQEIIATQGPLKKTLEDFWRLVWEQQVHVIIMLTVGMENGRVLCEHYWPANSTpVTHGHITIHLLAEE 1283
Cdd:cd14552    1 YINASFIDGYRQKDAYIATQGPLDHTVEDFWRMIWEWKSCSIVMLTEIKERSQNKCAQYWPEDGS-VSSGDITVELKDQT 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2499757  1284 PEDEWTRREFQLQHGTEQKQRRVKQLQFTTWPDHSVPEAPSSLLAFVELVQEQVQATqGKGPILVHCSAGVGRTGTFVAL 1363
Cdd:cd14552   80 DYEDYTLRDFLVTKGKGGSTRTVRQFHFHGWPEVGIPDNGKGMIDLIAAVQKQQQQS-GNHPITVHCSAGAGRTGTFCAL 158

                        170       180       190
                 ....*....|....*....|....*....|....*...
gi 2499757  1364 LRLLRQLEEEKVADVFNTVYILRLHRPLMIQTLSQYIF 1401
Cdd:cd14552  159 STVLERVKAEGVLDVFQVVKSLRLQRPHMVQTLEQYEF 196
R-PTP-D-2 cd14628
PTP-like domain of receptor-type tyrosine-protein phosphatase D, repeat 2; Receptor-type ...
 1153-1407 5.78e-58

PTP-like domain of receptor-type tyrosine-protein phosphatase D, repeat 2; Receptor-type tyrosine-protein phosphatase-like D (PTPRD), also known as receptor-type tyrosine-protein phosphatase delta (R-PTP-delta), belongs to the LAR (leukocyte common antigen-related) family of receptor-type tyrosine-protein phosphatases (RPTPs), which belong to the larger family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. LAR-RPTPs are synaptic adhesion molecules that play roles in various aspects of neuronal development, including axon guidance, neurite extension, and synapse formation and function. PTPRD is involved in pre-synaptic differentiation through interaction with SLITRK2. It contains an extracellular region with three immunoglobulin-like (Ig) domains and four to eight fibronectin type III (FN3) repeats (determined by alternative splicing), a single transmembrane domain, followed by an intracellular region with a membrane-proximal catalytic PTP domain (repeat 1, also called D1) and a membrane-distal non-catalytic PTP-like domain (repeat 2, also called D2). This model represents the non-catalytic PTP-like domain (repeat 2). Although described as non-catalytic, this domain contains the catalytic cysteine and the active site signature motif, HCSAGxGRxG.


Pssm-ID: 350476 [Multi-domain]  Cd Length: 292  Bit Score: 202.65  E-value: 5.78e-58
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2499757  1153 EFEELKEVGKDQPR-LEAEHPDNIIKNRYPHVLPYDHSRVRLTQLPGEPHSDYINANFIPGYSHTQEIIATQGPLKKTLE 1231
Cdd:cd14628   30 EFKRLASSKAHTSRfISANLPCNKFKNRLVNIMPYESTRVCLQPIRGVEGSDYINASFIDGYRQQKAYIATQGPLAETTE 109

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2499757  1232 DFWRLVWEQQVHVIIMLTVGMENGRVLCEHYWPANSTpVTHGHITIHLLAEEPEDEWTRREFQLQHGTEQKQRRVKQLQF 1311
Cdd:cd14628  110 DFWRMLWEHNSTIVVMLTKLREMGREKCHQYWPAERS-ARYQYFVVDPMAEYNMPQYILREFKVTDARDGQSRTVRQFQF 188

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2499757  1312 TTWPDHSVPEAPSSLLAFVELVQEQVQATQGKGPILVHCSAGVGRTGTFVALLRLLRQLEEEKVADVFNTVYILRLHRPL 1391
Cdd:cd14628  189 TDWPEQGVPKSGEGFIDFIGQVHKTKEQFGQDGPISVHCSAGVGRTGVFITLSIVLERMRYEGVVDIFQTVKMLRTQRPA 268

                        250
                 ....*....|....*.
gi 2499757  1392 MIQTLSQYIFLHSCLL 1407
Cdd:cd14628  269 MVQTEDQYQFCYRAAL 284
R-PTP-S-2 cd14627
PTP-like domain of receptor-type tyrosine-protein phosphatase S, repeat 2; Receptor-type ...
 1153-1407 1.18e-57

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: 201.50  E-value: 1.18e-57
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2499757  1153 EFEELKEVGKDQPR-LEAEHPDNIIKNRYPHVLPYDHSRVRLTQLPGEPHSDYINANFIPGYSHTQEIIATQGPLKKTLE 1231
Cdd:cd14627   31 EFKRLANSKAHTSRfISANLPCNKFKNRLVNIMPYETTRVCLQPIRGVEGSDYINASFIDGYRQQKAYIATQGPLAETTE 110

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2499757  1232 DFWRLVWEQQVHVIIMLTVGMENGRVLCEHYWPANSTpVTHGHITIHLLAEEPEDEWTRREFQLQHGTEQKQRRVKQLQF 1311
Cdd:cd14627  111 DFWRMLWENNSTIVVMLTKLREMGREKCHQYWPAERS-ARYQYFVVDPMAEYNMPQYILREFKVTDARDGQSRTVRQFQF 189

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2499757  1312 TTWPDHSVPEAPSSLLAFVELVQEQVQATQGKGPILVHCSAGVGRTGTFVALLRLLRQLEEEKVADVFNTVYILRLHRPL 1391
Cdd:cd14627  190 TDWPEQGVPKSGEGFIDFIGQVHKTKEQFGQDGPISVHCSAGVGRTGVFITLSIVLERMRYEGVVDIFQTVKMLRTQRPA 269

                        250
                 ....*....|....*.
gi 2499757  1392 MIQTLSQYIFLHSCLL 1407
Cdd:cd14627  270 MVQTEDEYQFCYQAAL 285
PTPc-N20_13 cd14538
catalytic domain of tyrosine-protein phosphatase non-receptor type 20 and type 13; ...
 1204-1407 2.54e-57

catalytic domain of tyrosine-protein phosphatase non-receptor type 20 and type 13; Tyrosine-protein phosphatase non-receptor type 20 (PTPN20) and type 13 (PTPN13, also known as PTPL1) belong to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. Human PTPN20 is a widely expressed phosphatase with a dynamic subcellular distribution that is targeted to sites of actin polymerization. Human PTPN13 is an important regulator of tumor aggressiveness.


Pssm-ID: 350386 [Multi-domain]  Cd Length: 207  Bit Score: 197.60  E-value: 2.54e-57
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2499757  1204 YINANFI--PGYSHTQEIIATQGPLKKTLEDFWRLVWEQQVHVIIMLTVGMENGRVLCEHYWP--ANSTPVTHGHITIHL 1279
Cdd:cd14538    1 YINASHIriPVGGDTYHYIACQGPLPNTTGDFWQMVWEQKSEVIAMVTQDVEGGKVKCHRYWPdsLNKPLICGGRLEVSL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2499757  1280 LAEEPEDEWTRREFQLQHGTEQKQRRVKQLQFTTWPDHSVPEAPSSLLAFVELVQEQVQAtqgkGPILVHCSAGVGRTGT 1359
Cdd:cd14538   81 EKYQSLQDFVIRRISLRDKETGEVHHITHLNFTTWPDHGTPQSADPLLRFIRYMRRIHNS----GPIVVHCSAGIGRTGV 156

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*...
gi 2499757  1360 FVALLRLLRQLEEEKVADVFNTVYILRLHRPLMIQTLSQYIFLHSCLL 1407
Cdd:cd14538  157 LITIDVALGLIERDLPFDIQDIVKDLREQRQGMIQTKDQYIFCYKACL 204
R-PTPc-E-1 cd14620
catalytic domain of receptor-type tyrosine-protein phosphatase E, repeat 1; Receptor-type ...
 1180-1407 3.37e-57

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: 197.86  E-value: 3.37e-57
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2499757  1180 YPHVLPYDHSRVRLTQLPGEPHSDYINANFIPGYSHTQEIIATQGPLKKTLEDFWRLVWEQQVHVIIMLTVGMENGRVLC 1259
Cdd:cd14620    1 YPNILPYDHSRVILSQLDGIPCSDYINASYIDGYKEKNKFIAAQGPKQETVNDFWRMVWEQKSATIVMLTNLKERKEEKC 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2499757  1260 EHYWPANSTpVTHGHITIHLlaeepED-----EWTRREFQLQ---HGTEQKQRRVKQLQFTTWPDHSVPEAPSSLLAFVE 1331
Cdd:cd14620   81 YQYWPDQGC-WTYGNIRVAV-----EDcvvlvDYTIRKFCIQpqlPDGCKAPRLVTQLHFTSWPDFGVPFTPIGMLKFLK 154

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2499757  1332 LVQEQVQATqgKGPILVHCSAGVGRTGTFVALLRLLRQLEEEKVADVFNTVYILRLHRPLMIQTLSQYIFLHSCLL 1407
Cdd:cd14620  155 KVKSVNPVH--AGPIVVHCSAGVGRTGTFIVIDAMIDMMHAEQKVDVFEFVSRIRNQRPQMVQTDMQYSFIYQALL 228
PTPc-N3_4 cd14541
catalytic domain of tyrosine-protein phosphatase non-receptor type 21 and type 14; ...
 1203-1407 3.77e-57

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: 197.17  E-value: 3.77e-57
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2499757  1203 DYINANF----IPGYSHTQEIIATQGPLKKTLEDFWRLVWEQQVHVIIMLTVGMENGRVLCEHYWPANSTPVTHGHITIH 1278
Cdd:cd14541    1 DYINANYvnmeIPGSGIVNRYIAAQGPLPNTCADFWQMVWEQKSTLIVMLTTLVERGRVKCHQYWPDLGETMQFGNLQIT 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2499757  1279 LLAEEPEDEWTRREFQLQHGTEQKQRRVKQLQFTTWPDHSVPEAPSSLLAFVELVqeqVQATQGKG-PILVHCSAGVGRT 1357
Cdd:cd14541   81 CVSEEVTPSFAFREFILTNTNTGEERHITQMQYLAWPDHGVPDDSSDFLDFVKRV---RQNRVGMVePTVVHCSAGIGRT 157

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|
gi 2499757  1358 GTFVALLRLLRQLEEEKVADVFNTVYILRLHRPLMIQTLSQYIFLHSCLL 1407
Cdd:cd14541  158 GVLITMETAMCLIEANEPVYPLDIVRTMRDQRAMLIQTPSQYRFVCEAIL 207
R-PTPc-A-2 cd14623
catalytic domain of receptor-type tyrosine-protein phosphatase A, repeat 2; Receptor-type ...
 1179-1403 1.89e-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: 195.65  E-value: 1.89e-56
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2499757  1179 RYPHVLPYDHSRVRLTQLPGEPHSDYINANFIPGYSHTQEIIATQGPLKKTLEDFWRLVWEQQVHVIIMLTVGMENGRVL 1258
Cdd:cd14623    1 RVLQIIPYEFNRVIIPVKRGEENTDYVNASFIDGYRQKDSYIASQGPLQHTIEDFWRMIWEWKSCSIVMLTELEERGQEK 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2499757  1259 CEHYWPANSTpVTHGHITIHLLAEEPEDEWTRREFQLQHGTEQKQRRVKQLQFTTWPDHSVPEAPSSLLAFVELVQEQvQ 1338
Cdd:cd14623   81 CAQYWPSDGS-VSYGDITIELKKEEECESYTVRDLLVTNTRENKSRQIRQFHFHGWPEVGIPSDGKGMINIIAAVQKQ-Q 158

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2499757  1339 ATQGKGPILVHCSAGVGRTGTFVALLRLLRQLEEEKVADVFNTVYILRLHRPLMIQTLSQYIFLH 1403
Cdd:cd14623  159 QQSGNHPITVHCSAGAGRTGTFCALSTVLERVKAEGILDVFQTVKSLRLQRPHMVQTLEQYEFCY 223
PTPc-N7 cd14612
catalytic domain of tyrosine-protein phosphatase non-receptor type 7; Tyrosine-protein ...
 1168-1406 1.19e-55

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


Pssm-ID: 350460 [Multi-domain]  Cd Length: 247  Bit Score: 194.28  E-value: 1.19e-55
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2499757  1168 EAEHPDNIIKNRYPHVLPYDHSRVRLtQLPG--EPHSDYINANFIPGYS-HTQEIIATQGPLKKTLEDFWRLVWEQQVHV 1244
Cdd:cd14612    9 ELDIPGHASKDRYKTILPNPQSRVCL-RRAGsqEEEGSYINANYIRGYDgKEKAYIATQGPMLNTVSDFWEMVWQEECPI 87

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2499757  1245 IIMLTvGMENGRVLCEHYWPANSTpvTHGHITIHLLAEEPEDEWTRREFQLQHGTEQkqRRVKQLQFTTWPDHSVPEAPS 1324
Cdd:cd14612   88 IVMIT-KLKEKKEKCVHYWPEKEG--TYGRFEIRVQDMKECDGYTIRDLTIQLEEES--RSVKHYWFSSWPDHQTPESAG 162

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2499757  1325 SLLAFVELVQEQVQATQGKGPILVHCSAGVGRTGTFVALLRLLRQLEEEKVADVFNTVYILRLHRPLMIQTLSQYIFLHS 1404
Cdd:cd14612  163 PLLRLVAEVEESRQTAASPGPIVVHCSAGIGRTGCFIATSIGCQQLKDTGKVDILGIVCQLRLDRGGMIQTSEQYQFLHH 242


                 ..
gi 2499757  1405 CL 1406
Cdd:cd14612  243 TL 244
R-PTP-F-2 cd14629
PTP-like domain of receptor-type tyrosine-protein phosphatase F, repeat 2; Receptor-type ...
 1167-1399 7.45e-55

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: 193.79  E-value: 7.45e-55
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2499757  1167 LEAEHPDNIIKNRYPHVLPYDHSRVRLTQLPGEPHSDYINANFIPGYSHTQEIIATQGPLKKTLEDFWRLVWEQQVHVII 1246
Cdd:cd14629   46 ISANLPCNKFKNRLVNIMPYELTRVCLQPIRGVEGSDYINASFIDGYRQQKAYIATQGPLAETTEDFWRMLWEHNSTIVV 125

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2499757  1247 MLTVGMENGRVLCEHYWPANSTpVTHGHITIHLLAEEPEDEWTRREFQLQHGTEQKQRRVKQLQFTTWPDHSVPEAPSSL 1326
Cdd:cd14629  126 MLTKLREMGREKCHQYWPAERS-ARYQYFVVDPMAEYNMPQYILREFKVTDARDGQSRTIRQFQFTDWPEQGVPKTGEGF 204

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2499757  1327 LAFVELVQEQVQATQGKGPILVHCSAGVGRTGTFVALLRLLRQLEEEKVADVFNTVYILRLHRPLMIQTLSQY 1399
Cdd:cd14629  205 IDFIGQVHKTKEQFGQDGPITVHCSAGVGRTGVFITLSIVLERMRYEGVVDMFQTVKTLRTQRPAMVQTEDQY 277
R-PTPc-E-2 cd14622
catalytic domain of receptor-type tyrosine-protein phosphatase E, repeat 2; Receptor-type ...
 1203-1403 7.70e-55

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: 190.22  E-value: 7.70e-55
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2499757  1203 DYINANFIPGYSHTQEIIATQGPLKKTLEDFWRLVWEQQVHVIIMLTVGMENGRVLCEHYWPANSTpVTHGHITIHLLAE 1282
Cdd:cd14622    1 DYINASFIDGYRQKDYFIATQGPLAHTVEDFWRMVWEWKCHTIVMLTELQEREQEKCVQYWPSEGS-VTHGEITIEIKND 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2499757  1283 EPEDEWTRREFQLQHGTEQKQRRVKQLQFTTWPDHSVPEAPSSLLAFVELVQEQVQATqGKGPILVHCSAGVGRTGTFVA 1362
Cdd:cd14622   80 TLLETISIRDFLVTYNQEKQTRLVRQFHFHGWPEIGIPAEGKGMIDLIAAVQKQQQQT-GNHPIVVHCSAGAGRTGTFIA 158

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|.
gi 2499757  1363 LLRLLRQLEEEKVADVFNTVYILRLHRPLMIQTLSQYIFLH 1403
Cdd:cd14622  159 LSNILERVKAEGLLDVFQTVKSLRLQRPHMVQTLEQYEFCY 199
PTPc-N12 cd14604
catalytic domain of tyrosine-protein phosphatase non-receptor type 12; Tyrosine-protein ...
 1137-1403 7.83e-55

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: 193.61  E-value: 7.83e-55
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2499757  1137 QSYEAKSAHAHQTFFQEFEELKEVG------KDQPRLEAEHPDNIIKNRYPHVLPYDHSRVRLTQLPGEPHSDYINANFI 1210
Cdd:cd14604   14 QAMKSTDHNGEDNFASDFMRLRRLStkyrteKIYPTATGEKEENVKKNRYKDILPFDHSRVKLTLKTSSQDSDYINANFI 93

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2499757  1211 PGYSHTQEIIATQGPLKKTLEDFWRLVWEQQVHVIIMLTVGMENGRVLCEHYWPA-NSTPVTHGHITIHLLAEEPEDEWT 1289
Cdd:cd14604   94 KGVYGPKAYIATQGPLANTVIDFWRMIWEYNVAIIVMACREFEMGRKKCERYWPLyGEEPMTFGPFRISCEAEQARTDYF 173

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2499757  1290 RREFQLQHgtEQKQRRVKQLQFTTWPDHSVPEAPSSLLAFVELVQEQVQatQGKGPILVHCSAGVGRTGTFVALLRLLRQ 1369
Cdd:cd14604  174 IRTLLLEF--QNETRRLYQFHYVNWPDHDVPSSFDSILDMISLMRKYQE--HEDVPICIHCSAGCGRTGAICAIDYTWNL 249

                        250       260       270
                 ....*....|....*....|....*....|....*..
gi 2499757  1370 LEEEKVAD---VFNTVYILRLHRPLMIQTLSQYIFLH 1403
Cdd:cd14604  250 LKAGKIPEefnVFNLIQEMRTQRHSAVQTKEQYELVH 286
PTPc-N3 cd14600
catalytic domain of tyrosine-protein phosphatase non-receptor type 3; Tyrosine-protein ...
 1169-1407 7.98e-55

catalytic domain of tyrosine-protein phosphatase non-receptor type 3; Tyrosine-protein phosphatase non-receptor type 3 (PTPN3), also called protein-tyrosine phosphatase H1 (PTP-H1), belongs to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. PTPN3 interacts with mitogen-activated protein kinase p38gamma and serves as its specific phosphatase. PTPN3 and p38gamma cooperate to promote Ras-induced oncogenesis. PTPN3 is a large modular protein containing an N-terminal FERM domain, a PDZ domain and a C-terminal catalytic PTP domain. Its PDZ domain binds with the PDZ-binding motif of p38gamma and enables efficient tyrosine dephosphorylation.


Pssm-ID: 350448 [Multi-domain]  Cd Length: 274  Bit Score: 192.76  E-value: 7.98e-55
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2499757  1169 AEHPDNIIKNRYPHVLPYDHSRVRLtqlpgEPHSDYINANF----IPGYSHTQEIIATQGPLKKTLEDFWRLVWEQQVHV 1244
Cdd:cd14600   35 AKLPQNMDKNRYKDVLPYDATRVVL-----QGNEDYINASYvnmeIPSANIVNKYIATQGPLPHTCAQFWQVVWEQKLSL 109

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2499757  1245 IIMLTVGMENGRVLCEHYWPANSTPVTHGHITIHLLAEEPEDEWTRREFQLQHGTEQKQRRVKQLQFTTWPDHSVPEAPS 1324
Cdd:cd14600  110 IVMLTTLTERGRTKCHQYWPDPPDVMEYGGFRVQCHSEDCTIAYVFREMLLTNTQTGEERTVTHLQYVAWPDHGVPDDSS 189

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2499757  1325 SLLAFVELVQEQVQATQgkgPILVHCSAGVGRTGTFVALLRLLRQLEEEKVADVFNTVYILRLHRPLMIQTLSQYIFLHS 1404
Cdd:cd14600  190 DFLEFVNYVRSKRVENE---PVLVHCSAGIGRTGVLVTMETAMCLTERNQPVYPLDIVRKMRDQRAMMVQTSSQYKFVCE 266


                 ...
gi 2499757  1405 CLL 1407
Cdd:cd14600  267 AIL 269
PTPc-N11 cd14605
catalytic domain of tyrosine-protein phosphatase non-receptor type 11; Tyrosine-protein ...
 1173-1403 8.42e-55

catalytic domain of tyrosine-protein phosphatase non-receptor type 11; Tyrosine-protein phosphatase non-receptor type 11 (PTPN11), also called SH2 domain-containing tyrosine phosphatase 2 (SHP-2 or SHP2), belongs to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. PTPN11 promotes the activation of the RAS/Mitogen-Activated Protein Kinases (MAPK) Extracellular-Regulated Kinases 1/2 (ERK1/2) pathway, a canonical signaling cascade that plays key roles in various cellular processes, including proliferation, survival, differentiation, migration, or metabolism. It also regulates the phosphoinositide 3-kinase (PI3K)/AKT pathway, a fundamental cascade that functions in cell survival, proliferation, migration, morphogenesis, and metabolism. PTPN11 dysregulation is associated with several developmental diseases and malignancies, such as Noonan syndrome and juvenile myelomonocytic leukemia. It contains two tandem SH2 domains, a catalytic PTP domain, and a C-terminal tail with regulatory properties.


Pssm-ID: 350453 [Multi-domain]  Cd Length: 253  Bit Score: 192.15  E-value: 8.42e-55
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2499757  1173 DNIIKNRYPHVLPYDHSRVRLTQ-LPGEPHSDYINANFIPGYSHTQEI--------IATQGPLKKTLEDFWRLVWEQQVH 1243
Cdd:cd14605    1 ENKNKNRYKNILPFDHTRVVLHDgDPNEPVSDYINANIIMPEFETKCNnskpkksyIATQGCLQNTVNDFWRMVFQENSR 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2499757  1244 VIIMLTVGMENGRVLCEHYWPANSTPVTHGHITIHLLAEEPEDEWTRREFQL-QHGTEQKQRRVKQLQFTTWPDHSVPEA 1322
Cdd:cd14605   81 VIVMTTKEVERGKSKCVKYWPDEYALKEYGVMRVRNVKESAAHDYILRELKLsKVGQGNTERTVWQYHFRTWPDHGVPSD 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2499757  1323 PSSLLAFVELVQEQVQATQGKGPILVHCSAGVGRTGTFVALLRLLRQLEEEKV---ADVFNTVYILRLHRPLMIQTLSQY 1399
Cdd:cd14605  161 PGGVLDFLEEVHHKQESIMDAGPVVVHCSAGIGRTGTFIVIDILIDIIREKGVdcdIDVPKTIQMVRSQRSGMVQTEAQY 240


                 ....
gi 2499757  1400 IFLH 1403
Cdd:cd14605  241 RFIY 244
PTPc-N5 cd14613
catalytic domain of tyrosine-protein phosphatase non-receptor type 5; Tyrosine-protein ...
 1168-1406 2.36e-54

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: 190.84  E-value: 2.36e-54
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2499757  1168 EAEHPDNIIKNRYPHVLPYDHSRVRLTQL-PGEPHSDYINANFIPGYSHTQEI-IATQGPLKKTLEDFWRLVWEQQVHVI 1245
Cdd:cd14613   19 EYDIPGLVRKNRYKTILPNPHSRVCLTSPdQDDPLSSYINANYIRGYGGEEKVyIATQGPTVNTVGDFWRMVWQERSPII 98

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2499757  1246 IMLTvGMENGRVLCEHYWPANStpVTHGHITIHLLAEEPEDEWTRREFQLQHGTEQkqRRVKQLQFTTWPDHSVPEAPSS 1325
Cdd:cd14613   99 VMIT-NIEEMNEKCTEYWPEEQ--VTYEGIEITVKQVIHADDYRLRLITLKSGGEE--RGLKHYWYTSWPDQKTPDNAPP 173

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2499757  1326 LLAFVELVQEQVQ-ATQGKGPILVHCSAGVGRTGTFVALLRLLRQLEEEKVADVFNTVYILRLHRPLMIQTLSQYIFLHS 1404
Cdd:cd14613  174 LLQLVQEVEEARQqAEPNCGPVIVHCSAGIGRTGCFIATSICCKQLRNEGVVDILRTTCQLRLDRGGMIQTCEQYQFVHH 253


                 ..
gi 2499757  1405 CL 1406
Cdd:cd14613  254 VL 255
R-PTP-C-2 cd14558
PTP-like domain of receptor-type tyrosine-protein phosphatase C, repeat 2; Receptor-type ...
 1204-1403 3.32e-54

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: 188.37  E-value: 3.32e-54
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2499757  1204 YINANFIPGYSHTQEIIATQGPLKKTLEDFWRLVWEQQVHVIIMLTVGMENGRVLCEHYWPANSTpvTHGHITIHLLAEE 1283
Cdd:cd14558    1 YINASFIDGYWGPKSLIATQGPLPDTIADFWQMIFQKKVKVIVMLTELKEGDQEQCAQYWGDEKK--TYGDIEVELKDTE 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2499757  1284 PEDEWTRREFQLQHGTEQKQRRVKQLQFTTWPDHSVPEAPSSLLAFVELVQEQVQATQGKG----PILVHCSAGVGRTGT 1359
Cdd:cd14558   79 KSPTYTVRVFEITHLKRKDSRTVYQYQYHKWKGEELPEKPKDLVDMIKSIKQKLPYKNSKHgrsvPIVVHCSDGSSRTGI 158

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....
gi 2499757  1360 FVALLRLLRQLEEEKVADVFNTVYILRLHRPLMIQTLSQYIFLH 1403
Cdd:cd14558  159 FCALWNLLESAETEKVVDVFQVVKALRKQRPGMVSTLEQYQFLY 202
R-PTPc-K-1 cd14631
catalytic domain of receptor-type tyrosine-protein phosphatase K, repeat 1; Receptor-type ...
 1190-1411 3.78e-54

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: 188.69  E-value: 3.78e-54
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2499757  1190 RVRLTQLPGEPHSDYINANFIPGYSHTQEIIATQGPLKKTLEDFWRLVWEQQVHVIIMLTVGMENGRVLCEHYWPANSTp 1269
Cdd:cd14631    1 RVILQPVEDDPSSDYINANYIDGYQRPSHYIATQGPVHETVYDFWRMIWQEQSACIVMVTNLVEVGRVKCYKYWPDDTE- 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2499757  1270 vTHGHITIHLLAEEPEDEWTRREFQLQHGTEQKQRRVKQLQFTTWPDHSVPEAPSSLLAFVELVqeQVQATQGKGPILVH 1349
Cdd:cd14631   80 -VYGDFKVTCVEMEPLAEYVVRTFTLERRGYNEIREVKQFHFTGWPDHGVPYHATGLLSFIRRV--KLSNPPSAGPIVVH 156

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2499757  1350 CSAGVGRTGTFVALLRLLRQLEEEKVADVFNTVYILRLHRPLMIQTLSQYIFLHSCLLNKIL 1411
Cdd:cd14631  157 CSAGAGRTGCYIVIDIMLDMAEREGVVDIYNCVKALRSRRINMVQTEEQYIFIHDAILEACL 218
R-PTPc-typeIIb-1 cd14555
catalytic domain of type IIb (or R2B) subfamily receptor-type tyrosine-protein phosphatases, ...
 1204-1411 7.54e-54

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: 187.43  E-value: 7.54e-54
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2499757  1204 YINANFIPGYSHTQEIIATQGPLKKTLEDFWRLVWEQQVHVIIMLTVGMENGRVLCEHYWPANSTpvTHGHITIHLLAEE 1283
Cdd:cd14555    1 YINANYIDGYHRPNHYIATQGPMQETVYDFWRMVWQENSASIVMVTNLVEVGRVKCSRYWPDDTE--VYGDIKVTLVETE 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2499757  1284 PEDEWTRREFQLQHGTEQKQRRVKQLQFTTWPDHSVPEAPSSLLAFVELVqeQVQATQGKGPILVHCSAGVGRTGTFVAL 1363
Cdd:cd14555   79 PLAEYVVRTFALERRGYHEIREVRQFHFTGWPDHGVPYHATGLLGFIRRV--KASNPPSAGPIVVHCSAGAGRTGCYIVI 156

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*...
gi 2499757  1364 LRLLRQLEEEKVADVFNTVYILRLHRPLMIQTLSQYIFLHSCLLNKIL 1411
Cdd:cd14555  157 DIMLDMAEREGVVDIYNCVKELRSRRVNMVQTEEQYIFIHDAILEACL 204
PTPc-N6 cd14606
catalytic domain of tyrosine-protein phosphatase non-receptor type 6; Tyrosine-protein ...
 1158-1410 8.84e-53

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: 186.62  E-value: 8.84e-53
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2499757  1158 KEVGKDQPRLEAEHPDNIIKNRYPHVLPYDHSRVRLT-QLPGEPHSDYINANFI------PGySHTQEIIATQGPLKKTL 1230
Cdd:cd14606    2 QEVKNLHQRLEGQRPENKSKNRYKNILPFDHSRVILQgRDSNIPGSDYINANYVknqllgPD-ENAKTYIASQGCLEATV 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2499757  1231 EDFWRLVWEQQVHVIIMLTVGMENGRVLCEHYWPANSTPVTHGHITIHLLAEEPEDEWTRREFQLQ--HGTEqKQRRVKQ 1308
Cdd:cd14606   81 NDFWQMAWQENSRVIVMTTREVEKGRNKCVPYWPEVGMQRAYGPYSVTNCGEHDTTEYKLRTLQVSplDNGE-LIREIWH 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2499757  1309 LQFTTWPDHSVPEAPSSLLAFVELVQEQVQATQGKGPILVHCSAGVGRTGTFVALLRLLRQLEEEKV---ADVFNTVYIL 1385
Cdd:cd14606  160 YQYLSWPDHGVPSEPGGVLSFLDQINQRQESLPHAGPIIVHCSAGIGRTGTIIVIDMLMENISTKGLdcdIDIQKTIQMV 239

                        250       260
                 ....*....|....*....|....*
gi 2499757  1386 RLHRPLMIQTLSQYIFLHSCLLNKI 1410
Cdd:cd14606  240 RAQRSGMVQTEAQYKFIYVAIAQFI 264
PTPc-N1_2 cd14545
catalytic domain of tyrosine-protein phosphatase non-receptor type 1 and type 2; ...
 1177-1401 1.58e-52

catalytic domain of tyrosine-protein phosphatase non-receptor type 1 and type 2; Tyrosine-protein phosphatase non-receptor type 1 (PTPN1) type 2 (PTPN2) belong to the family of classical tyrosine-specific protein tyrosine phosphatases, (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. PTPN1 (or PTP-1B) is the first PTP to be purified and characterized and is the prototypical intracellular PTP found in a wide variety of human tissues. It dephosphorylates and regulates the activity of a number of receptor tyrosine kinases, including the insulin receptor, the EGF receptor, and the PDGF receptor. PTPN2 (or TCPTP), a tumor suppressor, dephosphorylates and inactivates EGFRs, Src family kinases, Janus-activated kinases (JAKs)-1 and -3, and signal transducer and activators of transcription (STATs)-1, -3 and -5, in a cell type and context-dependent manner.


Pssm-ID: 350393 [Multi-domain]  Cd Length: 231  Bit Score: 184.52  E-value: 1.58e-52
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2499757  1177 KNRYPHVLPYDHSRVRLTQLPGEphSDYINANFIPGYSHTQEIIATQGPLKKTLEDFWRLVWEQQVHVIIMLTVGMENGR 1256
Cdd:cd14545    1 LNRYRDRDPYDHDRSRVKLKQGD--NDYINASLVEVEEAKRSYILTQGPLPNTSGHFWQMVWEQNSKAVIMLNKLMEKGQ 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2499757  1257 VLCEHYWPANSTP---VTHGHITIHLLAEEPEDEWTRREFQLQHGTEQKQRRVKQLQFTTWPDHSVPEAPSSLLAFVELV 1333
Cdd:cd14545   79 IKCAQYWPQGEGNamiFEDTGLKVTLLSEEDKSYYTVRTLELENLKTQETREVLHFHYTTWPDFGVPESPAAFLNFLQKV 158

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2499757  1334 QEQVQATQGKGPILVHCSAGVGRTGTFVALLRLLRQLEEEKVA--DVFNTVYILRLHRPLMIQTLSQYIF 1401
Cdd:cd14545  159 RESGSLSSDVGPPVVHCSAGIGRSGTFCLVDTCLVLIEKGNPSsvDVKKVLLEMRKYRMGLIQTPDQLRF 228
R-PTPc-U-1 cd14632
catalytic domain of receptor-type tyrosine-protein phosphatase U, repeat 1; Receptor-type ...
 1204-1411 4.44e-52

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: 182.17  E-value: 4.44e-52
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2499757  1204 YINANFIPGYSHTQEIIATQGPLKKTLEDFWRLVWEQQVHVIIMLTVGMENGRVLCEHYWPANSTpvTHGHITIHLLAEE 1283
Cdd:cd14632    1 YINANYIDGYHRSNHFIATQGPKQEMVYDFWRMVWQEHCSSIVMITKLVEVGRVKCSKYWPDDSD--TYGDIKITLLKTE 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2499757  1284 PEDEWTRREFQLQHGTEQKQRRVKQLQFTTWPDHSVPEAPSSLLAFVELVQEQVQATqgKGPILVHCSAGVGRTGTFVAL 1363
Cdd:cd14632   79 TLAEYSVRTFALERRGYSARHEVKQFHFTSWPEHGVPYHATGLLAFIRRVKASTPPD--AGPVVVHCSAGAGRTGCYIVL 156

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*...
gi 2499757  1364 LRLLRQLEEEKVADVFNTVYILRLHRPLMIQTLSQYIFLHSCLLNKIL 1411
Cdd:cd14632  157 DVMLDMAECEGVVDIYNCVKTLCSRRINMIQTEEQYIFIHDAILEACL 204
R-PTPc-C-1 cd14557
catalytic domain of receptor-type tyrosine-protein phosphatase C, repeat 1; Receptor-type ...
 1204-1403 9.52e-52

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: 181.18  E-value: 9.52e-52
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2499757  1204 YINANFIPGYSHTQEIIATQGPLKKTLEDFWRLVWEQQVHVIIMLTVGMENGRVLCEHYWPA-NSTPVTHGHITIHLLAE 1282
Cdd:cd14557    1 YINASYIDGFKEPRKYIAAQGPKDETVDDFWRMIWEQKSTVIVMVTRCEEGNRNKCAQYWPSmEEGSRAFGDVVVKINEE 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2499757  1283 EPEDEWTRREFQLQHGTEQ-KQRRVKQLQFTTWPDHSVPEAPSSLLAfvelVQEQVQATQG--KGPILVHCSAGVGRTGT 1359
Cdd:cd14557   81 KICPDYIIRKLNINNKKEKgSGREVTHIQFTSWPDHGVPEDPHLLLK----LRRRVNAFNNffSGPIVVHCSAGVGRTGT 156

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....
gi 2499757  1360 FVALLRLLRQLEEEKVADVFNTVYILRLHRPLMIQTLSQYIFLH 1403
Cdd:cd14557  157 YIGIDAMLEGLEAEGRVDVYGYVVKLRRQRCLMVQVEAQYILIH 200
R-PTPc-R cd14611
catalytic domain of receptor-type tyrosine-protein phosphatase R; Receptor-type ...
 1177-1403 1.68e-51

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: 181.65  E-value: 1.68e-51
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2499757  1177 KNRYPHVLPYDHSRVRL-TQLPGEPHSDYINANFIPGYSHTQEI-IATQGPLKKTLEDFWRLVWEQQVHVIIMLTVGMEN 1254
Cdd:cd14611    2 KNRYKTILPNPHSRVCLkPKNSNDSLSTYINANYIRGYGGKEKAfIATQGPMINTVNDFWQMVWQEDSPVIVMITKLKEK 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2499757  1255 GRVlCEHYWPANSTpvTHGHITIHLLAEEPEDEWTRREFQLQHGTeqKQRRVKQLQFTTWPDHSVPEAPSSLLAFVELVQ 1334
Cdd:cd14611   82 NEK-CVLYWPEKRG--IYGKVEVLVNSVKECDNYTIRNLTLKQGS--QSRSVKHYWYTSWPDHKTPDSAQPLLQLMLDVE 156

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2499757  1335 EQVQATQGKGPILVHCSAGVGRTGTFVALLRLLRQLEEEKVADVFNTVYILRLHRPLMIQTLSQYIFLH 1403
Cdd:cd14611  157 EDRLASPGRGPVVVHCSAGIGRTGCFIATTIGCQQLKEEGVVDVLSIVCQLRVDRGGMVQTSEQYEFVH 225
PTPc-N22_18_12 cd14542
catalytic domain of tyrosine-protein phosphatase non-receptor type 22, type 18 and type 12; ...
 1204-1403 1.46e-50

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: 178.00  E-value: 1.46e-50
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2499757  1204 YINANFIPGYSHTQEIIATQGPLKKTLEDFWRLVWEQQVHVIIMLTVGMENGRVLCEHYWPANSTPV-THGHITIHLLAE 1282
Cdd:cd14542    1 YINANFIKGVSGSKAYIATQGPLPNTVLDFWRMIWEYNVQVIVMACREFEMGKKKCERYWPEEGEEQlQFGPFKISLEKE 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2499757  1283 EPE-DEWTRREFQLQHGTEqkQRRVKQLQFTTWPDHSVPEAPSSLLAFVELVQEqvqaTQGKG--PILVHCSAGVGRTGT 1359
Cdd:cd14542   81 KRVgPDFLIRTLKVTFQKE--SRTVYQFHYTAWPDHGVPSSVDPILDLVRLVRD----YQGSEdvPICVHCSAGCGRTGT 154

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*..
gi 2499757  1360 FVALLRLLRQLEEEKVAD---VFNTVYILRLHRPLMIQTLSQYIFLH 1403
Cdd:cd14542  155 ICAIDYVWNLLKTGKIPEefsLFDLVREMRKQRPAMVQTKEQYELVY 201
PTPc-N22 cd14602
catalytic domain of tyrosine-protein phosphatase non-receptor type 22; Tyrosine-protein ...
 1177-1408 1.88e-50

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: 178.88  E-value: 1.88e-50
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2499757  1177 KNRYPHVLPYDHSRVRLTQLPGEPHSDYINANFIPGYSHTQEIIATQGPLKKTLEDFWRLVWEQQVHVIIMLTVGMENGR 1256
Cdd:cd14602    1 KNRYKDILPYDHSRVELSLITSDEDSDYINANFIKGVYGPRAYIATQGPLSTTLLDFWRMIWEYSVLIIVMACMEFEMGK 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2499757  1257 VLCEHYWP-ANSTPVTHGHITIHLLAEEPEDEWTRREFQLQHGTEqkQRRVKQLQFTTWPDHSVpeaPSSLLAFVELVQE 1335
Cdd:cd14602   81 KKCERYWAePGEMQLEFGPFSVTCEAEKRKSDYIIRTLKVKFNSE--TRTIYQFHYKNWPDHDV---PSSIDPILELIWD 155

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2499757  1336 --QVQATQGKgPILVHCSAGVGRTGTFVALLRLLRQLEEEKVAD---VFNTVYILRLHRPLMIQTLSQYIFLHSCLLN 1408
Cdd:cd14602  156 vrCYQEDDSV-PICIHCSAGCGRTGVICAIDYTWMLLKDGIIPEnfsVFSLIQEMRTQRPSLVQTKEQYELVYNAVIE 232
PTPc-N13 cd14597
catalytic domain of tyrosine-protein phosphatase non-receptor type 13; Tyrosine-protein ...
 1173-1407 4.55e-50

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: 177.71  E-value: 4.55e-50
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2499757  1173 DNIIKNRYPHVLPYDHSRVRLtqlpGEPHsDYINANFI--PGYSHTQEIIATQGPLKKTLEDFWRLVWEQQVHVIIMLTV 1250
Cdd:cd14597    2 ENRKKNRYKNILPYDTTRVPL----GDEG-GYINASFIkmPVGDEEFVYIACQGPLPTTVADFWQMVWEQKSTVIAMMTQ 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2499757  1251 GMENGRVLCEHYWP--ANSTPVTHGHITIHLLAEEPEDEWTRREFQLQHGTEQKQRRVKQLQFTTWPDHSVPEAPSSLLA 1328
Cdd:cd14597   77 EVEGGKIKCQRYWPeiLGKTTMVDNRLQLTLVRMQQLKNFVIRVLELEDIQTREVRHITHLNFTAWPDHDTPSQPEQLLT 156

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2499757  1329 FVELVQEQVQAtqgkGPILVHCSAGVGRTGTFVALLRLLRQLEEEKVADVFNTVYILRLHRPLMIQTLSQYIFLHSCLL 1407
Cdd:cd14597  157 FISYMRHIHKS----GPIITHCSAGIGRSGTLICIDVVLGLISKDLDFDISDIVRTMRLQRHGMVQTEDQYIFCYQVIL 231
PTPc-N1 cd14608
catalytic domain of tyrosine-protein phosphatase non-receptor type 1; Tyrosine-protein ...
 1154-1401 2.64e-49

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: 177.14  E-value: 2.64e-49
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2499757  1154 FEELKEVGKDQPRLEAEHPDNIIKNRYPHVLPYDHSRVRLTQlpgePHSDYINANFIPGYSHTQEIIATQGPLKKTLEDF 1233
Cdd:cd14608    5 YQDIRHEASDFPCRVAKLPKNKNRNRYRDVSPFDHSRIKLHQ----EDNDYINASLIKMEEAQRSYILTQGPLPNTCGHF 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2499757  1234 WRLVWEQQVHVIIMLTVGMENGRVLCEHYWPA---NSTPVTHGHITIHLLAEEPEDEWTRREFQLQHGTEQKQRRVKQLQ 1310
Cdd:cd14608   81 WEMVWEQKSRGVVMLNRVMEKGSLKCAQYWPQkeeKEMIFEDTNLKLTLISEDIKSYYTVRQLELENLTTQETREILHFH 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2499757  1311 FTTWPDHSVPEAPSSLLAFVELVQEQVQATQGKGPILVHCSAGVGRTGTFVALLRLLRQLEEEK---VADVFNTVYILRL 1387
Cdd:cd14608  161 YTTWPDFGVPESPASFLNFLFKVRESGSLSPEHGPVVVHCSAGIGRSGTFCLADTCLLLMDKRKdpsSVDIKKVLLEMRK 240

                        250
                 ....*....|....
gi 2499757  1388 HRPLMIQTLSQYIF 1401
Cdd:cd14608  241 FRMGLIQTADQLRF 254
R-PTPc-Z-1 cd17668
catalytic domain of receptor-type tyrosine-protein phosphatase Z, repeat 1; Receptor-type ...
 1204-1407 1.84e-48

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: 172.09  E-value: 1.84e-48
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2499757  1204 YINANFIPGYSHTQEIIATQGPLKKTLEDFWRLVWEQQVHVIIMLTVGMENGRVLCEHYWPANSTP------VTHGhiTI 1277
Cdd:cd17668    1 YINANYVDGYNKPKAYIAAQGPLKSTAEDFWRMIWEHNVEVIVMITNLVEKGRRKCDQYWPADGSEeygnflVTQK--SV 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2499757  1278 HLLAEEPEDEWTRREFQLQHGTE---QKQRRVKQLQFTTWPDHSVPEAPSSLLAFVElvQEQVQATQGKGPILVHCSAGV 1354
Cdd:cd17668   79 QVLAYYTVRNFTLRNTKIKKGSQkgrPSGRVVTQYHYTQWPDMGVPEYTLPVLTFVR--KASYAKRHAVGPVVVHCSAGV 156

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|...
gi 2499757  1355 GRTGTFVALLRLLRQLEEEKVADVFNTVYILRLHRPLMIQTLSQYIFLHSCLL 1407
Cdd:cd17668  157 GRTGTYIVLDSMLQQIQHEGTVNIFGFLKHIRSQRNYLVQTEEQYVFIHDALV 209
PTP-N23 cd14539
PTP-like domain of tyrosine-protein phosphatase non-receptor type 23; Tyrosine-protein ...
 1204-1403 4.09e-48

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: 171.03  E-value: 4.09e-48
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2499757  1204 YINANFIPGYSHT-QEIIATQGPLKKTLEDFWRLVWEQQVHVIIMLTVGMENGRVLCEHYWPAN-STPVTHGHITIHLLA 1281
Cdd:cd14539    1 YINASLIEDLTPYcPRFIATQAPLPGTAADFWLMVYEQQVSVIVMLVSEQENEKQKVHRYWPTErGQALVYGAITVSLQS 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2499757  1282 EEPEDEWTRREFQLQHGTEQKQRRVKQLQFTTWPDHSVPEAPSSLLAFVELVQEQVQATQG-KGPILVHCSAGVGRTGTF 1360
Cdd:cd14539   81 VRTTPTHVERIISIQHKDTRLSRSVVHLQFTTWPELGLPDSPNPLLRFIEEVHSHYLQQRSlQTPIVVHCSSGVGRTGAF 160

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....
gi 2499757  1361 -VALLRLLRQLEEEKVADVFNTVYILRLHRPLMIQTLSQYIFLH 1403
Cdd:cd14539  161 cLLYAAVQEIEAGNGIPDLPQLVRKMRQQRKYMLQEKEHLKFCY 204
PTPc-N21_14 cd14540
catalytic domain of tyrosine-protein phosphatase non-receptor type 21 and type 14; ...
 1204-1407 1.03e-46

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: 167.63  E-value: 1.03e-46
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2499757  1204 YINANFIPGYSHTQEI--IATQGPLKKTLEDFWRLVWEQQVHVIIMLTVGMENGRVLCEHYWPA---NSTPVTHGHITIH 1278
Cdd:cd14540    1 YINASHITATVGGKQRfyIAAQGPLQNTVGDFWQMVWEQGVYLVVMVTAEEEGGREKCFRYWPTlggEHDALTFGEYKVS 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2499757  1279 LLAEEPEDEWTRREFQLQHGTEQKQRRVKQLQFTTWPDHSVPEAPSSLLAFVELVQE------QVQATQGKG-PILVHCS 1351
Cdd:cd14540   81 TKFSVSSGCYTTTGLRVKHTLSGQSRTVWHLQYTDWPDHGCPEDVSGFLDFLEEINSvrrhtnQDVAGHNRNpPTLVHCS 160

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 2499757  1352 AGVGRTGTFVALLRLLRQLEEEKVADVFNTVYILRLHRPLMIQTLSQYIFLHSCLL 1407
Cdd:cd14540  161 AGVGRTGVVILADLMLYCLDHNEELDIPRVLALLRHQRMLLVQTLAQYKFVYNVLI 216
PTPc-N4 cd14601
catalytic domain of tyrosine-protein phosphatase non-receptor type 4; Tyrosine-protein ...
 1203-1407 2.64e-46

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


Pssm-ID: 350449 [Multi-domain]  Cd Length: 212  Bit Score: 165.89  E-value: 2.64e-46
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2499757  1203 DYINANFI----PGYSHTQEIIATQGPLKKTLEDFWRLVWEQQVHVIIMLTVGMENGRVLCEHYWPANSTPVTHGHITIH 1278
Cdd:cd14601    1 DYINANYInmeiPSSSIINRYIACQGPLPNTCSDFWQMTWEQGSSMVVMLTTQVERGRVKCHQYWPEPSGSSSYGGFQVT 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2499757  1279 LLAEEPEDEWTRREFQLQHGTEQKQRRVKQLQFTTWPDHSVPEAPSSLLAFVELVQEqvQATQGKGPILVHCSAGVGRTG 1358
Cdd:cd14601   81 CHSEEGNPAYVFREMTLTNLEKNESRPLTQIQYIAWPDHGVPDDSSDFLDFVCLVRN--KRAGKDEPVVVHCSAGIGRTG 158

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*....
gi 2499757  1359 TFVALLRLLRQLEEEKVADVFNTVYILRLHRPLMIQTLSQYIFLHSCLL 1407
Cdd:cd14601  159 VLITMETAMCLIECNQPVYPLDIVRTMRDQRAMMIQTPSQYRFVCEAIL 207
R-PTPc-A-E-1 cd14551
catalytic domain of receptor-type tyrosine-protein phosphatase A and E, repeat 1; ...
 1204-1403 4.12e-46

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: 165.09  E-value: 4.12e-46
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2499757  1204 YINANFIPGYSHTQEIIATQGPLKKTLEDFWRLVWEQQVHVIIMLTVGMENGRVLCEHYWPaNSTPVTHGHITIHLlaee 1283
Cdd:cd14551    1 YINASYIDGYQEKNKFIAAQGPKDETVNDFWRMIWEQGSATIVMVTNLKERKEKKCSQYWP-DQGCWTYGNLRVRV---- 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2499757  1284 pED-----EWTRREFQLQH----GTEQKQRRVKQLQFTTWPDHSVPEAPSSLLAFVELVQEQVqaTQGKGPILVHCSAGV 1354
Cdd:cd14551   76 -EDtvvlvDYTTRKFCIQKvnrgIGEKRVRLVTQFHFTSWPDFGVPFTPIGMLKFLKKVKSAN--PPRAGPIVVHCSAGV 152

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*....
gi 2499757  1355 GRTGTFVALLRLLRQLEEEKVADVFNTVYILRLHRPLMIQTLSQYIFLH 1403
Cdd:cd14551  153 GRTGTFIVIDAMLDMMHAEGKVDVFGFVSRIRQQRSQMVQTDMQYVFIY 201
PTPc-N2 cd14607
catalytic domain of tyrosine-protein phosphatase non-receptor type 2; Tyrosine-protein ...
 1156-1360 5.10e-46

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: 167.07  E-value: 5.10e-46
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2499757  1156 ELKEVGKDQPRLEAEHPDNIIKNRYPHVLPYDHSRVRLTQLpgepHSDYINANFIPGYSHTQEIIATQGPLKKTLEDFWR 1235
Cdd:cd14607    6 EIRNESHDYPHRVAKYPENRNRNRYRDVSPYDHSRVKLQNT----ENDYINASLVVIEEAQRSYILTQGPLPNTCCHFWL 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2499757  1236 LVWEQQVHVIIMLTVGMENGRVLCEHYWPANSTPV---THGHITIHLLAEEPEDEWTRREFQLQHGTEQKQRRVKQLQFT 1312
Cdd:cd14607   82 MVWQQKTKAVVMLNRIVEKDSVKCAQYWPTDEEEVlsfKETGFSVKLLSEDVKSYYTVHLLQLENINSGETRTISHFHYT 161

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*...
gi 2499757  1313 TWPDHSVPEAPSSLLAFVELVQEQVQATQGKGPILVHCSAGVGRTGTF 1360
Cdd:cd14607  162 TWPDFGVPESPASFLNFLFKVRESGSLSPEHGPAVVHCSAGIGRSGTF 209
R-PTP-N2 cd14610
PTP-like domain of receptor-type tyrosine-protein phosphatase N2; Receptor-type ...
 1169-1401 2.40e-44

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: 162.92  E-value: 2.40e-44
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2499757  1169 AEHPDNIIKNRYPHVLPYDHSRVRLTQLPGEPHSDYINANFI-------PGYshtqeiIATQGPLKKTLEDFWRLVWEQQ 1241
Cdd:cd14610   39 AQREENVQKNRSLAVLPYDHSRIILKAENSHSHSDYINASPImdhdprnPAY------IATQGPLPATVADFWQMVWESG 112

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2499757  1242 VHVIIMLTVGMENGRVLCEHYWPANSTPVTHGHiTIHLLAEEPE-DEWTRREFQLQHGTEQKQRRVKQLQFTTWPDHSVP 1320
Cdd:cd14610  113 CVVIVMLTPLAENGVKQCYHYWPDEGSNLYHIY-EVNLVSEHIWcEDFLVRSFYLKNLQTNETRTVTQFHFLSWNDQGVP 191

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2499757  1321 EAPSSLLAFVELVQeqvQATQGKG-PILVHCSAGVGRTGTFV-ALLRLLRQLEEEKVADVFNTVYILRLHRPLMIQTLSQ 1398
Cdd:cd14610  192 ASTRSLLDFRRKVN---KCYRGRScPIIVHCSDGAGRSGTYIlIDMVLNKMAKGAKEIDIAATLEHLRDQRPGMVQTKEQ 268


                 ...
gi 2499757  1399 YIF 1401
Cdd:cd14610  269 FEF 271
PTP_tm pfam18861
TM proximal of protein tyrosine phosphatase, receptor type J; Protein tyrosine phosphatases ...
 950-1069 2.47e-43

TM proximal of protein tyrosine phosphatase, receptor type J; Protein tyrosine phosphatases (PTPs) are known to be signaling molecules that regulate a variety of cellular processes, including cell growth, differentiation, mitotic cycle, and oncogenic transformation. PTP receptor type J possesses an extracellular region containing five fibronectin type III repeats, the transmembrane region included in this Pfam entry, and a intracytoplasmic catalytic domain. This entry probably contains part of a Fn3 domain at the N-terminus.


Pssm-ID: 465889  Cd Length: 126  Bit Score: 153.92  E-value: 2.47e-43
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2499757     950 RGMFGKDDGQIQWYGIIATINMTLAQPSREAINYTWYDHYYRGCESFLALLFPNPFYPePWAGPRSWTVPVGTEDCdnTQ 1029
Cdd:pfam18861    3 FSLFNSSNGPIKAYGVIVTTNDSLNRPLKEYLNKTYYDWKYKKTDSYLATVTPNPFTS-PRSSSRSLTVPVGTGSK--WQ 79

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*..
gi 2499757    1030 EICNGRLKSGFQYRFSVVAFSRL-------NTPETILAFSAFSEPRA 1069
Cdd:pfam18861   80 GYCNGPLKPLGSYRFSVAAFTRLefddgliDGEESYVSFTPFSEPIA 126
PTPc-N14 cd14599
catalytic domain of tyrosine-protein phosphatase non-receptor type 14; Tyrosine-protein ...
 1151-1407 3.20e-43

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: 159.78  E-value: 3.20e-43
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2499757  1151 FQEFEELKEVGKDQPRLEAEHPDNIIKNRYPHVLPYDHSRVRLTQLPgEPHSDYINANFIPGYSHTQE--IIATQGPLKK 1228
Cdd:cd14599   15 FTEYEQIPKKKADGVFTTATLPENAERNRIREVVPYEENRVELVPTK-ENNTGYINASHIKVTVGGEEwhYIATQGPLPH 93

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2499757  1229 TLEDFWRLVWEQQVHVIIMLTVGMENGRVLCEHYWP---ANSTPVTHGHITIHLLAEEPEDEWTRREFQLQHGTEQKQRR 1305
Cdd:cd14599   94 TCHDFWQMVWEQGVNVIAMVTAEEEGGRSKSHRYWPklgSKHSSATYGKFKVTTKFRTDSGCYATTGLKVKHLLSGQERT 173

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2499757  1306 VKQLQFTTWPDHSVPEAPSSLLAFVELVQEQVQATQG--------KGPILVHCSAGVGRTGTFVALLRLLRQLEEEKVAD 1377
Cdd:cd14599  174 VWHLQYTDWPDHGCPEEVQGFLSYLEEIQSVRRHTNSmldstkncNPPIVVHCSAGVGRTGVVILTELMIGCLEHNEKVE 253

                        250       260       270
                 ....*....|....*....|....*....|
gi 2499757  1378 VFNTVYILRLHRPLMIQTLSQYIFLHSCLL 1407
Cdd:cd14599  254 VPVMLRHLREQRMFMIQTIAQYKFVYQVLI 283
R-PTP-N cd14609
PTP-like domain of receptor-type tyrosine-protein phosphatase N; Receptor-type ...
 1169-1401 2.24e-42

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: 157.12  E-value: 2.24e-42
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2499757  1169 AEHPDNIIKNRYPHVLPYDHSRVRLTQLPGEPHSDYINANFI-------PGYshtqeiIATQGPLKKTLEDFWRLVWEQQ 1241
Cdd:cd14609   37 AQGEANVKKNRNPDFVPYDHARIKLKAESNPSRSDYINASPIiehdprmPAY------IATQGPLSHTIADFWQMVWENG 110

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2499757  1242 VHVIIMLTVGMENGRVLCEHYWPANSTPVTHGHiTIHLLAEEPE-DEWTRREFQLQHGTEQKQRRVKQLQFTTWPDHSVP 1320
Cdd:cd14609  111 CTVIVMLTPLVEDGVKQCDRYWPDEGSSLYHIY-EVNLVSEHIWcEDFLVRSFYLKNVQTQETRTLTQFHFLSWPAEGIP 189

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2499757  1321 EAPSSLLAFVELVQeqvQATQGKG-PILVHCSAGVGRTGTFV-ALLRLLRQLEEEKVADVFNTVYILRLHRPLMIQTLSQ 1398
Cdd:cd14609  190 SSTRPLLDFRRKVN---KCYRGRScPIIVHCSDGAGRTGTYIlIDMVLNRMAKGVKEIDIAATLEHVRDQRPGMVRTKDQ 266


                 ...
gi 2499757  1399 YIF 1401
Cdd:cd14609  267 FEF 269
R-PTPc-typeIIb-2 cd14556
PTP domain of type IIb (or R2B) subfamily receptor-type tyrosine-protein phosphatases, repeat ...
 1204-1403 5.87e-42

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: 152.95  E-value: 5.87e-42
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2499757  1204 YINANFIPGYSHTQEIIATQGPLKKTLEDFWRLVWEQQVHVIIMLTvGMENGRVLCEHYWPANSTPvTHGHITIHLLAEE 1283
Cdd:cd14556    1 YINAALLDSYKQPAAFIVTQHPLPNTVTDFWRLVYDYGCTSIVMLN-QLDPKDQSCPQYWPDEGSG-TYGPIQVEFVSTT 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2499757  1284 PEDEWTRREFQLQHGT--EQKQRRVKQLQFTTWPDH-SVPEAPSSLLAFVELVqEQVQATQGKGPILVHCSAGVGRTGTF 1360
Cdd:cd14556   79 IDEDVISRIFRLQNTTrpQEGYRMVQQFQFLGWPRDrDTPPSKRALLKLLSEV-EKWQEQSGEGPIVVHCLNGVGRSGVF 157

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|...
gi 2499757  1361 VALLRLLRQLEEEKVADVFNTVYILRLHRPLMIQTLSQYIFLH 1403
Cdd:cd14556  158 CAISSVCERIKVENVVDVFQAVKTLRNHRPNMVETEEQYKFCY 200
PTPc-N20 cd14596
catalytic domain of tyrosine-protein phosphatase non-receptor type 20; Tyrosine-protein ...
 1204-1407 7.91e-41

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: 150.28  E-value: 7.91e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2499757  1204 YINANFI--PGYSHTQEIIATQGPLKKTLEDFWRLVWEQQVHVIIMLTVGMENGRVLCEHYWPAN-STPVTHGHITIHLL 1280
Cdd:cd14596    1 YINASYItmPVGEEELFYIATQGPLPSTIDDFWQMVWENRSDVIAMMTREVERGKVKCHRYWPETlQEPMELENYQLRLE 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2499757  1281 AEEPEDEWTRREFQLQHGTEQKQRRVKQLQFTTWPDHSVPEAPSSLLAFVELvqeqVQATQGKGPILVHCSAGVGRTGTF 1360
Cdd:cd14596   81 NYQALQYFIIRIIKLVEKETGENRLIKHLQFTTWPDHGTPQSSDQLVKFICY----MRKVHNTGPIVVHCSAGIGRAGVL 156

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*..
gi 2499757  1361 VALLRLLRQLEEEKVADVFNTVYILRLHRPLMIQTLSQYIFLHSCLL 1407
Cdd:cd14596  157 ICVDVLLSLIEKDLSFNIKDIVREMRQQRYGMIQTKDQYLFCYKVVL 203
PHA02738 PHA02738
hypothetical protein; Provisional
 1153-1401 1.77e-40

hypothetical protein; Provisional


Pssm-ID: 222923 [Multi-domain]  Cd Length: 320  Bit Score: 153.16  E-value: 1.77e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2499757   1153 EFEELkeVGKDQPRLEAEHPD--------NIIKNRYPHVLPYDHSRVrltQLPGEPH-SDYINANFIPGYSHTQEIIATQ 1223
Cdd:PHA02738   22 DCEEV--ITREHQKVISEKVDgtfnaekkNRKLNRYLDAVCFDHSRV---ILPAERNrGDYINANYVDGFEYKKKFICGQ 96

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2499757   1224 GPLKKTLEDFWRLVWEQQVHVIIMLTVGMENGRVLCEHYWP-ANSTPVTHGHITIHLLAEEPEDEWTRREFQLQHGTEQK 1302
Cdd:PHA02738   97 APTRQTCYDFYRMLWMEHVQIIVMLCKKKENGREKCFPYWSdVEQGSIRFGKFKITTTQVETHPHYVKSTLLLTDGTSAT 176

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2499757   1303 QrRVKQLQFTTWPDHSVPEAPSSLLAFV--------ELVQEQVQATQGKG---PILVHCSAGVGRTGTFVALLRLLRQLE 1371
Cdd:PHA02738  177 Q-TVTHFNFTAWPDHDVPKNTSEFLNFVlevrqcqkELAQESLQIGHNRLqppPIVVHCNAGLGRTPCYCVVDISISRFD 255

                         250       260       270
                  ....*....|....*....|....*....|
gi 2499757   1372 EEKVADVFNTVYILRLHRPLMIQTLSQYIF 1401
Cdd:PHA02738  256 ACATVSIPSIVSSIRNQRYYSLFIPFQYFF 285
R-PTP-N-N2 cd14546
PTP-like domain of receptor-type tyrosine-protein phosphatase-like N and N2; Receptor-type ...
 1204-1405 3.09e-39

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: 145.66  E-value: 3.09e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2499757  1204 YINANFI-------PGYshtqeiIATQGPLKKTLEDFWRLVWEQQVHVIIMLTVGMENGRVLCEHYWPANSTPVtHGHIT 1276
Cdd:cd14546    1 YINASTIydhdprnPAY------IATQGPLPHTIADFWQMIWEQGCVVIVMLTRLQENGVKQCARYWPEEGSEV-YHIYE 73

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2499757  1277 IHLLAEEP-EDEWTRREFQLQHGTEQKQRRVKQLQFTTWPDHSVPEAPSSLLAFVELVQeqvQATQGKG-PILVHCSAGV 1354
Cdd:cd14546   74 VHLVSEHIwCDDYLVRSFYLKNLQTSETRTVTQFHFLSWPDEGIPASAKPLLEFRRKVN---KSYRGRScPIVVHCSDGA 150

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|..
gi 2499757  1355 GRTGTFVAL-LRLLRQLEEEKVADVFNTVYILRLHRPLMIQTLSQYIFLHSC 1405
Cdd:cd14546  151 GRTGTYILIdMVLNRMAKGAKEIDIAATLEHLRDQRPGMVKTKDQFEFVLTA 202
PTPc-N21 cd14598
catalytic domain of tyrosine-protein phosphatase non-receptor type 21; Tyrosine-protein ...
 1204-1407 7.84e-39

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: 144.73  E-value: 7.84e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2499757  1204 YINANFIPGYSHTQE--IIATQGPLKKTLEDFWRLVWEQQVHVIIMLTVGMENGRVLCEHYWP---ANSTPVTHGHITIH 1278
Cdd:cd14598    1 YINASHIKVTVGGKEwdYIATQGPLQNTCQDFWQMVWEQGVAIIAMVTAEEEGGREKSFRYWPrlgSRHNTVTYGRFKIT 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2499757  1279 LLAEEPEDEWTRREFQLQHGTEQKQRRVKQLQFTTWPDHSVPEAPSSLLAFVELVQEQVQATQGKG-------PILVHCS 1351
Cdd:cd14598   81 TRFRTDSGCYATTGLKIKHLLTGQERTVWHLQYTDWPEHGCPEDLKGFLSYLEEIQSVRRHTNSTIdpkspnpPVLVHCS 160

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 2499757  1352 AGVGRTGTFVALLRLLRQLEEEKVADVFNTVYILRLHRPLMIQTLSQYIFLHSCLL 1407
Cdd:cd14598  161 AGVGRTGVVILSEIMIACLEHNEMLDIPRVLDMLRQQRMMMVQTLSQYTFVYKVLI 216
PHA02747 PHA02747
protein tyrosine phosphatase; Provisional
 1147-1403 7.84e-38

protein tyrosine phosphatase; Provisional


Pssm-ID: 165114 [Multi-domain]  Cd Length: 312  Bit Score: 145.14  E-value: 7.84e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2499757   1147 HQTFFQEFEELKEvgkdqprlEAEHPDNIIKNRYPHVLPYDHSRVRLTQLPGEPhSDYINANFIPGYSHTQEIIATQGPL 1226
Cdd:PHA02747   32 HQIILKPFDGLIA--------NFEKPENQPKNRYWDIPCWDHNRVILDSGGGST-SDYIHANWIDGFEDDKKFIATQGPF 102

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2499757   1227 KKTLEDFWRLVWEQQVHVIIMLT-VGMENGRVLCEHYW--PANSTPVTHGHItIHLLAEEPEDEWTRREFQLQHGTEQKQ 1303
Cdd:PHA02747  103 AETCADFWKAVWQEHCSIIVMLTpTKGTNGEEKCYQYWclNEDGNIDMEDFR-IETLKTSVRAKYILTLIEITDKILKDS 181

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2499757   1304 RRVKQLQFTTWPdhsVPEAPSSLLAFVELVQ--EQVQATQGK---------GPILVHCSAGVGRTGTFVALLRLLRQLEE 1372
Cdd:PHA02747  182 RKISHFQCSEWF---EDETPSDHPDFIKFIKiiDINRKKSGKlfnpkdallCPIVVHCSDGVGKTGIFCAVDICLNQLVK 258

                         250       260       270
                  ....*....|....*....|....*....|.
gi 2499757   1373 EKVADVFNTVYILRLHRPLMIQTLSQYIFLH 1403
Cdd:PHA02747  259 RKAICLAKTAEKIREQRHAGIMNFDDYLFIQ 289
PTPc_plant_PTP1 cd17658
protein tyrosine phosphatase 1 from Arabidopsis thaliana and similar plant PTPs; Arabidopsis ...
 1204-1404 1.00e-37

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: 141.06  E-value: 1.00e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2499757  1204 YINANFI--PGYSHTQEIIATQGPLKKTLEDFWRLVWEQQVHVIIMLTVGMENGRVL-CEHYWPANS-TPVTHGHITIHL 1279
Cdd:cd17658    1 YINASLVetPASESLPKFIATQGPLPHTFEDFWEMVIQQRCPVIIMLTRLVDNYSTAkCADYFPAEEnESREFGRISVTN 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2499757  1280 LAEEPEDE-WTRREFQLQH-GTEQKQRRVKQLQFTTWPDHSVPEapsSLLAFVELVQEQVQATQGKGPILVHCSAGVGRT 1357
Cdd:cd17658   81 KKLKHSQHsITLRVLEVQYiESEEPPLSVLHIQYPEWPDHGVPK---DTRSVRELLKRLYGIPPSAGPIVVHCSAGIGRT 157

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*....
gi 2499757  1358 GTFVALLRLLRQLEEEKVA--DVFNTVYILRLHRPLMIQTLSQYIFLHS 1404
Cdd:cd17658  158 GAYCTIHNTIRRILEGDMSavDLSKTVRKFRSQRIGMVQTQDQYIFCYA 206
PHA02742 PHA02742
protein tyrosine phosphatase; Provisional
 1174-1407 1.20e-36

protein tyrosine phosphatase; Provisional


Pssm-ID: 165109 [Multi-domain]  Cd Length: 303  Bit Score: 141.29  E-value: 1.20e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2499757   1174 NIIKNRYPHVLPYDHSRVRLTQLPGepHSDYINANFIPGYSHTQEIIATQGPLKKTLEDFWRLVWEQQVHVIIMLTVGME 1253
Cdd:PHA02742   52 NMKKCRYPDAPCFDRNRVILKIEDG--GDDFINASYVDGHNAKGRFICTQAPLEETALDFWQAIFQDQVRVIVMITKIME 129

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2499757   1254 NGRVLCEHYW-PANSTPVTHGHITIHLLAEEPEDEWTRREFQLQHGTEQKQRRVKQLQFTTWPDHSVPEAPSSLLAFVEL 1332
Cdd:PHA02742  130 DGKEACYPYWmPHERGKATHGEFKIKTKKIKSFRNYAVTNLCLTDTNTGASLDIKHFAYEDWPHGGLPRDPNKFLDFVLA 209

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2499757   1333 VQEQVQATQ---------GKGPILVHCSAGVGRTGTFVALLRLLRQLEEEKVADVFNTVYILRLHRPLMIQTLSQYIFLH 1403
Cdd:PHA02742  210 VREADLKADvdikgenivKEPPILVHCSAGLDRAGAFCAIDICISKYNERAIIPLLSIVRDLRKQRHNCLSLPQQYIFCY 289


                  ....
gi 2499757   1404 SCLL 1407
Cdd:PHA02742  290 FIVL 293
COG5599 COG5599
Protein tyrosine phosphatase [Signal transduction mechanisms];
1128-1402 1.34e-35

Protein tyrosine phosphatase [Signal transduction mechanisms];


Pssm-ID: 444335 [Multi-domain]  Cd Length: 282  Bit Score: 137.53  E-value: 1.34e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2499757  1128 RPIPIHSFRQSYEAKSAHahqtffqEFEELKEVGKDqPRLEaEHPDNIIKNRYPHVLPYDHSRVRltqlpgePHSDYINA 1207
Cdd:COG5599    5 NPIAIKSEEEKINSRLST-------LTNELAPSHND-PQYL-QNINGSPLNRFRDIQPYKETALR-------ANLGYLNA 68

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2499757  1208 NFIPGYSHTQEIiATQGPLKKTLEDFWRLVWEQQVHVIIMLT--VGMENGRVLCEHYWPANSTpvtHGHITIHLLAEEPE 1285
Cdd:COG5599   69 NYIQVIGNHRYI-ATQYPLEEQLEDFFQMLFDNNTPVLVVLAsdDEISKPKVKMPVYFRQDGE---YGKYEVSSELTESI 144

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2499757  1286 ---DEWTRREFQL-QHGTEQKQRRVKQLQFTTWPDHSVPEApSSLLAFVELV-QEQVQATQGKGPILVHCSAGVGRTGTF 1360
Cdd:COG5599  145 qlrDGIEARTYVLtIKGTGQKKIEIPVLHVKNWPDHGAISA-EALKNLADLIdKKEKIKDPDKLLPVVHCRAGVGRTGTL 223

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*
gi 2499757  1361 VALLRLLRQLEEEKVADV-FNTVYI-LRLHR-PLMIQTLSQYIFL 1402
Cdd:COG5599  224 IACLALSKSINALVQITLsVEEIVIdMRTSRnGGMVQTSEQLDVL 268
PTPc_DSPc smart00012
Protein tyrosine phosphatase, catalytic domain, undefined specificity; Protein tyrosine ...
 1306-1408 6.38e-34

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


Pssm-ID: 214469 [Multi-domain]  Cd Length: 105  Bit Score: 126.32  E-value: 6.38e-34
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2499757     1306 VKQLQFTTWPDHSVPEAPSSLLAFVELVQEQVQATQGKGPILVHCSAGVGRTGTFVA-LLRLLRQLEEEKVADVFNTVYI 1384
Cdd:smart00012    2 VKHYHYTGWPDHGVPESPDSILELLRAVKKNLNQSESSGPVVVHCSAGVGRTGTFVAiDILLQQLEAEAGEVDIFDTVKE 81

                            90       100
                    ....*....|....*....|....
gi 2499757     1385 LRLHRPLMIQTLSQYIFLHSCLLN 1408
Cdd:smart00012   82 LRSQRPGMVQTEEQYLFLYRALLE 105
PTPc_motif smart00404
Protein tyrosine phosphatase, catalytic domain motif;
1306-1408 6.38e-34

Protein tyrosine phosphatase, catalytic domain motif;


Pssm-ID: 214649 [Multi-domain]  Cd Length: 105  Bit Score: 126.32  E-value: 6.38e-34
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2499757     1306 VKQLQFTTWPDHSVPEAPSSLLAFVELVQEQVQATQGKGPILVHCSAGVGRTGTFVA-LLRLLRQLEEEKVADVFNTVYI 1384
Cdd:smart00404    2 VKHYHYTGWPDHGVPESPDSILELLRAVKKNLNQSESSGPVVVHCSAGVGRTGTFVAiDILLQQLEAEAGEVDIFDTVKE 81

                            90       100
                    ....*....|....*....|....
gi 2499757     1385 LRLHRPLMIQTLSQYIFLHSCLLN 1408
Cdd:smart00404   82 LRSQRPGMVQTEEQYLFLYRALLE 105
PHA02746 PHA02746
protein tyrosine phosphatase; Provisional
 1172-1412 4.27e-33

protein tyrosine phosphatase; Provisional


Pssm-ID: 165113 [Multi-domain]  Cd Length: 323  Bit Score: 131.69  E-value: 4.27e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2499757   1172 PDNIIKNRYPHVLPYDHSRV-------------------RLTQLPGEPHSDYINANFIPGYSHTQEIIATQGPLKKTLED 1232
Cdd:PHA02746   49 KENLKKNRFHDIPCWDHSRVvinaheslkmfdvgdsdgkKIEVTSEDNAENYIHANFVDGFKEANKFICAQGPKEDTSED 128

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2499757   1233 FWRLVWEQQVHVIIMLTvGMENGRVLCEHYW-PANSTPVTHGHITIHLLAEEPEDEWTRREFQLQHGTEQKQRRVKQLQF 1311
Cdd:PHA02746  129 FFKLISEHESQVIVSLT-DIDDDDEKCFELWtKEEDSELAFGRFVAKILDIIEELSFTKTRLMITDKISDTSREIHHFWF 207

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2499757   1312 TTWPDHSVPEAPSSLLAFV--------ELVQEQVQATQGKGPILVHCSAGVGRTGTFVALLRLLRQLEEEKVADVFNTVY 1383
Cdd:PHA02746  208 PDWPDNGIPTGMAEFLELInkvneeqaELIKQADNDPQTLGPIVVHCSAGIGRAGTFCAIDNALEQLEKEKEVCLGEIVL 287

                         250       260
                  ....*....|....*....|....*....
gi 2499757   1384 ILRLHRPLMIQTLSQYIFLHSCLLNKILE 1412
Cdd:PHA02746  288 KIRKQRHSSVFLPEQYAFCYKALKYAIIE 316
R5-PTP-2 cd14550
PTP-like domain of R5 subfamily receptor-type tyrosine-protein phosphatases, repeat 2; The R5 ...
 1204-1402 1.24e-32

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: 126.28  E-value: 1.24e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2499757  1204 YINANFIPGYSHTQEIIATQGPLKKTLEDFWRLVWEQQVHVIIMLTVGMENGRvlCEHYWPANSTPVTHGHITIHLLAEE 1283
Cdd:cd14550    1 YINASYLQGYRRSNEFIITQHPLEHTIKDFWQMIWDHNSQTIVMLTDNELNED--EPIYWPTKEKPLECETFKVTLSGED 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2499757  1284 -----PEDEWTRREFQLQHGTEQKQRRVKQLQFTTWPDHSVPeaPSSLLAFVELVQEQVQatQGKGPILVHCSAGVGRTG 1358
Cdd:cd14550   79 hsclsNEIRLIVRDFILESTQDDYVLEVRQFQCPSWPNPCSP--IHTVFELINTVQEWAQ--QRDGPIVVHDRYGGVQAA 154

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....
gi 2499757  1359 TFVALLRLLRQLEEEKVADVFNTVYILRLHRPLMIQTLSQYIFL 1402
Cdd:cd14550  155 TFCALTTLHQQLEHESSVDVYQVAKLYHLMRPGVFTSKEDYQFL 198
R-PTP-Z-2 cd17669
catalytic domain of receptor-type tyrosine-protein phosphatase Z, repeat 2; Receptor-type ...
 1204-1407 4.78e-29

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: 116.25  E-value: 4.78e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2499757  1204 YINANFIPGYSHTQEIIATQGPLKKTLEDFWRLVWEQQVHVIIMLTvgmeNGRVLCEH---YWPANSTPVTHGHITIHLL 1280
Cdd:cd17669    1 YINASYIMGYYQSNEFIITQHPLLHTIKDFWRMIWDHNAQLIVMLP----DGQNMAEDefvYWPNKDEPINCETFKVTLI 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2499757  1281 AEE-----PEDEWTRREFQLQHGTEQKQRRVKQLQFTTWPDhsvPEAP-SSLLAFVELVQEqvQATQGKGPILVHCSAGV 1354
Cdd:cd17669   77 AEEhkclsNEEKLIIQDFILEATQDDYVLEVRHFQCPKWPN---PDSPiSKTFELISIIKE--EAANRDGPMIVHDEHGG 151

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|...
gi 2499757  1355 GRTGTFVALLRLLRQLEEEKVADVFNTVYILRLHRPLMIQTLSQYIFLHSCLL 1407
Cdd:cd17669  152 VTAGTFCALTTLMHQLEKENSVDVYQVAKMINLMRPGVFTDIEQYQFLYKAIL 204
R-PTPc-T-2 cd14634
PTP domain of receptor-type tyrosine-protein phosphatase T, repeat 2; Receptor-type ...
 1204-1408 2.02e-28

PTP domain of receptor-type tyrosine-protein phosphatase T, repeat 2; Receptor-type tyrosine-protein phosphatase T (PTPRT), also known as receptor-type tyrosine-protein phosphatase rho (RPTP-rho or PTPrho), belongs to the type IIb subfamily of receptor protein tyrosine phosphatases (RPTPs), which belong to the larger family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. PTPRT is highly expressed in the nervous system and it plays a critical role in regulation of synaptic formation and neuronal development. It dephosphorylates a specific tyrosine residue in syntaxin-binding protein 1, a key component of synaptic vesicle fusion machinery, and regulates its binding to syntaxin 1. PTPRT has been identified as a potential candidate gene for autism spectrum disorder (ASD) susceptibility. It contains an extracellular region with an Meprin-A5 (neuropilin)-mu (MAM) domain, an immunoglobulin (Ig) domain, and four fibronectin type III (FN3) repeats, a transmembrane domain, and an intracellular segment with a juxtamembrane domain similar to the cytoplasmic domain of classical cadherins and two tandem PTP domains. This model represents the second (repeat 2) PTP domain.


Pssm-ID: 350482 [Multi-domain]  Cd Length: 206  Bit Score: 114.35  E-value: 2.02e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2499757  1204 YINANFIPGYSHTQEIIATQGPLKKTLEDFWRLVWEQQVHVIIMLTvGMENGRvLCEHYWPANSTpVTHGHITIHLLAEE 1283
Cdd:cd14634    1 YINAALMDSHKQPAAFIVTQHPLPNTVADFWRLVFDYNCSSVVMLN-EMDAAQ-LCMQYWPEKTS-CCYGPIQVEFVSAD 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2499757  1284 PEDEWTRREFQLQHGTEQKQ--RRVKQLQFTTWPDH-SVPEAPSSLLAFVE-LVQEQVQATQGKGPILVHCSAGVGRTGT 1359
Cdd:cd14634   78 IDEDIISRIFRICNMARPQDgyRIVQHLQYIGWPAYrDTPPSKRSILKVVRrLEKWQEQYDGREGRTVVHCLNGGGRSGT 157

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*....
gi 2499757  1360 FVALLRLLRQLEEEKVADVFNTVYILRLHRPLMIQTLSQYIFLHSCLLN 1408
Cdd:cd14634  158 FCAICSVCEMIQQQNIIDVFHTVKTLRNNKSNMVETLEQYKFVYEVALE 206
R-PTPc-M-2 cd14635
PTP domain of receptor-type tyrosine-protein phosphatase M, repeat 2; Receptor-type ...
 1204-1407 9.26e-28

PTP domain of receptor-type tyrosine-protein phosphatase M, repeat 2; Receptor-type tyrosine-protein phosphatase M (PTPRM), also known as protein-tyrosine phosphatase mu (R-PTP-mu or PTPmu), belongs to the type IIb subfamily of receptor protein tyrosine phosphatases (RPTPs), which belong to the larger family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. PTPRM/PTPmu is a homophilic cell adhesion molecule expressed in CNS neurons and glia. It is required for E-, N-, and R-cadherin-dependent neurite outgrowth. Loss of PTPmu contributes to tumor cell migration and dispersal of human glioblastomas. PTPRM contains an extracellular region with an Meprin-A5 (neuropilin)-mu (MAM) domain, an immunoglobulin (Ig) domain, and four fibronectin type III (FN3) repeats, a transmembrane domain, and an intracellular segment with a juxtamembrane domain similar to the cytoplasmic domain of classical cadherins and two tandem PTP domains. This model represents the second (repeat 2) PTP domain.


Pssm-ID: 350483 [Multi-domain]  Cd Length: 206  Bit Score: 112.47  E-value: 9.26e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2499757  1204 YINANFIPGYSHTQEIIATQGPLKKTLEDFWRLVWEQQVHVIIMLTvgMENGRVLCEHYWPANSTPvTHGHITIHLLAEE 1283
Cdd:cd14635    1 YINAALMDSYKQPSAFIVTQHPLPNTVKDFWRLVLDYHCTSIVMLN--DVDPAQLCPQYWPENGVH-RHGPIQVEFVSAD 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2499757  1284 PEDEWTRREFQLQHGTEQKQ--RRVKQLQFTTWPDHSvpEAPSSLLAFVELVQE----QVQATQGKGPILVHCSAGVGRT 1357
Cdd:cd14635   78 LEEDIISRIFRIYNAARPQDgyRMVQQFQFLGWPMYR--DTPVSKRSFLKLIRQvdkwQEEYNGGEGRTVVHCLNGGGRS 155

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|
gi 2499757  1358 GTFVALLRLLRQLEEEKVADVFNTVYILRLHRPLMIQTLSQYIFLHSCLL 1407
Cdd:cd14635  156 GTFCAISIVCEMLRHQRAVDVFHAVKTLRNNKPNMVDLLDQYKFCYEVAL 205
R-PTPc-U-2 cd14637
PTP domain of receptor-type tyrosine-protein phosphatase U, repeat 2; Receptor-type ...
 1204-1407 7.66e-27

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


Pssm-ID: 350485 [Multi-domain]  Cd Length: 207  Bit Score: 110.00  E-value: 7.66e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2499757  1204 YINANFIPGYSHTQEIIATQGPLKKTLEDFWRLVWEQQVHVIIMLT-VGMENGRVLCEHYWPaNSTPVTHGHITIHLLAE 1282
Cdd:cd14637    1 YINAALTDSYTRSAAFIVTLHPLQNTTTDFWRLVYDYGCTSVVMLNqLNQSNSAWPCLQYWP-EPGLQQYGPMEVEFVSG 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2499757  1283 EPEDEWTRREFQLQHGT--EQKQRRVKQLQFTTW-PDHSVPEAPSSLLAFVELVqEQVQATQGKGPILVHCSAGVGRTGT 1359
Cdd:cd14637   80 SADEDIVTRLFRVQNITrlQEGHLMVRHFQFLRWsAYRDTPDSKKAFLHLLASV-EKWQRESGEGRTVVHCLNGGGRSGT 158

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*...
gi 2499757  1360 FVALLRLLRQLEEEKVADVFNTVYILRLHRPLMIQTLSQYIFLHSCLL 1407
Cdd:cd14637  159 YCASAMILEMIRCHNIVDVFYAVKTLRNYKPNMVETLEQYRFCYEIAL 206
R-PTP-G-2 cd17670
PTP-like domain of receptor-type tyrosine-protein phosphatase G, repeat 2; Receptor-type ...
 1204-1408 6.13e-26

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: 107.07  E-value: 6.13e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2499757  1204 YINANFIPGYSHTQEIIATQGPLKKTLEDFWRLVWEQQVHVIIMLTvgmeNGRVLCEH---YWPANSTPVTHGHITIHLL 1280
Cdd:cd17670    1 YINASYIMGYYRSNEFIITQHPLPHTTKDFWRMIWDHNAQIIVMLP----DNQGLAEDefvYWPSREESMNCEAFTVTLI 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2499757  1281 AEE-----PEDEWTRREFQLQHGTEQKQRRVKQLQFTTWPDhsvPEAP-SSLLAFVELVQEqvQATQGKGPILVHCSAGV 1354
Cdd:cd17670   77 SKDrlclsNEEQIIIHDFILEATQDDYVLEVRHFQCPKWPN---PDAPiSSTFELINVIKE--EALTRDGPTIVHDEFGA 151

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....
gi 2499757  1355 GRTGTFVALLRLLRQLEEEKVADVFNTVYILRLHRPLMIQTLSQYIFLHSCLLN 1408
Cdd:cd17670  152 VSAGTLCALTTLSQQLENENAVDVYQVAKMINLMRPGVFTDIEQYQFLYKAMLS 205
R-PTPc-K-2 cd14636
PTP domain of receptor-type tyrosine-protein phosphatase K, repeat 2; Receptor-type ...
 1204-1407 1.18e-25

PTP domain of receptor-type tyrosine-protein phosphatase K, repeat 2; Receptor-type tyrosine-protein phosphatase K (PTPRK), also known as receptor-type tyrosine-protein phosphatase kappa (RPTP-kappa or PTPkappa), belongs to the type IIb subfamily of receptor protein tyrosine phosphatases (RPTPs), which belong to the larger family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. PTPRK is widely expressed and has been shown to stimulate cell motility and neurite outgrowth. It is required for anti-proliferative and pro-migratory effects of TGF-beta, suggesting a role in regulation, maintenance, and restoration of cell adhesion. It is a potential tumour suppressor in primary central nervous system lymphomas, colorectal cancer, and breast cancer. It contains an extracellular region with an Meprin-A5 (neuropilin)-mu (MAM) domain, an immunoglobulin (Ig) domain, and four fibronectin type III (FN3) repeats, a transmembrane domain, and an intracellular segment with a juxtamembrane domain similar to the cytoplasmic domain of classical cadherins and two tandem PTP domains. This model represents the second (repeat 2) PTP domain.


Pssm-ID: 350484 [Multi-domain]  Cd Length: 206  Bit Score: 106.26  E-value: 1.18e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2499757  1204 YINANFIPGYSHTQEIIATQGPLKKTLEDFWRLVWEQQVHVIIMLT-VGMENGrvlCEHYWPANSTpVTHGHITIHLLAE 1282
Cdd:cd14636    1 YINAALMDSYRQPAAFIVTQHPLPNTVKDFWRLVYDYGCTSIVMLNeVDLAQG---CPQYWPEEGM-LRYGPIQVECMSC 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2499757  1283 EPEDEWTRREFQLQHGTEQKQ--RRVKQLQFTTWPDHSvpEAPSSLLAFVELVQE----QVQATQGKGPILVHCSAGVGR 1356
Cdd:cd14636   77 SMDCDVISRIFRICNLTRPQEgyLMVQQFQYLGWASHR--EVPGSKRSFLKLILQvekwQEECDEGEGRTIIHCLNGGGR 154

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|.
gi 2499757  1357 TGTFVALLRLLRQLEEEKVADVFNTVYILRLHRPLMIQTLSQYIFLHSCLL 1407
Cdd:cd14636  155 SGMFCAISIVCEMIKRQNVVDVFHAVKTLRNSKPNMVETPEQYRFCYDVAL 205
R-PTPc-V cd14618
catalytic domain of receptor-type tyrosine-protein phosphatase V; Receptor-type ...
 1477-1693 6.80e-24

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: 101.94  E-value: 6.80e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2499757  1477 HSQEQFALVEECPEDSMLEASLFPGGPSGCDHVVltgSAGP-----KELWEMVWEHDAHVLVSL--GLPDTKEKPPDIWP 1549
Cdd:cd14618   11 HSRVRLSQLGGEPHSDYINANFIPGYTSPQEFIA---TQGPlkktiEDFWRLVWEQQVCNIIMLtvGMENGRVLCDHYWP 87

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2499757  1550 VEMQPIVTDMVTVHRVSESNTTTgWPSTLFRVIHGESGKERQVQCLQFPC-SESGCELPANTLLTFLDAVGQCCFRGKSK 1628
Cdd:cd14618   88 SESTPVSYGHITVHLLAQSSEDE-WTRREFKLWHEDLRKERRVKHLHYTAwPDHGIPESTSSLMAFRELVREHVQATKGK 166

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2499757  1629 KPgtLLSHSSKNTNQLGTFLAMEQLLQQAGTERTVDVFNVALKQSQACGLMTPTLEQYIYLYNCL 1693
Cdd:cd14618  167 GP--TLVHCSAGVGRSGTFIALDRLLRQLKEEKVVDVFNTVYILRMHRYLMIQTLSQYIFLHSCI 229
Y_phosphatase pfam00102
Protein-tyrosine phosphatase;
1518-1693 1.86e-18

Protein-tyrosine phosphatase;


Pssm-ID: 459674 [Multi-domain]  Cd Length: 234  Bit Score: 86.53  E-value: 1.86e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2499757    1518 KELWEMVWEHDAHVLVSLGLPD--TKEKPPDIWPVEM-QPIVTDMVTVHRVSESNTTTGWPSTLFRVIHGESGKERQVQC 1594
Cdd:pfam00102   56 EDFWRMVWEEKVTIIVMLTELEekGREKCAQYWPEEEgESLEYGDFTVTLKKEKEDEKDYTVRTLEVSNGGSEETRTVKH 135

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2499757    1595 LQFPC-SESGCELPANTLLTFLDAVGQCCFRGKSkkpGTLLSHSSKNTNQLGTFLAMEQLLQQAGTERTVDVFNVALK-Q 1672
Cdd:pfam00102  136 FHYTGwPDHGVPESPNSLLDLLRKVRKSSLDGRS---GPIVVHCSAGIGRTGTFIAIDIALQQLEAEGEVDIFQIVKElR 212

                          170       180
                   ....*....|....*....|.
gi 2499757    1673 SQACGLMTpTLEQYIYLYNCL 1693
Cdd:pfam00102  213 SQRPGMVQ-TLEQYIFLYDAI 232
R3-PTPc cd14548
catalytic domain of R3 subfamily receptor-type tyrosine-protein phosphatases and similar ...
 1470-1690 5.80e-18

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: 84.71  E-value: 5.80e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2499757  1470 NSIVSRRHSQEQFALVEECPEDSMLEASLFPGGPSGCDHVVltgSAGP-----KELWEMVWEHDAHVLVSL--GLPDTKE 1542
Cdd:cd14548    3 TNILPYDHSRVKLIPINEEEGSDYINANYIPGYNSPREFIA---TQGPlpgtkDDFWRMVWEQNSHTIVMLtqCMEKGRV 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2499757  1543 KPPDIWPVEMQPIVTDMVTVHRVSESnTTTGWPSTLFRVIHGEsgKERQVQCLQFPC-SESGCELPANTLLTFLDAVGQc 1621
Cdd:cd14548   80 KCDHYWPFDQDPVYYGDITVTMLSES-VLPDWTIREFKLERGD--EVRSVRQFHFTAwPDHGVPEAPDSLLRFVRLVRD- 155

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2499757  1622 cFRGKSKKPgtLLSHSSKNTNQLGTFLAMEQLLQQAGTERTVDVFNVALKQSQACGLMTPTLEQYIYLY 1690
Cdd:cd14548  156 -YIKQEKGP--TIVHCSAGVGRTGTFIALDRLLQQIESEDYVDIFGIVYDLRKHRPLMVQTEAQYIFLH 221
PTPc cd00047
catalytic domain of protein tyrosine phosphatases; Protein tyrosine phosphatases (PTP, EC 3.1. ...
 1521-1690 2.62e-17

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: 81.95  E-value: 2.62e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2499757  1521 WEMVWEHDAHVLVSLG--LPDTKEKPPDIWPVEM-QPIVTDMVTVHRVSEsNTTTGWPSTLFRVIHGESGKERQVQCLQF 1597
Cdd:cd00047   31 WRMVWEQKVSVIVMLTnlVEKGREKCERYWPEEGgKPLEYGDITVTLVSE-EELSDYTIRTLELSPKGCSESREVTHLHY 109

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2499757  1598 P-CSESGCELPANTLLTFLDAVgqCCFRGKSKKPgtLLSHSSKNTNQLGTFLAMEQLLQQAGTERTVDVFNVALKQSQAC 1676
Cdd:cd00047  110 TgWPDHGVPSSPEDLLALVRRV--RKEARKPNGP--IVVHCSAGVGRTGTFIAIDILLERLEAEGEVDVFEIVKALRKQR 185

                        170
                 ....*....|....
gi 2499757  1677 GLMTPTLEQYIYLY 1690
Cdd:cd00047  186 PGMVQTLEQYEFIY 199
PTPc smart00194
Protein tyrosine phosphatase, catalytic domain;
1521-1693 5.96e-17

Protein tyrosine phosphatase, catalytic domain;


Pssm-ID: 214550 [Multi-domain]  Cd Length: 259  Bit Score: 82.71  E-value: 5.96e-17
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2499757     1521 WEMVWEHDAHVLVSLGLPD--TKEKPPDIWPVEM-QPIVTDMVTVHRVSEsNTTTGWPSTLFRVIHGESGKERQVQCLQF 1597
Cdd:smart00194   86 WRMVWEQKVTVIVMLTELVekGREKCAQYWPDEEgEPLTYGDITVTLKSV-EKVDDYTIRTLEVTNTGCSETRTVTHYHY 164

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2499757     1598 ---PcsESGCELPANTLLTFLDAVGQCcfrgKSKKPGTLLSHSSKNTNQLGTFLAMEQLLQQAGTERTVDVFNVALK-QS 1673
Cdd:smart00194  165 tnwP--DHGVPESPESILDLIRAVRKS----QSTSTGPIVVHCSAGVGRTGTFIAIDILLQQLEAGKEVDIFEIVKElRS 238

                           170       180
                    ....*....|....*....|
gi 2499757     1674 QACGlMTPTLEQYIYLYNCL 1693
Cdd:smart00194  239 QRPG-MVQTEEQYIFLYRAI 257
R-PTPc-J cd14615
catalytic domain of receptor-type tyrosine-protein phosphatase J; Receptor-type ...
 1484-1692 1.78e-14

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: 74.47  E-value: 1.78e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2499757  1484 LVEECPEDSMLEASLFPGGPSGCDHVvltGSAGP-----KELWEMVWEHDAHVLVSLG--LPDTKEKPPDIWPVEMQPIV 1556
Cdd:cd14615   17 SVQSHSTDDYINANYMPGYNSKKEFI---AAQGPlpntvKDFWRMVWEKNVYAIVMLTkcVEQGRTKCEEYWPSKQKKDY 93

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2499757  1557 TDMvTVHRVSESnTTTGWPSTLFRVIHGESGKERQVQCLQFpCSESGCELPANT--LLTFLDAVGQccFRGKSKKPGTLL 1634
Cdd:cd14615   94 GDI-TVTMTSEI-VLPEWTIRDFTVKNAQTNESRTVRHFHF-TSWPDHGVPETTdlLINFRHLVRE--YMKQNPPNSPIL 168

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 2499757  1635 SHSSKNTNQLGTFLAMEQLLQQAGTERTVDVFNVALKQSQACGLMTPTLEQYIYLYNC 1692
Cdd:cd14615  169 VHCSAGVGRTGTFIAIDRLIYQIENENVVDVYGIVYDLRMHRPLMVQTEDQYVFLNQC 226
R-PTPc-H cd14619
catalytic domain of receptor-type tyrosine-protein phosphatase H; Receptor-type ...
 1477-1693 1.50e-13

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: 72.23  E-value: 1.50e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2499757  1477 HSQEQFALVEECPEDSMLEASLFPGGPSGCDHVvltGSAGP-----KELWEMVWEHDAHVLVSLG--LPDTKEKPPDIWP 1549
Cdd:cd14619   11 WSRVPLKPIHEEPGSDYINANYMPGYWSSQEFI---ATQGPlpqtvGDFWRMIWEQQSSTIVMLTncMEAGRVKCEHYWP 87

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2499757  1550 VEMQPIVTDMVTVHRVSEsNTTTGWPSTLFRVIHGESGKERQVQCLQFPC-SESGCELPANTLLTFLDAVGQccFRGKSK 1628
Cdd:cd14619   88 LDYTPCTYGHLRVTVVSE-EVMENWTVREFLLKQVEEQKTLSVRHFHFTAwPDHGVPSSTDTLLAFRRLLRQ--WLDQTM 164

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2499757  1629 KPGTLLSHSSKNTNQLGTFLAMEQLLQQAGTERTVDVFNVALKQSQACGLMTPTLEQYIYLYNCL 1693
Cdd:cd14619  165 SGGPTVVHCSAGVGRTGTLIALDVLLQQLQSEGLLGPFSFVQKMRENRPLMVQTESQYVFLHQCI 229
R-PTP-C-2 cd14558
PTP-like domain of receptor-type tyrosine-protein phosphatase C, repeat 2; Receptor-type ...
 1519-1690 1.88e-12

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: 68.19  E-value: 1.88e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2499757  1519 ELWEMVWEHDAHVLVSLGlpDTKEKPPDI----WPVEMQpIVTDMVTVhrVSESNTTTGWPSTLFRVIHGESGKERQVQC 1594
Cdd:cd14558   29 DFWQMIFQKKVKVIVMLT--ELKEGDQEQcaqyWGDEKK-TYGDIEVE--LKDTEKSPTYTVRVFEITHLKRKDSRTVYQ 103

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2499757  1595 LQFPcSESGCELPAN--TLLTFLDAVGQCC--FRGKSKKPGTLLSHSSKNTNQLGTFLAMEQLLQQAGTERTVDVFNVA- 1669
Cdd:cd14558  104 YQYH-KWKGEELPEKpkDLVDMIKSIKQKLpyKNSKHGRSVPIVVHCSDGSSRTGIFCALWNLLESAETEKVVDVFQVVk 182

                        170       180
                 ....*....|....*....|...
gi 2499757  1670 --LKQSQAcglMTPTLEQYIYLY 1690
Cdd:cd14558  183 alRKQRPG---MVSTLEQYQFLY 202
R-PTP-Z-2 cd17669
catalytic domain of receptor-type tyrosine-protein phosphatase Z, repeat 2; Receptor-type ...
 1518-1693 4.78e-12

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: 66.94  E-value: 4.78e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2499757  1518 KELWEMVWEHDAHVLVSLglPDTKEKPPD---IWPVEMQPIVTDMVTVHRVSESNTTTGWPSTLfrVIHG---ESGKE-- 1589
Cdd:cd17669   28 KDFWRMIWDHNAQLIVML--PDGQNMAEDefvYWPNKDEPINCETFKVTLIAEEHKCLSNEEKL--IIQDfilEATQDdy 103

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2499757  1590 ----RQVQCLQFPCSESgcelPANTLLTFLDAVGQccfrGKSKKPGTLLSHSSKNTNQLGTFLAMEQLLQQAGTERTVDV 1665
Cdd:cd17669  104 vlevRHFQCPKWPNPDS----PISKTFELISIIKE----EAANRDGPMIVHDEHGGVTAGTFCALTTLMHQLEKENSVDV 175

                        170       180       190
                 ....*....|....*....|....*....|..
gi 2499757  1666 FNVAlkqsQACGLMTP----TLEQYIYLYNCL 1693
Cdd:cd17669  176 YQVA----KMINLMRPgvftDIEQYQFLYKAI 203
R5-PTP-2 cd14550
PTP-like domain of R5 subfamily receptor-type tyrosine-protein phosphatases, repeat 2; The R5 ...
 1518-1691 6.51e-12

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: 66.58  E-value: 6.51e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2499757  1518 KELWEMVWEHDAHVLVSLGLPDTKEKPPDIWPVEMQPIVTDMVTVHRVSESNTTTGWPSTLF---RVIhgESGKE----- 1589
Cdd:cd14550   28 KDFWQMIWDHNSQTIVMLTDNELNEDEPIYWPTKEKPLECETFKVTLSGEDHSCLSNEIRLIvrdFIL--ESTQDdyvle 105

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2499757  1590 -RQVQCLQFPCSESgcelPANTLLTFLDAVGqccfRGKSKKPGTLLSHSSKNTNQLGTFLAMEQLLQQAGTERTVDVFNV 1668
Cdd:cd14550  106 vRQFQCPSWPNPCS----PIHTVFELINTVQ----EWAQQRDGPIVVHDRYGGVQAATFCALTTLHQQLEHESSVDVYQV 177

                        170       180
                 ....*....|....*....|....*..
gi 2499757  1669 ALKQSqacgLMTP----TLEQYIYLYN 1691
Cdd:cd14550  178 AKLYH----LMRPgvftSKEDYQFLYK 200
R-PTPc-D-1 cd14624
catalytic domain of receptor-type tyrosine-protein phosphatase D, repeat 1; Receptor-type ...
 1422-1700 2.21e-11

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: 66.68  E-value: 2.21e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2499757  1422 PISVMDFAQACAKRAANANAGFLKEYKLL---KQAIKDGTGSLLPPPDYNQNSIVSRRHSQEQFALVEECPEDSMLEASL 1498
Cdd:cd14624    3 PIPILELADHIERLKANDNLKFSQEYESIdpgQQFTWEHSNLEVNKPKNRYANVIAYDHSRVLLSAIEGIPGSDYINANY 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2499757  1499 FPGGPSGCDHVVLTGSAgPK---ELWEMVWEHDAHVLVSLGLPDTKE--KPPDIWP---VEMQPIVtdMVTVHRVSESNT 1570
Cdd:cd14624   83 IDGYRKQNAYIATQGAL-PEtfgDFWRMIWEQRSATVVMMTKLEERSrvKCDQYWPsrgTETYGLI--QVTLLDTVELAT 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2499757  1571 TTGWPSTLFRVIHGESGKERQVQCLQFPcsESGCELPANTLLTFLDAVGQCcfrgKSKKPGTLLSHSSKNTNQLGTFLAM 1650
Cdd:cd14624  160 YCVRTFALYKNGSSEKREVRQFQFTAWP--DHGVPEHPTPFLAFLRRVKTC----NPPDAGPMVVHCSAGVGRTGCFIVI 233

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|.
gi 2499757  1651 EQLLQQAGTERTVDVF-NVALKQSQAcGLMTPTLEQYIYLYNCLNSALLNG 1700
Cdd:cd14624  234 DAMLERIKHEKTVDIYgHVTLMRAQR-NYMVQTEDQYIFIHDALLEAVTCG 283
R-PTPc-B cd14617
catalytic domain of receptor-type tyrosine-protein phosphatase B; Receptor-type ...
 1470-1690 1.44e-10

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: 63.01  E-value: 1.44e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2499757  1470 NSIVSRRHSQEQFALVEECPEDSMLEASLFPGGPSGCDHVVLTGS-AGPKE-LWEMVWEHDAH--VLVSLGLPDTKEKPP 1545
Cdd:cd14617    4 NNILPYDSTRVKLSNVDDDPCSDYINASYIPGNNFRREYIATQGPlPGTKDdFWKMVWEQNVHniVMVTQCVEKGRVKCD 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2499757  1546 DIWPVEMQPIVTDMVTVHRVSESnTTTGWPSTLFRvIHGESGKE-----RQVQCLQFPcsESGCELPANTLLTFLDAVGQ 1620
Cdd:cd14617   84 HYWPADQDSLYYGDLIVQMLSES-VLPEWTIREFK-ICSEEQLDaprlvRHFHYTVWP--DHGVPETTQSLIQFVRTVRD 159

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2499757  1621 ccFRGKSKKPGTLLSHSSKNTNQLGTFLAMEQLLQQAGTERTVDVFNVALKQSQACGLMTPTLEQYIYLY 1690
Cdd:cd14617  160 --YINRTPGSGPTVVHCSAGVGRTGTFIALDRILQQLDSKDSVDIYGAVHDLRLHRVHMVQTECQYVYLH 227
R-PTPc-A-1 cd14621
catalytic domain of receptor-type tyrosine-protein phosphatase A, repeat 1; Receptor-type ...
 1422-1700 1.70e-10

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: 64.27  E-value: 1.70e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2499757  1422 PISVMDFAQACAKRAANANAGFLKEYKLLK----QAIKDGTGSLLPPPDYNQNSIVSRRHSQEQFALVEECPEDSMLEAS 1497
Cdd:cd14621    7 PLPVDKLEEEINRRMADDNKLFREEFNALPacpiQATCEAASKEENKEKNRYVNILPYDHSRVHLTPVEGVPDSDYINAS 86

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2499757  1498 LFPGGPsgcDHVVLTGSAGPKE-----LWEMVWEHD-AHVLVSLGLPDTKE-KPPDIWPVEMQPIVTDMvtvhRVSESNT 1570
Cdd:cd14621   87 FINGYQ---EKNKFIAAQGPKEetvndFWRMIWEQNtATIVMVTNLKERKEcKCAQYWPDQGCWTYGNI----RVSVEDV 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2499757  1571 TTGWPSTL----FRVIHGESGKERQVQCLQFPCS---ESGCELPANTLLTFLDAVGQCcfrgKSKKPGTLLSHSSKNTNQ 1643
Cdd:cd14621  160 TVLVDYTVrkfcIQQVGDVTNKKPQRLITQFHFTswpDFGVPFTPIGMLKFLKKVKNC----NPQYAGAIVVHCSAGVGR 235

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 2499757  1644 LGTFLAMEQLLQQAGTERTVDVFN-VALKQSQACGlMTPTLEQYIYLYNCLNSALLNG 1700
Cdd:cd14621  236 TGTFIVIDAMLDMMHAERKVDVYGfVSRIRAQRCQ-MVQTDMQYVFIYQALLEHYLYG 292
R-PTPc-O cd14614
catalytic domain of receptor-type tyrosine-protein phosphatase O; Receptor-type ...
 1494-1693 2.05e-10

catalytic domain of receptor-type tyrosine-protein phosphatase O; Receptor-type tyrosine-protein phosphatase O (PTPRO or R-PTP-O), also known as glomerular epithelial protein 1 or protein tyrosine phosphatase U2 (PTP-U2), belongs to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. PTPRO is a member of the R3 subfamily of receptor-type phosphotyrosine phosphatases (RPTP), characterized by a unique modular composition consisting of multiple extracellular fibronectin type III (FN3) repeats and a single (most RPTP subtypes have two) cytoplasmic catalytic PTP domain. It is essential for sustaining the structure and function of foot processes by regulating tyrosine phosphorylation of podocyte proteins. It has been identified as a synaptic cell adhesion molecule (CAM) that serves as a potent initiator of synapse formation. It is also a tumor suppressor in several types of cancer, such as hepatocellular carcinoma, lung cancer, and breast cancer.


Pssm-ID: 350462 [Multi-domain]  Cd Length: 245  Bit Score: 62.98  E-value: 2.05e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2499757  1494 LEASLFPGGPSGCDHVvltGSAGP-----KELWEMVWEHDAHVLVSLGLPDTKE--KPPDIWPVEMQPIVTDMVTVHRVS 1566
Cdd:cd14614   43 INANYIPGYNSPQEYI---ATQGPlpetrNDFWKMVLQQKSQIIVMLTQCNEKRrvKCDHYWPFTEEPVAYGDITVEMLS 119

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2499757  1567 ESNTTTgWPSTLFRVIHGEsgkerQVQCL------QFPCSESGCELPANTLLTFLDAVGQccfrGKSKKPGTLLSHSSKN 1640
Cdd:cd14614  120 EEEQPD-WAIREFRVSYAD-----EVQDVmhfnytAWPDHGVPTANAAESILQFVQMVRQ----QAVKSKGPMIIHCSAG 189

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|...
gi 2499757  1641 TNQLGTFLAMEQLLQQAGTERTVDVFNVALKQSQACGLMTPTLEQYIYLYNCL 1693
Cdd:cd14614  190 VGRTGTFIALDRLLQHIRDHEFVDILGLVSEMRSYRMSMVQTEEQYIFIHQCV 242
R-PTPc-F-1 cd14626
catalytic domain of receptor-type tyrosine-protein phosphatase F, repeat 1; Receptor-type ...
 1427-1696 5.42e-09

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: 59.28  E-value: 5.42e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2499757  1427 DFAQACAKRAANANAGFLKEYKLL---KQAIKDGTGSLLPPPDYNQNSIVSRRHSQEQFALVEECPEDSMLEASLFPGGP 1503
Cdd:cd14626    2 DLADNIERLKANDGLKFSQEYESIdpgQQFTWENSNLEVNKPKNRYANVIAYDHSRVILTSVDGVPGSDYINANYIDGYR 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2499757  1504 SGCDHVVLTGSAgPKEL---WEMVWEHDAHVLVSLGLPDTKE--KPPDIWPVE-MQPIVTDMVTVHRVSESNTTTGWPST 1577
Cdd:cd14626   82 KQNAYIATQGPL-PETLsdfWRMVWEQRTATIVMMTRLEEKSrvKCDQYWPIRgTETYGMIQVTLLDTVELATYSVRTFA 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2499757  1578 LFRVIHGESGKERQVQCLQFPcsESGCELPANTLLTFLDAVGQCcfrgKSKKPGTLLSHSSKNTNQLGTFLAMEQLLQQA 1657
Cdd:cd14626  161 LYKNGSSEKREVRQFQFMAWP--DHGVPEYPTPILAFLRRVKAC----NPPDAGPMVVHCSAGVGRTGCFIVIDAMLERM 234

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|
gi 2499757  1658 GTERTVDVF-NVALKQSQAcGLMTPTLEQYIYLYNCLNSA 1696
Cdd:cd14626  235 KHEKTVDIYgHVTCMRSQR-NYMVQTEDQYIFIHEALLEA 273
FN3 COG3401
Fibronectin type 3 domain [General function prediction only];
377-749 5.66e-09

Fibronectin type 3 domain [General function prediction only];


Pssm-ID: 442628 [Multi-domain]  Cd Length: 603  Bit Score: 60.79  E-value: 5.66e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2499757   377 PYDAWVEGSTWLAESAALPREVPGARLWLDGLEASKQPGRRALlYSDDAPGSLGNISVPSGATHViFCGLVPGAHYRVDI 456
Cdd:COG3401   44 LSVTTKESPGTLLVAAGLSSGGGLGTGGRAGTTSGVAAVAVAA-APPTATGLTTLTGSGSVGGAT-NTGLTSSDEVPSPA 121

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2499757   457 ASSTGDISQSISGYTSPLPPQSLEVISRSSPSDLTIAWGPAPGQLEGYKVTWHqDGSQRSPGDLVDLGPDTLSLTLKSLV 536
Cdd:COG3401  122 VGTATTATAVAGGAATAGTYALGAGLYGVDGANASGTTASSVAGAGVVVSPDT-SATAAVATTSLTVTSTTLVDGGGDIE 200

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2499757   537 PGSCYT--VSAWAWAGNLDSDSQ--KIHSCTRPAPPTNLSlGFAHQPAALKASWyHPPGGRDAFHLRLYRlrpltlesek 612
Cdd:COG3401  201 PGTTYYyrVAATDTGGESAPSNEvsVTTPTTPPSAPTGLT-ATADTPGSVTLSW-DPVTESDATGYRVYR---------- 268

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2499757   613 vlpREAQNFSWAQLTAGCE---------------FQVQLSTLWG--SERSSSANAT-GWTPPSAPTLVNVTSDAPTQLQV 674
Cdd:COG3401  269 ---SNSGDGPFTKVATVTTtsytdtgltngttyyYRVTAVDAAGneSAPSNVVSVTtDLTPPAAPSGLTATAVGSSSITL 345

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2499757   675 SWAHVPGGR-SRYQVtLYQESTRTATSIMGPKEDGTSFL--GLTPGTKYKVEVISW--AGPLYTAAANVSAWTYPLIPNE 749
Cdd:COG3401  346 SWTASSDADvTGYNV-YRSTSGGGTYTKIAETVTTTSYTdtGLTPGTTYYYKVTAVdaAGNESAPSEEVSATTASAASGE 424
R-PTP-G-2 cd17670
PTP-like domain of receptor-type tyrosine-protein phosphatase G, repeat 2; Receptor-type ...
 1518-1695 6.90e-09

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: 57.77  E-value: 6.90e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2499757  1518 KELWEMVWEHDAHVLVSlgLPDTKEKPPD---IWPVEMQPIVTDMVTVHRVSESNTTTGWPSTLfrVIHG---ESGKE-- 1589
Cdd:cd17670   28 KDFWRMIWDHNAQIIVM--LPDNQGLAEDefvYWPSREESMNCEAFTVTLISKDRLCLSNEEQI--IIHDfilEATQDdy 103

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2499757  1590 ----RQVQCLQFPCSESgcelPANTLLTFLDAVGQCCFrgksKKPGTLLSHSSKNTNQLGTFLAMEQLLQQAGTERTVDV 1665
Cdd:cd17670  104 vlevRHFQCPKWPNPDA----PISSTFELINVIKEEAL----TRDGPTIVHDEFGAVSAGTLCALTTLSQQLENENAVDV 175

                        170       180       190
                 ....*....|....*....|....*....|....
gi 2499757  1666 FNVAlkqsQACGLMTP----TLEQYIYLYNCLNS 1695
Cdd:cd17670  176 YQVA----KMINLMRPgvftDIEQYQFLYKAMLS 205
CDKN3-like cd14505
cyclin-dependent kinase inhibitor 3 and similar proteins; This family is composed of ...
 1289-1403 1.14e-08

cyclin-dependent kinase inhibitor 3 and similar proteins; This family is composed of eukaryotic cyclin-dependent kinase inhibitor 3 (CDKN3) and related archaeal and bacterial proteins. CDKN3 is also known as kinase-associated phosphatase (KAP), CDK2-associated dual-specificity phosphatase, cyclin-dependent kinase interactor 1 (CDI1), or cyclin-dependent kinase-interacting protein 2 (CIP2). It has been characterized as dual-specificity phosphatase, which function as a protein-serine/threonine phosphatase (EC 3.1.3.16) and protein-tyrosine-phosphatase (EC 3.1.3.48). It dephosphorylates CDK2 at a threonine residue in a cyclin-dependent manner, resulting in the inhibition of G1/S cell cycle progression. It also interacts with CDK1 and controls progression through mitosis by dephosphorylating CDC2. CDKN3 may also function as a tumor suppressor; its loss of function was found in a variety of cancers including glioblastoma and hepatocellular carcinoma. However, it has also been found over-expressed in many cancers such as breast, cervical, lung and prostate cancers, and may also have an oncogenic function.


Pssm-ID: 350355 [Multi-domain]  Cd Length: 163  Bit Score: 56.12  E-value: 1.14e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2499757  1289 TRREFQlQHGTEQKQRRVKQLQFTtWPDHSVPE--APSSLLAFVELVQEQVQATQGKGPILVHCSAGVGRTGTfVALLRL 1366
Cdd:cd14505   52 TDGELE-ELGVPDLLEQYQQAGIT-WHHLPIPDggVPSDIAQWQELLEELLSALENGKKVLIHCKGGLGRTGL-IAACLL 128

                         90       100       110
                 ....*....|....*....|....*....|....*..
gi 2499757  1367 LRQLEEEKVADVFNTVyilRLHRPLMIQTLSQYIFLH 1403
Cdd:cd14505  129 LELGDTLDPEQAIAAV---RALRPGAIQTPKQENFLH 162
PHA02740 PHA02740
protein tyrosine phosphatase; Provisional
 1182-1360 1.26e-08

protein tyrosine phosphatase; Provisional


Pssm-ID: 165107 [Multi-domain]  Cd Length: 298  Bit Score: 58.44  E-value: 1.26e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2499757   1182 HVLPYDHSRVRLTQlpgepHSDYINANFIPGYSHTQEIIATQGPLKKTLEDFWRLVWEQQVHVIIMLTVGMENGRVlcEH 1261
Cdd:PHA02740   61 HITRLLHRRIKLFN-----DEKVLDARFVDGYDFEQKFICIINLCEDACDKFLQALSDNKVQIIVLISRHADKKCF--NQ 133

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2499757   1262 YWPANS-TPVTHGHITIHLLA--EEPEDEWTRREFQLQHGTEQKqrrVKQLQFTTWPDHSVPEAPSSLLAFVELV----- 1333
Cdd:PHA02740  134 FWSLKEgCVITSDKFQIETLEiiIKPHFNLTLLSLTDKFGQAQK---ISHFQYTAWPADGFSHDPDAFIDFFCNIddlca 210

                         170       180
                  ....*....|....*....|....*...
gi 2499757   1334 QEQVQATQGK-GPILVHCSAGVGRTGTF 1360
Cdd:PHA02740  211 DLEKHKADGKiAPIIIDCIDGISSSAVF 238
CDC14 COG2453
Protein-tyrosine phosphatase [Signal transduction mechanisms];
1314-1362 1.49e-07

Protein-tyrosine phosphatase [Signal transduction mechanisms];


Pssm-ID: 441989 [Multi-domain]  Cd Length: 140  Bit Score: 52.28  E-value: 1.49e-07
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*....
gi 2499757  1314 WPDHSVPEaPSSLLAFVELVQEQVQAtqgKGPILVHCSAGVGRTGTFVA 1362
Cdd:COG2453   55 IPDFGAPD-DEQLQEAVDFIDEALRE---GKKVLVHCRGGIGRTGTVAA 99
FN3 cd00063
Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein ...
 656-725 1.82e-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: 50.57  E-value: 1.82e-07
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2499757   656 PSAPTLVNVTSDAPTQLQVSWAHVPGGRSR---YQVTLYQESTRTATSIMGPKEDGTSFL--GLTPGTKYKVEVI 725
Cdd:cd00063    1 PSPPTNLRVTDVTSTSVTLSWTPPEDDGGPitgYVVEYREKGSGDWKEVEVTPGSETSYTltGLKPGTEYEFRVR 75
R-PTPc-LAR-1 cd14553
catalytic domain of LAR family receptor-type tyrosine-protein phosphatases, repeat 1; The LAR ...
 1519-1696 1.95e-07

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: 53.94  E-value: 1.95e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2499757  1519 ELWEMVWEHDAHVLVSLglpdTKE------KPPDIWPVEMQPIVTDM-VTVHRVSESNTTTgwpSTLFRVIHGESGKERQ 1591
Cdd:cd14553   61 DFWRMVWEQRSATIVMM----TKLeersrvKCDQYWPTRGTETYGLIqVTLLDTVELATYT---VRTFALHKNGSSEKRE 133

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2499757  1592 VQCLQFPC-SESGC-ELPAnTLLTFLDAVGQCCfrgkSKKPGTLLSHSSKNTNQLGTFLAMEQLLQQAGTERTVDVF-NV 1668
Cdd:cd14553  134 VRQFQFTAwPDHGVpEHPT-PFLAFLRRVKACN----PPDAGPIVVHCSAGVGRTGCFIVIDSMLERIKHEKTVDIYgHV 208

                        170       180
                 ....*....|....*....|....*...
gi 2499757  1669 ALKQSQAcGLMTPTLEQYIYLYNCLNSA 1696
Cdd:cd14553  209 TCLRAQR-NYMVQTEDQYIFIHDALLEA 235
R-PTPc-A-E-2 cd14552
catalytic domain of receptor-type tyrosine-protein phosphatase A and E, repeat 2; ...
 1514-1690 3.35e-07

catalytic domain of receptor-type tyrosine-protein phosphatase A and E, repeat 2; Receptor-type tyrosine-protein phosphatase A (PTPRA) and E (PTPRE) belong to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. PTPRA and PTPRE share several functions including regulation of Src family kinases and voltage-gated potassium (Kv) channels. They both contain a small extracellular domain, a transmembrane segment, and an intracellular region containing two tandem catalytic PTP domains. This model represents the second PTP domain (repeat 2).


Pssm-ID: 350400 [Multi-domain]  Cd Length: 202  Bit Score: 52.66  E-value: 3.35e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2499757  1514 SAGP-----KELWEMVWEHDAHVLVSLglPDTKEKPPD----IWPVEMQPIVTDMVtvhrVSESNTTTGWPSTL--FRVI 1582
Cdd:cd14552   19 TQGPldhtvEDFWRMIWEWKSCSIVML--TEIKERSQNkcaqYWPEDGSVSSGDIT----VELKDQTDYEDYTLrdFLVT 92

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2499757  1583 HGESGKERQVQCLQF---PcsESGceLPANTLlTFLDAVGQCCFRGKSKKPGTLLSHSSKNTNQLGTFLAMEQLLQQAGT 1659
Cdd:cd14552   93 KGKGGSTRTVRQFHFhgwP--EVG--IPDNGK-GMIDLIAAVQKQQQQSGNHPITVHCSAGAGRTGTFCALSTVLERVKA 167

                        170       180       190
                 ....*....|....*....|....*....|.
gi 2499757  1660 ERTVDVFNVALKQSQACGLMTPTLEQYIYLY 1690
Cdd:cd14552  168 EGVLDVFQVVKSLRLQRPHMVQTLEQYEFCY 198
PHA02746 PHA02746
protein tyrosine phosphatase; Provisional
 1516-1698 6.70e-07

protein tyrosine phosphatase; Provisional


Pssm-ID: 165113 [Multi-domain]  Cd Length: 323  Bit Score: 53.11  E-value: 6.70e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2499757   1516 GPKE-----LWEMVWEHDAHVLVSLG-LPDTKEKPPDIWPVEMQPIVTDMVTVHRVSESNTTTGWPSTLFRVIHGESGKE 1589
Cdd:PHA02746  120 GPKEdtsedFFKLISEHESQVIVSLTdIDDDDEKCFELWTKEEDSELAFGRFVAKILDIIEELSFTKTRLMITDKISDTS 199

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2499757   1590 RQVQCLQFP-CSESGCELPANTLLTFLDAVGQCCFRGK------SKKPGTLLSHSSKNTNQLGTFLAMEQLLQQAGTERT 1662
Cdd:PHA02746  200 REIHHFWFPdWPDNGIPTGMAEFLELINKVNEEQAELIkqadndPQTLGPIVVHCSAGIGRAGTFCAIDNALEQLEKEKE 279

                         170       180       190
                  ....*....|....*....|....*....|....*...
gi 2499757   1663 VDVFNVALK--QSQACGLMTPtlEQYIYLYNCLNSALL 1698
Cdd:PHA02746  280 VCLGEIVLKirKQRHSSVFLP--EQYAFCYKALKYAII 315
PTP_DSP_cys cd14494
cys-based protein tyrosine phosphatase and dual-specificity phosphatase superfamily; This ...
 1326-1403 7.47e-07

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


Pssm-ID: 350344 [Multi-domain]  Cd Length: 113  Bit Score: 49.27  E-value: 7.47e-07
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2499757  1326 LLAFVELVQEQVQatqGKGPILVHCSAGVGRTGTFVALLRLLRQLEEEKVAdvfntVYILRLHRPLMI-QTLSQYIFLH 1403
Cdd:cd14494   42 VDRFLEVLDQAEK---PGEPVLVHCKAGVGRTGTLVACYLVLLGGMSAEEA-----VRIVRLIRPGGIpQTIEQLDFLI 112
PTP_YopH-like cd14559
YopH and related bacterial protein tyrosine phosphatases; Yersinia outer protein H (YopH) ...
 1220-1399 1.15e-06

YopH and related bacterial protein tyrosine phosphatases; Yersinia outer protein H (YopH) belongs to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. YopH is an essential virulence determinant of the pathogenic bacterium by dephosphorylating several focal adhesion proteins including p130Cas in human epithelial cells, resulting in the disruption of focal adhesions and cell detachment from the extracellular matrix. It contains an N-terminal domain that contains signals required for TTSS-mediated delivery of YopH into host cells and a C-terminal catalytic PTP domain.


Pssm-ID: 350407 [Multi-domain]  Cd Length: 227  Bit Score: 51.63  E-value: 1.15e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2499757  1220 IATQGPLKKTLEDFWRLVWEQQVHVIIMLTVGMENGRVLCEHYWPANSTpvtHGHITI---HLLAEEPEDEWTRREFQLQ 1296
Cdd:cd14559   32 IACQYPKNEQLEDHLKMLADNRTPCLVVLASNKDIQRKGLPPYFRQSGT---YGSVTVkskKTGKDELVDGLKADMYNLK 108

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2499757  1297 HGTEQKQRRVKQLQFTTWPDHSvpeaPSSLLAFVELVQEQVQATQGKGPIL-----------------VHCSAGVGRTGT 1359
Cdd:cd14559  109 ITDGNKTITIPVVHVTNWPDHT----AISSEGLKELADLVNKSAEEKRNFYkskgssaindknkllpvIHCRAGVGRTGQ 184

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|
gi 2499757  1360 FVALLRLLRQLEEEKVADVFNTVYILRLHRplMIQTLSQY 1399
Cdd:cd14559  185 LAAAMELNKSPNNLSVEDIVSDMRTSRNGK--MVQKDEQL 222
R-PTP-LAR-2 cd14554
PTP-like domain of the LAR family receptor-type tyrosine-protein phosphatases, repeat 2; The ...
 1519-1690 2.64e-06

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: 50.60  E-value: 2.64e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2499757  1519 ELWEMVWEHDAHVLVSLglpdTK------EKPPDIWPVE----MQPIVTDMVTVHRVSESNTTTgwpstlFRVIHGESGK 1588
Cdd:cd14554   64 DFWRMLWEHNSTIIVML----TKlremgrEKCHQYWPAErsarYQYFVVDPMAEYNMPQYILRE------FKVTDARDGQ 133

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2499757  1589 ERQVQCLQF--------PCSESGcelpantlltFLDAVGQcCFRGKSK--KPGTLLSHSSKNTNQLGTFLAMEQLLQQAG 1658
Cdd:cd14554  134 SRTVRQFQFtdwpeqgvPKSGEG----------FIDFIGQ-VHKTKEQfgQEGPITVHCSAGVGRTGVFITLSIVLERMR 202

                        170       180       190
                 ....*....|....*....|....*....|...
gi 2499757  1659 TERTVDVFN-VALKQSQACGlMTPTLEQYIYLY 1690
Cdd:cd14554  203 YEGVVDVFQtVKLLRTQRPA-MVQTEDQYQFCY 234
R-PTPc-S-1 cd14625
catalytic domain of receptor-type tyrosine-protein phosphatase S, repeat 1; Receptor-type ...
 1422-1697 2.66e-06

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: 51.25  E-value: 2.66e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2499757  1422 PISVMDFAQACAKRAANANAGFLKEYKLL---KQAIKDGTGSLLPPPDYNQNSIVSRRHSQEQFALVEECPEDSMLEASL 1498
Cdd:cd14625    3 PIPISELAEHTERLKANDNLKLSQEYESIdpgQQFTWEHSNLEVNKPKNRYANVIAYDHSRVILQPIEGIMGSDYINANY 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2499757  1499 FPGGPSGCDHVVLTGSAgPK---ELWEMVWEHDAHVLVSLGLPDTKE--KPPDIWPVEMQPiVTDMVTVHRVSESNTTTG 1573
Cdd:cd14625   83 IDGYRKQNAYIATQGPL-PEtfgDFWRMVWEQRSATVVMMTKLEEKSriKCDQYWPSRGTE-TYGMIQVTLLDTIELATF 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2499757  1574 WPSTlFRVIHGESGKERQVQCLQFPC-SESGCELPANTLLTFLDAVGQCcfrgKSKKPGTLLSHSSKNTNQLGTFLAMEQ 1652
Cdd:cd14625  161 CVRT-FSLHKNGSSEKREVRQFQFTAwPDHGVPEYPTPFLAFLRRVKTC----NPPDAGPIVVHCSAGVGRTGCFIVIDA 235

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*.
gi 2499757  1653 LLQQAGTERTVDVF-NVALKQSQAcGLMTPTLEQYIYLYNCLNSAL 1697
Cdd:cd14625  236 MLERIKHEKTVDIYgHVTLMRSQR-NYMVQTEDQYSFIHDALLEAV 280
FN3 COG3401
Fibronectin type 3 domain [General function prediction only];
451-743 3.06e-06

Fibronectin type 3 domain [General function prediction only];


Pssm-ID: 442628 [Multi-domain]  Cd Length: 603  Bit Score: 51.93  E-value: 3.06e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2499757   451 HYRVDIASSTGDISQS-----ISGYTSPLPPQSLEVISRSSPSdLTIAWGPAPGQ-LEGYKVtwHQDGSQRSPGDLVDLG 524
Cdd:COG3401  206 YYRVAATDTGGESAPSnevsvTTPTTPPSAPTGLTATADTPGS-VTLSWDPVTESdATGYRV--YRSNSGDGPFTKVATV 282

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2499757   525 PDTlSLTLKSLVPGS--CYTVSAWAWAGNLDSDSQKIH---SCTRPAPPTNLSLGfAHQPAALKASWYHPPGGrDAFHLR 599
Cdd:COG3401  283 TTT-SYTDTGLTNGTtyYYRVTAVDAAGNESAPSNVVSvttDLTPPAAPSGLTAT-AVGSSSITLSWTASSDA-DVTGYN 359

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2499757   600 LYRLRPLTLESEKV-LPREAQNFSWAQLTAGCEFQVQL----STLWGSERSSSANATGWTPPSAPTLVNVTSDAPTQLQV 674
Cdd:COG3401  360 VYRSTSGGGTYTKIaETVTTTSYTDTGLTPGTTYYYKVtavdAAGNESAPSEEVSATTASAASGESLTASVDAVPLTDVA 439

                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2499757   675 SWAHVPGGRSRYQVTLYQESTRTATSIMGPKE----DGTSFLGLTPGTKYKVEVISWAGPLYTAAANVSAWTY 743
Cdd:COG3401  440 GATAAASAASNPGVSAAVLADGGDTGNAVPFTttssTVTATTTDTTTANLSVTTGSLVGGSGASSVTNSVSVI 512
PTPc-N21_14 cd14540
catalytic domain of tyrosine-protein phosphatase non-receptor type 21 and type 14; ...
 1518-1693 6.16e-06

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: 48.99  E-value: 6.16e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2499757  1518 KELWEMVWEHDAHVLVSLG--LPDTKEKPPDIWPVEMQPIVTDMVTVHRVS-ESNTTTG-WPSTLFRVIHGESGKERQVQ 1593
Cdd:cd14540   30 GDFWQMVWEQGVYLVVMVTaeEEGGREKCFRYWPTLGGEHDALTFGEYKVStKFSVSSGcYTTTGLRVKHTLSGQSRTVW 109

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2499757  1594 CLQFP-CSESGCELPANTLLTFLDAVGQC------CFRGKSKKPGTLLsHSSKNTNQLGTFLAMEQLLQQAGTERTVDVF 1666
Cdd:cd14540  110 HLQYTdWPDHGCPEDVSGFLDFLEEINSVrrhtnqDVAGHNRNPPTLV-HCSAGVGRTGVVILADLMLYCLDHNEELDIP 188

                        170       180
                 ....*....|....*....|....*..
gi 2499757  1667 NVALKQSQACGLMTPTLEQYIYLYNCL 1693
Cdd:cd14540  189 RVLALLRHQRMLLVQTLAQYKFVYNVL 215
FN3 COG3401
Fibronectin type 3 domain [General function prediction only];
642-765 7.06e-06

Fibronectin type 3 domain [General function prediction only];


Pssm-ID: 442628 [Multi-domain]  Cd Length: 603  Bit Score: 50.77  E-value: 7.06e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2499757   642 SERSSSANAT-GWTPPSAPTLVNVTSDAPTQLQVSWAHVPGGR-SRYQVtLYQESTRTATSIMGpKEDGTSFL--GLTPG 717
Cdd:COG3401  218 SAPSNEVSVTtPTTPPSAPTGLTATADTPGSVTLSWDPVTESDaTGYRV-YRSNSGDGPFTKVA-TVTTTSYTdtGLTNG 295

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 2499757   718 TKYKVEVISwagplYTAAANVSAW----------TYPLIPNELLVSMQAGSAvVNLAW 765
Cdd:COG3401  296 TTYYYRVTA-----VDAAGNESAPsnvvsvttdlTPPAAPSGLTATAVGSSS-ITLSW 347
R-PTPc-T-1 cd14630
catalytic domain of receptor-type tyrosine-protein phosphatase T, repeat 1; Receptor-type ...
 1466-1698 8.00e-06

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: 49.25  E-value: 8.00e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2499757  1466 DYNQN-----SIVSRRHSQEQFALVEECPEDSMLEASLFPGGPSGCDHVVLTGSAGP--KELWEMVWEHDAH--VLVSLG 1536
Cdd:cd14630    1 DENRNknrygNIISYDHSRVRLQLLDGDPHSDYINANYIDGYHRPRHYIATQGPMQEtvKDFWRMIWQENSAsvVMVTNL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2499757  1537 LPDTKEKPPDIWPVEMQ---PIVTDMVTVHRVSESNTTTgwpSTLFRVIHGESGKERQVQCLQFPcsESGCELPANTLLT 1613
Cdd:cd14630   81 VEVGRVKCVRYWPDDTEvygDIKVTLIETEPLAEYVIRT---FTVQKKGYHEIREIRQFHFTSWP--DHGVPCYATGLLG 155

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2499757  1614 FLDAVgqccfrgKSKKP---GTLLSHSSKNTNQLGTFLAMEQLLQQAGTERTVDVFNVALKQSQACGLMTPTLEQYIYLY 1690
Cdd:cd14630  156 FVRQV-------KFLNPpdaGPIVVHCSAGAGRTGCFIAIDIMLDMAENEGVVDIFNCVRELRAQRVNMVQTEEQYVFVH 228


                 ....*...
gi 2499757  1691 NCLNSALL 1698
Cdd:cd14630  229 DAILEACL 236
fn3 pfam00041
Fibronectin type III domain;
657-726 9.67e-06

Fibronectin type III domain;


Pssm-ID: 394996 [Multi-domain]  Cd Length: 85  Bit Score: 45.48  E-value: 9.67e-06
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2499757     657 SAPTLVNVTSDAPTQLQVSWAHVPGGRS---RYQVTLYQE-STRTATSIMGPK-EDGTSFLGLTPGTKYKVEVIS 726
Cdd:pfam00041    1 SAPSNLTVTDVTSTSLTVSWTPPPDGNGpitGYEVEYRPKnSGEPWNEITVPGtTTSVTLTGLKPGTEYEVRVQA 75
FN3 smart00060
Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, ...
 473-547 9.72e-06

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: 45.30  E-value: 9.72e-06
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2499757      473 PLPPQSLEVISRSSPSdLTIAW-GPAPGQLEGYKVTWH-QDGSQRSPGDLVDLGPDTLSLTLKSLVPGSCYTVSAWA 547
Cdd:smart00060    1 PSPPSNLRVTDVTSTS-VTLSWePPPDDGITGYIVGYRvEYREEGSEWKEVNVTPSSTSYTLTGLKPGTEYEFRVRA 76
R-PTPc-Q cd14616
catalytic domain of receptor-type tyrosine-protein phosphatase Q; Receptor-type ...
 1511-1690 1.06e-05

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: 48.36  E-value: 1.06e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2499757  1511 LTGSAGpkELWEMVWEHDAHVLVSLG--LPDTKEKPPDIWPVEMQPI-VTDMVTVHRVSEsNTTTGWPSTLFRV-IHGES 1586
Cdd:cd14616   49 LPGTVG--DFWRMVWETRAKTIVMLTqcFEKGRIRCHQYWPEDNKPVtVFGDIVITKLME-DVQIDWTIRDLKIeRHGDY 125

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2499757  1587 GKERQVQCLQFPcsESGCELPANTLLTFLDAVgqccfrgKSKKPG---TLLSHSSKNTNQLGTFLAMEQLLQQAGTERTV 1663
Cdd:cd14616  126 MMVRQCNFTSWP--EHGVPESSAPLIHFVKLV-------RASRAHdntPMIVHCSAGVGRTGVFIALDHLTQHINDHDFV 196

                        170       180
                 ....*....|....*....|....*....
gi 2499757  1664 DVFNVA--LKQSQACglMTPTLEQYIYLY 1690
Cdd:cd14616  197 DIYGLVaeLRSERMC--MVQNLAQYIFLH 223
R-PTP-D-2 cd14628
PTP-like domain of receptor-type tyrosine-protein phosphatase D, repeat 2; Receptor-type ...
 1518-1690 1.07e-05

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: 49.34  E-value: 1.07e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2499757  1518 KELWEMVWEHDAHVLVSL-GLPDT-KEKPPDIWPVEMQPIVTDMVtVHRVSESNTttgwPSTL---FRVIHGESGKERQV 1592
Cdd:cd14628  109 EDFWRMLWEHNSTIVVMLtKLREMgREKCHQYWPAERSARYQYFV-VDPMAEYNM----PQYIlreFKVTDARDGQSRTV 183

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2499757  1593 QCLQFP-CSESGCELPANTLLTFLDAVGQCcfRGKSKKPGTLLSHSSKNTNQLGTFLAMEQLLQQAGTERTVDVFN-VAL 1670
Cdd:cd14628  184 RQFQFTdWPEQGVPKSGEGFIDFIGQVHKT--KEQFGQDGPISVHCSAGVGRTGVFITLSIVLERMRYEGVVDIFQtVKM 261

                        170       180
                 ....*....|....*....|
gi 2499757  1671 KQSQACGlMTPTLEQYIYLY 1690
Cdd:cd14628  262 LRTQRPA-MVQTEDQYQFCY 280
FN3 cd00063
Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein ...
 473-555 1.15e-05

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: 45.57  E-value: 1.15e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2499757   473 PLPPQSLEVISRSSPSdLTIAWGPAP---GQLEGYKVTWHQDGSQRsPGDLVDLGPDTLSLTLKSLVPGSCYTVSAWAWA 549
Cdd:cd00063    1 PSPPTNLRVTDVTSTS-VTLSWTPPEddgGPITGYVVEYREKGSGD-WKEVEVTPGSETSYTLTGLKPGTEYEFRVRAVN 78


                 ....*.
gi 2499757   550 GNLDSD 555
Cdd:cd00063   79 GGGESP 84
fn3 pfam00041
Fibronectin type III domain;
475-544 2.52e-05

Fibronectin type III domain;


Pssm-ID: 394996 [Multi-domain]  Cd Length: 85  Bit Score: 44.33  E-value: 2.52e-05
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2499757     475 PPQSLEVISRSSpSDLTIAWGPAP---GQLEGYKVTWHQDGSQrSPGDLVDLGPDTLSLTLKSLVPGSCYTVS 544
Cdd:pfam00041    2 APSNLTVTDVTS-TSLTVSWTPPPdgnGPITGYEVEYRPKNSG-EPWNEITVPGTTTSVTLTGLKPGTEYEVR 72
PTPc-N20_13 cd14538
catalytic domain of tyrosine-protein phosphatase non-receptor type 20 and type 13; ...
 1518-1697 2.67e-05

catalytic domain of tyrosine-protein phosphatase non-receptor type 20 and type 13; Tyrosine-protein phosphatase non-receptor type 20 (PTPN20) and type 13 (PTPN13, also known as PTPL1) belong to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. Human PTPN20 is a widely expressed phosphatase with a dynamic subcellular distribution that is targeted to sites of actin polymerization. Human PTPN13 is an important regulator of tumor aggressiveness.


Pssm-ID: 350386 [Multi-domain]  Cd Length: 207  Bit Score: 46.98  E-value: 2.67e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2499757  1518 KELWEMVWEHDAHV--LVSLGLPDTKEKPPDIWPVemQPIVTDMVTVH---RVSESNTTTGWPSTLFRVIHGESGKERQV 1592
Cdd:cd14538   30 GDFWQMVWEQKSEViaMVTQDVEGGKVKCHRYWPD--SLNKPLICGGRlevSLEKYQSLQDFVIRRISLRDKETGEVHHI 107

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2499757  1593 QCLQF---PcsESGCELPANTLLTFLdavgqcCFRGKSKKPGTLLSHSSKNTNQLGTFLAMEQLLQQAGTERTVDVFN-V 1668
Cdd:cd14538  108 THLNFttwP--DHGTPQSADPLLRFI------RYMRRIHNSGPIVVHCSAGIGRTGVLITIDVALGLIERDLPFDIQDiV 179

                        170       180
                 ....*....|....*....|....*....
gi 2499757  1669 ALKQSQACGlMTPTLEQYIYLYNCLNSAL 1697
Cdd:cd14538  180 KDLREQRQG-MIQTKDQYIFCYKACLEVL 207
FN3 smart00060
Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, ...
 656-725 3.05e-05

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


Pssm-ID: 214495 [Multi-domain]  Cd Length: 83  Bit Score: 44.14  E-value: 3.05e-05
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2499757      656 PSAPTLVNVTSDAPTQLQVSWAHVPGGRSRYQVTLYQESTRTATS---IMGPKEDGTSFL--GLTPGTKYKVEVI 725
Cdd:smart00060    1 PSPPSNLRVTDVTSTSVTLSWEPPPDDGITGYIVGYRVEYREEGSewkEVNVTPSSTSYTltGLKPGTEYEFRVR 75
PTPc_DSPc smart00012
Protein tyrosine phosphatase, catalytic domain, undefined specificity; Protein tyrosine ...
 1590-1695 3.14e-05

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: 44.66  E-value: 3.14e-05
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2499757     1590 RQVQCLQFPcsESGCELPANTLLTFLDAVGQCCFRGKSKKPgtLLSHSSKNTNQLGTFLAMEQLLQQAGTE-RTVDVFNV 1668
Cdd:smart00012    3 KHYHYTGWP--DHGVPESPDSILELLRAVKKNLNQSESSGP--VVVHCSAGVGRTGTFVAIDILLQQLEAEaGEVDIFDT 78

                            90       100
                    ....*....|....*....|....*...
gi 2499757     1669 ALK-QSQACGLMTpTLEQYIYLYNCLNS 1695
Cdd:smart00012   79 VKElRSQRPGMVQ-TEEQYLFLYRALLE 105
PTPc_motif smart00404
Protein tyrosine phosphatase, catalytic domain motif;
1590-1695 3.14e-05

Protein tyrosine phosphatase, catalytic domain motif;


Pssm-ID: 214649 [Multi-domain]  Cd Length: 105  Bit Score: 44.66  E-value: 3.14e-05
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2499757     1590 RQVQCLQFPcsESGCELPANTLLTFLDAVGQCCFRGKSKKPgtLLSHSSKNTNQLGTFLAMEQLLQQAGTE-RTVDVFNV 1668
Cdd:smart00404    3 KHYHYTGWP--DHGVPESPDSILELLRAVKKNLNQSESSGP--VVVHCSAGVGRTGTFVAIDILLQQLEAEaGEVDIFDT 78

                            90       100
                    ....*....|....*....|....*...
gi 2499757     1669 ALK-QSQACGLMTpTLEQYIYLYNCLNS 1695
Cdd:smart00404   79 VKElRSQRPGMVQ-TEEQYLFLYRALLE 105
R-PTP-F-2 cd14629
PTP-like domain of receptor-type tyrosine-protein phosphatase F, repeat 2; Receptor-type ...
 1518-1690 3.81e-05

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: 47.41  E-value: 3.81e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2499757  1518 KELWEMVWEHDAHVLVSL-GLPDT-KEKPPDIWPVEMQPIVTDMVtVHRVSESNTttgwPSTL---FRVIHGESGKERQV 1592
Cdd:cd14629  110 EDFWRMLWEHNSTIVVMLtKLREMgREKCHQYWPAERSARYQYFV-VDPMAEYNM----PQYIlreFKVTDARDGQSRTI 184

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2499757  1593 QCLQFP-CSESGCelpANTLLTFLDAVGQcCFRGKSK--KPGTLLSHSSKNTNQLGTFLAMEQLLQQAGTERTVDVFNVA 1669
Cdd:cd14629  185 RQFQFTdWPEQGV---PKTGEGFIDFIGQ-VHKTKEQfgQDGPITVHCSAGVGRTGVFITLSIVLERMRYEGVVDMFQTV 260

                        170       180
                 ....*....|....*....|.
gi 2499757  1670 LKQSQACGLMTPTLEQYIYLY 1690
Cdd:cd14629  261 KTLRTQRPAMVQTEDQYQLCY 281
R-PTPc-typeIIb-1 cd14555
catalytic domain of type IIb (or R2B) subfamily receptor-type tyrosine-protein phosphatases, ...
 1518-1698 4.91e-05

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: 46.45  E-value: 4.91e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2499757  1518 KELWEMVW-EHDAHV-----LVSLG-------LPDTKEKPPDI--WPVEMQPI---VTDMVTVHR--VSESNTT-----T 1572
Cdd:cd14555   28 YDFWRMVWqENSASIvmvtnLVEVGrvkcsryWPDDTEVYGDIkvTLVETEPLaeyVVRTFALERrgYHEIREVrqfhfT 107

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2499757  1573 GWPStlfrviHGesgkerqvqclqFPCSESGcelpantLLTFLDAVgqccfrgKSKKP---GTLLSHSSKNTNQLGTFLA 1649
Cdd:cd14555  108 GWPD------HG------------VPYHATG-------LLGFIRRV-------KASNPpsaGPIVVHCSAGAGRTGCYIV 155

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|
gi 2499757  1650 MEQLLQQAGTERTVDVFN-VALKQSQACGlMTPTLEQYIYLYNCLNSALL 1698
Cdd:cd14555  156 IDIMLDMAEREGVVDIYNcVKELRSRRVN-MVQTEEQYIFIHDAILEACL 204
PTPc-N11_6 cd14544
catalytic domain of tyrosine-protein phosphatase non-receptor type 11 and type 6; ...
 1519-1690 8.88e-05

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: 45.92  E-value: 8.88e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2499757  1519 ELWEMVWEHDAHVLV--SLGLPDTKEKPPDIWPVEMQPIVTDMVTVHRVSESNTTTGWPSTLFRVIHGESGKERQVQCLQ 1596
Cdd:cd14544   67 DFWSMVWQENSRVIVmtTKEVERGKNKCVRYWPDEGMQKQYGPYRVQNVSEHDTTDYTLRELQVSKLDQGDPIREIWHYQ 146

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2499757  1597 F---PcsESGCELPANTLLTFLDAVGQccfRGKS-KKPGTLLSHSSKNTNQLGTFLAMEQLLQQ---AGTERTVDVFN-V 1668
Cdd:cd14544  147 YlswP--DHGVPSDPGGVLNFLEDVNQ---RQESlPHAGPIVVHCSAGIGRTGTFIVIDMLLDQikrKGLDCDIDIQKtI 221

                        170       180
                 ....*....|....*....|..
gi 2499757  1669 ALKQSQACGlMTPTLEQYIYLY 1690
Cdd:cd14544  222 QMVRSQRSG-MVQTEAQYKFIY 242
fn3 pfam00041
Fibronectin type III domain;
148-201 8.99e-05

Fibronectin type III domain;


Pssm-ID: 394996 [Multi-domain]  Cd Length: 85  Bit Score: 42.79  E-value: 8.99e-05
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 2499757     148 SWS---DAPGDQDSYQLLLYHLESQTLACNVSVSPDTLSYSFGDLLPGTQYVLEVIT 201
Cdd:pfam00041   19 SWTpppDGNGPITGYEVEYRPKNSGEPWNEITVPGTTTSVTLTGLKPGTEYEVRVQA 75
PTPc-KIM cd14547
catalytic domain of the kinase interaction motif (KIM) family of protein-tyrosine phosphatases; ...
 1519-1686 9.58e-05

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: 45.47  E-value: 9.58e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2499757  1519 ELWEMVWEHDAHVLVSL-GLPDTKEKPPDIWPVEMQPIVTDM-VTVHRVsesNTTTGWPSTLFRVIHGesGKERQVQCLQ 1596
Cdd:cd14547   56 DFWRMVWQEKTPIIVMItNLTEAKEKCAQYWPEEENETYGDFeVTVQSV---KETDGYTVRKLTLKYG--GEKRYLKHYW 130

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2499757  1597 FPcSESGCELP--ANTLLTFLDAVGQCcfRGKSKKPGTLLSHSSKNTNQLGTFLAMEQLLQQAGTERTVDVFNVALKQSQ 1674
Cdd:cd14547  131 YT-SWPDHKTPeaAQPLLSLVQEVEEA--RQTEPHRGPIVVHCSAGIGRTGCFIATSIGCQQLREEGVVDVLGIVCQLRL 207

                        170
                 ....*....|..
gi 2499757  1675 ACGLMTPTLEQY 1686
Cdd:cd14547  208 DRGGMVQTAEQY 219
R-PTPc-A-2 cd14623
catalytic domain of receptor-type tyrosine-protein phosphatase A, repeat 2; Receptor-type ...
 1512-1690 1.14e-04

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


Pssm-ID: 350471 [Multi-domain]  Cd Length: 228  Bit Score: 45.42  E-value: 1.14e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2499757  1512 TGSAGP-----KELWEMVWEHDAHVLVSLGLPDTK--EKPPDIWPVEMQPIVTDM-VTVHRVSESNTTTgwpSTLFRVIH 1583
Cdd:cd14623   42 IASQGPlqhtiEDFWRMIWEWKSCSIVMLTELEERgqEKCAQYWPSDGSVSYGDItIELKKEEECESYT---VRDLLVTN 118

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2499757  1584 GESGKERQVQCLQF-PCSESGCELPANTLLTFLDAVGQccfrgKSKKPGT--LLSHSSKNTNQLGTFLAMEQLLQQAGTE 1660
Cdd:cd14623  119 TRENKSRQIRQFHFhGWPEVGIPSDGKGMINIIAAVQK-----QQQQSGNhpITVHCSAGAGRTGTFCALSTVLERVKAE 193

                        170       180       190
                 ....*....|....*....|....*....|
gi 2499757  1661 RTVDVFNVALKQSQACGLMTPTLEQYIYLY 1690
Cdd:cd14623  194 GILDVFQTVKSLRLQRPHMVQTLEQYEFCY 223
R-PTPc-C-1 cd14557
catalytic domain of receptor-type tyrosine-protein phosphatase C, repeat 1; Receptor-type ...
 1516-1690 1.40e-04

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: 44.82  E-value: 1.40e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2499757  1516 GPKE-----LWEMVWEHDAHVLVSLGLPD--TKEKPPDIWP-VEMQPIVTDMVTVHRVSESNtttgWPSTLFRVIH---- 1583
Cdd:cd14557   21 GPKDetvddFWRMIWEQKSTVIVMVTRCEegNRNKCAQYWPsMEEGSRAFGDVVVKINEEKI----CPDYIIRKLNinnk 96

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2499757  1584 GESGKERQVQCLQFPC-SESGCELPANTLLTFLDAVGQccFRGKSKKPgtLLSHSSKNTNQLGTFLAMEQLLQQAGTERT 1662
Cdd:cd14557   97 KEKGSGREVTHIQFTSwPDHGVPEDPHLLLKLRRRVNA--FNNFFSGP--IVVHCSAGVGRTGTYIGIDAMLEGLEAEGR 172

                        170       180
                 ....*....|....*....|....*....
gi 2499757  1663 VDVFNVALK-QSQACgLMTPTLEQYIYLY 1690
Cdd:cd14557  173 VDVYGYVVKlRRQRC-LMVQVEAQYILIH 200
PTP_PTPDC1 cd14506
protein tyrosine phosphatase domain of PTP domain-containing protein 1; protein tyrosine ...
 1314-1403 1.84e-04

protein tyrosine phosphatase domain of PTP domain-containing protein 1; protein tyrosine phosphatase domain-containing protein 1 (PTPDC1) is an uncharacterized non-receptor class protein-tyrosine phosphatase (PTP). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. Small interfering RNA (siRNA) knockdown of the ptpdc1 gene is associated with elongated cilia.


Pssm-ID: 350356 [Multi-domain]  Cd Length: 206  Bit Score: 44.65  E-value: 1.84e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2499757  1314 WPDHSVPeAPSSLLAFVElVQEQVQATQGKgpILVHCSAGVGRTGTFVALLRLLRQLEEEKVAdvfntVYILRLHRPLMI 1393
Cdd:cd14506   84 WKDYGVP-SLTTILDIVK-VMAFALQEGGK--VAVHCHAGLGRTGVLIACYLVYALRMSADQA-----IRLVRSKRPNSI 154

                         90
                 ....*....|
gi 2499757  1394 QTLSQYIFLH 1403
Cdd:cd14506  155 QTRGQVLCVR 164
R-PTP-S-2 cd14627
PTP-like domain of receptor-type tyrosine-protein phosphatase S, repeat 2; Receptor-type ...
 1518-1690 1.91e-04

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: 45.49  E-value: 1.91e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2499757  1518 KELWEMVWEHDAHVLVSL-GLPDT-KEKPPDIWPVEMQPIVTDMVtVHRVSESNTttgwPSTL---FRVIHGESGKERQV 1592
Cdd:cd14627  110 EDFWRMLWENNSTIVVMLtKLREMgREKCHQYWPAERSARYQYFV-VDPMAEYNM----PQYIlreFKVTDARDGQSRTV 184

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2499757  1593 QCLQFP-CSESGCELPANTLLTFLDAVGQCcfRGKSKKPGTLLSHSSKNTNQLGTFLAMEQLLQQAGTERTVDVFN-VAL 1670
Cdd:cd14627  185 RQFQFTdWPEQGVPKSGEGFIDFIGQVHKT--KEQFGQDGPISVHCSAGVGRTGVFITLSIVLERMRYEGVVDIFQtVKM 262

                        170       180
                 ....*....|....*....|
gi 2499757  1671 KQSQACGlMTPTLEQYIYLY 1690
Cdd:cd14627  263 LRTQRPA-MVQTEDEYQFCY 281
TpbA-like cd14529
bacterial protein tyrosine and dual-specificity phosphatases related to Pseudomonas aeruginosa ...
 1330-1362 5.58e-04

bacterial protein tyrosine and dual-specificity phosphatases related to Pseudomonas aeruginosa TpbA; This subfamily contains bacterial protein tyrosine phosphatases (PTPs) and dual-specificity phosphatases (DUSPs) related to Pseudomonas aeruginosa TpbA, a DUSP that negatively regulates biofilm formation by converting extracellular quorum sensing signals and to Mycobacterium tuberculosis PtpB, a PTP virulence factor that attenuates host immune defenses by interfering with signal transduction pathways in macrophages. PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides, while DUSPs function as protein-serine/threonine phosphatases (EC 3.1.3.16) and PTPs.


Pssm-ID: 350378 [Multi-domain]  Cd Length: 158  Bit Score: 42.36  E-value: 5.58e-04
                         10        20        30
                 ....*....|....*....|....*....|...
gi 2499757  1330 VELVQEQVQATQGKGPILVHCSAGVGRTGTFVA 1362
Cdd:cd14529   76 VQSFLLIMDLKLAPGPVLIHCKHGKDRTGLVSA 108
PTPc-N9 cd14543
catalytic domain of tyrosine-protein phosphatase non-receptor type 9; Tyrosine-protein ...
 1442-1690 8.06e-04

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: 43.12  E-value: 8.06e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2499757  1442 GFLKEYKLLKQAIKDGT--GSLLPppdYNQ-----NSIVSRRHSQEQFALVEECPEDSMLEASLFPGGPSGCDHVvltGS 1514
Cdd:cd14543    4 GIYEEYEDIRREPPAGTflCSLAP---ANQeknryGDVLCLDQSRVKLPKRNGDERTDYINANFMDGYKQKNAYI---AT 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2499757  1515 AGPKE-----LWEMVWEHdaHVLVSLGLPDTKE----KPPDIWPVE--MQPIVTDM-VTVHRVSESNTTTgwpSTLFRVI 1582
Cdd:cd14543   78 QGPLPktysdFWRMVWEQ--KVLVIVMTTRVVErgrvKCGQYWPLEegSSLRYGDLtVTNLSVENKEHYK---KTTLEIH 152

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2499757  1583 HGESGKERQVQCLQF---PcsESGCELPANTLLTFLDAVGQ----CC------FRGKSKKPgTLLSHSSKNTNQLGTFLA 1649
Cdd:cd14543  153 NTETDESRQVTHFQFtswP--DFGVPSSAAALLDFLGEVRQqqalAVkamgdrWKGHPPGP-PIVVHCSAGIGRTGTFCT 229

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|...
gi 2499757  1650 MEQLLQQAGTERTVDVFN-VALKQSQ-ACGLMTPtlEQYIYLY 1690
Cdd:cd14543  230 LDICLSQLEDVGTLNVMQtVRRMRTQrAFSIQTP--DQYYFCY 270
DUSP23 cd14504
dual specificity phosphatase 23; Dual specificity phosphatase 23 (DUSP23), also known as ...
 1315-1362 9.86e-04

dual specificity phosphatase 23; Dual specificity phosphatase 23 (DUSP23), also known as VH1-like phosphatase Z (VHZ) or low molecular mass dual specificity phosphatase 3 (LDP-3), functions as a protein-serine/threonine phosphatase (EC 3.1.3.16) and a protein-tyrosine-phosphatase (EC 3.1.3.48). It deactivates its MAPK substrates by dephosphorylating the threonine and tyrosine residues in the conserved Thr-Xaa-Tyr motif residing in their activation sites. DUSP23 is an atypical DUSP; it contains the catalytic dual specificity phosphatase domain but lacks the N-terminal Cdc25/rhodanese-like domain that is present in typical DUSPs or MKPs. It is able to enhance activation of JNK and p38 MAPK, and has been shown to dephosphorylate p44-ERK1 (MAPK3) in vitro. It has been associated with cell growth and human primary cancers. It has also been identified as a cell-cell adhesion regulatory protein; it promotes the dephosphorylation of beta-catenin at Tyr 142 and enhances the interaction between alpha- and beta-catenin.


Pssm-ID: 350354 [Multi-domain]  Cd Length: 142  Bit Score: 41.11  E-value: 9.86e-04
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*...
gi 2499757  1315 PDHSVPEaPSSLLAFVELVQEQVqaTQGKgPILVHCSAGVGRTGTFVA 1362
Cdd:cd14504   58 EDYTPPT-LEQIDEFLDIVEEAN--AKNE-AVLVHCLAGKGRTGTMLA 101
CDC14_C cd14499
C-terminal dual-specificity phosphatase domain of CDC14 family proteins; The cell division ...
 1315-1362 1.04e-03

C-terminal dual-specificity phosphatase domain of CDC14 family proteins; The cell division control protein 14 (CDC14) family is highly conserved in all eukaryotes, although the roles of its members seem to have diverged during evolution. Yeast Cdc14, the best characterized member of this family, is a dual-specificity phosphatase that plays key roles in cell cycle control. It preferentially dephosphorylates cyclin-dependent kinase (CDK) targets, which makes it the main antagonist of CDK in the cell. Cdc14 functions at the end of mitosis and it triggers the events that completely eliminates the activity of CDK and other mitotic kinases. It is also involved in coordinating the nuclear division cycle with cytokinesis through the cytokinesis checkpoint, and in chromosome segregation. Cdc14 phosphatases also function in DNA replication, DNA damage checkpoint, and DNA repair. Vertebrates may contain more than one Cdc14 homolog; humans have three (CDC14A, CDC14B, and CDC14C). CDC14 family proteins contain a highly conserved N-terminal pseudophosphatase domain that contributes to substrate specificity and a C-terminal catalytic dual-specificity phosphatase domain with the PTP signature motif.


Pssm-ID: 350349 [Multi-domain]  Cd Length: 174  Bit Score: 41.67  E-value: 1.04e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*...
gi 2499757  1315 PDHSVPEaPSSLLAFVELVQEQvqatqgKGPILVHCSAGVGRTGTFVA 1362
Cdd:cd14499   88 PDGSTPS-DDIVKKFLDICENE------KGAIAVHCKAGLGRTGTLIA 128
PTP_VSP_TPTE cd14510
protein tyrosine phosphatase-like catalytic domain of voltage-sensitive phosphatase ...
 1315-1361 1.32e-03

protein tyrosine phosphatase-like catalytic domain of voltage-sensitive phosphatase/transmembrane phosphatase with tensin homology; Voltage-sensitive phosphatase (VSP) proteins comprise a family of phosphoinositide phosphatases with substrates that include phosphatidylinositol-4,5-diphosphate and phosphatidylinositol-3,4,5-trisphosphate. This family is conserved in deuterostomes; VSP was first identified as a sperm flagellar plasma membrane protein in Ciona intestinalis. Gene duplication events in primates resulted in the presence of paralogs, transmembrane phosphatase with tensin homology (TPTE) and TPTE2, that retain protein domain architecture but, in the case of TPTE, have lost catalytic activity. TPTE, also called cancer/testis antigen 44 (CT44), may play a role in the signal transduction pathways of the endocrine or spermatogenic function of the testis. TPTE2, also called TPTE and PTEN homologous inositol lipid phosphatase (TPIP), occurs in several differentially spliced forms; TPIP alpha displays phosphoinositide 3-phosphatase activity and is localized on the endoplasmic reticulum, while TPIP beta is cytosolic and lacks detectable phosphatase activity. VSP/TPTE proteins contain an N-terminal voltage sensor consisting of four transmembrane segments, a protein tyrosine phosphatase (PTP)-like phosphoinositide phosphatase catalytic domain, followed by a regulatory C2 domain.


Pssm-ID: 350360 [Multi-domain]  Cd Length: 177  Bit Score: 41.58  E-value: 1.32e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*..
gi 2499757  1315 PDHSVPEAPSsLLAFVELVQEQVQATQgKGPILVHCSAGVGRTGTFV 1361
Cdd:cd14510   82 DDHNVPTLDE-MLSFTAEVREWMAADP-KNVVAIHCKGGKGRTGTMV 126
DSPc smart00195
Dual specificity phosphatase, catalytic domain;
1338-1362 1.53e-03

Dual specificity phosphatase, catalytic domain;


Pssm-ID: 214551 [Multi-domain]  Cd Length: 138  Bit Score: 40.73  E-value: 1.53e-03
                            10        20
                    ....*....|....*....|....*
gi 2499757     1338 QATQGKGPILVHCSAGVGRTGTFVA 1362
Cdd:smart00195   73 DAESKGGKVLVHCQAGVSRSATLII 97
PTP_PTEN-like cd14497
protein tyrosine phosphatase-like domain of phosphatase and tensin homolog and similar ...
 1216-1362 1.72e-03

protein tyrosine phosphatase-like domain of phosphatase and tensin homolog and similar proteins; Phosphatase and tensin homolog (PTEN) is a tumor suppressor that acts as a dual-specificity protein phosphatase and as a lipid phosphatase. It dephosphorylates phosphoinositide trisphosphate. In addition to PTEN, this family includes tensins, voltage-sensitive phosphatases (VSPs), and auxilins. They all contain a protein tyrosine phosphatase-like domain although not all are active phosphatases. Tensins are intracellular proteins that act as links between the extracellular matrix and the cytoskeleton, and thereby mediate signaling for cell shape and motility, and they may or may not have phosphatase activity. VSPs are phosphoinositide phosphatases with substrates that include phosphatidylinositol-4,5-diphosphate and phosphatidylinositol-3,4,5-trisphosphate. Auxilins are J domain-containing proteins that facilitate Hsc70-mediated dissociation of clathrin from clathrin-coated vesicles, and they do not exhibit phosphatase activity.


Pssm-ID: 350347 [Multi-domain]  Cd Length: 160  Bit Score: 41.03  E-value: 1.72e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2499757  1216 TQEIIATQGPLKKTLEDFWRlvweQQVHVIIMLtvgmengrvLCEHYwpanstpvtHGHITIHLLAEEPEDEWTRREFQL 1295
Cdd:cd14497    6 TPRIIAMSFPATGYPESLYR----NSIDDVANF---------LNTHH---------PDHYMIFNLSEEEYDDDSKFEGRV 63

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2499757  1296 QH-GteqkqrrvkqlqfttWPDHSVPeaPSSLL-AFVELVQEQVQATQgKGPILVHCSAGVGRTGTFVA 1362
Cdd:cd14497   64 LHyG---------------FPDHHPP--PLGLLlEIVDDIDSWLSEDP-NNVAVVHCKAGKGRTGTVIC 114
DSPc pfam00782
Dual specificity phosphatase, catalytic domain; Ser/Thr and Tyr protein phosphatases. The ...
 1326-1362 3.22e-03

Dual specificity phosphatase, catalytic domain; Ser/Thr and Tyr protein phosphatases. The enzyme's tertiary fold is highly similar to that of tyrosine-specific phosphatases, except for a "recognition" region.


Pssm-ID: 395632 [Multi-domain]  Cd Length: 127  Bit Score: 39.55  E-value: 3.22e-03
                           10        20        30
                   ....*....|....*....|....*....|....*...
gi 2499757    1326 LLAFVELVQEQV-QATQGKGPILVHCSAGVGRTGTFVA 1362
Cdd:pfam00782   51 ISKYLEEAVEFIdDARQKGGKVLVHCQAGISRSATLII 88
FN3 smart00060
Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, ...
 49-110 3.74e-03

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: 37.98  E-value: 3.74e-03
                            10        20        30        40        50        60
                    ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2499757       49 STSLFLSWVAAELGGFD-YALSLRSVNSSGSPEGQQLQAHTNESGFEFHGLVPGSRYQLKLTV 110
Cdd:smart00060   14 STSVTLSWEPPPDDGITgYIVGYRVEYREEGSEWKEVNVTPSSTSYTLTGLKPGTEYEFRVRA 76
fn3 pfam00041
Fibronectin type III domain;
49-109 5.99e-03

Fibronectin type III domain;


Pssm-ID: 394996 [Multi-domain]  Cd Length: 85  Bit Score: 37.39  E-value: 5.99e-03
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2499757      49 STSLFLSWVAAELGG---FDYALSLRSVNSSGSPegQQLQAHTNESGFEFHGLVPGSRYQLKLT 109
Cdd:pfam00041   13 STSLTVSWTPPPDGNgpiTGYEVEYRPKNSGEPW--NEITVPGTTTSVTLTGLKPGTEYEVRVQ 74
PTPc-N22_18_12 cd14542
catalytic domain of tyrosine-protein phosphatase non-receptor type 22, type 18 and type 12; ...
 1519-1691 7.92e-03

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: 39.71  E-value: 7.92e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2499757  1519 ELWEMVWEHDAHVLV------SLGlpdtKEKPPDIWPVEMQP-IVTDMVTVHRVSESNTTTGWpstLFRVIHGESGKERQ 1591
Cdd:cd14542   29 DFWRMIWEYNVQVIVmacrefEMG----KKKCERYWPEEGEEqLQFGPFKISLEKEKRVGPDF---LIRTLKVTFQKESR 101

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2499757  1592 VQClQFPCS---ESGCELPANTLLTFLDAVGqcCFRGKSKKPgtLLSHSSKNTNQLGTFLAME---QLLQQAGTERTVDV 1665
Cdd:cd14542  102 TVY-QFHYTawpDHGVPSSVDPILDLVRLVR--DYQGSEDVP--ICVHCSAGCGRTGTICAIDyvwNLLKTGKIPEEFSL 176

                        170       180
                 ....*....|....*....|....*....
gi 2499757  1666 FNVAL---KQSQAcglMTPTLEQYIYLYN 1691
Cdd:cd14542  177 FDLVRemrKQRPA---MVQTKEQYELVYR 202
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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