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Conserved domains on  [gi|158303304|ref|NP_031981|]
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receptor-type tyrosine-protein phosphatase V precursor [Mus musculus]

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 8.97e-155

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: 471.73  E-value: 8.97e-155
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158303304 1178 NRYPHVLPYDHSRVRLTQLSGEPHSDYINANFIPGYSHPQEIIATQGPLKKTLEDFWRLVWEQQVHVIIMLTVGMENGRV 1257
Cdd:cd14618     1 NRYPHVLPYDHSRVRLSQLGGEPHSDYINANFIPGYTSPQEFIATQGPLKKTIEDFWRLVWEQQVCNIIMLTVGMENGRV 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158303304 1258 LCEHYWPVNSTPVTHGHITTHLLAEESEDEWTRREFQLQHGAEQKQRRVKQLQFTTWPDHSVPEAPSSLLAFVELVQEEV 1337
Cdd:cd14618    81 LCDHYWPSESTPVSYGHITVHLLAQSSEDEWTRREFKLWHEDLRKERRVKHLHYTAWPDHGIPESTSSLMAFRELVREHV 160

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158303304 1338 KATQGKGPILVHCSAGVGRTGTFVALLRLLRQLEEEQVVDVFNTVYILRLHRPLMIQTLSQYIFLHSCLL 1407
Cdd:cd14618   161 QATKGKGPTLVHCSAGVGRSGTFIALDRLLRQLKEEKVVDVFNTVYILRMHRYLMIQTLSQYIFLHSCIL 230
PTP_tm pfam18861
TM proximal of protein tyrosine phosphatase, receptor type J; Protein tyrosine phosphatases ...
 948-1069 8.65e-50

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: 172.41  E-value: 8.65e-50
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158303304   948 VTRGMFGKDDGQIQWYGIIATINMTLAQPSQEAINHTWYDHYYRGHDSYLALLFPNPFYPePWAVPRSWTVPVGTEDCdn 1027
Cdd:pfam18861    1 IQFSLFNSSNGPIKAYGVIVTTNDSLNRPLKEYLNKTYYDWKYKKTDSYLATVTPNPFTS-PRSSSRSLTVPVGTGSK-- 77

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*....
gi 158303304  1028 TQEICNGHLKPGFQYRFSIAAFSRL-------SSPETILAFSAFSEPQA 1069
Cdd:pfam18861   78 WQGYCNGPLKPLGSYRFSVAAFTRLefddgliDGEESYVSFTPFSEPIA 126
PTP_DSP_cys super family cl28904
cys-based protein tyrosine phosphatase and dual-specificity phosphatase superfamily; This ...
 1477-1692 1.28e-20

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: 92.70  E-value: 1.28e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158303304 1477 HSQEQLALVEESPADNMLAASLFPGGPSGRDHVVltgSAGP-----KELWEMVWEHGAYVLVSL--GLPDTKEKPQDIWP 1549
Cdd:cd14618    11 HSRVRLSQLGGEPHSDYINANFIPGYTSPQEFIA---TQGPlkktiEDFWRLVWEQQVCNIIMLtvGMENGRVLCDHYWP 87

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158303304 1550 MEMQPIVTDMVTVHRVAESNTAGWPSTLIRVIHGDSGTERQVQCLQFPHCETGS--ELPAnTLLTFLDAVGQCCSrgNSK 1627
Cdd:cd14618    88 SESTPVSYGHITVHLLAQSSEDEWTRREFKLWHEDLRKERRVKHLHYTAWPDHGipESTS-SLMAFRELVREHVQ--ATK 164

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 158303304 1628 KPGTLLSHSSKVTNQLSTFLAMEQLLQQAGTERTVDVFSVALKQTQACGLKTPTLEQYIYLYNCL 1692
Cdd:cd14618   165 GKGPTLVHCSAGVGRSGTFIALDRLLRQLKEEKVVDVFNTVYILRMHRYLMIQTLSQYIFLHSCI 229
FN3 super family cl27307
Fibronectin type 3 domain [General function prediction only];
378-749 5.69e-11

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: 67.33  E-value: 5.69e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158303304  378 YDAWVEGSIWLAESAARPMEVPGARLWLEGLEATKQPGRRALLYSVDAPGLLGNISVSSGATHV-TFCGLVPGAHYRVDI 456
Cdd:COG3401    42 VVLSVTTKESPGTLLVAAGLSSGGGLGTGGRAGTTSGVAAVAVAAAPPTATGLTTLTGSGSVGGaTNTGLTSSDEVPSPA 121

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158303304  457 ASSMGDITQSLTGYTSPLPPQSLEIISRNSPSDLTIGWAPAPGQMEGYKVTWHqDGSQRSPGDLVDLGPDISSLTLKSLV 536
Cdd:COG3401   122 VGTATTATAVAGGAATAGTYALGAGLYGVDGANASGTTASSVAGAGVVVSPDT-SATAAVATTSLTVTSTTLVDGGGDIE 200

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158303304  537 PGSCYTVSAWAW-SGNLSSDSQKIH---SCTRPAPPTNLSlGFAHQPATLRASWcHPPGGRDAFQLRLYRlRPLTLESEK 612
Cdd:COG3401   201 PGTTYYYRVAATdTGGESAPSNEVSvttPTTPPSAPTGLT-ATADTPGSVTLSW-DPVTESDATGYRVYR-SNSGDGPFT 277

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158303304  613 ILSQEAQN-FSWAQLPAG--YEFQVQLSTLWGsEESGSAN----TTGWTPPSAPTLVNVTSEAPTQLHVSWVHAAG-DRS 684
Cdd:COG3401   278 KVATVTTTsYTDTGLTNGttYYYRVTAVDAAG-NESAPSNvvsvTTDLTPPAAPSGLTATAVGSSSITLSWTASSDaDVT 356

                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 158303304  685 SYQVtLYQESTRTATSIVGPKADSTSFW--GLTPGTK--YKVEAISWAGPLYTAAANVSAWTYPLTPNE 749
Cdd:COG3401   357 GYNV-YRSTSGGGTYTKIAETVTTTSYTdtGLTPGTTyyYKVTAVDAAGNESAPSEEVSATTASAASGE 424
FN3 smart00060
Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, ...
 36-110 2.03e-04

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: 41.83  E-value: 2.03e-04
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 158303304     36 GPPLSVNVSSRGkPTSLFLSWVA-AEPGGFDYALCLRAMNLSGFPEGQQLQAHTNESSFEFHGLVPGSRYQLELTV 110
Cdd:smart00060    2 SPPSNLRVTDVT-STSVTLSWEPpPDDGITGYIVGYRVEYREEGSEWKEVNVTPSSTSYTLTGLKPGTEYEFRVRA 76
fn3 pfam00041
Fibronectin type III domain;
131-201 2.60e-04

Fibronectin type III domain;


:

Pssm-ID: 394996 [Multi-domain]  Cd Length: 85  Bit Score: 41.25  E-value: 2.60e-04
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 158303304   131 VRGLQLHSTGSpASLEASWS---DASGDQDSYQLLlYHPESHTLACN-VSVSPDTLSYNFGDLLPGSQYVLEVIT 201
Cdd:pfam00041    3 PSNLTVTDVTS-TSLTVSWTpppDGNGPITGYEVE-YRPKNSGEPWNeITVPGTTTSVTLTGLKPGTEYEVRVQA 75
 
Name Accession Description Interval E-value
R-PTPc-V cd14618
catalytic domain of receptor-type tyrosine-protein phosphatase V; Receptor-type ...
 1178-1407 8.97e-155

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: 471.73  E-value: 8.97e-155
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158303304 1178 NRYPHVLPYDHSRVRLTQLSGEPHSDYINANFIPGYSHPQEIIATQGPLKKTLEDFWRLVWEQQVHVIIMLTVGMENGRV 1257
Cdd:cd14618     1 NRYPHVLPYDHSRVRLSQLGGEPHSDYINANFIPGYTSPQEFIATQGPLKKTIEDFWRLVWEQQVCNIIMLTVGMENGRV 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158303304 1258 LCEHYWPVNSTPVTHGHITTHLLAEESEDEWTRREFQLQHGAEQKQRRVKQLQFTTWPDHSVPEAPSSLLAFVELVQEEV 1337
Cdd:cd14618    81 LCDHYWPSESTPVSYGHITVHLLAQSSEDEWTRREFKLWHEDLRKERRVKHLHYTAWPDHGIPESTSSLMAFRELVREHV 160

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158303304 1338 KATQGKGPILVHCSAGVGRTGTFVALLRLLRQLEEEQVVDVFNTVYILRLHRPLMIQTLSQYIFLHSCLL 1407
Cdd:cd14618   161 QATKGKGPTLVHCSAGVGRSGTFIALDRLLRQLKEEKVVDVFNTVYILRMHRYLMIQTLSQYIFLHSCIL 230
PTPc smart00194
Protein tyrosine phosphatase, catalytic domain;
1150-1408 1.24e-105

Protein tyrosine phosphatase, catalytic domain;


Pssm-ID: 214550 [Multi-domain]  Cd Length: 259  Bit Score: 337.71  E-value: 1.24e-105
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158303304   1150 FFQEFEELKEVGK-DQPRLEAEHPANITKNRYPHVLPYDHSRVRLTQLSGEPhSDYINANFIPGYSHPQEIIATQGPLKK 1228
Cdd:smart00194    2 LEEEFEKLDRLKPdDESCTVAAFPENRDKNRYKDVLPYDHTRVKLKPPPGEG-SDYINASYIDGPNGPKAYIATQGPLPS 80

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158303304   1229 TLEDFWRLVWEQQVHVIIMLTVGMENGRVLCEHYWPVN-STPVTHGHITTHLLAEESEDEWTRREFQLQHGAEQKQRRVK 1307
Cdd:smart00194   81 TVEDFWRMVWEQKVTVIVMLTELVEKGREKCAQYWPDEeGEPLTYGDITVTLKSVEKVDDYTIRTLEVTNTGCSETRTVT 160

                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158303304   1308 QLQFTTWPDHSVPEAPSSLLAFVELVqEEVKATQgKGPILVHCSAGVGRTGTFVALLRLLRQLEEEQVVDVFNTVYILRL 1387
Cdd:smart00194  161 HYHYTNWPDHGVPESPESILDLIRAV-RKSQSTS-TGPIVVHCSAGVGRTGTFIAIDILLQQLEAGKEVDIFEIVKELRS 238

                           250       260
                    ....*....|....*....|.
gi 158303304   1388 HRPLMIQTLSQYIFLHSCLLN 1408
Cdd:smart00194  239 QRPGMVQTEEQYIFLYRAILE 259
Y_phosphatase pfam00102
Protein-tyrosine phosphatase;
1174-1408 4.68e-100

Protein-tyrosine phosphatase;


Pssm-ID: 459674 [Multi-domain]  Cd Length: 234  Bit Score: 320.73  E-value: 4.68e-100
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158303304  1174 NITKNRYPHVLPYDHSRVRLTqlSGEPHSDYINANFIPGYSHPQEIIATQGPLKKTLEDFWRLVWEQQVHVIIMLTVGME 1253
Cdd:pfam00102    1 NLEKNRYKDVLPYDHTRVKLT--GDPGPSDYINASYIDGYKKPKKYIATQGPLPNTVEDFWRMVWEEKVTIIVMLTELEE 78

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158303304  1254 NGRVLCEHYWP-VNSTPVTHGHITTHLLAEES-EDEWTRREFQLQHGAEQKQRRVKQLQFTTWPDHSVPEAPSSLLAFVE 1331
Cdd:pfam00102   79 KGREKCAQYWPeEEGESLEYGDFTVTLKKEKEdEKDYTVRTLEVSNGGSEETRTVKHFHYTGWPDHGVPESPNSLLDLLR 158

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 158303304  1332 LVqEEVKATQGKGPILVHCSAGVGRTGTFVALLRLLRQLEEEQVVDVFNTVYILRLHRPLMIQTLSQYIFLHSCLLN 1408
Cdd:pfam00102  159 KV-RKSSLDGRSGPIVVHCSAGIGRTGTFIAIDIALQQLEAEGEVDIFQIVKELRSQRPGMVQTLEQYIFLYDAILE 234
PTP_tm pfam18861
TM proximal of protein tyrosine phosphatase, receptor type J; Protein tyrosine phosphatases ...
 948-1069 8.65e-50

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: 172.41  E-value: 8.65e-50
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158303304   948 VTRGMFGKDDGQIQWYGIIATINMTLAQPSQEAINHTWYDHYYRGHDSYLALLFPNPFYPePWAVPRSWTVPVGTEDCdn 1027
Cdd:pfam18861    1 IQFSLFNSSNGPIKAYGVIVTTNDSLNRPLKEYLNKTYYDWKYKKTDSYLATVTPNPFTS-PRSSSRSLTVPVGTGSK-- 77

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*....
gi 158303304  1028 TQEICNGHLKPGFQYRFSIAAFSRL-------SSPETILAFSAFSEPQA 1069
Cdd:pfam18861   78 WQGYCNGPLKPLGSYRFSVAAFTRLefddgliDGEESYVSFTPFSEPIA 126
PHA02738 PHA02738
hypothetical protein; Provisional
 1170-1401 9.90e-39

hypothetical protein; Provisional


Pssm-ID: 222923 [Multi-domain]  Cd Length: 320  Bit Score: 148.15  E-value: 9.90e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158303304 1170 EHPANITKNRYPHVLPYDHSRVRLTqlSGEPHSDYINANFIPGYSHPQEIIATQGPLKKTLEDFWRLVWEQQVHVIIMLT 1249
Cdd:PHA02738   45 AEKKNRKLNRYLDAVCFDHSRVILP--AERNRGDYINANYVDGFEYKKKFICGQAPTRQTCYDFYRMLWMEHVQIIVMLC 122

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158303304 1250 VGMENGRVLCEHYWP-VNSTPVTHGHITTHLLAEESEDEWTRREFQLQHGAEQKQrRVKQLQFTTWPDHSVPEAPSSLLA 1328
Cdd:PHA02738  123 KKKENGREKCFPYWSdVEQGSIRFGKFKITTTQVETHPHYVKSTLLLTDGTSATQ-TVTHFNFTAWPDHDVPKNTSEFLN 201

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158303304 1329 FV--------ELVQEEVKATQGKG---PILVHCSAGVGRTGTFVALLRLLRQLEEEQVVDVFNTVYILRLHRPLMIQTLS 1397
Cdd:PHA02738  202 FVlevrqcqkELAQESLQIGHNRLqppPIVVHCNAGLGRTPCYCVVDISISRFDACATVSIPSIVSSIRNQRYYSLFIPF 281


                  ....
gi 158303304 1398 QYIF 1401
Cdd:PHA02738  282 QYFF 285
COG5599 COG5599
Protein tyrosine phosphatase [Signal transduction mechanisms];
1148-1402 9.27e-36

Protein tyrosine phosphatase [Signal transduction mechanisms];


Pssm-ID: 444335 [Multi-domain]  Cd Length: 282  Bit Score: 137.92  E-value: 9.27e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158303304 1148 QAFFQEFEELKEVGKDQpRLEAEHPANIT---KNRYPHVLPYDHSRVRltqlsgePHSDYINANFIPGYShPQEIIATQG 1224
Cdd:COG5599    14 EKINSRLSTLTNELAPS-HNDPQYLQNINgspLNRFRDIQPYKETALR-------ANLGYLNANYIQVIG-NHRYIATQY 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158303304 1225 PLKKTLEDFWRLVWEQQVHVIIMLT--VGMENGRVLCEHYWPVNSTpvtHGHITTHLLAEESE---DEWTRREFQL-QHG 1298
Cdd:COG5599    85 PLEEQLEDFFQMLFDNNTPVLVVLAsdDEISKPKVKMPVYFRQDGE---YGKYEVSSELTESIqlrDGIEARTYVLtIKG 161

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158303304 1299 AEQKQRRVKQLQFTTWPDHSVPEApSSLLAFVELV-QEEVKATQGKGPILVHCSAGVGRTGTFVALL--RLLRQLEEEQV 1375
Cdd:COG5599   162 TGQKKIEIPVLHVKNWPDHGAISA-EALKNLADLIdKKEKIKDPDKLLPVVHCRAGVGRTGTLIACLalSKSINALVQIT 240

                         250       260
                  ....*....|....*....|....*...
gi 158303304 1376 VDVFNTVYILRLHR-PLMIQTLSQYIFL 1402
Cdd:COG5599   241 LSVEEIVIDMRTSRnGGMVQTSEQLDVL 268
R-PTPc-V cd14618
catalytic domain of receptor-type tyrosine-protein phosphatase V; Receptor-type ...
 1477-1692 1.28e-20

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: 92.70  E-value: 1.28e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158303304 1477 HSQEQLALVEESPADNMLAASLFPGGPSGRDHVVltgSAGP-----KELWEMVWEHGAYVLVSL--GLPDTKEKPQDIWP 1549
Cdd:cd14618    11 HSRVRLSQLGGEPHSDYINANFIPGYTSPQEFIA---TQGPlkktiEDFWRLVWEQQVCNIIMLtvGMENGRVLCDHYWP 87

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158303304 1550 MEMQPIVTDMVTVHRVAESNTAGWPSTLIRVIHGDSGTERQVQCLQFPHCETGS--ELPAnTLLTFLDAVGQCCSrgNSK 1627
Cdd:cd14618    88 SESTPVSYGHITVHLLAQSSEDEWTRREFKLWHEDLRKERRVKHLHYTAWPDHGipESTS-SLMAFRELVREHVQ--ATK 164

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 158303304 1628 KPGTLLSHSSKVTNQLSTFLAMEQLLQQAGTERTVDVFSVALKQTQACGLKTPTLEQYIYLYNCL 1692
Cdd:cd14618   165 GKGPTLVHCSAGVGRSGTFIALDRLLRQLKEEKVVDVFNTVYILRMHRYLMIQTLSQYIFLHSCI 229
PTPc smart00194
Protein tyrosine phosphatase, catalytic domain;
1521-1692 8.20e-14

Protein tyrosine phosphatase, catalytic domain;


Pssm-ID: 214550 [Multi-domain]  Cd Length: 259  Bit Score: 73.46  E-value: 8.20e-14
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158303304   1521 WEMVWEHGAYVLVSLGLPD--TKEKPQDIWPMEM-QPIVTDMVTVHRVAESNTAGWPSTLIRVIHGDSGTERQVQCLQF- 1596
Cdd:smart00194   86 WRMVWEQKVTVIVMLTELVekGREKCAQYWPDEEgEPLTYGDITVTLKSVEKVDDYTIRTLEVTNTGCSETRTVTHYHYt 165

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158303304   1597 --PHCETgselPANT--LLTFLDAVGQCCSRGNskkpGTLLSHSSKVTNQLSTFLAMEQLLQQAGTERTVDVFSVALK-Q 1671
Cdd:smart00194  166 nwPDHGV----PESPesILDLIRAVRKSQSTST----GPIVVHCSAGVGRTGTFIAIDILLQQLEAGKEVDIFEIVKElR 237

                           170       180
                    ....*....|....*....|.
gi 158303304   1672 TQACGLkTPTLEQYIYLYNCL 1692
Cdd:smart00194  238 SQRPGM-VQTEEQYIFLYRAI 257
Y_phosphatase pfam00102
Protein-tyrosine phosphatase;
1518-1692 9.82e-13

Protein-tyrosine phosphatase;


Pssm-ID: 459674 [Multi-domain]  Cd Length: 234  Bit Score: 69.58  E-value: 9.82e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158303304  1518 KELWEMVWEHGAYVLVSLGLPD--TKEKPQDIWPMEM-QPIVTDMVTVH-RVAESNTAGWPSTLIRVIHGDSGTERQVQC 1593
Cdd:pfam00102   56 EDFWRMVWEEKVTIIVMLTELEekGREKCAQYWPEEEgESLEYGDFTVTlKKEKEDEKDYTVRTLEVSNGGSEETRTVKH 135

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158303304  1594 LQF---PHCETgselPANT--LLTFLDAVGQCCSRGNSkkpGTLLSHSSKVTNQLSTFLAMEQLLQQAGTERTVDVFSVA 1668
Cdd:pfam00102  136 FHYtgwPDHGV----PESPnsLLDLLRKVRKSSLDGRS---GPIVVHCSAGIGRTGTFIAIDIALQQLEAEGEVDIFQIV 208

                          170       180
                   ....*....|....*....|....*
gi 158303304  1669 LK-QTQACGLKTpTLEQYIYLYNCL 1692
Cdd:pfam00102  209 KElRSQRPGMVQ-TLEQYIFLYDAI 232
FN3 COG3401
Fibronectin type 3 domain [General function prediction only];
378-749 5.69e-11

Fibronectin type 3 domain [General function prediction only];


Pssm-ID: 442628 [Multi-domain]  Cd Length: 603  Bit Score: 67.33  E-value: 5.69e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158303304  378 YDAWVEGSIWLAESAARPMEVPGARLWLEGLEATKQPGRRALLYSVDAPGLLGNISVSSGATHV-TFCGLVPGAHYRVDI 456
Cdd:COG3401    42 VVLSVTTKESPGTLLVAAGLSSGGGLGTGGRAGTTSGVAAVAVAAAPPTATGLTTLTGSGSVGGaTNTGLTSSDEVPSPA 121

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158303304  457 ASSMGDITQSLTGYTSPLPPQSLEIISRNSPSDLTIGWAPAPGQMEGYKVTWHqDGSQRSPGDLVDLGPDISSLTLKSLV 536
Cdd:COG3401   122 VGTATTATAVAGGAATAGTYALGAGLYGVDGANASGTTASSVAGAGVVVSPDT-SATAAVATTSLTVTSTTLVDGGGDIE 200

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158303304  537 PGSCYTVSAWAW-SGNLSSDSQKIH---SCTRPAPPTNLSlGFAHQPATLRASWcHPPGGRDAFQLRLYRlRPLTLESEK 612
Cdd:COG3401   201 PGTTYYYRVAATdTGGESAPSNEVSvttPTTPPSAPTGLT-ATADTPGSVTLSW-DPVTESDATGYRVYR-SNSGDGPFT 277

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158303304  613 ILSQEAQN-FSWAQLPAG--YEFQVQLSTLWGsEESGSAN----TTGWTPPSAPTLVNVTSEAPTQLHVSWVHAAG-DRS 684
Cdd:COG3401   278 KVATVTTTsYTDTGLTNGttYYYRVTAVDAAG-NESAPSNvvsvTTDLTPPAAPSGLTATAVGSSSITLSWTASSDaDVT 356

                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 158303304  685 SYQVtLYQESTRTATSIVGPKADSTSFW--GLTPGTK--YKVEAISWAGPLYTAAANVSAWTYPLTPNE 749
Cdd:COG3401   357 GYNV-YRSTSGGGTYTKIAETVTTTSYTdtGLTPGTTyyYKVTAVDAAGNESAPSEEVSATTASAASGE 424
FN3 cd00063
Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein ...
 656-730 3.46e-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: 49.80  E-value: 3.46e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158303304  656 PSAPTLVNVTSEAPTQLHVSWVHAAGDRS---SYQVTLYQESTRTATSIVGPKADSTSF--WGLTPGTKY--KVEAISWA 728
Cdd:cd00063     1 PSPPTNLRVTDVTSTSVTLSWTPPEDDGGpitGYVVEYREKGSGDWKEVEVTPGSETSYtlTGLKPGTEYefRVRAVNGG 80


                  ..
gi 158303304  729 GP 730
Cdd:cd00063    81 GE 82
FN3 smart00060
Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, ...
 656-730 2.28e-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: 47.22  E-value: 2.28e-06
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158303304    656 PSAPTLVNVTSEAPTQLHVSWVHAAGDRS-----SYQVTLYQESTRTATSIVGPKADSTSFWGLTPGTKY--KVEAISWA 728
Cdd:smart00060    1 PSPPSNLRVTDVTSTSVTLSWEPPPDDGItgyivGYRVEYREEGSEWKEVNVTPSSTSYTLTGLKPGTEYefRVRAVNGA 80


                    ..
gi 158303304    729 GP 730
Cdd:smart00060   81 GE 82
PHA02746 PHA02746
protein tyrosine phosphatase; Provisional
 1516-1696 6.78e-06

protein tyrosine phosphatase; Provisional


Pssm-ID: 165113 [Multi-domain]  Cd Length: 323  Bit Score: 50.03  E-value: 6.78e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158303304 1516 GPKE-----LWEMVWEHGAYVLVSLG-LPDTKEKPQDIWPMEMQPIVTDMVTVHRVAE-SNTAGWPSTLIRVIHGDSGTE 1588
Cdd:PHA02746  120 GPKEdtsedFFKLISEHESQVIVSLTdIDDDDEKCFELWTKEEDSELAFGRFVAKILDiIEELSFTKTRLMITDKISDTS 199

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158303304 1589 RQVQCLQFPHCETGSeLPAN--TLLTFLDAVGQCCSR------GNSKKPGTLLSHSSKVTNQLSTFLAMEQLLQQAGTER 1660
Cdd:PHA02746  200 REIHHFWFPDWPDNG-IPTGmaEFLELINKVNEEQAElikqadNDPQTLGPIVVHCSAGIGRAGTFCAIDNALEQLEKEK 278

                         170       180       190
                  ....*....|....*....|....*....|....*.
gi 158303304 1661 TVDVFSVALKQTQACGLKTPTLEQYIYLYNCLNSAL 1696
Cdd:PHA02746  279 EVCLGEIVLKIRKQRHSSVFLPEQYAFCYKALKYAI 314
fn3 pfam00041
Fibronectin type III domain;
657-722 1.03e-05

Fibronectin type III domain;


Pssm-ID: 394996 [Multi-domain]  Cd Length: 85  Bit Score: 45.48  E-value: 1.03e-05
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 158303304   657 SAPTLVNVTSEAPTQLHVSWVHAA---GDRSSYQVTLYQEST--RTATSIVGPKADSTSFWGLTPGTKYKV 722
Cdd:pfam00041    1 SAPSNLTVTDVTSTSLTVSWTPPPdgnGPITGYEVEYRPKNSgePWNEITVPGTTTSVTLTGLKPGTEYEV 71
FN3 smart00060
Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, ...
 36-110 2.03e-04

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: 41.83  E-value: 2.03e-04
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 158303304     36 GPPLSVNVSSRGkPTSLFLSWVA-AEPGGFDYALCLRAMNLSGFPEGQQLQAHTNESSFEFHGLVPGSRYQLELTV 110
Cdd:smart00060    2 SPPSNLRVTDVT-STSVTLSWEPpPDDGITGYIVGYRVEYREEGSEWKEVNVTPSSTSYTLTGLKPGTEYEFRVRA 76
fn3 pfam00041
Fibronectin type III domain;
131-201 2.60e-04

Fibronectin type III domain;


Pssm-ID: 394996 [Multi-domain]  Cd Length: 85  Bit Score: 41.25  E-value: 2.60e-04
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 158303304   131 VRGLQLHSTGSpASLEASWS---DASGDQDSYQLLlYHPESHTLACN-VSVSPDTLSYNFGDLLPGSQYVLEVIT 201
Cdd:pfam00041    3 PSNLTVTDVTS-TSLTVSWTpppDGNGPITGYEVE-YRPKNSGEPWNeITVPGTTTSVTLTGLKPGTEYEVRVQA 75
fn3 pfam00041
Fibronectin type III domain;
36-109 7.64e-04

Fibronectin type III domain;


Pssm-ID: 394996 [Multi-domain]  Cd Length: 85  Bit Score: 40.09  E-value: 7.64e-04
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 158303304    36 GPPLSVNVSSRGkPTSLFLSWVAAEPGG---FDYALCLRAMNLSGfpEGQQLQAHTNESSFEFHGLVPGSRYQLELT 109
Cdd:pfam00041    1 SAPSNLTVTDVT-STSLTVSWTPPPDGNgpiTGYEVEYRPKNSGE--PWNEITVPGTTTSVTLTGLKPGTEYEVRVQ 74
 
Name Accession Description Interval E-value
R-PTPc-V cd14618
catalytic domain of receptor-type tyrosine-protein phosphatase V; Receptor-type ...
 1178-1407 8.97e-155

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: 471.73  E-value: 8.97e-155
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158303304 1178 NRYPHVLPYDHSRVRLTQLSGEPHSDYINANFIPGYSHPQEIIATQGPLKKTLEDFWRLVWEQQVHVIIMLTVGMENGRV 1257
Cdd:cd14618     1 NRYPHVLPYDHSRVRLSQLGGEPHSDYINANFIPGYTSPQEFIATQGPLKKTIEDFWRLVWEQQVCNIIMLTVGMENGRV 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158303304 1258 LCEHYWPVNSTPVTHGHITTHLLAEESEDEWTRREFQLQHGAEQKQRRVKQLQFTTWPDHSVPEAPSSLLAFVELVQEEV 1337
Cdd:cd14618    81 LCDHYWPSESTPVSYGHITVHLLAQSSEDEWTRREFKLWHEDLRKERRVKHLHYTAWPDHGIPESTSSLMAFRELVREHV 160

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158303304 1338 KATQGKGPILVHCSAGVGRTGTFVALLRLLRQLEEEQVVDVFNTVYILRLHRPLMIQTLSQYIFLHSCLL 1407
Cdd:cd14618   161 QATKGKGPTLVHCSAGVGRSGTFIALDRLLRQLKEEKVVDVFNTVYILRMHRYLMIQTLSQYIFLHSCIL 230
R3-PTPc cd14548
catalytic domain of R3 subfamily receptor-type tyrosine-protein phosphatases and similar ...
 1179-1404 1.59e-125

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: 391.72  E-value: 1.59e-125
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158303304 1179 RYPHVLPYDHSRVRLTQLSGEPHSDYINANFIPGYSHPQEIIATQGPLKKTLEDFWRLVWEQQVHVIIMLTVGMENGRVL 1258
Cdd:cd14548     1 RYTNILPYDHSRVKLIPINEEEGSDYINANYIPGYNSPREFIATQGPLPGTKDDFWRMVWEQNSHTIVMLTQCMEKGRVK 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158303304 1259 CEHYWPVNSTPVTHGHITTHLLAEESEDEWTRREFQLQHGaeQKQRRVKQLQFTTWPDHSVPEAPSSLLAFVELVQEEVK 1338
Cdd:cd14548    81 CDHYWPFDQDPVYYGDITVTMLSESVLPDWTIREFKLERG--DEVRSVRQFHFTAWPDHGVPEAPDSLLRFVRLVRDYIK 158

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 158303304 1339 atQGKGPILVHCSAGVGRTGTFVALLRLLRQLEEEQVVDVFNTVYILRLHRPLMIQTLSQYIFLHS 1404
Cdd:cd14548   159 --QEKGPTIVHCSAGVGRTGTFIALDRLLQQIESEDYVDIFGIVYDLRKHRPLMVQTEAQYIFLHQ 222
PTPc smart00194
Protein tyrosine phosphatase, catalytic domain;
1150-1408 1.24e-105

Protein tyrosine phosphatase, catalytic domain;


Pssm-ID: 214550 [Multi-domain]  Cd Length: 259  Bit Score: 337.71  E-value: 1.24e-105
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158303304   1150 FFQEFEELKEVGK-DQPRLEAEHPANITKNRYPHVLPYDHSRVRLTQLSGEPhSDYINANFIPGYSHPQEIIATQGPLKK 1228
Cdd:smart00194    2 LEEEFEKLDRLKPdDESCTVAAFPENRDKNRYKDVLPYDHTRVKLKPPPGEG-SDYINASYIDGPNGPKAYIATQGPLPS 80

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158303304   1229 TLEDFWRLVWEQQVHVIIMLTVGMENGRVLCEHYWPVN-STPVTHGHITTHLLAEESEDEWTRREFQLQHGAEQKQRRVK 1307
Cdd:smart00194   81 TVEDFWRMVWEQKVTVIVMLTELVEKGREKCAQYWPDEeGEPLTYGDITVTLKSVEKVDDYTIRTLEVTNTGCSETRTVT 160

                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158303304   1308 QLQFTTWPDHSVPEAPSSLLAFVELVqEEVKATQgKGPILVHCSAGVGRTGTFVALLRLLRQLEEEQVVDVFNTVYILRL 1387
Cdd:smart00194  161 HYHYTNWPDHGVPESPESILDLIRAV-RKSQSTS-TGPIVVHCSAGVGRTGTFIAIDILLQQLEAGKEVDIFEIVKELRS 238

                           250       260
                    ....*....|....*....|.
gi 158303304   1388 HRPLMIQTLSQYIFLHSCLLN 1408
Cdd:smart00194  239 QRPGMVQTEEQYIFLYRAILE 259
Y_phosphatase pfam00102
Protein-tyrosine phosphatase;
1174-1408 4.68e-100

Protein-tyrosine phosphatase;


Pssm-ID: 459674 [Multi-domain]  Cd Length: 234  Bit Score: 320.73  E-value: 4.68e-100
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158303304  1174 NITKNRYPHVLPYDHSRVRLTqlSGEPHSDYINANFIPGYSHPQEIIATQGPLKKTLEDFWRLVWEQQVHVIIMLTVGME 1253
Cdd:pfam00102    1 NLEKNRYKDVLPYDHTRVKLT--GDPGPSDYINASYIDGYKKPKKYIATQGPLPNTVEDFWRMVWEEKVTIIVMLTELEE 78

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158303304  1254 NGRVLCEHYWP-VNSTPVTHGHITTHLLAEES-EDEWTRREFQLQHGAEQKQRRVKQLQFTTWPDHSVPEAPSSLLAFVE 1331
Cdd:pfam00102   79 KGREKCAQYWPeEEGESLEYGDFTVTLKKEKEdEKDYTVRTLEVSNGGSEETRTVKHFHYTGWPDHGVPESPNSLLDLLR 158

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 158303304  1332 LVqEEVKATQGKGPILVHCSAGVGRTGTFVALLRLLRQLEEEQVVDVFNTVYILRLHRPLMIQTLSQYIFLHSCLLN 1408
Cdd:pfam00102  159 KV-RKSSLDGRSGPIVVHCSAGIGRTGTFIAIDIALQQLEAEGEVDIFQIVKELRSQRPGMVQTLEQYIFLYDAILE 234
R-PTPc-H cd14619
catalytic domain of receptor-type tyrosine-protein phosphatase H; Receptor-type ...
 1178-1410 8.47e-92

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: 297.19  E-value: 8.47e-92
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158303304 1178 NRYPHVLPYDHSRVRLTQLSGEPHSDYINANFIPGYSHPQEIIATQGPLKKTLEDFWRLVWEQQVHVIIMLTVGMENGRV 1257
Cdd:cd14619     1 NRFRNVLPYDWSRVPLKPIHEEPGSDYINANYMPGYWSSQEFIATQGPLPQTVGDFWRMIWEQQSSTIVMLTNCMEAGRV 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158303304 1258 LCEHYWPVNSTPVTHGHITTHLLAEESEDEWTRREFQLQHGAEQKQRRVKQLQFTTWPDHSVPEAPSSLLAFVELVQEEV 1337
Cdd:cd14619    81 KCEHYWPLDYTPCTYGHLRVTVVSEEVMENWTVREFLLKQVEEQKTLSVRHFHFTAWPDHGVPSSTDTLLAFRRLLRQWL 160

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 158303304 1338 KATQGKGPILVHCSAGVGRTGTFVALLRLLRQLEEEQVVDVFNTVYILRLHRPLMIQTLSQYIFLHSCLLNKI 1410
Cdd:cd14619   161 DQTMSGGPTVVHCSAGVGRTGTLIALDVLLQQLQSEGLLGPFSFVQKMRENRPLMVQTESQYVFLHQCILDFL 233
R-PTPc-J cd14615
catalytic domain of receptor-type tyrosine-protein phosphatase J; Receptor-type ...
 1178-1408 3.06e-88

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: 287.10  E-value: 3.06e-88
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158303304 1178 NRYPHVLPYDHSRVRLTQLSgEPHSDYINANFIPGYSHPQEIIATQGPLKKTLEDFWRLVWEQQVHVIIMLTVGMENGRV 1257
Cdd:cd14615     1 NRYNNVLPYDISRVKLSVQS-HSTDDYINANYMPGYNSKKEFIAAQGPLPNTVKDFWRMVWEKNVYAIVMLTKCVEQGRT 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158303304 1258 LCEHYWPvNSTPVTHGHITTHLLAEESEDEWTRREFQLQHGAEQKQRRVKQLQFTTWPDHSVPEAPSSLLAFVELVQEEV 1337
Cdd:cd14615    80 KCEEYWP-SKQKKDYGDITVTMTSEIVLPEWTIRDFTVKNAQTNESRTVRHFHFTSWPDHGVPETTDLLINFRHLVREYM 158

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 158303304 1338 KATQGKGPILVHCSAGVGRTGTFVALLRLLRQLEEEQVVDVFNTVYILRLHRPLMIQTLSQYIFLHSCLLN 1408
Cdd:cd14615   159 KQNPPNSPILVHCSAGVGRTGTFIAIDRLIYQIENENVVDVYGIVYDLRMHRPLMVQTEDQYVFLNQCALD 229
R-PTPc-O cd14614
catalytic domain of receptor-type tyrosine-protein phosphatase O; Receptor-type ...
 1163-1407 8.73e-85

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: 277.93  E-value: 8.73e-85
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158303304 1163 DQPRLEAEHPANITKNRYPHVLPYDHSRVRLTQLSGEPHSDYINANFIPGYSHPQEIIATQGPLKKTLEDFWRLVWEQQV 1242
Cdd:cd14614     1 DIPHFAADLPVNRCKNRYTNILPYDFSRVKLVSMHEEEGSDYINANYIPGYNSPQEYIATQGPLPETRNDFWKMVLQQKS 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158303304 1243 HVIIMLTVGMENGRVLCEHYWPVNSTPVTHGHITTHLLAEESEDEWTRREFQLQHGAEQKqrRVKQLQFTTWPDHSVP-- 1320
Cdd:cd14614    81 QIIVMLTQCNEKRRVKCDHYWPFTEEPVAYGDITVEMLSEEEQPDWAIREFRVSYADEVQ--DVMHFNYTAWPDHGVPta 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158303304 1321 EAPSSLLAFVELVQEevKATQGKGPILVHCSAGVGRTGTFVALLRLLRQLEEEQVVDVFNTVYILRLHRPLMIQTLSQYI 1400
Cdd:cd14614   159 NAAESILQFVQMVRQ--QAVKSKGPMIIHCSAGVGRTGTFIALDRLLQHIRDHEFVDILGLVSEMRSYRMSMVQTEEQYI 236


                  ....*..
gi 158303304 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 1.07e-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: 266.84  E-value: 1.07e-81
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158303304 1204 YINANFIPGYSHPQEIIATQGPLKKTLEDFWRLVWEQQVHVIIMLTVGMENGRVLCEHYWPVN-STPVTHGHITTHLLAE 1282
Cdd:cd00047     1 YINASYIDGYRGPKEYIATQGPLPNTVEDFWRMVWEQKVSVIVMLTNLVEKGREKCERYWPEEgGKPLEYGDITVTLVSE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158303304 1283 ESEDEWTRREFQLQHGAEQKQRRVKQLQFTTWPDHSVPEAPSSLLAFVELVQEEVKatQGKGPILVHCSAGVGRTGTFVA 1362
Cdd:cd00047    81 EELSDYTIRTLELSPKGCSESREVTHLHYTGWPDHGVPSSPEDLLALVRRVRKEAR--KPNGPIVVHCSAGVGRTGTFIA 158

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|.
gi 158303304 1363 LLRLLRQLEEEQVVDVFNTVYILRLHRPLMIQTLSQYIFLH 1403
Cdd:cd00047   159 IDILLERLEAEGEVDVFEIVKALRKQRPGMVQTLEQYEFIY 199
R-PTPc-LAR-1 cd14553
catalytic domain of LAR family receptor-type tyrosine-protein phosphatases, repeat 1; The LAR ...
 1172-1410 1.78e-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: 265.03  E-value: 1.78e-80
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158303304 1172 PANITKNRYPHVLPYDHSRVRLTQLSGEPHSDYINANFIPGYSHPQEIIATQGPLKKTLEDFWRLVWEQQVHVIIMLTVG 1251
Cdd:cd14553     1 EVNKPKNRYANVIAYDHSRVILQPIEGVPGSDYINANYCDGYRKQNAYIATQGPLPETFGDFWRMVWEQRSATIVMMTKL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158303304 1252 MENGRVLCEHYWPVNSTPvTHGHITTHLLAEESEDEWTRREFQLQHGAEQKQRRVKQLQFTTWPDHSVPEAPSSLLAFVe 1331
Cdd:cd14553    81 EERSRVKCDQYWPTRGTE-TYGLIQVTLLDTVELATYTVRTFALHKNGSSEKREVRQFQFTAWPDHGVPEHPTPFLAFL- 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158303304 1332 lvqEEVKA--TQGKGPILVHCSAGVGRTGTFVALLRLLRQLEEEQVVDVFNTVYILRLHRPLMIQTLSQYIFLHSCLLNK 1409
Cdd:cd14553   159 ---RRVKAcnPPDAGPIVVHCSAGVGRTGCFIVIDSMLERIKHEKTVDIYGHVTCLRAQRNYMVQTEDQYIFIHDALLEA 235


                  .
gi 158303304 1410 I 1410
Cdd:cd14553   236 V 236
R-PTPc-B cd14617
catalytic domain of receptor-type tyrosine-protein phosphatase B; Receptor-type ...
 1178-1403 3.32e-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: 264.09  E-value: 3.32e-80
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158303304 1178 NRYPHVLPYDHSRVRLTQLSGEPHSDYINANFIPGYSHPQEIIATQGPLKKTLEDFWRLVWEQQVHVIIMLTVGMENGRV 1257
Cdd:cd14617     1 NRYNNILPYDSTRVKLSNVDDDPCSDYINASYIPGNNFRREYIATQGPLPGTKDDFWKMVWEQNVHNIVMVTQCVEKGRV 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158303304 1258 LCEHYWPVNSTPVTHGHITTHLLAEESEDEWTRREFQLQhGAEQ--KQRRVKQLQFTTWPDHSVPEAPSSLLAFVELVQE 1335
Cdd:cd14617    81 KCDHYWPADQDSLYYGDLIVQMLSESVLPEWTIREFKIC-SEEQldAPRLVRHFHYTVWPDHGVPETTQSLIQFVRTVRD 159

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 158303304 1336 EVKATQGKGPILVHCSAGVGRTGTFVALLRLLRQLEEEQVVDVFNTVYILRLHRPLMIQTLSQYIFLH 1403
Cdd:cd14617   160 YINRTPGSGPTVVHCSAGVGRTGTFIALDRILQQLDSKDSVDIYGAVHDLRLHRVHMVQTECQYVYLH 227
PTPc-N9 cd14543
catalytic domain of tyrosine-protein phosphatase non-receptor type 9; Tyrosine-protein ...
 1154-1404 5.69e-75

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: 250.74  E-value: 5.69e-75
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158303304 1154 FEELKEVGKDQPR---LEAEHPANITKNRYPHVLPYDHSRVRLTQLSGEPHSDYINANFIPGYSHPQEIIATQGPLKKTL 1230
Cdd:cd14543     6 YEEYEDIRREPPAgtfLCSLAPANQEKNRYGDVLCLDQSRVKLPKRNGDERTDYINANFMDGYKQKNAYIATQGPLPKTY 85

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158303304 1231 EDFWRLVWEQQVHVIIMLTVGMENGRVLCEHYWPVNS-TPVTHGHIT-THLLAEESEDeWTRREFQLQHGAEQKQRRVKQ 1308
Cdd:cd14543    86 SDFWRMVWEQKVLVIVMTTRVVERGRVKCGQYWPLEEgSSLRYGDLTvTNLSVENKEH-YKKTTLEIHNTETDESRQVTH 164

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158303304 1309 LQFTTWPDHSVPEAPSSLLAFVELVQEE----VKA--TQGKG-----PILVHCSAGVGRTGTFVALLRLLRQLEEEQVVD 1377
Cdd:cd14543   165 FQFTSWPDFGVPSSAAALLDFLGEVRQQqalaVKAmgDRWKGhppgpPIVVHCSAGIGRTGTFCTLDICLSQLEDVGTLN 244

                         250       260
                  ....*....|....*....|....*..
gi 158303304 1378 VFNTVYILRLHRPLMIQTLSQYIFLHS 1404
Cdd:cd14543   245 VMQTVRRMRTQRAFSIQTPDQYYFCYK 271
R-PTPc-F-1 cd14626
catalytic domain of receptor-type tyrosine-protein phosphatase F, repeat 1; Receptor-type ...
 1150-1407 1.34e-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: 1.34e-68
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158303304 1150 FFQEFEEL---KEVGKDQPRLEAEHPanitKNRYPHVLPYDHSRVRLTQLSGEPHSDYINANFIPGYSHPQEIIATQGPL 1226
Cdd:cd14626    18 FSQEYESIdpgQQFTWENSNLEVNKP----KNRYANVIAYDHSRVILTSVDGVPGSDYINANYIDGYRKQNAYIATQGPL 93

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158303304 1227 KKTLEDFWRLVWEQQVHVIIMLTVGMENGRVLCEHYWPVNSTPvTHGHITTHLLAEESEDEWTRREFQLQHGAEQKQRRV 1306
Cdd:cd14626    94 PETLSDFWRMVWEQRTATIVMMTRLEEKSRVKCDQYWPIRGTE-TYGMIQVTLLDTVELATYSVRTFALYKNGSSEKREV 172

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158303304 1307 KQLQFTTWPDHSVPEAPSSLLAFVelvqEEVKATQ--GKGPILVHCSAGVGRTGTFVALLRLLRQLEEEQVVDVFNTVYI 1384
Cdd:cd14626   173 RQFQFMAWPDHGVPEYPTPILAFL----RRVKACNppDAGPMVVHCSAGVGRTGCFIVIDAMLERMKHEKTVDIYGHVTC 248

                         250       260
                  ....*....|....*....|...
gi 158303304 1385 LRLHRPLMIQTLSQYIFLHSCLL 1407
Cdd:cd14626   249 MRSQRNYMVQTEDQYIFIHEALL 271
R-PTPc-T-1 cd14630
catalytic domain of receptor-type tyrosine-protein phosphatase T, repeat 1; Receptor-type ...
 1174-1411 1.54e-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: 225.29  E-value: 1.54e-66
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158303304 1174 NITKNRYPHVLPYDHSRVRLTQLSGEPHSDYINANFIPGYSHPQEIIATQGPLKKTLEDFWRLVWEQQVHVIIMLTVGME 1253
Cdd:cd14630     3 NRNKNRYGNIISYDHSRVRLQLLDGDPHSDYINANYIDGYHRPRHYIATQGPMQETVKDFWRMIWQENSASVVMVTNLVE 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158303304 1254 NGRVLCEHYWPvNSTPVtHGHITTHLLAEESEDEWTRREFQLQHGAEQKQRRVKQLQFTTWPDHSVPEAPSSLLAFVElv 1333
Cdd:cd14630    83 VGRVKCVRYWP-DDTEV-YGDIKVTLIETEPLAEYVIRTFTVQKKGYHEIREIRQFHFTSWPDHGVPCYATGLLGFVR-- 158

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 158303304 1334 QEEVKATQGKGPILVHCSAGVGRTGTFVALLRLLRQLEEEQVVDVFNTVYILRLHRPLMIQTLSQYIFLHSCLLNKIL 1411
Cdd:cd14630   159 QVKFLNPPDAGPIVVHCSAGAGRTGCFIAIDIMLDMAENEGVVDIFNCVRELRAQRVNMVQTEEQYVFVHDAILEACL 236
PTPc-KIM cd14547
catalytic domain of the kinase interaction motif (KIM) family of protein-tyrosine phosphatases; ...
 1178-1403 2.65e-66

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: 223.81  E-value: 2.65e-66
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158303304 1178 NRYPHVLPYDHSRVRLTQLSGEPHSDYINANFIPGYSHPQEI-IATQGPLKKTLEDFWRLVWEQQVHVIIMLTvGMENGR 1256
Cdd:cd14547     1 NRYKTILPNEHSRVCLPSVDDDPLSSYINANYIRGYDGEEKAyIATQGPLPNTVADFWRMVWQEKTPIIVMIT-NLTEAK 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158303304 1257 VLCEHYWPVnSTPVTHGHITTHLLAEESEDEWTRREFQLQHGAEQkqRRVKQLQFTTWPDHSVPEAPSSLLAFVELVQEE 1336
Cdd:cd14547    80 EKCAQYWPE-EENETYGDFEVTVQSVKETDGYTVRKLTLKYGGEK--RYLKHYWYTSWPDHKTPEAAQPLLSLVQEVEEA 156

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 158303304 1337 VKATQGKGPILVHCSAGVGRTGTFVALLRLLRQLEEEQVVDVFNTVYILRLHRPLMIQTLSQYIFLH 1403
Cdd:cd14547   157 RQTEPHRGPIVVHCSAGIGRTGCFIATSIGCQQLREEGVVDVLGIVCQLRLDRGGMVQTAEQYEFVH 223
R5-PTPc-1 cd14549
catalytic domain of R5 subfamily receptor-type tyrosine-protein phosphatases, repeat 1; The R5 ...
 1204-1403 3.91e-66

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: 222.61  E-value: 3.91e-66
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158303304 1204 YINANFIPGYSHPQEIIATQGPLKKTLEDFWRLVWEQQVHVIIMLTVGMENGRVLCEHYWPVNSTPvTHGHITTHLLAEE 1283
Cdd:cd14549     1 YINANYVDGYNKARAYIATQGPLPSTFDDFWRMVWEQNSAIIVMITNLVERGRRKCDQYWPKEGTE-TYGNIQVTLLSTE 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158303304 1284 SEDEWTRREFQLQHGAEQK------QRRVKQLQFTTWPDHSVPEAPSSLLAFVElvqeevKATQ----GKGPILVHCSAG 1353
Cdd:cd14549    80 VLATYTVRTFSLKNLKLKKvkgrssERVVYQYHYTQWPDHGVPDYTLPVLSFVR------KSSAanppGAGPIVVHCSAG 153

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|
gi 158303304 1354 VGRTGTFVALLRLLRQLEEEQVVDVFNTVYILRLHRPLMIQTLSQYIFLH 1403
Cdd:cd14549   154 VGRTGTYIVIDSMLQQIQDKGTVNVFGFLKHIRTQRNYLVQTEEQYIFIH 203
R-PTPc-D-1 cd14624
catalytic domain of receptor-type tyrosine-protein phosphatase D, repeat 1; Receptor-type ...
 1127-1413 4.16e-65

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: 222.68  E-value: 4.16e-65
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158303304 1127 HRPIPSHSFRQSYEAKSARAHQAFFQEFEEL---KEVGKDQPRLEAEHPanitKNRYPHVLPYDHSRVRLTQLSGEPHSD 1203
Cdd:cd14624     1 HPPIPILELADHIERLKANDNLKFSQEYESIdpgQQFTWEHSNLEVNKP----KNRYANVIAYDHSRVLLSAIEGIPGSD 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158303304 1204 YINANFIPGYSHPQEIIATQGPLKKTLEDFWRLVWEQQVHVIIMLTVGMENGRVLCEHYWPVNSTPvTHGHITTHLLAEE 1283
Cdd:cd14624    77 YINANYIDGYRKQNAYIATQGALPETFGDFWRMIWEQRSATVVMMTKLEERSRVKCDQYWPSRGTE-TYGLIQVTLLDTV 155

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158303304 1284 SEDEWTRREFQLQHGAEQKQRRVKQLQFTTWPDHSVPEAPSSLLAFVELVQeeVKATQGKGPILVHCSAGVGRTGTFVAL 1363
Cdd:cd14624   156 ELATYCVRTFALYKNGSSEKREVRQFQFTAWPDHGVPEHPTPFLAFLRRVK--TCNPPDAGPMVVHCSAGVGRTGCFIVI 233

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|
gi 158303304 1364 LRLLRQLEEEQVVDVFNTVYILRLHRPLMIQTLSQYIFLHSCLLNKILEG 1413
Cdd:cd14624   234 DAMLERIKHEKTVDIYGHVTLMRAQRNYMVQTEDQYIFIHDALLEAVTCG 283
R-PTPc-G-1 cd17667
catalytic domain of receptor-type tyrosine-protein phosphatase G, repeat 1; Receptor-type ...
 1150-1411 5.26e-65

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: 222.22  E-value: 5.26e-65
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158303304 1150 FFQEFEELKEVGKDQpRLEAEH---PANITKNRYPHVLPYDHSRVRLTQLSGE--PHSDYINANFIPGYSHPQEIIATQG 1224
Cdd:cd17667     1 FSEDFEEVQRCTADM-NITAEHsnhPDNKHKNRYINILAYDHSRVKLRPLPGKdsKHSDYINANYVDGYNKAKAYIATQG 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158303304 1225 PLKKTLEDFWRLVWEQQVHVIIMLTVGMENGRVLCEHYWPVNSTPvTHGHITTHLLAEESEDEWTRREFQLQH------- 1297
Cdd:cd17667    80 PLKSTFEDFWRMIWEQNTGIIVMITNLVEKGRRKCDQYWPTENSE-EYGNIIVTLKSTKIHACYTVRRFSIRNtkvkkgq 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158303304 1298 ----GAEQKQRRVKQLQFTTWPDHSVPEAPSSLLAFVElvQEEVKATQGKGPILVHCSAGVGRTGTFVALLRLLRQLEEE 1373
Cdd:cd17667   159 kgnpKGRQNERTVIQYHYTQWPDMGVPEYALPVLTFVR--RSSAARTPEMGPVLVHCSAGVGRTGTYIVIDSMLQQIKDK 236

                         250       260       270
                  ....*....|....*....|....*....|....*...
gi 158303304 1374 QVVDVFNTVYILRLHRPLMIQTLSQYIFLHSCLLNKIL 1411
Cdd:cd17667   237 STVNVLGFLKHIRTQRNYLVQTEEQYIFIHDALLEAIL 274
R-PTPc-Q cd14616
catalytic domain of receptor-type tyrosine-protein phosphatase Q; Receptor-type ...
 1178-1403 6.53e-65

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: 219.78  E-value: 6.53e-65
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158303304 1178 NRYPHVLPYDHSRVRLTQLSGEPHSDYINANFIPGYSHPQEIIATQGPLKKTLEDFWRLVWEQQVHVIIMLTVGMENGRV 1257
Cdd:cd14616     1 NRFPNIKPYNNNRVKLIADAGVPGSDYINASYISGYLCPNEFIATQGPLPGTVGDFWRMVWETRAKTIVMLTQCFEKGRI 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158303304 1258 LCEHYWPVNSTPVT-HGHITTHLLAEESEDEWTRREFQLQ-HGaeqKQRRVKQLQFTTWPDHSVPEAPSSLLAFVELVQe 1335
Cdd:cd14616    81 RCHQYWPEDNKPVTvFGDIVITKLMEDVQIDWTIRDLKIErHG---DYMMVRQCNFTSWPEHGVPESSAPLIHFVKLVR- 156

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 158303304 1336 eVKATQGKGPILVHCSAGVGRTGTFVALLRLLRQLEEEQVVDVFNTVYILRLHRPLMIQTLSQYIFLH 1403
Cdd:cd14616   157 -ASRAHDNTPMIVHCSAGVGRTGVFIALDHLTQHINDHDFVDIYGLVAELRSERMCMVQNLAQYIFLH 223
R-PTP-LAR-2 cd14554
PTP-like domain of the LAR family receptor-type tyrosine-protein phosphatases, repeat 2; The ...
 1169-1403 1.84e-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: 219.32  E-value: 1.84e-64
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158303304 1169 AEHPANITKNRYPHVLPYDHSRVRLTQLSGEPHSDYINANFIPGYSHPQEIIATQGPLKKTLEDFWRLVWEQQVHVIIML 1248
Cdd:cd14554     1 ANLPCNKFKNRLVNILPYESTRVCLQPIRGVEGSDYINASFIDGYRQRGAYIATQGPLAETTEDFWRMLWEHNSTIIVML 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158303304 1249 TVGMENGRVLCEHYWPVNsTPVTHGHITTHLLAEESEDEWTRREFQLQHGAEQKQRRVKQLQFTTWPDHSVPEAPSSLLA 1328
Cdd:cd14554    81 TKLREMGREKCHQYWPAE-RSARYQYFVVDPMAEYNMPQYILREFKVTDARDGQSRTVRQFQFTDWPEQGVPKSGEGFID 159

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 158303304 1329 FVELVQEeVKATQGK-GPILVHCSAGVGRTGTFVALLRLLRQLEEEQVVDVFNTVYILRLHRPLMIQTLSQYIFLH 1403
Cdd:cd14554   160 FIGQVHK-TKEQFGQeGPITVHCSAGVGRTGVFITLSIVLERMRYEGVVDVFQTVKLLRTQRPAMVQTEDQYQFCY 234
R-PTPc-S-1 cd14625
catalytic domain of receptor-type tyrosine-protein phosphatase S, repeat 1; Receptor-type ...
 1127-1410 5.42e-63

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: 216.88  E-value: 5.42e-63
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158303304 1127 HRPIPSHSFRQSYEAKSARAHQAFFQEFEEL---KEVGKDQPRLEAEHPanitKNRYPHVLPYDHSRVRLTQLSGEPHSD 1203
Cdd:cd14625     1 HPPIPISELAEHTERLKANDNLKLSQEYESIdpgQQFTWEHSNLEVNKP----KNRYANVIAYDHSRVILQPIEGIMGSD 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158303304 1204 YINANFIPGYSHPQEIIATQGPLKKTLEDFWRLVWEQQVHVIIMLTVGMENGRVLCEHYWPVNSTPvTHGHITTHLLAEE 1283
Cdd:cd14625    77 YINANYIDGYRKQNAYIATQGPLPETFGDFWRMVWEQRSATVVMMTKLEEKSRIKCDQYWPSRGTE-TYGMIQVTLLDTI 155

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158303304 1284 SEDEWTRREFQLQHGAEQKQRRVKQLQFTTWPDHSVPEAPSSLLAFVELVQeeVKATQGKGPILVHCSAGVGRTGTFVAL 1363
Cdd:cd14625   156 ELATFCVRTFSLHKNGSSEKREVRQFQFTAWPDHGVPEYPTPFLAFLRRVK--TCNPPDAGPIVVHCSAGVGRTGCFIVI 233

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*..
gi 158303304 1364 LRLLRQLEEEQVVDVFNTVYILRLHRPLMIQTLSQYIFLHSCLLNKI 1410
Cdd:cd14625   234 DAMLERIKHEKTVDIYGHVTLMRSQRNYMVQTEDQYSFIHDALLEAV 280
PTP_fungal cd18533
fungal protein tyrosine phosphatases; This subfamily contains Saccharomyces cerevisiae ...
 1204-1403 3.16e-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: 211.72  E-value: 3.16e-62
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158303304 1204 YINANFI-PGYSHPQEIIATQGPLKKTLEDFWRLVWEQQVHVIIMLTVGMENGRVLCEHYWPVNSTPVTHGHITTHLLAE 1282
Cdd:cd18533     1 YINASYItLPGTSSKRYIATQGPLPATIGDFWKMIWQNNVGVIVMLTPLVENGREKCDQYWPSGEYEGEYGDLTVELVSE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158303304 1283 ESEDEW--TRREFQLQHGAEQKqRRVKQLQFTTWPDHSVPEAPSSLLAFVELVQEEVKATQGKGPILVHCSAGVGRTGTF 1360
Cdd:cd18533    81 EENDDGgfIVREFELSKEDGKV-KKVYHIQYKSWPDFGVPDSPEDLLTLIKLKRELNDSASLDPPIIVHCSAGVGRTGTF 159

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 158303304 1361 VA--------LLRLLRQLEEEQVVD-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 ...
 1149-1411 1.84e-61

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: 211.82  E-value: 1.84e-61
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158303304 1149 AFFQEFEELKEvGKDQPRLEAEHPANITKNRYPHVLPYDHSRVRLTQLSGEPHSDYINANFIPGYSHPQEIIATQGPLKK 1228
Cdd:cd14633    16 GFKEEYESFFE-GQSAPWDSAKKDENRMKNRYGNIIAYDHSRVRLQPIEGETSSDYINGNYIDGYHRPNHYIATQGPMQE 94

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158303304 1229 TLEDFWRLVWEQQVHVIIMLTVGMENGRVLCEHYWPVNSTpvTHGHITTHLLAEESEDEWTRREFQLQHGAEQKQRRVKQ 1308
Cdd:cd14633    95 TIYDFWRMVWHENTASIIMVTNLVEVGRVKCCKYWPDDTE--IYKDIKVTLIETELLAEYVIRTFAVEKRGVHEIREIRQ 172

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158303304 1309 LQFTTWPDHSVPEAPSSLLAFVELVQEevKATQGKGPILVHCSAGVGRTGTFVALLRLLRQLEEEQVVDVFNTVYILRLH 1388
Cdd:cd14633   173 FHFTGWPDHGVPYHATGLLGFVRQVKS--KSPPNAGPLVVHCSAGAGRTGCFIVIDIMLDMAEREGVVDIYNCVRELRSR 250

                         250       260
                  ....*....|....*....|...
gi 158303304 1389 RPLMIQTLSQYIFLHSCLLNKIL 1411
Cdd:cd14633   251 RVNMVQTEEQYVFIHDAILEACL 273
PTPc-N18 cd14603
catalytic domain of tyrosine-protein phosphatase non-receptor type 18; Tyrosine-protein ...
 1172-1403 2.08e-61

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: 211.61  E-value: 2.08e-61
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158303304 1172 PANITKNRYPHVLPYDHSRVRLTQLSGEPHSDYINANFIPGYSHPQEIIATQGPLKKTLEDFWRLVWEQQVHVIIMLTVG 1251
Cdd:cd14603    28 KENVKKNRYKDILPYDQTRVILSLLQEEGHSDYINANFIKGVDGSRAYIATQGPLSHTVLDFWRMIWQYGVKVILMACRE 107

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158303304 1252 MENGRVLCEHYWPVNSTPVTHGHITTHLLAEE--SEDEWTRrefQLQHGAEQKQRRVKQLQFTTWPDHSVPEAPSSLLAF 1329
Cdd:cd14603   108 IEMGKKKCERYWAQEQEPLQTGPFTITLVKEKrlNEEVILR---TLKVTFQKESRSVSHFQYMAWPDHGIPDSPDCMLAM 184

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 158303304 1330 VELVQEevKATQGKGPILVHCSAGVGRTGTFVALLRLLRQLEEEQVVD---VFNTVYILRLHRPLMIQTLSQYIFLH 1403
Cdd:cd14603   185 IELARR--LQGSGPEPLCVHCSAGCGRTGVICTVDYVRQLLLTQRIPPdfsIFDVVLEMRKQRPAAVQTEEQYEFLY 259
PTPc-N11_6 cd14544
catalytic domain of tyrosine-protein phosphatase non-receptor type 11 and type 6; ...
 1174-1403 2.97e-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: 204.62  E-value: 2.97e-59
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158303304 1174 NITKNRYPHVLPYDHSRVRLTQL-SGEPHSDYINANFI-------PGYSHPQEIIATQGPLKKTLEDFWRLVWEQQVHVI 1245
Cdd:cd14544     1 NKGKNRYKNILPFDHTRVILKDRdPNVPGSDYINANYIrnenegpTTDENAKTYIATQGCLENTVSDFWSMVWQENSRVI 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158303304 1246 IMLTVGMENGRVLCEHYWPVNSTPVTHGHITTHLLAEESEDEWTRREFQLQHGAEQK-QRRVKQLQFTTWPDHSVPEAPS 1324
Cdd:cd14544    81 VMTTKEVERGKNKCVRYWPDEGMQKQYGPYRVQNVSEHDTTDYTLRELQVSKLDQGDpIREIWHYQYLSWPDHGVPSDPG 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158303304 1325 SLLAFVELVQEEVKATQGKGPILVHCSAGVGRTGTFVALLRLLRQLEEEQV---VDVFNTVYILRLHRPLMIQTLSQYIF 1401
Cdd:cd14544   161 GVLNFLEDVNQRQESLPHAGPIVVHCSAGIGRTGTFIVIDMLLDQIKRKGLdcdIDIQKTIQMVRSQRSGMVQTEAQYKF 240


                  ..
gi 158303304 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 ...
 1125-1416 2.08e-58

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: 204.10  E-value: 2.08e-58
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158303304 1125 RTHRPIPSHSFRQSYEAKSARAHQAFFQEFEELKEVGKDQPRLEAEHPANITKNRYPHVLPYDHSRVRLTQLSGEPHSDY 1204
Cdd:cd14621     3 RKYPPLPVDKLEEEINRRMADDNKLFREEFNALPACPIQATCEAASKEENKEKNRYVNILPYDHSRVHLTPVEGVPDSDY 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158303304 1205 INANFIPGYSHPQEIIATQGPLKKTLEDFWRLVWEQQVHVIIMLTVGMENGRVLCEHYWPvNSTPVTHGHITTHLLAEES 1284
Cdd:cd14621    83 INASFINGYQEKNKFIAAQGPKEETVNDFWRMIWEQNTATIVMVTNLKERKECKCAQYWP-DQGCWTYGNIRVSVEDVTV 161

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158303304 1285 EDEWTRREFQLQH----GAEQKQRRVKQLQFTTWPDHSVPEAPSSLLAFVelvqEEVKAT--QGKGPILVHCSAGVGRTG 1358
Cdd:cd14621   162 LVDYTVRKFCIQQvgdvTNKKPQRLITQFHFTSWPDFGVPFTPIGMLKFL----KKVKNCnpQYAGAIVVHCSAGVGRTG 237

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 158303304 1359 TFVALLRLLRQLEEEQVVDVFNTVYILRLHRPLMIQTLSQYIFLHSCLLNKILEGPSD 1416
Cdd:cd14621   238 TFIVIDAMLDMMHAERKVDVYGFVSRIRAQRCQMVQTDMQYVFIYQALLEHYLYGDTE 295
R-PTP-D-2 cd14628
PTP-like domain of receptor-type tyrosine-protein phosphatase D, repeat 2; Receptor-type ...
 1153-1407 5.08e-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: 5.08e-58
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158303304 1153 EFEELKEVGKDQPR-LEAEHPANITKNRYPHVLPYDHSRVRLTQLSGEPHSDYINANFIPGYSHPQEIIATQGPLKKTLE 1231
Cdd:cd14628    30 EFKRLASSKAHTSRfISANLPCNKFKNRLVNIMPYESTRVCLQPIRGVEGSDYINASFIDGYRQQKAYIATQGPLAETTE 109

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158303304 1232 DFWRLVWEQQVHVIIMLTVGMENGRVLCEHYWPVNSTpVTHGHITTHLLAEESEDEWTRREFQLQHGAEQKQRRVKQLQF 1311
Cdd:cd14628   110 DFWRMLWEHNSTIVVMLTKLREMGREKCHQYWPAERS-ARYQYFVVDPMAEYNMPQYILREFKVTDARDGQSRTVRQFQF 188

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158303304 1312 TTWPDHSVPEAPSSLLAFVELVQEEVKATQGKGPILVHCSAGVGRTGTFVALLRLLRQLEEEQVVDVFNTVYILRLHRPL 1391
Cdd:cd14628   189 TDWPEQGVPKSGEGFIDFIGQVHKTKEQFGQDGPISVHCSAGVGRTGVFITLSIVLERMRYEGVVDIFQTVKMLRTQRPA 268

                         250
                  ....*....|....*.
gi 158303304 1392 MIQTLSQYIFLHSCLL 1407
Cdd:cd14628   269 MVQTEDQYQFCYRAAL 284
PTPc-N20_13 cd14538
catalytic domain of tyrosine-protein phosphatase non-receptor type 20 and type 13; ...
 1204-1407 9.18e-58

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: 198.75  E-value: 9.18e-58
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158303304 1204 YINANFI--PGYSHPQEIIATQGPLKKTLEDFWRLVWEQQVHVIIMLTVGMENGRVLCEHYWP--VNSTPVTHGHITTHL 1279
Cdd:cd14538     1 YINASHIriPVGGDTYHYIACQGPLPNTTGDFWQMVWEQKSEVIAMVTQDVEGGKVKCHRYWPdsLNKPLICGGRLEVSL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158303304 1280 LAEESEDEWTRREFQLQHGAEQKQRRVKQLQFTTWPDHSVPEAPSSLLAFVELvqeeVKATQGKGPILVHCSAGVGRTGT 1359
Cdd:cd14538    81 EKYQSLQDFVIRRISLRDKETGEVHHITHLNFTTWPDHGTPQSADPLLRFIRY----MRRIHNSGPIVVHCSAGIGRTGV 156

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*...
gi 158303304 1360 FVALLRLLRQLEEEQVVDVFNTVYILRLHRPLMIQTLSQYIFLHSCLL 1407
Cdd:cd14538   157 LITIDVALGLIERDLPFDIQDIVKDLREQRQGMIQTKDQYIFCYKACL 204
R-PTP-S-2 cd14627
PTP-like domain of receptor-type tyrosine-protein phosphatase S, repeat 2; Receptor-type ...
 1153-1407 1.03e-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: 201.89  E-value: 1.03e-57
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158303304 1153 EFEELKEVGKDQPR-LEAEHPANITKNRYPHVLPYDHSRVRLTQLSGEPHSDYINANFIPGYSHPQEIIATQGPLKKTLE 1231
Cdd:cd14627    31 EFKRLANSKAHTSRfISANLPCNKFKNRLVNIMPYETTRVCLQPIRGVEGSDYINASFIDGYRQQKAYIATQGPLAETTE 110

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158303304 1232 DFWRLVWEQQVHVIIMLTVGMENGRVLCEHYWPVNSTpVTHGHITTHLLAEESEDEWTRREFQLQHGAEQKQRRVKQLQF 1311
Cdd:cd14627   111 DFWRMLWENNSTIVVMLTKLREMGREKCHQYWPAERS-ARYQYFVVDPMAEYNMPQYILREFKVTDARDGQSRTVRQFQF 189

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158303304 1312 TTWPDHSVPEAPSSLLAFVELVQEEVKATQGKGPILVHCSAGVGRTGTFVALLRLLRQLEEEQVVDVFNTVYILRLHRPL 1391
Cdd:cd14627   190 TDWPEQGVPKSGEGFIDFIGQVHKTKEQFGQDGPISVHCSAGVGRTGVFITLSIVLERMRYEGVVDIFQTVKMLRTQRPA 269

                         250
                  ....*....|....*.
gi 158303304 1392 MIQTLSQYIFLHSCLL 1407
Cdd:cd14627   270 MVQTEDEYQFCYQAAL 285
R-PTPc-E-1 cd14620
catalytic domain of receptor-type tyrosine-protein phosphatase E, repeat 1; Receptor-type ...
 1180-1407 5.24e-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: 197.47  E-value: 5.24e-57
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158303304 1180 YPHVLPYDHSRVRLTQLSGEPHSDYINANFIPGYSHPQEIIATQGPLKKTLEDFWRLVWEQQVHVIIMLTVGMENGRVLC 1259
Cdd:cd14620     1 YPNILPYDHSRVILSQLDGIPCSDYINASYIDGYKEKNKFIAAQGPKQETVNDFWRMVWEQKSATIVMLTNLKERKEEKC 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158303304 1260 EHYWPvNSTPVTHGHITTHLlaeesED-----EWTRREFQLQ---HGAEQKQRRVKQLQFTTWPDHSVPEAPSSLLAFVE 1331
Cdd:cd14620    81 YQYWP-DQGCWTYGNIRVAV-----EDcvvlvDYTIRKFCIQpqlPDGCKAPRLVTQLHFTSWPDFGVPFTPIGMLKFLK 154

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 158303304 1332 LVQEEVKATqgKGPILVHCSAGVGRTGTFVALLRLLRQLEEEQVVDVFNTVYILRLHRPLMIQTLSQYIFLHSCLL 1407
Cdd:cd14620   155 KVKSVNPVH--AGPIVVHCSAGVGRTGTFIVIDAMIDMMHAEQKVDVFEFVSRIRNQRPQMVQTDMQYSFIYQALL 228
PTPc-N7 cd14612
catalytic domain of tyrosine-protein phosphatase non-receptor type 7; Tyrosine-protein ...
 1168-1406 1.19e-56

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: 196.98  E-value: 1.19e-56
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158303304 1168 EAEHPANITKNRYPHVLPYDHSRVRL-TQLSGEPHSDYINANFIPGYS-HPQEIIATQGPLKKTLEDFWRLVWEQQVHVI 1245
Cdd:cd14612     9 ELDIPGHASKDRYKTILPNPQSRVCLrRAGSQEEEGSYINANYIRGYDgKEKAYIATQGPMLNTVSDFWEMVWQEECPII 88

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158303304 1246 IMLTvGMENGRVLCEHYWPVNSTpvTHGHITTHLLAEESEDEWTRREFQLQHGAEQkqRRVKQLQFTTWPDHSVPEAPSS 1325
Cdd:cd14612    89 VMIT-KLKEKKEKCVHYWPEKEG--TYGRFEIRVQDMKECDGYTIRDLTIQLEEES--RSVKHYWFSSWPDHQTPESAGP 163

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158303304 1326 LLAFVELVQEEVKATQGKGPILVHCSAGVGRTGTFVALLRLLRQLEEEQVVDVFNTVYILRLHRPLMIQTLSQYIFLHSC 1405
Cdd:cd14612   164 LLRLVAEVEESRQTAASPGPIVVHCSAGIGRTGCFIATSIGCQQLKDTGKVDILGIVCQLRLDRGGMIQTSEQYQFLHHT 243


                  .
gi 158303304 1406 L 1406
Cdd:cd14612   244 L 244
R-PTP-C-2 cd14558
PTP-like domain of receptor-type tyrosine-protein phosphatase C, repeat 2; Receptor-type ...
 1204-1403 2.71e-56

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: 194.15  E-value: 2.71e-56
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158303304 1204 YINANFIPGYSHPQEIIATQGPLKKTLEDFWRLVWEQQVHVIIMLTVGMENGRVLCEHYWPVNSTpvTHGHITTHLLAEE 1283
Cdd:cd14558     1 YINASFIDGYWGPKSLIATQGPLPDTIADFWQMIFQKKVKVIVMLTELKEGDQEQCAQYWGDEKK--TYGDIEVELKDTE 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158303304 1284 SEDEWTRREFQLQHGAEQKQRRVKQLQFTTWPDHSVPEAPSSLLAFVELVQEEVKATQGKG----PILVHCSAGVGRTGT 1359
Cdd:cd14558    79 KSPTYTVRVFEITHLKRKDSRTVYQYQYHKWKGEELPEKPKDLVDMIKSIKQKLPYKNSKHgrsvPIVVHCSDGSSRTGI 158

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....
gi 158303304 1360 FVALLRLLRQLEEEQVVDVFNTVYILRLHRPLMIQTLSQYIFLH 1403
Cdd:cd14558   159 FCALWNLLESAETEKVVDVFQVVKALRKQRPGMVSTLEQYQFLY 202
R-PTPc-A-E-2 cd14552
catalytic domain of receptor-type tyrosine-protein phosphatase A and E, repeat 2; ...
 1204-1401 3.13e-56

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: 194.02  E-value: 3.13e-56
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158303304 1204 YINANFIPGYSHPQEIIATQGPLKKTLEDFWRLVWEQQVHVIIMLTVGMENGRVLCEHYWPVNSTpVTHGHITTHLLAEE 1283
Cdd:cd14552     1 YINASFIDGYRQKDAYIATQGPLDHTVEDFWRMIWEWKSCSIVMLTEIKERSQNKCAQYWPEDGS-VSSGDITVELKDQT 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158303304 1284 SEDEWTRREFQLQHGAEQKQRRVKQLQFTTWPDHSVPEAPSSLLAFVELVQEEVKATqGKGPILVHCSAGVGRTGTFVAL 1363
Cdd:cd14552    80 DYEDYTLRDFLVTKGKGGSTRTVRQFHFHGWPEVGIPDNGKGMIDLIAAVQKQQQQS-GNHPITVHCSAGAGRTGTFCAL 158

                         170       180       190
                  ....*....|....*....|....*....|....*...
gi 158303304 1364 LRLLRQLEEEQVVDVFNTVYILRLHRPLMIQTLSQYIF 1401
Cdd:cd14552   159 STVLERVKAEGVLDVFQVVKSLRLQRPHMVQTLEQYEF 196
PTPc-N3_4 cd14541
catalytic domain of tyrosine-protein phosphatase non-receptor type 21 and type 14; ...
 1203-1407 1.34e-55

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: 192.54  E-value: 1.34e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158303304 1203 DYINANF----IPGYSHPQEIIATQGPLKKTLEDFWRLVWEQQVHVIIMLTVGMENGRVLCEHYWPVNSTPVTHGHITTH 1278
Cdd:cd14541     1 DYINANYvnmeIPGSGIVNRYIAAQGPLPNTCADFWQMVWEQKSTLIVMLTTLVERGRVKCHQYWPDLGETMQFGNLQIT 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158303304 1279 LLAEESEDEWTRREFQLQHGAEQKQRRVKQLQFTTWPDHSVPEAPSSLLAFVELVqeeVKATQGKG-PILVHCSAGVGRT 1357
Cdd:cd14541    81 CVSEEVTPSFAFREFILTNTNTGEERHITQMQYLAWPDHGVPDDSSDFLDFVKRV---RQNRVGMVePTVVHCSAGIGRT 157

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|
gi 158303304 1358 GTFVALLRLLRQLEEEQVVDVFNTVYILRLHRPLMIQTLSQYIFLHSCLL 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 4.21e-55

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: 191.80  E-value: 4.21e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158303304 1179 RYPHVLPYDHSRVRLTQLSGEPHSDYINANFIPGYSHPQEIIATQGPLKKTLEDFWRLVWEQQVHVIIMLTVGMENGRVL 1258
Cdd:cd14623     1 RVLQIIPYEFNRVIIPVKRGEENTDYVNASFIDGYRQKDSYIASQGPLQHTIEDFWRMIWEWKSCSIVMLTELEERGQEK 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158303304 1259 CEHYWPVNSTpVTHGHITTHLLAEESEDEWTRREFQLQHGAEQKQRRVKQLQFTTWPDHSVPEAPSSLLAFVELVQEEvK 1338
Cdd:cd14623    81 CAQYWPSDGS-VSYGDITIELKKEEECESYTVRDLLVTNTRENKSRQIRQFHFHGWPEVGIPSDGKGMINIIAAVQKQ-Q 158

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 158303304 1339 ATQGKGPILVHCSAGVGRTGTFVALLRLLRQLEEEQVVDVFNTVYILRLHRPLMIQTLSQYIFLH 1403
Cdd:cd14623   159 QQSGNHPITVHCSAGAGRTGTFCALSTVLERVKAEGILDVFQTVKSLRLQRPHMVQTLEQYEFCY 223
R-PTP-F-2 cd14629
PTP-like domain of receptor-type tyrosine-protein phosphatase F, repeat 2; Receptor-type ...
 1167-1399 8.41e-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: 193.40  E-value: 8.41e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158303304 1167 LEAEHPANITKNRYPHVLPYDHSRVRLTQLSGEPHSDYINANFIPGYSHPQEIIATQGPLKKTLEDFWRLVWEQQVHVII 1246
Cdd:cd14629    46 ISANLPCNKFKNRLVNIMPYELTRVCLQPIRGVEGSDYINASFIDGYRQQKAYIATQGPLAETTEDFWRMLWEHNSTIVV 125

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158303304 1247 MLTVGMENGRVLCEHYWPVNSTpVTHGHITTHLLAEESEDEWTRREFQLQHGAEQKQRRVKQLQFTTWPDHSVPEAPSSL 1326
Cdd:cd14629   126 MLTKLREMGREKCHQYWPAERS-ARYQYFVVDPMAEYNMPQYILREFKVTDARDGQSRTIRQFQFTDWPEQGVPKTGEGF 204

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 158303304 1327 LAFVELVQEEVKATQGKGPILVHCSAGVGRTGTFVALLRLLRQLEEEQVVDVFNTVYILRLHRPLMIQTLSQY 1399
Cdd:cd14629   205 IDFIGQVHKTKEQFGQDGPITVHCSAGVGRTGVFITLSIVLERMRYEGVVDMFQTVKTLRTQRPAMVQTEDQY 277
R-PTPc-K-1 cd14631
catalytic domain of receptor-type tyrosine-protein phosphatase K, repeat 1; Receptor-type ...
 1190-1411 1.12e-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: 190.23  E-value: 1.12e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158303304 1190 RVRLTQLSGEPHSDYINANFIPGYSHPQEIIATQGPLKKTLEDFWRLVWEQQVHVIIMLTVGMENGRVLCEHYWPVNSTp 1269
Cdd:cd14631     1 RVILQPVEDDPSSDYINANYIDGYQRPSHYIATQGPVHETVYDFWRMIWQEQSACIVMVTNLVEVGRVKCYKYWPDDTE- 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158303304 1270 vTHGHITTHLLAEESEDEWTRREFQLQHGAEQKQRRVKQLQFTTWPDHSVPEAPSSLLAFVELVQeeVKATQGKGPILVH 1349
Cdd:cd14631    80 -VYGDFKVTCVEMEPLAEYVVRTFTLERRGYNEIREVKQFHFTGWPDHGVPYHATGLLSFIRRVK--LSNPPSAGPIVVH 156

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 158303304 1350 CSAGVGRTGTFVALLRLLRQLEEEQVVDVFNTVYILRLHRPLMIQTLSQYIFLHSCLLNKIL 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 1.33e-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: 189.36  E-value: 1.33e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158303304 1204 YINANFIPGYSHPQEIIATQGPLKKTLEDFWRLVWEQQVHVIIMLTVGMENGRVLCEHYWPVNSTpvTHGHITTHLLAEE 1283
Cdd:cd14555     1 YINANYIDGYHRPNHYIATQGPMQETVYDFWRMVWQENSASIVMVTNLVEVGRVKCSRYWPDDTE--VYGDIKVTLVETE 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158303304 1284 SEDEWTRREFQLQHGAEQKQRRVKQLQFTTWPDHSVPEAPSSLLAFVELVQeeVKATQGKGPILVHCSAGVGRTGTFVAL 1363
Cdd:cd14555    79 PLAEYVVRTFALERRGYHEIREVRQFHFTGWPDHGVPYHATGLLGFIRRVK--ASNPPSAGPIVVHCSAGAGRTGCYIVI 156

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*...
gi 158303304 1364 LRLLRQLEEEQVVDVFNTVYILRLHRPLMIQTLSQYIFLHSCLLNKIL 1411
Cdd:cd14555   157 DIMLDMAEREGVVDIYNCVKELRSRRVNMVQTEEQYIFIHDAILEACL 204
PTPc-N12 cd14604
catalytic domain of tyrosine-protein phosphatase non-receptor type 12; Tyrosine-protein ...
 1137-1403 4.76e-54

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: 191.68  E-value: 4.76e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158303304 1137 QSYEAKSARAHQAFFQEFEELKEVG------KDQPRLEAEHPANITKNRYPHVLPYDHSRVRLTQLSGEPHSDYINANFI 1210
Cdd:cd14604    14 QAMKSTDHNGEDNFASDFMRLRRLStkyrteKIYPTATGEKEENVKKNRYKDILPFDHSRVKLTLKTSSQDSDYINANFI 93

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158303304 1211 PGYSHPQEIIATQGPLKKTLEDFWRLVWEQQVHVIIMLTVGMENGRVLCEHYWPV-NSTPVTHGHITTHLLAEESEDEWT 1289
Cdd:cd14604    94 KGVYGPKAYIATQGPLANTVIDFWRMIWEYNVAIIVMACREFEMGRKKCERYWPLyGEEPMTFGPFRISCEAEQARTDYF 173

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158303304 1290 RREFQLQHgaEQKQRRVKQLQFTTWPDHSVPEAPSSLLAFVELVQEEvkATQGKGPILVHCSAGVGRTGTFVALLRLLRQ 1369
Cdd:cd14604   174 IRTLLLEF--QNETRRLYQFHYVNWPDHDVPSSFDSILDMISLMRKY--QEHEDVPICIHCSAGCGRTGAICAIDYTWNL 249

                         250       260       270
                  ....*....|....*....|....*....|....*..
gi 158303304 1370 LEEEQV---VDVFNTVYILRLHRPLMIQTLSQYIFLH 1403
Cdd:cd14604   250 LKAGKIpeeFNVFNLIQEMRTQRHSAVQTKEQYELVH 286
PTPc-N3 cd14600
catalytic domain of tyrosine-protein phosphatase non-receptor type 3; Tyrosine-protein ...
 1169-1407 6.42e-54

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


Pssm-ID: 350448 [Multi-domain]  Cd Length: 274  Bit Score: 190.45  E-value: 6.42e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158303304 1169 AEHPANITKNRYPHVLPYDHSRVRLtqlsgEPHSDYINANF----IPGYSHPQEIIATQGPLKKTLEDFWRLVWEQQVHV 1244
Cdd:cd14600    35 AKLPQNMDKNRYKDVLPYDATRVVL-----QGNEDYINASYvnmeIPSANIVNKYIATQGPLPHTCAQFWQVVWEQKLSL 109

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158303304 1245 IIMLTVGMENGRVLCEHYWPVNSTPVTHG--HITTHllAEESEDEWTRREFQLQHGAEQKQRRVKQLQFTTWPDHSVPEA 1322
Cdd:cd14600   110 IVMLTTLTERGRTKCHQYWPDPPDVMEYGgfRVQCH--SEDCTIAYVFREMLLTNTQTGEERTVTHLQYVAWPDHGVPDD 187

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158303304 1323 PSSLLAFVELVQEEVKATQgkgPILVHCSAGVGRTGTFVALLRLLRQLEEEQVVDVFNTVYILRLHRPLMIQTLSQYIFL 1402
Cdd:cd14600   188 SSDFLEFVNYVRSKRVENE---PVLVHCSAGIGRTGVLVTMETAMCLTERNQPVYPLDIVRKMRDQRAMMVQTSSQYKFV 264


                  ....*
gi 158303304 1403 HSCLL 1407
Cdd:cd14600   265 CEAIL 269
PTPc-N11 cd14605
catalytic domain of tyrosine-protein phosphatase non-receptor type 11; Tyrosine-protein ...
 1174-1403 2.86e-53

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: 187.53  E-value: 2.86e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158303304 1174 NITKNRYPHVLPYDHSRVRLTQLS-GEPHSDYINANFI-PGY------SHPQE-IIATQGPLKKTLEDFWRLVWEQQVHV 1244
Cdd:cd14605     2 NKNKNRYKNILPFDHTRVVLHDGDpNEPVSDYINANIImPEFetkcnnSKPKKsYIATQGCLQNTVNDFWRMVFQENSRV 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158303304 1245 IIMLTVGMENGRVLCEHYWPVNSTPVTHGHITTHLLAEESEDEWTRREFQL-QHGAEQKQRRVKQLQFTTWPDHSVPEAP 1323
Cdd:cd14605    82 IVMTTKEVERGKSKCVKYWPDEYALKEYGVMRVRNVKESAAHDYILRELKLsKVGQGNTERTVWQYHFRTWPDHGVPSDP 161

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158303304 1324 SSLLAFVELVQEEVKATQGKGPILVHCSAGVGRTGTFVALLRLLRQLEEEQV---VDVFNTVYILRLHRPLMIQTLSQYI 1400
Cdd:cd14605   162 GGVLDFLEEVHHKQESIMDAGPVVVHCSAGIGRTGTFIVIDILIDIIREKGVdcdIDVPKTIQMVRSQRSGMVQTEAQYR 241


                  ...
gi 158303304 1401 FLH 1403
Cdd:cd14605   242 FIY 244
PTPc-N6 cd14606
catalytic domain of tyrosine-protein phosphatase non-receptor type 6; Tyrosine-protein ...
 1158-1410 7.69e-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: 187.01  E-value: 7.69e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158303304 1158 KEVGKDQPRLEAEHPANITKNRYPHVLPYDHSRVRLT-QLSGEPHSDYINANFI------PGySHPQEIIATQGPLKKTL 1230
Cdd:cd14606     2 QEVKNLHQRLEGQRPENKSKNRYKNILPFDHSRVILQgRDSNIPGSDYINANYVknqllgPD-ENAKTYIASQGCLEATV 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158303304 1231 EDFWRLVWEQQVHVIIMLTVGMENGRVLCEHYWPVNSTPVTHGHITTHLLAEESEDEWTRREFQLQ--HGAEqKQRRVKQ 1308
Cdd:cd14606    81 NDFWQMAWQENSRVIVMTTREVEKGRNKCVPYWPEVGMQRAYGPYSVTNCGEHDTTEYKLRTLQVSplDNGE-LIREIWH 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158303304 1309 LQFTTWPDHSVPEAPSSLLAFVELVQEEVKATQGKGPILVHCSAGVGRTGTFVALLRLLRQLEEEQV---VDVFNTVYIL 1385
Cdd:cd14606   160 YQYLSWPDHGVPSEPGGVLSFLDQINQRQESLPHAGPIIVHCSAGIGRTGTIIVIDMLMENISTKGLdcdIDIQKTIQMV 239

                         250       260
                  ....*....|....*....|....*
gi 158303304 1386 RLHRPLMIQTLSQYIFLHSCLLNKI 1410
Cdd:cd14606   240 RAQRSGMVQTEAQYKFIYVAIAQFI 264
R-PTPc-R cd14611
catalytic domain of receptor-type tyrosine-protein phosphatase R; Receptor-type ...
 1176-1403 8.64e-53

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: 185.12  E-value: 8.64e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158303304 1176 TKNRYPHVLPYDHSRVRL-TQLSGEPHSDYINANFIPGYSHPQEI-IATQGPLKKTLEDFWRLVWEQQVHVIIMLTVGME 1253
Cdd:cd14611     1 TKNRYKTILPNPHSRVCLkPKNSNDSLSTYINANYIRGYGGKEKAfIATQGPMINTVNDFWQMVWQEDSPVIVMITKLKE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158303304 1254 NGRVlCEHYWPVNSTpvTHGHITTHLLAEESEDEWTRREFQLQHGAeqKQRRVKQLQFTTWPDHSVPEAPSSLLAFVELV 1333
Cdd:cd14611    81 KNEK-CVLYWPEKRG--IYGKVEVLVNSVKECDNYTIRNLTLKQGS--QSRSVKHYWYTSWPDHKTPDSAQPLLQLMLDV 155

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158303304 1334 QEEVKATQGKGPILVHCSAGVGRTGTFVALLRLLRQLEEEQVVDVFNTVYILRLHRPLMIQTLSQYIFLH 1403
Cdd:cd14611   156 EEDRLASPGRGPVVVHCSAGIGRTGCFIATTIGCQQLKEEGVVDVLSIVCQLRVDRGGMVQTSEQYEFVH 225
R-PTPc-E-2 cd14622
catalytic domain of receptor-type tyrosine-protein phosphatase E, repeat 2; Receptor-type ...
 1203-1403 9.00e-53

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


Pssm-ID: 350470 [Multi-domain]  Cd Length: 205  Bit Score: 184.44  E-value: 9.00e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158303304 1203 DYINANFIPGYSHPQEIIATQGPLKKTLEDFWRLVWEQQVHVIIMLTVGMENGRVLCEHYWPVNSTpVTHGHITTHLLAE 1282
Cdd:cd14622     1 DYINASFIDGYRQKDYFIATQGPLAHTVEDFWRMVWEWKCHTIVMLTELQEREQEKCVQYWPSEGS-VTHGEITIEIKND 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158303304 1283 ESEDEWTRREFQLQHGAEQKQRRVKQLQFTTWPDHSVPEAPSSLLAFVELVQEEVKATqGKGPILVHCSAGVGRTGTFVA 1362
Cdd:cd14622    80 TLLETISIRDFLVTYNQEKQTRLVRQFHFHGWPEIGIPAEGKGMIDLIAAVQKQQQQT-GNHPIVVHCSAGAGRTGTFIA 158

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|.
gi 158303304 1363 LLRLLRQLEEEQVVDVFNTVYILRLHRPLMIQTLSQYIFLH 1403
Cdd:cd14622   159 LSNILERVKAEGLLDVFQTVKSLRLQRPHMVQTLEQYEFCY 199
PTPc-N1_2 cd14545
catalytic domain of tyrosine-protein phosphatase non-receptor type 1 and type 2; ...
 1177-1401 9.06e-53

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: 185.29  E-value: 9.06e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158303304 1177 KNRYPHVLPYDHSRVRLTQLSGEphSDYINANFIPGYSHPQEIIATQGPLKKTLEDFWRLVWEQQVHVIIMLTVGMENGR 1256
Cdd:cd14545     1 LNRYRDRDPYDHDRSRVKLKQGD--NDYINASLVEVEEAKRSYILTQGPLPNTSGHFWQMVWEQNSKAVIMLNKLMEKGQ 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158303304 1257 VLCEHYWPVNSTP---VTHGHITTHLLAEESEDEWTRREFQLQHGAEQKQRRVKQLQFTTWPDHSVPEAPSSLLAFVELV 1333
Cdd:cd14545    79 IKCAQYWPQGEGNamiFEDTGLKVTLLSEEDKSYYTVRTLELENLKTQETREVLHFHYTTWPDFGVPESPAAFLNFLQKV 158

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158303304 1334 QEEVKATQGKGPILVHCSAGVGRTGTF--VALLRLLRQLEEEQVVDVFNTVYILRLHRPLMIQTLSQYIF 1401
Cdd:cd14545   159 RESGSLSSDVGPPVVHCSAGIGRSGTFclVDTCLVLIEKGNPSSVDVKKVLLEMRKYRMGLIQTPDQLRF 228
PTPc-N5 cd14613
catalytic domain of tyrosine-protein phosphatase non-receptor type 5; Tyrosine-protein ...
 1168-1406 2.04e-52

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: 185.45  E-value: 2.04e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158303304 1168 EAEHPANITKNRYPHVLPYDHSRVRLTQLS-GEPHSDYINANFIPGYSHPQEI-IATQGPLKKTLEDFWRLVWEQQVHVI 1245
Cdd:cd14613    19 EYDIPGLVRKNRYKTILPNPHSRVCLTSPDqDDPLSSYINANYIRGYGGEEKVyIATQGPTVNTVGDFWRMVWQERSPII 98

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158303304 1246 IMLTvGMENGRVLCEHYWPVNStpVTHGHITTHLLAEESEDEWTRREFQLQHGAEQkqRRVKQLQFTTWPDHSVPEAPSS 1325
Cdd:cd14613    99 VMIT-NIEEMNEKCTEYWPEEQ--VTYEGIEITVKQVIHADDYRLRLITLKSGGEE--RGLKHYWYTSWPDQKTPDNAPP 173

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158303304 1326 LLAFVELVQEEVK-ATQGKGPILVHCSAGVGRTGTFVALLRLLRQLEEEQVVDVFNTVYILRLHRPLMIQTLSQYIFLHS 1404
Cdd:cd14613   174 LLQLVQEVEEARQqAEPNCGPVIVHCSAGIGRTGCFIATSICCKQLRNEGVVDILRTTCQLRLDRGGMIQTCEQYQFVHH 253


                  ..
gi 158303304 1405 CL 1406
Cdd:cd14613   254 VL 255
R-PTPc-C-1 cd14557
catalytic domain of receptor-type tyrosine-protein phosphatase C, repeat 1; Receptor-type ...
 1204-1403 2.89e-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: 182.72  E-value: 2.89e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158303304 1204 YINANFIPGYSHPQEIIATQGPLKKTLEDFWRLVWEQQVHVIIMLTVGMENGRVLCEHYWP-VNSTPVTHGHITTHLLAE 1282
Cdd:cd14557     1 YINASYIDGFKEPRKYIAAQGPKDETVDDFWRMIWEQKSTVIVMVTRCEEGNRNKCAQYWPsMEEGSRAFGDVVVKINEE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158303304 1283 ESEDEWTRREFQLQHGAEQ-KQRRVKQLQFTTWPDHSVPEAPSSLLAfvelVQEEVKATQG--KGPILVHCSAGVGRTGT 1359
Cdd:cd14557    81 KICPDYIIRKLNINNKKEKgSGREVTHIQFTSWPDHGVPEDPHLLLK----LRRRVNAFNNffSGPIVVHCSAGVGRTGT 156

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....
gi 158303304 1360 FVALLRLLRQLEEEQVVDVFNTVYILRLHRPLMIQTLSQYIFLH 1403
Cdd:cd14557   157 YIGIDAMLEGLEAEGRVDVYGYVVKLRRQRCLMVQVEAQYILIH 200
R-PTPc-U-1 cd14632
catalytic domain of receptor-type tyrosine-protein phosphatase U, repeat 1; Receptor-type ...
 1204-1411 3.34e-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: 182.56  E-value: 3.34e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158303304 1204 YINANFIPGYSHPQEIIATQGPLKKTLEDFWRLVWEQQVHVIIMLTVGMENGRVLCEHYWPVNSTpvTHGHITTHLLAEE 1283
Cdd:cd14632     1 YINANYIDGYHRSNHFIATQGPKQEMVYDFWRMVWQEHCSSIVMITKLVEVGRVKCSKYWPDDSD--TYGDIKITLLKTE 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158303304 1284 SEDEWTRREFQLQHGAEQKQRRVKQLQFTTWPDHSVPEAPSSLLAFVELVQEEVKATqgKGPILVHCSAGVGRTGTFVAL 1363
Cdd:cd14632    79 TLAEYSVRTFALERRGYSARHEVKQFHFTSWPEHGVPYHATGLLAFIRRVKASTPPD--AGPVVVHCSAGAGRTGCYIVL 156

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*...
gi 158303304 1364 LRLLRQLEEEQVVDVFNTVYILRLHRPLMIQTLSQYIFLHSCLLNKIL 1411
Cdd:cd14632   157 DVMLDMAECEGVVDIYNCVKTLCSRRINMIQTEEQYIFIHDAILEACL 204
PTPc-N22 cd14602
catalytic domain of tyrosine-protein phosphatase non-receptor type 22; Tyrosine-protein ...
 1177-1408 7.18e-52

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: 182.73  E-value: 7.18e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158303304 1177 KNRYPHVLPYDHSRVRLTQLSGEPHSDYINANFIPGYSHPQEIIATQGPLKKTLEDFWRLVWEQQVHVIIMLTVGMENGR 1256
Cdd:cd14602     1 KNRYKDILPYDHSRVELSLITSDEDSDYINANFIKGVYGPRAYIATQGPLSTTLLDFWRMIWEYSVLIIVMACMEFEMGK 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158303304 1257 VLCEHYWP-VNSTPVTHGHITTHLLAEESEDEWTRREFQLQHGAEqkQRRVKQLQFTTWPDHSVPEAPSSLLAFVelvqE 1335
Cdd:cd14602    81 KKCERYWAePGEMQLEFGPFSVTCEAEKRKSDYIIRTLKVKFNSE--TRTIYQFHYKNWPDHDVPSSIDPILELI----W 154

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 158303304 1336 EVKATQGKG--PILVHCSAGVGRTGTFVALLRLLRQLEEEQV---VDVFNTVYILRLHRPLMIQTLSQYIFLHSCLLN 1408
Cdd:cd14602   155 DVRCYQEDDsvPICIHCSAGCGRTGVICAIDYTWMLLKDGIIpenFSVFSLIQEMRTQRPSLVQTKEQYELVYNAVIE 232
PTPc-N13 cd14597
catalytic domain of tyrosine-protein phosphatase non-receptor type 13; Tyrosine-protein ...
 1174-1407 9.97e-51

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: 179.64  E-value: 9.97e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158303304 1174 NITKNRYPHVLPYDHSRVRLtqlsGEPHsDYINANFI--PGYSHPQEIIATQGPLKKTLEDFWRLVWEQQVHVIIMLTVG 1251
Cdd:cd14597     3 NRKKNRYKNILPYDTTRVPL----GDEG-GYINASFIkmPVGDEEFVYIACQGPLPTTVADFWQMVWEQKSTVIAMMTQE 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158303304 1252 MENGRVLCEHYWP--VNSTPVTHGHITTHLLAEESEDEWTRREFQLQHGAEQKQRRVKQLQFTTWPDHSVPEAPSSLLAF 1329
Cdd:cd14597    78 VEGGKIKCQRYWPeiLGKTTMVDNRLQLTLVRMQQLKNFVIRVLELEDIQTREVRHITHLNFTAWPDHDTPSQPEQLLTF 157

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 158303304 1330 VELVQEEVKAtqgkGPILVHCSAGVGRTGTFVALLRLLRQLEEEQVVDVFNTVYILRLHRPLMIQTLSQYIFLHSCLL 1407
Cdd:cd14597   158 ISYMRHIHKS----GPIITHCSAGIGRSGTLICIDVVLGLISKDLDFDISDIVRTMRLQRHGMVQTEDQYIFCYQVIL 231
R-PTPc-Z-1 cd17668
catalytic domain of receptor-type tyrosine-protein phosphatase Z, repeat 1; Receptor-type ...
 1204-1407 2.97e-50

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: 177.09  E-value: 2.97e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158303304 1204 YINANFIPGYSHPQEIIATQGPLKKTLEDFWRLVWEQQVHVIIMLTVGMENGRVLCEHYWPVNSTP------VTHGhiTT 1277
Cdd:cd17668     1 YINANYVDGYNKPKAYIAAQGPLKSTAEDFWRMIWEHNVEVIVMITNLVEKGRRKCDQYWPADGSEeygnflVTQK--SV 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158303304 1278 HLLAEESEDEWTRREFQLQHGAE---QKQRRVKQLQFTTWPDHSVPEAPSSLLAFVElvqeevKATQGK----GPILVHC 1350
Cdd:cd17668    79 QVLAYYTVRNFTLRNTKIKKGSQkgrPSGRVVTQYHYTQWPDMGVPEYTLPVLTFVR------KASYAKrhavGPVVVHC 152

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 158303304 1351 SAGVGRTGTFVALLRLLRQLEEEQVVDVFNTVYILRLHRPLMIQTLSQYIFLHSCLL 1407
Cdd:cd17668   153 SAGVGRTGTYIVLDSMLQQIQHEGTVNIFGFLKHIRSQRNYLVQTEEQYVFIHDALV 209
PTP_tm pfam18861
TM proximal of protein tyrosine phosphatase, receptor type J; Protein tyrosine phosphatases ...
 948-1069 8.65e-50

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: 172.41  E-value: 8.65e-50
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158303304   948 VTRGMFGKDDGQIQWYGIIATINMTLAQPSQEAINHTWYDHYYRGHDSYLALLFPNPFYPePWAVPRSWTVPVGTEDCdn 1027
Cdd:pfam18861    1 IQFSLFNSSNGPIKAYGVIVTTNDSLNRPLKEYLNKTYYDWKYKKTDSYLATVTPNPFTS-PRSSSRSLTVPVGTGSK-- 77

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*....
gi 158303304  1028 TQEICNGHLKPGFQYRFSIAAFSRL-------SSPETILAFSAFSEPQA 1069
Cdd:pfam18861   78 WQGYCNGPLKPLGSYRFSVAAFTRLefddgliDGEESYVSFTPFSEPIA 126
PTPc-N22_18_12 cd14542
catalytic domain of tyrosine-protein phosphatase non-receptor type 22, type 18 and type 12; ...
 1204-1403 3.32e-49

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: 173.76  E-value: 3.32e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158303304 1204 YINANFIPGYSHPQEIIATQGPLKKTLEDFWRLVWEQQVHVIIMLTVGMENGRVLCEHYWPVNSTPV-THGHITTHLLAE 1282
Cdd:cd14542     1 YINANFIKGVSGSKAYIATQGPLPNTVLDFWRMIWEYNVQVIVMACREFEMGKKKCERYWPEEGEEQlQFGPFKISLEKE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158303304 1283 ESE-DEWTRREFQLQHGAEqkQRRVKQLQFTTWPDHSVPEAPSSLLAFVELVQEevkaTQGKG--PILVHCSAGVGRTGT 1359
Cdd:cd14542    81 KRVgPDFLIRTLKVTFQKE--SRTVYQFHYTAWPDHGVPSSVDPILDLVRLVRD----YQGSEdvPICVHCSAGCGRTGT 154

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*..
gi 158303304 1360 FVALLRLLRQLEEEQVVD---VFNTVYILRLHRPLMIQTLSQYIFLH 1403
Cdd:cd14542   155 ICAIDYVWNLLKTGKIPEefsLFDLVREMRKQRPAMVQTKEQYELVY 201
PTPc-N1 cd14608
catalytic domain of tyrosine-protein phosphatase non-receptor type 1; Tyrosine-protein ...
 1154-1420 2.02e-48

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: 174.44  E-value: 2.02e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158303304 1154 FEELKEVGKDQPRLEAEHPANITKNRYPHVLPYDHSRVRLTQLSgephSDYINANFIPGYSHPQEIIATQGPLKKTLEDF 1233
Cdd:cd14608     5 YQDIRHEASDFPCRVAKLPKNKNRNRYRDVSPFDHSRIKLHQED----NDYINASLIKMEEAQRSYILTQGPLPNTCGHF 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158303304 1234 WRLVWEQQVHVIIMLTVGMENGRVLCEHYWPV---NSTPVTHGHITTHLLAEESEDEWTRREFQLQHGAEQKQRRVKQLQ 1310
Cdd:cd14608    81 WEMVWEQKSRGVVMLNRVMEKGSLKCAQYWPQkeeKEMIFEDTNLKLTLISEDIKSYYTVRQLELENLTTQETREILHFH 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158303304 1311 FTTWPDHSVPEAPSSLLAFVELVQEEVKATQGKGPILVHCSAGVGRTGTFVALLR---LLRQLEEEQVVDVFNTVYILRL 1387
Cdd:cd14608   161 YTTWPDFGVPESPASFLNFLFKVRESGSLSPEHGPVVVHCSAGIGRSGTFCLADTcllLMDKRKDPSSVDIKKVLLEMRK 240

                         250       260       270
                  ....*....|....*....|....*....|....*
gi 158303304 1388 HRPLMIQTLSQYIFLHSCLLN--KILEGPSDASDS 1420
Cdd:cd14608   241 FRMGLIQTADQLRFSYLAVIEgaKFIMGDSSVQDQ 275
PTP-N23 cd14539
PTP-like domain of tyrosine-protein phosphatase non-receptor type 23; Tyrosine-protein ...
 1204-1403 1.73e-46

PTP-like domain of tyrosine-protein phosphatase non-receptor type 23; Tyrosine-protein phosphatase non-receptor type 23 (PTPN23), also called His domain-containing protein tyrosine phosphatase (HD-PTP) or protein tyrosine phosphatase TD14 (PTP-TD14), is a catalytically inactive member of the tyrosine-specific protein tyrosine phosphatase (PTP) family. Human PTPN23 may be involved in the regulation of small nuclear ribonucleoprotein assembly and pre-mRNA splicing by modifying the survival motor neuron (SMN) complex. It plays a role in ciliogenesis and is part of endosomal sorting complex required for transport (ESCRT) pathways. PTPN23 contains five domains: a BRO1-like domain that plays a role in endosomal sorting; a V-domain that interacts with Lys63-linked polyubiquitinated substrates; a central proline-rich region that might recruit SH3-containing proteins; a PTP-like domain; and a proteolytic degradation-targeting motif, also known as a PEST sequence.


Pssm-ID: 350387 [Multi-domain]  Cd Length: 205  Bit Score: 166.41  E-value: 1.73e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158303304 1204 YINANFIPGYS-HPQEIIATQGPLKKTLEDFWRLVWEQQVHVIIMLTVGMENGRVLCEHYWPVN-STPVTHGHITTHLLA 1281
Cdd:cd14539     1 YINASLIEDLTpYCPRFIATQAPLPGTAADFWLMVYEQQVSVIVMLVSEQENEKQKVHRYWPTErGQALVYGAITVSLQS 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158303304 1282 EESEDEWTRREFQLQHGAEQKQRRVKQLQFTTWPDHSVPEAPSSLLAFVELVQEEVKATQG-KGPILVHCSAGVGRTGTF 1360
Cdd:cd14539    81 VRTTPTHVERIISIQHKDTRLSRSVVHLQFTTWPELGLPDSPNPLLRFIEEVHSHYLQQRSlQTPIVVHCSSGVGRTGAF 160

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....
gi 158303304 1361 -VALLRLLRQLEEEQVVDVFNTVYILRLHRPLMIQTLSQYIFLH 1403
Cdd:cd14539   161 cLLYAAVQEIEAGNGIPDLPQLVRKMRQQRKYMLQEKEHLKFCY 204
R-PTPc-A-E-1 cd14551
catalytic domain of receptor-type tyrosine-protein phosphatase A and E, repeat 1; ...
 1204-1403 2.51e-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: 165.86  E-value: 2.51e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158303304 1204 YINANFIPGYSHPQEIIATQGPLKKTLEDFWRLVWEQQVHVIIMLTVGMENGRVLCEHYWPvNSTPVTHGHITTHLLAEE 1283
Cdd:cd14551     1 YINASYIDGYQEKNKFIAAQGPKDETVNDFWRMIWEQGSATIVMVTNLKERKEKKCSQYWP-DQGCWTYGNLRVRVEDTV 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158303304 1284 SEDEWTRREFQLQH----GAEQKQRRVKQLQFTTWPDHSVPEAPSSLLAFVELVQEEVkaTQGKGPILVHCSAGVGRTGT 1359
Cdd:cd14551    80 VLVDYTTRKFCIQKvnrgIGEKRVRLVTQFHFTSWPDFGVPFTPIGMLKFLKKVKSAN--PPRAGPIVVHCSAGVGRTGT 157

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....
gi 158303304 1360 FVALLRLLRQLEEEQVVDVFNTVYILRLHRPLMIQTLSQYIFLH 1403
Cdd:cd14551   158 FIVIDAMLDMMHAEGKVDVFGFVSRIRQQRSQMVQTDMQYVFIY 201
PTPc-N4 cd14601
catalytic domain of tyrosine-protein phosphatase non-receptor type 4; Tyrosine-protein ...
 1203-1407 2.84e-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: 2.84e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158303304 1203 DYINANFI----PGYSHPQEIIATQGPLKKTLEDFWRLVWEQQVHVIIMLTVGMENGRVLCEHYWPVNSTPVTHGHITTH 1278
Cdd:cd14601     1 DYINANYInmeiPSSSIINRYIACQGPLPNTCSDFWQMTWEQGSSMVVMLTTQVERGRVKCHQYWPEPSGSSSYGGFQVT 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158303304 1279 LLAEESEDEWTRREFQLQHGAEQKQRRVKQLQFTTWPDHSVPEAPSSLLAFVELVQEevKATQGKGPILVHCSAGVGRTG 1358
Cdd:cd14601    81 CHSEEGNPAYVFREMTLTNLEKNESRPLTQIQYIAWPDHGVPDDSSDFLDFVCLVRN--KRAGKDEPVVVHCSAGIGRTG 158

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*....
gi 158303304 1359 TFVALLRLLRQLEEEQVVDVFNTVYILRLHRPLMIQTLSQYIFLHSCLL 1407
Cdd:cd14601   159 VLITMETAMCLIECNQPVYPLDIVRTMRDQRAMMIQTPSQYRFVCEAIL 207
PTPc-N2 cd14607
catalytic domain of tyrosine-protein phosphatase non-receptor type 2; Tyrosine-protein ...
 1156-1401 9.50e-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: 166.29  E-value: 9.50e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158303304 1156 ELKEVGKDQPRLEAEHPANITKNRYPHVLPYDHSRVRLTQLSgephSDYINANFIPGYSHPQEIIATQGPLKKTLEDFWR 1235
Cdd:cd14607     6 EIRNESHDYPHRVAKYPENRNRNRYRDVSPYDHSRVKLQNTE----NDYINASLVVIEEAQRSYILTQGPLPNTCCHFWL 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158303304 1236 LVWEQQVHVIIMLTVGMENGRVLCEHYWPVNSTPV---THGHITTHLLAEESEDEWTRREFQLQHGAEQKQRRVKQLQFT 1312
Cdd:cd14607    82 MVWQQKTKAVVMLNRIVEKDSVKCAQYWPTDEEEVlsfKETGFSVKLLSEDVKSYYTVHLLQLENINSGETRTISHFHYT 161

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158303304 1313 TWPDHSVPEAPSSLLAFVELVQEEVKATQGKGPILVHCSAGVGRTGTF--VALLRLLRQLEEEQVVDVFNTVYILRLHRP 1390
Cdd:cd14607   162 TWPDFGVPESPASFLNFLFKVRESGSLSPEHGPAVVHCSAGIGRSGTFslVDTCLVLMEKKDPDSVDIKQVLLDMRKYRM 241

                         250
                  ....*....|.
gi 158303304 1391 LMIQTLSQYIF 1401
Cdd:cd14607   242 GLIQTPDQLRF 252
PTPc-N21_14 cd14540
catalytic domain of tyrosine-protein phosphatase non-receptor type 21 and type 14; ...
 1204-1407 1.78e-45

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: 163.78  E-value: 1.78e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158303304 1204 YINANFIPGYSHPQEI--IATQGPLKKTLEDFWRLVWEQQVHVIIMLTVGMENGRVLCEHYWP---VNSTPVTHGHITTH 1278
Cdd:cd14540     1 YINASHITATVGGKQRfyIAAQGPLQNTVGDFWQMVWEQGVYLVVMVTAEEEGGREKCFRYWPtlgGEHDALTFGEYKVS 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158303304 1279 LLAEESEDEWTRREFQLQHGAEQKQRRVKQLQFTTWPDHSVPEAPSSLLAFVELVQE-------EVKATQGKGPILVHCS 1351
Cdd:cd14540    81 TKFSVSSGCYTTTGLRVKHTLSGQSRTVWHLQYTDWPDHGCPEDVSGFLDFLEEINSvrrhtnqDVAGHNRNPPTLVHCS 160

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 158303304 1352 AGVGRTGTFVALLRLLRQLEEEQVVDVFNTVYILRLHRPLMIQTLSQYIFLHSCLL 1407
Cdd:cd14540   161 AGVGRTGVVILADLMLYCLDHNEELDIPRVLALLRHQRMLLVQTLAQYKFVYNVLI 216
R-PTP-N2 cd14610
PTP-like domain of receptor-type tyrosine-protein phosphatase N2; Receptor-type ...
 1169-1401 1.58e-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: 163.69  E-value: 1.58e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158303304 1169 AEHPANITKNRYPHVLPYDHSRVRLTQLSGEPHSDYINANFI-------PGYshpqeiIATQGPLKKTLEDFWRLVWEQQ 1241
Cdd:cd14610    39 AQREENVQKNRSLAVLPYDHSRIILKAENSHSHSDYINASPImdhdprnPAY------IATQGPLPATVADFWQMVWESG 112

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158303304 1242 VHVIIMLTVGMENGRVLCEHYWPVNSTPVTHGH----ITTHLLAEesedEWTRREFQLQHGAEQKQRRVKQLQFTTWPDH 1317
Cdd:cd14610   113 CVVIVMLTPLAENGVKQCYHYWPDEGSNLYHIYevnlVSEHIWCE----DFLVRSFYLKNLQTNETRTVTQFHFLSWNDQ 188

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158303304 1318 SVPEAPSSLLAFVELVQeevKATQGKG-PILVHCSAGVGRTGTFV-ALLRLLRQLEEEQVVDVFNTVYILRLHRPLMIQT 1395
Cdd:cd14610   189 GVPASTRSLLDFRRKVN---KCYRGRScPIIVHCSDGAGRSGTYIlIDMVLNKMAKGAKEIDIAATLEHLRDQRPGMVQT 265


                  ....*.
gi 158303304 1396 LSQYIF 1401
Cdd:cd14610   266 KEQFEF 271
R-PTP-N cd14609
PTP-like domain of receptor-type tyrosine-protein phosphatase N; Receptor-type ...
 1169-1401 5.59e-44

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: 161.74  E-value: 5.59e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158303304 1169 AEHPANITKNRYPHVLPYDHSRVRLTQLSGEPHSDYINANFI-------PGYshpqeiIATQGPLKKTLEDFWRLVWEQQ 1241
Cdd:cd14609    37 AQGEANVKKNRNPDFVPYDHARIKLKAESNPSRSDYINASPIiehdprmPAY------IATQGPLSHTIADFWQMVWENG 110

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158303304 1242 VHVIIMLTVGMENGRVLCEHYWPVNSTPVTHGH----ITTHLLAEesedEWTRREFQLQHGAEQKQRRVKQLQFTTWPDH 1317
Cdd:cd14609   111 CTVIVMLTPLVEDGVKQCDRYWPDEGSSLYHIYevnlVSEHIWCE----DFLVRSFYLKNVQTQETRTLTQFHFLSWPAE 186

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158303304 1318 SVPEAPSSLLAFVELVQeevKATQGKG-PILVHCSAGVGRTGTFV-ALLRLLRQLEEEQVVDVFNTVYILRLHRPLMIQT 1395
Cdd:cd14609   187 GIPSSTRPLLDFRRKVN---KCYRGRScPIIVHCSDGAGRTGTYIlIDMVLNRMAKGVKEIDIAATLEHVRDQRPGMVRT 263


                  ....*.
gi 158303304 1396 LSQYIF 1401
Cdd:cd14609   264 KDQFEF 269
PTPc-N14 cd14599
catalytic domain of tyrosine-protein phosphatase non-receptor type 14; Tyrosine-protein ...
 1151-1407 1.76e-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: 160.55  E-value: 1.76e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158303304 1151 FQEFEELKEVGKDQPRLEAEHPANITKNRYPHVLPYDHSRVRLTQlSGEPHSDYINANFIPGYSHPQE--IIATQGPLKK 1228
Cdd:cd14599    15 FTEYEQIPKKKADGVFTTATLPENAERNRIREVVPYEENRVELVP-TKENNTGYINASHIKVTVGGEEwhYIATQGPLPH 93

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158303304 1229 TLEDFWRLVWEQQVHVIIMLTVGMENGRVLCEHYWP---VNSTPVTHG--HITTHLLAEESedEWTRREFQLQHGAEQKQ 1303
Cdd:cd14599    94 TCHDFWQMVWEQGVNVIAMVTAEEEGGRSKSHRYWPklgSKHSSATYGkfKVTTKFRTDSG--CYATTGLKVKHLLSGQE 171

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158303304 1304 RRVKQLQFTTWPDHSVPEAPSSLLAFVELVQEEVKATQG--------KGPILVHCSAGVGRTGTFVALLRLLRQLEEEQV 1375
Cdd:cd14599   172 RTVWHLQYTDWPDHGCPEEVQGFLSYLEEIQSVRRHTNSmldstkncNPPIVVHCSAGVGRTGVVILTELMIGCLEHNEK 251

                         250       260       270
                  ....*....|....*....|....*....|..
gi 158303304 1376 VDVFNTVYILRLHRPLMIQTLSQYIFLHSCLL 1407
Cdd:cd14599   252 VEVPVMLRHLREQRMFMIQTIAQYKFVYQVLI 283
R-PTPc-typeIIb-2 cd14556
PTP domain of type IIb (or R2B) subfamily receptor-type tyrosine-protein phosphatases, repeat ...
 1204-1403 8.77e-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: 152.56  E-value: 8.77e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158303304 1204 YINANFIPGYSHPQEIIATQGPLKKTLEDFWRLVWEQQVHVIIMLTvGMENGRVLCEHYWPVNSTPvTHGHITTHLLAEE 1283
Cdd:cd14556     1 YINAALLDSYKQPAAFIVTQHPLPNTVTDFWRLVYDYGCTSIVMLN-QLDPKDQSCPQYWPDEGSG-TYGPIQVEFVSTT 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158303304 1284 SEDEWTRREFQLQHGA--EQKQRRVKQLQFTTWPDHSvpEAPSSLLAFVELVQEEVKATQ--GKGPILVHCSAGVGRTGT 1359
Cdd:cd14556    79 IDEDVISRIFRLQNTTrpQEGYRMVQQFQFLGWPRDR--DTPPSKRALLKLLSEVEKWQEqsGEGPIVVHCLNGVGRSGV 156

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....
gi 158303304 1360 FVALLRLLRQLEEEQVVDVFNTVYILRLHRPLMIQTLSQYIFLH 1403
Cdd:cd14556   157 FCAISSVCERIKVENVVDVFQAVKTLRNHRPNMVETEEQYKFCY 200
PTPc-N20 cd14596
catalytic domain of tyrosine-protein phosphatase non-receptor type 20; Tyrosine-protein ...
 1204-1407 1.51e-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: 152.21  E-value: 1.51e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158303304 1204 YINANFI--PGYSHPQEIIATQGPLKKTLEDFWRLVWEQQVHVIIMLTVGMENGRVLCEHYWPVN-STPVTHGHITTHLL 1280
Cdd:cd14596     1 YINASYItmPVGEEELFYIATQGPLPSTIDDFWQMVWENRSDVIAMMTREVERGKVKCHRYWPETlQEPMELENYQLRLE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158303304 1281 AEESEDEWTRREFQLQHGAEQKQRRVKQLQFTTWPDHSVPEAPSSLLAFVELvqeeVKATQGKGPILVHCSAGVGRTGTF 1360
Cdd:cd14596    81 NYQALQYFIIRIIKLVEKETGENRLIKHLQFTTWPDHGTPQSSDQLVKFICY----MRKVHNTGPIVVHCSAGIGRAGVL 156

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*..
gi 158303304 1361 VALLRLLRQLEEEQVVDVFNTVYILRLHRPLMIQTLSQYIFLHSCLL 1407
Cdd:cd14596   157 ICVDVLLSLIEKDLSFNIKDIVREMRQQRYGMIQTKDQYLFCYKVVL 203
R-PTP-N-N2 cd14546
PTP-like domain of receptor-type tyrosine-protein phosphatase-like N and N2; Receptor-type ...
 1204-1405 3.23e-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: 3.23e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158303304 1204 YINANFIpgYSH-PQE--IIATQGPLKKTLEDFWRLVWEQQVHVIIMLTVGMENGRVLCEHYWPVNSTPVtHGHITTHLL 1280
Cdd:cd14546     1 YINASTI--YDHdPRNpaYIATQGPLPHTIADFWQMIWEQGCVVIVMLTRLQENGVKQCARYWPEEGSEV-YHIYEVHLV 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158303304 1281 AEES-EDEWTRREFQLQHGAEQKQRRVKQLQFTTWPDHSVPEAPSSLLAFVELVQeevKATQGKG-PILVHCSAGVGRTG 1358
Cdd:cd14546    78 SEHIwCDDYLVRSFYLKNLQTSETRTVTQFHFLSWPDEGIPASAKPLLEFRRKVN---KSYRGRScPIVVHCSDGAGRTG 154

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*...
gi 158303304 1359 TFVAL-LRLLRQLEEEQVVDVFNTVYILRLHRPLMIQTLSQYIFLHSC 1405
Cdd:cd14546   155 TYILIdMVLNRMAKGAKEIDIAATLEHLRDQRPGMVKTKDQFEFVLTA 202
PHA02738 PHA02738
hypothetical protein; Provisional
 1170-1401 9.90e-39

hypothetical protein; Provisional


Pssm-ID: 222923 [Multi-domain]  Cd Length: 320  Bit Score: 148.15  E-value: 9.90e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158303304 1170 EHPANITKNRYPHVLPYDHSRVRLTqlSGEPHSDYINANFIPGYSHPQEIIATQGPLKKTLEDFWRLVWEQQVHVIIMLT 1249
Cdd:PHA02738   45 AEKKNRKLNRYLDAVCFDHSRVILP--AERNRGDYINANYVDGFEYKKKFICGQAPTRQTCYDFYRMLWMEHVQIIVMLC 122

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158303304 1250 VGMENGRVLCEHYWP-VNSTPVTHGHITTHLLAEESEDEWTRREFQLQHGAEQKQrRVKQLQFTTWPDHSVPEAPSSLLA 1328
Cdd:PHA02738  123 KKKENGREKCFPYWSdVEQGSIRFGKFKITTTQVETHPHYVKSTLLLTDGTSATQ-TVTHFNFTAWPDHDVPKNTSEFLN 201

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158303304 1329 FV--------ELVQEEVKATQGKG---PILVHCSAGVGRTGTFVALLRLLRQLEEEQVVDVFNTVYILRLHRPLMIQTLS 1397
Cdd:PHA02738  202 FVlevrqcqkELAQESLQIGHNRLqppPIVVHCNAGLGRTPCYCVVDISISRFDACATVSIPSIVSSIRNQRYYSLFIPF 281


                  ....
gi 158303304 1398 QYIF 1401
Cdd:PHA02738  282 QYFF 285
PHA02747 PHA02747
protein tyrosine phosphatase; Provisional
 1147-1403 1.02e-38

protein tyrosine phosphatase; Provisional


Pssm-ID: 165114 [Multi-domain]  Cd Length: 312  Bit Score: 147.84  E-value: 1.02e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158303304 1147 HQAFFQEFEELKEvgkdqprlEAEHPANITKNRYPHVLPYDHSRVRLTQLSGEPhSDYINANFIPGYSHPQEIIATQGPL 1226
Cdd:PHA02747   32 HQIILKPFDGLIA--------NFEKPENQPKNRYWDIPCWDHNRVILDSGGGST-SDYIHANWIDGFEDDKKFIATQGPF 102

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158303304 1227 KKTLEDFWRLVWEQQVHVIIMLT-VGMENGRVLCEHYWPV--NSTPVTHGHItTHLLAEESEDEWTRREFQLQHGAEQKQ 1303
Cdd:PHA02747  103 AETCADFWKAVWQEHCSIIVMLTpTKGTNGEEKCYQYWCLneDGNIDMEDFR-IETLKTSVRAKYILTLIEITDKILKDS 181

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158303304 1304 RRVKQLQFTTWPdhsVPEAPSSLLAFVELVQ--EEVKATQGK---------GPILVHCSAGVGRTGTFVALLRLLRQLEE 1372
Cdd:PHA02747  182 RKISHFQCSEWF---EDETPSDHPDFIKFIKiiDINRKKSGKlfnpkdallCPIVVHCSDGVGKTGIFCAVDICLNQLVK 258

                         250       260       270
                  ....*....|....*....|....*....|.
gi 158303304 1373 EQVVDVFNTVYILRLHRPLMIQTLSQYIFLH 1403
Cdd:PHA02747  259 RKAICLAKTAEKIREQRHAGIMNFDDYLFIQ 289
PTPc-N21 cd14598
catalytic domain of tyrosine-protein phosphatase non-receptor type 21; Tyrosine-protein ...
 1204-1407 4.60e-38

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: 142.81  E-value: 4.60e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158303304 1204 YINANFIPGYSHPQE--IIATQGPLKKTLEDFWRLVWEQQVHVIIMLTVGMENGRVLCEHYWP---VNSTPVTHGH--IT 1276
Cdd:cd14598     1 YINASHIKVTVGGKEwdYIATQGPLQNTCQDFWQMVWEQGVAIIAMVTAEEEGGREKSFRYWPrlgSRHNTVTYGRfkIT 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158303304 1277 THLLAEESEdeWTRREFQLQHGAEQKQRRVKQLQFTTWPDHSVPEAPSSLLAFVELVQEEVKATQGKG-------PILVH 1349
Cdd:cd14598    81 TRFRTDSGC--YATTGLKIKHLLTGQERTVWHLQYTDWPEHGCPEDLKGFLSYLEEIQSVRRHTNSTIdpkspnpPVLVH 158

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 158303304 1350 CSAGVGRTGTFVALLRLLRQLEEEQVVDVFNTVYILRLHRPLMIQTLSQYIFLHSCLL 1407
Cdd:cd14598   159 CSAGVGRTGVVILSEIMIACLEHNEMLDIPRVLDMLRQQRMMMVQTLSQYTFVYKVLI 216
PHA02742 PHA02742
protein tyrosine phosphatase; Provisional
 1174-1407 1.42e-37

protein tyrosine phosphatase; Provisional


Pssm-ID: 165109 [Multi-domain]  Cd Length: 303  Bit Score: 143.99  E-value: 1.42e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158303304 1174 NITKNRYPHVLPYDHSRVRLTQLSGepHSDYINANFIPGYSHPQEIIATQGPLKKTLEDFWRLVWEQQVHVIIMLTVGME 1253
Cdd:PHA02742   52 NMKKCRYPDAPCFDRNRVILKIEDG--GDDFINASYVDGHNAKGRFICTQAPLEETALDFWQAIFQDQVRVIVMITKIME 129

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158303304 1254 NGRVLCEHYW-PVNSTPVTHGHITTHLLAEESEDEWTRREFQLQHGAEQKQRRVKQLQFTTWPDHSVPEAPSSLLAFVEL 1332
Cdd:PHA02742  130 DGKEACYPYWmPHERGKATHGEFKIKTKKIKSFRNYAVTNLCLTDTNTGASLDIKHFAYEDWPHGGLPRDPNKFLDFVLA 209

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158303304 1333 VQE-----EV----KATQGKGPILVHCSAGVGRTGTFVALLRLLRQLEEEQVVDVFNTVYILRLHRPLMIQTLSQYIFLH 1403
Cdd:PHA02742  210 VREadlkaDVdikgENIVKEPPILVHCSAGLDRAGAFCAIDICISKYNERAIIPLLSIVRDLRKQRHNCLSLPQQYIFCY 289


                  ....
gi 158303304 1404 SCLL 1407
Cdd:PHA02742  290 FIVL 293
PTPc_plant_PTP1 cd17658
protein tyrosine phosphatase 1 from Arabidopsis thaliana and similar plant PTPs; Arabidopsis ...
 1204-1404 2.44e-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: 139.91  E-value: 2.44e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158303304 1204 YINANFIPGYSHPQ--EIIATQGPLKKTLEDFWRLVWEQQVHVIIMLTVGMENGRVL-CEHYWPVNS-TPVTHGHIT-TH 1278
Cdd:cd17658     1 YINASLVETPASESlpKFIATQGPLPHTFEDFWEMVIQQRCPVIIMLTRLVDNYSTAkCADYFPAEEnESREFGRISvTN 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158303304 1279 LLAEESEDEWTRREFQLQHGAEQKQ-RRVKQLQFTTWPDHSVPeapssllAFVELVQEEVKATQG----KGPILVHCSAG 1353
Cdd:cd17658    81 KKLKHSQHSITLRVLEVQYIESEEPpLSVLHIQYPEWPDHGVP-------KDTRSVRELLKRLYGippsAGPIVVHCSAG 153

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 158303304 1354 VGRTGTFVALLRLLRQLEEEQV--VDVFNTVYILRLHRPLMIQTLSQYIFLHS 1404
Cdd:cd17658   154 IGRTGAYCTIHNTIRRILEGDMsaVDLSKTVRKFRSQRIGMVQTQDQYIFCYA 206
COG5599 COG5599
Protein tyrosine phosphatase [Signal transduction mechanisms];
1148-1402 9.27e-36

Protein tyrosine phosphatase [Signal transduction mechanisms];


Pssm-ID: 444335 [Multi-domain]  Cd Length: 282  Bit Score: 137.92  E-value: 9.27e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158303304 1148 QAFFQEFEELKEVGKDQpRLEAEHPANIT---KNRYPHVLPYDHSRVRltqlsgePHSDYINANFIPGYShPQEIIATQG 1224
Cdd:COG5599    14 EKINSRLSTLTNELAPS-HNDPQYLQNINgspLNRFRDIQPYKETALR-------ANLGYLNANYIQVIG-NHRYIATQY 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158303304 1225 PLKKTLEDFWRLVWEQQVHVIIMLT--VGMENGRVLCEHYWPVNSTpvtHGHITTHLLAEESE---DEWTRREFQL-QHG 1298
Cdd:COG5599    85 PLEEQLEDFFQMLFDNNTPVLVVLAsdDEISKPKVKMPVYFRQDGE---YGKYEVSSELTESIqlrDGIEARTYVLtIKG 161

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158303304 1299 AEQKQRRVKQLQFTTWPDHSVPEApSSLLAFVELV-QEEVKATQGKGPILVHCSAGVGRTGTFVALL--RLLRQLEEEQV 1375
Cdd:COG5599   162 TGQKKIEIPVLHVKNWPDHGAISA-EALKNLADLIdKKEKIKDPDKLLPVVHCRAGVGRTGTLIACLalSKSINALVQIT 240

                         250       260
                  ....*....|....*....|....*...
gi 158303304 1376 VDVFNTVYILRLHR-PLMIQTLSQYIFL 1402
Cdd:COG5599   241 LSVEEIVIDMRTSRnGGMVQTSEQLDVL 268
PTPc_motif smart00404
Protein tyrosine phosphatase, catalytic domain motif;
1306-1408 7.73e-35

Protein tyrosine phosphatase, catalytic domain motif;


Pssm-ID: 214649 [Multi-domain]  Cd Length: 105  Bit Score: 129.02  E-value: 7.73e-35
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158303304   1306 VKQLQFTTWPDHSVPEAPSSLLAFVELVQEEVKATQGKGPILVHCSAGVGRTGTFVA-LLRLLRQLEEEQVVDVFNTVYI 1384
Cdd:smart00404    2 VKHYHYTGWPDHGVPESPDSILELLRAVKKNLNQSESSGPVVVHCSAGVGRTGTFVAiDILLQQLEAEAGEVDIFDTVKE 81

                            90       100
                    ....*....|....*....|....
gi 158303304   1385 LRLHRPLMIQTLSQYIFLHSCLLN 1408
Cdd:smart00404   82 LRSQRPGMVQTEEQYLFLYRALLE 105
PTPc_DSPc smart00012
Protein tyrosine phosphatase, catalytic domain, undefined specificity; Protein tyrosine ...
 1306-1408 7.73e-35

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: 129.02  E-value: 7.73e-35
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158303304   1306 VKQLQFTTWPDHSVPEAPSSLLAFVELVQEEVKATQGKGPILVHCSAGVGRTGTFVA-LLRLLRQLEEEQVVDVFNTVYI 1384
Cdd:smart00012    2 VKHYHYTGWPDHGVPESPDSILELLRAVKKNLNQSESSGPVVVHCSAGVGRTGTFVAiDILLQQLEAEAGEVDIFDTVKE 81

                            90       100
                    ....*....|....*....|....
gi 158303304   1385 LRLHRPLMIQTLSQYIFLHSCLLN 1408
Cdd:smart00012   82 LRSQRPGMVQTEEQYLFLYRALLE 105
PHA02746 PHA02746
protein tyrosine phosphatase; Provisional
 1172-1412 3.00e-34

protein tyrosine phosphatase; Provisional


Pssm-ID: 165113 [Multi-domain]  Cd Length: 323  Bit Score: 135.16  E-value: 3.00e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158303304 1172 PANITKNRYPHVLPYDHSRV-------------------RLTQLSGEPHSDYINANFIPGYSHPQEIIATQGPLKKTLED 1232
Cdd:PHA02746   49 KENLKKNRFHDIPCWDHSRVvinaheslkmfdvgdsdgkKIEVTSEDNAENYIHANFVDGFKEANKFICAQGPKEDTSED 128

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158303304 1233 FWRLVWEQQVHVIIMLTvGMENGRVLCEHYWPV-NSTPVTHGHITTHLLAEESEDEWTRREFQLQHGAEQKQRRVKQLQF 1311
Cdd:PHA02746  129 FFKLISEHESQVIVSLT-DIDDDDEKCFELWTKeEDSELAFGRFVAKILDIIEELSFTKTRLMITDKISDTSREIHHFWF 207

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158303304 1312 TTWPDHSVPEAPSSLLAFVELVQEEVKA--------TQGKGPILVHCSAGVGRTGTFVALLRLLRQLEEEQVVDVFNTVY 1383
Cdd:PHA02746  208 PDWPDNGIPTGMAEFLELINKVNEEQAElikqadndPQTLGPIVVHCSAGIGRAGTFCAIDNALEQLEKEKEVCLGEIVL 287

                         250       260
                  ....*....|....*....|....*....
gi 158303304 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 2.48e-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: 125.51  E-value: 2.48e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158303304 1204 YINANFIPGYSHPQEIIATQGPLKKTLEDFWRLVWEQQVHVIIMLTVGMENGRvlCEHYWPVNSTPVTHGHITTHLLAEE 1283
Cdd:cd14550     1 YINASYLQGYRRSNEFIITQHPLEHTIKDFWQMIWDHNSQTIVMLTDNELNED--EPIYWPTKEKPLECETFKVTLSGED 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158303304 1284 -----SEDEWTRREFQLQHGAEQKQRRVKQLQFTTWPDHSVPeaPSSLLAFVELVQEEvkATQGKGPILVHCSAGVGRTG 1358
Cdd:cd14550    79 hsclsNEIRLIVRDFILESTQDDYVLEVRQFQCPSWPNPCSP--IHTVFELINTVQEW--AQQRDGPIVVHDRYGGVQAA 154

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....
gi 158303304 1359 TFVALLRLLRQLEEEQVVDVFNTVYILRLHRPLMIQTLSQYIFL 1402
Cdd:cd14550   155 TFCALTTLHQQLEHESSVDVYQVAKLYHLMRPGVFTSKEDYQFL 198
R-PTPc-T-2 cd14634
PTP domain of receptor-type tyrosine-protein phosphatase T, repeat 2; Receptor-type ...
 1204-1408 1.81e-29

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: 117.43  E-value: 1.81e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158303304 1204 YINANFIPGYSHPQEIIATQGPLKKTLEDFWRLVWEQQVHVIIMLTvGMENGRvLCEHYWPvNSTPVTHGHITTHLLAEE 1283
Cdd:cd14634     1 YINAALMDSHKQPAAFIVTQHPLPNTVADFWRLVFDYNCSSVVMLN-EMDAAQ-LCMQYWP-EKTSCCYGPIQVEFVSAD 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158303304 1284 SEDEWTRREFQLQHGAEQKQ--RRVKQLQFTTWPDH-SVPEAPSSLLAFVE-LVQEEVKATQGKGPILVHCSAGVGRTGT 1359
Cdd:cd14634    78 IDEDIISRIFRICNMARPQDgyRIVQHLQYIGWPAYrDTPPSKRSILKVVRrLEKWQEQYDGREGRTVVHCLNGGGRSGT 157

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*....
gi 158303304 1360 FVALLRLLRQLEEEQVVDVFNTVYILRLHRPLMIQTLSQYIFLHSCLLN 1408
Cdd:cd14634   158 FCAICSVCEMIQQQNIIDVFHTVKTLRNNKSNMVETLEQYKFVYEVALE 206
R-PTP-Z-2 cd17669
catalytic domain of receptor-type tyrosine-protein phosphatase Z, repeat 2; Receptor-type ...
 1204-1407 2.04e-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: 117.40  E-value: 2.04e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158303304 1204 YINANFIPGYSHPQEIIATQGPLKKTLEDFWRLVWEQQVHVIIMLTvgmeNGRVLCEH---YWPVNSTPVTHGHITTHLL 1280
Cdd:cd17669     1 YINASYIMGYYQSNEFIITQHPLLHTIKDFWRMIWDHNAQLIVMLP----DGQNMAEDefvYWPNKDEPINCETFKVTLI 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158303304 1281 AEE-----SEDEWTRREFQLQHGAEQKQRRVKQLQFTTWPDhsvPEAP-SSLLAFVELVQEEvkATQGKGPILVHCSAGV 1354
Cdd:cd17669    77 AEEhkclsNEEKLIIQDFILEATQDDYVLEVRHFQCPKWPN---PDSPiSKTFELISIIKEE--AANRDGPMIVHDEHGG 151

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 158303304 1355 GRTGTFVALLRLLRQLEEEQVVDVFNTVYILRLHRPLMIQTLSQYIFLHSCLL 1407
Cdd:cd17669   152 VTAGTFCALTTLMHQLEKENSVDVYQVAKMINLMRPGVFTDIEQYQFLYKAIL 204
R-PTPc-M-2 cd14635
PTP domain of receptor-type tyrosine-protein phosphatase M, repeat 2; Receptor-type ...
 1204-1407 3.93e-29

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: 116.33  E-value: 3.93e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158303304 1204 YINANFIPGYSHPQEIIATQGPLKKTLEDFWRLVWEQQVHVIIMLTvgMENGRVLCEHYWPVNSTPvTHGHITTHLLAEE 1283
Cdd:cd14635     1 YINAALMDSYKQPSAFIVTQHPLPNTVKDFWRLVLDYHCTSIVMLN--DVDPAQLCPQYWPENGVH-RHGPIQVEFVSAD 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158303304 1284 SEDEWTRREFQLQHGAEQKQ--RRVKQLQFTTWPDHSvpEAPSSLLAFVELVQEEVKATQ----GKGPILVHCSAGVGRT 1357
Cdd:cd14635    78 LEEDIISRIFRIYNAARPQDgyRMVQQFQFLGWPMYR--DTPVSKRSFLKLIRQVDKWQEeyngGEGRTVVHCLNGGGRS 155

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|
gi 158303304 1358 GTFVALLRLLRQLEEEQVVDVFNTVYILRLHRPLMIQTLSQYIFLHSCLL 1407
Cdd:cd14635   156 GTFCAISIVCEMLRHQRAVDVFHAVKTLRNNKPNMVDLLDQYKFCYEVAL 205
R-PTP-G-2 cd17670
PTP-like domain of receptor-type tyrosine-protein phosphatase G, repeat 2; Receptor-type ...
 1204-1408 1.85e-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: 108.61  E-value: 1.85e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158303304 1204 YINANFIPGYSHPQEIIATQGPLKKTLEDFWRLVWEQQVHVIIMLTvgmeNGRVLCEH---YWP-----VNSTPVTHGHI 1275
Cdd:cd17670     1 YINASYIMGYYRSNEFIITQHPLPHTTKDFWRMIWDHNAQIIVMLP----DNQGLAEDefvYWPsreesMNCEAFTVTLI 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158303304 1276 TTHLLAEESEDEWTRREFQLQHGAEQKQRRVKQLQFTTWPDhsvPEAP-SSLLAFVELVQEEvkATQGKGPILVHCSAGV 1354
Cdd:cd17670    77 SKDRLCLSNEEQIIIHDFILEATQDDYVLEVRHFQCPKWPN---PDAPiSSTFELINVIKEE--ALTRDGPTIVHDEFGA 151

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....
gi 158303304 1355 GRTGTFVALLRLLRQLEEEQVVDVFNTVYILRLHRPLMIQTLSQYIFLHSCLLN 1408
Cdd:cd17670   152 VSAGTLCALTTLSQQLENENAVDVYQVAKMINLMRPGVFTDIEQYQFLYKAMLS 205
R-PTPc-U-2 cd14637
PTP domain of receptor-type tyrosine-protein phosphatase U, repeat 2; Receptor-type ...
 1204-1407 5.22e-26

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: 107.30  E-value: 5.22e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158303304 1204 YINANFIPGYSHPQEIIATQGPLKKTLEDFWRLVWEQQVHVIIMLT-VGMENGRVLCEHYWPvNSTPVTHGHITTHLLAE 1282
Cdd:cd14637     1 YINAALTDSYTRSAAFIVTLHPLQNTTTDFWRLVYDYGCTSVVMLNqLNQSNSAWPCLQYWP-EPGLQQYGPMEVEFVSG 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158303304 1283 ESEDEWTRREFQLQHGA--EQKQRRVKQLQFTTW-PDHSVPEAPSS---LLAFVELVQEEvkatQGKGPILVHCSAGVGR 1356
Cdd:cd14637    80 SADEDIVTRLFRVQNITrlQEGHLMVRHFQFLRWsAYRDTPDSKKAflhLLASVEKWQRE----SGEGRTVVHCLNGGGR 155

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|.
gi 158303304 1357 TGTFVALLRLLRQLEEEQVVDVFNTVYILRLHRPLMIQTLSQYIFLHSCLL 1407
Cdd:cd14637   156 SGTYCASAMILEMIRCHNIVDVFYAVKTLRNYKPNMVETLEQYRFCYEIAL 206
R-PTPc-K-2 cd14636
PTP domain of receptor-type tyrosine-protein phosphatase K, repeat 2; Receptor-type ...
 1204-1407 5.96e-26

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: 107.42  E-value: 5.96e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158303304 1204 YINANFIPGYSHPQEIIATQGPLKKTLEDFWRLVWEQQVHVIIMLT-VGMENGrvlCEHYWPVNSTpVTHGHITTHLLAE 1282
Cdd:cd14636     1 YINAALMDSYRQPAAFIVTQHPLPNTVKDFWRLVYDYGCTSIVMLNeVDLAQG---CPQYWPEEGM-LRYGPIQVECMSC 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158303304 1283 ESEDEWTRREFQLQHGAEQKQ--RRVKQLQFTTWPDHSvpEAPSSLLAFVELV------QEEVKatQGKGPILVHCSAGV 1354
Cdd:cd14636    77 SMDCDVISRIFRICNLTRPQEgyLMVQQFQYLGWASHR--EVPGSKRSFLKLIlqvekwQEECD--EGEGRTIIHCLNGG 152

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 158303304 1355 GRTGTFVALLRLLRQLEEEQVVDVFNTVYILRLHRPLMIQTLSQYIFLHSCLL 1407
Cdd:cd14636   153 GRSGMFCAISIVCEMIKRQNVVDVFHAVKTLRNSKPNMVETPEQYRFCYDVAL 205
R-PTPc-V cd14618
catalytic domain of receptor-type tyrosine-protein phosphatase V; Receptor-type ...
 1477-1692 1.28e-20

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: 92.70  E-value: 1.28e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158303304 1477 HSQEQLALVEESPADNMLAASLFPGGPSGRDHVVltgSAGP-----KELWEMVWEHGAYVLVSL--GLPDTKEKPQDIWP 1549
Cdd:cd14618    11 HSRVRLSQLGGEPHSDYINANFIPGYTSPQEFIA---TQGPlkktiEDFWRLVWEQQVCNIIMLtvGMENGRVLCDHYWP 87

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158303304 1550 MEMQPIVTDMVTVHRVAESNTAGWPSTLIRVIHGDSGTERQVQCLQFPHCETGS--ELPAnTLLTFLDAVGQCCSrgNSK 1627
Cdd:cd14618    88 SESTPVSYGHITVHLLAQSSEDEWTRREFKLWHEDLRKERRVKHLHYTAWPDHGipESTS-SLMAFRELVREHVQ--ATK 164

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 158303304 1628 KPGTLLSHSSKVTNQLSTFLAMEQLLQQAGTERTVDVFSVALKQTQACGLKTPTLEQYIYLYNCL 1692
Cdd:cd14618   165 GKGPTLVHCSAGVGRSGTFIALDRLLRQLKEEKVVDVFNTVYILRMHRYLMIQTLSQYIFLHSCI 229
R3-PTPc cd14548
catalytic domain of R3 subfamily receptor-type tyrosine-protein phosphatases and similar ...
 1477-1689 7.13e-17

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: 81.63  E-value: 7.13e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158303304 1477 HSQEQLALVEESPADNMLAASLFPGGPSGRDHVVltgSAGP-----KELWEMVWEHGAYVLVSL--GLPDTKEKPQDIWP 1549
Cdd:cd14548    10 HSRVKLIPINEEEGSDYINANYIPGYNSPREFIA---TQGPlpgtkDDFWRMVWEQNSHTIVMLtqCMEKGRVKCDHYWP 86

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158303304 1550 MEMQPIVTDMVTVHRVAESNTAGWPSTLIRVIHGD-SGTERQVQCLQFPHCETGSelPANTLLTFLDAVGQccSRGNSKK 1628
Cdd:cd14548    87 FDQDPVYYGDITVTMLSESVLPDWTIREFKLERGDeVRSVRQFHFTAWPDHGVPE--APDSLLRFVRLVRD--YIKQEKG 162

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 158303304 1629 PgtLLSHSSKVTNQLSTFLAMEQLLQQAGTERTVDVFSVALKQTQACGLKTPTLEQYIYLY 1689
Cdd:cd14548   163 P--TIVHCSAGVGRTGTFIALDRLLQQIESEDYVDIFGIVYDLRKHRPLMVQTEAQYIFLH 221
PTPc cd00047
catalytic domain of protein tyrosine phosphatases; Protein tyrosine phosphatases (PTP, EC 3.1. ...
 1521-1689 6.52e-14

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: 72.32  E-value: 6.52e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158303304 1521 WEMVWEHGAYVLVSLG--LPDTKEKPQDIWPMEM-QPIVTDMVTVHRVAESNTAGWPSTLIRVIHGDSGTERQVQCLQFP 1597
Cdd:cd00047    31 WRMVWEQKVSVIVMLTnlVEKGREKCERYWPEEGgKPLEYGDITVTLVSEEELSDYTIRTLELSPKGCSESREVTHLHYT 110

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158303304 1598 HCETGSeLPANT--LLTFLDAVgqCCSRGNSKKPgtLLSHSSKVTNQLSTFLAMEQLLQQAGTERTVDVFSVALKQ-TQA 1674
Cdd:cd00047   111 GWPDHG-VPSSPedLLALVRRV--RKEARKPNGP--IVVHCSAGVGRTGTFIAIDILLERLEAEGEVDVFEIVKALrKQR 185

                         170
                  ....*....|....*
gi 158303304 1675 CGLKTpTLEQYIYLY 1689
Cdd:cd00047   186 PGMVQ-TLEQYEFIY 199
PTPc smart00194
Protein tyrosine phosphatase, catalytic domain;
1521-1692 8.20e-14

Protein tyrosine phosphatase, catalytic domain;


Pssm-ID: 214550 [Multi-domain]  Cd Length: 259  Bit Score: 73.46  E-value: 8.20e-14
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158303304   1521 WEMVWEHGAYVLVSLGLPD--TKEKPQDIWPMEM-QPIVTDMVTVHRVAESNTAGWPSTLIRVIHGDSGTERQVQCLQF- 1596
Cdd:smart00194   86 WRMVWEQKVTVIVMLTELVekGREKCAQYWPDEEgEPLTYGDITVTLKSVEKVDDYTIRTLEVTNTGCSETRTVTHYHYt 165

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158303304   1597 --PHCETgselPANT--LLTFLDAVGQCCSRGNskkpGTLLSHSSKVTNQLSTFLAMEQLLQQAGTERTVDVFSVALK-Q 1671
Cdd:smart00194  166 nwPDHGV----PESPesILDLIRAVRKSQSTST----GPIVVHCSAGVGRTGTFIAIDILLQQLEAGKEVDIFEIVKElR 237

                           170       180
                    ....*....|....*....|.
gi 158303304   1672 TQACGLkTPTLEQYIYLYNCL 1692
Cdd:smart00194  238 SQRPGM-VQTEEQYIFLYRAI 257
Y_phosphatase pfam00102
Protein-tyrosine phosphatase;
1518-1692 9.82e-13

Protein-tyrosine phosphatase;


Pssm-ID: 459674 [Multi-domain]  Cd Length: 234  Bit Score: 69.58  E-value: 9.82e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158303304  1518 KELWEMVWEHGAYVLVSLGLPD--TKEKPQDIWPMEM-QPIVTDMVTVH-RVAESNTAGWPSTLIRVIHGDSGTERQVQC 1593
Cdd:pfam00102   56 EDFWRMVWEEKVTIIVMLTELEekGREKCAQYWPEEEgESLEYGDFTVTlKKEKEDEKDYTVRTLEVSNGGSEETRTVKH 135

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158303304  1594 LQF---PHCETgselPANT--LLTFLDAVGQCCSRGNSkkpGTLLSHSSKVTNQLSTFLAMEQLLQQAGTERTVDVFSVA 1668
Cdd:pfam00102  136 FHYtgwPDHGV----PESPnsLLDLLRKVRKSSLDGRS---GPIVVHCSAGIGRTGTFIAIDIALQQLEAEGEVDIFQIV 208

                          170       180
                   ....*....|....*....|....*
gi 158303304  1669 LK-QTQACGLKTpTLEQYIYLYNCL 1692
Cdd:pfam00102  209 KElRSQRPGMVQ-TLEQYIFLYDAI 232
R-PTPc-J cd14615
catalytic domain of receptor-type tyrosine-protein phosphatase J; Receptor-type ...
 1470-1691 2.62e-11

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


Pssm-ID: 350463 [Multi-domain]  Cd Length: 229  Bit Score: 65.22  E-value: 2.62e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158303304 1470 NSIASCHHSQEQLaLVEESPADNMLAASLFPGGPSGRDHVvltGSAGP-----KELWEMVWEHGAYVLVSLG--LPDTKE 1542
Cdd:cd14615     4 NNVLPYDISRVKL-SVQSHSTDDYINANYMPGYNSKKEFI---AAQGPlpntvKDFWRMVWEKNVYAIVMLTkcVEQGRT 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158303304 1543 KPQDIWPMEMQPIVTDMvTVHRVAESNTAGWPSTLIRVIHGDSGTERQVQCLQFP----HcetgsELPANT--LLTFLDA 1616
Cdd:cd14615    80 KCEEYWPSKQKKDYGDI-TVTMTSEIVLPEWTIRDFTVKNAQTNESRTVRHFHFTswpdH-----GVPETTdlLINFRHL 153

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 158303304 1617 VGQCCSRGNSKKPgtLLSHSSKVTNQLSTFLAMEQLLQQAGTERTVDVFSVALKQTQACGLKTPTLEQYIYLYNC 1691
Cdd:cd14615   154 VREYMKQNPPNSP--ILVHCSAGVGRTGTFIAIDRLIYQIENENVVDVYGIVYDLRMHRPLMVQTEDQYVFLNQC 226
R5-PTP-2 cd14550
PTP-like domain of R5 subfamily receptor-type tyrosine-protein phosphatases, repeat 2; The R5 ...
 1518-1690 3.83e-11

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: 64.26  E-value: 3.83e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158303304 1518 KELWEMVWEHGAYVLVSLGLPDTKEKPQDIWPMEMQPIVTDMVTVHRVAESNTAgwPSTLIRVIHGDSGTE--------- 1588
Cdd:cd14550    28 KDFWQMIWDHNSQTIVMLTDNELNEDEPIYWPTKEKPLECETFKVTLSGEDHSC--LSNEIRLIVRDFILEstqddyvle 105

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158303304 1589 -RQVQCLQFPHCETgselPANTLLTFLDAVgqccSRGNSKKPGTLLSHSSKVTNQLSTFLAMEQLLQQAGTERTVDVFSV 1667
Cdd:cd14550   106 vRQFQCPSWPNPCS----PIHTVFELINTV----QEWAQQRDGPIVVHDRYGGVQAATFCALTTLHQQLEHESSVDVYQV 177

                         170       180
                  ....*....|....*....|....*..
gi 158303304 1668 AlKQTQacgLKTP----TLEQYIYLYN 1690
Cdd:cd14550   178 A-KLYH---LMRPgvftSKEDYQFLYK 200
R-PTPc-H cd14619
catalytic domain of receptor-type tyrosine-protein phosphatase H; Receptor-type ...
 1477-1692 4.62e-11

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


Pssm-ID: 350467 [Multi-domain]  Cd Length: 233  Bit Score: 64.52  E-value: 4.62e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158303304 1477 HSQEQLALVEESPADNMLAASLFPGGPSGRDHVvltGSAGP-----KELWEMVWEHGAYVLVSLG--LPDTKEKPQDIWP 1549
Cdd:cd14619    11 WSRVPLKPIHEEPGSDYINANYMPGYWSSQEFI---ATQGPlpqtvGDFWRMIWEQQSSTIVMLTncMEAGRVKCEHYWP 87

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158303304 1550 MEMQPIVTDMVTVHRVAESNTAGWPS---TLIRVIHGDSGTERQVQCLQFPhcETGSELPANTLLTFLDAVGQCCSRGNS 1626
Cdd:cd14619    88 LDYTPCTYGHLRVTVVSEEVMENWTVrefLLKQVEEQKTLSVRHFHFTAWP--DHGVPSSTDTLLAFRRLLRQWLDQTMS 165

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 158303304 1627 KKPGTLlsHSSKVTNQLSTFLAMEQLLQQAGTERTVDVFSVALKQTQACGLKTPTLEQYIYLYNCL 1692
Cdd:cd14619   166 GGPTVV--HCSAGVGRTGTLIALDVLLQQLQSEGLLGPFSFVQKMRENRPLMVQTESQYVFLHQCI 229
FN3 COG3401
Fibronectin type 3 domain [General function prediction only];
378-749 5.69e-11

Fibronectin type 3 domain [General function prediction only];


Pssm-ID: 442628 [Multi-domain]  Cd Length: 603  Bit Score: 67.33  E-value: 5.69e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158303304  378 YDAWVEGSIWLAESAARPMEVPGARLWLEGLEATKQPGRRALLYSVDAPGLLGNISVSSGATHV-TFCGLVPGAHYRVDI 456
Cdd:COG3401    42 VVLSVTTKESPGTLLVAAGLSSGGGLGTGGRAGTTSGVAAVAVAAAPPTATGLTTLTGSGSVGGaTNTGLTSSDEVPSPA 121

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158303304  457 ASSMGDITQSLTGYTSPLPPQSLEIISRNSPSDLTIGWAPAPGQMEGYKVTWHqDGSQRSPGDLVDLGPDISSLTLKSLV 536
Cdd:COG3401   122 VGTATTATAVAGGAATAGTYALGAGLYGVDGANASGTTASSVAGAGVVVSPDT-SATAAVATTSLTVTSTTLVDGGGDIE 200

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158303304  537 PGSCYTVSAWAW-SGNLSSDSQKIH---SCTRPAPPTNLSlGFAHQPATLRASWcHPPGGRDAFQLRLYRlRPLTLESEK 612
Cdd:COG3401   201 PGTTYYYRVAATdTGGESAPSNEVSvttPTTPPSAPTGLT-ATADTPGSVTLSW-DPVTESDATGYRVYR-SNSGDGPFT 277

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158303304  613 ILSQEAQN-FSWAQLPAG--YEFQVQLSTLWGsEESGSAN----TTGWTPPSAPTLVNVTSEAPTQLHVSWVHAAG-DRS 684
Cdd:COG3401   278 KVATVTTTsYTDTGLTNGttYYYRVTAVDAAG-NESAPSNvvsvTTDLTPPAAPSGLTATAVGSSSITLSWTASSDaDVT 356

                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 158303304  685 SYQVtLYQESTRTATSIVGPKADSTSFW--GLTPGTK--YKVEAISWAGPLYTAAANVSAWTYPLTPNE 749
Cdd:COG3401   357 GYNV-YRSTSGGGTYTKIAETVTTTSYTdtGLTPGTTyyYKVTAVDAAGNESAPSEEVSATTASAASGE 424
R-PTPc-B cd14617
catalytic domain of receptor-type tyrosine-protein phosphatase B; Receptor-type ...
 1470-1689 6.67e-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: 61.09  E-value: 6.67e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158303304 1470 NSIASCHHSQEQLALVEESPADNMLAASLFPGGPSGRDHVVLTGS-AGPKE-LWEMVWEHGAY--VLVSLGLPDTKEKPQ 1545
Cdd:cd14617     4 NNILPYDSTRVKLSNVDDDPCSDYINASYIPGNNFRREYIATQGPlPGTKDdFWKMVWEQNVHniVMVTQCVEKGRVKCD 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158303304 1546 DIWPMEMQPIVTDMVTVHRVAESNTAGWPSTLIRVIhgdsgTERQVQC----LQFPHC---ETGSELPANTLLTFLDAVG 1618
Cdd:cd14617    84 HYWPADQDSLYYGDLIVQMLSESVLPEWTIREFKIC-----SEEQLDAprlvRHFHYTvwpDHGVPETTQSLIQFVRTVR 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158303304 1619 QCCSRGNSkkPGTLLSHSSKVTNQLSTFLAMEQLLQQAGTERTVDVFS---------VALKQTQAcglktptleQYIYLY 1689
Cdd:cd14617   159 DYINRTPG--SGPTVVHCSAGVGRTGTFIALDRILQQLDSKDSVDIYGavhdlrlhrVHMVQTEC---------QYVYLH 227
R-PTPc-D-1 cd14624
catalytic domain of receptor-type tyrosine-protein phosphatase D, repeat 1; Receptor-type ...
 1422-1696 6.73e-10

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: 62.06  E-value: 6.73e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158303304 1422 PIPVMNFAQACAKRAANANAGFLKEYRLL---KQAIKDETGSLLPSPDYNQNSIASCHHSQEQLALVEESPADNMLAASL 1498
Cdd:cd14624     3 PIPILELADHIERLKANDNLKFSQEYESIdpgQQFTWEHSNLEVNKPKNRYANVIAYDHSRVLLSAIEGIPGSDYINANY 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158303304 1499 FPGGPSGRDHVVLTGSAgPK---ELWEMVWEH-GAYVLVSLGLPD-TKEKPQDIWPMEMQPiVTDMVTVHRVAESNTAGW 1573
Cdd:cd14624    83 IDGYRKQNAYIATQGAL-PEtfgDFWRMIWEQrSATVVMMTKLEErSRVKCDQYWPSRGTE-TYGLIQVTLLDTVELATY 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158303304 1574 PSTLIRVIHGDSGTERQVQCLQFPHC-ETGSELPANTLLTFLDAVGQCcsrgNSKKPGTLLSHSSKVTNQLSTFLAMEQL 1652
Cdd:cd14624   161 CVRTFALYKNGSSEKREVRQFQFTAWpDHGVPEHPTPFLAFLRRVKTC----NPPDAGPMVVHCSAGVGRTGCFIVIDAM 236

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*
gi 158303304 1653 LQQAGTERTVDVFS-VALKQTQAcGLKTPTLEQYIYLYNCLNSAL 1696
Cdd:cd14624   237 LERIKHEKTVDIYGhVTLMRAQR-NYMVQTEDQYIFIHDALLEAV 280
R-PTP-C-2 cd14558
PTP-like domain of receptor-type tyrosine-protein phosphatase C, repeat 2; Receptor-type ...
 1519-1689 9.60e-10

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: 60.10  E-value: 9.60e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158303304 1519 ELWEMVWEHGAYVLVSLGlpDTKEKPQDI----WPMEMQpIVTDMVtvhrVAESNTAGWPSTLIRVI---HGDSGTERQV 1591
Cdd:cd14558    29 DFWQMIFQKKVKVIVMLT--ELKEGDQEQcaqyWGDEKK-TYGDIE----VELKDTEKSPTYTVRVFeitHLKRKDSRTV 101

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158303304 1592 QCLQFPHCeTGSELPAN--TLLTFLDAVGQCCSRGNSKKPGT--LLSHSSKVTNQLSTFLAMEQLLQQAGTERTVDVFSV 1667
Cdd:cd14558   102 YQYQYHKW-KGEELPEKpkDLVDMIKSIKQKLPYKNSKHGRSvpIVVHCSDGSSRTGIFCALWNLLESAETEKVVDVFQV 180

                         170       180
                  ....*....|....*....|....*
gi 158303304 1668 A---LKQTQACglkTPTLEQYIYLY 1689
Cdd:cd14558   181 VkalRKQRPGM---VSTLEQYQFLY 202
R-PTP-Z-2 cd17669
catalytic domain of receptor-type tyrosine-protein phosphatase Z, repeat 2; Receptor-type ...
 1518-1692 1.46e-09

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: 59.62  E-value: 1.46e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158303304 1518 KELWEMVWEHGAYVLVSlgLPDTKEKPQD---IWPMEMQPIVTDMVTVHRVAE-----SNTAGW--PSTLIRVIHGDSGT 1587
Cdd:cd17669    28 KDFWRMIWDHNAQLIVM--LPDGQNMAEDefvYWPNKDEPINCETFKVTLIAEehkclSNEEKLiiQDFILEATQDDYVL 105

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158303304 1588 E-RQVQCLQFPHCETgselPANTLLTFLDAVGQccsrGNSKKPGTLLSHSSKVTNQLSTFLAMEQLLQQAGTERTVDVFS 1666
Cdd:cd17669   106 EvRHFQCPKWPNPDS----PISKTFELISIIKE----EAANRDGPMIVHDEHGGVTAGTFCALTTLMHQLEKENSVDVYQ 177

                         170       180       190
                  ....*....|....*....|....*....|
gi 158303304 1667 VAlkqtQACGLKTP----TLEQYIYLYNCL 1692
Cdd:cd17669   178 VA----KMINLMRPgvftDIEQYQFLYKAI 203
R-PTPc-O cd14614
catalytic domain of receptor-type tyrosine-protein phosphatase O; Receptor-type ...
 1478-1692 4.02e-09

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


Pssm-ID: 350462 [Multi-domain]  Cd Length: 245  Bit Score: 59.13  E-value: 4.02e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158303304 1478 SQEQLALVEESPADNMLAASLFPGGPSGRDHVvltGSAGP-----KELWEMVWEHGAYVLVSLGLPDTKE--KPQDIWPM 1550
Cdd:cd14614    27 SRVKLVSMHEEEGSDYINANYIPGYNSPQEYI---ATQGPlpetrNDFWKMVLQQKSQIIVMLTQCNEKRrvKCDHYWPF 103

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158303304 1551 EMQPIVTDMVTVHRVAESNTAGWPSTLIRVIHGDsgterQVQCL------QFPHCETGSELPANTLLTFLDAVGQccsrG 1624
Cdd:cd14614   104 TEEPVAYGDITVEMLSEEEQPDWAIREFRVSYAD-----EVQDVmhfnytAWPDHGVPTANAAESILQFVQMVRQ----Q 174

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 158303304 1625 NSKKPGTLLSHSSKVTNQLSTFLAMEQLLQQAGTERTVDVFSVALKQTQACGLKTPTLEQYIYLYNCL 1692
Cdd:cd14614   175 AVKSKGPMIIHCSAGVGRTGTFIALDRLLQHIRDHEFVDILGLVSEMRSYRMSMVQTEEQYIFIHQCV 242
R-PTPc-A-1 cd14621
catalytic domain of receptor-type tyrosine-protein phosphatase A, repeat 1; Receptor-type ...
 1422-1692 1.32e-08

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: 58.50  E-value: 1.32e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158303304 1422 PIPVMNFAQACAKRAANANAGFLKEYRLLK----QAIKDETGSLLPSPDYNQNSIASCHHSQEQLALVEESPADNMLAAS 1497
Cdd:cd14621     7 PLPVDKLEEEINRRMADDNKLFREEFNALPacpiQATCEAASKEENKEKNRYVNILPYDHSRVHLTPVEGVPDSDYINAS 86

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158303304 1498 LFPGGpsgRDHVVLTGSAGPKE-----LWEMVWEHG-AYVLVSLGLPDTKE-KPQDIWPME-------MQPIVTDMVT-- 1561
Cdd:cd14621    87 FINGY---QEKNKFIAAQGPKEetvndFWRMIWEQNtATIVMVTNLKERKEcKCAQYWPDQgcwtygnIRVSVEDVTVlv 163

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158303304 1562 --------VHRVAESnTAGWPSTLIRVIHGDSGTERQVqclqfPHCETGselpantLLTFLDAVGQCcsrgNSKKPGTLL 1633
Cdd:cd14621   164 dytvrkfcIQQVGDV-TNKKPQRLITQFHFTSWPDFGV-----PFTPIG-------MLKFLKKVKNC----NPQYAGAIV 226

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 158303304 1634 SHSSKVTNQLSTFLAMEQLLQQAGTERTVDVFS-VALKQTQACGLkTPTLEQYIYLYNCL 1692
Cdd:cd14621   227 VHCSAGVGRTGTFIVIDAMLDMMHAERKVDVYGfVSRIRAQRCQM-VQTDMQYVFIYQAL 285
PHA02740 PHA02740
protein tyrosine phosphatase; Provisional
 1182-1406 2.51e-08

protein tyrosine phosphatase; Provisional


Pssm-ID: 165107 [Multi-domain]  Cd Length: 298  Bit Score: 57.28  E-value: 2.51e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158303304 1182 HVLPYDHSRVRLTQlsgepHSDYINANFIPGYSHPQEIIATQGPLKKTLEDFWRLVWEQQVHVIIMLTVGMENGRVlcEH 1261
Cdd:PHA02740   61 HITRLLHRRIKLFN-----DEKVLDARFVDGYDFEQKFICIINLCEDACDKFLQALSDNKVQIIVLISRHADKKCF--NQ 133

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158303304 1262 YWPVNSTPVthghITTHLLAEESEDEWTRREFQL-------QHGAEQKqrrVKQLQFTTWPDHSVPEAPSSLLAFVELVQ 1334
Cdd:PHA02740  134 FWSLKEGCV----ITSDKFQIETLEIIIKPHFNLtllsltdKFGQAQK---ISHFQYTAWPADGFSHDPDAFIDFFCNID 206

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 158303304 1335 ------EEVKATQGKGPILVHCSAGVGRTGTFVALLRLLRQLEEEQVVDVFNTVYILRLHRPLMIQTLSQYIFLHSCL 1406
Cdd:PHA02740  207 dlcadlEKHKADGKIAPIIIDCIDGISSSAVFCVFDICATEFDKTGMLSIANALKKVRQKKYGCMNCLDDYVFCYHLI 284
CDKN3-like cd14505
cyclin-dependent kinase inhibitor 3 and similar proteins; This family is composed of ...
 1289-1403 1.54e-07

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: 52.65  E-value: 1.54e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158303304 1289 TRREFQlQHGAEQKQRRVKQLQFTtWPDHSVPE--APSSLLAFVELVQEEVKATQGKGPILVHCSAGVGRTGTfVALLRL 1366
Cdd:cd14505    52 TDGELE-ELGVPDLLEQYQQAGIT-WHHLPIPDggVPSDIAQWQELLEELLSALENGKKVLIHCKGGLGRTGL-IAACLL 128

                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 158303304 1367 LRQLEEEQVVDVFNTVyilRLHRPLMIQTLSQYIFLH 1403
Cdd:cd14505   129 LELGDTLDPEQAIAAV---RALRPGAIQTPKQENFLH 162
PTP_YopH-like cd14559
YopH and related bacterial protein tyrosine phosphatases; Yersinia outer protein H (YopH) ...
 1220-1399 2.64e-07

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: 53.56  E-value: 2.64e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158303304 1220 IATQGPLKKTLEDFWRLVWEQQVHVIIMLTVGMENGRVLCEHYWPVNSTpvtHGHITT---HLLAEESEDEWTRREFQLQ 1296
Cdd:cd14559    32 IACQYPKNEQLEDHLKMLADNRTPCLVVLASNKDIQRKGLPPYFRQSGT---YGSVTVkskKTGKDELVDGLKADMYNLK 108

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158303304 1297 HGAEQKQRRVKQLQFTTWPDHSvpeaPSSLLAFVELVQEEVKATQGKGPIL-----------------VHCSAGVGRTGT 1359
Cdd:cd14559   109 ITDGNKTITIPVVHVTNWPDHT----AISSEGLKELADLVNKSAEEKRNFYkskgssaindknkllpvIHCRAGVGRTGQ 184

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|
gi 158303304 1360 FVALLRLLRQLEEEQVVDVFNTVYILRLHRplMIQTLSQY 1399
Cdd:cd14559   185 LAAAMELNKSPNNLSVEDIVSDMRTSRNGK--MVQKDEQL 222
FN3 COG3401
Fibronectin type 3 domain [General function prediction only];
461-765 3.20e-07

Fibronectin type 3 domain [General function prediction only];


Pssm-ID: 442628 [Multi-domain]  Cd Length: 603  Bit Score: 55.39  E-value: 3.20e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158303304  461 GDITQSLTGYTSPLPPQSLEIISRNSPSDLTIGWAPAPGQMEGYKVTWHQDGSQRSPGDLVDLGPDISSLTLKslVPGSC 540
Cdd:COG3401    32 SGKTILVYLAVVLSVTTKESPGTLLVAAGLSSGGGLGTGGRAGTTSGVAAVAVAAAPPTATGLTTLTGSGSVG--GATNT 109

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158303304  541 YTVSAWAWSGNLSSDSQKIHSCTRPAPPTNLSLGFAH------QPATLRASWCHPPGGRDAFQLRLYRLRPLTLESEKIL 614
Cdd:COG3401   110 GLTSSDEVPSPAVGTATTATAVAGGAATAGTYALGAGlygvdgANASGTTASSVAGAGVVVSPDTSATAAVATTSLTVTS 189

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158303304  615 SQEAQNFSWAQLPAGYEFQVQlSTLWGSEESGSAN---TTGWTPPSAPTLVNVTSEAPTQLHVSWV-HAAGDRSSYQVtL 690
Cdd:COG3401   190 TTLVDGGGDIEPGTTYYYRVA-ATDTGGESAPSNEvsvTTPTTPPSAPTGLTATADTPGSVTLSWDpVTESDATGYRV-Y 267

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158303304  691 YQESTRTATSIVGpKADSTSF--WGLTPGTKY--KVEAiswagplYTAAANVSAW----------TYPLTPNELLASMQA 756
Cdd:COG3401   268 RSNSGDGPFTKVA-TVTTTSYtdTGLTNGTTYyyRVTA-------VDAAGNESAPsnvvsvttdlTPPAAPSGLTATAVG 339


                  ....*....
gi 158303304  757 GSAvVNLAW 765
Cdd:COG3401   340 SSS-ITLSW 347
FN3 cd00063
Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein ...
 656-730 3.46e-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: 49.80  E-value: 3.46e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158303304  656 PSAPTLVNVTSEAPTQLHVSWVHAAGDRS---SYQVTLYQESTRTATSIVGPKADSTSF--WGLTPGTKY--KVEAISWA 728
Cdd:cd00063     1 PSPPTNLRVTDVTSTSVTLSWTPPEDDGGpitGYVVEYREKGSGDWKEVEVTPGSETSYtlTGLKPGTEYefRVRAVNGG 80


                  ..
gi 158303304  729 GP 730
Cdd:cd00063    81 GE 82
CDC14 COG2453
Protein-tyrosine phosphatase [Signal transduction mechanisms];
1314-1362 5.88e-07

Protein-tyrosine phosphatase [Signal transduction mechanisms];


Pssm-ID: 441989 [Multi-domain]  Cd Length: 140  Bit Score: 50.35  E-value: 5.88e-07
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*....
gi 158303304 1314 WPDHSVPEaPSSLLAFVELVQEEVKAtqgKGPILVHCSAGVGRTGTFVA 1362
Cdd:COG2453    55 IPDFGAPD-DEQLQEAVDFIDEALRE---GKKVLVHCRGGIGRTGTVAA 99
PTP_DSP_cys cd14494
cys-based protein tyrosine phosphatase and dual-specificity phosphatase superfamily; This ...
 1326-1403 1.13e-06

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: 48.89  E-value: 1.13e-06
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 158303304 1326 LLAFVELVQEEVKatqGKGPILVHCSAGVGRTGTFVALLRLLRQLeeeqvVDVFNTVYILRLHRPLMI-QTLSQYIFLH 1403
Cdd:cd14494    42 VDRFLEVLDQAEK---PGEPVLVHCKAGVGRTGTLVACYLVLLGG-----MSAEEAVRIVRLIRPGGIpQTIEQLDFLI 112
R-PTPc-Q cd14616
catalytic domain of receptor-type tyrosine-protein phosphatase Q; Receptor-type ...
 1511-1689 1.73e-06

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: 51.06  E-value: 1.73e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158303304 1511 LTGSAGpkELWEMVWEHGAYVLVSLG--LPDTKEKPQDIWPMEMQPI-VTDMVTVHRVAESNTAGWPSTLIRV-IHGDSG 1586
Cdd:cd14616    49 LPGTVG--DFWRMVWETRAKTIVMLTqcFEKGRIRCHQYWPEDNKPVtVFGDIVITKLMEDVQIDWTIRDLKIeRHGDYM 126

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158303304 1587 TERQVQCLQFPhcETGSELPANTLLTFLDAVGqcCSRGNSKKPgtLLSHSSKVTNQLSTFLAMEQLLQQAGTERTVDVFS 1666
Cdd:cd14616   127 MVRQCNFTSWP--EHGVPESSAPLIHFVKLVR--ASRAHDNTP--MIVHCSAGVGRTGVFIALDHLTQHINDHDFVDIYG 200

                         170       180
                  ....*....|....*....|....*
gi 158303304 1667 VA--LKQTQACGLKtpTLEQYIYLY 1689
Cdd:cd14616   201 LVaeLRSERMCMVQ--NLAQYIFLH 223
FN3 smart00060
Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, ...
 656-730 2.28e-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: 47.22  E-value: 2.28e-06
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158303304    656 PSAPTLVNVTSEAPTQLHVSWVHAAGDRS-----SYQVTLYQESTRTATSIVGPKADSTSFWGLTPGTKY--KVEAISWA 728
Cdd:smart00060    1 PSPPSNLRVTDVTSTSVTLSWEPPPDDGItgyivGYRVEYREEGSEWKEVNVTPSSTSYTLTGLKPGTEYefRVRAVNGA 80


                    ..
gi 158303304    729 GP 730
Cdd:smart00060   81 GE 82
R-PTPc-S-1 cd14625
catalytic domain of receptor-type tyrosine-protein phosphatase S, repeat 1; Receptor-type ...
 1422-1696 3.32e-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: 50.86  E-value: 3.32e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158303304 1422 PIPVMNFAQACAKRAANANAGFLKEYRLL---KQAIKDETGSLLPSPDYNQNSIASCHHSQEQLALVEESPADNMLAASL 1498
Cdd:cd14625     3 PIPISELAEHTERLKANDNLKLSQEYESIdpgQQFTWEHSNLEVNKPKNRYANVIAYDHSRVILQPIEGIMGSDYINANY 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158303304 1499 FPGGpsgRDHVVLTGSAGP-----KELWEMVWEHGAYVLVSLGLPDTKE--KPQDIWPMEMqpivTDMVTVHRVAESNTA 1571
Cdd:cd14625    83 IDGY---RKQNAYIATQGPlpetfGDFWRMVWEQRSATVVMMTKLEEKSriKCDQYWPSRG----TETYGMIQVTLLDTI 155

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158303304 1572 GWPSTLIRV--IHGDSGTE-RQVQCLQFPHC-ETGSELPANTLLTFLDAVGQCcsrgNSKKPGTLLSHSSKVTNQLSTFL 1647
Cdd:cd14625   156 ELATFCVRTfsLHKNGSSEkREVRQFQFTAWpDHGVPEYPTPFLAFLRRVKTC----NPPDAGPIVVHCSAGVGRTGCFI 231

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|
gi 158303304 1648 AMEQLLQQAGTERTVDVFS-VALKQTQAcGLKTPTLEQYIYLYNCLNSAL 1696
Cdd:cd14625   232 VIDAMLERIKHEKTVDIYGhVTLMRSQR-NYMVQTEDQYSFIHDALLEAV 280
R-PTPc-F-1 cd14626
catalytic domain of receptor-type tyrosine-protein phosphatase F, repeat 1; Receptor-type ...
 1437-1695 5.32e-06

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: 50.03  E-value: 5.32e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158303304 1437 ANANAGFLKEYRLLK--QAIKDETGSL-LPSPDYNQNSIASCHHSQEQLALVEESPADNMLAASLFPGGpsgRDHVVLTG 1513
Cdd:cd14626    12 ANDGLKFSQEYESIDpgQQFTWENSNLeVNKPKNRYANVIAYDHSRVILTSVDGVPGSDYINANYIDGY---RKQNAYIA 88

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158303304 1514 SAGP-----KELWEMVWEHGAYVLVSLGLPDTKE--KPQDIWPMEMqpivTDMVTVHRVAESNTAGWPSTLIRV--IHGD 1584
Cdd:cd14626    89 TQGPlpetlSDFWRMVWEQRTATIVMMTRLEEKSrvKCDQYWPIRG----TETYGMIQVTLLDTVELATYSVRTfaLYKN 164

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158303304 1585 SGTE----RQVQCLQFPhcETGSELPANTLLTFLDAVGQCcsrgNSKKPGTLLSHSSKVTNQLSTFLAMEQLLQQAGTER 1660
Cdd:cd14626   165 GSSEkrevRQFQFMAWP--DHGVPEYPTPILAFLRRVKAC----NPPDAGPMVVHCSAGVGRTGCFIVIDAMLERMKHEK 238

                         250       260       270
                  ....*....|....*....|....*....|....*.
gi 158303304 1661 TVDVFS-VALKQTQAcGLKTPTLEQYIYLYNCLNSA 1695
Cdd:cd14626   239 TVDIYGhVTCMRSQR-NYMVQTEDQYIFIHEALLEA 273
PHA02746 PHA02746
protein tyrosine phosphatase; Provisional
 1516-1696 6.78e-06

protein tyrosine phosphatase; Provisional


Pssm-ID: 165113 [Multi-domain]  Cd Length: 323  Bit Score: 50.03  E-value: 6.78e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158303304 1516 GPKE-----LWEMVWEHGAYVLVSLG-LPDTKEKPQDIWPMEMQPIVTDMVTVHRVAE-SNTAGWPSTLIRVIHGDSGTE 1588
Cdd:PHA02746  120 GPKEdtsedFFKLISEHESQVIVSLTdIDDDDEKCFELWTKEEDSELAFGRFVAKILDiIEELSFTKTRLMITDKISDTS 199

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158303304 1589 RQVQCLQFPHCETGSeLPAN--TLLTFLDAVGQCCSR------GNSKKPGTLLSHSSKVTNQLSTFLAMEQLLQQAGTER 1660
Cdd:PHA02746  200 REIHHFWFPDWPDNG-IPTGmaEFLELINKVNEEQAElikqadNDPQTLGPIVVHCSAGIGRAGTFCAIDNALEQLEKEK 278

                         170       180       190
                  ....*....|....*....|....*....|....*.
gi 158303304 1661 TVDVFSVALKQTQACGLKTPTLEQYIYLYNCLNSAL 1696
Cdd:PHA02746  279 EVCLGEIVLKIRKQRHSSVFLPEQYAFCYKALKYAI 314
fn3 pfam00041
Fibronectin type III domain;
657-722 1.03e-05

Fibronectin type III domain;


Pssm-ID: 394996 [Multi-domain]  Cd Length: 85  Bit Score: 45.48  E-value: 1.03e-05
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 158303304   657 SAPTLVNVTSEAPTQLHVSWVHAA---GDRSSYQVTLYQEST--RTATSIVGPKADSTSFWGLTPGTKYKV 722
Cdd:pfam00041    1 SAPSNLTVTDVTSTSLTVSWTPPPdgnGPITGYEVEYRPKNSgePWNEITVPGTTTSVTLTGLKPGTEYEV 71
R-PTP-LAR-2 cd14554
PTP-like domain of the LAR family receptor-type tyrosine-protein phosphatases, repeat 2; The ...
 1519-1689 1.05e-05

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: 48.67  E-value: 1.05e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158303304 1519 ELWEMVWEHGAYVLVSLglpdTK------EKPQDIWPMEmQPIVTDMVTVHRVAESNtagWPSTLIRVIH------GDSG 1586
Cdd:cd14554    64 DFWRMLWEHNSTIIVML----TKlremgrEKCHQYWPAE-RSARYQYFVVDPMAEYN---MPQYILREFKvtdardGQSR 135

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158303304 1587 TERQVQCLQFPhcETGSELPANtllTFLDAVGQCC-SRGNSKKPGTLLSHSSKVTNQLSTFLAMEQLLQQAGTERTVDVF 1665
Cdd:cd14554   136 TVRQFQFTDWP--EQGVPKSGE---GFIDFIGQVHkTKEQFGQEGPITVHCSAGVGRTGVFITLSIVLERMRYEGVVDVF 210

                         170       180
                  ....*....|....*....|....*
gi 158303304 1666 -SVALKQTQACGLkTPTLEQYIYLY 1689
Cdd:cd14554   211 qTVKLLRTQRPAM-VQTEDQYQFCY 234
R-PTPc-A-E-2 cd14552
catalytic domain of receptor-type tyrosine-protein phosphatase A and E, repeat 2; ...
 1514-1689 1.48e-05

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


Pssm-ID: 350400 [Multi-domain]  Cd Length: 202  Bit Score: 47.65  E-value: 1.48e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158303304 1514 SAGP-----KELWEMVWEHGAYVLVSlgLPDTKEKPQD----IWPMEMQPIVTDmVTVHRVAESNTAGWPSTLIRVIHGD 1584
Cdd:cd14552    19 TQGPldhtvEDFWRMIWEWKSCSIVM--LTEIKERSQNkcaqYWPEDGSVSSGD-ITVELKDQTDYEDYTLRDFLVTKGK 95

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158303304 1585 SGTERQVQCLQFpHCETGSELPANTlLTFLDAVGQCCSRGNSKKPGTLLSHSSKVTNQLSTFLAMEQLLQQAGTERTVDV 1664
Cdd:cd14552    96 GGSTRTVRQFHF-HGWPEVGIPDNG-KGMIDLIAAVQKQQQQSGNHPITVHCSAGAGRTGTFCALSTVLERVKAEGVLDV 173

                         170       180
                  ....*....|....*....|....*....
gi 158303304 1665 FSValkqTQACGLKTP----TLEQYIYLY 1689
Cdd:cd14552   174 FQV----VKSLRLQRPhmvqTLEQYEFCY 198
R-PTP-G-2 cd17670
PTP-like domain of receptor-type tyrosine-protein phosphatase G, repeat 2; Receptor-type ...
 1518-1694 2.34e-05

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: 47.37  E-value: 2.34e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158303304 1518 KELWEMVWEHGAYVLVSlgLPDTKEKPQD---IWPMEMQPIVTDMVTV-----HRVAESNTAGW--PSTLIRVIHGDSGT 1587
Cdd:cd17670    28 KDFWRMIWDHNAQIIVM--LPDNQGLAEDefvYWPSREESMNCEAFTVtliskDRLCLSNEEQIiiHDFILEATQDDYVL 105

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158303304 1588 E-RQVQCLQFPHcetgSELPANTLLTFLDAVGQccsrGNSKKPGTLLSHSSKVTNQLSTFLAMEQLLQQAGTERTVDVFS 1666
Cdd:cd17670   106 EvRHFQCPKWPN----PDAPISSTFELINVIKE----EALTRDGPTIVHDEFGAVSAGTLCALTTLSQQLENENAVDVYQ 177

                         170       180       190
                  ....*....|....*....|....*....|..
gi 158303304 1667 VAlkqtQACGLKTP----TLEQYIYLYNCLNS 1694
Cdd:cd17670   178 VA----KMINLMRPgvftDIEQYQFLYKAMLS 205
R-PTP-D-2 cd14628
PTP-like domain of receptor-type tyrosine-protein phosphatase D, repeat 2; Receptor-type ...
 1506-1689 4.50e-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: 47.42  E-value: 4.50e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158303304 1506 RDHVVLTGSAGP-----KELWEMVWEHGAYVLVSL-GLPDT-KEKPQDIWPMEMQPIVTDMVtVHRVAESNTAGWPSTLI 1578
Cdd:cd14628    92 RQQKAYIATQGPlaettEDFWRMLWEHNSTIVVMLtKLREMgREKCHQYWPAERSARYQYFV-VDPMAEYNMPQYILREF 170

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158303304 1579 RVIHGDSGTERQVQCLQFphcetgSELPANTLLT----FLDAVGQCC-SRGNSKKPGTLLSHSSKVTNQLSTFLAMEQLL 1653
Cdd:cd14628   171 KVTDARDGQSRTVRQFQF------TDWPEQGVPKsgegFIDFIGQVHkTKEQFGQDGPISVHCSAGVGRTGVFITLSIVL 244

                         170       180       190
                  ....*....|....*....|....*....|....*..
gi 158303304 1654 QQAGTERTVDVF-SVALKQTQACGLkTPTLEQYIYLY 1689
Cdd:cd14628   245 ERMRYEGVVDIFqTVKMLRTQRPAM-VQTEDQYQFCY 280
R-PTPc-T-1 cd14630
catalytic domain of receptor-type tyrosine-protein phosphatase T, repeat 1; Receptor-type ...
 1466-1695 5.93e-05

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: 46.56  E-value: 5.93e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158303304 1466 DYNQN-----SIASCHHSQEQLALVEESPADNMLAASLFPGGPSGRDHVVLTGSAGP--KELWEMVWEH--GAYVLVSLG 1536
Cdd:cd14630     1 DENRNknrygNIISYDHSRVRLQLLDGDPHSDYINANYIDGYHRPRHYIATQGPMQEtvKDFWRMIWQEnsASVVMVTNL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158303304 1537 LPDTKEKPQDIWPMEMQ---PIVTDMVTVHRVAESNTAGWpsTLIRVIHGDSGTERQVQCLQFPhcETGSELPANTLLTF 1613
Cdd:cd14630    81 VEVGRVKCVRYWPDDTEvygDIKVTLIETEPLAEYVIRTF--TVQKKGYHEIREIRQFHFTSWP--DHGVPCYATGLLGF 156

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158303304 1614 LDAVGQCcsrgNSKKPGTLLSHSSKVTNQLSTFLAMEQLLQQAGTERTVDVFSVALK-QTQACGLkTPTLEQYIYLYNCL 1692
Cdd:cd14630   157 VRQVKFL----NPPDAGPIVVHCSAGAGRTGCFIAIDIMLDMAENEGVVDIFNCVRElRAQRVNM-VQTEEQYVFVHDAI 231


                  ...
gi 158303304 1693 NSA 1695
Cdd:cd14630   232 LEA 234
FN3 smart00060
Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, ...
 473-551 8.34e-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: 42.60  E-value: 8.34e-05
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158303304    473 PLPPQSLEIISRNSPSdLTIGW-APAPGQMEGYKVTWH-QDGSQRSPGDLVDLGPDISSLTLKSLVPGSCYTVSAWAWSG 550
Cdd:smart00060    1 PSPPSNLRVTDVTSTS-VTLSWePPPDDGITGYIVGYRvEYREEGSEWKEVNVTPSSTSYTLTGLKPGTEYEFRVRAVNG 79


                    .
gi 158303304    551 N 551
Cdd:smart00060   80 A 80
CDC14_C cd14499
C-terminal dual-specificity phosphatase domain of CDC14 family proteins; The cell division ...
 1315-1362 1.55e-04

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: 44.37  E-value: 1.55e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*...
gi 158303304 1315 PDHSVPEaPSSLLAFVELVQEEvkatqgKGPILVHCSAGVGRTGTFVA 1362
Cdd:cd14499    88 PDGSTPS-DDIVKKFLDICENE------KGAIAVHCKAGLGRTGTLIA 128
FN3 smart00060
Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, ...
 36-110 2.03e-04

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: 41.83  E-value: 2.03e-04
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 158303304     36 GPPLSVNVSSRGkPTSLFLSWVA-AEPGGFDYALCLRAMNLSGFPEGQQLQAHTNESSFEFHGLVPGSRYQLELTV 110
Cdd:smart00060    2 SPPSNLRVTDVT-STSVTLSWEPpPDDGITGYIVGYRVEYREEGSEWKEVNVTPSSTSYTLTGLKPGTEYEFRVRA 76
fn3 pfam00041
Fibronectin type III domain;
475-544 2.20e-04

Fibronectin type III domain;


Pssm-ID: 394996 [Multi-domain]  Cd Length: 85  Bit Score: 41.63  E-value: 2.20e-04
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 158303304   475 PPQSLEIiSRNSPSDLTIGWAPAP---GQMEGYKVTWHQDGSQrSPGDLVDLGPDISSLTLKSLVPGSCYTVS 544
Cdd:pfam00041    2 APSNLTV-TDVTSTSLTVSWTPPPdgnGPITGYEVEYRPKNSG-EPWNEITVPGTTTSVTLTGLKPGTEYEVR 72
fn3 pfam00041
Fibronectin type III domain;
131-201 2.60e-04

Fibronectin type III domain;


Pssm-ID: 394996 [Multi-domain]  Cd Length: 85  Bit Score: 41.25  E-value: 2.60e-04
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 158303304   131 VRGLQLHSTGSpASLEASWS---DASGDQDSYQLLlYHPESHTLACN-VSVSPDTLSYNFGDLLPGSQYVLEVIT 201
Cdd:pfam00041    3 PSNLTVTDVTS-TSLTVSWTpppDGNGPITGYEVE-YRPKNSGEPWNeITVPGTTTSVTLTGLKPGTEYEVRVQA 75
R-PTP-F-2 cd14629
PTP-like domain of receptor-type tyrosine-protein phosphatase F, repeat 2; Receptor-type ...
 1492-1689 3.45e-04

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: 44.72  E-value: 3.45e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158303304 1492 NMLAASLFPGGPSGRDHVVLTG--SAGPKELWEMVWEHGAYVLVSL-GLPDT-KEKPQDIWPMEMQPIVTDMVtVHRVAE 1567
Cdd:cd14629    82 DYINASFIDGYRQQKAYIATQGplAETTEDFWRMLWEHNSTIVVMLtKLREMgREKCHQYWPAERSARYQYFV-VDPMAE 160

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158303304 1568 SNTAGWPSTLIRVIHGDSGTERQVQCLQFPHC-ETGseLPaNTLLTFLDAVGQCC-SRGNSKKPGTLLSHSSKVTNQLST 1645
Cdd:cd14629   161 YNMPQYILREFKVTDARDGQSRTIRQFQFTDWpEQG--VP-KTGEGFIDFIGQVHkTKEQFGQDGPITVHCSAGVGRTGV 237

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*
gi 158303304 1646 FLAMEQLLQQAGTERTVDVF-SVALKQTQACGLkTPTLEQYIYLY 1689
Cdd:cd14629   238 FITLSIVLERMRYEGVVDMFqTVKTLRTQRPAM-VQTEDQYQLCY 281
R-PTPc-LAR-1 cd14553
catalytic domain of LAR family receptor-type tyrosine-protein phosphatases, repeat 1; The LAR ...
 1519-1695 4.27e-04

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: 43.92  E-value: 4.27e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158303304 1519 ELWEMVWEHGAYVLVSLglpdTKE------KPQDIWPMEMQPIVTDM-VTVHRVAEsnTAGWPSTLIRVIHGDSGTERQV 1591
Cdd:cd14553    61 DFWRMVWEQRSATIVMM----TKLeersrvKCDQYWPTRGTETYGLIqVTLLDTVE--LATYTVRTFALHKNGSSEKREV 134

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158303304 1592 QCLQFphceTG------SELPAnTLLTFLDAVGQCcsrgNSKKPGTLLSHSSKVTNQLSTFLAMEQLLQQAGTERTVDVF 1665
Cdd:cd14553   135 RQFQF----TAwpdhgvPEHPT-PFLAFLRRVKAC----NPPDAGPIVVHCSAGVGRTGCFIVIDSMLERIKHEKTVDIY 205

                         170       180       190
                  ....*....|....*....|....*....|.
gi 158303304 1666 S-VALKQTQAcGLKTPTLEQYIYLYNCLNSA 1695
Cdd:cd14553   206 GhVTCLRAQR-NYMVQTEDQYIFIHDALLEA 235
DUSP23 cd14504
dual specificity phosphatase 23; Dual specificity phosphatase 23 (DUSP23), also known as ...
 1315-1362 4.36e-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: 42.26  E-value: 4.36e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*...
gi 158303304 1315 PDHSVPEaPSSLLAFVELVQEEVKATQgkgPILVHCSAGVGRTGTFVA 1362
Cdd:cd14504    58 EDYTPPT-LEQIDEFLDIVEEANAKNE---AVLVHCLAGKGRTGTMLA 101
FN3 cd00063
Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein ...
 473-555 4.42e-04

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: 40.94  E-value: 4.42e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158303304  473 PLPPQSLEIiSRNSPSDLTIGWAPAP---GQMEGYKVTWHQDGSQRsPGDLVDLGPDISSLTLKSLVPGSCYTVSAWAWS 549
Cdd:cd00063     1 PSPPTNLRV-TDVTSTSVTLSWTPPEddgGPITGYVVEYREKGSGD-WKEVEVTPGSETSYTLTGLKPGTEYEFRVRAVN 78


                  ....*.
gi 158303304  550 GNLSSD 555
Cdd:cd00063    79 GGGESP 84
R-PTPc-A-E-1 cd14551
catalytic domain of receptor-type tyrosine-protein phosphatase A and E, repeat 1; ...
 1516-1689 5.93e-04

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: 42.98  E-value: 5.93e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158303304 1516 GPKE-----LWEMVWEHGAYVLVSL-GLPDTKE-KPQDIWPMEMQPIVTDM-VTVHRVAESNTAGWPSTLIRVIHGDSGT 1587
Cdd:cd14551    21 GPKDetvndFWRMIWEQGSATIVMVtNLKERKEkKCSQYWPDQGCWTYGNLrVRVEDTVVLVDYTTRKFCIQKVNRGIGE 100

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158303304 1588 ERQVQCLQFPHC---ETGSELPANTLLTFLDAVGQCcsrgNSKKPGTLLSHSSKVTNQLSTFLAMEQLLQQAGTERTVDV 1664
Cdd:cd14551   101 KRVRLVTQFHFTswpDFGVPFTPIGMLKFLKKVKSA----NPPRAGPIVVHCSAGVGRTGTFIVIDAMLDMMHAEGKVDV 176

                         170       180
                  ....*....|....*....|....*
gi 158303304 1665 FSVALKQTQACGLKTPTLEQYIYLY 1689
Cdd:cd14551   177 FGFVSRIRQQRSQMVQTDMQYVFIY 201
fn3 pfam00041
Fibronectin type III domain;
36-109 7.64e-04

Fibronectin type III domain;


Pssm-ID: 394996 [Multi-domain]  Cd Length: 85  Bit Score: 40.09  E-value: 7.64e-04
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 158303304    36 GPPLSVNVSSRGkPTSLFLSWVAAEPGG---FDYALCLRAMNLSGfpEGQQLQAHTNESSFEFHGLVPGSRYQLELT 109
Cdd:pfam00041    1 SAPSNLTVTDVT-STSLTVSWTPPPDGNgpiTGYEVEYRPKNSGE--PWNEITVPGTTTSVTLTGLKPGTEYEVRVQ 74
R-PTP-S-2 cd14627
PTP-like domain of receptor-type tyrosine-protein phosphatase S, repeat 2; Receptor-type ...
 1506-1689 8.07e-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: 43.57  E-value: 8.07e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158303304 1506 RDHVVLTGSAGP-----KELWEMVWEHGAYVLVSL-GLPDT-KEKPQDIWPMEMQPIVTDMVtVHRVAESNTAGWPSTLI 1578
Cdd:cd14627    93 RQQKAYIATQGPlaettEDFWRMLWENNSTIVVMLtKLREMgREKCHQYWPAERSARYQYFV-VDPMAEYNMPQYILREF 171

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158303304 1579 RVIHGDSGTERQVQCLQFphcetgSELPANTLLT----FLDAVGQCC-SRGNSKKPGTLLSHSSKVTNQLSTFLAMEQLL 1653
Cdd:cd14627   172 KVTDARDGQSRTVRQFQF------TDWPEQGVPKsgegFIDFIGQVHkTKEQFGQDGPISVHCSAGVGRTGVFITLSIVL 245

                         170       180       190
                  ....*....|....*....|....*....|....*..
gi 158303304 1654 QQAGTERTVDVF-SVALKQTQACGLkTPTLEQYIYLY 1689
Cdd:cd14627   246 ERMRYEGVVDIFqTVKMLRTQRPAM-VQTEDEYQFCY 281
R-PTPc-E-1 cd14620
catalytic domain of receptor-type tyrosine-protein phosphatase E, repeat 1; Receptor-type ...
 1477-1692 1.30e-03

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: 42.24  E-value: 1.30e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158303304 1477 HSQEQLALVEESPADNMLAASlFPGGPSGRDHVVltGSAGPKE-----LWEMVWEHGAYVLVSlgLPDTKEKPQD----I 1547
Cdd:cd14620     9 HSRVILSQLDGIPCSDYINAS-YIDGYKEKNKFI--AAQGPKQetvndFWRMVWEQKSATIVM--LTNLKERKEEkcyqY 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158303304 1548 WPMEMQPIVTDMvtvhRVAESNTAGWPSTLIR------VIHGDSGTERQVQCLQFPHC-ETGSELPANTLLTFLDAVGQC 1620
Cdd:cd14620    84 WPDQGCWTYGNI----RVAVEDCVVLVDYTIRkfciqpQLPDGCKAPRLVTQLHFTSWpDFGVPFTPIGMLKFLKKVKSV 159

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 158303304 1621 csrgNSKKPGTLLSHSSKVTNQLSTFLAMEQLLQQAGTERTVDVFS-VALKQTQACGLkTPTLEQYIYLYNCL 1692
Cdd:cd14620   160 ----NPVHAGPIVVHCSAGVGRTGTFIVIDAMIDMMHAEQKVDVFEfVSRIRNQRPQM-VQTDMQYSFIYQAL 227
PTP_VSP_TPTE cd14510
protein tyrosine phosphatase-like catalytic domain of voltage-sensitive phosphatase ...
 1315-1361 1.65e-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: 41.19  E-value: 1.65e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*..
gi 158303304 1315 PDHSVPEAPSsLLAFVELVQEEVKATQgKGPILVHCSAGVGRTGTFV 1361
Cdd:cd14510    82 DDHNVPTLDE-MLSFTAEVREWMAADP-KNVVAIHCKGGKGRTGTMV 126
PTP_PTPDC1 cd14506
protein tyrosine phosphatase domain of PTP domain-containing protein 1; protein tyrosine ...
 1314-1403 1.85e-03

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


Pssm-ID: 350356 [Multi-domain]  Cd Length: 206  Bit Score: 41.57  E-value: 1.85e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158303304 1314 WPDHSVPeAPSSLLAFVELVQEEVKaTQGKgpILVHCSAGVGRTGTFVALLRllrqleeeqvvdVFNT-------VYILR 1386
Cdd:cd14506    84 WKDYGVP-SLTTILDIVKVMAFALQ-EGGK--VAVHCHAGLGRTGVLIACYL------------VYALrmsadqaIRLVR 147

                          90
                  ....*....|....*..
gi 158303304 1387 LHRPLMIQTLSQYIFLH 1403
Cdd:cd14506   148 SKRPNSIQTRGQVLCVR 164
DSPc smart00195
Dual specificity phosphatase, catalytic domain;
1338-1362 2.05e-03

Dual specificity phosphatase, catalytic domain;


Pssm-ID: 214551 [Multi-domain]  Cd Length: 138  Bit Score: 40.34  E-value: 2.05e-03
                            10        20
                    ....*....|....*....|....*
gi 158303304   1338 KATQGKGPILVHCSAGVGRTGTFVA 1362
Cdd:smart00195   73 DAESKGGKVLVHCQAGVSRSATLII 97
PTPc-N5 cd14613
catalytic domain of tyrosine-protein phosphatase non-receptor type 5; Tyrosine-protein ...
 1445-1693 2.28e-03

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: 41.77  E-value: 2.28e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158303304 1445 KEYRLLKQAIKDETGSLLPSPdynqnsiaschHSQEQL-ALVEESPADNMLAASLFPGgpSGRDHVVLTGSAGP-----K 1518
Cdd:cd14613    18 KEYDIPGLVRKNRYKTILPNP-----------HSRVCLtSPDQDDPLSSYINANYIRG--YGGEEKVYIATQGPtvntvG 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158303304 1519 ELWEMVW-EHGAYVLVSLGLPDTKEKPQDIWPMEMQPIVTDMVTVHRVAESNtagwpSTLIRVIHGDSGTE----RQVQC 1593
Cdd:cd14613    85 DFWRMVWqERSPIIVMITNIEEMNEKCTEYWPEEQVTYEGIEITVKQVIHAD-----DYRLRLITLKSGGEerglKHYWY 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158303304 1594 LQFPHCETGSELPAntLLTFLDAVGQC--CSRGNSkkpGTLLSHSSKVTNQLSTFLAMEQLLQQAGTERTVDVFSVALKQ 1671
Cdd:cd14613   160 TSWPDQKTPDNAPP--LLQLVQEVEEArqQAEPNC---GPVIVHCSAGIGRTGCFIATSICCKQLRNEGVVDILRTTCQL 234

                         250       260
                  ....*....|....*....|..
gi 158303304 1672 TQACGLKTPTLEQYIYLYNCLN 1693
Cdd:cd14613   235 RLDRGGMIQTCEQYQFVHHVLS 256
PHA02747 PHA02747
protein tyrosine phosphatase; Provisional
 1519-1688 2.39e-03

protein tyrosine phosphatase; Provisional


Pssm-ID: 165114 [Multi-domain]  Cd Length: 312  Bit Score: 41.91  E-value: 2.39e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158303304 1519 ELWEMVWEHGAYVLVSL---GLPDTKEKPQDIW-PMEMQPIVTDMVTVHRVAESNTAGWPSTLIRVIHGDSGTERQV--- 1591
Cdd:PHA02747  108 DFWKAVWQEHCSIIVMLtptKGTNGEEKCYQYWcLNEDGNIDMEDFRIETLKTSVRAKYILTLIEITDKILKDSRKIshf 187

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158303304 1592 QCLQFPHCETGSELPANT-LLTFLDAVGQcCSRGNSKKPGTLLS----HSSKVTNQLSTFLAMEQLLQQAGTERTVDVFS 1666
Cdd:PHA02747  188 QCSEWFEDETPSDHPDFIkFIKIIDINRK-KSGKLFNPKDALLCpivvHCSDGVGKTGIFCAVDICLNQLVKRKAICLAK 266

                         170       180
                  ....*....|....*....|....
gi 158303304 1667 VA--LKQTQACGLKTPtlEQYIYL 1688
Cdd:PHA02747  267 TAekIREQRHAGIMNF--DDYLFI 288
DSPc pfam00782
Dual specificity phosphatase, catalytic domain; Ser/Thr and Tyr protein phosphatases. The ...
 1338-1362 5.04e-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: 38.78  E-value: 5.04e-03
                           10        20
                   ....*....|....*....|....*
gi 158303304  1338 KATQGKGPILVHCSAGVGRTGTFVA 1362
Cdd:pfam00782   64 DARQKGGKVLVHCQAGISRSATLII 88
TpbA-like cd14529
bacterial protein tyrosine and dual-specificity phosphatases related to Pseudomonas aeruginosa ...
 1344-1362 6.29e-03

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: 39.28  E-value: 6.29e-03
                          10
                  ....*....|....*....
gi 158303304 1344 GPILVHCSAGVGRTGTFVA 1362
Cdd:cd14529    90 GPVLIHCKHGKDRTGLVSA 108
PTPc-N21_14 cd14540
catalytic domain of tyrosine-protein phosphatase non-receptor type 21 and type 14; ...
 1518-1692 7.15e-03

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: 39.75  E-value: 7.15e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158303304 1518 KELWEMVWEHGAYVLVSLG--LPDTKEKPQDIWP---MEMQPIVTDMVTVHRVAESNTAGWPSTLIRVIHGDSGTERQVQ 1592
Cdd:cd14540    30 GDFWQMVWEQGVYLVVMVTaeEEGGREKCFRYWPtlgGEHDALTFGEYKVSTKFSVSSGCYTTTGLRVKHTLSGQSRTVW 109

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158303304 1593 CLQF---PhcETGSELPANTLLTFLDAVGQC------CSRGNSKKPGTLLSHSSKVTNQLSTFLAmEQLLQQAGTERTVD 1663
Cdd:cd14540   110 HLQYtdwP--DHGCPEDVSGFLDFLEEINSVrrhtnqDVAGHNRNPPTLVHCSAGVGRTGVVILA-DLMLYCLDHNEELD 186

                         170       180
                  ....*....|....*....|....*....
gi 158303304 1664 VFSVALKQTQACGLKTPTLEQYIYLYNCL 1692
Cdd:cd14540   187 IPRVLALLRHQRMLLVQTLAQYKFVYNVL 215
R-PTPc-C-1 cd14557
catalytic domain of receptor-type tyrosine-protein phosphatase C, repeat 1; Receptor-type ...
 1516-1689 9.20e-03

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: 39.43  E-value: 9.20e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158303304 1516 GPKE-----LWEMVWEHGAYVLVSLGLPD--TKEKPQDIWP-MEMQPIVTDMVTVHRVAESNtagWPSTLIRVIH----G 1583
Cdd:cd14557    21 GPKDetvddFWRMIWEQKSTVIVMVTRCEegNRNKCAQYWPsMEEGSRAFGDVVVKINEEKI---CPDYIIRKLNinnkK 97

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158303304 1584 DSGTERQVQCLQF---PhcETGSELPANTLLTFLDAVGQCcsrgNSKKPGTLLSHSSKVTNQLSTFLAMEQLLQQAGTER 1660
Cdd:cd14557    98 EKGSGREVTHIQFtswP--DHGVPEDPHLLLKLRRRVNAF----NNFFSGPIVVHCSAGVGRTGTYIGIDAMLEGLEAEG 171

                         170       180       190
                  ....*....|....*....|....*....|
gi 158303304 1661 TVDVFSVALK-QTQACgLKTPTLEQYIYLY 1689
Cdd:cd14557   172 RVDVYGYVVKlRRQRC-LMVQVEAQYILIH 200
 
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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