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Conserved domains on  [gi|2034231280|dbj|GFO06830|]
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receptor-type tyrosine-protein phosphatase kappa [Plakobranchus ocellatus]

Protein Classification

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
PTPc smart00194
Protein tyrosine phosphatase, catalytic domain;
1151-1406 5.68e-82

Protein tyrosine phosphatase, catalytic domain;


:

Pssm-ID: 214550 [Multi-domain]  Cd Length: 259  Bit Score: 270.30  E-value: 5.68e-82
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2034231280  1151 FKDEFHALPH-KSQKATDNTARRQG-SHLNRFPHLLPYDHSLVQLRPDVTSRGSYVNASFLPGYKKTPAYIAAQSPyNEE 1228
Cdd:smart00194    2 LEEEFEKLDRlKPDDESCTVAAFPEnRDKNRYKDVLPYDHTRVKLKPPPGEGSDYINASYIDGPNGPKAYIATQGP-LPS 80
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2034231280  1229 TVLDFWRLIYQRSIKTVVMITNVVEDHIVKCTQYWP--TQTKASFGDIFfLHLIEVNEYADYIIRTIGVKMKGDSDSKIV 1306
Cdd:smart00194   81 TVEDFWRMVWEQKVTVIVMLTELVEKGREKCAQYWPdeEGEPLTYGDIT-VTLKSVEKVDDYTIRTLEVTNTGCSETRTV 159
                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2034231280  1307 RLFEFTSWPDHGVPDDPIPFLDMRYKVRRYQHDSPSPILVHCGTGMARTGVFIAVDALIDQYASEGRVMVYDFVRRLRKD 1386
Cdd:smart00194  160 THYHYTNWPDHGVPESPESILDLIRAVRKSQSTSTGPIVVHCSAGVGRTGTFIAIDILLQQLEAGKEVDIFEIVKELRSQ 239
                           250       260
                    ....*....|....*....|
gi 2034231280  1387 RPFMVRTLKQYVFIYEAIFE 1406
Cdd:smart00194  240 RPGMVQTEEQYIFLYRAILE 259
PTPc smart00194
Protein tyrosine phosphatase, catalytic domain;
1438-1704 4.45e-65

Protein tyrosine phosphatase, catalytic domain;


:

Pssm-ID: 214550 [Multi-domain]  Cd Length: 259  Bit Score: 221.76  E-value: 4.45e-65
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2034231280  1438 LRDQYKLLETFTrsPRRDQCKTAQLEINVHKNRYLDVLAADHYRPILTSqgPGAQATDYINAVYVDGYLRRNQFIVTQTP 1517
Cdd:smart00194    2 LEEEFEKLDRLK--PDDESCTVAAFPENRDKNRYKDVLPYDHTRVKLKP--PPGEGSDYINASYIDGPNGPKAYIATQGP 77
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2034231280  1518 LHTTVLDFWRLVWDHDIRTIVMVENFKHEDDTR-AEYWPpaASGGVMKQLEPFFLETTACYQQENITVRNLRLLSTQhpR 1596
Cdd:smart00194   78 LPSTVEDFWRMVWEQKVTVIVMLTELVEKGREKcAQYWP--DEEGEPLTYGDITVTLKSVEKVDDYTIRTLEVTNTG--C 153
                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2034231280  1597 DPARFVRQFQFNAWAEHaMAPQSKTMMLDLVDSVFDWQEeacANERPVLVHCQDGSSHSGLFTTLAVVCERMEEDGEVDV 1676
Cdd:smart00194  154 SETRTVTHYHYTNWPDH-GVPESPESILDLIRAVRKSQS---TSTGPIVVHCSAGVGRTGTFIAIDILLQQLEAGKEVDI 229
                           250       260
                    ....*....|....*....|....*...
gi 2034231280  1677 YRTIKHIKRRRGQIIADYDQFRFCYKAV 1704
Cdd:smart00194  230 FEIVKELRSQRPGMVQTEEQYIFLYRAI 257
FU smart00261
Furin-like repeats;
55-96 8.02e-12

Furin-like repeats;


:

Pssm-ID: 214589 [Multi-domain]  Cd Length: 45  Bit Score: 61.37  E-value: 8.02e-12
                            10        20        30        40
                    ....*....|....*....|....*....|....*....|...
gi 2034231280    55 VCVACDPSCEGCSGEGPTLCTACKIGYRLQAAGCV-VCPEGFY 96
Cdd:smart00261    3 ECKPCHPECATCTGPGPDDCTSCKHGFFLDGGKCVsECPPGTY 45
FN3 cd00063
Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein ...
416-509 1.05e-06

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: 48.65  E-value: 1.05e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2034231280  416 PVAPTamvsGLNVSGITATEAFVTWSNMPCNQqkGPSGNYELELTPVGGNTVRYVLTENRRA----FTGLAPFTEHNVRI 491
Cdd:cd00063      1 PSPPT----NLRVTDVTSTSVTLSWTPPEDDG--GPITGYVVEYREKGSGDWKEVEVTPGSEtsytLTGLKPGTEYEFRV 74
                           90
                   ....*....|....*....
gi 2034231280  492 RYANQVGRGPF-TSREFQT 509
Cdd:cd00063     75 RAVNGGGESPPsESVTVTT 93
FN3 super family cl27307
Fibronectin type 3 domain [General function prediction only];
385-848 9.84e-05

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: 47.30  E-value: 9.84e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2034231280  385 VLTWSKYSFTIDAQAETVDVSEVRTLTKISDPVAPTAMVS---GLNVSGITATEAFVTWSNMPCNqqKGPSGNYELELTP 461
Cdd:COG3401      4 SYLTSLDAGIAASAAANTAVNALSKAGGSGKTILVYLAVVlsvTTKESPGTLLVAAGLSSGGGLG--TGGRAGTTSGVAA 81
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2034231280  462 VGGNTVRYVLTENRRAFTGLAPFTEHNVRIRYANQVGRGPFTSREFQTLEGVPTAVQIVSATATSTTITVTFDPPLRTNG 541
Cdd:COG3401     82 VAVAAAPPTATGLTTLTGSGSVGGATNTGLTSSDEVPSPAVGTATTATAVAGGAATAGTYALGAGLYGVDGANASGTTAS 161
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2034231280  542 ILVSYTVTFSTTSDFNETESRTEQGRSG-LRSIIVGRLQADTLYYLKMAASTNAGIGQYGSVTSRRTLEAPPPAEdIDLR 620
Cdd:COG3401    162 SVAGAGVVVSPDTSATAAVATTSLTVTStTLVDGGGDIEPGTTYYYRVAATDTGGESAPSNEVSVTTPTTPPSAP-TGLT 240
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2034231280  621 SDSQTVNCLSLSWDPPQNRAgdiqsykprpptfvrssytnvtlniepvmskyvpITSYRLHvllltnsnRNLPFQSAPGY 700
Cdd:COG3401    241 ATADTPGSVTLSWDPVTESD----------------------------------ATGYRVY--------RSNSGDGPFTK 278
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2034231280  701 ITAELESSavpntiefvigdgevyggYTNQPLESNSNYRIYYVAVSTLNNETT-SNYDSLTlpfptvPFDPALAPPLPLS 779
Cdd:COG3401    279 VATVTTTS------------------YTDTGLTNGTTYYYRVTAVDAAGNESApSNVVSVT------TDLTPPAAPSGLT 334
                          410       420       430       440       450       460
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2034231280  780 LSSRTTECLNLTWVTPTglSPLITSFDFTTSRAGDSDDTPITRSVPATdrAFQQCNLAPFTLYTVRISA 848
Cdd:COG3401    335 ATAVGSSSITLSWTASS--DADVTGYNVYRSTSGGGTYTKIAETVTTT--SYTDTGLTPGTTYYYKVTA 399
Furin-like super family cl25784
Furin-like cysteine rich region;
43-138 3.76e-04

Furin-like cysteine rich region;


The actual alignment was detected with superfamily member pfam00757:

Pssm-ID: 395614 [Multi-domain]  Cd Length: 143  Bit Score: 42.42  E-value: 3.76e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2034231280   43 NEYCKERADATAVCvaCDPSCEG-CSGEGPTLCTACKiGYRLQAAgCVV-CPEGFY--GINCATECNCLNKVCDNV---- 114
Cdd:pfam00757   35 PEQCKKRCTKPGEC--CHEQCLGgCTGPNDSDCLACR-HFNDEGT-CVDqCPPGTYqfGWRCVTFKECPKSHLPGYnplv 110
                           90       100       110
                   ....*....|....*....|....*....|....
gi 2034231280  115 --NGACaIWKCKRGYTGI--------PfCRDKCP 138
Cdd:pfam00757  111 ihNGEC-VRECPSGYTEVennsrkceP-CEGLCP 142
FN3 super family cl21522
Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein ...
190-284 2.11e-03

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.


The actual alignment was detected with superfamily member pfam00041:

Pssm-ID: 473895 [Multi-domain]  Cd Length: 85  Bit Score: 38.94  E-value: 2.11e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2034231280  190 PEVVSVQCNNITIQWDAfneeDNIGQGPVYAYNVEVRlnqtENGTSGPWQTKQTVLHveggnppklTYRISVSGLEPDKD 269
Cdd:pfam00041    6 LTVTDVTSTSLTVSWTP----PPDGNGPITGYEVEYR----PKNSGEPWNEITVPGT---------TTSVTLTGLKPGTE 68
                           90
                   ....*....|....*.
gi 2034231280  270 YNFRVNTI-GANSGKP 284
Cdd:pfam00041   69 YEVRVQAVnGGGEGPP 84
 
Name Accession Description Interval E-value
PTPc smart00194
Protein tyrosine phosphatase, catalytic domain;
1151-1406 5.68e-82

Protein tyrosine phosphatase, catalytic domain;


Pssm-ID: 214550 [Multi-domain]  Cd Length: 259  Bit Score: 270.30  E-value: 5.68e-82
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2034231280  1151 FKDEFHALPH-KSQKATDNTARRQG-SHLNRFPHLLPYDHSLVQLRPDVTSRGSYVNASFLPGYKKTPAYIAAQSPyNEE 1228
Cdd:smart00194    2 LEEEFEKLDRlKPDDESCTVAAFPEnRDKNRYKDVLPYDHTRVKLKPPPGEGSDYINASYIDGPNGPKAYIATQGP-LPS 80
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2034231280  1229 TVLDFWRLIYQRSIKTVVMITNVVEDHIVKCTQYWP--TQTKASFGDIFfLHLIEVNEYADYIIRTIGVKMKGDSDSKIV 1306
Cdd:smart00194   81 TVEDFWRMVWEQKVTVIVMLTELVEKGREKCAQYWPdeEGEPLTYGDIT-VTLKSVEKVDDYTIRTLEVTNTGCSETRTV 159
                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2034231280  1307 RLFEFTSWPDHGVPDDPIPFLDMRYKVRRYQHDSPSPILVHCGTGMARTGVFIAVDALIDQYASEGRVMVYDFVRRLRKD 1386
Cdd:smart00194  160 THYHYTNWPDHGVPESPESILDLIRAVRKSQSTSTGPIVVHCSAGVGRTGTFIAIDILLQQLEAGKEVDIFEIVKELRSQ 239
                           250       260
                    ....*....|....*....|
gi 2034231280  1387 RPFMVRTLKQYVFIYEAIFE 1406
Cdd:smart00194  240 RPGMVQTEEQYIFLYRAILE 259
PTPc cd00047
catalytic domain of protein tyrosine phosphatases; Protein tyrosine phosphatases (PTP, EC 3.1. ...
1203-1402 2.20e-77

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: 254.52  E-value: 2.20e-77
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2034231280 1203 YVNASFLPGYKKTPAYIAAQSPyNEETVLDFWRLIYQRSIKTVVMITNVVEDHIVKCTQYWPT--QTKASFGDiFFLHLI 1280
Cdd:cd00047      1 YINASYIDGYRGPKEYIATQGP-LPNTVEDFWRMVWEQKVSVIVMLTNLVEKGREKCERYWPEegGKPLEYGD-ITVTLV 78
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2034231280 1281 EVNEYADYIIRTIGVKMKGDSDSKIVRLFEFTSWPDHGVPDDPIPFLDMRYKVRRYQHDSPSPILVHCGTGMARTGVFIA 1360
Cdd:cd00047     79 SEEELSDYTIRTLELSPKGCSESREVTHLHYTGWPDHGVPSSPEDLLALVRRVRKEARKPNGPIVVHCSAGVGRTGTFIA 158
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|..
gi 2034231280 1361 VDALIDQYASEGRVMVYDFVRRLRKDRPFMVRTLKQYVFIYE 1402
Cdd:cd00047    159 IDILLERLEAEGEVDVFEIVKALRKQRPGMVQTLEQYEFIYE 200
Y_phosphatase pfam00102
Protein-tyrosine phosphatase;
1178-1406 2.65e-76

Protein-tyrosine phosphatase;


Pssm-ID: 459674 [Multi-domain]  Cd Length: 234  Bit Score: 252.93  E-value: 2.65e-76
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2034231280 1178 NRFPHLLPYDHSLVQLRPDVTSRGsYVNASFLPGYKKTPAYIAAQSPYnEETVLDFWRLIYQRSIKTVVMITNVVEDHIV 1257
Cdd:pfam00102    5 NRYKDVLPYDHTRVKLTGDPGPSD-YINASYIDGYKKPKKYIATQGPL-PNTVEDFWRMVWEEKVTIIVMLTELEEKGRE 82
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2034231280 1258 KCTQYWPTQTKAS--FGDiFFLHLIEVNEY-ADYIIRTIGVKMKGDSDSKIVRLFEFTSWPDHGVPDDPIPFLDMRYKVR 1334
Cdd:pfam00102   83 KCAQYWPEEEGESleYGD-FTVTLKKEKEDeKDYTVRTLEVSNGGSEETRTVKHFHYTGWPDHGVPESPNSLLDLLRKVR 161
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2034231280 1335 RYQHDSPS-PILVHCGTGMARTGVFIAVDALIDQYASEGRVMVYDFVRRLRKDRPFMVRTLKQYVFIYEAIFE 1406
Cdd:pfam00102  162 KSSLDGRSgPIVVHCSAGIGRTGTFIAIDIALQQLEAEGEVDIFQIVKELRSQRPGMVQTLEQYIFLYDAILE 234
PTPc smart00194
Protein tyrosine phosphatase, catalytic domain;
1438-1704 4.45e-65

Protein tyrosine phosphatase, catalytic domain;


Pssm-ID: 214550 [Multi-domain]  Cd Length: 259  Bit Score: 221.76  E-value: 4.45e-65
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2034231280  1438 LRDQYKLLETFTrsPRRDQCKTAQLEINVHKNRYLDVLAADHYRPILTSqgPGAQATDYINAVYVDGYLRRNQFIVTQTP 1517
Cdd:smart00194    2 LEEEFEKLDRLK--PDDESCTVAAFPENRDKNRYKDVLPYDHTRVKLKP--PPGEGSDYINASYIDGPNGPKAYIATQGP 77
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2034231280  1518 LHTTVLDFWRLVWDHDIRTIVMVENFKHEDDTR-AEYWPpaASGGVMKQLEPFFLETTACYQQENITVRNLRLLSTQhpR 1596
Cdd:smart00194   78 LPSTVEDFWRMVWEQKVTVIVMLTELVEKGREKcAQYWP--DEEGEPLTYGDITVTLKSVEKVDDYTIRTLEVTNTG--C 153
                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2034231280  1597 DPARFVRQFQFNAWAEHaMAPQSKTMMLDLVDSVFDWQEeacANERPVLVHCQDGSSHSGLFTTLAVVCERMEEDGEVDV 1676
Cdd:smart00194  154 SETRTVTHYHYTNWPDH-GVPESPESILDLIRAVRKSQS---TSTGPIVVHCSAGVGRTGTFIAIDILLQQLEAGKEVDI 229
                           250       260
                    ....*....|....*....|....*...
gi 2034231280  1677 YRTIKHIKRRRGQIIADYDQFRFCYKAV 1704
Cdd:smart00194  230 FEIVKELRSQRPGMVQTEEQYIFLYRAI 257
Y_phosphatase pfam00102
Protein-tyrosine phosphatase;
1465-1704 2.24e-60

Protein-tyrosine phosphatase;


Pssm-ID: 459674 [Multi-domain]  Cd Length: 234  Bit Score: 207.09  E-value: 2.24e-60
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2034231280 1465 NVHKNRYLDVLAADHYRPILTSQGPGaqaTDYINAVYVDGYLRRNQFIVTQTPLHTTVLDFWRLVWDHDIRTIVMVENFk 1544
Cdd:pfam00102    1 NLEKNRYKDVLPYDHTRVKLTGDPGP---SDYINASYIDGYKKPKKYIATQGPLPNTVEDFWRMVWEEKVTIIVMLTEL- 76
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2034231280 1545 hEDDTR---AEYWPPAASGGVMKqlEPFFLETTACYQQE-NITVRNLRLlsTQHPRDPARFVRQFQFNAWAEHaMAPQSK 1620
Cdd:pfam00102   77 -EEKGRekcAQYWPEEEGESLEY--GDFTVTLKKEKEDEkDYTVRTLEV--SNGGSEETRTVKHFHYTGWPDH-GVPESP 150
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2034231280 1621 TMMLDLVDSVFDWQEEACANerPVLVHCQDGSSHSGLFTTLAVVCERMEEDGEVDVYRTIKHIKRRRGQIIADYDQFRFC 1700
Cdd:pfam00102  151 NSLLDLLRKVRKSSLDGRSG--PIVVHCSAGIGRTGTFIAIDIALQQLEAEGEVDIFQIVKELRSQRPGMVQTLEQYIFL 228

                   ....
gi 2034231280 1701 YKAV 1704
Cdd:pfam00102  229 YDAI 232
R-PTPc-typeIIb-2 cd14556
PTP domain of type IIb (or R2B) subfamily receptor-type tyrosine-protein phosphatases, repeat ...
1496-1701 2.10e-56

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: 194.55  E-value: 2.10e-56
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2034231280 1496 YINAVYVDGYLRRNQFIVTQTPLHTTVLDFWRLVWDHDIRTIVMVENFKHEDDTRAEYWPPAASGgvmkQLEPFFLETTA 1575
Cdd:cd14556      1 YINAALLDSYKQPAAFIVTQHPLPNTVTDFWRLVYDYGCTSIVMLNQLDPKDQSCPQYWPDEGSG----TYGPIQVEFVS 76
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2034231280 1576 CYQQENITVRNLRLLSTQHPRDPARFVRQFQFNAWAEHAMAPQSKTMMLDLVDSVFDWQEEacANERPVLVHCQDGSSHS 1655
Cdd:cd14556     77 TTIDEDVISRIFRLQNTTRPQEGYRMVQQFQFLGWPRDRDTPPSKRALLKLLSEVEKWQEQ--SGEGPIVVHCLNGVGRS 154
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*.
gi 2034231280 1656 GLFTTLAVVCERMEEDGEVDVYRTIKHIKRRRGQIIADYDQFRFCY 1701
Cdd:cd14556    155 GVFCAISSVCERIKVENVVDVFQAVKTLRNHRPNMVETEEQYKFCY 200
PHA02738 PHA02738
hypothetical protein; Provisional
1169-1404 1.94e-38

hypothetical protein; Provisional


Pssm-ID: 222923 [Multi-domain]  Cd Length: 320  Bit Score: 146.99  E-value: 1.94e-38
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2034231280 1169 TARRQGSHLNRFPHLLPYDHSLVQLrPDVTSRGSYVNASFLPGYKKTPAYIAAQSPyNEETVLDFWRLIYQRSIKTVVMI 1248
Cdd:PHA02738    44 NAEKKNRKLNRYLDAVCFDHSRVIL-PAERNRGDYINANYVDGFEYKKKFICGQAP-TRQTCYDFYRMLWMEHVQIIVML 121
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2034231280 1249 TNVVEDHIVKCTQYWPT--QTKASFGDiFFLHLIEVNEYADYIIRTIGVKmKGDSDSKIVRLFEFTSWPDHGVPDDPIPF 1326
Cdd:PHA02738   122 CKKKENGREKCFPYWSDveQGSIRFGK-FKITTTQVETHPHYVKSTLLLT-DGTSATQTVTHFNFTAWPDHDVPKNTSEF 199
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2034231280 1327 LDMRYKVRRYQHD-------------SPSPILVHCGTGMARTGVFIAVDALIDQYASEGRVMVYDFVRRLRKDRPFMVRT 1393
Cdd:PHA02738   200 LNFVLEVRQCQKElaqeslqighnrlQPPPIVVHCNAGLGRTPCYCVVDISISRFDACATVSIPSIVSSIRNQRYYSLFI 279
                          250
                   ....*....|.
gi 2034231280 1394 LKQYVFIYEAI 1404
Cdd:PHA02738   280 PFQYFFCYRAV 290
COG5599 COG5599
Protein tyrosine phosphatase [Signal transduction mechanisms];
1174-1400 3.89e-28

Protein tyrosine phosphatase [Signal transduction mechanisms];


Pssm-ID: 444335 [Multi-domain]  Cd Length: 282  Bit Score: 115.96  E-value: 3.89e-28
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2034231280 1174 GSHLNRFPHLLPYDHSLVQlrpdvtSRGSYVNASFLPGYKKTpAYIAAQSPYnEETVLDFWRLIYQRSIKTVVMITNVVE 1253
Cdd:COG5599     42 GSPLNRFRDIQPYKETALR------ANLGYLNANYIQVIGNH-RYIATQYPL-EEQLEDFFQMLFDNNTPVLVVLASDDE 113
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2034231280 1254 DH--IVKCTQYWPTQTKASFGDIFFLHLIEVNEYADYIIRTIGVKMKGDSDSKI-VRLFEFTSWPDHGVPDDPI--PFLD 1328
Cdd:COG5599    114 ISkpKVKMPVYFRQDGEYGKYEVSSELTESIQLRDGIEARTYVLTIKGTGQKKIeIPVLHVKNWPDHGAISAEAlkNLAD 193
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2034231280 1329 MRYKVRRYQHDSPSPILVHCGTGMARTGVFIAVDALIDQYASEG--RVMVYDFVRRLRKDR-PFMVRTLKQYVFI 1400
Cdd:COG5599    194 LIDKKEKIKDPDKLLPVVHCRAGVGRTGTLIACLALSKSINALVqiTLSVEEIVIDMRTSRnGGMVQTSEQLDVL 268
PHA02746 PHA02746
protein tyrosine phosphatase; Provisional
1465-1704 3.71e-27

protein tyrosine phosphatase; Provisional


Pssm-ID: 165113 [Multi-domain]  Cd Length: 323  Bit Score: 114.36  E-value: 3.71e-27
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2034231280 1465 NVHKNRYLDVLAADHYRPILTSQG-----------PGAQ-------ATDYINAVYVDGYLRRNQFIVTQTPLHTTVLDFW 1526
Cdd:PHA02746    51 NLKKNRFHDIPCWDHSRVVINAHEslkmfdvgdsdGKKIevtsednAENYIHANFVDGFKEANKFICAQGPKEDTSEDFF 130
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2034231280 1527 RLVWDHDIRTIVMVENFKHEDDTRAEYWppAASGGVMKQLEPFFLETTACYQQENITVRNLRLlsTQHPRDPARFVRQFQ 1606
Cdd:PHA02746   131 KLISEHESQVIVSLTDIDDDDEKCFELW--TKEEDSELAFGRFVAKILDIIEELSFTKTRLMI--TDKISDTSREIHHFW 206
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2034231280 1607 FNAWAEHAMaPQSKTMMLDLVDSVFDWQEEACANER-------PVLVHCQDGSSHSGLFTTLAVVCERMEEDGEVDVYRT 1679
Cdd:PHA02746   207 FPDWPDNGI-PTGMAEFLELINKVNEEQAELIKQADndpqtlgPIVVHCSAGIGRAGTFCAIDNALEQLEKEKEVCLGEI 285
                          250       260
                   ....*....|....*....|....*
gi 2034231280 1680 IKHIKRRRGQIIADYDQFRFCYKAV 1704
Cdd:PHA02746   286 VLKIRKQRHSSVFLPEQYAFCYKAL 310
FU smart00261
Furin-like repeats;
55-96 8.02e-12

Furin-like repeats;


Pssm-ID: 214589 [Multi-domain]  Cd Length: 45  Bit Score: 61.37  E-value: 8.02e-12
                            10        20        30        40
                    ....*....|....*....|....*....|....*....|...
gi 2034231280    55 VCVACDPSCEGCSGEGPTLCTACKIGYRLQAAGCV-VCPEGFY 96
Cdd:smart00261    3 ECKPCHPECATCTGPGPDDCTSCKHGFFLDGGKCVsECPPGTY 45
FU cd00064
Furin-like repeats. Cysteine rich region. Exact function of the domain is not known. Furin is ...
58-104 7.59e-10

Furin-like repeats. Cysteine rich region. Exact function of the domain is not known. Furin is a serine-kinase dependent proprotein processor. Other members of this family include endoproteases and cell surface receptors.


Pssm-ID: 238021 [Multi-domain]  Cd Length: 49  Bit Score: 55.99  E-value: 7.59e-10
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*...
gi 2034231280   58 ACDPSCEGCSGEGPTLCTACKIGYRLQAAGCV-VCPEGFYGINCATEC 104
Cdd:cd00064      1 PCHPSCATCTGPGPDQCTSCRHGFYLDGGTCVsECPEGTYADTEGGVC 48
FN3 cd00063
Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein ...
416-509 1.05e-06

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: 48.65  E-value: 1.05e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2034231280  416 PVAPTamvsGLNVSGITATEAFVTWSNMPCNQqkGPSGNYELELTPVGGNTVRYVLTENRRA----FTGLAPFTEHNVRI 491
Cdd:cd00063      1 PSPPT----NLRVTDVTSTSVTLSWTPPEDDG--GPITGYVVEYREKGSGDWKEVEVTPGSEtsytLTGLKPGTEYEFRV 74
                           90
                   ....*....|....*....
gi 2034231280  492 RYANQVGRGPF-TSREFQT 509
Cdd:cd00063     75 RAVNGGGESPPsESVTVTT 93
fn3 pfam00041
Fibronectin type III domain;
423-503 7.17e-06

Fibronectin type III domain;


Pssm-ID: 394996 [Multi-domain]  Cd Length: 85  Bit Score: 45.87  E-value: 7.17e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2034231280  423 VSGLNVSGITATEAFVTWSnmPCNQQKGPSGNYELELTPVGG----NTVRYVLTENRRAFTGLAPFTEHNVRIRYANQVG 498
Cdd:pfam00041    3 PSNLTVTDVTSTSLTVSWT--PPPDGNGPITGYEVEYRPKNSgepwNEITVPGTTTSVTLTGLKPGTEYEVRVQAVNGGG 80

                   ....*
gi 2034231280  499 RGPFT 503
Cdd:pfam00041   81 EGPPS 85
FN3 smart00060
Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, ...
416-500 7.21e-06

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


Pssm-ID: 214495 [Multi-domain]  Cd Length: 83  Bit Score: 45.68  E-value: 7.21e-06
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2034231280   416 PVAPtamvSGLNVSGITATEAFVTWSNMPCNQQKGPSGNYELELTPVGGNTVRYVLTENRRAFT--GLAPFTEHNVRIRY 493
Cdd:smart00060    1 PSPP----SNLRVTDVTSTSVTLSWEPPPDDGITGYIVGYRVEYREEGSEWKEVNVTPSSTSYTltGLKPGTEYEFRVRA 76

                    ....*..
gi 2034231280   494 ANQVGRG 500
Cdd:smart00060   77 VNGAGEG 83
VSP pfam03302
Giardia variant-specific surface protein;
38-106 3.43e-05

Giardia variant-specific surface protein;


Pssm-ID: 146106 [Multi-domain]  Cd Length: 397  Bit Score: 48.43  E-value: 3.43e-05
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2034231280   38 KQCEANEYCKERADA----TAVCVACDPSCEGCSGEGpTLCTACKIGYRLQAAGCVVCP--EGFYGINCATEC-NC 106
Cdd:pfam03302  264 KTCTSNTVCTTCMDGyvktSDSCTKCDSSCETCTGAT-TTCKTCATGYYKSGTGCVSCTssESDNGITGVKGClNC 338
FN3 COG3401
Fibronectin type 3 domain [General function prediction only];
385-848 9.84e-05

Fibronectin type 3 domain [General function prediction only];


Pssm-ID: 442628 [Multi-domain]  Cd Length: 603  Bit Score: 47.30  E-value: 9.84e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2034231280  385 VLTWSKYSFTIDAQAETVDVSEVRTLTKISDPVAPTAMVS---GLNVSGITATEAFVTWSNMPCNqqKGPSGNYELELTP 461
Cdd:COG3401      4 SYLTSLDAGIAASAAANTAVNALSKAGGSGKTILVYLAVVlsvTTKESPGTLLVAAGLSSGGGLG--TGGRAGTTSGVAA 81
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2034231280  462 VGGNTVRYVLTENRRAFTGLAPFTEHNVRIRYANQVGRGPFTSREFQTLEGVPTAVQIVSATATSTTITVTFDPPLRTNG 541
Cdd:COG3401     82 VAVAAAPPTATGLTTLTGSGSVGGATNTGLTSSDEVPSPAVGTATTATAVAGGAATAGTYALGAGLYGVDGANASGTTAS 161
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2034231280  542 ILVSYTVTFSTTSDFNETESRTEQGRSG-LRSIIVGRLQADTLYYLKMAASTNAGIGQYGSVTSRRTLEAPPPAEdIDLR 620
Cdd:COG3401    162 SVAGAGVVVSPDTSATAAVATTSLTVTStTLVDGGGDIEPGTTYYYRVAATDTGGESAPSNEVSVTTPTTPPSAP-TGLT 240
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2034231280  621 SDSQTVNCLSLSWDPPQNRAgdiqsykprpptfvrssytnvtlniepvmskyvpITSYRLHvllltnsnRNLPFQSAPGY 700
Cdd:COG3401    241 ATADTPGSVTLSWDPVTESD----------------------------------ATGYRVY--------RSNSGDGPFTK 278
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2034231280  701 ITAELESSavpntiefvigdgevyggYTNQPLESNSNYRIYYVAVSTLNNETT-SNYDSLTlpfptvPFDPALAPPLPLS 779
Cdd:COG3401    279 VATVTTTS------------------YTDTGLTNGTTYYYRVTAVDAAGNESApSNVVSVT------TDLTPPAAPSGLT 334
                          410       420       430       440       450       460
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2034231280  780 LSSRTTECLNLTWVTPTglSPLITSFDFTTSRAGDSDDTPITRSVPATdrAFQQCNLAPFTLYTVRISA 848
Cdd:COG3401    335 ATAVGSSSITLSWTASS--DADVTGYNVYRSTSGGGTYTKIAETVTTT--SYTDTGLTPGTTYYYKVTA 399
FN3 cd00063
Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein ...
774-864 1.01e-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: 42.87  E-value: 1.01e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2034231280  774 PPLPLSLSSRTTECLNLTWVTPTGLSPLITSFDFTTSRAGDSDDTPITrSVPATDRAFQQCNLAPFTLYTVRISARIGQE 853
Cdd:cd00063      3 PPTNLRVTDVTSTSVTLSWTPPEDDGGPITGYVVEYREKGSGDWKEVE-VTPGSETSYTLTGLKPGTEYEFRVRAVNGGG 81
                           90
                   ....*....|..
gi 2034231280  854 VSA-TTTETFLT 864
Cdd:cd00063     82 ESPpSESVTVTT 93
fn3 pfam00041
Fibronectin type III domain;
774-858 1.59e-04

Fibronectin type III domain;


Pssm-ID: 394996 [Multi-domain]  Cd Length: 85  Bit Score: 42.02  E-value: 1.59e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2034231280  774 PPLPLSLSSRTTECLNLTWVTPTGLSPLITSFDFTTSRAGDSDDtPITRSVPATDRAFQQCNLAPFTLYTVRISARIGQE 853
Cdd:pfam00041    2 APSNLTVTDVTSTSLTVSWTPPPDGNGPITGYEVEYRPKNSGEP-WNEITVPGTTTSVTLTGLKPGTEYEVRVQAVNGGG 80

                   ....*
gi 2034231280  854 VSATT 858
Cdd:pfam00041   81 EGPPS 85
Furin-like pfam00757
Furin-like cysteine rich region;
43-138 3.76e-04

Furin-like cysteine rich region;


Pssm-ID: 395614 [Multi-domain]  Cd Length: 143  Bit Score: 42.42  E-value: 3.76e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2034231280   43 NEYCKERADATAVCvaCDPSCEG-CSGEGPTLCTACKiGYRLQAAgCVV-CPEGFY--GINCATECNCLNKVCDNV---- 114
Cdd:pfam00757   35 PEQCKKRCTKPGEC--CHEQCLGgCTGPNDSDCLACR-HFNDEGT-CVDqCPPGTYqfGWRCVTFKECPKSHLPGYnplv 110
                           90       100       110
                   ....*....|....*....|....*....|....
gi 2034231280  115 --NGACaIWKCKRGYTGI--------PfCRDKCP 138
Cdd:pfam00757  111 ihNGEC-VRECPSGYTEVennsrkceP-CEGLCP 142
EGF_Lam cd00055
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ...
104-145 4.36e-04

Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous components of basement membranes that mediate cell adhesion, growth migration, and differentiation; the laminin-type epidermal growth factor-like module occurs in tandem arrays; the domain contains 4 disulfide bonds (loops a-d) the first three resemble epidermal growth factor (EGF); the number of copies of this domain in the different forms of laminins is highly variable ranging from 3 up to 22 copies


Pssm-ID: 238012  Cd Length: 50  Bit Score: 39.64  E-value: 4.36e-04
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*..
gi 2034231280  104 CNC-----LNKVCDNVNGACaiwKCKRGYTGiPFCrDKCPAGTFGLD 145
Cdd:cd00055      2 CDCnghgsLSGQCDPGTGQC---ECKPNTTG-RRC-DRCAPGYYGLP 43
fn3 pfam00041
Fibronectin type III domain;
190-284 2.11e-03

Fibronectin type III domain;


Pssm-ID: 394996 [Multi-domain]  Cd Length: 85  Bit Score: 38.94  E-value: 2.11e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2034231280  190 PEVVSVQCNNITIQWDAfneeDNIGQGPVYAYNVEVRlnqtENGTSGPWQTKQTVLHveggnppklTYRISVSGLEPDKD 269
Cdd:pfam00041    6 LTVTDVTSTSLTVSWTP----PPDGNGPITGYEVEYR----PKNSGEPWNEITVPGT---------TTSVTLTGLKPGTE 68
                           90
                   ....*....|....*.
gi 2034231280  270 YNFRVNTI-GANSGKP 284
Cdd:pfam00041   69 YEVRVQAVnGGGEGPP 84
FN3 cd00063
Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein ...
190-274 3.11e-03

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: 38.63  E-value: 3.11e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2034231280  190 PEVVSVQCNNITIQWDAFNEEDnigqGPVYAYNVEVRlnqteNGTSGPWQTkqtvlhVEGGNPPKLTYRisVSGLEPDKD 269
Cdd:cd00063      7 LRVTDVTSTSVTLSWTPPEDDG----GPITGYVVEYR-----EKGSGDWKE------VEVTPGSETSYT--LTGLKPGTE 69

                   ....*
gi 2034231280  270 YNFRV 274
Cdd:cd00063     70 YEFRV 74
CDC14 COG2453
Protein-tyrosine phosphatase [Signal transduction mechanisms];
1624-1699 7.23e-03

Protein-tyrosine phosphatase [Signal transduction mechanisms];


Pssm-ID: 441989 [Multi-domain]  Cd Length: 140  Bit Score: 38.80  E-value: 7.23e-03
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2034231280 1624 LDLVDSVFDWQEEACANERPVLVHCQDGSSHSGLFTTLAVVcermeEDGeVDVYRTIKHIKRRRGQIIADYDQFRF 1699
Cdd:COG2453     63 DEQLQEAVDFIDEALREGKKVLVHCRGGIGRTGTVAAAYLV-----LLG-LSAEEALARVRAARPGAVETPAQRAF 132
 
Name Accession Description Interval E-value
PTPc smart00194
Protein tyrosine phosphatase, catalytic domain;
1151-1406 5.68e-82

Protein tyrosine phosphatase, catalytic domain;


Pssm-ID: 214550 [Multi-domain]  Cd Length: 259  Bit Score: 270.30  E-value: 5.68e-82
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2034231280  1151 FKDEFHALPH-KSQKATDNTARRQG-SHLNRFPHLLPYDHSLVQLRPDVTSRGSYVNASFLPGYKKTPAYIAAQSPyNEE 1228
Cdd:smart00194    2 LEEEFEKLDRlKPDDESCTVAAFPEnRDKNRYKDVLPYDHTRVKLKPPPGEGSDYINASYIDGPNGPKAYIATQGP-LPS 80
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2034231280  1229 TVLDFWRLIYQRSIKTVVMITNVVEDHIVKCTQYWP--TQTKASFGDIFfLHLIEVNEYADYIIRTIGVKMKGDSDSKIV 1306
Cdd:smart00194   81 TVEDFWRMVWEQKVTVIVMLTELVEKGREKCAQYWPdeEGEPLTYGDIT-VTLKSVEKVDDYTIRTLEVTNTGCSETRTV 159
                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2034231280  1307 RLFEFTSWPDHGVPDDPIPFLDMRYKVRRYQHDSPSPILVHCGTGMARTGVFIAVDALIDQYASEGRVMVYDFVRRLRKD 1386
Cdd:smart00194  160 THYHYTNWPDHGVPESPESILDLIRAVRKSQSTSTGPIVVHCSAGVGRTGTFIAIDILLQQLEAGKEVDIFEIVKELRSQ 239
                           250       260
                    ....*....|....*....|
gi 2034231280  1387 RPFMVRTLKQYVFIYEAIFE 1406
Cdd:smart00194  240 RPGMVQTEEQYIFLYRAILE 259
PTPc cd00047
catalytic domain of protein tyrosine phosphatases; Protein tyrosine phosphatases (PTP, EC 3.1. ...
1203-1402 2.20e-77

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: 254.52  E-value: 2.20e-77
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2034231280 1203 YVNASFLPGYKKTPAYIAAQSPyNEETVLDFWRLIYQRSIKTVVMITNVVEDHIVKCTQYWPT--QTKASFGDiFFLHLI 1280
Cdd:cd00047      1 YINASYIDGYRGPKEYIATQGP-LPNTVEDFWRMVWEQKVSVIVMLTNLVEKGREKCERYWPEegGKPLEYGD-ITVTLV 78
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2034231280 1281 EVNEYADYIIRTIGVKMKGDSDSKIVRLFEFTSWPDHGVPDDPIPFLDMRYKVRRYQHDSPSPILVHCGTGMARTGVFIA 1360
Cdd:cd00047     79 SEEELSDYTIRTLELSPKGCSESREVTHLHYTGWPDHGVPSSPEDLLALVRRVRKEARKPNGPIVVHCSAGVGRTGTFIA 158
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|..
gi 2034231280 1361 VDALIDQYASEGRVMVYDFVRRLRKDRPFMVRTLKQYVFIYE 1402
Cdd:cd00047    159 IDILLERLEAEGEVDVFEIVKALRKQRPGMVQTLEQYEFIYE 200
Y_phosphatase pfam00102
Protein-tyrosine phosphatase;
1178-1406 2.65e-76

Protein-tyrosine phosphatase;


Pssm-ID: 459674 [Multi-domain]  Cd Length: 234  Bit Score: 252.93  E-value: 2.65e-76
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2034231280 1178 NRFPHLLPYDHSLVQLRPDVTSRGsYVNASFLPGYKKTPAYIAAQSPYnEETVLDFWRLIYQRSIKTVVMITNVVEDHIV 1257
Cdd:pfam00102    5 NRYKDVLPYDHTRVKLTGDPGPSD-YINASYIDGYKKPKKYIATQGPL-PNTVEDFWRMVWEEKVTIIVMLTELEEKGRE 82
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2034231280 1258 KCTQYWPTQTKAS--FGDiFFLHLIEVNEY-ADYIIRTIGVKMKGDSDSKIVRLFEFTSWPDHGVPDDPIPFLDMRYKVR 1334
Cdd:pfam00102   83 KCAQYWPEEEGESleYGD-FTVTLKKEKEDeKDYTVRTLEVSNGGSEETRTVKHFHYTGWPDHGVPESPNSLLDLLRKVR 161
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2034231280 1335 RYQHDSPS-PILVHCGTGMARTGVFIAVDALIDQYASEGRVMVYDFVRRLRKDRPFMVRTLKQYVFIYEAIFE 1406
Cdd:pfam00102  162 KSSLDGRSgPIVVHCSAGIGRTGTFIAIDIALQQLEAEGEVDIFQIVKELRSQRPGMVQTLEQYIFLYDAILE 234
R3-PTPc cd14548
catalytic domain of R3 subfamily receptor-type tyrosine-protein phosphatases and similar ...
1179-1402 1.34e-70

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: 236.10  E-value: 1.34e-70
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2034231280 1179 RFPHLLPYDHSLVQLRPDVTSRGS-YVNASFLPGYKKTPAYIAAQSPYnEETVLDFWRLIYQRSIKTVVMITNVVEDHIV 1257
Cdd:cd14548      1 RYTNILPYDHSRVKLIPINEEEGSdYINANYIPGYNSPREFIATQGPL-PGTKDDFWRMVWEQNSHTIVMLTQCMEKGRV 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2034231280 1258 KCTQYWP-TQTKASFGDIFfLHLIEVNEYADYIIRTIGVKMKGDSdsKIVRLFEFTSWPDHGVPDDPIPFLDMRYKVRRY 1336
Cdd:cd14548     80 KCDHYWPfDQDPVYYGDIT-VTMLSESVLPDWTIREFKLERGDEV--RSVRQFHFTAWPDHGVPEAPDSLLRFVRLVRDY 156
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2034231280 1337 QHDSPSPILVHCGTGMARTGVFIAVDALIDQYASEGRVMVYDFVRRLRKDRPFMVRTLKQYVFIYE 1402
Cdd:cd14548    157 IKQEKGPTIVHCSAGVGRTGTFIALDRLLQQIESEDYVDIFGIVYDLRKHRPLMVQTEAQYIFLHQ 222
R-PTPc-LAR-1 cd14553
catalytic domain of LAR family receptor-type tyrosine-protein phosphatases, repeat 1; The LAR ...
1178-1406 2.07e-69

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: 233.44  E-value: 2.07e-69
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2034231280 1178 NRFPHLLPYDHSLVQLRPDVTSRGS-YVNASFLPGYKKTPAYIAAQSPYnEETVLDFWRLIYQRSIKTVVMITNVVEDHI 1256
Cdd:cd14553      7 NRYANVIAYDHSRVILQPIEGVPGSdYINANYCDGYRKQNAYIATQGPL-PETFGDFWRMVWEQRSATIVMMTKLEERSR 85
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2034231280 1257 VKCTQYWPTQTKASFGDIFfLHLIEVNEYADYIIRTIGVKMKGDSDSKIVRLFEFTSWPDHGVPDDPIPFLDMRYKVRRY 1336
Cdd:cd14553     86 VKCDQYWPTRGTETYGLIQ-VTLLDTVELATYTVRTFALHKNGSSEKREVRQFQFTAWPDHGVPEHPTPFLAFLRRVKAC 164
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2034231280 1337 QHDSPSPILVHCGTGMARTGVFIAVDALIDQYASEGRVMVYDFVRRLRKDRPFMVRTLKQYVFIYEAIFE 1406
Cdd:cd14553    165 NPPDAGPIVVHCSAGVGRTGCFIVIDSMLERIKHEKTVDIYGHVTCLRAQRNYMVQTEDQYIFIHDALLE 234
PTPc smart00194
Protein tyrosine phosphatase, catalytic domain;
1438-1704 4.45e-65

Protein tyrosine phosphatase, catalytic domain;


Pssm-ID: 214550 [Multi-domain]  Cd Length: 259  Bit Score: 221.76  E-value: 4.45e-65
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2034231280  1438 LRDQYKLLETFTrsPRRDQCKTAQLEINVHKNRYLDVLAADHYRPILTSqgPGAQATDYINAVYVDGYLRRNQFIVTQTP 1517
Cdd:smart00194    2 LEEEFEKLDRLK--PDDESCTVAAFPENRDKNRYKDVLPYDHTRVKLKP--PPGEGSDYINASYIDGPNGPKAYIATQGP 77
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2034231280  1518 LHTTVLDFWRLVWDHDIRTIVMVENFKHEDDTR-AEYWPpaASGGVMKQLEPFFLETTACYQQENITVRNLRLLSTQhpR 1596
Cdd:smart00194   78 LPSTVEDFWRMVWEQKVTVIVMLTELVEKGREKcAQYWP--DEEGEPLTYGDITVTLKSVEKVDDYTIRTLEVTNTG--C 153
                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2034231280  1597 DPARFVRQFQFNAWAEHaMAPQSKTMMLDLVDSVFDWQEeacANERPVLVHCQDGSSHSGLFTTLAVVCERMEEDGEVDV 1676
Cdd:smart00194  154 SETRTVTHYHYTNWPDH-GVPESPESILDLIRAVRKSQS---TSTGPIVVHCSAGVGRTGTFIAIDILLQQLEAGKEVDI 229
                           250       260
                    ....*....|....*....|....*...
gi 2034231280  1677 YRTIKHIKRRRGQIIADYDQFRFCYKAV 1704
Cdd:smart00194  230 FEIVKELRSQRPGMVQTEEQYIFLYRAI 257
R-PTPc-J cd14615
catalytic domain of receptor-type tyrosine-protein phosphatase J; Receptor-type ...
1178-1400 6.83e-63

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: 214.30  E-value: 6.83e-63
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2034231280 1178 NRFPHLLPYDHSLVQLRPDVTSRGSYVNASFLPGYKKTPAYIAAQSPYnEETVLDFWRLIYQRSIKTVVMITNVVEDHIV 1257
Cdd:cd14615      1 NRYNNVLPYDISRVKLSVQSHSTDDYINANYMPGYNSKKEFIAAQGPL-PNTVKDFWRMVWEKNVYAIVMLTKCVEQGRT 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2034231280 1258 KCTQYWPTQTKASFGDIFfLHLIEVNEYADYIIRTIGVKMKGDSDSKIVRLFEFTSWPDHGVPDDPIPFLDMRYKVRRY- 1336
Cdd:cd14615     80 KCEEYWPSKQKKDYGDIT-VTMTSEIVLPEWTIRDFTVKNAQTNESRTVRHFHFTSWPDHGVPETTDLLINFRHLVREYm 158
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2034231280 1337 -QHDSPSPILVHCGTGMARTGVFIAVDALIDQYASEGRVMVYDFVRRLRKDRPFMVRTLKQYVFI 1400
Cdd:cd14615    159 kQNPPNSPILVHCSAGVGRTGTFIAIDRLIYQIENENVVDVYGIVYDLRMHRPLMVQTEDQYVFL 223
R-PTPc-H cd14619
catalytic domain of receptor-type tyrosine-protein phosphatase H; Receptor-type ...
1178-1406 1.13e-61

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: 210.90  E-value: 1.13e-61
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2034231280 1178 NRFPHLLPYDHSLVQLRPDVTSRGS-YVNASFLPGYKKTPAYIAAQSPYnEETVLDFWRLIYQRSIKTVVMITNVVEDHI 1256
Cdd:cd14619      1 NRFRNVLPYDWSRVPLKPIHEEPGSdYINANYMPGYWSSQEFIATQGPL-PQTVGDFWRMIWEQQSSTIVMLTNCMEAGR 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2034231280 1257 VKCTQYWPTQ-TKASFGDIFfLHLIEVNEYADYIIRTIGVKMKGDSDSKIVRLFEFTSWPDHGVPDDPIPFLDMRYKVRR 1335
Cdd:cd14619     80 VKCEHYWPLDyTPCTYGHLR-VTVVSEEVMENWTVREFLLKQVEEQKTLSVRHFHFTAWPDHGVPSSTDTLLAFRRLLRQ 158
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2034231280 1336 Y--QHDSPSPILVHCGTGMARTGVFIAVDALIDQYASEGRVMVYDFVRRLRKDRPFMVRTLKQYVFIYEAIFE 1406
Cdd:cd14619    159 WldQTMSGGPTVVHCSAGVGRTGTLIALDVLLQQLQSEGLLGPFSFVQKMRENRPLMVQTESQYVFLHQCILD 231
R-PTPc-A-1 cd14621
catalytic domain of receptor-type tyrosine-protein phosphatase A, repeat 1; Receptor-type ...
1151-1413 1.43e-61

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: 213.35  E-value: 1.43e-61
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2034231280 1151 FKDEFHALPHKSQKAT-DNTARRQGSHLNRFPHLLPYDHSLVQLRP-DVTSRGSYVNASFLPGYKKTPAYIAAQSPyNEE 1228
Cdd:cd14621     28 FREEFNALPACPIQATcEAASKEENKEKNRYVNILPYDHSRVHLTPvEGVPDSDYINASFINGYQEKNKFIAAQGP-KEE 106
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2034231280 1229 TVLDFWRLIYQRSIKTVVMITNVVEDHIVKCTQYWPTQTKASFGDIFfLHLIEVNEYADYIIRTIGVKMKGDSDSK---- 1304
Cdd:cd14621    107 TVNDFWRMIWEQNTATIVMVTNLKERKECKCAQYWPDQGCWTYGNIR-VSVEDVTVLVDYTVRKFCIQQVGDVTNKkpqr 185
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2034231280 1305 IVRLFEFTSWPDHGVPDDPIPFLDMRYKVRRYQHDSPSPILVHCGTGMARTGVFIAVDALIDQYASEGRVMVYDFVRRLR 1384
Cdd:cd14621    186 LITQFHFTSWPDFGVPFTPIGMLKFLKKVKNCNPQYAGAIVVHCSAGVGRTGTFIVIDAMLDMMHAERKVDVYGFVSRIR 265
                          250       260
                   ....*....|....*....|....*....
gi 2034231280 1385 KDRPFMVRTLKQYVFIYEAIFEEFHAGDT 1413
Cdd:cd14621    266 AQRCQMVQTDMQYVFIYQALLEHYLYGDT 294
Y_phosphatase pfam00102
Protein-tyrosine phosphatase;
1465-1704 2.24e-60

Protein-tyrosine phosphatase;


Pssm-ID: 459674 [Multi-domain]  Cd Length: 234  Bit Score: 207.09  E-value: 2.24e-60
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2034231280 1465 NVHKNRYLDVLAADHYRPILTSQGPGaqaTDYINAVYVDGYLRRNQFIVTQTPLHTTVLDFWRLVWDHDIRTIVMVENFk 1544
Cdd:pfam00102    1 NLEKNRYKDVLPYDHTRVKLTGDPGP---SDYINASYIDGYKKPKKYIATQGPLPNTVEDFWRMVWEEKVTIIVMLTEL- 76
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2034231280 1545 hEDDTR---AEYWPPAASGGVMKqlEPFFLETTACYQQE-NITVRNLRLlsTQHPRDPARFVRQFQFNAWAEHaMAPQSK 1620
Cdd:pfam00102   77 -EEKGRekcAQYWPEEEGESLEY--GDFTVTLKKEKEDEkDYTVRTLEV--SNGGSEETRTVKHFHYTGWPDH-GVPESP 150
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2034231280 1621 TMMLDLVDSVFDWQEEACANerPVLVHCQDGSSHSGLFTTLAVVCERMEEDGEVDVYRTIKHIKRRRGQIIADYDQFRFC 1700
Cdd:pfam00102  151 NSLLDLLRKVRKSSLDGRSG--PIVVHCSAGIGRTGTFIAIDIALQQLEAEGEVDIFQIVKELRSQRPGMVQTLEQYIFL 228

                   ....
gi 2034231280 1701 YKAV 1704
Cdd:pfam00102  229 YDAI 232
R5-PTPc-1 cd14549
catalytic domain of R5 subfamily receptor-type tyrosine-protein phosphatases, repeat 1; The R5 ...
1203-1402 1.05e-59

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: 204.12  E-value: 1.05e-59
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2034231280 1203 YVNASFLPGYKKTPAYIAAQSPYnEETVLDFWRLIYQRSIKTVVMITNVVEDHIVKCTQYWPTQTKASFGDIFfLHLIEV 1282
Cdd:cd14549      1 YINANYVDGYNKARAYIATQGPL-PSTFDDFWRMVWEQNSAIIVMITNLVERGRRKCDQYWPKEGTETYGNIQ-VTLLST 78
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2034231280 1283 NEYADYIIRTIGVKM------KGDSDSKIVRLFEFTSWPDHGVPDDPIPFLDMRYKVRRYQHDSPSPILVHCGTGMARTG 1356
Cdd:cd14549     79 EVLATYTVRTFSLKNlklkkvKGRSSERVVYQYHYTQWPDHGVPDYTLPVLSFVRKSSAANPPGAGPIVVHCSAGVGRTG 158
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*.
gi 2034231280 1357 VFIAVDALIDQYASEGRVMVYDFVRRLRKDRPFMVRTLKQYVFIYE 1402
Cdd:cd14549    159 TYIVIDSMLQQIQDKGTVNVFGFLKHIRTQRNYLVQTEEQYIFIHD 204
R-PTPc-F-1 cd14626
catalytic domain of receptor-type tyrosine-protein phosphatase F, repeat 1; Receptor-type ...
1148-1406 1.71e-59

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: 206.43  E-value: 1.71e-59
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2034231280 1148 ALTFKDEFHALPHKSQKATDNTARRQGSHLNRFPHLLPYDHSLVQLRP-DVTSRGSYVNASFLPGYKKTPAYIAAQSPYn 1226
Cdd:cd14626     15 GLKFSQEYESIDPGQQFTWENSNLEVNKPKNRYANVIAYDHSRVILTSvDGVPGSDYINANYIDGYRKQNAYIATQGPL- 93
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2034231280 1227 EETVLDFWRLIYQRSIKTVVMITNVVEDHIVKCTQYWPTQTKASFGDIFfLHLIEVNEYADYIIRTIGVKMKGDSDSKIV 1306
Cdd:cd14626     94 PETLSDFWRMVWEQRTATIVMMTRLEEKSRVKCDQYWPIRGTETYGMIQ-VTLLDTVELATYSVRTFALYKNGSSEKREV 172
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2034231280 1307 RLFEFTSWPDHGVPDDPIPFLDMRYKVRRYQHDSPSPILVHCGTGMARTGVFIAVDALIDQYASEGRVMVYDFVRRLRKD 1386
Cdd:cd14626    173 RQFQFMAWPDHGVPEYPTPILAFLRRVKACNPPDAGPMVVHCSAGVGRTGCFIVIDAMLERMKHEKTVDIYGHVTCMRSQ 252
                          250       260
                   ....*....|....*....|
gi 2034231280 1387 RPFMVRTLKQYVFIYEAIFE 1406
Cdd:cd14626    253 RNYMVQTEDQYIFIHEALLE 272
R-PTPc-E-1 cd14620
catalytic domain of receptor-type tyrosine-protein phosphatase E, repeat 1; Receptor-type ...
1180-1406 5.55e-59

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: 203.25  E-value: 5.55e-59
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2034231280 1180 FPHLLPYDHSLVQLRP-DVTSRGSYVNASFLPGYKKTPAYIAAQSPyNEETVLDFWRLIYQRSIKTVVMITNVVEDHIVK 1258
Cdd:cd14620      1 YPNILPYDHSRVILSQlDGIPCSDYINASYIDGYKEKNKFIAAQGP-KQETVNDFWRMVWEQKSATIVMLTNLKERKEEK 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2034231280 1259 CTQYWPTQTKASFGDIFfLHLIEVNEYADYIIRTIGVKMKGDSDSKIVRL---FEFTSWPDHGVPDDPIPFLDMRYKVRR 1335
Cdd:cd14620     80 CYQYWPDQGCWTYGNIR-VAVEDCVVLVDYTIRKFCIQPQLPDGCKAPRLvtqLHFTSWPDFGVPFTPIGMLKFLKKVKS 158
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2034231280 1336 YQHDSPSPILVHCGTGMARTGVFIAVDALIDQYASEGRVMVYDFVRRLRKDRPFMVRTLKQYVFIYEAIFE 1406
Cdd:cd14620    159 VNPVHAGPIVVHCSAGVGRTGTFIVIDAMIDMMHAEQKVDVFEFVSRIRNQRPQMVQTDMQYSFIYQALLE 229
R-PTPc-T-1 cd14630
catalytic domain of receptor-type tyrosine-protein phosphatase T, repeat 1; Receptor-type ...
1178-1406 3.95e-58

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: 201.02  E-value: 3.95e-58
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2034231280 1178 NRFPHLLPYDHSLVQLRP-DVTSRGSYVNASFLPGYKKTPAYIAAQSPYnEETVLDFWRLIYQRSIKTVVMITNVVEDHI 1256
Cdd:cd14630      7 NRYGNIISYDHSRVRLQLlDGDPHSDYINANYIDGYHRPRHYIATQGPM-QETVKDFWRMIWQENSASVVMVTNLVEVGR 85
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2034231280 1257 VKCTQYWPTQTKAsFGDIFfLHLIEVNEYADYIIRTIGVKMKGDSDSKIVRLFEFTSWPDHGVPDDPIPFLDMRYKVRRY 1336
Cdd:cd14630     86 VKCVRYWPDDTEV-YGDIK-VTLIETEPLAEYVIRTFTVQKKGYHEIREIRQFHFTSWPDHGVPCYATGLLGFVRQVKFL 163
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2034231280 1337 QHDSPSPILVHCGTGMARTGVFIAVDALIDQYASEGRVMVYDFVRRLRKDRPFMVRTLKQYVFIYEAIFE 1406
Cdd:cd14630    164 NPPDAGPIVVHCSAGAGRTGCFIAIDIMLDMAENEGVVDIFNCVRELRAQRVNMVQTEEQYVFVHDAILE 233
PTP_fungal cd18533
fungal protein tyrosine phosphatases; This subfamily contains Saccharomyces cerevisiae ...
1203-1402 8.13e-57

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: 196.32  E-value: 8.13e-57
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2034231280 1203 YVNASFL-PGYKKTPAYIAAQSPYnEETVLDFWRLIYQRSIKTVVMITNVVEDHIVKCTQYWPTQTKASFGDIFFLHLIE 1281
Cdd:cd18533      1 YINASYItLPGTSSKRYIATQGPL-PATIGDFWKMIWQNNVGVIVMLTPLVENGREKCDQYWPSGEYEGEYGDLTVELVS 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2034231280 1282 VNEYAD--YIIRTIGVKmKGDSDSKIVRLFEFTSWPDHGVPDDPIPFLDM----RYKVRryQHDSPSPILVHCGTGMART 1355
Cdd:cd18533     80 EEENDDggFIVREFELS-KEDGKVKKVYHIQYKSWPDFGVPDSPEDLLTLiklkRELND--SASLDPPIIVHCSAGVGRT 156
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 2034231280 1356 GVFIAVDALID---------QYASEGRVMVYDFVRRLRKDRPFMVRTLKQYVFIYE 1402
Cdd:cd18533    157 GTFIALDSLLDelkrglsdsQDLEDSEDPVYEIVNQLRKQRMSMVQTLRQYIFLYD 212
R-PTPc-typeIIb-2 cd14556
PTP domain of type IIb (or R2B) subfamily receptor-type tyrosine-protein phosphatases, repeat ...
1496-1701 2.10e-56

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: 194.55  E-value: 2.10e-56
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2034231280 1496 YINAVYVDGYLRRNQFIVTQTPLHTTVLDFWRLVWDHDIRTIVMVENFKHEDDTRAEYWPPAASGgvmkQLEPFFLETTA 1575
Cdd:cd14556      1 YINAALLDSYKQPAAFIVTQHPLPNTVTDFWRLVYDYGCTSIVMLNQLDPKDQSCPQYWPDEGSG----TYGPIQVEFVS 76
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2034231280 1576 CYQQENITVRNLRLLSTQHPRDPARFVRQFQFNAWAEHAMAPQSKTMMLDLVDSVFDWQEEacANERPVLVHCQDGSSHS 1655
Cdd:cd14556     77 TTIDEDVISRIFRLQNTTRPQEGYRMVQQFQFLGWPRDRDTPPSKRALLKLLSEVEKWQEQ--SGEGPIVVHCLNGVGRS 154
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*.
gi 2034231280 1656 GLFTTLAVVCERMEEDGEVDVYRTIKHIKRRRGQIIADYDQFRFCY 1701
Cdd:cd14556    155 GVFCAISSVCERIKVENVVDVFQAVKTLRNHRPNMVETEEQYKFCY 200
R-PTPc-C-1 cd14557
catalytic domain of receptor-type tyrosine-protein phosphatase C, repeat 1; Receptor-type ...
1203-1402 3.93e-56

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: 193.89  E-value: 3.93e-56
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2034231280 1203 YVNASFLPGYKKTPAYIAAQSPyNEETVLDFWRLIYQRSIKTVVMITNVVEDHIVKCTQYWPT--QTKASFGDIFfLHLI 1280
Cdd:cd14557      1 YINASYIDGFKEPRKYIAAQGP-KDETVDDFWRMIWEQKSTVIVMVTRCEEGNRNKCAQYWPSmeEGSRAFGDVV-VKIN 78
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2034231280 1281 EVNEYADYIIRTIGVKMKGDSDS-KIVRLFEFTSWPDHGVPDDPIPFLDMRYKVRRYQHDSPSPILVHCGTGMARTGVFI 1359
Cdd:cd14557     79 EEKICPDYIIRKLNINNKKEKGSgREVTHIQFTSWPDHGVPEDPHLLLKLRRRVNAFNNFFSGPIVVHCSAGVGRTGTYI 158
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|...
gi 2034231280 1360 AVDALIDQYASEGRVMVYDFVRRLRKDRPFMVRTLKQYVFIYE 1402
Cdd:cd14557    159 GIDAMLEGLEAEGRVDVYGYVVKLRRQRCLMVQVEAQYILIHQ 201
R-PTPc-M-1 cd14633
catalytic domain of receptor-type tyrosine-protein phosphatase M, repeat 1; Receptor-type ...
1151-1406 5.47e-56

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: 196.42  E-value: 5.47e-56
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2034231280 1151 FKDEFHALPHKSQKATDNTARRQGSHLNRFPHLLPYDHSLVQLRPDVTSRGS-YVNASFLPGYKKTPAYIAAQSPYnEET 1229
Cdd:cd14633     17 FKEEYESFFEGQSAPWDSAKKDENRMKNRYGNIIAYDHSRVRLQPIEGETSSdYINGNYIDGYHRPNHYIATQGPM-QET 95
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2034231280 1230 VLDFWRLIYQRSIKTVVMITNVVEDHIVKCTQYWPTQTKAsFGDIFfLHLIEVNEYADYIIRTIGVKMKGDSDSKIVRLF 1309
Cdd:cd14633     96 IYDFWRMVWHENTASIIMVTNLVEVGRVKCCKYWPDDTEI-YKDIK-VTLIETELLAEYVIRTFAVEKRGVHEIREIRQF 173
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2034231280 1310 EFTSWPDHGVPDDPIPFLDMRYKVRRYQHDSPSPILVHCGTGMARTGVFIAVDALIDQYASEGRVMVYDFVRRLRKDRPF 1389
Cdd:cd14633    174 HFTGWPDHGVPYHATGLLGFVRQVKSKSPPNAGPLVVHCSAGAGRTGCFIVIDIMLDMAEREGVVDIYNCVRELRSRRVN 253
                          250
                   ....*....|....*..
gi 2034231280 1390 MVRTLKQYVFIYEAIFE 1406
Cdd:cd14633    254 MVQTEEQYVFIHDAILE 270
PTPc-N9 cd14543
catalytic domain of tyrosine-protein phosphatase non-receptor type 9; Tyrosine-protein ...
1178-1401 2.10e-55

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: 194.51  E-value: 2.10e-55
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2034231280 1178 NRFPHLLPYDHSLVQLRPDVTS-RGSYVNASFLPGYKKTPAYIAAQSPYnEETVLDFWRLIYQRSIKTVVMITNVVEDHI 1256
Cdd:cd14543     33 NRYGDVLCLDQSRVKLPKRNGDeRTDYINANFMDGYKQKNAYIATQGPL-PKTYSDFWRMVWEQKVLVIVMTTRVVERGR 111
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2034231280 1257 VKCTQYWPTQTKAS--FGDIFFLHLiEVNEYADYIIRTIGVKMKGDSDSKIVRLFEFTSWPDHGVPDDPIPFLDMRYKVR 1334
Cdd:cd14543    112 VKCGQYWPLEEGSSlrYGDLTVTNL-SVENKEHYKKTTLEIHNTETDESRQVTHFQFTSWPDFGVPSSAAALLDFLGEVR 190
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2034231280 1335 RYQ-------------HDSPSPILVHCGTGMARTGVFIAVDALIDQYASEGRVMVYDFVRRLRKDRPFMVRTLKQYVFIY 1401
Cdd:cd14543    191 QQQalavkamgdrwkgHPPGPPIVVHCSAGIGRTGTFCTLDICLSQLEDVGTLNVMQTVRRMRTQRAFSIQTPDQYYFCY 270
R-PTPc-D-1 cd14624
catalytic domain of receptor-type tyrosine-protein phosphatase D, repeat 1; Receptor-type ...
1149-1412 2.34e-55

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: 194.95  E-value: 2.34e-55
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2034231280 1149 LTFKDEFHALPHKSQKATDNTARRQGSHLNRFPHLLPYDHSLVQLRPDVTSRGS-YVNASFLPGYKKTPAYIAAQSPYnE 1227
Cdd:cd14624     22 LKFSQEYESIDPGQQFTWEHSNLEVNKPKNRYANVIAYDHSRVLLSAIEGIPGSdYINANYIDGYRKQNAYIATQGAL-P 100
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2034231280 1228 ETVLDFWRLIYQRSIKTVVMITNVVEDHIVKCTQYWPTQTKASFGdIFFLHLIEVNEYADYIIRTIGVKMKGDSDSKIVR 1307
Cdd:cd14624    101 ETFGDFWRMIWEQRSATVVMMTKLEERSRVKCDQYWPSRGTETYG-LIQVTLLDTVELATYCVRTFALYKNGSSEKREVR 179
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2034231280 1308 LFEFTSWPDHGVPDDPIPFLDMRYKVRRYQHDSPSPILVHCGTGMARTGVFIAVDALIDQYASEGRVMVYDFVRRLRKDR 1387
Cdd:cd14624    180 QFQFTAWPDHGVPEHPTPFLAFLRRVKTCNPPDAGPMVVHCSAGVGRTGCFIVIDAMLERIKHEKTVDIYGHVTLMRAQR 259
                          250       260
                   ....*....|....*....|....*
gi 2034231280 1388 PFMVRTLKQYVFIYEAIFEEFHAGD 1412
Cdd:cd14624    260 NYMVQTEDQYIFIHDALLEAVTCGN 284
R-PTPc-S-1 cd14625
catalytic domain of receptor-type tyrosine-protein phosphatase S, repeat 1; Receptor-type ...
1178-1406 3.46e-55

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: 194.16  E-value: 3.46e-55
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2034231280 1178 NRFPHLLPYDHSLVQLRPDVTSRGS-YVNASFLPGYKKTPAYIAAQSPYnEETVLDFWRLIYQRSIKTVVMITNVVEDHI 1256
Cdd:cd14625     51 NRYANVIAYDHSRVILQPIEGIMGSdYINANYIDGYRKQNAYIATQGPL-PETFGDFWRMVWEQRSATVVMMTKLEEKSR 129
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2034231280 1257 VKCTQYWPTQTKASFGDIFfLHLIEVNEYADYIIRTIGVKMKGDSDSKIVRLFEFTSWPDHGVPDDPIPFLDMRYKVRRY 1336
Cdd:cd14625    130 IKCDQYWPSRGTETYGMIQ-VTLLDTIELATFCVRTFSLHKNGSSEKREVRQFQFTAWPDHGVPEYPTPFLAFLRRVKTC 208
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2034231280 1337 QHDSPSPILVHCGTGMARTGVFIAVDALIDQYASEGRVMVYDFVRRLRKDRPFMVRTLKQYVFIYEAIFE 1406
Cdd:cd14625    209 NPPDAGPIVVHCSAGVGRTGCFIVIDAMLERIKHEKTVDIYGHVTLMRSQRNYMVQTEDQYSFIHDALLE 278
R-PTPc-typeIIb-1 cd14555
catalytic domain of type IIb (or R2B) subfamily receptor-type tyrosine-protein phosphatases, ...
1203-1406 1.76e-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: 1.76e-54
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2034231280 1203 YVNASFLPGYKKTPAYIAAQSPYnEETVLDFWRLIYQRSIKTVVMITNVVEDHIVKCTQYWPTQTKAsFGDIFFLhLIEV 1282
Cdd:cd14555      1 YINANYIDGYHRPNHYIATQGPM-QETVYDFWRMVWQENSASIVMVTNLVEVGRVKCSRYWPDDTEV-YGDIKVT-LVET 77
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2034231280 1283 NEYADYIIRTIGVKMKGDSDSKIVRLFEFTSWPDHGVPDDPIPFLDMRYKVRRYQHDSPSPILVHCGTGMARTGVFIAVD 1362
Cdd:cd14555     78 EPLAEYVVRTFALERRGYHEIREVRQFHFTGWPDHGVPYHATGLLGFIRRVKASNPPSAGPIVVHCSAGAGRTGCYIVID 157
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....
gi 2034231280 1363 ALIDQYASEGRVMVYDFVRRLRKDRPFMVRTLKQYVFIYEAIFE 1406
Cdd:cd14555    158 IMLDMAEREGVVDIYNCVKELRSRRVNMVQTEEQYIFIHDAILE 201
R-PTPc-G-1 cd17667
catalytic domain of receptor-type tyrosine-protein phosphatase G, repeat 1; Receptor-type ...
1176-1409 8.47e-54

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: 189.86  E-value: 8.47e-54
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2034231280 1176 HLNRFPHLLPYDHSLVQLRP---DVTSRGSYVNASFLPGYKKTPAYIAAQSPYnEETVLDFWRLIYQRSIKTVVMITNVV 1252
Cdd:cd17667     29 HKNRYINILAYDHSRVKLRPlpgKDSKHSDYINANYVDGYNKAKAYIATQGPL-KSTFEDFWRMIWEQNTGIIVMITNLV 107
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2034231280 1253 EDHIVKCTQYWPTQTKASFGDIFfLHLIEVNEYADYIIRTIGVK-----------MKGDSDSKIVRLFEFTSWPDHGVPD 1321
Cdd:cd17667    108 EKGRRKCDQYWPTENSEEYGNII-VTLKSTKIHACYTVRRFSIRntkvkkgqkgnPKGRQNERTVIQYHYTQWPDMGVPE 186
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2034231280 1322 DPIPFLDMRYKVRRYQHDSPSPILVHCGTGMARTGVFIAVDALIDQYASEGRVMVYDFVRRLRKDRPFMVRTLKQYVFIY 1401
Cdd:cd17667    187 YALPVLTFVRRSSAARTPEMGPVLVHCSAGVGRTGTYIVIDSMLQQIKDKSTVNVLGFLKHIRTQRNYLVQTEEQYIFIH 266

                   ....*...
gi 2034231280 1402 EAIFEEFH 1409
Cdd:cd17667    267 DALLEAIL 274
R-PTPc-A-E-1 cd14551
catalytic domain of receptor-type tyrosine-protein phosphatase A and E, repeat 1; ...
1203-1402 1.07e-53

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: 187.04  E-value: 1.07e-53
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2034231280 1203 YVNASFLPGYKKTPAYIAAQSPyNEETVLDFWRLIYQRSIKTVVMITNVVEDHIVKCTQYWPTQTKASFGDIFfLHLIEV 1282
Cdd:cd14551      1 YINASYIDGYQEKNKFIAAQGP-KDETVNDFWRMIWEQGSATIVMVTNLKERKEKKCSQYWPDQGCWTYGNLR-VRVEDT 78
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2034231280 1283 NEYADYIIRTIGVKMKGD-SDSKIVRL---FEFTSWPDHGVPDDPIPFLDMRYKVRRYQHDSPSPILVHCGTGMARTGVF 1358
Cdd:cd14551     79 VVLVDYTTRKFCIQKVNRgIGEKRVRLvtqFHFTSWPDFGVPFTPIGMLKFLKKVKSANPPRAGPIVVHCSAGVGRTGTF 158
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....
gi 2034231280 1359 IAVDALIDQYASEGRVMVYDFVRRLRKDRPFMVRTLKQYVFIYE 1402
Cdd:cd14551    159 IVIDAMLDMMHAEGKVDVFGFVSRIRQQRSQMVQTDMQYVFIYQ 202
R-PTPc-Q cd14616
catalytic domain of receptor-type tyrosine-protein phosphatase Q; Receptor-type ...
1178-1402 6.37e-53

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: 185.50  E-value: 6.37e-53
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2034231280 1178 NRFPHLLPYDHSLVQLRPDVTSRGS-YVNASFLPGYKKTPAYIAAQSPYnEETVLDFWRLIYQRSIKTVVMITNVVEDHI 1256
Cdd:cd14616      1 NRFPNIKPYNNNRVKLIADAGVPGSdYINASYISGYLCPNEFIATQGPL-PGTVGDFWRMVWETRAKTIVMLTQCFEKGR 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2034231280 1257 VKCTQYWPTQTK--ASFGDIFFLHLIEVNEYaDYIIRTIGVKMKGDSdsKIVRLFEFTSWPDHGVPDDPIPFLDMRYKVR 1334
Cdd:cd14616     80 IRCHQYWPEDNKpvTVFGDIVITKLMEDVQI-DWTIRDLKIERHGDY--MMVRQCNFTSWPEHGVPESSAPLIHFVKLVR 156
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2034231280 1335 RYQHDSPSPILVHCGTGMARTGVFIAVDALIDQYASEGRVMVYDFVRRLRKDRPFMVRTLKQYVFIYE 1402
Cdd:cd14616    157 ASRAHDNTPMIVHCSAGVGRTGVFIALDHLTQHINDHDFVDIYGLVAELRSERMCMVQNLAQYIFLHQ 224
R-PTP-LAR-2 cd14554
PTP-like domain of the LAR family receptor-type tyrosine-protein phosphatases, repeat 2; The ...
1176-1403 1.63e-52

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: 185.04  E-value: 1.63e-52
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2034231280 1176 HLNRFPHLLPYDHSLVQLRPDVTSRGS-YVNASFLPGYKKTPAYIAAQSPYNEeTVLDFWRLIYQRSIKTVVMITNVVED 1254
Cdd:cd14554      8 FKNRLVNILPYESTRVCLQPIRGVEGSdYINASFIDGYRQRGAYIATQGPLAE-TTEDFWRMLWEHNSTIIVMLTKLREM 86
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2034231280 1255 HIVKCTQYWPTQTKASFGdIFFLHLIEVNEYADYIIRTIGVKMKGDSDSKIVRLFEFTSWPDHGVPDDPIPFLDMRYKVR 1334
Cdd:cd14554     87 GREKCHQYWPAERSARYQ-YFVVDPMAEYNMPQYILREFKVTDARDGQSRTVRQFQFTDWPEQGVPKSGEGFIDFIGQVH 165
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2034231280 1335 RY--QHDSPSPILVHCGTGMARTGVFIAVDALIDQYASEGRVMVYDFVRRLRKDRPFMVRTLKQYVFIYEA 1403
Cdd:cd14554    166 KTkeQFGQEGPITVHCSAGVGRTGVFITLSIVLERMRYEGVVDVFQTVKLLRTQRPAMVQTEDQYQFCYRA 236
R-PTPc-V cd14618
catalytic domain of receptor-type tyrosine-protein phosphatase V; Receptor-type ...
1178-1405 2.46e-52

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: 183.99  E-value: 2.46e-52
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2034231280 1178 NRFPHLLPYDHS---LVQLRPDVTSrgSYVNASFLPGYKKTPAYIAAQSPYnEETVLDFWRLIYQRSIKTVVMITNVVED 1254
Cdd:cd14618      1 NRYPHVLPYDHSrvrLSQLGGEPHS--DYINANFIPGYTSPQEFIATQGPL-KKTIEDFWRLVWEQQVCNIIMLTVGMEN 77
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2034231280 1255 HIVKCTQYWPTQ-TKASFGDIFfLHLIEVNEYADYIIRTIGVKMKGDSDSKIVRLFEFTSWPDHGVPDDPIPFLDMRYKV 1333
Cdd:cd14618     78 GRVLCDHYWPSEsTPVSYGHIT-VHLLAQSSEDEWTRREFKLWHEDLRKERRVKHLHYTAWPDHGIPESTSSLMAFRELV 156
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2034231280 1334 RRYQHDS--PSPILVHCGTGMARTGVFIAVDALIDQYASEGRVMVYDFVRRLRKDRPFMVRTLKQYVFIYEAIF 1405
Cdd:cd14618    157 REHVQATkgKGPTLVHCSAGVGRSGTFIALDRLLRQLKEEKVVDVFNTVYILRMHRYLMIQTLSQYIFLHSCIL 230
PTPc-KIM cd14547
catalytic domain of the kinase interaction motif (KIM) family of protein-tyrosine phosphatases; ...
1178-1401 1.18e-51

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: 181.83  E-value: 1.18e-51
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2034231280 1178 NRFPHLLPYDHSLVQLRPDVT-SRGSYVNASFLPGYK-KTPAYIAAQSPYNEeTVLDFWRLIYQRSIKTVVMITNVVEDH 1255
Cdd:cd14547      1 NRYKTILPNEHSRVCLPSVDDdPLSSYINANYIRGYDgEEKAYIATQGPLPN-TVADFWRMVWQEKTPIIVMITNLTEAK 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2034231280 1256 iVKCTQYWPTQTKASFGDIFFLhLIEVNEYADYIIRTIGVKMKGDSdsKIVRLFEFTSWPDHGVPDDPIPFLDMRYKVR- 1334
Cdd:cd14547     80 -EKCAQYWPEEENETYGDFEVT-VQSVKETDGYTVRKLTLKYGGEK--RYLKHYWYTSWPDHKTPEAAQPLLSLVQEVEe 155
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2034231280 1335 -RYQHDSPSPILVHCGTGMARTGVFIAVDALIDQYASEGRVMVYDFVRRLRKDRPFMVRTLKQYVFIY 1401
Cdd:cd14547    156 aRQTEPHRGPIVVHCSAGIGRTGCFIATSIGCQQLREEGVVDVLGIVCQLRLDRGGMVQTAEQYEFVH 223
PTPc-N18 cd14603
catalytic domain of tyrosine-protein phosphatase non-receptor type 18; Tyrosine-protein ...
1178-1408 1.76e-51

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: 183.10  E-value: 1.76e-51
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2034231280 1178 NRFPHLLPYDHSLVQLRPDVTSRGS-YVNASFLPGYKKTPAYIAAQSPYNEeTVLDFWRLIYQRSIKTVVMITNVVEDHI 1256
Cdd:cd14603     34 NRYKDILPYDQTRVILSLLQEEGHSdYINANFIKGVDGSRAYIATQGPLSH-TVLDFWRMIWQYGVKVILMACREIEMGK 112
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2034231280 1257 VKCTQYWP-TQTKASFGdIFFLHLIEVNEY-ADYIIRTIGVKMKgdSDSKIVRLFEFTSWPDHGVPDDPIPFLDMRYKVR 1334
Cdd:cd14603    113 KKCERYWAqEQEPLQTG-PFTITLVKEKRLnEEVILRTLKVTFQ--KESRSVSHFQYMAWPDHGIPDSPDCMLAMIELAR 189
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2034231280 1335 RYQHDSPSPILVHCGTGMARTGVFIAVDaLIDQYASEGRVM----VYDFVRRLRKDRPFMVRTLKQYVFIYEAIFEEF 1408
Cdd:cd14603    190 RLQGSGPEPLCVHCSAGCGRTGVICTVD-YVRQLLLTQRIPpdfsIFDVVLEMRKQRPAAVQTEEQYEFLYHTVAQMF 266
PTPc cd00047
catalytic domain of protein tyrosine phosphatases; Protein tyrosine phosphatases (PTP, EC 3.1. ...
1496-1702 3.04e-51

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: 179.79  E-value: 3.04e-51
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2034231280 1496 YINAVYVDGYLRRNQFIVTQTPLHTTVLDFWRLVWDHDIRTIVMVENFKHEDDTRAE-YWPPaaSGGVMKQLEPFFLETT 1574
Cdd:cd00047      1 YINASYIDGYRGPKEYIATQGPLPNTVEDFWRMVWEQKVSVIVMLTNLVEKGREKCErYWPE--EGGKPLEYGDITVTLV 78
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2034231280 1575 ACYQQENITVRNLRLLSTQHprDPARFVRQFQFNAWAEHAmAPQSktmMLDLVDSVFDWQEEACANERPVLVHCQDGSSH 1654
Cdd:cd00047     79 SEEELSDYTIRTLELSPKGC--SESREVTHLHYTGWPDHG-VPSS---PEDLLALVRRVRKEARKPNGPIVVHCSAGVGR 152
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*...
gi 2034231280 1655 SGLFTTLAVVCERMEEDGEVDVYRTIKHIKRRRGQIIADYDQFRFCYK 1702
Cdd:cd00047    153 TGTFIAIDILLERLEAEGEVDVFEIVKALRKQRPGMVQTLEQYEFIYE 200
R-PTP-C-2 cd14558
PTP-like domain of receptor-type tyrosine-protein phosphatase C, repeat 2; Receptor-type ...
1203-1402 3.94e-50

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: 176.81  E-value: 3.94e-50
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2034231280 1203 YVNASFLPGYKKTPAYIAAQSPYnEETVLDFWRLIYQRSIKTVVMITNVVEDHIVKCTQYWPtQTKASFGDIFfLHLIEV 1282
Cdd:cd14558      1 YINASFIDGYWGPKSLIATQGPL-PDTIADFWQMIFQKKVKVIVMLTELKEGDQEQCAQYWG-DEKKTYGDIE-VELKDT 77
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2034231280 1283 NEYADYIIRTIGVKMKGDSDSKIVRLFEFTSWPDHGVPDDPIPFLDMRYKVRRYQHDSPS------PILVHCGTGMARTG 1356
Cdd:cd14558     78 EKSPTYTVRVFEITHLKRKDSRTVYQYQYHKWKGEELPEKPKDLVDMIKSIKQKLPYKNSkhgrsvPIVVHCSDGSSRTG 157
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*.
gi 2034231280 1357 VFIAVDALIDQYASEGRVMVYDFVRRLRKDRPFMVRTLKQYVFIYE 1402
Cdd:cd14558    158 IFCALWNLLESAETEKVVDVFQVVKALRKQRPGMVSTLEQYQFLYD 203
R-PTPc-U-1 cd14632
catalytic domain of receptor-type tyrosine-protein phosphatase U, repeat 1; Receptor-type ...
1203-1406 9.08e-50

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: 175.62  E-value: 9.08e-50
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2034231280 1203 YVNASFLPGYKKTPAYIAAQSPyNEETVLDFWRLIYQRSIKTVVMITNVVEDHIVKCTQYWPtQTKASFGDIFFLhLIEV 1282
Cdd:cd14632      1 YINANYIDGYHRSNHFIATQGP-KQEMVYDFWRMVWQEHCSSIVMITKLVEVGRVKCSKYWP-DDSDTYGDIKIT-LLKT 77
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2034231280 1283 NEYADYIIRTIGVKMKGDSDSKIVRLFEFTSWPDHGVPDDPIPFLDMrykVRRYQHDSP---SPILVHCGTGMARTGVFI 1359
Cdd:cd14632     78 ETLAEYSVRTFALERRGYSARHEVKQFHFTSWPEHGVPYHATGLLAF---IRRVKASTPpdaGPVVVHCSAGAGRTGCYI 154
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*..
gi 2034231280 1360 AVDALIDQYASEGRVMVYDFVRRLRKDRPFMVRTLKQYVFIYEAIFE 1406
Cdd:cd14632    155 VLDVMLDMAECEGVVDIYNCVKTLCSRRINMIQTEEQYIFIHDAILE 201
R-PTPc-K-1 cd14631
catalytic domain of receptor-type tyrosine-protein phosphatase K, repeat 1; Receptor-type ...
1203-1406 1.88e-49

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: 175.21  E-value: 1.88e-49
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2034231280 1203 YVNASFLPGYKKTPAYIAAQSPYNEeTVLDFWRLIYQRSIKTVVMITNVVEDHIVKCTQYWPTQTKAsFGDiFFLHLIEV 1282
Cdd:cd14631     15 YINANYIDGYQRPSHYIATQGPVHE-TVYDFWRMIWQEQSACIVMVTNLVEVGRVKCYKYWPDDTEV-YGD-FKVTCVEM 91
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2034231280 1283 NEYADYIIRTIGVKMKGDSDSKIVRLFEFTSWPDHGVPDDPIPFLDMRYKVRRYQHDSPSPILVHCGTGMARTGVFIAVD 1362
Cdd:cd14631     92 EPLAEYVVRTFTLERRGYNEIREVKQFHFTGWPDHGVPYHATGLLSFIRRVKLSNPPSAGPIVVHCSAGAGRTGCYIVID 171
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....
gi 2034231280 1363 ALIDQYASEGRVMVYDFVRRLRKDRPFMVRTLKQYVFIYEAIFE 1406
Cdd:cd14631    172 IMLDMAEREGVVDIYNCVKALRSRRINMVQTEEQYIFIHDAILE 215
R-PTPc-A-E-2 cd14552
catalytic domain of receptor-type tyrosine-protein phosphatase A and E, repeat 2; ...
1203-1404 2.86e-49

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: 174.38  E-value: 2.86e-49
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2034231280 1203 YVNASFLPGYKKTPAYIAAQSPYnEETVLDFWRLIYQRSIKTVVMITNVVEDHIVKCTQYWPTQTKASFGDiFFLHLIEV 1282
Cdd:cd14552      1 YINASFIDGYRQKDAYIATQGPL-DHTVEDFWRMIWEWKSCSIVMLTEIKERSQNKCAQYWPEDGSVSSGD-ITVELKDQ 78
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2034231280 1283 NEYADYIIRTIGVKMKGDSDSKIVRLFEFTSWPDHGVPDDPIPFLDMRYKVRRYQHDSPS-PILVHCGTGMARTGVFIAV 1361
Cdd:cd14552     79 TDYEDYTLRDFLVTKGKGGSTRTVRQFHFHGWPEVGIPDNGKGMIDLIAAVQKQQQQSGNhPITVHCSAGAGRTGTFCAL 158
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|...
gi 2034231280 1362 DALIDQYASEGRVMVYDFVRRLRKDRPFMVRTLKQYVFIYEAI 1404
Cdd:cd14552    159 STVLERVKAEGVLDVFQVVKSLRLQRPHMVQTLEQYEFCYKVV 201
R-PTPc-Z-1 cd17668
catalytic domain of receptor-type tyrosine-protein phosphatase Z, repeat 1; Receptor-type ...
1203-1404 4.07e-49

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: 174.01  E-value: 4.07e-49
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2034231280 1203 YVNASFLPGYKKTPAYIAAQSPYnEETVLDFWRLIYQRSIKTVVMITNVVEDHIVKCTQYWPTQTKASFGDiFFLHLIEV 1282
Cdd:cd17668      1 YINANYVDGYNKPKAYIAAQGPL-KSTAEDFWRMIWEHNVEVIVMITNLVEKGRRKCDQYWPADGSEEYGN-FLVTQKSV 78
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2034231280 1283 NEYADYIIRTIGVK--------MKGDSDSKIVRLFEFTSWPDHGVPDDPIPFLDMRYKVRRYQHDSPSPILVHCGTGMAR 1354
Cdd:cd17668     79 QVLAYYTVRNFTLRntkikkgsQKGRPSGRVVTQYHYTQWPDMGVPEYTLPVLTFVRKASYAKRHAVGPVVVHCSAGVGR 158
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|
gi 2034231280 1355 TGVFIAVDALIDQYASEGRVMVYDFVRRLRKDRPFMVRTLKQYVFIYEAI 1404
Cdd:cd17668    159 TGTYIVLDSMLQQIQHEGTVNIFGFLKHIRSQRNYLVQTEEQYVFIHDAL 208
PTPc-N22_18_12 cd14542
catalytic domain of tyrosine-protein phosphatase non-receptor type 22, type 18 and type 12; ...
1203-1401 1.14e-48

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: 172.61  E-value: 1.14e-48
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2034231280 1203 YVNASFLPGYKKTPAYIAAQSPYnEETVLDFWRLIYQRSIKTVVMITNVVEDHIVKCTQYWPTQTKAS--FGDIFFLHLI 1280
Cdd:cd14542      1 YINANFIKGVSGSKAYIATQGPL-PNTVLDFWRMIWEYNVQVIVMACREFEMGKKKCERYWPEEGEEQlqFGPFKISLEK 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2034231280 1281 EVNEYADYIIRTIgvKMKGDSDSKIVRLFEFTSWPDHGVPDDPIPFLDMRYKVRRYQHDSPSPILVHCGTGMARTGVFIA 1360
Cdd:cd14542     80 EKRVGPDFLIRTL--KVTFQKESRTVYQFHYTAWPDHGVPSSVDPILDLVRLVRDYQGSEDVPICVHCSAGCGRTGTICA 157
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*
gi 2034231280 1361 VD----ALIDQYASEgRVMVYDFVRRLRKDRPFMVRTLKQYVFIY 1401
Cdd:cd14542    158 IDyvwnLLKTGKIPE-EFSLFDLVREMRKQRPAMVQTKEQYELVY 201
R-PTP-LAR-2 cd14554
PTP-like domain of the LAR family receptor-type tyrosine-protein phosphatases, repeat 2; The ...
1460-1703 1.80e-46

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: 167.70  E-value: 1.80e-46
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2034231280 1460 AQLEINVHKNRYLDVLAADHYRPILTSQgPGAQATDYINAVYVDGYLRRNQFIVTQTPLHTTVLDFWRLVWDHDIRTIVM 1539
Cdd:cd14554      1 ANLPCNKFKNRLVNILPYESTRVCLQPI-RGVEGSDYINASFIDGYRQRGAYIATQGPLAETTEDFWRMLWEHNSTIIVM 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2034231280 1540 VENFKH-EDDTRAEYWPPAASggvmKQLEPFFLETTACYQQENITVRNLRLlsTQHPRDPARFVRQFQFNAWAEHAMaPQ 1618
Cdd:cd14554     80 LTKLREmGREKCHQYWPAERS----ARYQYFVVDPMAEYNMPQYILREFKV--TDARDGQSRTVRQFQFTDWPEQGV-PK 152
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2034231280 1619 SKTMMLDLVDSVFDWQEEAcANERPVLVHCQDGSSHSGLFTTLAVVCERMEEDGEVDVYRTIKHIKRRRGQIIADYDQFR 1698
Cdd:cd14554    153 SGEGFIDFIGQVHKTKEQF-GQEGPITVHCSAGVGRTGVFITLSIVLERMRYEGVVDVFQTVKLLRTQRPAMVQTEDQYQ 231

                   ....*
gi 2034231280 1699 FCYKA 1703
Cdd:cd14554    232 FCYRA 236
R-PTP-D-2 cd14628
PTP-like domain of receptor-type tyrosine-protein phosphatase D, repeat 2; Receptor-type ...
1178-1412 2.78e-46

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: 169.14  E-value: 2.78e-46
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2034231280 1178 NRFPHLLPYDHSLVQLRPDVTSRGS-YVNASFLPGYKKTPAYIAAQSPYnEETVLDFWRLIYQRSIKTVVMITNVVEDHI 1256
Cdd:cd14628     56 NRLVNIMPYESTRVCLQPIRGVEGSdYINASFIDGYRQQKAYIATQGPL-AETTEDFWRMLWEHNSTIVVMLTKLREMGR 134
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2034231280 1257 VKCTQYWPTQTKASFGDIFFLHLIEVNeYADYIIRTIGVKMKGDSDSKIVRLFEFTSWPDHGVPDDPIPFLDMRYKVRRY 1336
Cdd:cd14628    135 EKCHQYWPAERSARYQYFVVDPMAEYN-MPQYILREFKVTDARDGQSRTVRQFQFTDWPEQGVPKSGEGFIDFIGQVHKT 213
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2034231280 1337 --QHDSPSPILVHCGTGMARTGVFIAVDALIDQYASEGRVMVYDFVRRLRKDRPFMVRTLKQYVFIYEAIFEEFHAGD 1412
Cdd:cd14628    214 keQFGQDGPISVHCSAGVGRTGVFITLSIVLERMRYEGVVDIFQTVKMLRTQRPAMVQTEDQYQFCYRAALEYLGSFD 291
R-PTP-S-2 cd14627
PTP-like domain of receptor-type tyrosine-protein phosphatase S, repeat 2; Receptor-type ...
1178-1406 3.19e-46

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: 168.76  E-value: 3.19e-46
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2034231280 1178 NRFPHLLPYDHSLVQLRPDVTSRGS-YVNASFLPGYKKTPAYIAAQSPYnEETVLDFWRLIYQRSIKTVVMITNVVEDHI 1256
Cdd:cd14627     57 NRLVNIMPYETTRVCLQPIRGVEGSdYINASFIDGYRQQKAYIATQGPL-AETTEDFWRMLWENNSTIVVMLTKLREMGR 135
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2034231280 1257 VKCTQYWPTQTKASFGDIFFLHLIEVNeYADYIIRTIGVKMKGDSDSKIVRLFEFTSWPDHGVPDDPIPFLDMRYKVRRY 1336
Cdd:cd14627    136 EKCHQYWPAERSARYQYFVVDPMAEYN-MPQYILREFKVTDARDGQSRTVRQFQFTDWPEQGVPKSGEGFIDFIGQVHKT 214
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2034231280 1337 --QHDSPSPILVHCGTGMARTGVFIAVDALIDQYASEGRVMVYDFVRRLRKDRPFMVRTLKQYVFIYEAIFE 1406
Cdd:cd14627    215 keQFGQDGPISVHCSAGVGRTGVFITLSIVLERMRYEGVVDIFQTVKMLRTQRPAMVQTEDEYQFCYQAALE 286
R-PTP-N cd14609
PTP-like domain of receptor-type tyrosine-protein phosphatase N; Receptor-type ...
1154-1410 3.66e-46

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: 168.29  E-value: 3.66e-46
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2034231280 1154 EFHAL-PHKSQKATDNTARRQGS-HLNRFPHLLPYDHSLVQLRPDVT-SRGSYVNASFLPGYK-KTPAYIAAQSPYNEeT 1229
Cdd:cd14609     20 EWQALcAYQAEPNTCSTAQGEANvKKNRNPDFVPYDHARIKLKAESNpSRSDYINASPIIEHDpRMPAYIATQGPLSH-T 98
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2034231280 1230 VLDFWRLIYQRSIKTVVMITNVVEDHIVKCTQYWPTQTKASFgdifflHLIEVNEYA------DYIIRTIGVKMKGDSDS 1303
Cdd:cd14609     99 IADFWQMVWENGCTVIVMLTPLVEDGVKQCDRYWPDEGSSLY------HIYEVNLVSehiwceDFLVRSFYLKNVQTQET 172
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2034231280 1304 KIVRLFEFTSWPDHGVPDDPIPFLDMRYKVRRYQHDSPSPILVHCGTGMARTGVFIAVDALIDQYASEGR-VMVYDFVRR 1382
Cdd:cd14609    173 RTLTQFHFLSWPAEGIPSSTRPLLDFRRKVNKCYRGRSCPIIVHCSDGAGRTGTYILIDMVLNRMAKGVKeIDIAATLEH 252
                          250       260
                   ....*....|....*....|....*...
gi 2034231280 1383 LRKDRPFMVRTLKQYVFIYEAIFEEFHA 1410
Cdd:cd14609    253 VRDQRPGMVRTKDQFEFALTAVAEEVNA 280
PTPc-N11_6 cd14544
catalytic domain of tyrosine-protein phosphatase non-receptor type 11 and type 6; ...
1178-1404 5.82e-46

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: 166.48  E-value: 5.82e-46
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2034231280 1178 NRFPHLLPYDHSLVQLRP-DVTSRGS-YVNASFL-------PGYKKTPAYIAAQSPYnEETVLDFWRLIYQRSIKTVVMI 1248
Cdd:cd14544      5 NRYKNILPFDHTRVILKDrDPNVPGSdYINANYIrnenegpTTDENAKTYIATQGCL-ENTVSDFWSMVWQENSRVIVMT 83
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2034231280 1249 TNVVEDHIVKCTQYWPTQTKASFGDIFFLHLIEVNEYADYIIRTIGV-KMKGDSDSKIVRLFEFTSWPDHGVPDDPIPFL 1327
Cdd:cd14544     84 TKEVERGKNKCVRYWPDEGMQKQYGPYRVQNVSEHDTTDYTLRELQVsKLDQGDPIREIWHYQYLSWPDHGVPSDPGGVL 163
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2034231280 1328 DMRYKV-RRYQH-DSPSPILVHCGTGMARTGVFIAVDALIDQYASEG---RVMVYDFVRRLRKDRPFMVRTLKQYVFIYE 1402
Cdd:cd14544    164 NFLEDVnQRQESlPHAGPIVVHCSAGIGRTGTFIVIDMLLDQIKRKGldcDIDIQKTIQMVRSQRSGMVQTEAQYKFIYV 243

                   ..
gi 2034231280 1403 AI 1404
Cdd:cd14544    244 AV 245
PTPc-N3_4 cd14541
catalytic domain of tyrosine-protein phosphatase non-receptor type 21 and type 14; ...
1203-1409 1.37e-45

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: 164.04  E-value: 1.37e-45
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2034231280 1203 YVNASF----LPGYKKTPAYIAAQSPYnEETVLDFWRLIYQRSIKTVVMITNVVEDHIVKCTQYWPTQTKASFGDIFFLH 1278
Cdd:cd14541      2 YINANYvnmeIPGSGIVNRYIAAQGPL-PNTCADFWQMVWEQKSTLIVMLTTLVERGRVKCHQYWPDLGETMQFGNLQIT 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2034231280 1279 LIEVNEYADYIIRTIGVKMKGDSDSKIVRLFEFTSWPDHGVPDDPIPFLDMRYKVRRYQHDSPSPILVHCGTGMARTGVF 1358
Cdd:cd14541     81 CVSEEVTPSFAFREFILTNTNTGEERHITQMQYLAWPDHGVPDDSSDFLDFVKRVRQNRVGMVEPTVVHCSAGIGRTGVL 160
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 2034231280 1359 IAVD---ALIdqyasEGRVMVY--DFVRRLRKDRPFMVRTLKQYVFIYEAIFEEFH 1409
Cdd:cd14541    161 ITMEtamCLI-----EANEPVYplDIVRTMRDQRAMLIQTPSQYRFVCEAILRVYE 211
R-PTP-F-2 cd14629
PTP-like domain of receptor-type tyrosine-protein phosphatase F, repeat 2; Receptor-type ...
1178-1406 7.03e-45

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: 164.90  E-value: 7.03e-45
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2034231280 1178 NRFPHLLPYDHSLVQLRPDVTSRGS-YVNASFLPGYKKTPAYIAAQSPYNEETVlDFWRLIYQRSIKTVVMITNVVEDHI 1256
Cdd:cd14629     57 NRLVNIMPYELTRVCLQPIRGVEGSdYINASFIDGYRQQKAYIATQGPLAETTE-DFWRMLWEHNSTIVVMLTKLREMGR 135
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2034231280 1257 VKCTQYWPTQTKASFGDIFFLHLIEVNeYADYIIRTIGVKMKGDSDSKIVRLFEFTSWPDHGVPDDPIPFLDMRYKVRRY 1336
Cdd:cd14629    136 EKCHQYWPAERSARYQYFVVDPMAEYN-MPQYILREFKVTDARDGQSRTIRQFQFTDWPEQGVPKTGEGFIDFIGQVHKT 214
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2034231280 1337 --QHDSPSPILVHCGTGMARTGVFIAVDALIDQYASEGRVMVYDFVRRLRKDRPFMVRTLKQYVFIYEAIFE 1406
Cdd:cd14629    215 keQFGQDGPITVHCSAGVGRTGVFITLSIVLERMRYEGVVDMFQTVKTLRTQRPAMVQTEDQYQLCYRAALE 286
PTPc-N20_13 cd14538
catalytic domain of tyrosine-protein phosphatase non-receptor type 20 and type 13; ...
1203-1406 1.24e-44

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: 161.00  E-value: 1.24e-44
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2034231280 1203 YVNASF--LPGYKKTPAYIAAQSPYnEETVLDFWRLIYQRSIKTVVMITNVVEDHIVKCTQYWPTQTKAS--FGDIFFLH 1278
Cdd:cd14538      1 YINASHirIPVGGDTYHYIACQGPL-PNTTGDFWQMVWEQKSEVIAMVTQDVEGGKVKCHRYWPDSLNKPliCGGRLEVS 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2034231280 1279 LIEVNEYADYIIRTIGVKMKGDSDSKIVRLFEFTSWPDHGVPDDPIPFLD-MRYkVRRYQHDspSPILVHCGTGMARTGV 1357
Cdd:cd14538     80 LEKYQSLQDFVIRRISLRDKETGEVHHITHLNFTTWPDHGTPQSADPLLRfIRY-MRRIHNS--GPIVVHCSAGIGRTGV 156
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*....
gi 2034231280 1358 FIAVDALIDQYASEGRVMVYDFVRRLRKDRPFMVRTLKQYVFIYEAIFE 1406
Cdd:cd14538    157 LITIDVALGLIERDLPFDIQDIVKDLREQRQGMIQTKDQYIFCYKACLE 205
R-PTPc-B cd14617
catalytic domain of receptor-type tyrosine-protein phosphatase B; Receptor-type ...
1178-1402 1.47e-44

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: 161.63  E-value: 1.47e-44
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2034231280 1178 NRFPHLLPYDHSLVQLRPDVTSRGS-YVNASFLPGYKKTPAYIAAQSPYnEETVLDFWRLIYQRSIKTVVMITNVVEDHI 1256
Cdd:cd14617      1 NRYNNILPYDSTRVKLSNVDDDPCSdYINASYIPGNNFRREYIATQGPL-PGTKDDFWKMVWEQNVHNIVMVTQCVEKGR 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2034231280 1257 VKCTQYWPTQTKA-SFGDIFfLHLIEVNEYADYIIRTIGVKMKGDSDS-KIVRLFEFTSWPDHGVPDDPIPFLDMRYKVR 1334
Cdd:cd14617     80 VKCDHYWPADQDSlYYGDLI-VQMLSESVLPEWTIREFKICSEEQLDApRLVRHFHYTVWPDHGVPETTQSLIQFVRTVR 158
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2034231280 1335 RYQHDSPS--PILVHCGTGMARTGVFIAVDALIDQYASEGRVMVYDFVRRLRKDRPFMVRTLKQYVFIYE 1402
Cdd:cd14617    159 DYINRTPGsgPTVVHCSAGVGRTGTFIALDRILQQLDSKDSVDIYGAVHDLRLHRVHMVQTECQYVYLHQ 228
R-PTPc-O cd14614
catalytic domain of receptor-type tyrosine-protein phosphatase O; Receptor-type ...
1178-1404 4.98e-44

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: 160.82  E-value: 4.98e-44
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2034231280 1178 NRFPHLLPYDHSLVQLRPDVTSRGS-YVNASFLPGYKKTPAYIAAQSPYnEETVLDFWRLIYQRSIKTVVMITNVVEDHI 1256
Cdd:cd14614     16 NRYTNILPYDFSRVKLVSMHEEEGSdYINANYIPGYNSPQEYIATQGPL-PETRNDFWKMVLQQKSQIIVMLTQCNEKRR 94
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2034231280 1257 VKCTQYWP-TQTKASFGDIFFLHLIEvNEYADYIIRTIGVKMkGDsDSKIVRLFEFTSWPDHGVP-----DDPIPFLDMr 1330
Cdd:cd14614     95 VKCDHYWPfTEEPVAYGDITVEMLSE-EEQPDWAIREFRVSY-AD-EVQDVMHFNYTAWPDHGVPtanaaESILQFVQM- 170
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2034231280 1331 ykVRRYQHDSPSPILVHCGTGMARTGVFIAVDALIDQYASEGRVMVYDFVRRLRKDRPFMVRTLKQYVFIYEAI 1404
Cdd:cd14614    171 --VRQQAVKSKGPMIIHCSAGVGRTGTFIALDRLLQHIRDHEFVDILGLVSEMRSYRMSMVQTEEQYIFIHQCV 242
PTPc-N7 cd14612
catalytic domain of tyrosine-protein phosphatase non-receptor type 7; Tyrosine-protein ...
1178-1401 7.53e-44

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: 160.39  E-value: 7.53e-44
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2034231280 1178 NRFPHLLPYDHSLVQLRPDVTSR--GSYVNASFLPGYKKTP-AYIAAQSPYnEETVLDFWRLIYQRSIKTVVMITNVVED 1254
Cdd:cd14612     19 DRYKTILPNPQSRVCLRRAGSQEeeGSYINANYIRGYDGKEkAYIATQGPM-LNTVSDFWEMVWQEECPIIVMITKLKEK 97
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2034231280 1255 HiVKCTQYWPTQtKASFGDiFFLHLIEVNEYADYIIRTIGVKMKGDSDSkiVRLFEFTSWPDHGVPDDPIPFLDMRYKV- 1333
Cdd:cd14612     98 K-EKCVHYWPEK-EGTYGR-FEIRVQDMKECDGYTIRDLTIQLEEESRS--VKHYWFSSWPDHQTPESAGPLLRLVAEVe 172
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2034231280 1334 -RRYQHDSPSPILVHCGTGMARTGVFIAVDALIDQYASEGRVMVYDFVRRLRKDRPFMVRTLKQYVFIY 1401
Cdd:cd14612    173 eSRQTAASPGPIVVHCSAGIGRTGCFIATSIGCQQLKDTGKVDILGIVCQLRLDRGGMIQTSEQYQFLH 241
R-PTPc-E-2 cd14622
catalytic domain of receptor-type tyrosine-protein phosphatase E, repeat 2; Receptor-type ...
1203-1404 1.06e-43

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: 158.24  E-value: 1.06e-43
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2034231280 1203 YVNASFLPGYKKTPAYIAAQSPYnEETVLDFWRLIYQRSIKTVVMITNVVEDHIVKCTQYWPTQTKASFGDIFFLhlIEV 1282
Cdd:cd14622      2 YINASFIDGYRQKDYFIATQGPL-AHTVEDFWRMVWEWKCHTIVMLTELQEREQEKCVQYWPSEGSVTHGEITIE--IKN 78
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2034231280 1283 NEYADYI-IRTIGVKMKGDSDSKIVRLFEFTSWPDHGVPDDPIPFLDMRYKVRRYQHDSPS-PILVHCGTGMARTGVFIA 1360
Cdd:cd14622     79 DTLLETIsIRDFLVTYNQEKQTRLVRQFHFHGWPEIGIPAEGKGMIDLIAAVQKQQQQTGNhPIVVHCSAGAGRTGTFIA 158
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....
gi 2034231280 1361 VDALIDQYASEGRVMVYDFVRRLRKDRPFMVRTLKQYVFIYEAI 1404
Cdd:cd14622    159 LSNILERVKAEGLLDVFQTVKSLRLQRPHMVQTLEQYEFCYRVV 202
R-PTPc-A-2 cd14623
catalytic domain of receptor-type tyrosine-protein phosphatase A, repeat 2; Receptor-type ...
1179-1406 1.62e-43

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: 158.67  E-value: 1.62e-43
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2034231280 1179 RFPHLLPYDHSLVQLRpdvTSRGS----YVNASFLPGYKKTPAYIAAQSPYnEETVLDFWRLIYQRSIKTVVMITNVVED 1254
Cdd:cd14623      1 RVLQIIPYEFNRVIIP---VKRGEentdYVNASFIDGYRQKDSYIASQGPL-QHTIEDFWRMIWEWKSCSIVMLTELEER 76
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2034231280 1255 HIVKCTQYWPTQTKASFGDIFfLHLIEVNEYADYIIRTIGVKMKGDSDSKIVRLFEFTSWPDHGVPDDPIPFLDMRYKVR 1334
Cdd:cd14623     77 GQEKCAQYWPSDGSVSYGDIT-IELKKEEECESYTVRDLLVTNTRENKSRQIRQFHFHGWPEVGIPSDGKGMINIIAAVQ 155
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2034231280 1335 RYQHDSPS-PILVHCGTGMARTGVFIAVDALIDQYASEGRVMVYDFVRRLRKDRPFMVRTLKQYVFIYEAIFE 1406
Cdd:cd14623    156 KQQQQSGNhPITVHCSAGAGRTGTFCALSTVLERVKAEGILDVFQTVKSLRLQRPHMVQTLEQYEFCYKVVQE 228
PTPc-N22 cd14602
catalytic domain of tyrosine-protein phosphatase non-receptor type 22; Tyrosine-protein ...
1178-1408 2.07e-43

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: 158.46  E-value: 2.07e-43
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2034231280 1178 NRFPHLLPYDHSLVQLRPDVTSRGS-YVNASFLPGYKKTPAYIAAQSPYNEeTVLDFWRLIYQRSIKTVVMITNVVEDHI 1256
Cdd:cd14602      2 NRYKDILPYDHSRVELSLITSDEDSdYINANFIKGVYGPRAYIATQGPLST-TLLDFWRMIWEYSVLIIVMACMEFEMGK 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2034231280 1257 VKCTQYW--PTQTKASFGDIFFLHLIEVNEyADYIIRTIGVKMkgDSDSKIVRLFEFTSWPDHGVPDDPIPFLDMRYKVR 1334
Cdd:cd14602     81 KKCERYWaePGEMQLEFGPFSVTCEAEKRK-SDYIIRTLKVKF--NSETRTIYQFHYKNWPDHDVPSSIDPILELIWDVR 157
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2034231280 1335 RYQHDSPSPILVHCGTGMARTGVFIAVD----ALIDQYASEGrVMVYDFVRRLRKDRPFMVRTLKQYVFIYEAIFEEF 1408
Cdd:cd14602    158 CYQEDDSVPICIHCSAGCGRTGVICAIDytwmLLKDGIIPEN-FSVFSLIQEMRTQRPSLVQTKEQYELVYNAVIELF 234
R-PTP-N-N2 cd14546
PTP-like domain of receptor-type tyrosine-protein phosphatase-like N and N2; Receptor-type ...
1203-1409 1.09e-42

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: 155.68  E-value: 1.09e-42
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2034231280 1203 YVNASFLPGYK-KTPAYIAAQSPYnEETVLDFWRLIYQRSIKTVVMITNVVEDHIVKCTQYWPtQTKASFGDIFFLHLI- 1280
Cdd:cd14546      1 YINASTIYDHDpRNPAYIATQGPL-PHTIADFWQMIWEQGCVVIVMLTRLQENGVKQCARYWP-EEGSEVYHIYEVHLVs 78
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2034231280 1281 EVNEYADYIIRTIGVKMKGDSDSKIVRLFEFTSWPDHGVPDDPIPFLDMRYKVRRYQHDSPSPILVHCGTGMARTGVFIA 1360
Cdd:cd14546     79 EHIWCDDYLVRSFYLKNLQTSETRTVTQFHFLSWPDEGIPASAKPLLEFRRKVNKSYRGRSCPIVVHCSDGAGRTGTYIL 158
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|
gi 2034231280 1361 VDALIDQYASEGR-VMVYDFVRRLRKDRPFMVRTLKQYVFIYEAIFEEFH 1409
Cdd:cd14546    159 IDMVLNRMAKGAKeIDIAATLEHLRDQRPGMVKTKDQFEFVLTAVAEEVN 208
R-PTPc-E-2 cd14622
catalytic domain of receptor-type tyrosine-protein phosphatase E, repeat 2; Receptor-type ...
1495-1707 3.16e-41

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: 151.31  E-value: 3.16e-41
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2034231280 1495 DYINAVYVDGYLRRNQFIVTQTPLHTTVLDFWRLVWDHDIRTIVMVENFKH-EDDTRAEYWPpaaSGGVMKQLEpFFLET 1573
Cdd:cd14622      1 DYINASFIDGYRQKDYFIATQGPLAHTVEDFWRMVWEWKCHTIVMLTELQErEQEKCVQYWP---SEGSVTHGE-ITIEI 76
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2034231280 1574 TACYQQENITVRNLRLLSTQHPRdpARFVRQFQFNAWAEHAMAPQSKTmMLDLVDSVFDWQEEACANerPVLVHCQDGSS 1653
Cdd:cd14622     77 KNDTLLETISIRDFLVTYNQEKQ--TRLVRQFHFHGWPEIGIPAEGKG-MIDLIAAVQKQQQQTGNH--PIVVHCSAGAG 151
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....
gi 2034231280 1654 HSGLFTTLAVVCERMEEDGEVDVYRTIKHIKRRRGQIIADYDQFRFCYKAVWDF 1707
Cdd:cd14622    152 RTGTFIALSNILERVKAEGLLDVFQTVKSLRLQRPHMVQTLEQYEFCYRVVQDF 205
R-PTP-D-2 cd14628
PTP-like domain of receptor-type tyrosine-protein phosphatase D, repeat 2; Receptor-type ...
1459-1708 6.30e-41

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: 153.35  E-value: 6.30e-41
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2034231280 1459 TAQLEINVHKNRYLDVLAADHYRPILTSQgPGAQATDYINAVYVDGYLRRNQFIVTQTPLHTTVLDFWRLVWDHDIRTIV 1538
Cdd:cd14628     46 SANLPCNKFKNRLVNIMPYESTRVCLQPI-RGVEGSDYINASFIDGYRQQKAYIATQGPLAETTEDFWRMLWEHNSTIVV 124
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2034231280 1539 MVENFKHEDDTRA-EYWPPAASGgvmkQLEPFFLETTACYQQENITVRNLRLLSTQHPRdpARFVRQFQFNAWAEHAMaP 1617
Cdd:cd14628    125 MLTKLREMGREKChQYWPAERSA----RYQYFVVDPMAEYNMPQYILREFKVTDARDGQ--SRTVRQFQFTDWPEQGV-P 197
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2034231280 1618 QSKTMMLDLVDSVFDWQEEAcANERPVLVHCQDGSSHSGLFTTLAVVCERMEEDGEVDVYRTIKHIKRRRGQIIADYDQF 1697
Cdd:cd14628    198 KSGEGFIDFIGQVHKTKEQF-GQDGPISVHCSAGVGRTGVFITLSIVLERMRYEGVVDIFQTVKMLRTQRPAMVQTEDQY 276
                          250
                   ....*....|.
gi 2034231280 1698 RFCYKAVWDFM 1708
Cdd:cd14628    277 QFCYRAALEYL 287
PTPc-N11 cd14605
catalytic domain of tyrosine-protein phosphatase non-receptor type 11; Tyrosine-protein ...
1178-1404 7.09e-41

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: 152.09  E-value: 7.09e-41
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2034231280 1178 NRFPHLLPYDHSLVQLRP-DVTSRGS-YVNASF-LPGY-------KKTPAYIAAQSPYnEETVLDFWRLIYQRSIKTVVM 1247
Cdd:cd14605      6 NRYKNILPFDHTRVVLHDgDPNEPVSdYINANIiMPEFetkcnnsKPKKSYIATQGCL-QNTVNDFWRMVFQENSRVIVM 84
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2034231280 1248 ITNVVEDHIVKCTQYWPTQTKASFGDIFFLHLIEVNEYADYIIRTIGVKMKGDSDS-KIVRLFEFTSWPDHGVPDDPIPF 1326
Cdd:cd14605     85 TTKEVERGKSKCVKYWPDEYALKEYGVMRVRNVKESAAHDYILRELKLSKVGQGNTeRTVWQYHFRTWPDHGVPSDPGGV 164
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2034231280 1327 LDMRYKVRRYQHD--SPSPILVHCGTGMARTGVFIAVDALIDQYASEG---RVMVYDFVRRLRKDRPFMVRTLKQYVFIY 1401
Cdd:cd14605    165 LDFLEEVHHKQESimDAGPVVVHCSAGIGRTGTFIVIDILIDIIREKGvdcDIDVPKTIQMVRSQRSGMVQTEAQYRFIY 244

                   ...
gi 2034231280 1402 EAI 1404
Cdd:cd14605    245 MAV 247
R-PTP-N2 cd14610
PTP-like domain of receptor-type tyrosine-protein phosphatase N2; Receptor-type ...
1154-1410 8.25e-41

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: 152.90  E-value: 8.25e-41
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2034231280 1154 EFHAL-PHKSQKATDNTARR-QGSHLNRFPHLLPYDHSLVQLRPDVT-SRGSYVNASFLPGYK-KTPAYIAAQSPYnEET 1229
Cdd:cd14610     22 EWEALcAYQAEPNATNVAQReENVQKNRSLAVLPYDHSRIILKAENShSHSDYINASPIMDHDpRNPAYIATQGPL-PAT 100
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2034231280 1230 VLDFWRLIYQRSIKTVVMITNVVEDHIVKCTQYWPTQTKASFgdifflHLIEVNEYA------DYIIRTIGVKMKGDSDS 1303
Cdd:cd14610    101 VADFWQMVWESGCVVIVMLTPLAENGVKQCYHYWPDEGSNLY------HIYEVNLVSehiwceDFLVRSFYLKNLQTNET 174
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2034231280 1304 KIVRLFEFTSWPDHGVPDDPIPFLDMRYKVRRYQHDSPSPILVHCGTGMARTGVFIAVDALIDQYASEGR-VMVYDFVRR 1382
Cdd:cd14610    175 RTVTQFHFLSWNDQGVPASTRSLLDFRRKVNKCYRGRSCPIIVHCSDGAGRSGTYILIDMVLNKMAKGAKeIDIAATLEH 254
                          250       260
                   ....*....|....*....|....*...
gi 2034231280 1383 LRKDRPFMVRTLKQYVFIYEAIFEEFHA 1410
Cdd:cd14610    255 LRDQRPGMVQTKEQFEFALTAVAEEVNA 282
R-PTP-S-2 cd14627
PTP-like domain of receptor-type tyrosine-protein phosphatase S, repeat 2; Receptor-type ...
1459-1708 1.01e-40

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: 152.96  E-value: 1.01e-40
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2034231280 1459 TAQLEINVHKNRYLDVLAADHYRPILTSQgPGAQATDYINAVYVDGYLRRNQFIVTQTPLHTTVLDFWRLVWDHDIRTIV 1538
Cdd:cd14627     47 SANLPCNKFKNRLVNIMPYETTRVCLQPI-RGVEGSDYINASFIDGYRQQKAYIATQGPLAETTEDFWRMLWENNSTIVV 125
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2034231280 1539 MVENFKHEDDTRA-EYWPPAASGgvmkQLEPFFLETTACYQQENITVRNLRLLSTQHPRdpARFVRQFQFNAWAEHAMaP 1617
Cdd:cd14627    126 MLTKLREMGREKChQYWPAERSA----RYQYFVVDPMAEYNMPQYILREFKVTDARDGQ--SRTVRQFQFTDWPEQGV-P 198
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2034231280 1618 QSKTMMLDLVDSVFDWQEEAcANERPVLVHCQDGSSHSGLFTTLAVVCERMEEDGEVDVYRTIKHIKRRRGQIIADYDQF 1697
Cdd:cd14627    199 KSGEGFIDFIGQVHKTKEQF-GQDGPISVHCSAGVGRTGVFITLSIVLERMRYEGVVDIFQTVKMLRTQRPAMVQTEDEY 277
                          250
                   ....*....|.
gi 2034231280 1698 RFCYKAVWDFM 1708
Cdd:cd14627    278 QFCYQAALEYL 288
R-PTP-F-2 cd14629
PTP-like domain of receptor-type tyrosine-protein phosphatase F, repeat 2; Receptor-type ...
1428-1708 3.05e-40

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: 151.42  E-value: 3.05e-40
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2034231280 1428 QKNPRTGKTYLRDQYKLLETFTRSPRRdqCKTAQLEINVHKNRYLDVLAADHYRPILTSQgPGAQATDYINAVYVDGYLR 1507
Cdd:cd14629     18 QVPPGESVTAMELEFKLLANSKAHTSR--FISANLPCNKFKNRLVNIMPYELTRVCLQPI-RGVEGSDYINASFIDGYRQ 94
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2034231280 1508 RNQFIVTQTPLHTTVLDFWRLVWDHDIRTIVMVENFKHEDDTRA-EYWPPAASGgvmkQLEPFFLETTACYQQENITVRN 1586
Cdd:cd14629     95 QKAYIATQGPLAETTEDFWRMLWEHNSTIVVMLTKLREMGREKChQYWPAERSA----RYQYFVVDPMAEYNMPQYILRE 170
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2034231280 1587 LRLLSTQHPRdpARFVRQFQFNAWAEHAMaPQSKTMMLDLVDSVFDWQEEAcANERPVLVHCQDGSSHSGLFTTLAVVCE 1666
Cdd:cd14629    171 FKVTDARDGQ--SRTIRQFQFTDWPEQGV-PKTGEGFIDFIGQVHKTKEQF-GQDGPITVHCSAGVGRTGVFITLSIVLE 246
                          250       260       270       280
                   ....*....|....*....|....*....|....*....|..
gi 2034231280 1667 RMEEDGEVDVYRTIKHIKRRRGQIIADYDQFRFCYKAVWDFM 1708
Cdd:cd14629    247 RMRYEGVVDMFQTVKTLRTQRPAMVQTEDQYQLCYRAALEYL 288
PTPc-N9 cd14543
catalytic domain of tyrosine-protein phosphatase non-receptor type 9; Tyrosine-protein ...
1465-1702 3.60e-40

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: 150.59  E-value: 3.60e-40
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2034231280 1465 NVHKNRYLDVLAADHYRPILTSQGpGAQATDYINAVYVDGYLRRNQFIVTQTPLHTTVLDFWRLVWDHDIRTIVMVenfk 1544
Cdd:cd14543     29 NQEKNRYGDVLCLDQSRVKLPKRN-GDERTDYINANFMDGYKQKNAYIATQGPLPKTYSDFWRMVWEQKVLVIVMT---- 103
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2034231280 1545 heddTRAE---------YWPpaasggvmkqlepffLETTACYQQENITVRNLRLLSTQH-----------PRDPARFVRQ 1604
Cdd:cd14543    104 ----TRVVergrvkcgqYWP---------------LEEGSSLRYGDLTVTNLSVENKEHykkttleihntETDESRQVTH 164
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2034231280 1605 FQFNAWAEHAMaPQSKTMMLDLVDSVFDWQEEACAN----------ERPVLVHCQDGSSHSGLFTTLAVVCERMEEDGEV 1674
Cdd:cd14543    165 FQFTSWPDFGV-PSSAAALLDFLGEVRQQQALAVKAmgdrwkghppGPPIVVHCSAGIGRTGTFCTLDICLSQLEDVGTL 243
                          250       260
                   ....*....|....*....|....*...
gi 2034231280 1675 DVYRTIKHIKRRRGQIIADYDQFRFCYK 1702
Cdd:cd14543    244 NVMQTVRRMRTQRAFSIQTPDQYYFCYK 271
PTPc-N5 cd14613
catalytic domain of tyrosine-protein phosphatase non-receptor type 5; Tyrosine-protein ...
1178-1404 4.40e-40

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: 150.01  E-value: 4.40e-40
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2034231280 1178 NRFPHLLPYDHSLVQL----RPDVTSrgSYVNASFLPGY-KKTPAYIAAQSPyNEETVLDFWRLIYQRSIKTVVMITNVv 1252
Cdd:cd14613     29 NRYKTILPNPHSRVCLtspdQDDPLS--SYINANYIRGYgGEEKVYIATQGP-TVNTVGDFWRMVWQERSPIIVMITNI- 104
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2034231280 1253 EDHIVKCTQYWPTQTKASFG-DIFFLHLIEVNeyaDYIIRTIgvKMKGDSDSKIVRLFEFTSWPDHGVPDDPIPFLDMRY 1331
Cdd:cd14613    105 EEMNEKCTEYWPEEQVTYEGiEITVKQVIHAD---DYRLRLI--TLKSGGEERGLKHYWYTSWPDQKTPDNAPPLLQLVQ 179
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2034231280 1332 KV---RRYQHDSPSPILVHCGTGMARTGVFIAVDALIDQYASEGRVMVYDFVRRLRKDRPFMVRTLKQYVFIYEAI 1404
Cdd:cd14613    180 EVeeaRQQAEPNCGPVIVHCSAGIGRTGCFIATSICCKQLRNEGVVDILRTTCQLRLDRGGMIQTCEQYQFVHHVL 255
R-PTPc-LAR-1 cd14553
catalytic domain of LAR family receptor-type tyrosine-protein phosphatases, repeat 1; The LAR ...
1463-1704 4.63e-40

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: 149.08  E-value: 4.63e-40
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2034231280 1463 EINVHKNRYLDVLAADHYRPILtSQGPGAQATDYINAVYVDGYLRRNQFIVTQTPLHTTVLDFWRLVWDHDIRTIVMVEn 1542
Cdd:cd14553      1 EVNKPKNRYANVIAYDHSRVIL-QPIEGVPGSDYINANYCDGYRKQNAYIATQGPLPETFGDFWRMVWEQRSATIVMMT- 78
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2034231280 1543 fKHEDDTRA---EYWPPAAS---GGVMKQLepffLETT--ACYqqeniTVRNLRLLSTQHPRdpARFVRQFQFNAWAEHA 1614
Cdd:cd14553     79 -KLEERSRVkcdQYWPTRGTetyGLIQVTL----LDTVelATY-----TVRTFALHKNGSSE--KREVRQFQFTAWPDHG 146
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2034231280 1615 MaPQSKTMMLDLVDSVfdwqeEAC--ANERPVLVHCQDGSSHSGLFTTLAVVCERMEEDGEVDVYRTIKHIKRRRGQIIA 1692
Cdd:cd14553    147 V-PEHPTPFLAFLRRV-----KACnpPDAGPIVVHCSAGVGRTGCFIVIDSMLERIKHEKTVDIYGHVTCLRAQRNYMVQ 220
                          250
                   ....*....|..
gi 2034231280 1693 DYDQFRFCYKAV 1704
Cdd:cd14553    221 TEDQYIFIHDAL 232
R-PTPc-F-1 cd14626
catalytic domain of receptor-type tyrosine-protein phosphatase F, repeat 1; Receptor-type ...
1458-1704 5.65e-40

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: 150.19  E-value: 5.65e-40
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2034231280 1458 KTAQLEINVHKNRYLDVLAADHYRPILTSQGpGAQATDYINAVYVDGYLRRNQFIVTQTPLHTTVLDFWRLVWDHDIRTI 1537
Cdd:cd14626     34 ENSNLEVNKPKNRYANVIAYDHSRVILTSVD-GVPGSDYINANYIDGYRKQNAYIATQGPLPETLSDFWRMVWEQRTATI 112
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2034231280 1538 VMVENFKHEDDTRA-EYWPPAASGGV-MKQLEPFFLETTACYqqeniTVRNLRLLstQHPRDPARFVRQFQFNAWAEHAM 1615
Cdd:cd14626    113 VMMTRLEEKSRVKCdQYWPIRGTETYgMIQVTLLDTVELATY-----SVRTFALY--KNGSSEKREVRQFQFMAWPDHGV 185
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2034231280 1616 aPQSKTMMLDLVDSVfdwqeEAC--ANERPVLVHCQDGSSHSGLFTTLAVVCERMEEDGEVDVYRTIKHIKRRRGQIIAD 1693
Cdd:cd14626    186 -PEYPTPILAFLRRV-----KACnpPDAGPMVVHCSAGVGRTGCFIVIDAMLERMKHEKTVDIYGHVTCMRSQRNYMVQT 259
                          250
                   ....*....|.
gi 2034231280 1694 YDQFRFCYKAV 1704
Cdd:cd14626    260 EDQYIFIHEAL 270
R-PTPc-R cd14611
catalytic domain of receptor-type tyrosine-protein phosphatase R; Receptor-type ...
1178-1401 7.25e-40

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: 148.14  E-value: 7.25e-40
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2034231280 1178 NRFPHLLPYDHSLVQLRPDVT--SRGSYVNASFLPGYK-KTPAYIAAQSPYNEeTVLDFWRLIYQRSIKTVVMITNVVED 1254
Cdd:cd14611      3 NRYKTILPNPHSRVCLKPKNSndSLSTYINANYIRGYGgKEKAFIATQGPMIN-TVNDFWQMVWQEDSPVIVMITKLKEK 81
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2034231280 1255 HiVKCTQYWPtQTKASFGDIFFLhLIEVNEYADYIIRTIGVKMKGDSDSkiVRLFEFTSWPDHGVPDDPIPFLDMRYKVR 1334
Cdd:cd14611     82 N-EKCVLYWP-EKRGIYGKVEVL-VNSVKECDNYTIRNLTLKQGSQSRS--VKHYWYTSWPDHKTPDSAQPLLQLMLDVE 156
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2034231280 1335 RYQHDSPS--PILVHCGTGMARTGVFIAVDALIDQYASEGRVMVYDFVRRLRKDRPFMVRTLKQYVFIY 1401
Cdd:cd14611    157 EDRLASPGrgPVVVHCSAGIGRTGCFIATTIGCQQLKEEGVVDVLSIVCQLRVDRGGMVQTSEQYEFVH 225
R-PTPc-A-E-2 cd14552
catalytic domain of receptor-type tyrosine-protein phosphatase A and E, repeat 2; ...
1496-1704 1.33e-39

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: 146.26  E-value: 1.33e-39
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2034231280 1496 YINAVYVDGYLRRNQFIVTQTPLHTTVLDFWRLVWDHDIRTIVMVENFKH-EDDTRAEYWPPAAS---GGVMKQLEpffl 1571
Cdd:cd14552      1 YINASFIDGYRQKDAYIATQGPLDHTVEDFWRMIWEWKSCSIVMLTEIKErSQNKCAQYWPEDGSvssGDITVELK---- 76
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2034231280 1572 ETTACyqqENITVRNLRLLSTQHprDPARFVRQFQFNAWAEHAMaPQSKTMMLDLVDSVFDWQEEAcaNERPVLVHCQDG 1651
Cdd:cd14552     77 DQTDY---EDYTLRDFLVTKGKG--GSTRTVRQFHFHGWPEVGI-PDNGKGMIDLIAAVQKQQQQS--GNHPITVHCSAG 148
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|...
gi 2034231280 1652 SSHSGLFTTLAVVCERMEEDGEVDVYRTIKHIKRRRGQIIADYDQFRFCYKAV 1704
Cdd:cd14552    149 AGRTGTFCALSTVLERVKAEGVLDVFQVVKSLRLQRPHMVQTLEQYEFCYKVV 201
R-PTPc-K-2 cd14636
PTP domain of receptor-type tyrosine-protein phosphatase K, repeat 2; Receptor-type ...
1496-1701 8.75e-39

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: 144.40  E-value: 8.75e-39
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2034231280 1496 YINAVYVDGYLRRNQFIVTQTPLHTTVLDFWRLVWDHDIRTIVMVENFkheDDTRA--EYWPPAAsggvMKQLEPFFLET 1573
Cdd:cd14636      1 YINAALMDSYRQPAAFIVTQHPLPNTVKDFWRLVYDYGCTSIVMLNEV---DLAQGcpQYWPEEG----MLRYGPIQVEC 73
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2034231280 1574 TACYQQENITVRNLRLLSTQHPRDPARFVRQFQFNAWAEHAMAPQSKTMMLDLVDSVFDWQEEACANERPVLVHCQDGSS 1653
Cdd:cd14636     74 MSCSMDCDVISRIFRICNLTRPQEGYLMVQQFQYLGWASHREVPGSKRSFLKLILQVEKWQEECDEGEGRTIIHCLNGGG 153
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*...
gi 2034231280 1654 HSGLFTTLAVVCERMEEDGEVDVYRTIKHIKRRRGQIIADYDQFRFCY 1701
Cdd:cd14636    154 RSGMFCAISIVCEMIKRQNVVDVFHAVKTLRNSKPNMVETPEQYRFCY 201
PTPc-N12 cd14604
catalytic domain of tyrosine-protein phosphatase non-receptor type 12; Tyrosine-protein ...
1166-1408 9.05e-39

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: 147.39  E-value: 9.05e-39
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2034231280 1166 TDNTARRQGSHLNRFPHLLPYDHSLVQLRPDVTSRGS-YVNASFLPGYKKTPAYIAAQSPYnEETVLDFWRLIYQRSIKT 1244
Cdd:cd14604     49 TATGEKEENVKKNRYKDILPFDHSRVKLTLKTSSQDSdYINANFIKGVYGPKAYIATQGPL-ANTVIDFWRMIWEYNVAI 127
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2034231280 1245 VVMITNVVEDHIVKCTQYWPT--QTKASFGDiFFLHLIEVNEYADYIIRTIGVKMkgDSDSKIVRLFEFTSWPDHGVPDD 1322
Cdd:cd14604    128 IVMACREFEMGRKKCERYWPLygEEPMTFGP-FRISCEAEQARTDYFIRTLLLEF--QNETRRLYQFHYVNWPDHDVPSS 204
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2034231280 1323 PIPFLDMRYKVRRYQHDSPSPILVHCGTGMARTGVFIAVDALIDQYASeGRV----MVYDFVRRLRKDRPFMVRTLKQYV 1398
Cdd:cd14604    205 FDSILDMISLMRKYQEHEDVPICIHCSAGCGRTGAICAIDYTWNLLKA-GKIpeefNVFNLIQEMRTQRHSAVQTKEQYE 283
                          250
                   ....*....|
gi 2034231280 1399 FIYEAIFEEF 1408
Cdd:cd14604    284 LVHRAIAQLF 293
R3-PTPc cd14548
catalytic domain of R3 subfamily receptor-type tyrosine-protein phosphatases and similar ...
1470-1699 1.20e-38

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: 144.42  E-value: 1.20e-38
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2034231280 1470 RYLDVLAADHYRPILTSQgPGAQATDYINAVYVDGYLRRNQFIVTQTPLHTTVLDFWRLVWDHDIRTIVMVENFKHEDDT 1549
Cdd:cd14548      1 RYTNILPYDHSRVKLIPI-NEEEGSDYINANYIPGYNSPREFIATQGPLPGTKDDFWRMVWEQNSHTIVMLTQCMEKGRV 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2034231280 1550 RAE-YWP----PAASGGVMKQLepffletTACYQQENITVRNLRLLStqhpRDPARFVRQFQFNAWAEHAmAPQSKTMML 1624
Cdd:cd14548     80 KCDhYWPfdqdPVYYGDITVTM-------LSESVLPDWTIREFKLER----GDEVRSVRQFHFTAWPDHG-VPEAPDSLL 147
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2034231280 1625 DLVDSVFDWQEeacANERPVLVHCQDGSSHSGLFTTLAVVCERMEEDGEVDVYRTIKHIKRRRGQIIADYDQFRF 1699
Cdd:cd14548    148 RFVRLVRDYIK---QEKGPTIVHCSAGVGRTGTFIALDRLLQQIESEDYVDIFGIVYDLRKHRPLMVQTEAQYIF 219
PHA02738 PHA02738
hypothetical protein; Provisional
1169-1404 1.94e-38

hypothetical protein; Provisional


Pssm-ID: 222923 [Multi-domain]  Cd Length: 320  Bit Score: 146.99  E-value: 1.94e-38
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2034231280 1169 TARRQGSHLNRFPHLLPYDHSLVQLrPDVTSRGSYVNASFLPGYKKTPAYIAAQSPyNEETVLDFWRLIYQRSIKTVVMI 1248
Cdd:PHA02738    44 NAEKKNRKLNRYLDAVCFDHSRVIL-PAERNRGDYINANYVDGFEYKKKFICGQAP-TRQTCYDFYRMLWMEHVQIIVML 121
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2034231280 1249 TNVVEDHIVKCTQYWPT--QTKASFGDiFFLHLIEVNEYADYIIRTIGVKmKGDSDSKIVRLFEFTSWPDHGVPDDPIPF 1326
Cdd:PHA02738   122 CKKKENGREKCFPYWSDveQGSIRFGK-FKITTTQVETHPHYVKSTLLLT-DGTSATQTVTHFNFTAWPDHDVPKNTSEF 199
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2034231280 1327 LDMRYKVRRYQHD-------------SPSPILVHCGTGMARTGVFIAVDALIDQYASEGRVMVYDFVRRLRKDRPFMVRT 1393
Cdd:PHA02738   200 LNFVLEVRQCQKElaqeslqighnrlQPPPIVVHCNAGLGRTPCYCVVDISISRFDACATVSIPSIVSSIRNQRYYSLFI 279
                          250
                   ....*....|.
gi 2034231280 1394 LKQYVFIYEAI 1404
Cdd:PHA02738   280 PFQYFFCYRAV 290
R-PTPc-A-2 cd14623
catalytic domain of receptor-type tyrosine-protein phosphatase A, repeat 2; Receptor-type ...
1470-1704 2.26e-38

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: 144.03  E-value: 2.26e-38
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2034231280 1470 RYLDVLAADHYRPILTSQgPGAQATDYINAVYVDGYLRRNQFIVTQTPLHTTVLDFWRLVWDHDIRTIVMVENFKHEDDT 1549
Cdd:cd14623      1 RVLQIIPYEFNRVIIPVK-RGEENTDYVNASFIDGYRQKDSYIASQGPLQHTIEDFWRMIWEWKSCSIVMLTELEERGQE 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2034231280 1550 R-AEYWPpaaSGGVMKQLEpFFLETTACYQQENITVRNLrlLSTQHPRDPARFVRQFQFNAWAEHAMaPQSKTMMLDLVD 1628
Cdd:cd14623     80 KcAQYWP---SDGSVSYGD-ITIELKKEEECESYTVRDL--LVTNTRENKSRQIRQFHFHGWPEVGI-PSDGKGMINIIA 152
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2034231280 1629 SVFDWQEEAcaNERPVLVHCQDGSSHSGLFTTLAVVCERMEEDGEVDVYRTIKHIKRRRGQIIADYDQFRFCYKAV 1704
Cdd:cd14623    153 AVQKQQQQS--GNHPITVHCSAGAGRTGTFCALSTVLERVKAEGILDVFQTVKSLRLQRPHMVQTLEQYEFCYKVV 226
R-PTPc-M-2 cd14635
PTP domain of receptor-type tyrosine-protein phosphatase M, repeat 2; Receptor-type ...
1496-1702 6.12e-38

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: 141.75  E-value: 6.12e-38
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2034231280 1496 YINAVYVDGYLRRNQFIVTQTPLHTTVLDFWRLVWDHDIRTIVMVENFKhEDDTRAEYWPpaaSGGVMKQlEPFFLETTA 1575
Cdd:cd14635      1 YINAALMDSYKQPSAFIVTQHPLPNTVKDFWRLVLDYHCTSIVMLNDVD-PAQLCPQYWP---ENGVHRH-GPIQVEFVS 75
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2034231280 1576 CYQQENITVRNLRLLSTQHPRDPARFVRQFQFNAWAEHAMAPQSKTMMLDLVDSVFDWQEEACANERPVLVHCQDGSSHS 1655
Cdd:cd14635     76 ADLEEDIISRIFRIYNAARPQDGYRMVQQFQFLGWPMYRDTPVSKRSFLKLIRQVDKWQEEYNGGEGRTVVHCLNGGGRS 155
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*..
gi 2034231280 1656 GLFTTLAVVCERMEEDGEVDVYRTIKHIKRRRGQIIADYDQFRFCYK 1702
Cdd:cd14635    156 GTFCAISIVCEMLRHQRAVDVFHAVKTLRNNKPNMVDLLDQYKFCYE 202
R-PTP-C-2 cd14558
PTP-like domain of receptor-type tyrosine-protein phosphatase C, repeat 2; Receptor-type ...
1496-1701 6.46e-38

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: 141.76  E-value: 6.46e-38
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2034231280 1496 YINAVYVDGYLRRNQFIVTQTPLHTTVLDFWRLVWDHDIRTIVMVENFKHEDDTR-AEYWPPAAsggvmKQLEPFFLETT 1574
Cdd:cd14558      1 YINASFIDGYWGPKSLIATQGPLPDTIADFWQMIFQKKVKVIVMLTELKEGDQEQcAQYWGDEK-----KTYGDIEVELK 75
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2034231280 1575 ACYQQENITVRNLRLLSTQhpRDPARFVRQFQFNAWAEHAMaPQSKTMMLDLVDSVFDWQEE---ACANERPVLVHCQDG 1651
Cdd:cd14558     76 DTEKSPTYTVRVFEITHLK--RKDSRTVYQYQYHKWKGEEL-PEKPKDLVDMIKSIKQKLPYknsKHGRSVPIVVHCSDG 152
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|
gi 2034231280 1652 SSHSGLFTTLAVVCERMEEDGEVDVYRTIKHIKRRRGQIIADYDQFRFCY 1701
Cdd:cd14558    153 SSRTGIFCALWNLLESAETEKVVDVFQVVKALRKQRPGMVSTLEQYQFLY 202
R5-PTP-2 cd14550
PTP-like domain of R5 subfamily receptor-type tyrosine-protein phosphatases, repeat 2; The R5 ...
1496-1702 2.20e-37

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: 140.15  E-value: 2.20e-37
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2034231280 1496 YINAVYVDGYLRRNQFIVTQTPLHTTVLDFWRLVWDHDIRTIVMVENfKHEDDTRAEYWP----PAASGG--VMKQLEpf 1569
Cdd:cd14550      1 YINASYLQGYRRSNEFIITQHPLEHTIKDFWQMIWDHNSQTIVMLTD-NELNEDEPIYWPtkekPLECETfkVTLSGE-- 77
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2034231280 1570 flETTACYQQENITVRNLRLLSTQHPRDPArfVRQFQFNAWAeHAMAPQSKTmmLDLVDSVfdwQEEACANERPVLVHCQ 1649
Cdd:cd14550     78 --DHSCLSNEIRLIVRDFILESTQDDYVLE--VRQFQCPSWP-NPCSPIHTV--FELINTV---QEWAQQRDGPIVVHDR 147
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|...
gi 2034231280 1650 DGSSHSGLFTTLAVVCERMEEDGEVDVYRTIKHIKRRRGQIIADYDQFRFCYK 1702
Cdd:cd14550    148 YGGVQAATFCALTTLHQQLEHESSVDVYQVAKLYHLMRPGVFTSKEDYQFLYK 200
R-PTPc-T-2 cd14634
PTP domain of receptor-type tyrosine-protein phosphatase T, repeat 2; Receptor-type ...
1496-1706 2.31e-37

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: 140.16  E-value: 2.31e-37
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2034231280 1496 YINAVYVDGYLRRNQFIVTQTPLHTTVLDFWRLVWDHDIRTIVMVenfkHEDDTRA---EYWPPAASGGvmkqLEPFFLE 1572
Cdd:cd14634      1 YINAALMDSHKQPAAFIVTQHPLPNTVADFWRLVFDYNCSSVVML----NEMDAAQlcmQYWPEKTSCC----YGPIQVE 72
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2034231280 1573 TTACYQQENITVRNLRLLSTQHPRDPARFVRQFQFNAWAEHAMAPQSKTMMLDLVDSVFDWQEEACANERPVLVHCQDGS 1652
Cdd:cd14634     73 FVSADIDEDIISRIFRICNMARPQDGYRIVQHLQYIGWPAYRDTPPSKRSILKVVRRLEKWQEQYDGREGRTVVHCLNGG 152
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....
gi 2034231280 1653 SHSGLFTTLAVVCERMEEDGEVDVYRTIKHIKRRRGQIIADYDQFRFCYKAVWD 1706
Cdd:cd14634    153 GRSGTFCAICSVCEMIQQQNIIDVFHTVKTLRNNKSNMVETLEQYKFVYEVALE 206
PTPc-N1 cd14608
catalytic domain of tyrosine-protein phosphatase non-receptor type 1; Tyrosine-protein ...
1152-1415 3.88e-37

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: 142.09  E-value: 3.88e-37
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2034231280 1152 KDEFHALPHKSQKATDNTARrqgshlNRFPHLLPYDHSLVQLRPDVTSrgsYVNASFLPGYKKTPAYIAAQSPYnEETVL 1231
Cdd:cd14608      9 RHEASDFPCRVAKLPKNKNR------NRYRDVSPFDHSRIKLHQEDND---YINASLIKMEEAQRSYILTQGPL-PNTCG 78
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2034231280 1232 DFWRLIYQRSIKTVVMITNVVEDHIVKCTQYWPT--QTKASFGDI-FFLHLIEVNEYADYIIRTIGVKMKGDSDSKIVRL 1308
Cdd:cd14608     79 HFWEMVWEQKSRGVVMLNRVMEKGSLKCAQYWPQkeEKEMIFEDTnLKLTLISEDIKSYYTVRQLELENLTTQETREILH 158
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2034231280 1309 FEFTSWPDHGVPDDPIPFLDMRYKVRRYQHDSPS--PILVHCGTGMARTGVFIAVDA---LIDQYASEGRVMVYDFVRRL 1383
Cdd:cd14608    159 FHYTTWPDFGVPESPASFLNFLFKVRESGSLSPEhgPVVVHCSAGIGRSGTFCLADTcllLMDKRKDPSSVDIKKVLLEM 238
                          250       260       270
                   ....*....|....*....|....*....|....
gi 2034231280 1384 RKDRPFMVRTLKQYVFIYEAIFE--EFHAGDTMI 1415
Cdd:cd14608    239 RKFRMGLIQTADQLRFSYLAVIEgaKFIMGDSSV 272
R-PTPc-typeIIb-2 cd14556
PTP domain of type IIb (or R2B) subfamily receptor-type tyrosine-protein phosphatases, repeat ...
1203-1402 4.44e-37

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: 139.08  E-value: 4.44e-37
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2034231280 1203 YVNASFLPGYKKTPAYIAAQSPYnEETVLDFWRLIYQRSIKTVVMItNVVEDHIVKCTQYWPTQTKASFGDIFFLHLIEV 1282
Cdd:cd14556      1 YINAALLDSYKQPAAFIVTQHPL-PNTVTDFWRLVYDYGCTSIVML-NQLDPKDQSCPQYWPDEGSGTYGPIQVEFVSTT 78
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2034231280 1283 NEyADYIIRTIGVK--MKGDSDSKIVRLFEFTSWPDHG-VPDDPIPFLDMRYKVRRYQHDSPS-PILVHCGTGMARTGVF 1358
Cdd:cd14556     79 ID-EDVISRIFRLQntTRPQEGYRMVQQFQFLGWPRDRdTPPSKRALLKLLSEVEKWQEQSGEgPIVVHCLNGVGRSGVF 157
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....
gi 2034231280 1359 IAVDALIDQYASEGRVMVYDFVRRLRKDRPFMVRTLKQYVFIYE 1402
Cdd:cd14556    158 CAISSVCERIKVENVVDVFQAVKTLRNHRPNMVETEEQYKFCYD 201
PTPc-N3 cd14600
catalytic domain of tyrosine-protein phosphatase non-receptor type 3; Tyrosine-protein ...
1178-1404 9.23e-37

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: 140.76  E-value: 9.23e-37
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2034231280 1178 NRFPHLLPYDHSLVQLRPDvtsrGSYVNASF----LPGYKKTPAYIAAQSPYnEETVLDFWRLIYQRSIKTVVMITNVVE 1253
Cdd:cd14600     44 NRYKDVLPYDATRVVLQGN----EDYINASYvnmeIPSANIVNKYIATQGPL-PHTCAQFWQVVWEQKLSLIVMLTTLTE 118
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2034231280 1254 DHIVKCTQYWPtqtkasfgdifflHLIEVNEYAD-------------YIIRTIGVKMKGDSDSKIVRLFEFTSWPDHGVP 1320
Cdd:cd14600    119 RGRTKCHQYWP-------------DPPDVMEYGGfrvqchsedctiaYVFREMLLTNTQTGEERTVTHLQYVAWPDHGVP 185
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2034231280 1321 DDPIPFLDMRYKVRRYQHDSpSPILVHCGTGMARTGVFIAVDALIDQYASEGRVMVYDFVRRLRKDRPFMVRTLKQYVFI 1400
Cdd:cd14600    186 DDSSDFLEFVNYVRSKRVEN-EPVLVHCSAGIGRTGVLVTMETAMCLTERNQPVYPLDIVRKMRDQRAMMVQTSSQYKFV 264

                   ....
gi 2034231280 1401 YEAI 1404
Cdd:cd14600    265 CEAI 268
PTPc-N2 cd14607
catalytic domain of tyrosine-protein phosphatase non-receptor type 2; Tyrosine-protein ...
1149-1404 9.24e-37

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: 140.10  E-value: 9.24e-37
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2034231280 1149 LTFKDEFHALPHKSQKATDNTARrqgshlNRFPHLLPYDHSLVQLRpdvTSRGSYVNASFLPGYKKTPAYIAAQSPYnEE 1228
Cdd:cd14607      5 LEIRNESHDYPHRVAKYPENRNR------NRYRDVSPYDHSRVKLQ---NTENDYINASLVVIEEAQRSYILTQGPL-PN 74
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2034231280 1229 TVLDFWRLIYQRSIKTVVMITNVVEDHIVKCTQYWPTQTKA--SFGDI-FFLHLIEVNEYADYIIRTIGVKMKGDSDSKI 1305
Cdd:cd14607     75 TCCHFWLMVWQQKTKAVVMLNRIVEKDSVKCAQYWPTDEEEvlSFKETgFSVKLLSEDVKSYYTVHLLQLENINSGETRT 154
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2034231280 1306 VRLFEFTSWPDHGVPDDPIPFLDMRYKVRRYQHDSPS--PILVHCGTGMARTGVFIAVDA--LIDQYASEGRVMVYDFVR 1381
Cdd:cd14607    155 ISHFHYTTWPDFGVPESPASFLNFLFKVRESGSLSPEhgPAVVHCSAGIGRSGTFSLVDTclVLMEKKDPDSVDIKQVLL 234
                          250       260
                   ....*....|....*....|...
gi 2034231280 1382 RLRKDRPFMVRTLKQYVFIYEAI 1404
Cdd:cd14607    235 DMRKYRMGLIQTPDQLRFSYMAV 257
PTPc-N1_2 cd14545
catalytic domain of tyrosine-protein phosphatase non-receptor type 1 and type 2; ...
1177-1401 1.11e-36

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: 139.06  E-value: 1.11e-36
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2034231280 1177 LNRFPHLLPYDHSLVQLRpDVTSRGSYVNASFLPGYKKTPAYIAAQSPYnEETVLDFWRLIYQRSIKTVVMITNVVEDHI 1256
Cdd:cd14545      1 LNRYRDRDPYDHDRSRVK-LKQGDNDYINASLVEVEEAKRSYILTQGPL-PNTSGHFWQMVWEQNSKAVIMLNKLMEKGQ 78
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2034231280 1257 VKCTQYWPTQTKASFG---DIFFLHLIEVNEYADYIIRTIGVKMKGDSDSKIVRLFEFTSWPDHGVPDDPIPFLDMRYKV 1333
Cdd:cd14545     79 IKCAQYWPQGEGNAMIfedTGLKVTLLSEEDKSYYTVRTLELENLKTQETREVLHFHYTTWPDFGVPESPAAFLNFLQKV 158
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2034231280 1334 RRYQHDSPS--PILVHCGTGMARTGVFIAVD---ALIDQyASEGRVMVYDFVRRLRKDRPFMVRTLKQYVFIY 1401
Cdd:cd14545    159 RESGSLSSDvgPPVVHCSAGIGRSGTFCLVDtclVLIEK-GNPSSVDVKKVLLEMRKYRMGLIQTPDQLRFSY 230
PTPc-N13 cd14597
catalytic domain of tyrosine-protein phosphatase non-receptor type 13; Tyrosine-protein ...
1178-1404 1.23e-36

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: 139.19  E-value: 1.23e-36
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2034231280 1178 NRFPHLLPYDHSLVQLRPDvtsrGSYVNASF--LPGYKKTPAYIAAQSPYnEETVLDFWRLIYQRSIKTVVMITNVVEDH 1255
Cdd:cd14597      7 NRYKNILPYDTTRVPLGDE----GGYINASFikMPVGDEEFVYIACQGPL-PTTVADFWQMVWEQKSTVIAMMTQEVEGG 81
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2034231280 1256 IVKCTQYWPTQTKAS--FGDIFFLHLIEVNEYADYIIRTIGVKMKGDSDSKIVRLFEFTSWPDHGVPDDPIPFLDMrYKV 1333
Cdd:cd14597     82 KIKCQRYWPEILGKTtmVDNRLQLTLVRMQQLKNFVIRVLELEDIQTREVRHITHLNFTAWPDHDTPSQPEQLLTF-ISY 160
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2034231280 1334 RRYQHDSpSPILVHCGTGMARTGVFIAVDALIDQYASEGRVMVYDFVRRLRKDRPFMVRTLKQYVFIYEAI 1404
Cdd:cd14597    161 MRHIHKS-GPIITHCSAGIGRSGTLICIDVVLGLISKDLDFDISDIVRTMRLQRHGMVQTEDQYIFCYQVI 230
PTPc-N6 cd14606
catalytic domain of tyrosine-protein phosphatase non-receptor type 6; Tyrosine-protein ...
1161-1404 1.44e-36

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: 140.02  E-value: 1.44e-36
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2034231280 1161 KSQKATDNTARRQGSHLNRFPHLLPYDHSLVQLR-PDVTSRGS-YVNASF----LPGYKKTP-AYIAAQSPYNEeTVLDF 1233
Cdd:cd14606      5 KNLHQRLEGQRPENKSKNRYKNILPFDHSRVILQgRDSNIPGSdYINANYvknqLLGPDENAkTYIASQGCLEA-TVNDF 83
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2034231280 1234 WRLIYQRSIKTVVMITNVVEDHIVKCTQYWP-TQTKASFGDiFFLHLIEVNEYADYIIRTIGVKMKGDSDS-KIVRLFEF 1311
Cdd:cd14606     84 WQMAWQENSRVIVMTTREVEKGRNKCVPYWPeVGMQRAYGP-YSVTNCGEHDTTEYKLRTLQVSPLDNGELiREIWHYQY 162
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2034231280 1312 TSWPDHGVPDDP---IPFLDmryKVRRYQHDSPS--PILVHCGTGMARTGVFIAVDALIDQYASEG---RVMVYDFVRRL 1383
Cdd:cd14606    163 LSWPDHGVPSEPggvLSFLD---QINQRQESLPHagPIIVHCSAGIGRTGTIIVIDMLMENISTKGldcDIDIQKTIQMV 239
                          250       260
                   ....*....|....*....|.
gi 2034231280 1384 RKDRPFMVRTLKQYVFIYEAI 1404
Cdd:cd14606    240 RAQRSGMVQTEAQYKFIYVAI 260
PTPc-N4 cd14601
catalytic domain of tyrosine-protein phosphatase non-receptor type 4; Tyrosine-protein ...
1203-1406 9.25e-36

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: 135.84  E-value: 9.25e-36
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2034231280 1203 YVNASFL----PGYKKTPAYIAAQSPYnEETVLDFWRLIYQRSIKTVVMITNVVEDHIVKCTQYWPTQT-KASFGDI-FF 1276
Cdd:cd14601      2 YINANYInmeiPSSSIINRYIACQGPL-PNTCSDFWQMTWEQGSSMVVMLTTQVERGRVKCHQYWPEPSgSSSYGGFqVT 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2034231280 1277 LHLIEVNeyADYIIRTIGVKMKGDSDSKIVRLFEFTSWPDHGVPDDPIPFLDMRYKVRRYQHDSPSPILVHCGTGMARTG 1356
Cdd:cd14601     81 CHSEEGN--PAYVFREMTLTNLEKNESRPLTQIQYIAWPDHGVPDDSSDFLDFVCLVRNKRAGKDEPVVVHCSAGIGRTG 158
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|
gi 2034231280 1357 VFIAVDALIDQYASEGRVMVYDFVRRLRKDRPFMVRTLKQYVFIYEAIFE 1406
Cdd:cd14601    159 VLITMETAMCLIECNQPVYPLDIVRTMRDQRAMMIQTPSQYRFVCEAILK 208
R-PTPc-M-1 cd14633
catalytic domain of receptor-type tyrosine-protein phosphatase M, repeat 1; Receptor-type ...
1459-1704 4.79e-35

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: 135.94  E-value: 4.79e-35
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2034231280 1459 TAQLEINVHKNRYLDVLAADHYRPILTSQgPGAQATDYINAVYVDGYLRRNQFIVTQTPLHTTVLDFWRLVWDHDIRTIV 1538
Cdd:cd14633     34 SAKKDENRMKNRYGNIIAYDHSRVRLQPI-EGETSSDYINGNYIDGYHRPNHYIATQGPMQETIYDFWRMVWHENTASII 112
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2034231280 1539 MVENFKHEDDTR-AEYWPpaasggvmkqlepfflETTACYQQENITVRNLRLLSTQHPRDPA---------RFVRQFQFN 1608
Cdd:cd14633    113 MVTNLVEVGRVKcCKYWP----------------DDTEIYKDIKVTLIETELLAEYVIRTFAvekrgvheiREIRQFHFT 176
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2034231280 1609 AWAEHAMaPQSKTMMLDLVDSVfdwQEEACANERPVLVHCQDGSSHSGLFTTLAVVCERMEEDGEVDVYRTIKHIKRRRG 1688
Cdd:cd14633    177 GWPDHGV-PYHATGLLGFVRQV---KSKSPPNAGPLVVHCSAGAGRTGCFIVIDIMLDMAEREGVVDIYNCVRELRSRRV 252
                          250
                   ....*....|....*.
gi 2034231280 1689 QIIADYDQFRFCYKAV 1704
Cdd:cd14633    253 NMVQTEEQYVFIHDAI 268
R-PTPc-J cd14615
catalytic domain of receptor-type tyrosine-protein phosphatase J; Receptor-type ...
1469-1706 5.84e-35

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: 134.17  E-value: 5.84e-35
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2034231280 1469 NRYLDVLAADHYRPILTSqgPGAQATDYINAVYVDGYLRRNQFIVTQTPLHTTVLDFWRLVWDHDIRTIVMVENFKHEDD 1548
Cdd:cd14615      1 NRYNNVLPYDISRVKLSV--QSHSTDDYINANYMPGYNSKKEFIAAQGPLPNTVKDFWRMVWEKNVYAIVMLTKCVEQGR 78
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2034231280 1549 TRA-EYWPPAASggvmKQLEPFFLETTACYQQENITVRNLRLLSTQhpRDPARFVRQFQFNAWAEHAMaPQSKTMMLDLV 1627
Cdd:cd14615     79 TKCeEYWPSKQK----KDYGDITVTMTSEIVLPEWTIRDFTVKNAQ--TNESRTVRHFHFTSWPDHGV-PETTDLLINFR 151
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2034231280 1628 DSVFDWQEEaCANERPVLVHCQDGSSHSGLFTTLAVVCERMEEDGEVDVYRTIKHIKRRRGQIIADYDQFRFCYKAVWD 1706
Cdd:cd14615    152 HLVREYMKQ-NPPNSPILVHCSAGVGRTGTFIAIDRLIYQIENENVVDVYGIVYDLRMHRPLMVQTEDQYVFLNQCALD 229
PHA02742 PHA02742
protein tyrosine phosphatase; Provisional
1178-1401 6.62e-35

protein tyrosine phosphatase; Provisional


Pssm-ID: 165109 [Multi-domain]  Cd Length: 303  Bit Score: 136.29  E-value: 6.62e-35
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2034231280 1178 NRFPHLLPYDHSLVQLRpdvTSRG--SYVNASFLPGYKKTPAYIAAQSPYnEETVLDFWRLIYQRSIKTVVMITNVVEDH 1255
Cdd:PHA02742    56 CRYPDAPCFDRNRVILK---IEDGgdDFINASYVDGHNAKGRFICTQAPL-EETALDFWQAIFQDQVRVIVMITKIMEDG 131
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2034231280 1256 IVKCTQYWPT--QTKASFGDiFFLHLIEVNEYADYIIRTIGVKMKGDSDSKIVRLFEFTSWPDHGVPDDPIPFLDMRYKV 1333
Cdd:PHA02742   132 KEACYPYWMPheRGKATHGE-FKIKTKKIKSFRNYAVTNLCLTDTNTGASLDIKHFAYEDWPHGGLPRDPNKFLDFVLAV 210
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2034231280 1334 RRYQHDS-----------PSPILVHCGTGMARTGVFIAVDALIDQYASEGRVMVYDFVRRLRKDRPFMVRTLKQYVFIY 1401
Cdd:PHA02742   211 READLKAdvdikgenivkEPPILVHCSAGLDRAGAFCAIDICISKYNERAIIPLLSIVRDLRKQRHNCLSLPQQYIFCY 289
PTPc-N21_14 cd14540
catalytic domain of tyrosine-protein phosphatase non-receptor type 21 and type 14; ...
1203-1401 6.72e-35

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: 133.35  E-value: 6.72e-35
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2034231280 1203 YVNASFLPGY--KKTPAYIAAQSPYnEETVLDFWRLIYQRSIKTVVMITNVVEDHIVKCTQYWPTQT----KASFGDiFF 1276
Cdd:cd14540      1 YINASHITATvgGKQRFYIAAQGPL-QNTVGDFWQMVWEQGVYLVVMVTAEEEGGREKCFRYWPTLGgehdALTFGE-YK 78
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2034231280 1277 LHLIEVNEYADYIIRTIGVKMKGDSDSKIVRLFEFTSWPDHGVPDDPIPFLDMRYK---VRR--YQ----HDSPSPILVH 1347
Cdd:cd14540     79 VSTKFSVSSGCYTTTGLRVKHTLSGQSRTVWHLQYTDWPDHGCPEDVSGFLDFLEEinsVRRhtNQdvagHNRNPPTLVH 158
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....
gi 2034231280 1348 CGTGMARTGVFIAVDALIDQYASEGRVMVYDFVRRLRKDRPFMVRTLKQYVFIY 1401
Cdd:cd14540    159 CSAGVGRTGVVILADLMLYCLDHNEELDIPRVLALLRHQRMLLVQTLAQYKFVY 212
R-PTPc-S-1 cd14625
catalytic domain of receptor-type tyrosine-protein phosphatase S, repeat 1; Receptor-type ...
1460-1704 7.69e-35

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: 135.61  E-value: 7.69e-35
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2034231280 1460 AQLEINVHKNRYLDVLAADHYRPILTSQgPGAQATDYINAVYVDGYLRRNQFIVTQTPLHTTVLDFWRLVWDHDIRTIVM 1539
Cdd:cd14625     42 SNLEVNKPKNRYANVIAYDHSRVILQPI-EGIMGSDYINANYIDGYRKQNAYIATQGPLPETFGDFWRMVWEQRSATVVM 120
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2034231280 1540 VENFKHEDDTRA-EYWPPAASgGVMKQLEPFFLETTacyQQENITVRNLRLlsTQHPRDPARFVRQFQFNAWAEHAMaPQ 1618
Cdd:cd14625    121 MTKLEEKSRIKCdQYWPSRGT-ETYGMIQVTLLDTI---ELATFCVRTFSL--HKNGSSEKREVRQFQFTAWPDHGV-PE 193
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2034231280 1619 SKTMMLDLVDSVfdwqeEAC--ANERPVLVHCQDGSSHSGLFTTLAVVCERMEEDGEVDVYRTIKHIKRRRGQIIADYDQ 1696
Cdd:cd14625    194 YPTPFLAFLRRV-----KTCnpPDAGPIVVHCSAGVGRTGCFIVIDAMLERIKHEKTVDIYGHVTLMRSQRNYMVQTEDQ 268

                   ....*...
gi 2034231280 1697 FRFCYKAV 1704
Cdd:cd14625    269 YSFIHDAL 276
R-PTPc-V cd14618
catalytic domain of receptor-type tyrosine-protein phosphatase V; Receptor-type ...
1469-1704 3.11e-34

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: 131.99  E-value: 3.11e-34
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2034231280 1469 NRYLDVLAADHYRPILTsQGPGAQATDYINAVYVDGYLRRNQFIVTQTPLHTTVLDFWRLVWDHDIRTIVMV----ENFK 1544
Cdd:cd14618      1 NRYPHVLPYDHSRVRLS-QLGGEPHSDYINANFIPGYTSPQEFIATQGPLKKTIEDFWRLVWEQQVCNIIMLtvgmENGR 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2034231280 1545 HEDDtraEYWP----PAASGGVMKQLepffletTACYQQENITVRNLRLlstQHPRDPA-RFVRQFQFNAWAEHAMaPQS 1619
Cdd:cd14618     80 VLCD---HYWPsestPVSYGHITVHL-------LAQSSEDEWTRREFKL---WHEDLRKeRRVKHLHYTAWPDHGI-PES 145
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2034231280 1620 KTMMLDLVDSVFDwQEEACANERPVLVHCQDGSSHSGLFTTLAVVCERMEEDGEVDVYRTIKHIKRRRGQIIADYDQFRF 1699
Cdd:cd14618    146 TSSLMAFRELVRE-HVQATKGKGPTLVHCSAGVGRSGTFIALDRLLRQLKEEKVVDVFNTVYILRMHRYLMIQTLSQYIF 224

                   ....*
gi 2034231280 1700 CYKAV 1704
Cdd:cd14618    225 LHSCI 229
R-PTPc-A-1 cd14621
catalytic domain of receptor-type tyrosine-protein phosphatase A, repeat 1; Receptor-type ...
1438-1704 4.19e-34

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: 134.00  E-value: 4.19e-34
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2034231280 1438 LRDQYKLLETftrSPRRDQCKTAQLEINVHKNRYLDVLAADHYRPILTSQgPGAQATDYINAVYVDGYLRRNQFIVTQTP 1517
Cdd:cd14621     28 FREEFNALPA---CPIQATCEAASKEENKEKNRYVNILPYDHSRVHLTPV-EGVPDSDYINASFINGYQEKNKFIAAQGP 103
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2034231280 1518 LHTTVLDFWRLVWDHDIRTIVMVENFKHEDDTR-AEYWPPAAS---GGVMKQLEPFFLETtacyqqeNITVRN--LRLLS 1591
Cdd:cd14621    104 KEETVNDFWRMIWEQNTATIVMVTNLKERKECKcAQYWPDQGCwtyGNIRVSVEDVTVLV-------DYTVRKfcIQQVG 176
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2034231280 1592 TQHPRDPARFVRQFQFNAWAEHAMaPQSKTMMLDLVDSVfdwqeEACANER--PVLVHCQDGSSHSGLFTTLAVVCERME 1669
Cdd:cd14621    177 DVTNKKPQRLITQFHFTSWPDFGV-PFTPIGMLKFLKKV-----KNCNPQYagAIVVHCSAGVGRTGTFIVIDAMLDMMH 250
                          250       260       270
                   ....*....|....*....|....*....|....*
gi 2034231280 1670 EDGEVDVYRTIKHIKRRRGQIIADYDQFRFCYKAV 1704
Cdd:cd14621    251 AERKVDVYGFVSRIRAQRCQMVQTDMQYVFIYQAL 285
R5-PTPc-1 cd14549
catalytic domain of R5 subfamily receptor-type tyrosine-protein phosphatases, repeat 1; The R5 ...
1496-1701 6.60e-34

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: 130.16  E-value: 6.60e-34
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2034231280 1496 YINAVYVDGYLRRNQFIVTQTPLHTTVLDFWRLVWDHDIRTIVMVENFKhEDDTR--AEYWPpaaSGGVM--KQLEPFFL 1571
Cdd:cd14549      1 YINANYVDGYNKARAYIATQGPLPSTFDDFWRMVWEQNSAIIVMITNLV-ERGRRkcDQYWP---KEGTEtyGNIQVTLL 76
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2034231280 1572 ETT--ACYQQENITVRNLRlLSTQHPRDPARFVRQFQFNAWAEHAMaPQSKTMMLDLVdsvfdwQEEACANER---PVLV 1646
Cdd:cd14549     77 STEvlATYTVRTFSLKNLK-LKKVKGRSSERVVYQYHYTQWPDHGV-PDYTLPVLSFV------RKSSAANPPgagPIVV 148
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 2034231280 1647 HCQDGSSHSGLFTTLAVVCERMEEDGEVDVYRTIKHIKRRRGQIIADYDQFRFCY 1701
Cdd:cd14549    149 HCSAGVGRTGTYIVIDSMLQQIQDKGTVNVFGFLKHIRTQRNYLVQTEEQYIFIH 203
R-PTPc-G-1 cd17667
catalytic domain of receptor-type tyrosine-protein phosphatase G, repeat 1; Receptor-type ...
1465-1704 1.56e-33

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: 131.31  E-value: 1.56e-33
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2034231280 1465 NVHKNRYLDVLAADHYRPILTS-QGPGAQATDYINAVYVDGYLRRNQFIVTQTPLHTTVLDFWRLVWDHDIRTIVMVENF 1543
Cdd:cd17667     27 NKHKNRYINILAYDHSRVKLRPlPGKDSKHSDYINANYVDGYNKAKAYIATQGPLKSTFEDFWRMIWEQNTGIIVMITNL 106
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2034231280 1544 KHEDDTRA-EYWPPAAS---GGVMKQLEPffLETTACYQQENITVRNLRLLSTQ----HPRDPARFVRQFQFNAWAEHAM 1615
Cdd:cd17667    107 VEKGRRKCdQYWPTENSeeyGNIIVTLKS--TKIHACYTVRRFSIRNTKVKKGQkgnpKGRQNERTVIQYHYTQWPDMGV 184
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2034231280 1616 aPQSKTMMLDLVDSVFDWQeeaCANERPVLVHCQDGSSHSGLFTTLAVVCERMEEDGEVDVYRTIKHIKRRRGQIIADYD 1695
Cdd:cd17667    185 -PEYALPVLTFVRRSSAAR---TPEMGPVLVHCSAGVGRTGTYIVIDSMLQQIKDKSTVNVLGFLKHIRTQRNYLVQTEE 260

                   ....*....
gi 2034231280 1696 QFRFCYKAV 1704
Cdd:cd17667    261 QYIFIHDAL 269
R-PTP-Z-2 cd17669
catalytic domain of receptor-type tyrosine-protein phosphatase Z, repeat 2; Receptor-type ...
1496-1704 1.62e-33

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: 128.96  E-value: 1.62e-33
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2034231280 1496 YINAVYVDGYLRRNQFIVTQTPLHTTVLDFWRLVWDHDIRTIVMVENFKHEDDTRAEYWPpaasggvmKQLEPFFLET-- 1573
Cdd:cd17669      1 YINASYIMGYYQSNEFIITQHPLLHTIKDFWRMIWDHNAQLIVMLPDGQNMAEDEFVYWP--------NKDEPINCETfk 72
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2034231280 1574 --------TACYQQENITVRNLRLLSTQHprDPARFVRQFQFNAWAeHAMAPQSKTmmLDLVDSVfdwQEEACANERPVL 1645
Cdd:cd17669     73 vtliaeehKCLSNEEKLIIQDFILEATQD--DYVLEVRHFQCPKWP-NPDSPISKT--FELISII---KEEAANRDGPMI 144
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 2034231280 1646 VHCQDGSSHSGLFTTLAVVCERMEEDGEVDVYRTIKHIKRRRGQIIADYDQFRFCYKAV 1704
Cdd:cd17669    145 VHDEHGGVTAGTFCALTTLMHQLEKENSVDVYQVAKMINLMRPGVFTDIEQYQFLYKAI 203
PTPc-N20 cd14596
catalytic domain of tyrosine-protein phosphatase non-receptor type 20; Tyrosine-protein ...
1203-1406 1.99e-33

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: 128.71  E-value: 1.99e-33
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2034231280 1203 YVNASF--LPGYKKTPAYIAAQSPYnEETVLDFWRLIYQRSIKTVVMITNVVEDHIVKCTQYWPTQTKASF-GDIFFLHL 1279
Cdd:cd14596      1 YINASYitMPVGEEELFYIATQGPL-PSTIDDFWQMVWENRSDVIAMMTREVERGKVKCHRYWPETLQEPMeLENYQLRL 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2034231280 1280 IEVNEYADYIIRTIGVKMKGDSDSKIVRLFEFTSWPDHGVPDDPIPFLDMRYKVRRYQhdSPSPILVHCGTGMARTGVFI 1359
Cdd:cd14596     80 ENYQALQYFIIRIIKLVEKETGENRLIKHLQFTTWPDHGTPQSSDQLVKFICYMRKVH--NTGPIVVHCSAGIGRAGVLI 157
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*..
gi 2034231280 1360 AVDALIDQYASEGRVMVYDFVRRLRKDRPFMVRTLKQYVFIYEAIFE 1406
Cdd:cd14596    158 CVDVLLSLIEKDLSFNIKDIVREMRQQRYGMIQTKDQYLFCYKVVLE 204
PTPc-KIM cd14547
catalytic domain of the kinase interaction motif (KIM) family of protein-tyrosine phosphatases; ...
1469-1699 3.41e-33

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: 128.67  E-value: 3.41e-33
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2034231280 1469 NRYLDVLAADHYRPILTSQgPGAQATDYINAVYVDGY-LRRNQFIVTQTPLHTTVLDFWRLVWDHDIRTIVMVENFKHED 1547
Cdd:cd14547      1 NRYKTILPNEHSRVCLPSV-DDDPLSSYINANYIRGYdGEEKAYIATQGPLPNTVADFWRMVWQEKTPIIVMITNLTEAK 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2034231280 1548 DTRAEYWPPaasgGVMKQLEPFFLETTACYQQENITVRNLRLLSTQHprdpARFVRQFQFNAWAEHAmAPQSKTMMLDLV 1627
Cdd:cd14547     80 EKCAQYWPE----EENETYGDFEVTVQSVKETDGYTVRKLTLKYGGE----KRYLKHYWYTSWPDHK-TPEAAQPLLSLV 150
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2034231280 1628 DSVFDWQEEAcANERPVLVHCQDGSSHSGLFTTLAVVCERMEEDGEVDVYRTIKHIKRRRGQIIADYDQFRF 1699
Cdd:cd14547    151 QEVEEARQTE-PHRGPIVVHCSAGIGRTGCFIATSIGCQQLREEGVVDVLGIVCQLRLDRGGMVQTAEQYEF 221
PTPc-N11_6 cd14544
catalytic domain of tyrosine-protein phosphatase non-receptor type 11 and type 6; ...
1465-1704 3.42e-33

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: 129.89  E-value: 3.42e-33
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2034231280 1465 NVHKNRYLDVLAADHYRPILTSQGPGAQATDYINAVYV-----DGYLRRNQ--FIVTQTPLHTTVLDFWRLVWDHDIRTI 1537
Cdd:cd14544      1 NKGKNRYKNILPFDHTRVILKDRDPNVPGSDYINANYIrneneGPTTDENAktYIATQGCLENTVSDFWSMVWQENSRVI 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2034231280 1538 VMVEnfKHEDDTR---AEYWPPAasgGVMKQLEPFFLETTACYQQENITVRNLrLLSTQHPRDPARFVRQFQFNAWAEHA 1614
Cdd:cd14544     81 VMTT--KEVERGKnkcVRYWPDE---GMQKQYGPYRVQNVSEHDTTDYTLREL-QVSKLDQGDPIREIWHYQYLSWPDHG 154
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2034231280 1615 MaPQSKTMMLDLVDSVfDWQEEACANERPVLVHCQDGSSHSGLFTTLAVVCERMEEDG---EVDVYRTIKHIKRRRGQII 1691
Cdd:cd14544    155 V-PSDPGGVLNFLEDV-NQRQESLPHAGPIVVHCSAGIGRTGTFIVIDMLLDQIKRKGldcDIDIQKTIQMVRSQRSGMV 232
                          250
                   ....*....|...
gi 2034231280 1692 ADYDQFRFCYKAV 1704
Cdd:cd14544    233 QTEAQYKFIYVAV 245
R-PTPc-E-1 cd14620
catalytic domain of receptor-type tyrosine-protein phosphatase E, repeat 1; Receptor-type ...
1471-1704 5.69e-33

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: 128.52  E-value: 5.69e-33
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2034231280 1471 YLDVLAADHYRPILTsQGPGAQATDYINAVYVDGYLRRNQFIVTQTPLHTTVLDFWRLVWDHDIRTIVMVENFKHEDDTR 1550
Cdd:cd14620      1 YPNILPYDHSRVILS-QLDGIPCSDYINASYIDGYKEKNKFIAAQGPKQETVNDFWRMVWEQKSATIVMLTNLKERKEEK 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2034231280 1551 A-EYWPPAAS---GGVMKQLEPFFLETtacyqqeNITVRNLrLLSTQHPRD--PARFVRQFQFNAWAEHAMaPQSKTMML 1624
Cdd:cd14620     80 CyQYWPDQGCwtyGNIRVAVEDCVVLV-------DYTIRKF-CIQPQLPDGckAPRLVTQLHFTSWPDFGV-PFTPIGML 150
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2034231280 1625 DLVDSVfdwQEEACANERPVLVHCQDGSSHSGLFTTLAVVCERMEEDGEVDVYRTIKHIKRRRGQIIADYDQFRFCYKAV 1704
Cdd:cd14620    151 KFLKKV---KSVNPVHAGPIVVHCSAGVGRTGTFIVIDAMIDMMHAEQKVDVFEFVSRIRNQRPQMVQTDMQYSFIYQAL 227
R-PTPc-D-1 cd14624
catalytic domain of receptor-type tyrosine-protein phosphatase D, repeat 1; Receptor-type ...
1460-1704 8.58e-33

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: 129.47  E-value: 8.58e-33
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2034231280 1460 AQLEINVHKNRYLDVLAADHYRpILTSQGPGAQATDYINAVYVDGYLRRNQFIVTQTPLHTTVLDFWRLVWDHDIRTIVM 1539
Cdd:cd14624     42 SNLEVNKPKNRYANVIAYDHSR-VLLSAIEGIPGSDYINANYIDGYRKQNAYIATQGALPETFGDFWRMIWEQRSATVVM 120
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2034231280 1540 VENFKHEDDTRA-EYWPPAAS---GGVMKQLEPFFLETTACyqqenitVRNLRLLstQHPRDPARFVRQFQFNAWAEHAM 1615
Cdd:cd14624    121 MTKLEERSRVKCdQYWPSRGTetyGLIQVTLLDTVELATYC-------VRTFALY--KNGSSEKREVRQFQFTAWPDHGV 191
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2034231280 1616 aPQSKTMMLDLVDSVfdwqeEAC--ANERPVLVHCQDGSSHSGLFTTLAVVCERMEEDGEVDVYRTIKHIKRRRGQIIAD 1693
Cdd:cd14624    192 -PEHPTPFLAFLRRV-----KTCnpPDAGPMVVHCSAGVGRTGCFIVIDAMLERIKHEKTVDIYGHVTLMRAQRNYMVQT 265
                          250
                   ....*....|.
gi 2034231280 1694 YDQFRFCYKAV 1704
Cdd:cd14624    266 EDQYIFIHDAL 276
PHA02746 PHA02746
protein tyrosine phosphatase; Provisional
1166-1404 1.67e-32

protein tyrosine phosphatase; Provisional


Pssm-ID: 165113 [Multi-domain]  Cd Length: 323  Bit Score: 130.15  E-value: 1.67e-32
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2034231280 1166 TDNTARRQGSHLNRFPHLLPYDHSLVQL-----------------RPDVTSRGS---YVNASFLPGYKKTPAYIAAQSPy 1225
Cdd:PHA02746    43 TNHFLKKENLKKNRFHDIPCWDHSRVVInaheslkmfdvgdsdgkKIEVTSEDNaenYIHANFVDGFKEANKFICAQGP- 121
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2034231280 1226 NEETVLDFWRLIYQRSIKTVVMITNVVEDHiVKCTQYW--PTQTKASFGDiFFLHLIEVNEYADYIIRTIGVKMKGDSDS 1303
Cdd:PHA02746   122 KEDTSEDFFKLISEHESQVIVSLTDIDDDD-EKCFELWtkEEDSELAFGR-FVAKILDIIEELSFTKTRLMITDKISDTS 199
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2034231280 1304 KIVRLFEFTSWPDHGVPDDPIPFLDMRYKVRRYQHD----------SPSPILVHCGTGMARTGVFIAVDALIDQYASEGR 1373
Cdd:PHA02746   200 REIHHFWFPDWPDNGIPTGMAEFLELINKVNEEQAElikqadndpqTLGPIVVHCSAGIGRAGTFCAIDNALEQLEKEKE 279
                          250       260       270
                   ....*....|....*....|....*....|.
gi 2034231280 1374 VMVYDFVRRLRKDRPFMVRTLKQYVFIYEAI 1404
Cdd:PHA02746   280 VCLGEIVLKIRKQRHSSVFLPEQYAFCYKAL 310
PTPc-N5 cd14613
catalytic domain of tyrosine-protein phosphatase non-receptor type 5; Tyrosine-protein ...
1466-1704 6.03e-32

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: 126.52  E-value: 6.03e-32
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2034231280 1466 VHKNRYLDVLAADHYRPILTSQGPGAQATDYINAVYVDGYLRRNQ-FIVTQTPLHTTVLDFWRLVWDHDIRTIVMVENFK 1544
Cdd:cd14613     26 VRKNRYKTILPNPHSRVCLTSPDQDDPLSSYINANYIRGYGGEEKvYIATQGPTVNTVGDFWRMVWQERSPIIVMITNIE 105
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2034231280 1545 HEDDTRAEYWPpaasggvmkqlepfflETTACYQQENITVRN--------LRLLSTQHPRDpARFVRQFQFNAWAEHAmA 1616
Cdd:cd14613    106 EMNEKCTEYWP----------------EEQVTYEGIEITVKQvihaddyrLRLITLKSGGE-ERGLKHYWYTSWPDQK-T 167
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2034231280 1617 PQSKTMMLDLVDSVFDWQEEACANERPVLVHCQDGSSHSGLFTTLAVVCERMEEDGEVDVYRTIKHIKRRRGQIIADYDQ 1696
Cdd:cd14613    168 PDNAPPLLQLVQEVEEARQQAEPNCGPVIVHCSAGIGRTGCFIATSICCKQLRNEGVVDILRTTCQLRLDRGGMIQTCEQ 247

                   ....*...
gi 2034231280 1697 FRFCYKAV 1704
Cdd:cd14613    248 YQFVHHVL 255
R-PTPc-U-2 cd14637
PTP domain of receptor-type tyrosine-protein phosphatase U, repeat 2; Receptor-type ...
1496-1704 6.23e-32

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: 124.64  E-value: 6.23e-32
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2034231280 1496 YINAVYVDGYLRRNQFIVTQTPLHTTVLDFWRLVWDHDIRTIVMVENFKHEDDTRA--EYWPPAAsggvMKQLEPFFLET 1573
Cdd:cd14637      1 YINAALTDSYTRSAAFIVTLHPLQNTTTDFWRLVYDYGCTSVVMLNQLNQSNSAWPclQYWPEPG----LQQYGPMEVEF 76
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2034231280 1574 TACYQQENITVRNLRLLSTQHPRDPARFVRQFQFNAWAEHAMAPQSKTMMLDLVDSVFDWQEEaCANERPVlVHCQDGSS 1653
Cdd:cd14637     77 VSGSADEDIVTRLFRVQNITRLQEGHLMVRHFQFLRWSAYRDTPDSKKAFLHLLASVEKWQRE-SGEGRTV-VHCLNGGG 154
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|.
gi 2034231280 1654 HSGLFTTLAVVCERMEEDGEVDVYRTIKHIKRRRGQIIADYDQFRFCYKAV 1704
Cdd:cd14637    155 RSGTYCASAMILEMIRCHNIVDVFYAVKTLRNYKPNMVETLEQYRFCYEIA 205
R-PTPc-R cd14611
catalytic domain of receptor-type tyrosine-protein phosphatase R; Receptor-type ...
1468-1701 6.87e-32

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: 125.03  E-value: 6.87e-32
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2034231280 1468 KNRYLDVLAADHYRPILTSQGPGAQATDYINAVYVDGYL-RRNQFIVTQTPLHTTVLDFWRLVWDHDIRTIVMVENFKHE 1546
Cdd:cd14611      2 KNRYKTILPNPHSRVCLKPKNSNDSLSTYINANYIRGYGgKEKAFIATQGPMINTVNDFWQMVWQEDSPVIVMITKLKEK 81
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2034231280 1547 DDTRAEYWPPAAsgGVMKQLEPFFLETTACyqqENITVRNLRLLSTQHprdpARFVRQFQFNAWAEHAmAPQSKTMMLDL 1626
Cdd:cd14611     82 NEKCVLYWPEKR--GIYGKVEVLVNSVKEC---DNYTIRNLTLKQGSQ----SRSVKHYWYTSWPDHK-TPDSAQPLLQL 151
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2034231280 1627 vdsVFDWQEE--ACANERPVLVHCQDGSSHSGLFTTLAVVCERMEEDGEVDVYRTIKHIKRRRGQIIADYDQFRFCY 1701
Cdd:cd14611    152 ---MLDVEEDrlASPGRGPVVVHCSAGIGRTGCFIATTIGCQQLKEEGVVDVLSIVCQLRVDRGGMVQTSEQYEFVH 225
R-PTP-N2 cd14610
PTP-like domain of receptor-type tyrosine-protein phosphatase N2; Receptor-type ...
1435-1709 7.47e-32

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: 126.71  E-value: 7.47e-32
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2034231280 1435 KTYLRDQYKLLETFTRSPrrDQCKTAQLEINVHKNRYLDVLAADHYRPILTSQGpGAQATDYINAVYVDGYLRRN-QFIV 1513
Cdd:cd14610     16 KNRLEKEWEALCAYQAEP--NATNVAQREENVQKNRSLAVLPYDHSRIILKAEN-SHSHSDYINASPIMDHDPRNpAYIA 92
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2034231280 1514 TQTPLHTTVLDFWRLVWDHDIRTIVMVENFKhEDDTRA--EYWPPAASGGVMKQLEPFFLETTACyqqENITVRNLRLLS 1591
Cdd:cd14610     93 TQGPLPATVADFWQMVWESGCVVIVMLTPLA-ENGVKQcyHYWPDEGSNLYHIYEVNLVSEHIWC---EDFLVRSFYLKN 168
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2034231280 1592 TQhpRDPARFVRQFQFNAWAEHAMaPQSKTMMLDlvdsvFDWQEEACANER--PVLVHCQDGSSHSGLFTTLAVVCERME 1669
Cdd:cd14610    169 LQ--TNETRTVTQFHFLSWNDQGV-PASTRSLLD-----FRRKVNKCYRGRscPIIVHCSDGAGRSGTYILIDMVLNKMA 240
                          250       260       270       280
                   ....*....|....*....|....*....|....*....|.
gi 2034231280 1670 EDG-EVDVYRTIKHIKRRRGQIIADYDQFRFCYKAVWDFMN 1709
Cdd:cd14610    241 KGAkEIDIAATLEHLRDQRPGMVQTKEQFEFALTAVAEEVN 281
PTPc-N7 cd14612
catalytic domain of tyrosine-protein phosphatase non-receptor type 7; Tyrosine-protein ...
1459-1701 8.77e-32

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: 125.33  E-value: 8.77e-32
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2034231280 1459 TAQLEINVH--KNRYLDVLAADHYRPILTSQGPGAQATDYINAVYVDGYL-RRNQFIVTQTPLHTTVLDFWRLVWDHDIR 1535
Cdd:cd14612      7 PEELDIPGHasKDRYKTILPNPQSRVCLRRAGSQEEEGSYINANYIRGYDgKEKAYIATQGPMLNTVSDFWEMVWQEECP 86
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2034231280 1536 TIVMVENFKHEDDTRAEYWPPAASggvmkQLEPFFLETTACYQQENITVRNlrlLSTQHPRDpARFVRQFQFNAWAEHaM 1615
Cdd:cd14612     87 IIVMITKLKEKKEKCVHYWPEKEG-----TYGRFEIRVQDMKECDGYTIRD---LTIQLEEE-SRSVKHYWFSSWPDH-Q 156
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2034231280 1616 APQSKTMMLDLVDSVFDWQEEAcANERPVLVHCQDGSSHSGLFTTLAVVCERMEEDGEVDVYRTIKHIKRRRGQIIADYD 1695
Cdd:cd14612    157 TPESAGPLLRLVAEVEESRQTA-ASPGPIVVHCSAGIGRTGCFIATSIGCQQLKDTGKVDILGIVCQLRLDRGGMIQTSE 235

                   ....*.
gi 2034231280 1696 QFRFCY 1701
Cdd:cd14612    236 QYQFLH 241
PTP-N23 cd14539
PTP-like domain of tyrosine-protein phosphatase non-receptor type 23; Tyrosine-protein ...
1203-1402 1.02e-31

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: 124.03  E-value: 1.02e-31
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2034231280 1203 YVNASFLPGYKKT-PAYIAAQSPYnEETVLDFWRLIYQRSIKTVVMITNVVEDHIVKCTQYWPTQTKAS--FGDIfFLHL 1279
Cdd:cd14539      1 YINASLIEDLTPYcPRFIATQAPL-PGTAADFWLMVYEQQVSVIVMLVSEQENEKQKVHRYWPTERGQAlvYGAI-TVSL 78
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2034231280 1280 IEVNEYADYIIRTIGVKMKGDSDSKIVRLFEFTSWPDHGVPDDPIPFLDMRYKVRRY---QHDSPSPILVHCGTGMARTG 1356
Cdd:cd14539     79 QSVRTTPTHVERIISIQHKDTRLSRSVVHLQFTTWPELGLPDSPNPLLRFIEEVHSHylqQRSLQTPIVVHCSSGVGRTG 158
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*..
gi 2034231280 1357 VFIAVDALIDQYASE-GRVMVYDFVRRLRKDRPFMVRTLKQYVFIYE 1402
Cdd:cd14539    159 AFCLLYAAVQEIEAGnGIPDLPQLVRKMRQQRKYMLQEKEHLKFCYE 205
PTPc-N18 cd14603
catalytic domain of tyrosine-protein phosphatase non-receptor type 18; Tyrosine-protein ...
1465-1704 1.25e-31

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: 125.71  E-value: 1.25e-31
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2034231280 1465 NVHKNRYLDVLAADHYRPILTSQGPGAQaTDYINAVYVDGYLRRNQFIVTQTPLHTTVLDFWRLVWDHDIRTIVM----V 1540
Cdd:cd14603     30 NVKKNRYKDILPYDQTRVILSLLQEEGH-SDYINANFIKGVDGSRAYIATQGPLSHTVLDFWRMIWQYGVKVILMacreI 108
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2034231280 1541 ENFKHeddtRAE-YWPPAASggvMKQLEPFFLETTACYQ-QENITVRNLRLLStqhpRDPARFVRQFQFNAWAEHAMaPQ 1618
Cdd:cd14603    109 EMGKK----KCErYWAQEQE---PLQTGPFTITLVKEKRlNEEVILRTLKVTF----QKESRSVSHFQYMAWPDHGI-PD 176
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2034231280 1619 SKTMMLDLVDSVFDWQEEacaNERPVLVHCQDGSSHSGLFTTLAVV-----CERMEEDgeVDVYRTIKHIKRRRGQIIAD 1693
Cdd:cd14603    177 SPDCMLAMIELARRLQGS---GPEPLCVHCSAGCGRTGVICTVDYVrqlllTQRIPPD--FSIFDVVLEMRKQRPAAVQT 251
                          250
                   ....*....|.
gi 2034231280 1694 YDQFRFCYKAV 1704
Cdd:cd14603    252 EEQYEFLYHTV 262
R-PTP-G-2 cd17670
PTP-like domain of receptor-type tyrosine-protein phosphatase G, repeat 2; Receptor-type ...
1496-1704 3.06e-31

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: 122.48  E-value: 3.06e-31
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2034231280 1496 YINAVYVDGYLRRNQFIVTQTPLHTTVLDFWRLVWDHDIRTIVMVENFKHEDDTRAEYWPPAASGgvmKQLEPFFLETTA 1575
Cdd:cd17670      1 YINASYIMGYYRSNEFIITQHPLPHTTKDFWRMIWDHNAQIIVMLPDNQGLAEDEFVYWPSREES---MNCEAFTVTLIS 77
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2034231280 1576 ----CY-QQENITVRNLRLLSTQHprDPARFVRQFQFNAWAEhAMAPQSKTmmLDLVDSVfdwQEEACANERPVLVHCQD 1650
Cdd:cd17670     78 kdrlCLsNEEQIIIHDFILEATQD--DYVLEVRHFQCPKWPN-PDAPISST--FELINVI---KEEALTRDGPTIVHDEF 149
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....
gi 2034231280 1651 GSSHSGLFTTLAVVCERMEEDGEVDVYRTIKHIKRRRGQIIADYDQFRFCYKAV 1704
Cdd:cd17670    150 GAVSAGTLCALTTLSQQLENENAVDVYQVAKMINLMRPGVFTDIEQYQFLYKAM 203
PTPc-N14 cd14599
catalytic domain of tyrosine-protein phosphatase non-receptor type 14; Tyrosine-protein ...
1154-1406 5.25e-31

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: 124.72  E-value: 5.25e-31
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2034231280 1154 EFHALPHKSQKATDNTAR-RQGSHLNRFPHLLPYDHSLVQLRPDVTSRGSYVNASFLpgyKKTPA-----YIAAQSPYnE 1227
Cdd:cd14599     17 EYEQIPKKKADGVFTTATlPENAERNRIREVVPYEENRVELVPTKENNTGYINASHI---KVTVGgeewhYIATQGPL-P 92
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2034231280 1228 ETVLDFWRLIYQRSIKTVVMITNVVEDHIVKCTQYWPT----QTKASFGDIFFLHLIEVNE--YAdyiirTIGVKMKG-- 1299
Cdd:cd14599     93 HTCHDFWQMVWEQGVNVIAMVTAEEEGGRSKSHRYWPKlgskHSSATYGKFKVTTKFRTDSgcYA-----TTGLKVKHll 167
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2034231280 1300 DSDSKIVRLFEFTSWPDHGVPDDP---IPFLDMRYKVRRYQH-------DSPSPILVHCGTGMARTGVFIAVDALIDQYA 1369
Cdd:cd14599    168 SGQERTVWHLQYTDWPDHGCPEEVqgfLSYLEEIQSVRRHTNsmldstkNCNPPIVVHCSAGVGRTGVVILTELMIGCLE 247
                          250       260       270
                   ....*....|....*....|....*....|....*..
gi 2034231280 1370 SEGRVMVYDFVRRLRKDRPFMVRTLKQYVFIYEAIFE 1406
Cdd:cd14599    248 HNEKVEVPVMLRHLREQRMFMIQTIAQYKFVYQVLIQ 284
PTPc-N11 cd14605
catalytic domain of tyrosine-protein phosphatase non-receptor type 11; Tyrosine-protein ...
1465-1708 1.94e-30

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: 121.66  E-value: 1.94e-30
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2034231280 1465 NVHKNRYLDVLAADHYRPILTSQGPGAQATDYINAVYV--DGYLRRN------QFIVTQTPLHTTVLDFWRLVWDHDIRT 1536
Cdd:cd14605      2 NKNKNRYKNILPFDHTRVVLHDGDPNEPVSDYINANIImpEFETKCNnskpkkSYIATQGCLQNTVNDFWRMVFQENSRV 81
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2034231280 1537 IVMVENFKHEDDTR-AEYWPPAAS---GGVMKQLEpfFLETTAcyqqENITVRNLRlLSTQHPRDPARFVRQFQFNAWAE 1612
Cdd:cd14605     82 IVMTTKEVERGKSKcVKYWPDEYAlkeYGVMRVRN--VKESAA----HDYILRELK-LSKVGQGNTERTVWQYHFRTWPD 154
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2034231280 1613 HAMaPQSKTMMLDLVDSVfDWQEEACANERPVLVHCQDGSSHSGLFTTLAVVCERMEEDG---EVDVYRTIKHIKRRRGQ 1689
Cdd:cd14605    155 HGV-PSDPGGVLDFLEEV-HHKQESIMDAGPVVVHCSAGIGRTGTFIVIDILIDIIREKGvdcDIDVPKTIQMVRSQRSG 232
                          250
                   ....*....|....*....
gi 2034231280 1690 IIADYDQFRFCYKAVWDFM 1708
Cdd:cd14605    233 MVQTEAQYRFIYMAVQHYI 251
PTPc_motif smart00404
Protein tyrosine phosphatase, catalytic domain motif;
1305-1406 2.82e-30

Protein tyrosine phosphatase, catalytic domain motif;


Pssm-ID: 214649 [Multi-domain]  Cd Length: 105  Bit Score: 115.92  E-value: 2.82e-30
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2034231280  1305 IVRLFEFTSWPDHGVPDDPIPFLDMRYKVR--RYQHDSPSPILVHCGTGMARTGVFIAVDALIDQ-YASEGRVMVYDFVR 1381
Cdd:smart00404    1 TVKHYHYTGWPDHGVPESPDSILELLRAVKknLNQSESSGPVVVHCSAGVGRTGTFVAIDILLQQlEAEAGEVDIFDTVK 80
                            90       100
                    ....*....|....*....|....*
gi 2034231280  1382 RLRKDRPFMVRTLKQYVFIYEAIFE 1406
Cdd:smart00404   81 ELRSQRPGMVQTEEQYLFLYRALLE 105
PTPc_DSPc smart00012
Protein tyrosine phosphatase, catalytic domain, undefined specificity; Protein tyrosine ...
1305-1406 2.82e-30

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: 115.92  E-value: 2.82e-30
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2034231280  1305 IVRLFEFTSWPDHGVPDDPIPFLDMRYKVR--RYQHDSPSPILVHCGTGMARTGVFIAVDALIDQ-YASEGRVMVYDFVR 1381
Cdd:smart00012    1 TVKHYHYTGWPDHGVPESPDSILELLRAVKknLNQSESSGPVVVHCSAGVGRTGTFVAIDILLQQlEAEAGEVDIFDTVK 80
                            90       100
                    ....*....|....*....|....*
gi 2034231280  1382 RLRKDRPFMVRTLKQYVFIYEAIFE 1406
Cdd:smart00012   81 ELRSQRPGMVQTEEQYLFLYRALLE 105
R-PTPc-H cd14619
catalytic domain of receptor-type tyrosine-protein phosphatase H; Receptor-type ...
1469-1708 3.91e-30

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: 120.38  E-value: 3.91e-30
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2034231280 1469 NRYLDVLAADHYRPILTSQgPGAQATDYINAVYVDGYLRRNQFIVTQTPLHTTVLDFWRLVWDHDIRTIVMVENFKHEDD 1548
Cdd:cd14619      1 NRFRNVLPYDWSRVPLKPI-HEEPGSDYINANYMPGYWSSQEFIATQGPLPQTVGDFWRMIWEQQSSTIVMLTNCMEAGR 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2034231280 1549 TRAE-YWP----PAASGGVMKQLepffletTACYQQENITVRNLRLLSTQHPRDpaRFVRQFQFNAWAEHAMaPQSKTMM 1623
Cdd:cd14619     80 VKCEhYWPldytPCTYGHLRVTV-------VSEEVMENWTVREFLLKQVEEQKT--LSVRHFHFTAWPDHGV-PSSTDTL 149
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2034231280 1624 LDLVDSVFDWQEEACANErPVLVHCQDGSSHSGLFTTLAVVCERMEEDGEVDVYRTIKHIKRRRGQIIADYDQFRFCYKA 1703
Cdd:cd14619    150 LAFRRLLRQWLDQTMSGG-PTVVHCSAGVGRTGTLIALDVLLQQLQSEGLLGPFSFVQKMRENRPLMVQTESQYVFLHQC 228

                   ....*
gi 2034231280 1704 VWDFM 1708
Cdd:cd14619    229 ILDFL 233
R-PTP-N cd14609
PTP-like domain of receptor-type tyrosine-protein phosphatase N; Receptor-type ...
1435-1709 5.22e-30

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: 121.30  E-value: 5.22e-30
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2034231280 1435 KTYLRDQYKLLETFTRSPrrDQCKTAQLEINVHKNRYLDVLAADHYRPILTSQGPGAQaTDYINAV-YVDGYLRRNQFIV 1513
Cdd:cd14609     14 RDRLAKEWQALCAYQAEP--NTCSTAQGEANVKKNRNPDFVPYDHARIKLKAESNPSR-SDYINASpIIEHDPRMPAYIA 90
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2034231280 1514 TQTPLHTTVLDFWRLVWDHDIRTIVMVENFKHEDDTRAE-YWPPAASGGVMKQLEPFFLETTACyqqENITVRNLRLLST 1592
Cdd:cd14609     91 TQGPLSHTIADFWQMVWENGCTVIVMLTPLVEDGVKQCDrYWPDEGSSLYHIYEVNLVSEHIWC---EDFLVRSFYLKNV 167
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2034231280 1593 QhpRDPARFVRQFQFNAWAEHAMaPQSKTMMLDlvdsvFDWQEEACANER--PVLVHCQDGSSHSGLFTTLAVVCERMEE 1670
Cdd:cd14609    168 Q--TQETRTLTQFHFLSWPAEGI-PSSTRPLLD-----FRRKVNKCYRGRscPIIVHCSDGAGRTGTYILIDMVLNRMAK 239
                          250       260       270       280
                   ....*....|....*....|....*....|....*....|
gi 2034231280 1671 D-GEVDVYRTIKHIKRRRGQIIADYDQFRFCYKAVWDFMN 1709
Cdd:cd14609    240 GvKEIDIAATLEHVRDQRPGMVRTKDQFEFALTAVAEEVN 279
R-PTPc-U-1 cd14632
catalytic domain of receptor-type tyrosine-protein phosphatase U, repeat 1; Receptor-type ...
1496-1704 6.05e-30

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: 119.00  E-value: 6.05e-30
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2034231280 1496 YINAVYVDGYLRRNQFIVTQTPLHTTVLDFWRLVWDHDIRTIVMVENFKHEDDTR-AEYWPPAASGGVMKQLEPFFLETT 1574
Cdd:cd14632      1 YINANYIDGYHRSNHFIATQGPKQEMVYDFWRMVWQEHCSSIVMITKLVEVGRVKcSKYWPDDSDTYGDIKITLLKTETL 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2034231280 1575 ACYQQENITVRNlRLLSTQHPrdparfVRQFQFNAWAEHAMaPQSKTMMLDLVDSVfdwQEEACANERPVLVHCQDGSSH 1654
Cdd:cd14632     81 AEYSVRTFALER-RGYSARHE------VKQFHFTSWPEHGV-PYHATGLLAFIRRV---KASTPPDAGPVVVHCSAGAGR 149
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|
gi 2034231280 1655 SGLFTTLAVVCERMEEDGEVDVYRTIKHIKRRRGQIIADYDQFRFCYKAV 1704
Cdd:cd14632    150 TGCYIVLDVMLDMAECEGVVDIYNCVKTLCSRRINMIQTEEQYIFIHDAI 199
R-PTPc-T-1 cd14630
catalytic domain of receptor-type tyrosine-protein phosphatase T, repeat 1; Receptor-type ...
1465-1704 1.22e-29

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: 118.97  E-value: 1.22e-29
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2034231280 1465 NVHKNRYLDVLAADHYRpILTSQGPGAQATDYINAVYVDGYLRRNQFIVTQTPLHTTVLDFWRLVWDHDIRTIVMVENFK 1544
Cdd:cd14630      3 NRNKNRYGNIISYDHSR-VRLQLLDGDPHSDYINANYIDGYHRPRHYIATQGPMQETVKDFWRMIWQENSASVVMVTNLV 81
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2034231280 1545 HEDDTR-AEYWPPAASggVMKQLEPFFLETtacyqqENITVRNLRLLSTQHP-RDPARFVRQFQFNAWAEHAMaPQSKTM 1622
Cdd:cd14630     82 EVGRVKcVRYWPDDTE--VYGDIKVTLIET------EPLAEYVIRTFTVQKKgYHEIREIRQFHFTSWPDHGV-PCYATG 152
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2034231280 1623 MLDLVDSV-FDWQEEAcaneRPVLVHCQDGSSHSGLFTTLAVVCERMEEDGEVDVYRTIKHIKRRRGQIIADYDQFRFCY 1701
Cdd:cd14630    153 LLGFVRQVkFLNPPDA----GPIVVHCSAGAGRTGCFIAIDIMLDMAENEGVVDIFNCVRELRAQRVNMVQTEEQYVFVH 228

                   ...
gi 2034231280 1702 KAV 1704
Cdd:cd14630    229 DAI 231
PHA02747 PHA02747
protein tyrosine phosphatase; Provisional
1152-1400 1.37e-29

protein tyrosine phosphatase; Provisional


Pssm-ID: 165114 [Multi-domain]  Cd Length: 312  Bit Score: 121.26  E-value: 1.37e-29
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2034231280 1152 KDEFHALPHKS-QKATDNTARRQGSHLNRFPHLLPYDHSLVQLRPDVTSRGSYVNASFLPGYKKTPAYIAAQSPYnEETV 1230
Cdd:PHA02747    28 RDEHHQIILKPfDGLIANFEKPENQPKNRYWDIPCWDHNRVILDSGGGSTSDYIHANWIDGFEDDKKFIATQGPF-AETC 106
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2034231280 1231 LDFWRLIYQRSIKTVVMIT-----NVVEdhivKCTQYW-PTQTKASFGDIFFLHLIEVNEYADYIIRTIGVKMKGDSDSK 1304
Cdd:PHA02747   107 ADFWKAVWQEHCSIIVMLTptkgtNGEE----KCYQYWcLNEDGNIDMEDFRIETLKTSVRAKYILTLIEITDKILKDSR 182
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2034231280 1305 IVRLFEFTSWPDHGVPDDP---IPFLDMRYKVRR-------YQHDSPSPILVHCGTGMARTGVFIAVDALIDQYASEGRV 1374
Cdd:PHA02747   183 KISHFQCSEWFEDETPSDHpdfIKFIKIIDINRKksgklfnPKDALLCPIVVHCSDGVGKTGIFCAVDICLNQLVKRKAI 262
                          250       260
                   ....*....|....*....|....*.
gi 2034231280 1375 MVYDFVRRLRKDRPFMVRTLKQYVFI 1400
Cdd:PHA02747   263 CLAKTAEKIREQRHAGIMNFDDYLFI 288
PTPc_plant_PTP1 cd17658
protein tyrosine phosphatase 1 from Arabidopsis thaliana and similar plant PTPs; Arabidopsis ...
1203-1402 1.41e-29

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: 117.57  E-value: 1.41e-29
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2034231280 1203 YVNASFL--PGYKKTPAYIAAQSPYnEETVLDFWRLIYQRSIKTVVMITNVVEDH-IVKCTQYWPTqtkasfgdifflhl 1279
Cdd:cd17658      1 YINASLVetPASESLPKFIATQGPL-PHTFEDFWEMVIQQRCPVIIMLTRLVDNYsTAKCADYFPA-------------- 65
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2034231280 1280 iEVNEYADY-IIRTIGVKMKGDSDSKIVRLFE-----------------FTSWPDHGVPDDPIPfldMRYKVRRYQHDSP 1341
Cdd:cd17658     66 -EENESREFgRISVTNKKLKHSQHSITLRVLEvqyieseepplsvlhiqYPEWPDHGVPKDTRS---VRELLKRLYGIPP 141
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2034231280 1342 S--PILVHCGTGMARTGVFIAVDALIdQYASEGRVMVYDF---VRRLRKDRPFMVRTLKQYVFIYE 1402
Cdd:cd17658    142 SagPIVVHCSAGIGRTGAYCTIHNTI-RRILEGDMSAVDLsktVRKFRSQRIGMVQTQDQYIFCYA 206
R-PTPc-A-E-1 cd14551
catalytic domain of receptor-type tyrosine-protein phosphatase A and E, repeat 1; ...
1496-1702 7.01e-29

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: 115.78  E-value: 7.01e-29
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2034231280 1496 YINAVYVDGYLRRNQFIVTQTPLHTTVLDFWRLVWDHDIRTIVMVENFKHEDDTR-AEYWPPAA---SGGVMKQLEPffl 1571
Cdd:cd14551      1 YINASYIDGYQEKNKFIAAQGPKDETVNDFWRMIWEQGSATIVMVTNLKERKEKKcSQYWPDQGcwtYGNLRVRVED--- 77
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2034231280 1572 ettaCYQQENITVRNLrLLSTQHP---RDPARFVRQFQFNAWAEHAMaPQSKTMMLDLVDSVfdwqeEAC--ANERPVLV 1646
Cdd:cd14551     78 ----TVVLVDYTTRKF-CIQKVNRgigEKRVRLVTQFHFTSWPDFGV-PFTPIGMLKFLKKV-----KSAnpPRAGPIVV 146
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 2034231280 1647 HCQDGSSHSGLFTTLAVVCERMEEDGEVDVYRTIKHIKRRRGQIIADYDQFRFCYK 1702
Cdd:cd14551    147 HCSAGVGRTGTFIVIDAMLDMMHAEGKVDVFGFVSRIRQQRSQMVQTDMQYVFIYQ 202
PTPc-N12 cd14604
catalytic domain of tyrosine-protein phosphatase non-receptor type 12; Tyrosine-protein ...
1421-1704 7.05e-29

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: 118.50  E-value: 7.05e-29
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2034231280 1421 ERYHNWTQKNPRTGKTYLRDQYKL--LETFTRSPRRDQCKTAQLEINVHKNRYLDVLAADHYRPILTSQGPgAQATDYIN 1498
Cdd:cd14604     11 ERVQAMKSTDHNGEDNFASDFMRLrrLSTKYRTEKIYPTATGEKEENVKKNRYKDILPFDHSRVKLTLKTS-SQDSDYIN 89
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2034231280 1499 AVYVDGYLRRNQFIVTQTPLHTTVLDFWRLVWDHDIRTIVMV-ENFKHEDDTRAEYWPPAASGGVmkQLEPFFLETTACY 1577
Cdd:cd14604     90 ANFIKGVYGPKAYIATQGPLANTVIDFWRMIWEYNVAIIVMAcREFEMGRKKCERYWPLYGEEPM--TFGPFRISCEAEQ 167
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2034231280 1578 QQENITVRNLrLLSTQhprDPARFVRQFQFNAWAEHAMaPQSKTMMLDLVDSVFDWQEEacaNERPVLVHCQDGSSHSGL 1657
Cdd:cd14604    168 ARTDYFIRTL-LLEFQ---NETRRLYQFHYVNWPDHDV-PSSFDSILDMISLMRKYQEH---EDVPICIHCSAGCGRTGA 239
                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|..
gi 2034231280 1658 -----FTTLAVVCERMEEdgEVDVYRTIKHIKRRRGQIIADYDQFRFCYKAV 1704
Cdd:cd14604    240 icaidYTWNLLKAGKIPE--EFNVFNLIQEMRTQRHSAVQTKEQYELVHRAI 289
R-PTPc-Z-1 cd17668
catalytic domain of receptor-type tyrosine-protein phosphatase Z, repeat 1; Receptor-type ...
1496-1704 7.88e-29

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: 115.85  E-value: 7.88e-29
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2034231280 1496 YINAVYVDGYLRRNQFIVTQTPLHTTVLDFWRLVWDHDIRTIVMVENFKHEDDTRA-EYWPPAAS---GGVMKQLEPffL 1571
Cdd:cd17668      1 YINANYVDGYNKPKAYIAAQGPLKSTAEDFWRMIWEHNVEVIVMITNLVEKGRRKCdQYWPADGSeeyGNFLVTQKS--V 78
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2034231280 1572 ETTACYQQENITVRNLRLLS-TQHPRDPARFVRQFQFNAWAEHAMaPQSKTMMLDLVDSVFDWQEEACAnerPVLVHCQD 1650
Cdd:cd17668     79 QVLAYYTVRNFTLRNTKIKKgSQKGRPSGRVVTQYHYTQWPDMGV-PEYTLPVLTFVRKASYAKRHAVG---PVVVHCSA 154
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....
gi 2034231280 1651 GSSHSGLFTTLAVVCERMEEDGEVDVYRTIKHIKRRRGQIIADYDQFRFCYKAV 1704
Cdd:cd17668    155 GVGRTGTYIVLDSMLQQIQHEGTVNIFGFLKHIRSQRNYLVQTEEQYVFIHDAL 208
PTPc-N6 cd14606
catalytic domain of tyrosine-protein phosphatase non-receptor type 6; Tyrosine-protein ...
1465-1708 1.00e-28

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: 117.29  E-value: 1.00e-28
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2034231280 1465 NVHKNRYLDVLAADHYRPILTSQGPGAQATDYINAVYVDGYL-----RRNQFIVTQTPLHTTVLDFWRLVWDHDIRTIVM 1539
Cdd:cd14606     18 NKSKNRYKNILPFDHSRVILQGRDSNIPGSDYINANYVKNQLlgpdeNAKTYIASQGCLEATVNDFWQMAWQENSRVIVM 97
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2034231280 1540 VENFKHEDDTR-AEYWPPAasgGVMKQLEPFFLETTACYQQENITVRNLRlLSTQHPRDPARFVRQFQFNAWAEHAMaPQ 1618
Cdd:cd14606     98 TTREVEKGRNKcVPYWPEV---GMQRAYGPYSVTNCGEHDTTEYKLRTLQ-VSPLDNGELIREIWHYQYLSWPDHGV-PS 172
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2034231280 1619 SKTMMLDLVDSVFDWQEEaCANERPVLVHCQDGSSHSGLFTTLAVVCERMEEDG---EVDVYRTIKHIKRRRGQIIADYD 1695
Cdd:cd14606    173 EPGGVLSFLDQINQRQES-LPHAGPIIVHCSAGIGRTGTIIVIDMLMENISTKGldcDIDIQKTIQMVRAQRSGMVQTEA 251
                          250
                   ....*....|...
gi 2034231280 1696 QFRFCYKAVWDFM 1708
Cdd:cd14606    252 QYKFIYVAIAQFI 264
R-PTPc-typeIIb-1 cd14555
catalytic domain of type IIb (or R2B) subfamily receptor-type tyrosine-protein phosphatases, ...
1496-1704 2.48e-28

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: 114.24  E-value: 2.48e-28
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2034231280 1496 YINAVYVDGYLRRNQFIVTQTPLHTTVLDFWRLVWDHDIRTIVMVENFKHEDDTR-AEYWPpaasggvmkqlepfflETT 1574
Cdd:cd14555      1 YINANYIDGYHRPNHYIATQGPMQETVYDFWRMVWQENSASIVMVTNLVEVGRVKcSRYWP----------------DDT 64
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2034231280 1575 ACYQQENITVRNLRLLSTQHPRDPA---------RFVRQFQFNAWAEHAMaPQSKTMMLDLVDSVfdwQEEACANERPVL 1645
Cdd:cd14555     65 EVYGDIKVTLVETEPLAEYVVRTFAlerrgyheiREVRQFHFTGWPDHGV-PYHATGLLGFIRRV---KASNPPSAGPIV 140
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 2034231280 1646 VHCQDGSSHSGLFTTLAVVCERMEEDGEVDVYRTIKHIKRRRGQIIADYDQFRFCYKAV 1704
Cdd:cd14555    141 VHCSAGAGRTGCYIVIDIMLDMAEREGVVDIYNCVKELRSRRVNMVQTEEQYIFIHDAI 199
COG5599 COG5599
Protein tyrosine phosphatase [Signal transduction mechanisms];
1174-1400 3.89e-28

Protein tyrosine phosphatase [Signal transduction mechanisms];


Pssm-ID: 444335 [Multi-domain]  Cd Length: 282  Bit Score: 115.96  E-value: 3.89e-28
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2034231280 1174 GSHLNRFPHLLPYDHSLVQlrpdvtSRGSYVNASFLPGYKKTpAYIAAQSPYnEETVLDFWRLIYQRSIKTVVMITNVVE 1253
Cdd:COG5599     42 GSPLNRFRDIQPYKETALR------ANLGYLNANYIQVIGNH-RYIATQYPL-EEQLEDFFQMLFDNNTPVLVVLASDDE 113
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2034231280 1254 DH--IVKCTQYWPTQTKASFGDIFFLHLIEVNEYADYIIRTIGVKMKGDSDSKI-VRLFEFTSWPDHGVPDDPI--PFLD 1328
Cdd:COG5599    114 ISkpKVKMPVYFRQDGEYGKYEVSSELTESIQLRDGIEARTYVLTIKGTGQKKIeIPVLHVKNWPDHGAISAEAlkNLAD 193
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2034231280 1329 MRYKVRRYQHDSPSPILVHCGTGMARTGVFIAVDALIDQYASEG--RVMVYDFVRRLRKDR-PFMVRTLKQYVFI 1400
Cdd:COG5599    194 LIDKKEKIKDPDKLLPVVHCRAGVGRTGTLIACLALSKSINALVqiTLSVEEIVIDMRTSRnGGMVQTSEQLDVL 268
R-PTPc-K-1 cd14631
catalytic domain of receptor-type tyrosine-protein phosphatase K, repeat 1; Receptor-type ...
1493-1704 4.63e-28

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: 113.96  E-value: 4.63e-28
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2034231280 1493 ATDYINAVYVDGYLRRNQFIVTQTPLHTTVLDFWRLVWDHDIRTIVMVENFKHEDDTRA-EYWPPAASggVMKQLEPFFL 1571
Cdd:cd14631     12 SSDYINANYIDGYQRPSHYIATQGPVHETVYDFWRMIWQEQSACIVMVTNLVEVGRVKCyKYWPDDTE--VYGDFKVTCV 89
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2034231280 1572 ETTACYQqenITVRNLRLlsTQHPRDPARFVRQFQFNAWAEHAMaPQSKTMMLDLVDSVfdwQEEACANERPVLVHCQDG 1651
Cdd:cd14631     90 EMEPLAE---YVVRTFTL--ERRGYNEIREVKQFHFTGWPDHGV-PYHATGLLSFIRRV---KLSNPPSAGPIVVHCSAG 160
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|...
gi 2034231280 1652 SSHSGLFTTLAVVCERMEEDGEVDVYRTIKHIKRRRGQIIADYDQFRFCYKAV 1704
Cdd:cd14631    161 AGRTGCYIVIDIMLDMAEREGVVDIYNCVKALRSRRINMVQTEEQYIFIHDAI 213
PTPc-N1 cd14608
catalytic domain of tyrosine-protein phosphatase non-receptor type 1; Tyrosine-protein ...
1457-1704 1.19e-27

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: 114.35  E-value: 1.19e-27
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2034231280 1457 CKTAQLEINVHKNRYLDVLAADHYRPILTSQgpgaqATDYINAVYVDGYLRRNQFIVTQTPLHTTVLDFWRLVWDHDIRT 1536
Cdd:cd14608     17 CRVAKLPKNKNRNRYRDVSPFDHSRIKLHQE-----DNDYINASLIKMEEAQRSYILTQGPLPNTCGHFWEMVWEQKSRG 91
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2034231280 1537 IVMVENFKHEDDTR-AEYWPpaasggvMKQLEPFFLETT---ACYQQENI----TVRNLRL--LSTQHPRDparfVRQFQ 1606
Cdd:cd14608     92 VVMLNRVMEKGSLKcAQYWP-------QKEEKEMIFEDTnlkLTLISEDIksyyTVRQLELenLTTQETRE----ILHFH 160
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2034231280 1607 FNAWAEHAMaPQSKTMMLDLvdsVFDWQEEACANER--PVLVHCQDGSSHSGLFT---TLAVVCERMEEDGEVDVYRTIK 1681
Cdd:cd14608    161 YTTWPDFGV-PESPASFLNF---LFKVRESGSLSPEhgPVVVHCSAGIGRSGTFCladTCLLLMDKRKDPSSVDIKKVLL 236
                          250       260
                   ....*....|....*....|...
gi 2034231280 1682 HIKRRRGQIIADYDQFRFCYKAV 1704
Cdd:cd14608    237 EMRKFRMGLIQTADQLRFSYLAV 259
PHA02746 PHA02746
protein tyrosine phosphatase; Provisional
1465-1704 3.71e-27

protein tyrosine phosphatase; Provisional


Pssm-ID: 165113 [Multi-domain]  Cd Length: 323  Bit Score: 114.36  E-value: 3.71e-27
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2034231280 1465 NVHKNRYLDVLAADHYRPILTSQG-----------PGAQ-------ATDYINAVYVDGYLRRNQFIVTQTPLHTTVLDFW 1526
Cdd:PHA02746    51 NLKKNRFHDIPCWDHSRVVINAHEslkmfdvgdsdGKKIevtsednAENYIHANFVDGFKEANKFICAQGPKEDTSEDFF 130
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2034231280 1527 RLVWDHDIRTIVMVENFKHEDDTRAEYWppAASGGVMKQLEPFFLETTACYQQENITVRNLRLlsTQHPRDPARFVRQFQ 1606
Cdd:PHA02746   131 KLISEHESQVIVSLTDIDDDDEKCFELW--TKEEDSELAFGRFVAKILDIIEELSFTKTRLMI--TDKISDTSREIHHFW 206
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2034231280 1607 FNAWAEHAMaPQSKTMMLDLVDSVFDWQEEACANER-------PVLVHCQDGSSHSGLFTTLAVVCERMEEDGEVDVYRT 1679
Cdd:PHA02746   207 FPDWPDNGI-PTGMAEFLELINKVNEEQAELIKQADndpqtlgPIVVHCSAGIGRAGTFCAIDNALEQLEKEKEVCLGEI 285
                          250       260
                   ....*....|....*....|....*
gi 2034231280 1680 IKHIKRRRGQIIADYDQFRFCYKAV 1704
Cdd:PHA02746   286 VLKIRKQRHSSVFLPEQYAFCYKAL 310
PTPc-N1_2 cd14545
catalytic domain of tyrosine-protein phosphatase non-receptor type 1 and type 2; ...
1468-1702 5.02e-27

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: 111.33  E-value: 5.02e-27
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2034231280 1468 KNRYLDVLAADHYRPILTSQGPGaqaTDYINAVYVDGYLRRNQFIVTQTPLHTTVLDFWRLVWDHDIRTIVMVENFKHED 1547
Cdd:cd14545      1 LNRYRDRDPYDHDRSRVKLKQGD---NDYINASLVEVEEAKRSYILTQGPLPNTSGHFWQMVWEQNSKAVIMLNKLMEKG 77
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2034231280 1548 DTR-AEYWPPAASGGVMKQLEPFFLETTACYQQENITVRNLRL--LSTQHPRDparfVRQFQFNAWAEHAMaPQSKTMML 1624
Cdd:cd14545     78 QIKcAQYWPQGEGNAMIFEDTGLKVTLLSEEDKSYYTVRTLELenLKTQETRE----VLHFHYTTWPDFGV-PESPAAFL 152
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2034231280 1625 DLVDSVfdwQEEACANER--PVLVHCQDGSSHSGLF----TTLAVVCERMEedGEVDVYRTIKHIKRRRGQIIADYDQFR 1698
Cdd:cd14545    153 NFLQKV---RESGSLSSDvgPPVVHCSAGIGRSGTFclvdTCLVLIEKGNP--SSVDVKKVLLEMRKYRMGLIQTPDQLR 227

                   ....
gi 2034231280 1699 FCYK 1702
Cdd:cd14545    228 FSYL 231
R-PTPc-Q cd14616
catalytic domain of receptor-type tyrosine-protein phosphatase Q; Receptor-type ...
1469-1702 6.91e-27

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: 110.77  E-value: 6.91e-27
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2034231280 1469 NRYLDVLAADHYRPILTSQgPGAQATDYINAVYVDGYLRRNQFIVTQTPLHTTVLDFWRLVWDHDIRTIVMVENFKHEDD 1548
Cdd:cd14616      1 NRFPNIKPYNNNRVKLIAD-AGVPGSDYINASYISGYLCPNEFIATQGPLPGTVGDFWRMVWETRAKTIVMLTQCFEKGR 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2034231280 1549 TRA-EYWP----PAASGG---VMKQLEPFflettacyqQENITVRNLRLLSTQHprdpARFVRQFQFNAWAEHAMaPQSK 1620
Cdd:cd14616     80 IRChQYWPednkPVTVFGdivITKLMEDV---------QIDWTIRDLKIERHGD----YMMVRQCNFTSWPEHGV-PESS 145
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2034231280 1621 TMMLDLVDSVfdwQEEACANERPVLVHCQDGSSHSGLFTTLAVVCERMEEDGEVDVYRTIKHIKRRRGQIIADYDQFRFC 1700
Cdd:cd14616    146 APLIHFVKLV---RASRAHDNTPMIVHCSAGVGRTGVFIALDHLTQHINDHDFVDIYGLVAELRSERMCMVQNLAQYIFL 222

                   ..
gi 2034231280 1701 YK 1702
Cdd:cd14616    223 HQ 224
PHA02738 PHA02738
hypothetical protein; Provisional
1465-1710 1.51e-26

hypothetical protein; Provisional


Pssm-ID: 222923 [Multi-domain]  Cd Length: 320  Bit Score: 112.33  E-value: 1.51e-26
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2034231280 1465 NVHKNRYLDVLAADHYRPILTSQgpgAQATDYINAVYVDGYLRRNQFIVTQTPLHTTVLDFWRLVWDHDIRTIVMVenFK 1544
Cdd:PHA02738    49 NRKLNRYLDAVCFDHSRVILPAE---RNRGDYINANYVDGFEYKKKFICGQAPTRQTCYDFYRMLWMEHVQIIVML--CK 123
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2034231280 1545 HEDDTRAE---YWPPAASGGVmkQLEPFFLETTacyqqeNITVRNLRLLSTQHPRD---PARFVRQFQFNAWAEHAMaPQ 1618
Cdd:PHA02738   124 KKENGREKcfpYWSDVEQGSI--RFGKFKITTT------QVETHPHYVKSTLLLTDgtsATQTVTHFNFTAWPDHDV-PK 194
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2034231280 1619 SKTMMLDLVDSVFDWQEEACANE----------RPVLVHCQDGSSHSGLFTTLAVVCERMEEDGEVDVYRTIKHIKRRRG 1688
Cdd:PHA02738   195 NTSEFLNFVLEVRQCQKELAQESlqighnrlqpPPIVVHCNAGLGRTPCYCVVDISISRFDACATVSIPSIVSSIRNQRY 274
                          250       260
                   ....*....|....*....|..
gi 2034231280 1689 QIIADYDQFRFCYKAVWDFMNL 1710
Cdd:PHA02738   275 YSLFIPFQYFFCYRAVKRYVNL 296
PHA02742 PHA02742
protein tyrosine phosphatase; Provisional
1465-1710 2.15e-26

protein tyrosine phosphatase; Provisional


Pssm-ID: 165109 [Multi-domain]  Cd Length: 303  Bit Score: 111.63  E-value: 2.15e-26
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2034231280 1465 NVHKNRYLDVLAADHYRPILTSQGPGaqaTDYINAVYVDGYLRRNQFIVTQTPLHTTVLDFWRLVWDHDIRTIVMVENFk 1544
Cdd:PHA02742    52 NMKKCRYPDAPCFDRNRVILKIEDGG---DDFINASYVDGHNAKGRFICTQAPLEETALDFWQAIFQDQVRVIVMITKI- 127
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2034231280 1545 HEDDTRA--EYWPPAASGGVMKQlePFFLETTACYQQENITVRNLRLLSTQhpRDPARFVRQFQFNAWAeHAMAPQSKTM 1622
Cdd:PHA02742   128 MEDGKEAcyPYWMPHERGKATHG--EFKIKTKKIKSFRNYAVTNLCLTDTN--TGASLDIKHFAYEDWP-HGGLPRDPNK 202
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2034231280 1623 MLDLVDSV--------FDWQEEACANERPVLVHCQDGSSHSGLFTTLAVVCERMEEDGEVDVYRTIKHIKRRRGQIIADY 1694
Cdd:PHA02742   203 FLDFVLAVreadlkadVDIKGENIVKEPPILVHCSAGLDRAGAFCAIDICISKYNERAIIPLLSIVRDLRKQRHNCLSLP 282
                          250
                   ....*....|....*.
gi 2034231280 1695 DQFRFCYKAVWDFMNL 1710
Cdd:PHA02742   283 QQYIFCYFIVLIFAKL 298
PTPc-N22 cd14602
catalytic domain of tyrosine-protein phosphatase non-receptor type 22; Tyrosine-protein ...
1468-1704 3.12e-26

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: 109.16  E-value: 3.12e-26
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2034231280 1468 KNRYLDVLAADHYR---PILTSQgpgaQATDYINAVYVDGYLRRNQFIVTQTPLHTTVLDFWRLVWDHDIRTIVMV-ENF 1543
Cdd:cd14602      1 KNRYKDILPYDHSRvelSLITSD----EDSDYINANFIKGVYGPRAYIATQGPLSTTLLDFWRMIWEYSVLIIVMAcMEF 76
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2034231280 1544 KHEDDTRAEYWppAASGGVMKQLEPFfleTTACYQQENITVRNLRLLSTQHPRDpARFVRQFQFNAWAEHAMaPQSKTMM 1623
Cdd:cd14602     77 EMGKKKCERYW--AEPGEMQLEFGPF---SVTCEAEKRKSDYIIRTLKVKFNSE-TRTIYQFHYKNWPDHDV-PSSIDPI 149
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2034231280 1624 LDLVDSVFDWQEEacaNERPVLVHCQDGSSHSGlfttlaVVCE-----RMEEDGEV----DVYRTIKHIKRRRGQIIADY 1694
Cdd:cd14602    150 LELIWDVRCYQED---DSVPICIHCSAGCGRTG------VICAidytwMLLKDGIIpenfSVFSLIQEMRTQRPSLVQTK 220
                          250
                   ....*....|
gi 2034231280 1695 DQFRFCYKAV 1704
Cdd:cd14602    221 EQYELVYNAV 230
PTPc-N22_18_12 cd14542
catalytic domain of tyrosine-protein phosphatase non-receptor type 22, type 18 and type 12; ...
1496-1702 1.30e-25

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: 106.35  E-value: 1.30e-25
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2034231280 1496 YINAVYVDGYLRRNQFIVTQTPLHTTVLDFWRLVWDHDIRTIVMVENFKHEDDTRAE-YWPpaASGGVMKQLEPFfleTT 1574
Cdd:cd14542      1 YINANFIKGVSGSKAYIATQGPLPNTVLDFWRMIWEYNVQVIVMACREFEMGKKKCErYWP--EEGEEQLQFGPF---KI 75
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2034231280 1575 ACYQQEN----ITVRNLRLLSTQHPRDparfVRQFQFNAWAEHAMaPQSKTMMLDLVDSVFDWQEeacANERPVLVHCQD 1650
Cdd:cd14542     76 SLEKEKRvgpdFLIRTLKVTFQKESRT----VYQFHYTAWPDHGV-PSSVDPILDLVRLVRDYQG---SEDVPICVHCSA 147
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 2034231280 1651 GSSHSGLFTTLAVVCERMEEDG---EVDVYRTIKHIKRRRGQIIADYDQFRFCYK 1702
Cdd:cd14542    148 GCGRTGTICAIDYVWNLLKTGKipeEFSLFDLVREMRKQRPAMVQTKEQYELVYR 202
R-PTPc-T-2 cd14634
PTP domain of receptor-type tyrosine-protein phosphatase T, repeat 2; Receptor-type ...
1203-1406 2.81e-25

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: 105.49  E-value: 2.81e-25
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2034231280 1203 YVNASFLPGYKKTPAYIAAQSPYnEETVLDFWRLIYQRSIKTVVMITNVveDHIVKCTQYWPTQTKASFGDIFfLHLIEV 1282
Cdd:cd14634      1 YINAALMDSHKQPAAFIVTQHPL-PNTVADFWRLVFDYNCSSVVMLNEM--DAAQLCMQYWPEKTSCCYGPIQ-VEFVSA 76
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2034231280 1283 NEYADYIIRTIGV-KMKGDSDS-KIVRLFEFTSWPDHgvPDDPIPFLDMRYKVRRY-----QHDS-PSPILVHCGTGMAR 1354
Cdd:cd14634     77 DIDEDIISRIFRIcNMARPQDGyRIVQHLQYIGWPAY--RDTPPSKRSILKVVRRLekwqeQYDGrEGRTVVHCLNGGGR 154
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|..
gi 2034231280 1355 TGVFIAVDALIDQYASEGRVMVYDFVRRLRKDRPFMVRTLKQYVFIYEAIFE 1406
Cdd:cd14634    155 SGTFCAICSVCEMIQQQNIIDVFHTVKTLRNNKSNMVETLEQYKFVYEVALE 206
R-PTPc-B cd14617
catalytic domain of receptor-type tyrosine-protein phosphatase B; Receptor-type ...
1469-1702 7.20e-25

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: 105.00  E-value: 7.20e-25
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2034231280 1469 NRYLDVLAADHYRPILtSQGPGAQATDYINAVYVDGYLRRNQFIVTQTPLHTTVLDFWRLVWDHDIRTIVMVENFKHEDD 1548
Cdd:cd14617      1 NRYNNILPYDSTRVKL-SNVDDDPCSDYINASYIPGNNFRREYIATQGPLPGTKDDFWKMVWEQNVHNIVMVTQCVEKGR 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2034231280 1549 TRAE-YWP----PAASGGVMKQL--EPFFLETtacyqqeniTVRNLRlLSTQHPRDPARFVRQFQFNAWAEHAMaPQSKT 1621
Cdd:cd14617     80 VKCDhYWPadqdSLYYGDLIVQMlsESVLPEW---------TIREFK-ICSEEQLDAPRLVRHFHYTVWPDHGV-PETTQ 148
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2034231280 1622 MMLDLVDSVFDWQEEAcANERPVLVHCQDGSSHSGLFTTLAVVCERMEEDGEVDVYRTIKHIKRRRGQIIADYDQFRFCY 1701
Cdd:cd14617    149 SLIQFVRTVRDYINRT-PGSGPTVVHCSAGVGRTGTFIALDRILQQLDSKDSVDIYGAVHDLRLHRVHMVQTECQYVYLH 227

                   .
gi 2034231280 1702 K 1702
Cdd:cd14617    228 Q 228
R5-PTP-2 cd14550
PTP-like domain of R5 subfamily receptor-type tyrosine-protein phosphatases, repeat 2; The R5 ...
1203-1402 1.00e-24

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: 103.55  E-value: 1.00e-24
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2034231280 1203 YVNASFLPGYKKTPAYIAAQSPYnEETVLDFWRLIYQRSIKTVVMITNVVEDHivKCTQYWPTQTKASFGDIFFLHLIE- 1281
Cdd:cd14550      1 YINASYLQGYRRSNEFIITQHPL-EHTIKDFWQMIWDHNSQTIVMLTDNELNE--DEPIYWPTKEKPLECETFKVTLSGe 77
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2034231280 1282 ----VNEYADYIIRTIGVKMKGDSDSKIVRLFEFTSWPDhgvPDDPI-PFLDMRYKVRRYQHDSPSPILVHCGTGMARTG 1356
Cdd:cd14550     78 dhscLSNEIRLIVRDFILESTQDDYVLEVRQFQCPSWPN---PCSPIhTVFELINTVQEWAQQRDGPIVVHDRYGGVQAA 154
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*.
gi 2034231280 1357 VFIAVDALIDQYASEGRVMVYDFVRRLRKDRPFMVRTLKQYVFIYE 1402
Cdd:cd14550    155 TFCALTTLHQQLEHESSVDVYQVAKLYHLMRPGVFTSKEDYQFLYK 200
PTPc-N21_14 cd14540
catalytic domain of tyrosine-protein phosphatase non-receptor type 21 and type 14; ...
1496-1701 1.35e-24

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: 103.69  E-value: 1.35e-24
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2034231280 1496 YINAVYVDGYLRRNQ--FIVTQTPLHTTVLDFWRLVWDHDIRTIVMV---ENFKHEDDTRaeYWPPAASGGVMKQLEPF- 1569
Cdd:cd14540      1 YINASHITATVGGKQrfYIAAQGPLQNTVGDFWQMVWEQGVYLVVMVtaeEEGGREKCFR--YWPTLGGEHDALTFGEYk 78
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2034231280 1570 ----FLETTACYqqeniTVRNLRLLSTQHPRdpARFVRQFQFNAWAEHAMA--PQSKTMMLDLVDSV--FDWQEEACAN- 1640
Cdd:cd14540     79 vstkFSVSSGCY-----TTTGLRVKHTLSGQ--SRTVWHLQYTDWPDHGCPedVSGFLDFLEEINSVrrHTNQDVAGHNr 151
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2034231280 1641 ERPVLVHCQDGSSHSGLFTTLAVVCERMEEDGEVDVYRTIKHIKRRRGQIIADYDQFRFCY 1701
Cdd:cd14540    152 NPPTLVHCSAGVGRTGVVILADLMLYCLDHNEELDIPRVLALLRHQRMLLVQTLAQYKFVY 212
R-PTPc-K-2 cd14636
PTP domain of receptor-type tyrosine-protein phosphatase K, repeat 2; Receptor-type ...
1203-1406 3.61e-24

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: 102.03  E-value: 3.61e-24
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2034231280 1203 YVNASFLPGYKKTPAYIAAQSPYnEETVLDFWRLIYQRSIKTVVMITNVveDHIVKCTQYWPTQTKASFGDIFfLHLIEV 1282
Cdd:cd14636      1 YINAALMDSYRQPAAFIVTQHPL-PNTVKDFWRLVYDYGCTSIVMLNEV--DLAQGCPQYWPEEGMLRYGPIQ-VECMSC 76
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2034231280 1283 NEYADYIIRTIGV--KMKGDSDSKIVRLFEFTSWPDH-GVPDDPIPFLDMRYKVRRYQHD---SPSPILVHCGTGMARTG 1356
Cdd:cd14636     77 SMDCDVISRIFRIcnLTRPQEGYLMVQQFQYLGWASHrEVPGSKRSFLKLILQVEKWQEEcdeGEGRTIIHCLNGGGRSG 156
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|
gi 2034231280 1357 VFIAVDALIDQYASEGRVMVYDFVRRLRKDRPFMVRTLKQYVFIYEAIFE 1406
Cdd:cd14636    157 MFCAISIVCEMIKRQNVVDVFHAVKTLRNSKPNMVETPEQYRFCYDVALE 206
PHA02747 PHA02747
protein tyrosine phosphatase; Provisional
1465-1699 5.19e-24

protein tyrosine phosphatase; Provisional


Pssm-ID: 165114 [Multi-domain]  Cd Length: 312  Bit Score: 104.70  E-value: 5.19e-24
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2034231280 1465 NVHKNRYLDVLAADHYRPILTSQGpgAQATDYINAVYVDGYLRRNQFIVTQTPLHTTVLDFWRLVWDHDIRTIVMVENFK 1544
Cdd:PHA02747    51 NQPKNRYWDIPCWDHNRVILDSGG--GSTSDYIHANWIDGFEDDKKFIATQGPFAETCADFWKAVWQEHCSIIVMLTPTK 128
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2034231280 1545 HEDDTRA--EYWPPAASGGVMkqLEPFFLETTacyqqeNITVRNLRLLSTQHPRDP----ARFVRQFQFNAWAEHamapQ 1618
Cdd:PHA02747   129 GTNGEEKcyQYWCLNEDGNID--MEDFRIETL------KTSVRAKYILTLIEITDKilkdSRKISHFQCSEWFED----E 196
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2034231280 1619 SKTMMLDLVD-------------SVFDWQEEACAnerPVLVHCQDGSSHSGLFTTLAVVCERMEEDGEVDVYRTIKHIKR 1685
Cdd:PHA02747   197 TPSDHPDFIKfikiidinrkksgKLFNPKDALLC---PIVVHCSDGVGKTGIFCAVDICLNQLVKRKAICLAKTAEKIRE 273
                          250
                   ....*....|....
gi 2034231280 1686 RRGQIIADYDQFRF 1699
Cdd:PHA02747   274 QRHAGIMNFDDYLF 287
R-PTPc-C-1 cd14557
catalytic domain of receptor-type tyrosine-protein phosphatase C, repeat 1; Receptor-type ...
1496-1687 7.21e-24

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: 101.06  E-value: 7.21e-24
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2034231280 1496 YINAVYVDGYLRRNQFIVTQTPLHTTVLDFWRLVWDHDIRTIVMVENFKHEDDTR-AEYWPPaasggvMKQLEPFFLETT 1574
Cdd:cd14557      1 YINASYIDGFKEPRKYIAAQGPKDETVDDFWRMIWEQKSTVIVMVTRCEEGNRNKcAQYWPS------MEEGSRAFGDVV 74
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2034231280 1575 ACYQQE----NITVRNLRLLSTQHPRDpARFVRQFQFNAWAEHAMaPQSKTMMLDLVDSVFDWQEEACAnerPVLVHCQD 1650
Cdd:cd14557     75 VKINEEkicpDYIIRKLNINNKKEKGS-GREVTHIQFTSWPDHGV-PEDPHLLLKLRRRVNAFNNFFSG---PIVVHCSA 149
                          170       180       190
                   ....*....|....*....|....*....|....*..
gi 2034231280 1651 GSSHSGLFTTLAVVCERMEEDGEVDVYRTIKHIKRRR 1687
Cdd:cd14557    150 GVGRTGTYIGIDAMLEGLEAEGRVDVYGYVVKLRRQR 186
PTPc-N21 cd14598
catalytic domain of tyrosine-protein phosphatase non-receptor type 21; Tyrosine-protein ...
1203-1406 1.28e-23

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: 101.21  E-value: 1.28e-23
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2034231280 1203 YVNASFLpgyKKTPA-----YIAAQSPYnEETVLDFWRLIYQRSIKTVVMITNVVEDHIVKCTQYWP-------TQTKAS 1270
Cdd:cd14598      1 YINASHI---KVTVGgkewdYIATQGPL-QNTCQDFWQMVWEQGVAIIAMVTAEEEGGREKSFRYWPrlgsrhnTVTYGR 76
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2034231280 1271 FgDIFFLHLIEVNEYAdyiirTIGVKMKG--DSDSKIVRLFEFTSWPDHGVPDDP---IPFLDMRYKVRRYQHDSP---- 1341
Cdd:cd14598     77 F-KITTRFRTDSGCYA-----TTGLKIKHllTGQERTVWHLQYTDWPEHGCPEDLkgfLSYLEEIQSVRRHTNSTIdpks 150
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2034231280 1342 --SPILVHCGTGMARTGVFIAVDALIDQYASEGRVMVYDFVRRLRKDRPFMVRTLKQYVFIYEAIFE 1406
Cdd:cd14598    151 pnPPVLVHCSAGVGRTGVVILSEIMIACLEHNEMLDIPRVLDMLRQQRMMMVQTLSQYTFVYKVLIQ 217
PTP_fungal cd18533
fungal protein tyrosine phosphatases; This subfamily contains Saccharomyces cerevisiae ...
1496-1701 1.95e-23

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: 100.40  E-value: 1.95e-23
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2034231280 1496 YINAVYVD-GYLRRNQFIVTQTPLHTTVLDFWRLVWDHDIRTIVMVENFKHEDDTR-AEYWPPAASGGVMKQLEPFFLET 1573
Cdd:cd18533      1 YINASYITlPGTSSKRYIATQGPLPATIGDFWKMIWQNNVGVIVMLTPLVENGREKcDQYWPSGEYEGEYGDLTVELVSE 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2034231280 1574 TACyQQENITVRNLRLlstQHPRDPARFVRQFQFNAWAEHAmAPQSKTMMLDLVDSVfdwQE--EACANERPVLVHCQDG 1651
Cdd:cd18533     81 EEN-DDGGFIVREFEL---SKEDGKVKKVYHIQYKSWPDFG-VPDSPEDLLTLIKLK---RElnDSASLDPPIIVHCSAG 152
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 2034231280 1652 SSHSGLFTTLAVVCERMEEDGEVD---------VYRTIKHIKRRRGQIIADYDQFRFCY 1701
Cdd:cd18533    153 VGRTGTFIALDSLLDELKRGLSDSqdledsedpVYEIVNQLRKQRMSMVQTLRQYIFLY 211
R-PTP-N-N2 cd14546
PTP-like domain of receptor-type tyrosine-protein phosphatase-like N and N2; Receptor-type ...
1496-1704 2.93e-23

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: 99.44  E-value: 2.93e-23
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2034231280 1496 YINAVYVDGYLRRNQ-FIVTQTPLHTTVLDFWRLVWDHDIRTIVMVENFKhEDDTRAE--YWPPAASgGVMKQLEPFFL- 1571
Cdd:cd14546      1 YINASTIYDHDPRNPaYIATQGPLPHTIADFWQMIWEQGCVVIVMLTRLQ-ENGVKQCarYWPEEGS-EVYHIYEVHLVs 78
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2034231280 1572 ETTACyqqENITVRNLRLLSTQHprDPARFVRQFQFNAWAEHAMAPQSKTmMLDlvdsvFDWQEEACANER--PVLVHCQ 1649
Cdd:cd14546     79 EHIWC---DDYLVRSFYLKNLQT--SETRTVTQFHFLSWPDEGIPASAKP-LLE-----FRRKVNKSYRGRscPIVVHCS 147
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 2034231280 1650 DGSSHSGLFTTLAVVCERMEEDG-EVDVYRTIKHIKRRRGQIIADYDQFRFCYKAV 1704
Cdd:cd14546    148 DGAGRTGTYILIDMVLNRMAKGAkEIDIAATLEHLRDQRPGMVKTKDQFEFVLTAV 203
PTPc-N20_13 cd14538
catalytic domain of tyrosine-protein phosphatase non-receptor type 20 and type 13; ...
1496-1704 9.87e-23

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: 98.22  E-value: 9.87e-23
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2034231280 1496 YINAVYV-----DGYLRrnqFIVTQTPLHTTVLDFWRLVWDHDIRTIVMV----ENFK---HEddtraeYWPPAASGGVM 1563
Cdd:cd14538      1 YINASHIripvgGDTYH---YIACQGPLPNTTGDFWQMVWEQKSEVIAMVtqdvEGGKvkcHR------YWPDSLNKPLI 71
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2034231280 1564 KQlEPFFLETTACYQQENITVRnlRLLSTQHPRDPARFVRQFQFNAWAEHAmAPQSKTMMLDLVDSVfdwqeEACANERP 1643
Cdd:cd14538     72 CG-GRLEVSLEKYQSLQDFVIR--RISLRDKETGEVHHITHLNFTTWPDHG-TPQSADPLLRFIRYM-----RRIHNSGP 142
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2034231280 1644 VLVHCQDGSSHSGLFTTLAVVCERMEEDGEVDVYRTIKHIKRRRGQIIADYDQFRFCYKAV 1704
Cdd:cd14538    143 IVVHCSAGIGRTGVLITIDVALGLIERDLPFDIQDIVKDLREQRQGMIQTKDQYIFCYKAC 203
PTPc-N3 cd14600
catalytic domain of tyrosine-protein phosphatase non-receptor type 3; Tyrosine-protein ...
1460-1704 1.83e-22

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: 99.15  E-value: 1.83e-22
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2034231280 1460 AQLEINVHKNRYLDVLAADHYRPILtsQGpgaqATDYINAVYVD----GYLRRNQFIVTQTPLHTTVLDFWRLVWDHDIR 1535
Cdd:cd14600     35 AKLPQNMDKNRYKDVLPYDATRVVL--QG----NEDYINASYVNmeipSANIVNKYIATQGPLPHTCAQFWQVVWEQKLS 108
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2034231280 1536 TIVMVENFKHEDDTRA-EYWPPAASggVMKqlepfFLETTACYQQENITV----RNLRLLSTQHPRDpaRFVRQFQFNAW 1610
Cdd:cd14600    109 LIVMLTTLTERGRTKChQYWPDPPD--VME-----YGGFRVQCHSEDCTIayvfREMLLTNTQTGEE--RTVTHLQYVAW 179
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2034231280 1611 AEHAMaPQSKTMMLDLVDSVfdwQEEACANErPVLVHCQDGSSHSGLFTTLAVVCERMEEDGEVDVYRTIKHIKRRRGQI 1690
Cdd:cd14600    180 PDHGV-PDDSSDFLEFVNYV---RSKRVENE-PVLVHCSAGIGRTGVLVTMETAMCLTERNQPVYPLDIVRKMRDQRAMM 254
                          250
                   ....*....|....
gi 2034231280 1691 IADYDQFRFCYKAV 1704
Cdd:cd14600    255 VQTSSQYKFVCEAI 268
PTPc-N2 cd14607
catalytic domain of tyrosine-protein phosphatase non-receptor type 2; Tyrosine-protein ...
1458-1704 2.54e-22

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: 98.50  E-value: 2.54e-22
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2034231280 1458 KTAQLEINVHKNRYLDVLAADHYRPILTSQgpgaqATDYINAVYVDGYLRRNQFIVTQTPLHTTVLDFWRLVWDHDIRTI 1537
Cdd:cd14607     17 RVAKYPENRNRNRYRDVSPYDHSRVKLQNT-----ENDYINASLVVIEEAQRSYILTQGPLPNTCCHFWLMVWQQKTKAV 91
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2034231280 1538 VMVENFKHEDDTR-AEYWPpaasggVMKQLEPFFLETTACYQ--QENI-TVRNLRLLSTQHPRD-PARFVRQFQFNAWAE 1612
Cdd:cd14607     92 VMLNRIVEKDSVKcAQYWP------TDEEEVLSFKETGFSVKllSEDVkSYYTVHLLQLENINSgETRTISHFHYTTWPD 165
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2034231280 1613 HAMaPQSKTMMLDLvdsVFDWQEEACANER--PVLVHCQDGSSHSGLFT---TLAVVCERMEEDgEVDVYRTIKHIKRRR 1687
Cdd:cd14607    166 FGV-PESPASFLNF---LFKVRESGSLSPEhgPAVVHCSAGIGRSGTFSlvdTCLVLMEKKDPD-SVDIKQVLLDMRKYR 240
                          250
                   ....*....|....*..
gi 2034231280 1688 GQIIADYDQFRFCYKAV 1704
Cdd:cd14607    241 MGLIQTPDQLRFSYMAV 257
R-PTPc-U-2 cd14637
PTP domain of receptor-type tyrosine-protein phosphatase U, repeat 2; Receptor-type ...
1203-1406 3.53e-22

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: 96.52  E-value: 3.53e-22
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2034231280 1203 YVNASFLPGYKKTPAYIAAQSPYnEETVLDFWRLIYQRSIKTVVMITNVVEDHIV-KCTQYWPTQTKASFG--DIFFLHL 1279
Cdd:cd14637      1 YINAALTDSYTRSAAFIVTLHPL-QNTTTDFWRLVYDYGCTSVVMLNQLNQSNSAwPCLQYWPEPGLQQYGpmEVEFVSG 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2034231280 1280 iEVNEyaDYIIRTIGVK--MKGDSDSKIVRLFEFTSW-PDHGVPDDPIPFLDMRYKVRRYQHDS-PSPILVHCGTGMART 1355
Cdd:cd14637     80 -SADE--DIVTRLFRVQniTRLQEGHLMVRHFQFLRWsAYRDTPDSKKAFLHLLASVEKWQRESgEGRTVVHCLNGGGRS 156
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|.
gi 2034231280 1356 GVFIAVDALIDQYASEGRVMVYDFVRRLRKDRPFMVRTLKQYVFIYEAIFE 1406
Cdd:cd14637    157 GTYCASAMILEMIRCHNIVDVFYAVKTLRNYKPNMVETLEQYRFCYEIALE 207
R-PTPc-M-2 cd14635
PTP domain of receptor-type tyrosine-protein phosphatase M, repeat 2; Receptor-type ...
1203-1406 4.01e-22

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: 96.30  E-value: 4.01e-22
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2034231280 1203 YVNASFLPGYKKTPAYIAAQSPYnEETVLDFWRLIYQRSIKTVVMITNVveDHIVKCTQYWPTQTKASFGDIFfLHLIEV 1282
Cdd:cd14635      1 YINAALMDSYKQPSAFIVTQHPL-PNTVKDFWRLVLDYHCTSIVMLNDV--DPAQLCPQYWPENGVHRHGPIQ-VEFVSA 76
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2034231280 1283 NEYADYIIRTIGV--KMKGDSDSKIVRLFEFTSWPDH-GVPDDPIPFLDMRYKVRRYQHD---SPSPILVHCGTGMARTG 1356
Cdd:cd14635     77 DLEEDIISRIFRIynAARPQDGYRMVQQFQFLGWPMYrDTPVSKRSFLKLIRQVDKWQEEyngGEGRTVVHCLNGGGRSG 156
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|
gi 2034231280 1357 VFIAVDALIDQYASEGRVMVYDFVRRLRKDRPFMVRTLKQYVFIYEAIFE 1406
Cdd:cd14635    157 TFCAISIVCEMLRHQRAVDVFHAVKTLRNNKPNMVDLLDQYKFCYEVALE 206
R-PTPc-O cd14614
catalytic domain of receptor-type tyrosine-protein phosphatase O; Receptor-type ...
1459-1704 2.30e-21

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: 95.34  E-value: 2.30e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2034231280 1459 TAQLEINVHKNRYLDVLAADHYRPILTSQGpGAQATDYINAVYVDGYLRRNQFIVTQTPLHTTVLDFWRLVWDHDIRTIV 1538
Cdd:cd14614      6 AADLPVNRCKNRYTNILPYDFSRVKLVSMH-EEEGSDYINANYIPGYNSPQEYIATQGPLPETRNDFWKMVLQQKSQIIV 84
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2034231280 1539 MVENFKHEDDTRAE-YWP----PAASGGVMkqlepffLETTACYQQENITVRNLRLLSTQHPRDparfVRQFQFNAWAEH 1613
Cdd:cd14614     85 MLTQCNEKRRVKCDhYWPfteePVAYGDIT-------VEMLSEEEQPDWAIREFRVSYADEVQD----VMHFNYTAWPDH 153
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2034231280 1614 AMaPQSKTM--MLDLVDSVfdwQEEACANERPVLVHCQDGSSHSGLFTTLAVVCERMEEDGEVDVYRTIKHIKRRRGQII 1691
Cdd:cd14614    154 GV-PTANAAesILQFVQMV---RQQAVKSKGPMIIHCSAGVGRTGTFIALDRLLQHIRDHEFVDILGLVSEMRSYRMSMV 229
                          250
                   ....*....|...
gi 2034231280 1692 ADYDQFRFCYKAV 1704
Cdd:cd14614    230 QTEEQYIFIHQCV 242
PTP-N23 cd14539
PTP-like domain of tyrosine-protein phosphatase non-receptor type 23; Tyrosine-protein ...
1496-1702 5.20e-21

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: 92.83  E-value: 5.20e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2034231280 1496 YINAVYVDGYLRRN-QFIVTQTPLHTTVLDFWRLVWDHDIRTIVM-VENFKHEDDTRAEYWP-----PAASGGVmkqlep 1568
Cdd:cd14539      1 YINASLIEDLTPYCpRFIATQAPLPGTAADFWLMVYEQQVSVIVMlVSEQENEKQKVHRYWPtergqALVYGAI------ 74
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2034231280 1569 ffleTTACYQQENITVRNLRLLSTQH-PRDPARFVRQFQFNAWAEHAMaPQSKTMMLDLVDSVFDWQEEACANERPVLVH 1647
Cdd:cd14539     75 ----TVSLQSVRTTPTHVERIISIQHkDTRLSRSVVHLQFTTWPELGL-PDSPNPLLRFIEEVHSHYLQQRSLQTPIVVH 149
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 2034231280 1648 CQDGSSHSGLFTTL-AVVCERMEEDGEVDVYRTIKHIKRRRGQIIADYDQFRFCYK 1702
Cdd:cd14539    150 CSSGVGRTGAFCLLyAAVQEIEAGNGIPDLPQLVRKMRQQRKYMLQEKEHLKFCYE 205
R-PTP-Z-2 cd17669
catalytic domain of receptor-type tyrosine-protein phosphatase Z, repeat 2; Receptor-type ...
1203-1405 6.70e-21

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: 92.75  E-value: 6.70e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2034231280 1203 YVNASFLPGYKKTPAYIAAQSPYnEETVLDFWRLIYQRSIKTVVMIT---NVVEDHIVkctqYWPTQTKASFGDIFFLHL 1279
Cdd:cd17669      1 YINASYIMGYYQSNEFIITQHPL-LHTIKDFWRMIWDHNAQLIVMLPdgqNMAEDEFV----YWPNKDEPINCETFKVTL 75
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2034231280 1280 IE-----VNEYADYIIRTIGVKMKGDSDSKIVRLFEFTSWPDhgvPDDPIP-FLDMRYKVRRYQHDSPSPILVHCGTGMA 1353
Cdd:cd17669     76 IAeehkcLSNEEKLIIQDFILEATQDDYVLEVRHFQCPKWPN---PDSPISkTFELISIIKEEAANRDGPMIVHDEHGGV 152
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|..
gi 2034231280 1354 RTGVFIAVDALIDQYASEGRVMVYDFVRRLRKDRPFMVRTLKQYVFIYEAIF 1405
Cdd:cd17669    153 TAGTFCALTTLMHQLEKENSVDVYQVAKMINLMRPGVFTDIEQYQFLYKAIL 204
PTPc-N3_4 cd14541
catalytic domain of tyrosine-protein phosphatase non-receptor type 21 and type 14; ...
1495-1704 6.78e-21

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: 92.78  E-value: 6.78e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2034231280 1495 DYINAVYVDGYLRR----NQFIVTQTPLHTTVLDFWRLVWDHDIRTIVM----VENFK---HeddtraEYWPpaaSGGVM 1563
Cdd:cd14541      1 DYINANYVNMEIPGsgivNRYIAAQGPLPNTCADFWQMVWEQKSTLIVMlttlVERGRvkcH------QYWP---DLGET 71
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2034231280 1564 KQLEPFFLETTACYQQENITVRNLRLLSTQHPRDpaRFVRQFQFNAWAEHAMaPQSKTMMLDLVDSVFdwQEEACANErP 1643
Cdd:cd14541     72 MQFGNLQITCVSEEVTPSFAFREFILTNTNTGEE--RHITQMQYLAWPDHGV-PDDSSDFLDFVKRVR--QNRVGMVE-P 145
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2034231280 1644 VLVHCQDGSSHSGLFTTLAVVCERMEEDGEVDVYRTIKHIKRRRGQIIADYDQFRFCYKAV 1704
Cdd:cd14541    146 TVVHCSAGIGRTGVLITMETAMCLIEANEPVYPLDIVRTMRDQRAMLIQTPSQYRFVCEAI 206
PTPc_motif smart00404
Protein tyrosine phosphatase, catalytic domain motif;
1601-1704 1.96e-20

Protein tyrosine phosphatase, catalytic domain motif;


Pssm-ID: 214649 [Multi-domain]  Cd Length: 105  Bit Score: 87.80  E-value: 1.96e-20
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2034231280  1601 FVRQFQFNAWAEHaMAPQSKTMMLDLVDSVFDWQEeACANERPVLVHCQDGSSHSGLFTTLAVVCERME-EDGEVDVYRT 1679
Cdd:smart00404    1 TVKHYHYTGWPDH-GVPESPDSILELLRAVKKNLN-QSESSGPVVVHCSAGVGRTGTFVAIDILLQQLEaEAGEVDIFDT 78
                            90       100
                    ....*....|....*....|....*
gi 2034231280  1680 IKHIKRRRGQIIADYDQFRFCYKAV 1704
Cdd:smart00404   79 VKELRSQRPGMVQTEEQYLFLYRAL 103
PTPc_DSPc smart00012
Protein tyrosine phosphatase, catalytic domain, undefined specificity; Protein tyrosine ...
1601-1704 1.96e-20

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: 87.80  E-value: 1.96e-20
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2034231280  1601 FVRQFQFNAWAEHaMAPQSKTMMLDLVDSVFDWQEeACANERPVLVHCQDGSSHSGLFTTLAVVCERME-EDGEVDVYRT 1679
Cdd:smart00012    1 TVKHYHYTGWPDH-GVPESPDSILELLRAVKKNLN-QSESSGPVVVHCSAGVGRTGTFVAIDILLQQLEaEAGEVDIFDT 78
                            90       100
                    ....*....|....*....|....*
gi 2034231280  1680 IKHIKRRRGQIIADYDQFRFCYKAV 1704
Cdd:smart00012   79 VKELRSQRPGMVQTEEQYLFLYRAL 103
PTPc-N14 cd14599
catalytic domain of tyrosine-protein phosphatase non-receptor type 14; Tyrosine-protein ...
1459-1708 2.36e-19

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: 90.44  E-value: 2.36e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2034231280 1459 TAQLEINVHKNRYLDVLAADHYRPIL--TSQGPgaqaTDYINAVYVDGYLRRNQ--FIVTQTPLHTTVLDFWRLVWDHDI 1534
Cdd:cd14599     32 TATLPENAERNRIREVVPYEENRVELvpTKENN----TGYINASHIKVTVGGEEwhYIATQGPLPHTCHDFWQMVWEQGV 107
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2034231280 1535 RTIVMVENFKHEDDTRA-EYWPP------AASGGVMKQLEPFFLEtTACYQQENITVRNlrLLSTQHprdpaRFVRQFQF 1607
Cdd:cd14599    108 NVIAMVTAEEEGGRSKShRYWPKlgskhsSATYGKFKVTTKFRTD-SGCYATTGLKVKH--LLSGQE-----RTVWHLQY 179
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2034231280 1608 NAWAEHAMAPQSKTMM--LDLVDSVFDWQEEACANER----PVLVHCQDGSSHSG--LFTTLAVVCerMEEDGEVDVYRT 1679
Cdd:cd14599    180 TDWPDHGCPEEVQGFLsyLEEIQSVRRHTNSMLDSTKncnpPIVVHCSAGVGRTGvvILTELMIGC--LEHNEKVEVPVM 257
                          250       260
                   ....*....|....*....|....*....
gi 2034231280 1680 IKHIKRRRGQIIADYDQFRFCYKAVWDFM 1708
Cdd:cd14599    258 LRHLREQRMFMIQTIAQYKFVYQVLIQFL 286
R-PTP-G-2 cd17670
PTP-like domain of receptor-type tyrosine-protein phosphatase G, repeat 2; Receptor-type ...
1203-1405 7.44e-19

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: 86.66  E-value: 7.44e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2034231280 1203 YVNASFLPGYKKTPAYIAAQSPYnEETVLDFWRLIYQRSIKTVVMITN---VVEDHIVkctqYWPTQTKASFGDIFFLHL 1279
Cdd:cd17670      1 YINASYIMGYYRSNEFIITQHPL-PHTTKDFWRMIWDHNAQIIVMLPDnqgLAEDEFV----YWPSREESMNCEAFTVTL 75
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2034231280 1280 IE-----VNEYADYIIRTIGVKMKGDSDSKIVRLFEFTSWPDhgvPDDPI-PFLDMRYKVRRYQHDSPSPILVHCGTGMA 1353
Cdd:cd17670     76 ISkdrlcLSNEEQIIIHDFILEATQDDYVLEVRHFQCPKWPN---PDAPIsSTFELINVIKEEALTRDGPTIVHDEFGAV 152
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|..
gi 2034231280 1354 RTGVFIAVDALIDQYASEGRVMVYDFVRRLRKDRPFMVRTLKQYVFIYEAIF 1405
Cdd:cd17670    153 SAGTLCALTTLSQQLENENAVDVYQVAKMINLMRPGVFTDIEQYQFLYKAML 204
PTPc-N13 cd14597
catalytic domain of tyrosine-protein phosphatase non-receptor type 13; Tyrosine-protein ...
1465-1704 1.34e-18

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: 86.81  E-value: 1.34e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2034231280 1465 NVHKNRYLDVLAADHYRPILTSQGpgaqatDYINAVYVDGYLRRNQF--IVTQTPLHTTVLDFWRLVWDHDIRTI-VMVE 1541
Cdd:cd14597      3 NRKKNRYKNILPYDTTRVPLGDEG------GYINASFIKMPVGDEEFvyIACQGPLPTTVADFWQMVWEQKSTVIaMMTQ 76
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2034231280 1542 NFKHEDDTRAEYWPPAASGGVMKQlEPFFLETTACYQQENITVRNLRLLSTQhpRDPARFVRQFQFNAWAEHAmAPQSKT 1621
Cdd:cd14597     77 EVEGGKIKCQRYWPEILGKTTMVD-NRLQLTLVRMQQLKNFVIRVLELEDIQ--TREVRHITHLNFTAWPDHD-TPSQPE 152
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2034231280 1622 MMLDLVDSVFDWQEEAcanerPVLVHCQDGSSHSGLFTTLAVVCERMEEDGEVDVYRTIKHIKRRRGQIIADYDQFRFCY 1701
Cdd:cd14597    153 QLLTFISYMRHIHKSG-----PIITHCSAGIGRSGTLICIDVVLGLISKDLDFDISDIVRTMRLQRHGMVQTEDQYIFCY 227

                   ...
gi 2034231280 1702 KAV 1704
Cdd:cd14597    228 QVI 230
PTPc-N4 cd14601
catalytic domain of tyrosine-protein phosphatase non-receptor type 4; Tyrosine-protein ...
1495-1704 3.65e-17

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: 81.92  E-value: 3.65e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2034231280 1495 DYINAVYVDGYLRR----NQFIVTQTPLHTTVLDFWRLVWDHDIRTIVMVENFKHEDDTRA-EYWPPAASGGVMKQLEpf 1569
Cdd:cd14601      1 DYINANYINMEIPSssiiNRYIACQGPLPNTCSDFWQMTWEQGSSMVVMLTTQVERGRVKChQYWPEPSGSSSYGGFQ-- 78
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2034231280 1570 fletTACYQQENITVRNLRLLSTQH-PRDPARFVRQFQFNAWAEHAMaPQSKTMMLDLVDSVfdwQEEACANERPVLVHC 1648
Cdd:cd14601     79 ----VTCHSEEGNPAYVFREMTLTNlEKNESRPLTQIQYIAWPDHGV-PDDSSDFLDFVCLV---RNKRAGKDEPVVVHC 150
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 2034231280 1649 QDGSSHSGLFTTLAVVCERMEEDGEV---DVYRTIKHikrRRGQIIADYDQFRFCYKAV 1704
Cdd:cd14601    151 SAGIGRTGVLITMETAMCLIECNQPVyplDIVRTMRD---QRAMMIQTPSQYRFVCEAI 206
PTPc-N20 cd14596
catalytic domain of tyrosine-protein phosphatase non-receptor type 20; Tyrosine-protein ...
1496-1704 5.33e-17

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: 81.33  E-value: 5.33e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2034231280 1496 YINAVYVDGYL--RRNQFIVTQTPLHTTVLDFWRLVWDHDIRTIVMVENFKHEDDTRAE-YWPPAASggVMKQLEPFFLE 1572
Cdd:cd14596      1 YINASYITMPVgeEELFYIATQGPLPSTIDDFWQMVWENRSDVIAMMTREVERGKVKCHrYWPETLQ--EPMELENYQLR 78
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2034231280 1573 TTACYQQENITVRNLRLlsTQHPRDPARFVRQFQFNAWAEHAmAPQSKTMMLDlvdsvFDWQEEACANERPVLVHCQDGS 1652
Cdd:cd14596     79 LENYQALQYFIIRIIKL--VEKETGENRLIKHLQFTTWPDHG-TPQSSDQLVK-----FICYMRKVHNTGPIVVHCSAGI 150
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|..
gi 2034231280 1653 SHSGLFTTLAVVCERMEEDGEVDVYRTIKHIKRRRGQIIADYDQFRFCYKAV 1704
Cdd:cd14596    151 GRAGVLICVDVLLSLIEKDLSFNIKDIVREMRQQRYGMIQTKDQYLFCYKVV 202
PTPc-N21 cd14598
catalytic domain of tyrosine-protein phosphatase non-receptor type 21; Tyrosine-protein ...
1496-1708 1.77e-16

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: 80.40  E-value: 1.77e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2034231280 1496 YINAVYVDGYLRRNQ--FIVTQTPLHTTVLDFWRLVWDHDIRTIVMV---ENFKHEDDTRaeYWPPAASG------GVMK 1564
Cdd:cd14598      1 YINASHIKVTVGGKEwdYIATQGPLQNTCQDFWQMVWEQGVAIIAMVtaeEEGGREKSFR--YWPRLGSRhntvtyGRFK 78
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2034231280 1565 qLEPFFLETTACYQQENITVRNlrLLSTQHprdpaRFVRQFQFNAWAEHAMAPQSKTMM--LDLVDSV---FDWQEEACA 1639
Cdd:cd14598     79 -ITTRFRTDSGCYATTGLKIKH--LLTGQE-----RTVWHLQYTDWPEHGCPEDLKGFLsyLEEIQSVrrhTNSTIDPKS 150
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2034231280 1640 NERPVLVHCQDGSSHSGLFTTLAVVCERMEEDGEVDVYRTIKHIKRRRGQIIADYDQFRFCYKAVWDFM 1708
Cdd:cd14598    151 PNPPVLVHCSAGVGRTGVVILSEIMIACLEHNEMLDIPRVLDMLRQQRMMMVQTLSQYTFVYKVLIQFL 219
PTPc_plant_PTP1 cd17658
protein tyrosine phosphatase 1 from Arabidopsis thaliana and similar plant PTPs; Arabidopsis ...
1496-1701 8.64e-16

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: 77.89  E-value: 8.64e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2034231280 1496 YINAVYV--DGYLRRNQFIVTQTPLHTTVLDFWRLVWDHDIRTIVMVENFKHEDDTR--AEYWPPAAsgGVMKQLEPFFL 1571
Cdd:cd17658      1 YINASLVetPASESLPKFIATQGPLPHTFEDFWEMVIQQRCPVIIMLTRLVDNYSTAkcADYFPAEE--NESREFGRISV 78
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2034231280 1572 ETTAC-YQQENITVRNLRLLSTQHPrDPARFVRQFQFNAWAEHAMaPQSKTMMLDLVDSVFDWQEeacaNERPVLVHCQD 1650
Cdd:cd17658     79 TNKKLkHSQHSITLRVLEVQYIESE-EPPLSVLHIQYPEWPDHGV-PKDTRSVRELLKRLYGIPP----SAGPIVVHCSA 152
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|...
gi 2034231280 1651 GSSHSGLFTTLAVVCER-MEEDGE-VDVYRTIKHIKRRRGQIIADYDQFRFCY 1701
Cdd:cd17658    153 GIGRTGAYCTIHNTIRRiLEGDMSaVDLSKTVRKFRSQRIGMVQTQDQYIFCY 205
PHA02740 PHA02740
protein tyrosine phosphatase; Provisional
1161-1404 9.01e-13

protein tyrosine phosphatase; Provisional


Pssm-ID: 165107 [Multi-domain]  Cd Length: 298  Bit Score: 71.15  E-value: 9.01e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2034231280 1161 KSQKATDNTARRQGSHLnrfpHLLPYDHSLVQLRpdvtSRGSYVNASFLPGYKKTPAYIAAQSpYNEETVLDFWRLIYQR 1240
Cdd:PHA02740    44 KACAQAENKAKDENLAL----HITRLLHRRIKLF----NDEKVLDARFVDGYDFEQKFICIIN-LCEDACDKFLQALSDN 114
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2034231280 1241 SIKTVVMITNVVEDhivKC-TQYWPTQTK-ASFGDIFFLHLIEVNEYADYIIRTIGVKMKGDSDSKIVRlFEFTSWPDHG 1318
Cdd:PHA02740   115 KVQIIVLISRHADK---KCfNQFWSLKEGcVITSDKFQIETLEIIIKPHFNLTLLSLTDKFGQAQKISH-FQYTAWPADG 190
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2034231280 1319 VPDDPIPFLDMRYKV-------RRYQHDSP-SPILVHCGTGMARTGVFIAVDALIDQYASEGRVMVYDFVRRLRKDRPFM 1390
Cdd:PHA02740   191 FSHDPDAFIDFFCNIddlcadlEKHKADGKiAPIIIDCIDGISSSAVFCVFDICATEFDKTGMLSIANALKKVRQKKYGC 270
                          250
                   ....*....|....
gi 2034231280 1391 VRTLKQYVFIYEAI 1404
Cdd:PHA02740   271 MNCLDDYVFCYHLI 284
PHA02740 PHA02740
protein tyrosine phosphatase; Provisional
1497-1702 2.12e-12

protein tyrosine phosphatase; Provisional


Pssm-ID: 165107 [Multi-domain]  Cd Length: 298  Bit Score: 70.00  E-value: 2.12e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2034231280 1497 INAVYVDGYLRRNQFIVTQTPLHTTVLDFWRLVWDHDIRTIVMVENFKhEDDTRAEYWppAASGGVMKQLEPFFLETTAC 1576
Cdd:PHA02740    79 LDARFVDGYDFEQKFICIINLCEDACDKFLQALSDNKVQIIVLISRHA-DKKCFNQFW--SLKEGCVITSDKFQIETLEI 155
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2034231280 1577 YQQENItvrNLRLLSTQHPRDPARFVRQFQFNAWAEHAMAPQSKTmMLDLVDSVFDW-----QEEACANERPVLVHCQDG 1651
Cdd:PHA02740   156 IIKPHF---NLTLLSLTDKFGQAQKISHFQYTAWPADGFSHDPDA-FIDFFCNIDDLcadleKHKADGKIAPIIIDCIDG 231
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|.
gi 2034231280 1652 SSHSGLFTTLAVVCERMEEDGEVDVYRTIKHIKRRRGQIIADYDQFRFCYK 1702
Cdd:PHA02740   232 ISSSAVFCVFDICATEFDKTGMLSIANALKKVRQKKYGCMNCLDDYVFCYH 282
FU smart00261
Furin-like repeats;
55-96 8.02e-12

Furin-like repeats;


Pssm-ID: 214589 [Multi-domain]  Cd Length: 45  Bit Score: 61.37  E-value: 8.02e-12
                            10        20        30        40
                    ....*....|....*....|....*....|....*....|...
gi 2034231280    55 VCVACDPSCEGCSGEGPTLCTACKIGYRLQAAGCV-VCPEGFY 96
Cdd:smart00261    3 ECKPCHPECATCTGPGPDDCTSCKHGFFLDGGKCVsECPPGTY 45
FU cd00064
Furin-like repeats. Cysteine rich region. Exact function of the domain is not known. Furin is ...
58-104 7.59e-10

Furin-like repeats. Cysteine rich region. Exact function of the domain is not known. Furin is a serine-kinase dependent proprotein processor. Other members of this family include endoproteases and cell surface receptors.


Pssm-ID: 238021 [Multi-domain]  Cd Length: 49  Bit Score: 55.99  E-value: 7.59e-10
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*...
gi 2034231280   58 ACDPSCEGCSGEGPTLCTACKIGYRLQAAGCV-VCPEGFYGINCATEC 104
Cdd:cd00064      1 PCHPSCATCTGPGPDQCTSCRHGFYLDGGTCVsECPEGTYADTEGGVC 48
FN3 cd00063
Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein ...
416-509 1.05e-06

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: 48.65  E-value: 1.05e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2034231280  416 PVAPTamvsGLNVSGITATEAFVTWSNMPCNQqkGPSGNYELELTPVGGNTVRYVLTENRRA----FTGLAPFTEHNVRI 491
Cdd:cd00063      1 PSPPT----NLRVTDVTSTSVTLSWTPPEDDG--GPITGYVVEYREKGSGDWKEVEVTPGSEtsytLTGLKPGTEYEFRV 74
                           90
                   ....*....|....*....
gi 2034231280  492 RYANQVGRGPF-TSREFQT 509
Cdd:cd00063     75 RAVNGGGESPPsESVTVTT 93
PTP_DSP_cys cd14494
cys-based protein tyrosine phosphatase and dual-specificity phosphatase superfamily; This ...
1333-1402 6.73e-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: 46.57  E-value: 6.73e-06
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2034231280 1333 VRRYQHDSPSPILVHCGTGMARTGVFIAVDALIDQYASegrvmVYDFVRRLRKDRPFMVR-TLKQYVFIYE 1402
Cdd:cd14494     48 VLDQAEKPGEPVLVHCKAGVGRTGTLVACYLVLLGGMS-----AEEAVRIVRLIRPGGIPqTIEQLDFLIK 113
fn3 pfam00041
Fibronectin type III domain;
423-503 7.17e-06

Fibronectin type III domain;


Pssm-ID: 394996 [Multi-domain]  Cd Length: 85  Bit Score: 45.87  E-value: 7.17e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2034231280  423 VSGLNVSGITATEAFVTWSnmPCNQQKGPSGNYELELTPVGG----NTVRYVLTENRRAFTGLAPFTEHNVRIRYANQVG 498
Cdd:pfam00041    3 PSNLTVTDVTSTSLTVSWT--PPPDGNGPITGYEVEYRPKNSgepwNEITVPGTTTSVTLTGLKPGTEYEVRVQAVNGGG 80

                   ....*
gi 2034231280  499 RGPFT 503
Cdd:pfam00041   81 EGPPS 85
FN3 smart00060
Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, ...
416-500 7.21e-06

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


Pssm-ID: 214495 [Multi-domain]  Cd Length: 83  Bit Score: 45.68  E-value: 7.21e-06
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2034231280   416 PVAPtamvSGLNVSGITATEAFVTWSNMPCNQQKGPSGNYELELTPVGGNTVRYVLTENRRAFT--GLAPFTEHNVRIRY 493
Cdd:smart00060    1 PSPP----SNLRVTDVTSTSVTLSWEPPPDDGITGYIVGYRVEYREEGSEWKEVNVTPSSTSYTltGLKPGTEYEFRVRA 76

                    ....*..
gi 2034231280   494 ANQVGRG 500
Cdd:smart00060   77 VNGAGEG 83
PTP_DSP_cys cd14494
cys-based protein tyrosine phosphatase and dual-specificity phosphatase superfamily; This ...
1624-1702 1.28e-05

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: 45.80  E-value: 1.28e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2034231280 1624 LDLVDSVFDWQEEACANERPVLVHCQDGSSHSGLFttlaVVCERMEEDGEvDVYRTIKHIKRRRGQIIADY-DQFRFCYK 1702
Cdd:cd14494     39 LAMVDRFLEVLDQAEKPGEPVLVHCKAGVGRTGTL----VACYLVLLGGM-SAEEAVRIVRLIRPGGIPQTiEQLDFLIK 113
VSP pfam03302
Giardia variant-specific surface protein;
38-106 3.43e-05

Giardia variant-specific surface protein;


Pssm-ID: 146106 [Multi-domain]  Cd Length: 397  Bit Score: 48.43  E-value: 3.43e-05
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2034231280   38 KQCEANEYCKERADA----TAVCVACDPSCEGCSGEGpTLCTACKIGYRLQAAGCVVCP--EGFYGINCATEC-NC 106
Cdd:pfam03302  264 KTCTSNTVCTTCMDGyvktSDSCTKCDSSCETCTGAT-TTCKTCATGYYKSGTGCVSCTssESDNGITGVKGClNC 338
FN3 COG3401
Fibronectin type 3 domain [General function prediction only];
385-848 9.84e-05

Fibronectin type 3 domain [General function prediction only];


Pssm-ID: 442628 [Multi-domain]  Cd Length: 603  Bit Score: 47.30  E-value: 9.84e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2034231280  385 VLTWSKYSFTIDAQAETVDVSEVRTLTKISDPVAPTAMVS---GLNVSGITATEAFVTWSNMPCNqqKGPSGNYELELTP 461
Cdd:COG3401      4 SYLTSLDAGIAASAAANTAVNALSKAGGSGKTILVYLAVVlsvTTKESPGTLLVAAGLSSGGGLG--TGGRAGTTSGVAA 81
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2034231280  462 VGGNTVRYVLTENRRAFTGLAPFTEHNVRIRYANQVGRGPFTSREFQTLEGVPTAVQIVSATATSTTITVTFDPPLRTNG 541
Cdd:COG3401     82 VAVAAAPPTATGLTTLTGSGSVGGATNTGLTSSDEVPSPAVGTATTATAVAGGAATAGTYALGAGLYGVDGANASGTTAS 161
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2034231280  542 ILVSYTVTFSTTSDFNETESRTEQGRSG-LRSIIVGRLQADTLYYLKMAASTNAGIGQYGSVTSRRTLEAPPPAEdIDLR 620
Cdd:COG3401    162 SVAGAGVVVSPDTSATAAVATTSLTVTStTLVDGGGDIEPGTTYYYRVAATDTGGESAPSNEVSVTTPTTPPSAP-TGLT 240
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2034231280  621 SDSQTVNCLSLSWDPPQNRAgdiqsykprpptfvrssytnvtlniepvmskyvpITSYRLHvllltnsnRNLPFQSAPGY 700
Cdd:COG3401    241 ATADTPGSVTLSWDPVTESD----------------------------------ATGYRVY--------RSNSGDGPFTK 278
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2034231280  701 ITAELESSavpntiefvigdgevyggYTNQPLESNSNYRIYYVAVSTLNNETT-SNYDSLTlpfptvPFDPALAPPLPLS 779
Cdd:COG3401    279 VATVTTTS------------------YTDTGLTNGTTYYYRVTAVDAAGNESApSNVVSVT------TDLTPPAAPSGLT 334
                          410       420       430       440       450       460
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2034231280  780 LSSRTTECLNLTWVTPTglSPLITSFDFTTSRAGDSDDTPITRSVPATdrAFQQCNLAPFTLYTVRISA 848
Cdd:COG3401    335 ATAVGSSSITLSWTASS--DADVTGYNVYRSTSGGGTYTKIAETVTTT--SYTDTGLTPGTTYYYKVTA 399
FN3 cd00063
Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein ...
774-864 1.01e-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: 42.87  E-value: 1.01e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2034231280  774 PPLPLSLSSRTTECLNLTWVTPTGLSPLITSFDFTTSRAGDSDDTPITrSVPATDRAFQQCNLAPFTLYTVRISARIGQE 853
Cdd:cd00063      3 PPTNLRVTDVTSTSVTLSWTPPEDDGGPITGYVVEYREKGSGDWKEVE-VTPGSETSYTLTGLKPGTEYEFRVRAVNGGG 81
                           90
                   ....*....|..
gi 2034231280  854 VSA-TTTETFLT 864
Cdd:cd00063     82 ESPpSESVTVTT 93
PTP-MTMR3 cd14586
protein tyrosine phosphatase-like domain of myotubularin related phosphoinositide phosphatase ...
1583-1651 1.33e-04

protein tyrosine phosphatase-like domain of myotubularin related phosphoinositide phosphatase 3; Myotubularin related phosphoinositide phosphatase 3 (MTMR3), also known as FYVE domain-containing dual specificity protein phosphatase 1 (FYVE-DSP1) or Zinc finger FYVE domain-containing protein 10 (ZFYVE10), is enzymatically active and contains a C-terminal FYVE domain and an N-terminal PH-GRAM domain. In general, myotubularins are a unique subgroup of protein tyrosine phosphatases that use inositol phospholipids, rather than phosphoproteins, as substrates. They dephosphorylate the D-3 position of phosphatidylinositol 3-phosphate [PI(3)P] and phosphatidylinositol 3,5-bisphosphate [PI(3,5)P2], generating phosphatidylinositol and phosphatidylinositol 5-phosphate [PI(5)P], respectively. Together with phosphoinositide 5-kinase PIKfyve, phosphoinositide 3-phosphatase MTMR3 constitutes a phosphoinositide loop that produces PI(5)P via PI(3,5)P2 and regulates cell migration.


Pssm-ID: 350434  Cd Length: 317  Bit Score: 46.17  E-value: 1.33e-04
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2034231280 1583 TVRNLRLLSTQHPrDPARFVRQFQFNAWAEH-AMAPQSKTMMLDLVDSvfdwqeeacaNERPVLVHCQDG 1651
Cdd:cd14586    190 SFQSLRLLCTQMP-DPANWLSALESTKWLQHlSMLLKSALLVVHAVDR----------DQRPVLVHCSDG 248
PTP_PTPDC1 cd14506
protein tyrosine phosphatase domain of PTP domain-containing protein 1; protein tyrosine ...
1306-1445 1.37e-04

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


Pssm-ID: 350356 [Multi-domain]  Cd Length: 206  Bit Score: 45.03  E-value: 1.37e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2034231280 1306 VRLFEFtSWPDHGVPDdPIPFLDMrYKVRRYQHDSPSPILVHCGTGMARTGVFIAVdALIdqYASegRVMVYDFVRRLRK 1385
Cdd:cd14506     77 IYFYNF-GWKDYGVPS-LTTILDI-VKVMAFALQEGGKVAVHCHAGLGRTGVLIAC-YLV--YAL--RMSADQAIRLVRS 148
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 2034231280 1386 DRPFMVRTLKQYVFIYEaiFEEFHAGdtmidfdLKERYHNWTQKNPRTGKTYLRDQYKLL 1445
Cdd:cd14506    149 KRPNSIQTRGQVLCVRE--FAQFLLP-------LRNVFACPDPKAAVTLRQYLIRQRHLL 199
fn3 pfam00041
Fibronectin type III domain;
774-858 1.59e-04

Fibronectin type III domain;


Pssm-ID: 394996 [Multi-domain]  Cd Length: 85  Bit Score: 42.02  E-value: 1.59e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2034231280  774 PPLPLSLSSRTTECLNLTWVTPTGLSPLITSFDFTTSRAGDSDDtPITRSVPATDRAFQQCNLAPFTLYTVRISARIGQE 853
Cdd:pfam00041    2 APSNLTVTDVTSTSLTVSWTPPPDGNGPITGYEVEYRPKNSGEP-WNEITVPGTTTSVTLTGLKPGTEYEVRVQAVNGGG 80

                   ....*
gi 2034231280  854 VSATT 858
Cdd:pfam00041   81 EGPPS 85
Furin-like pfam00757
Furin-like cysteine rich region;
43-138 3.76e-04

Furin-like cysteine rich region;


Pssm-ID: 395614 [Multi-domain]  Cd Length: 143  Bit Score: 42.42  E-value: 3.76e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2034231280   43 NEYCKERADATAVCvaCDPSCEG-CSGEGPTLCTACKiGYRLQAAgCVV-CPEGFY--GINCATECNCLNKVCDNV---- 114
Cdd:pfam00757   35 PEQCKKRCTKPGEC--CHEQCLGgCTGPNDSDCLACR-HFNDEGT-CVDqCPPGTYqfGWRCVTFKECPKSHLPGYnplv 110
                           90       100       110
                   ....*....|....*....|....*....|....
gi 2034231280  115 --NGACaIWKCKRGYTGI--------PfCRDKCP 138
Cdd:pfam00757  111 ihNGEC-VRECPSGYTEVennsrkceP-CEGLCP 142
EGF_Lam cd00055
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ...
104-145 4.36e-04

Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous components of basement membranes that mediate cell adhesion, growth migration, and differentiation; the laminin-type epidermal growth factor-like module occurs in tandem arrays; the domain contains 4 disulfide bonds (loops a-d) the first three resemble epidermal growth factor (EGF); the number of copies of this domain in the different forms of laminins is highly variable ranging from 3 up to 22 copies


Pssm-ID: 238012  Cd Length: 50  Bit Score: 39.64  E-value: 4.36e-04
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*..
gi 2034231280  104 CNC-----LNKVCDNVNGACaiwKCKRGYTGiPFCrDKCPAGTFGLD 145
Cdd:cd00055      2 CDCnghgsLSGQCDPGTGQC---ECKPNTTG-RRC-DRCAPGYYGLP 43
PTP_YopH-like cd14559
YopH and related bacterial protein tyrosine phosphatases; Yersinia outer protein H (YopH) ...
1306-1398 4.42e-04

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: 43.54  E-value: 4.42e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2034231280 1306 VRLFEFTSWPDHG----------------VPDDPIPFLDMRYKVRRYQHDSPSPIlVHCGTGMARTGVFIAVDALIDQya 1369
Cdd:cd14559    118 IPVVHVTNWPDHTaisseglkeladlvnkSAEEKRNFYKSKGSSAINDKNKLLPV-IHCRAGVGRTGQLAAAMELNKS-- 194
                           90       100       110
                   ....*....|....*....|....*....|
gi 2034231280 1370 sEGRVMVYDFVRRLRKDR-PFMVRTLKQYV 1398
Cdd:cd14559    195 -PNNLSVEDIVSDMRTSRnGKMVQKDEQLD 223
CDC14 COG2453
Protein-tyrosine phosphatase [Signal transduction mechanisms];
1314-1402 5.44e-04

Protein-tyrosine phosphatase [Signal transduction mechanisms];


Pssm-ID: 441989 [Multi-domain]  Cd Length: 140  Bit Score: 41.88  E-value: 5.44e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2034231280 1314 WPDHGVPDDP-----IPFLDMRYKvrryqhdSPSPILVHCGTGMARTGVFIAVDALIDQYASEgrvmvyDFVRRLRKDRP 1388
Cdd:COG2453     55 IPDFGAPDDEqlqeaVDFIDEALR-------EGKKVLVHCRGGIGRTGTVAAAYLVLLGLSAE------EALARVRAARP 121
                           90
                   ....*....|....
gi 2034231280 1389 FMVRTLKQYVFIYE 1402
Cdd:COG2453    122 GAVETPAQRAFLER 135
GF_recep_IV pfam14843
Growth factor receptor domain IV; This is the fourth extracellular domain of receptor tyrosine ...
35-129 6.02e-04

Growth factor receptor domain IV; This is the fourth extracellular domain of receptor tyrosine protein kinases. Interaction between this domain and the furin-like domain (pfam00757) regulates the binding of ligands to the receptor L domains (pfam01030).


Pssm-ID: 464344 [Multi-domain]  Cd Length: 132  Bit Score: 41.59  E-value: 6.02e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2034231280   35 CMLKQCEANEYCKERadataVCVACDPSCEG------CSGEGPTLCTACKiGYRlQAAGCV-VCPEGFYGIN-----CAT 102
Cdd:pfam14843   35 CNILQGEPREYVVNS-----TCVPCHPECLPqngtatCSGPGADNCTKCA-HFR-DGPHCVsSCPSGVLGENdliwkYAD 107
                           90       100
                   ....*....|....*....|....*....
gi 2034231280  103 EcnclNKVCD--NVNgacaiwkCKRGYTG 129
Cdd:pfam14843  108 A----NGVCQpcHPN-------CTQGCTG 125
Furin-like_2 pfam15913
Furin-like repeat, cysteine-rich; The furin-like cysteine rich region has been found in a ...
56-104 6.30e-04

Furin-like repeat, cysteine-rich; The furin-like cysteine rich region has been found in a variety of proteins from eukaryotes that are involved in the mechanism of signal transduction by receptor tyrosine kinases, which involves receptor aggregation.


Pssm-ID: 464939 [Multi-domain]  Cd Length: 102  Bit Score: 40.88  E-value: 6.30e-04
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|.
gi 2034231280   56 CVACD-PSCEGCSGEgpTLCTACKIGYRLQAAGCVV-CPEGFYGINCATEC 104
Cdd:pfam15913   54 CTKCKaENCESCFSK--DFCTKCKEGFYLHKGKCLDtCPEGTAAQNSTMEC 102
VSP pfam03302
Giardia variant-specific surface protein;
30-174 6.84e-04

Giardia variant-specific surface protein;


Pssm-ID: 146106 [Multi-domain]  Cd Length: 397  Bit Score: 44.19  E-value: 6.84e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2034231280   30 KTQTPCMLKQCEANEYCKERADAT----AVCVACDPSCEGCSGEGPTLCTACKIGYRLQ----------AAGCVV-CPEG 94
Cdd:pfam03302   77 KECTVANCKTCEDQGQCQACNDGFyksgDACSPCHESCKTCSGGTASDCTECLTGKALRygndgtkgtcGEGCTTgTGAG 156
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2034231280   95 F------------YGINCATECNC-LNKVCDNvNGACAIWKCKRGYTGIPFCrDKCPAGTFGLD--CALTCHCPVGDTCS 159
Cdd:pfam03302  157 AcktcgltidgtsYCSECATETEYpQNGVCTS-TAARATATCKASSVANGMC-SSCANGYFRMNggCYETTKFPGKSVCE 234
                          170
                   ....*....|....*
gi 2034231280  160 NVNGDCGTGQCAPNY 174
Cdd:pfam03302  235 EANSGGTCQKEAPGY 249
fn3 pfam00041
Fibronectin type III domain;
190-284 2.11e-03

Fibronectin type III domain;


Pssm-ID: 394996 [Multi-domain]  Cd Length: 85  Bit Score: 38.94  E-value: 2.11e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2034231280  190 PEVVSVQCNNITIQWDAfneeDNIGQGPVYAYNVEVRlnqtENGTSGPWQTKQTVLHveggnppklTYRISVSGLEPDKD 269
Cdd:pfam00041    6 LTVTDVTSTSLTVSWTP----PPDGNGPITGYEVEYR----PKNSGEPWNEITVPGT---------TTSVTLTGLKPGTE 68
                           90
                   ....*....|....*.
gi 2034231280  270 YNFRVNTI-GANSGKP 284
Cdd:pfam00041   69 YEVRVQAVnGGGEGPP 84
FN3 cd00063
Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein ...
190-274 3.11e-03

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: 38.63  E-value: 3.11e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2034231280  190 PEVVSVQCNNITIQWDAFNEEDnigqGPVYAYNVEVRlnqteNGTSGPWQTkqtvlhVEGGNPPKLTYRisVSGLEPDKD 269
Cdd:cd00063      7 LRVTDVTSTSVTLSWTPPEDDG----GPITGYVVEYR-----EKGSGDWKE------VEVTPGSETSYT--LTGLKPGTE 69

                   ....*
gi 2034231280  270 YNFRV 274
Cdd:cd00063     70 YEFRV 74
VSP pfam03302
Giardia variant-specific surface protein;
47-180 5.77e-03

Giardia variant-specific surface protein;


Pssm-ID: 146106 [Multi-domain]  Cd Length: 397  Bit Score: 41.11  E-value: 5.77e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2034231280   47 KERADATAVCVAcdPSCEGCSGEGPTLCTACKIGYRL-QAAGCVVCPEGFYGINCATECNClNKVCDnvngACAIWKCKR 125
Cdd:pfam03302   14 KTKCTSSAPCKT--ENCKACSNDKREVCEECNSNNYLtPTSQCIDDCAKIGNYYYTTNANN-KKICK----ECTVANCKT 86
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2034231280  126 -GYTGipfCRDKCPAGTF--GLDCAlTCH----------------CPVGDTCSNVN----GDCGtGQCAPNYGGAGCQ 180
Cdd:pfam03302   87 cEDQG---QCQACNDGFYksGDACS-PCHescktcsggtasdcteCLTGKALRYGNdgtkGTCG-EGCTTGTGAGACK 159
CDC14 COG2453
Protein-tyrosine phosphatase [Signal transduction mechanisms];
1624-1699 7.23e-03

Protein-tyrosine phosphatase [Signal transduction mechanisms];


Pssm-ID: 441989 [Multi-domain]  Cd Length: 140  Bit Score: 38.80  E-value: 7.23e-03
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2034231280 1624 LDLVDSVFDWQEEACANERPVLVHCQDGSSHSGLFTTLAVVcermeEDGeVDVYRTIKHIKRRRGQIIADYDQFRF 1699
Cdd:COG2453     63 DEQLQEAVDFIDEALREGKKVLVHCRGGIGRTGTVAAAYLV-----LLG-LSAEEALARVRAARPGAVETPAQRAF 132
 
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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