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Conserved domains on  [gi|1316060223|ref|XP_023206085|]
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receptor-type tyrosine-protein phosphatase O isoform X2 [Xiphophorus maculatus]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
PTP_DSP_cys super family cl28904
cys-based protein tyrosine phosphatase and dual-specificity phosphatase superfamily; This ...
 928-1172 3.12e-173

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


The actual alignment was detected with superfamily member cd14614:

Pssm-ID: 475123 [Multi-domain]  Cd Length: 245  Bit Score: 510.20  E-value: 3.12e-173
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316060223  928 DLTHDAADLPVNRPKNRYTNILPYDFSRVKLVSMHNDEGADYINANYIPGYRHSKEYIATQGPLPETRNDFWKMVLQQKS 1007
Cdd:cd14614      1 DIPHFAADLPVNRCKNRYTNILPYDFSRVKLVSMHEEEGSDYINANYIPGYNSPQEYIATQGPLPETRNDFWKMVLQQKS 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316060223 1008 PIIVMLTQCNERRRVKCDHYWPFTDEPVMYGDISVEMLSEEGFPEWIIRKFRLGYADETLDVLHLNYTSWPDHGVPTVNA 1087
Cdd:cd14614     81 QIIVMLTQCNEKRRVKCDHYWPFTEEPVAYGDITVEMLSEEEQPDWAIREFRVSYADEVQDVMHFNYTAWPDHGVPTANA 160

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316060223 1088 IESILQFVHIVRQQADRTKDPVIVHCSAGVGRTGTFMALDRLMQHIREHEFVDILGMVSDMRSHRLSMVQTEEQYVFIHQ 1167
Cdd:cd14614    161 AESILQFVQMVRQQAVKSKGPMIIHCSAGVGRTGTFIALDRLLQHIRDHEFVDILGLVSEMRSYRMSMVQTEEQYIFIHQ 240


                   ....*
gi 1316060223 1168 CVLLM 1172
Cdd:cd14614    241 CVQLM 245
fn3 pfam00041
Fibronectin type III domain;
730-802 5.71e-06

Fibronectin type III domain;


:

Pssm-ID: 394996 [Multi-domain]  Cd Length: 85  Bit Score: 45.48  E-value: 5.71e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316060223  730 PPRLLLAVNATHSSVTLLWSE----DGVVDYYQVLCRP---NWASKELKAGEPITStaqvLTVSGLVPSSSYNCSVTSFS 802
Cdd:pfam00041    2 APSNLTVTDVTSTSLTVSWTPppdgNGPITGYEVEYRPknsGEPWNEITVPGTTTS----VTLTGLKPGTEYEVRVQAVN 77
FN3 cd00063
Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein ...
 437-527 3.99e-04

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


:

Pssm-ID: 238020 [Multi-domain]  Cd Length: 93  Bit Score: 40.56  E-value: 3.99e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316060223  437 PQGVSVRLLDSSTAAVSWAPSAQNhNGSLVS-VLSTTCLKPSLSQRMENTYCSEensTSDIISNLTPGAQYRVVVYHTNG 515
Cdd:cd00063      4 PTNLRVTDVTSTSVTLSWTPPEDD-GGPITGyVVEYREKGSGDWKEVEVTPGSE---TSYTLTGLKPGTEYEFRVRAVNG 79

                           90
                   ....*....|..
gi 1316060223  516 PLTSPPSEPVII 527
Cdd:cd00063     80 GGESPPSESVTV 91
FN3 cd00063
Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein ...
 531-631 5.34e-04

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


:

Pssm-ID: 238020 [Multi-domain]  Cd Length: 93  Bit Score: 40.17  E-value: 5.34e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316060223  531 PTGVRELAVYPLGPTAVVLSWQRP--YHVAFRKYILQTFffnpVTLASEWTTYYEIAATASviaTVRVTDLLPAWYYNFR 608
Cdd:cd00063      1 PSPPTNLRVTDVTSTSVTLSWTPPedDGGPITGYVVEYR----EKGSGDWKEVEVTPGSET---SYTLTGLKPGTEYEFR 73

                           90       100
                   ....*....|....*....|....*.
gi 1316060223  609 VSMVT---WGDPpltccdSSTVSFVT 631
Cdd:cd00063     74 VRAVNgggESPP------SESVTVTT 93
FN3 super family cl27307
Fibronectin type 3 domain [General function prediction only];
261-612 1.55e-03

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: 42.68  E-value: 1.55e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316060223  261 PTPRVSFNTTQNVTDSVAVGNGSRAEEEAEPQSYWLDPTEISPADRDEEFVNAVVSEYEDSNEPGSAM-AVPAEVPVLPT 339
Cdd:COG3401     69 TGGRAGTTSGVAAVAVAAAPPTATGLTTLTGSGSVGGATNTGLTSSDEVPSPAVGTATTATAVAGGAAtAGTYALGAGLY 148

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316060223  340 RLPPVLLELRWLPPRPPTSYDGFNVYIYRDGNSTEMATVDENTHEFFTELTEPGT-YRVQVTTLSSSGdcEARESSADTG 418
Cdd:COG3401    149 GVDGANASGTTASSVAGAGVVVSPDTSATAAVATTSLTVTSTTLVDGGGDIEPGTtYYYRVAATDTGG--ESAPSNEVSV 226

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316060223  419 FTFYLSPSgelleelreRPQGVSVRLLDSSTAAVSWAPSAQNH------------NGSLVSVlsttclkpslsqrmenty 486
Cdd:COG3401    227 TTPTTPPS---------APTGLTATADTPGSVTLSWDPVTESDatgyrvyrsnsgDGPFTKV------------------ 279

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316060223  487 cSEENSTSDIISNLTPGA--QYRVVVYHTNGpLTSPPSEP--VIIDIE-PTGVRELAVYPLGPTAVVLSWQRPYHVAFRK 561
Cdd:COG3401    280 -ATVTTTSYTDTGLTNGTtyYYRVTAVDAAG-NESAPSNVvsVTTDLTpPAAPSGLTATAVGSSSITLSWTASSDADVTG 357

                          330       340       350       360       370
                   ....*....|....*....|....*....|....*....|....*....|.
gi 1316060223  562 YILQtfffnpvTLASEWTTYYEIAATASViATVRVTDLLPAWYYNFRVSMV 612
Cdd:COG3401    358 YNVY-------RSTSGGGTYTKIAETVTT-TSYTDTGLTPGTTYYYKVTAV 400
 
Name Accession Description Interval E-value
R-PTPc-O cd14614
catalytic domain of receptor-type tyrosine-protein phosphatase O; Receptor-type ...
 928-1172 3.12e-173

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: 510.20  E-value: 3.12e-173
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316060223  928 DLTHDAADLPVNRPKNRYTNILPYDFSRVKLVSMHNDEGADYINANYIPGYRHSKEYIATQGPLPETRNDFWKMVLQQKS 1007
Cdd:cd14614      1 DIPHFAADLPVNRCKNRYTNILPYDFSRVKLVSMHEEEGSDYINANYIPGYNSPQEYIATQGPLPETRNDFWKMVLQQKS 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316060223 1008 PIIVMLTQCNERRRVKCDHYWPFTDEPVMYGDISVEMLSEEGFPEWIIRKFRLGYADETLDVLHLNYTSWPDHGVPTVNA 1087
Cdd:cd14614     81 QIIVMLTQCNEKRRVKCDHYWPFTEEPVAYGDITVEMLSEEEQPDWAIREFRVSYADEVQDVMHFNYTAWPDHGVPTANA 160

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316060223 1088 IESILQFVHIVRQQADRTKDPVIVHCSAGVGRTGTFMALDRLMQHIREHEFVDILGMVSDMRSHRLSMVQTEEQYVFIHQ 1167
Cdd:cd14614    161 AESILQFVQMVRQQAVKSKGPMIIHCSAGVGRTGTFIALDRLLQHIRDHEFVDILGLVSEMRSYRMSMVQTEEQYIFIHQ 240


                   ....*
gi 1316060223 1168 CVLLM 1172
Cdd:cd14614    241 CVQLM 245
PTPc smart00194
Protein tyrosine phosphatase, catalytic domain;
914-1170 3.21e-114

Protein tyrosine phosphatase, catalytic domain;


Pssm-ID: 214550 [Multi-domain]  Cd Length: 259  Bit Score: 355.81  E-value: 3.21e-114
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316060223   914 KFSLQFEELKSVGL-DLTHDAADLPVNRPKNRYTNILPYDFSRVKLvSMHNDEGADYINANYIPGYRHSKEYIATQGPLP 992
Cdd:smart00194    1 GLEEEFEKLDRLKPdDESCTVAAFPENRDKNRYKDVLPYDHTRVKL-KPPPGEGSDYINASYIDGPNGPKAYIATQGPLP 79

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316060223   993 ETRNDFWKMVLQQKSPIIVMLTQCNERRRVKCDHYWPFT-DEPVMYGDISVEMLSEEGFPEWIIRKFRLGYAD--ETLDV 1069
Cdd:smart00194   80 STVEDFWRMVWEQKVTVIVMLTELVEKGREKCAQYWPDEeGEPLTYGDITVTLKSVEKVDDYTIRTLEVTNTGcsETRTV 159

                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316060223  1070 LHLNYTSWPDHGVPtvNAIESILQFVHIVRQQADRTKDPVIVHCSAGVGRTGTFMALDRLMQHIREHEFVDILGMVSDMR 1149
Cdd:smart00194  160 THYHYTNWPDHGVP--ESPESILDLIRAVRKSQSTSTGPIVVHCSAGVGRTGTFIAIDILLQQLEAGKEVDIFEIVKELR 237

                           250       260
                    ....*....|....*....|.
gi 1316060223  1150 SHRLSMVQTEEQYVFIHQCVL 1170
Cdd:smart00194  238 SQRPGMVQTEEQYIFLYRAIL 258
Y_phosphatase pfam00102
Protein-tyrosine phosphatase;
939-1170 5.36e-105

Protein-tyrosine phosphatase;


Pssm-ID: 459674 [Multi-domain]  Cd Length: 234  Bit Score: 330.36  E-value: 5.36e-105
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316060223  939 NRPKNRYTNILPYDFSRVKLvsMHNDEGADYINANYIPGYRHSKEYIATQGPLPETRNDFWKMVLQQKSPIIVMLTQCNE 1018
Cdd:pfam00102    1 NLEKNRYKDVLPYDHTRVKL--TGDPGPSDYINASYIDGYKKPKKYIATQGPLPNTVEDFWRMVWEEKVTIIVMLTELEE 78

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316060223 1019 RRRVKCDHYWPFT-DEPVMYGDISVEMLSEEG-FPEWIIRKFRL--GYADETLDVLHLNYTSWPDHGVPTVNAieSILQF 1094
Cdd:pfam00102   79 KGREKCAQYWPEEeGESLEYGDFTVTLKKEKEdEKDYTVRTLEVsnGGSEETRTVKHFHYTGWPDHGVPESPN--SLLDL 156

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1316060223 1095 VHIVRQQADRTKD-PVIVHCSAGVGRTGTFMALDRLMQHIREHEFVDILGMVSDMRSHRLSMVQTEEQYVFIHQCVL 1170
Cdd:pfam00102  157 LRKVRKSSLDGRSgPIVVHCSAGIGRTGTFIAIDIALQQLEAEGEVDIFQIVKELRSQRPGMVQTLEQYIFLYDAIL 233
COG5599 COG5599
Protein tyrosine phosphatase [Signal transduction mechanisms];
920-1165 3.38e-47

Protein tyrosine phosphatase [Signal transduction mechanisms];


Pssm-ID: 444335 [Multi-domain]  Cd Length: 282  Bit Score: 170.66  E-value: 3.38e-47
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316060223  920 EELKSVGLDLTHDaaDLPVNRPKNRYTNILPYDFSRVKlvsmhndEGADYINANYIPGYRhSKEYIATQGPLPETRNDFW 999
Cdd:COG5599     25 NELAPSHNDPQYL--QNINGSPLNRFRDIQPYKETALR-------ANLGYLNANYIQVIG-NHRYIATQYPLEEQLEDFF 94

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316060223 1000 KMVLQQKSPIIVMLTQCNE--RRRVKCDHYWPFTDEpvmYG--DISVEMLSEEGFPEWI-IRKFRL---GYADETLDVLH 1071
Cdd:COG5599     95 QMLFDNNTPVLVVLASDDEisKPKVKMPVYFRQDGE---YGkyEVSSELTESIQLRDGIeARTYVLtikGTGQKKIEIPV 171

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316060223 1072 LNYTSWPDHGVPTVNAIESILQFVHIVRQQADRTKDPVIVHCSAGVGRTGTFMALDRLMQHIREHE--FVDILGMVSDMR 1149
Cdd:COG5599    172 LHVKNWPDHGAISAEALKNLADLIDKKEKIKDPDKLLPVVHCRAGVGRTGTLIACLALSKSINALVqiTLSVEEIVIDMR 251

                          250
                   ....*....|....*..
gi 1316060223 1150 SHR-LSMVQTEEQYVFI 1165
Cdd:COG5599    252 TSRnGGMVQTSEQLDVL 268
PHA02738 PHA02738
hypothetical protein; Provisional
 939-1169 1.92e-42

hypothetical protein; Provisional


Pssm-ID: 222923 [Multi-domain]  Cd Length: 320  Bit Score: 158.16  E-value: 1.92e-42
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316060223  939 NRPKNRYTNILPYDFSRVKLVSMHNDegADYINANYIPGYRHSKEYIATQGPLPETRNDFWKMVLQQKSPIIVMLTQCNE 1018
Cdd:PHA02738    49 NRKLNRYLDAVCFDHSRVILPAERNR--GDYINANYVDGFEYKKKFICGQAPTRQTCYDFYRMLWMEHVQIIVMLCKKKE 126

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316060223 1019 RRRVKCDHYWPFTDEPVM-YGDISVEMLSEEGFPEWIIRKFRLGYADE-TLDVLHLNYTSWPDHGVPtvNAIESILQFVH 1096
Cdd:PHA02738   127 NGREKCFPYWSDVEQGSIrFGKFKITTTQVETHPHYVKSTLLLTDGTSaTQTVTHFNFTAWPDHDVP--KNTSEFLNFVL 204

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316060223 1097 IVRQ-QADRTKD------------PVIVHCSAGVGRTGTFMALDRLMQHIREHEFVDILGMVSDMRSHRLSMVQTEEQYV 1163
Cdd:PHA02738   205 EVRQcQKELAQEslqighnrlqppPIVVHCNAGLGRTPCYCVVDISISRFDACATVSIPSIVSSIRNQRYYSLFIPFQYF 284


                   ....*.
gi 1316060223 1164 FIHQCV 1169
Cdd:PHA02738   285 FCYRAV 290
fn3 pfam00041
Fibronectin type III domain;
730-802 5.71e-06

Fibronectin type III domain;


Pssm-ID: 394996 [Multi-domain]  Cd Length: 85  Bit Score: 45.48  E-value: 5.71e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316060223  730 PPRLLLAVNATHSSVTLLWSE----DGVVDYYQVLCRP---NWASKELKAGEPITStaqvLTVSGLVPSSSYNCSVTSFS 802
Cdd:pfam00041    2 APSNLTVTDVTSTSLTVSWTPppdgNGPITGYEVEYRPknsGEPWNEITVPGTTTS----VTLTGLKPGTEYEVRVQAVN 77
FN3 cd00063
Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein ...
 728-816 1.28e-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: 42.10  E-value: 1.28e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316060223  728 PAPPRLLLAVNATHSSVTLLWS----EDGVVDYYQVLCRPNWASKELKAGEPITSTAQVlTVSGLVPSSSYNCSVTSFSY 803
Cdd:cd00063      1 PSPPTNLRVTDVTSTSVTLSWTppedDGGPITGYVVEYREKGSGDWKEVEVTPGSETSY-TLTGLKPGTEYEFRVRAVNG 79

                           90
                   ....*....|....
gi 1316060223  804 SSASRPA-RITVTT 816
Cdd:cd00063     80 GGESPPSeSVTVTT 93
FN3 cd00063
Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein ...
 437-527 3.99e-04

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


Pssm-ID: 238020 [Multi-domain]  Cd Length: 93  Bit Score: 40.56  E-value: 3.99e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316060223  437 PQGVSVRLLDSSTAAVSWAPSAQNhNGSLVS-VLSTTCLKPSLSQRMENTYCSEensTSDIISNLTPGAQYRVVVYHTNG 515
Cdd:cd00063      4 PTNLRVTDVTSTSVTLSWTPPEDD-GGPITGyVVEYREKGSGDWKEVEVTPGSE---TSYTLTGLKPGTEYEFRVRAVNG 79

                           90
                   ....*....|..
gi 1316060223  516 PLTSPPSEPVII 527
Cdd:cd00063     80 GGESPPSESVTV 91
fn3 pfam00041
Fibronectin type III domain;
437-522 4.36e-04

Fibronectin type III domain;


Pssm-ID: 394996 [Multi-domain]  Cd Length: 85  Bit Score: 40.48  E-value: 4.36e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316060223  437 PQGVSVRLLDSSTAAVSWAPSAQnHNGSLVSVLSTtcLKPSLSQRMENTYCSEENSTSDIISNLTPGAQYRVVVYHTNGP 516
Cdd:pfam00041    3 PSNLTVTDVTSTSLTVSWTPPPD-GNGPITGYEVE--YRPKNSGEPWNEITVPGTTTSVTLTGLKPGTEYEVRVQAVNGG 79


                   ....*.
gi 1316060223  517 LTSPPS 522
Cdd:pfam00041   80 GEGPPS 85
FN3 cd00063
Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein ...
 531-631 5.34e-04

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


Pssm-ID: 238020 [Multi-domain]  Cd Length: 93  Bit Score: 40.17  E-value: 5.34e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316060223  531 PTGVRELAVYPLGPTAVVLSWQRP--YHVAFRKYILQTFffnpVTLASEWTTYYEIAATASviaTVRVTDLLPAWYYNFR 608
Cdd:cd00063      1 PSPPTNLRVTDVTSTSVTLSWTPPedDGGPITGYVVEYR----EKGSGDWKEVEVTPGSET---SYTLTGLKPGTEYEFR 73

                           90       100
                   ....*....|....*....|....*.
gi 1316060223  609 VSMVT---WGDPpltccdSSTVSFVT 631
Cdd:cd00063     74 VRAVNgggESPP------SESVTVTT 93
FN3 smart00060
Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, ...
 531-613 6.63e-04

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


Pssm-ID: 214495 [Multi-domain]  Cd Length: 83  Bit Score: 39.91  E-value: 6.63e-04
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316060223   531 PTGVRELAVYPLGPTAVVLSWQRPYHVAFRKYILQtFFFNPVTLASEWTTYYEIAATASVIatvrVTDLLPAWYYNFRVS 610
Cdd:smart00060    1 PSPPSNLRVTDVTSTSVTLSWEPPPDDGITGYIVG-YRVEYREEGSEWKEVNVTPSSTSYT----LTGLKPGTEYEFRVR 75


                    ...
gi 1316060223   611 MVT 613
Cdd:smart00060   76 AVN 78
FN3 smart00060
Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, ...
 437-515 1.26e-03

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


Pssm-ID: 214495 [Multi-domain]  Cd Length: 83  Bit Score: 39.13  E-value: 1.26e-03
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316060223   437 PQGVSVRLLDSSTAAVSWAPSAQNHNGS-LVSVLSTTCLKPSLSQRMENTycseENSTSDIISNLTPGAQYRVVVYHTNG 515
Cdd:smart00060    4 PSNLRVTDVTSTSVTLSWEPPPDDGITGyIVGYRVEYREEGSEWKEVNVT----PSSTSYTLTGLKPGTEYEFRVRAVNG 79
FN3 COG3401
Fibronectin type 3 domain [General function prediction only];
261-612 1.55e-03

Fibronectin type 3 domain [General function prediction only];


Pssm-ID: 442628 [Multi-domain]  Cd Length: 603  Bit Score: 42.68  E-value: 1.55e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316060223  261 PTPRVSFNTTQNVTDSVAVGNGSRAEEEAEPQSYWLDPTEISPADRDEEFVNAVVSEYEDSNEPGSAM-AVPAEVPVLPT 339
Cdd:COG3401     69 TGGRAGTTSGVAAVAVAAAPPTATGLTTLTGSGSVGGATNTGLTSSDEVPSPAVGTATTATAVAGGAAtAGTYALGAGLY 148

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316060223  340 RLPPVLLELRWLPPRPPTSYDGFNVYIYRDGNSTEMATVDENTHEFFTELTEPGT-YRVQVTTLSSSGdcEARESSADTG 418
Cdd:COG3401    149 GVDGANASGTTASSVAGAGVVVSPDTSATAAVATTSLTVTSTTLVDGGGDIEPGTtYYYRVAATDTGG--ESAPSNEVSV 226

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316060223  419 FTFYLSPSgelleelreRPQGVSVRLLDSSTAAVSWAPSAQNH------------NGSLVSVlsttclkpslsqrmenty 486
Cdd:COG3401    227 TTPTTPPS---------APTGLTATADTPGSVTLSWDPVTESDatgyrvyrsnsgDGPFTKV------------------ 279

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316060223  487 cSEENSTSDIISNLTPGA--QYRVVVYHTNGpLTSPPSEP--VIIDIE-PTGVRELAVYPLGPTAVVLSWQRPYHVAFRK 561
Cdd:COG3401    280 -ATVTTTSYTDTGLTNGTtyYYRVTAVDAAG-NESAPSNVvsVTTDLTpPAAPSGLTATAVGSSSITLSWTASSDADVTG 357

                          330       340       350       360       370
                   ....*....|....*....|....*....|....*....|....*....|.
gi 1316060223  562 YILQtfffnpvTLASEWTTYYEIAATASViATVRVTDLLPAWYYNFRVSMV 612
Cdd:COG3401    358 YNVY-------RSTSGGGTYTKIAETVTT-TSYTDTGLTPGTTYYYKVTAV 400
FN3 smart00060
Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, ...
 728-802 1.66e-03

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


Pssm-ID: 214495 [Multi-domain]  Cd Length: 83  Bit Score: 38.75  E-value: 1.66e-03
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1316060223   728 PAPPRLLLAVNATHSSVTLLWS--EDGVVDYYQVLCRPNWASKELKAGE-PITSTAQVLTVSGLVPSSSYNCSVTSFS 802
Cdd:smart00060    1 PSPPSNLRVTDVTSTSVTLSWEppPDDGITGYIVGYRVEYREEGSEWKEvNVTPSSTSYTLTGLKPGTEYEFRVRAVN 78
 
Name Accession Description Interval E-value
R-PTPc-O cd14614
catalytic domain of receptor-type tyrosine-protein phosphatase O; Receptor-type ...
 928-1172 3.12e-173

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: 510.20  E-value: 3.12e-173
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316060223  928 DLTHDAADLPVNRPKNRYTNILPYDFSRVKLVSMHNDEGADYINANYIPGYRHSKEYIATQGPLPETRNDFWKMVLQQKS 1007
Cdd:cd14614      1 DIPHFAADLPVNRCKNRYTNILPYDFSRVKLVSMHEEEGSDYINANYIPGYNSPQEYIATQGPLPETRNDFWKMVLQQKS 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316060223 1008 PIIVMLTQCNERRRVKCDHYWPFTDEPVMYGDISVEMLSEEGFPEWIIRKFRLGYADETLDVLHLNYTSWPDHGVPTVNA 1087
Cdd:cd14614     81 QIIVMLTQCNEKRRVKCDHYWPFTEEPVAYGDITVEMLSEEEQPDWAIREFRVSYADEVQDVMHFNYTAWPDHGVPTANA 160

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316060223 1088 IESILQFVHIVRQQADRTKDPVIVHCSAGVGRTGTFMALDRLMQHIREHEFVDILGMVSDMRSHRLSMVQTEEQYVFIHQ 1167
Cdd:cd14614    161 AESILQFVQMVRQQAVKSKGPMIIHCSAGVGRTGTFIALDRLLQHIRDHEFVDILGLVSEMRSYRMSMVQTEEQYIFIHQ 240


                   ....*
gi 1316060223 1168 CVLLM 1172
Cdd:cd14614    241 CVQLM 245
R3-PTPc cd14548
catalytic domain of R3 subfamily receptor-type tyrosine-protein phosphatases and similar ...
 944-1167 1.54e-126

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: 387.10  E-value: 1.54e-126
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316060223  944 RYTNILPYDFSRVKLVSMHNDEGADYINANYIPGYRHSKEYIATQGPLPETRNDFWKMVLQQKSPIIVMLTQCNERRRVK 1023
Cdd:cd14548      1 RYTNILPYDHSRVKLIPINEEEGSDYINANYIPGYNSPREFIATQGPLPGTKDDFWRMVWEQNSHTIVMLTQCMEKGRVK 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316060223 1024 CDHYWPFTDEPVMYGDISVEMLSEEGFPEWIIRKFRLGYADETLDVLHLNYTSWPDHGVPtvNAIESILQFVHIVRQQAD 1103
Cdd:cd14548     81 CDHYWPFDQDPVYYGDITVTMLSESVLPDWTIREFKLERGDEVRSVRQFHFTAWPDHGVP--EAPDSLLRFVRLVRDYIK 158

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1316060223 1104 RTKDPVIVHCSAGVGRTGTFMALDRLMQHIREHEFVDILGMVSDMRSHRLSMVQTEEQYVFIHQ 1167
Cdd:cd14548    159 QEKGPTIVHCSAGVGRTGTFIALDRLLQQIESEDYVDIFGIVYDLRKHRPLMVQTEAQYIFLHQ 222
PTPc smart00194
Protein tyrosine phosphatase, catalytic domain;
914-1170 3.21e-114

Protein tyrosine phosphatase, catalytic domain;


Pssm-ID: 214550 [Multi-domain]  Cd Length: 259  Bit Score: 355.81  E-value: 3.21e-114
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316060223   914 KFSLQFEELKSVGL-DLTHDAADLPVNRPKNRYTNILPYDFSRVKLvSMHNDEGADYINANYIPGYRHSKEYIATQGPLP 992
Cdd:smart00194    1 GLEEEFEKLDRLKPdDESCTVAAFPENRDKNRYKDVLPYDHTRVKL-KPPPGEGSDYINASYIDGPNGPKAYIATQGPLP 79

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316060223   993 ETRNDFWKMVLQQKSPIIVMLTQCNERRRVKCDHYWPFT-DEPVMYGDISVEMLSEEGFPEWIIRKFRLGYAD--ETLDV 1069
Cdd:smart00194   80 STVEDFWRMVWEQKVTVIVMLTELVEKGREKCAQYWPDEeGEPLTYGDITVTLKSVEKVDDYTIRTLEVTNTGcsETRTV 159

                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316060223  1070 LHLNYTSWPDHGVPtvNAIESILQFVHIVRQQADRTKDPVIVHCSAGVGRTGTFMALDRLMQHIREHEFVDILGMVSDMR 1149
Cdd:smart00194  160 THYHYTNWPDHGVP--ESPESILDLIRAVRKSQSTSTGPIVVHCSAGVGRTGTFIAIDILLQQLEAGKEVDIFEIVKELR 237

                           250       260
                    ....*....|....*....|.
gi 1316060223  1150 SHRLSMVQTEEQYVFIHQCVL 1170
Cdd:smart00194  238 SQRPGMVQTEEQYIFLYRAIL 258
Y_phosphatase pfam00102
Protein-tyrosine phosphatase;
939-1170 5.36e-105

Protein-tyrosine phosphatase;


Pssm-ID: 459674 [Multi-domain]  Cd Length: 234  Bit Score: 330.36  E-value: 5.36e-105
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316060223  939 NRPKNRYTNILPYDFSRVKLvsMHNDEGADYINANYIPGYRHSKEYIATQGPLPETRNDFWKMVLQQKSPIIVMLTQCNE 1018
Cdd:pfam00102    1 NLEKNRYKDVLPYDHTRVKL--TGDPGPSDYINASYIDGYKKPKKYIATQGPLPNTVEDFWRMVWEEKVTIIVMLTELEE 78

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316060223 1019 RRRVKCDHYWPFT-DEPVMYGDISVEMLSEEG-FPEWIIRKFRL--GYADETLDVLHLNYTSWPDHGVPTVNAieSILQF 1094
Cdd:pfam00102   79 KGREKCAQYWPEEeGESLEYGDFTVTLKKEKEdEKDYTVRTLEVsnGGSEETRTVKHFHYTGWPDHGVPESPN--SLLDL 156

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1316060223 1095 VHIVRQQADRTKD-PVIVHCSAGVGRTGTFMALDRLMQHIREHEFVDILGMVSDMRSHRLSMVQTEEQYVFIHQCVL 1170
Cdd:pfam00102  157 LRKVRKSSLDGRSgPIVVHCSAGIGRTGTFIAIDIALQQLEAEGEVDIFQIVKELRSQRPGMVQTLEQYIFLYDAIL 233
R-PTPc-B cd14617
catalytic domain of receptor-type tyrosine-protein phosphatase B; Receptor-type ...
 943-1167 1.36e-97

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: 309.93  E-value: 1.36e-97
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316060223  943 NRYTNILPYDFSRVKLVSMHNDEGADYINANYIPGYRHSKEYIATQGPLPETRNDFWKMVLQQKSPIIVMLTQCNERRRV 1022
Cdd:cd14617      1 NRYNNILPYDSTRVKLSNVDDDPCSDYINASYIPGNNFRREYIATQGPLPGTKDDFWKMVWEQNVHNIVMVTQCVEKGRV 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316060223 1023 KCDHYWPFTDEPVMYGDISVEMLSEEGFPEWIIRKFRLGyADETLD----VLHLNYTSWPDHGVPtvNAIESILQFVHIV 1098
Cdd:cd14617     81 KCDHYWPADQDSLYYGDLIVQMLSESVLPEWTIREFKIC-SEEQLDaprlVRHFHYTVWPDHGVP--ETTQSLIQFVRTV 157

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1316060223 1099 RQQADRTKD--PVIVHCSAGVGRTGTFMALDRLMQHIREHEFVDILGMVSDMRSHRLSMVQTEEQYVFIHQ 1167
Cdd:cd14617    158 RDYINRTPGsgPTVVHCSAGVGRTGTFIALDRILQQLDSKDSVDIYGAVHDLRLHRVHMVQTECQYVYLHQ 228
R-PTPc-J cd14615
catalytic domain of receptor-type tyrosine-protein phosphatase J; Receptor-type ...
 943-1170 5.70e-90

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: 289.41  E-value: 5.70e-90
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316060223  943 NRYTNILPYDFSRVKLvSMHNDEGADYINANYIPGYRHSKEYIATQGPLPETRNDFWKMVLQQKSPIIVMLTQCNERRRV 1022
Cdd:cd14615      1 NRYNNVLPYDISRVKL-SVQSHSTDDYINANYMPGYNSKKEFIAAQGPLPNTVKDFWRMVWEKNVYAIVMLTKCVEQGRT 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316060223 1023 KCDHYWPfTDEPVMYGDISVEMLSEEGFPEWIIRKFRLGYAD--ETLDVLHLNYTSWPDHGVPtvNAIESILQFVHIVRQ 1100
Cdd:cd14615     80 KCEEYWP-SKQKKDYGDITVTMTSEIVLPEWTIRDFTVKNAQtnESRTVRHFHFTSWPDHGVP--ETTDLLINFRHLVRE 156

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1316060223 1101 QADRT--KDPVIVHCSAGVGRTGTFMALDRLMQHIREHEFVDILGMVSDMRSHRLSMVQTEEQYVFIHQCVL 1170
Cdd:cd14615    157 YMKQNppNSPILVHCSAGVGRTGTFIAIDRLIYQIENENVVDVYGIVYDLRMHRPLMVQTEDQYVFLNQCAL 228
PTPc cd00047
catalytic domain of protein tyrosine phosphatases; Protein tyrosine phosphatases (PTP, EC 3.1. ...
 969-1167 1.16e-89

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: 287.26  E-value: 1.16e-89
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316060223  969 YINANYIPGYRHSKEYIATQGPLPETRNDFWKMVLQQKSPIIVMLTQCNERRRVKCDHYWP-FTDEPVMYGDISVEMLSE 1047
Cdd:cd00047      1 YINASYIDGYRGPKEYIATQGPLPNTVEDFWRMVWEQKVSVIVMLTNLVEKGREKCERYWPeEGGKPLEYGDITVTLVSE 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316060223 1048 EGFPEWIIRKFRLGYAD--ETLDVLHLNYTSWPDHGVPTVnaIESILQFVHIVRQQADRTKDPVIVHCSAGVGRTGTFMA 1125
Cdd:cd00047     81 EELSDYTIRTLELSPKGcsESREVTHLHYTGWPDHGVPSS--PEDLLALVRRVRKEARKPNGPIVVHCSAGVGRTGTFIA 158

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|..
gi 1316060223 1126 LDRLMQHIREHEFVDILGMVSDMRSHRLSMVQTEEQYVFIHQ 1167
Cdd:cd00047    159 IDILLERLEAEGEVDVFEIVKALRKQRPGMVQTLEQYEFIYE 200
R-PTPc-LAR-1 cd14553
catalytic domain of LAR family receptor-type tyrosine-protein phosphatases, repeat 1; The LAR ...
 937-1170 1.22e-88

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: 285.83  E-value: 1.22e-88
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316060223  937 PVNRPKNRYTNILPYDFSRVKLVSMHNDEGADYINANYIPGYRHSKEYIATQGPLPETRNDFWKMVLQQKSPIIVMLTQC 1016
Cdd:cd14553      1 EVNKPKNRYANVIAYDHSRVILQPIEGVPGSDYINANYCDGYRKQNAYIATQGPLPETFGDFWRMVWEQRSATIVMMTKL 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316060223 1017 NERRRVKCDHYWPfTDEPVMYGDISVEMLSEEGFPEWIIRKFRL--GYADETLDVLHLNYTSWPDHGVPTVNAieSILQF 1094
Cdd:cd14553     81 EERSRVKCDQYWP-TRGTETYGLIQVTLLDTVELATYTVRTFALhkNGSSEKREVRQFQFTAWPDHGVPEHPT--PFLAF 157

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1316060223 1095 VHIVRQQADRTKDPVIVHCSAGVGRTGTFMALDRLMQHIREHEFVDILGMVSDMRSHRLSMVQTEEQYVFIHQCVL 1170
Cdd:cd14553    158 LRRVKACNPPDAGPIVVHCSAGVGRTGCFIVIDSMLERIKHEKTVDIYGHVTCLRAQRNYMVQTEDQYIFIHDALL 233
R-PTPc-H cd14619
catalytic domain of receptor-type tyrosine-protein phosphatase H; Receptor-type ...
 943-1170 1.05e-87

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: 283.32  E-value: 1.05e-87
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316060223  943 NRYTNILPYDFSRVKLVSMHNDEGADYINANYIPGYRHSKEYIATQGPLPETRNDFWKMVLQQKSPIIVMLTQCNERRRV 1022
Cdd:cd14619      1 NRFRNVLPYDWSRVPLKPIHEEPGSDYINANYMPGYWSSQEFIATQGPLPQTVGDFWRMIWEQQSSTIVMLTNCMEAGRV 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316060223 1023 KCDHYWPFTDEPVMYGDISVEMLSEEGFPEWIIRKFRLGYADE--TLDVLHLNYTSWPDHGVPTvnAIESILQFVHIVRQ 1100
Cdd:cd14619     81 KCEHYWPLDYTPCTYGHLRVTVVSEEVMENWTVREFLLKQVEEqkTLSVRHFHFTAWPDHGVPS--STDTLLAFRRLLRQ 158

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1316060223 1101 QADRTKD--PVIVHCSAGVGRTGTFMALDRLMQHIREHEFVDILGMVSDMRSHRLSMVQTEEQYVFIHQCVL 1170
Cdd:cd14619    159 WLDQTMSggPTVVHCSAGVGRTGTLIALDVLLQQLQSEGLLGPFSFVQKMRENRPLMVQTESQYVFLHQCIL 230
R-PTPc-V cd14618
catalytic domain of receptor-type tyrosine-protein phosphatase V; Receptor-type ...
 943-1170 2.82e-85

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: 276.44  E-value: 2.82e-85
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316060223  943 NRYTNILPYDFSRVKLVSMHNDEGADYINANYIPGYRHSKEYIATQGPLPETRNDFWKMVLQQKSPIIVMLTQCNERRRV 1022
Cdd:cd14618      1 NRYPHVLPYDHSRVRLSQLGGEPHSDYINANFIPGYTSPQEFIATQGPLKKTIEDFWRLVWEQQVCNIIMLTVGMENGRV 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316060223 1023 KCDHYWPFTDEPVMYGDISVEMLSEEGFPEWIIRKFRLGYADETLD--VLHLNYTSWPDHGVPtvNAIESILQFVHIVRQ 1100
Cdd:cd14618     81 LCDHYWPSESTPVSYGHITVHLLAQSSEDEWTRREFKLWHEDLRKErrVKHLHYTAWPDHGIP--ESTSSLMAFRELVRE 158

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1316060223 1101 QADRTKD--PVIVHCSAGVGRTGTFMALDRLMQHIREHEFVDILGMVSDMRSHRLSMVQTEEQYVFIHQCVL 1170
Cdd:cd14618    159 HVQATKGkgPTLVHCSAGVGRSGTFIALDRLLRQLKEEKVVDVFNTVYILRMHRYLMIQTLSQYIFLHSCIL 230
R-PTPc-Q cd14616
catalytic domain of receptor-type tyrosine-protein phosphatase Q; Receptor-type ...
 943-1167 2.41e-79

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: 259.84  E-value: 2.41e-79
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316060223  943 NRYTNILPYDFSRVKLVSMHNDEGADYINANYIPGYRHSKEYIATQGPLPETRNDFWKMVLQQKSPIIVMLTQCNERRRV 1022
Cdd:cd14616      1 NRFPNIKPYNNNRVKLIADAGVPGSDYINASYISGYLCPNEFIATQGPLPGTVGDFWRMVWETRAKTIVMLTQCFEKGRI 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316060223 1023 KCDHYWPFTDEPV-MYGDISVEMLSEEGFPEWIIRKFRLGYADETLDVLHLNYTSWPDHGVPTVNAieSILQFVHIVRQQ 1101
Cdd:cd14616     81 RCHQYWPEDNKPVtVFGDIVITKLMEDVQIDWTIRDLKIERHGDYMMVRQCNFTSWPEHGVPESSA--PLIHFVKLVRAS 158

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1316060223 1102 ADRTKDPVIVHCSAGVGRTGTFMALDRLMQHIREHEFVDILGMVSDMRSHRLSMVQTEEQYVFIHQ 1167
Cdd:cd14616    159 RAHDNTPMIVHCSAGVGRTGVFIALDHLTQHINDHDFVDIYGLVAELRSERMCMVQNLAQYIFLHQ 224
PTPc-KIM cd14547
catalytic domain of the kinase interaction motif (KIM) family of protein-tyrosine phosphatases; ...
 943-1167 6.87e-79

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: 258.48  E-value: 6.87e-79
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316060223  943 NRYTNILPYDFSRVKLVSMHNDEGADYINANYIPGYR-HSKEYIATQGPLPETRNDFWKMVLQQKSPIIVMLTQCNERRr 1021
Cdd:cd14547      1 NRYKTILPNEHSRVCLPSVDDDPLSSYINANYIRGYDgEEKAYIATQGPLPNTVADFWRMVWQEKTPIIVMITNLTEAK- 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316060223 1022 VKCDHYWPFtDEPVMYGDISVEMLSEEGFPEWIIRKFRLGYADETLDVLHLNYTSWPDHGVP-TVNAIESILQFVHIVRQ 1100
Cdd:cd14547     80 EKCAQYWPE-EENETYGDFEVTVQSVKETDGYTVRKLTLKYGGEKRYLKHYWYTSWPDHKTPeAAQPLLSLVQEVEEARQ 158

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1316060223 1101 QADRTKdPVIVHCSAGVGRTGTFMALDRLMQHIREHEFVDILGMVSDMRSHRLSMVQTEEQYVFIHQ 1167
Cdd:cd14547    159 TEPHRG-PIVVHCSAGIGRTGCFIATSIGCQQLREEGVVDVLGIVCQLRLDRGGMVQTAEQYEFVHR 224
PTPc-N9 cd14543
catalytic domain of tyrosine-protein phosphatase non-receptor type 9; Tyrosine-protein ...
 930-1166 1.26e-77

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: 256.91  E-value: 1.26e-77
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316060223  930 THDAADLPVNRPKNRYTNILPYDFSRVKLVSMHNDEGADYINANYIPGYRHSKEYIATQGPLPETRNDFWKMVLQQKSPI 1009
Cdd:cd14543     20 TFLCSLAPANQEKNRYGDVLCLDQSRVKLPKRNGDERTDYINANFMDGYKQKNAYIATQGPLPKTYSDFWRMVWEQKVLV 99

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316060223 1010 IVMLTQCNERRRVKCDHYWPFTDEPVM-YGDISVEMLSEEGFPEWIIRKFRL--GYADETLDVLHLNYTSWPDHGVPTVN 1086
Cdd:cd14543    100 IVMTTRVVERGRVKCGQYWPLEEGSSLrYGDLTVTNLSVENKEHYKKTTLEIhnTETDESRQVTHFQFTSWPDFGVPSSA 179

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316060223 1087 AieSILQFVHIVRQQ--------ADRTKD-----PVIVHCSAGVGRTGTFMALDRLMQHIREHEFVDILGMVSDMRSHRL 1153
Cdd:cd14543    180 A--ALLDFLGEVRQQqalavkamGDRWKGhppgpPIVVHCSAGIGRTGTFCTLDICLSQLEDVGTLNVMQTVRRMRTQRA 257

                          250
                   ....*....|...
gi 1316060223 1154 SMVQTEEQYVFIH 1166
Cdd:cd14543    258 FSIQTPDQYYFCY 270
R-PTPc-F-1 cd14626
catalytic domain of receptor-type tyrosine-protein phosphatase F, repeat 1; Receptor-type ...
 899-1170 1.76e-75

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: 251.11  E-value: 1.76e-75
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316060223  899 DFEAYFKDMSKDSAYKFSLQFEELKSvGLDLTHDAADLPVNRPKNRYTNILPYDFSRVKLVSMHNDEGADYINANYIPGY 978
Cdd:cd14626      2 DLADNIERLKANDGLKFSQEYESIDP-GQQFTWENSNLEVNKPKNRYANVIAYDHSRVILTSVDGVPGSDYINANYIDGY 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316060223  979 RHSKEYIATQGPLPETRNDFWKMVLQQKSPIIVMLTQCNERRRVKCDHYWPFTDEPVmYGDISVEMLSEEGFPEWIIRKF 1058
Cdd:cd14626     81 RKQNAYIATQGPLPETLSDFWRMVWEQRTATIVMMTRLEEKSRVKCDQYWPIRGTET-YGMIQVTLLDTVELATYSVRTF 159

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316060223 1059 RL--GYADETLDVLHLNYTSWPDHGVPTVNAieSILQFVHIVRQQADRTKDPVIVHCSAGVGRTGTFMALDRLMQHIREH 1136
Cdd:cd14626    160 ALykNGSSEKREVRQFQFMAWPDHGVPEYPT--PILAFLRRVKACNPPDAGPMVVHCSAGVGRTGCFIVIDAMLERMKHE 237

                          250       260       270
                   ....*....|....*....|....*....|....
gi 1316060223 1137 EFVDILGMVSDMRSHRLSMVQTEEQYVFIHQCVL 1170
Cdd:cd14626    238 KTVDIYGHVTCMRSQRNYMVQTEDQYIFIHEALL 271
R5-PTPc-1 cd14549
catalytic domain of R5 subfamily receptor-type tyrosine-protein phosphatases, repeat 1; The R5 ...
 969-1166 1.38e-74

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: 245.72  E-value: 1.38e-74
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316060223  969 YINANYIPGYRHSKEYIATQGPLPETRNDFWKMVLQQKSPIIVMLTQCNERRRVKCDHYWPfTDEPVMYGDISVEMLSEE 1048
Cdd:cd14549      1 YINANYVDGYNKARAYIATQGPLPSTFDDFWRMVWEQNSAIIVMITNLVERGRRKCDQYWP-KEGTETYGNIQVTLLSTE 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316060223 1049 GFPEWIIRKFRL---------GYADETLdVLHLNYTSWPDHGVPTVNAieSILQFVHIVRQQADRTKDPVIVHCSAGVGR 1119
Cdd:cd14549     80 VLATYTVRTFSLknlklkkvkGRSSERV-VYQYHYTQWPDHGVPDYTL--PVLSFVRKSSAANPPGAGPIVVHCSAGVGR 156

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*..
gi 1316060223 1120 TGTFMALDRLMQHIREHEFVDILGMVSDMRSHRLSMVQTEEQYVFIH 1166
Cdd:cd14549    157 TGTYIVIDSMLQQIQDKGTVNVFGFLKHIRTQRNYLVQTEEQYIFIH 203
R-PTP-LAR-2 cd14554
PTP-like domain of the LAR family receptor-type tyrosine-protein phosphatases, repeat 2; The ...
 934-1170 1.54e-71

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: 238.58  E-value: 1.54e-71
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316060223  934 ADLPVNRPKNRYTNILPYDFSRVKLVSMHNDEGADYINANYIPGYRHSKEYIATQGPLPETRNDFWKMVLQQKSPIIVML 1013
Cdd:cd14554      1 ANLPCNKFKNRLVNILPYESTRVCLQPIRGVEGSDYINASFIDGYRQRGAYIATQGPLAETTEDFWRMLWEHNSTIIVML 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316060223 1014 TQCNERRRVKCDHYWPfTDEPVMYGDISVEMLSEEGFPEWIIRKFRLGYA--DETLDVLHLNYTSWPDHGVPtvNAIESI 1091
Cdd:cd14554     81 TKLREMGREKCHQYWP-AERSARYQYFVVDPMAEYNMPQYILREFKVTDArdGQSRTVRQFQFTDWPEQGVP--KSGEGF 157

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316060223 1092 LQF---VHIVRQQADRTkDPVIVHCSAGVGRTGTFMALDRLMQHIREHEFVDILGMVSDMRSHRLSMVQTEEQYVFIHQC 1168
Cdd:cd14554    158 IDFigqVHKTKEQFGQE-GPITVHCSAGVGRTGVFITLSIVLERMRYEGVVDVFQTVKLLRTQRPAMVQTEDQYQFCYRA 236


                   ..
gi 1316060223 1169 VL 1170
Cdd:cd14554    237 AL 238
R-PTPc-S-1 cd14625
catalytic domain of receptor-type tyrosine-protein phosphatase S, repeat 1; Receptor-type ...
 894-1170 3.32e-70

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: 236.53  E-value: 3.32e-70
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316060223  894 PVQLDDFEAYFKDMSKDSAYKFSLQFEELKSvGLDLTHDAADLPVNRPKNRYTNILPYDFSRVKLVSMHNDEGADYINAN 973
Cdd:cd14625      3 PIPISELAEHTERLKANDNLKLSQEYESIDP-GQQFTWEHSNLEVNKPKNRYANVIAYDHSRVILQPIEGIMGSDYINAN 81

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316060223  974 YIPGYRHSKEYIATQGPLPETRNDFWKMVLQQKSPIIVMLTQCNERRRVKCDHYWPFTDEPVmYGDISVEMLSEEGFPEW 1053
Cdd:cd14625     82 YIDGYRKQNAYIATQGPLPETFGDFWRMVWEQRSATVVMMTKLEEKSRIKCDQYWPSRGTET-YGMIQVTLLDTIELATF 160

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316060223 1054 IIRKFRL--GYADETLDVLHLNYTSWPDHGVPTVNAieSILQFVHIVRQQADRTKDPVIVHCSAGVGRTGTFMALDRLMQ 1131
Cdd:cd14625    161 CVRTFSLhkNGSSEKREVRQFQFTAWPDHGVPEYPT--PFLAFLRRVKTCNPPDAGPIVVHCSAGVGRTGCFIVIDAMLE 238

                          250       260       270
                   ....*....|....*....|....*....|....*....
gi 1316060223 1132 HIREHEFVDILGMVSDMRSHRLSMVQTEEQYVFIHQCVL 1170
Cdd:cd14625    239 RIKHEKTVDIYGHVTLMRSQRNYMVQTEDQYSFIHDALL 277
R-PTPc-G-1 cd17667
catalytic domain of receptor-type tyrosine-protein phosphatase G, repeat 1; Receptor-type ...
 915-1170 2.46e-69

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: 233.77  E-value: 2.46e-69
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316060223  915 FSLQFEELK--SVGLDLTHDAADLPVNRPKNRYTNILPYDFSRVKLVSM--HNDEGADYINANYIPGYRHSKEYIATQGP 990
Cdd:cd17667      1 FSEDFEEVQrcTADMNITAEHSNHPDNKHKNRYINILAYDHSRVKLRPLpgKDSKHSDYINANYVDGYNKAKAYIATQGP 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316060223  991 LPETRNDFWKMVLQQKSPIIVMLTQCNERRRVKCDHYWPfTDEPVMYGDISVEMLSEEGFPEWIIRKFRL---------- 1060
Cdd:cd17667     81 LKSTFEDFWRMIWEQNTGIIVMITNLVEKGRRKCDQYWP-TENSEEYGNIIVTLKSTKIHACYTVRRFSIrntkvkkgqk 159

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316060223 1061 ----GYADETLdVLHLNYTSWPDHGVPTVNAieSILQFVHivRQQADRTKD--PVIVHCSAGVGRTGTFMALDRLMQHIR 1134
Cdd:cd17667    160 gnpkGRQNERT-VIQYHYTQWPDMGVPEYAL--PVLTFVR--RSSAARTPEmgPVLVHCSAGVGRTGTYIVIDSMLQQIK 234

                          250       260       270
                   ....*....|....*....|....*....|....*.
gi 1316060223 1135 EHEFVDILGMVSDMRSHRLSMVQTEEQYVFIHQCVL 1170
Cdd:cd17667    235 DKSTVNVLGFLKHIRTQRNYLVQTEEQYIFIHDALL 270
PTP_fungal cd18533
fungal protein tyrosine phosphatases; This subfamily contains Saccharomyces cerevisiae ...
 969-1167 5.71e-69

fungal protein tyrosine phosphatases; This subfamily contains Saccharomyces cerevisiae protein-tyrosine phosphatases 1 (PTP1) and 2 (PTP2), Schizosaccharomyces pombe PTP1, PTP2, and PTP3, and similar fungal proteins. PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides; they regulate phosphotyrosine levels in signal transduction pathways. PTP2, together with PTP3, is the major phosphatase that dephosphorylates and inactivates the MAP kinase HOG1 and also modulates its subcellular localization.


Pssm-ID: 350509 [Multi-domain]  Cd Length: 212  Bit Score: 230.21  E-value: 5.71e-69
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316060223  969 YINANYI-PGYRHSKEYIATQGPLPETRNDFWKMVLQQKSPIIVMLTQCNERRRVKCDHYWPFTDEPVMYGDISVEMLSE 1047
Cdd:cd18533      1 YINASYItLPGTSSKRYIATQGPLPATIGDFWKMIWQNNVGVIVMLTPLVENGREKCDQYWPSGEYEGEYGDLTVELVSE 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316060223 1048 EGFPEW--IIRKFRLGYADETL-DVLHLNYTSWPDHGVP-TVNAIESILQFVHIVRQQADRTKdPVIVHCSAGVGRTGTF 1123
Cdd:cd18533     81 EENDDGgfIVREFELSKEDGKVkKVYHIQYKSWPDFGVPdSPEDLLTLIKLKRELNDSASLDP-PIIVHCSAGVGRTGTF 159

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|...
gi 1316060223 1124 MALDRLMQHIREHEFVD---------ILGMVSDMRSHRLSMVQTEEQYVFIHQ 1167
Cdd:cd18533    160 IALDSLLDELKRGLSDSqdledsedpVYEIVNQLRKQRMSMVQTLRQYIFLYD 212
R-PTPc-D-1 cd14624
catalytic domain of receptor-type tyrosine-protein phosphatase D, repeat 1; Receptor-type ...
 894-1170 1.32e-68

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: 231.93  E-value: 1.32e-68
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316060223  894 PVQLDDFEAYFKDMSKDSAYKFSLQFEELKSvGLDLTHDAADLPVNRPKNRYTNILPYDFSRVKLVSMHNDEGADYINAN 973
Cdd:cd14624      3 PIPILELADHIERLKANDNLKFSQEYESIDP-GQQFTWEHSNLEVNKPKNRYANVIAYDHSRVLLSAIEGIPGSDYINAN 81

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316060223  974 YIPGYRHSKEYIATQGPLPETRNDFWKMVLQQKSPIIVMLTQCNERRRVKCDHYWPfTDEPVMYGDISVEMLSEEGFPEW 1053
Cdd:cd14624     82 YIDGYRKQNAYIATQGALPETFGDFWRMIWEQRSATVVMMTKLEERSRVKCDQYWP-SRGTETYGLIQVTLLDTVELATY 160

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316060223 1054 IIRKFRL--GYADETLDVLHLNYTSWPDHGVPtvNAIESILQFVHIVRQQADRTKDPVIVHCSAGVGRTGTFMALDRLMQ 1131
Cdd:cd14624    161 CVRTFALykNGSSEKREVRQFQFTAWPDHGVP--EHPTPFLAFLRRVKTCNPPDAGPMVVHCSAGVGRTGCFIVIDAMLE 238

                          250       260       270
                   ....*....|....*....|....*....|....*....
gi 1316060223 1132 HIREHEFVDILGMVSDMRSHRLSMVQTEEQYVFIHQCVL 1170
Cdd:cd14624    239 RIKHEKTVDIYGHVTLMRAQRNYMVQTEDQYIFIHDALL 277
PTPc-N18 cd14603
catalytic domain of tyrosine-protein phosphatase non-receptor type 18; Tyrosine-protein ...
 929-1173 3.90e-68

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: 230.10  E-value: 3.90e-68
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316060223  929 LTHDAADLPVNRPKNRYTNILPYDFSRVKLVSMHNDEGADYINANYIPGYRHSKEYIATQGPLPETRNDFWKMVLQQKSP 1008
Cdd:cd14603     20 CSTVAGGRKENVKKNRYKDILPYDQTRVILSLLQEEGHSDYINANFIKGVDGSRAYIATQGPLSHTVLDFWRMIWQYGVK 99

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316060223 1009 IIVMLTQCNERRRVKCDHYWPFTDEPVMYGDISVEMLSEEGF-PEWIIRKFRLGYADETLDVLHLNYTSWPDHGVPtvNA 1087
Cdd:cd14603    100 VILMACREIEMGKKKCERYWAQEQEPLQTGPFTITLVKEKRLnEEVILRTLKVTFQKESRSVSHFQYMAWPDHGIP--DS 177

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316060223 1088 IESILQFVHIVRQQADRTKDPVIVHCSAGVGRTGTFMALDR-----LMQHIREHefVDILGMVSDMRSHRLSMVQTEEQY 1162
Cdd:cd14603    178 PDCMLAMIELARRLQGSGPEPLCVHCSAGCGRTGVICTVDYvrqllLTQRIPPD--FSIFDVVLEMRKQRPAAVQTEEQY 255

                          250
                   ....*....|.
gi 1316060223 1163 VFIHQCVLLMW 1173
Cdd:cd14603    256 EFLYHTVAQMF 266
PTPc-N11_6 cd14544
catalytic domain of tyrosine-protein phosphatase non-receptor type 11 and type 6; ...
 939-1169 5.12e-67

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: 226.19  E-value: 5.12e-67
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316060223  939 NRPKNRYTNILPYDFSRVKLVSMHNDE-GADYINANYI-------PGYRHSKEYIATQGPLPETRNDFWKMVLQQKSPII 1010
Cdd:cd14544      1 NKGKNRYKNILPFDHTRVILKDRDPNVpGSDYINANYIrnenegpTTDENAKTYIATQGCLENTVSDFWSMVWQENSRVI 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316060223 1011 VMLTQCNERRRVKCDHYWPFTDEPVMYGDISVEMLSEEGFPEWIIRKF---RLGYADETLDVLHLNYTSWPDHGVPtvNA 1087
Cdd:cd14544     81 VMTTKEVERGKNKCVRYWPDEGMQKQYGPYRVQNVSEHDTTDYTLRELqvsKLDQGDPIREIWHYQYLSWPDHGVP--SD 158

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316060223 1088 IESILQFVHIV--RQQADRTKDPVIVHCSAGVGRTGTFMALDRLMQHIREHEF---VDILGMVSDMRSHRLSMVQTEEQY 1162
Cdd:cd14544    159 PGGVLNFLEDVnqRQESLPHAGPIVVHCSAGIGRTGTFIVIDMLLDQIKRKGLdcdIDIQKTIQMVRSQRSGMVQTEAQY 238


                   ....*..
gi 1316060223 1163 VFIHQCV 1169
Cdd:cd14544    239 KFIYVAV 245
R-PTPc-T-1 cd14630
catalytic domain of receptor-type tyrosine-protein phosphatase T, repeat 1; Receptor-type ...
 939-1170 1.37e-66

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


Pssm-ID: 350478 [Multi-domain]  Cd Length: 237  Bit Score: 224.52  E-value: 1.37e-66
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316060223  939 NRPKNRYTNILPYDFSRVKLVSMHNDEGADYINANYIPGYRHSKEYIATQGPLPETRNDFWKMVLQQKSPIIVMLTQCNE 1018
Cdd:cd14630      3 NRNKNRYGNIISYDHSRVRLQLLDGDPHSDYINANYIDGYHRPRHYIATQGPMQETVKDFWRMIWQENSASVVMVTNLVE 82

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316060223 1019 RRRVKCDHYWPftDEPVMYGDISVEMLSEEGFPEWIIRKF---RLGYaDETLDVLHLNYTSWPDHGVPTVNAieSILQFV 1095
Cdd:cd14630     83 VGRVKCVRYWP--DDTEVYGDIKVTLIETEPLAEYVIRTFtvqKKGY-HEIREIRQFHFTSWPDHGVPCYAT--GLLGFV 157

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1316060223 1096 HIVRQQADRTKDPVIVHCSAGVGRTGTFMALDRLMQHIREHEFVDILGMVSDMRSHRLSMVQTEEQYVFIHQCVL 1170
Cdd:cd14630    158 RQVKFLNPPDAGPIVVHCSAGAGRTGCFIAIDIMLDMAENEGVVDIFNCVRELRAQRVNMVQTEEQYVFVHDAIL 232
PTPc-N3_4 cd14541
catalytic domain of tyrosine-protein phosphatase non-receptor type 21 and type 14; ...
 968-1170 8.28e-65

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: 218.35  E-value: 8.28e-65
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316060223  968 DYINANY----IPGYRHSKEYIATQGPLPETRNDFWKMVLQQKSPIIVMLTQCNERRRVKCDHYWPFTDEPVMYGDISVE 1043
Cdd:cd14541      1 DYINANYvnmeIPGSGIVNRYIAAQGPLPNTCADFWQMVWEQKSTLIVMLTTLVERGRVKCHQYWPDLGETMQFGNLQIT 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316060223 1044 MLSEEGFPEWIIRKFRL--GYADETLDVLHLNYTSWPDHGVPTVNAieSILQFVHIVRQQADRTKDPVIVHCSAGVGRTG 1121
Cdd:cd14541     81 CVSEEVTPSFAFREFILtnTNTGEERHITQMQYLAWPDHGVPDDSS--DFLDFVKRVRQNRVGMVEPTVVHCSAGIGRTG 158

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*....
gi 1316060223 1122 TFMALDRLMQHIREHEFVDILGMVSDMRSHRLSMVQTEEQYVFIHQCVL 1170
Cdd:cd14541    159 VLITMETAMCLIEANEPVYPLDIVRTMRDQRAMLIQTPSQYRFVCEAIL 207
R-PTPc-M-1 cd14633
catalytic domain of receptor-type tyrosine-protein phosphatase M, repeat 1; Receptor-type ...
 899-1170 9.39e-64

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: 217.99  E-value: 9.39e-64
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316060223  899 DFEAYFKDMSKDSAYKFSLQFEELKSvGLDLTHDAADLPVNRPKNRYTNILPYDFSRVKLVSMHNDEGADYINANYIPGY 978
Cdd:cd14633      1 DLLQHITQMKCAEGYGFKEEYESFFE-GQSAPWDSAKKDENRMKNRYGNIIAYDHSRVRLQPIEGETSSDYINGNYIDGY 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316060223  979 RHSKEYIATQGPLPETRNDFWKMVLQQKSPIIVMLTQCNERRRVKCDHYWPftDEPVMYGDISVEMLSEEGFPEWIIRKF 1058
Cdd:cd14633     80 HRPNHYIATQGPMQETIYDFWRMVWHENTASIIMVTNLVEVGRVKCCKYWP--DDTEIYKDIKVTLIETELLAEYVIRTF 157

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316060223 1059 RLGY--ADETLDVLHLNYTSWPDHGVPTvnAIESILQFVHIVRQQADRTKDPVIVHCSAGVGRTGTFMALDRLMQHIREH 1136
Cdd:cd14633    158 AVEKrgVHEIREIRQFHFTGWPDHGVPY--HATGLLGFVRQVKSKSPPNAGPLVVHCSAGAGRTGCFIVIDIMLDMAERE 235

                          250       260       270
                   ....*....|....*....|....*....|....
gi 1316060223 1137 EFVDILGMVSDMRSHRLSMVQTEEQYVFIHQCVL 1170
Cdd:cd14633    236 GVVDIYNCVRELRSRRVNMVQTEEQYVFIHDAIL 269
PTPc-N7 cd14612
catalytic domain of tyrosine-protein phosphatase non-receptor type 7; Tyrosine-protein ...
 935-1171 2.53e-63

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: 215.47  E-value: 2.53e-63
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316060223  935 DLPVNRPKNRYTNILPYDFSRVKLVS-MHNDEGADYINANYIPGYR-HSKEYIATQGPLPETRNDFWKMVLQQKSPIIVM 1012
Cdd:cd14612     11 DIPGHASKDRYKTILPNPQSRVCLRRaGSQEEEGSYINANYIRGYDgKEKAYIATQGPMLNTVSDFWEMVWQEECPIIVM 90

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316060223 1013 LTQCNERRRvKCDHYWPftDEPVMYGDISVEMLSEEGFPEWIIRKFRLGYADETLDVLHLNYTSWPDHGVPtvNAIESIL 1092
Cdd:cd14612     91 ITKLKEKKE-KCVHYWP--EKEGTYGRFEIRVQDMKECDGYTIRDLTIQLEEESRSVKHYWFSSWPDHQTP--ESAGPLL 165

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316060223 1093 QFVHIV--RQQADRTKDPVIVHCSAGVGRTGTFMALDRLMQHIREHEFVDILGMVSDMRSHRLSMVQTEEQYVFIHQCVL 1170
Cdd:cd14612    166 RLVAEVeeSRQTAASPGPIVVHCSAGIGRTGCFIATSIGCQQLKDTGKVDILGIVCQLRLDRGGMIQTSEQYQFLHHTLA 245


                   .
gi 1316060223 1171 L 1171
Cdd:cd14612    246 L 246
R-PTPc-C-1 cd14557
catalytic domain of receptor-type tyrosine-protein phosphatase C, repeat 1; Receptor-type ...
 969-1167 1.45e-61

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: 208.91  E-value: 1.45e-61
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316060223  969 YINANYIPGYRHSKEYIATQGPLPETRNDFWKMVLQQKSPIIVMLTQCNERRRVKCDHYWPFTDE-PVMYGDISVEMLSE 1047
Cdd:cd14557      1 YINASYIDGFKEPRKYIAAQGPKDETVDDFWRMIWEQKSTVIVMVTRCEEGNRNKCAQYWPSMEEgSRAFGDVVVKINEE 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316060223 1048 EGFPEWIIRKFRLGYADETL---DVLHLNYTSWPDHGVPTVNAIesILQFVHIVRQQADRTKDPVIVHCSAGVGRTGTFM 1124
Cdd:cd14557     81 KICPDYIIRKLNINNKKEKGsgrEVTHIQFTSWPDHGVPEDPHL--LLKLRRRVNAFNNFFSGPIVVHCSAGVGRTGTYI 158

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|...
gi 1316060223 1125 ALDRLMQHIREHEFVDILGMVSDMRSHRLSMVQTEEQYVFIHQ 1167
Cdd:cd14557    159 GIDAMLEGLEAEGRVDVYGYVVKLRRQRCLMVQVEAQYILIHQ 201
PTPc-N3 cd14600
catalytic domain of tyrosine-protein phosphatase non-receptor type 3; Tyrosine-protein ...
 917-1175 2.29e-61

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: 211.25  E-value: 2.29e-61
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316060223  917 LQFEEL--KSVGLDLThdAADLPVNRPKNRYTNILPYDFSRVKLvsmhnDEGADYINANY----IPGYRHSKEYIATQGP 990
Cdd:cd14600     18 IQFEQLyrKKPGLAIT--CAKLPQNMDKNRYKDVLPYDATRVVL-----QGNEDYINASYvnmeIPSANIVNKYIATQGP 90

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316060223  991 LPETRNDFWKMVLQQKSPIIVMLTQCNERRRVKCDHYWPFTDEPVMYGDISVEMLSEEGFPEWIIRKFRLGYAD--ETLD 1068
Cdd:cd14600     91 LPHTCAQFWQVVWEQKLSLIVMLTTLTERGRTKCHQYWPDPPDVMEYGGFRVQCHSEDCTIAYVFREMLLTNTQtgEERT 170

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316060223 1069 VLHLNYTSWPDHGVPTVNAieSILQFVHIVRQQadRTKD-PVIVHCSAGVGRTGTFMALDRLMQHIREHEFVDILGMVSD 1147
Cdd:cd14600    171 VTHLQYVAWPDHGVPDDSS--DFLEFVNYVRSK--RVENePVLVHCSAGIGRTGVLVTMETAMCLTERNQPVYPLDIVRK 246

                          250       260
                   ....*....|....*....|....*...
gi 1316060223 1148 MRSHRLSMVQTEEQYVFIHQCVLLMWQK 1175
Cdd:cd14600    247 MRDQRAMMVQTSSQYKFVCEAILRVYEE 274
PTPc-N12 cd14604
catalytic domain of tyrosine-protein phosphatase non-receptor type 12; Tyrosine-protein ...
 939-1176 8.07e-61

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: 210.56  E-value: 8.07e-61
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316060223  939 NRPKNRYTNILPYDFSRVKLVSMHNDEGADYINANYIPGYRHSKEYIATQGPLPETRNDFWKMVLQQKSPIIVMLTQCNE 1018
Cdd:cd14604     57 NVKKNRYKDILPFDHSRVKLTLKTSSQDSDYINANFIKGVYGPKAYIATQGPLANTVIDFWRMIWEYNVAIIVMACREFE 136

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316060223 1019 RRRVKCDHYWP-FTDEPVMYGDISVEMLSEEGFPEWIIRKFRLGYADETLDVLHLNYTSWPDHGVPTvnAIESILQFVHI 1097
Cdd:cd14604    137 MGRKKCERYWPlYGEEPMTFGPFRISCEAEQARTDYFIRTLLLEFQNETRRLYQFHYVNWPDHDVPS--SFDSILDMISL 214

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316060223 1098 VRQQADRTKDPVIVHCSAGVGRTGTFMALD---RLMQHIREHEFVDILGMVSDMRSHRLSMVQTEEQYVFIHQCVLLMWQ 1174
Cdd:cd14604    215 MRKYQEHEDVPICIHCSAGCGRTGAICAIDytwNLLKAGKIPEEFNVFNLIQEMRTQRHSAVQTKEQYELVHRAIAQLFE 294


                   ..
gi 1316060223 1175 KK 1176
Cdd:cd14604    295 KQ 296
R-PTPc-E-1 cd14620
catalytic domain of receptor-type tyrosine-protein phosphatase E, repeat 1; Receptor-type ...
 945-1170 1.32e-60

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: 207.10  E-value: 1.32e-60
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316060223  945 YTNILPYDFSRVKLVSMHNDEGADYINANYIPGYRHSKEYIATQGPLPETRNDFWKMVLQQKSPIIVMLTQCNERRRVKC 1024
Cdd:cd14620      1 YPNILPYDHSRVILSQLDGIPCSDYINASYIDGYKEKNKFIAAQGPKQETVNDFWRMVWEQKSATIVMLTNLKERKEEKC 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316060223 1025 DHYWPftDEPV-MYGDISVEMLSEEGFPEWIIRKFRLGYADETLD-----VLHLNYTSWPDHGVPTVNAieSILQFVHIV 1098
Cdd:cd14620     81 YQYWP--DQGCwTYGNIRVAVEDCVVLVDYTIRKFCIQPQLPDGCkaprlVTQLHFTSWPDFGVPFTPI--GMLKFLKKV 156

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1316060223 1099 RQQADRTKDPVIVHCSAGVGRTGTFMALDRLMQHIREHEFVDILGMVSDMRSHRLSMVQTEEQYVFIHQCVL 1170
Cdd:cd14620    157 KSVNPVHAGPIVVHCSAGVGRTGTFIVIDAMIDMMHAEQKVDVFEFVSRIRNQRPQMVQTDMQYSFIYQALL 228
R-PTPc-A-1 cd14621
catalytic domain of receptor-type tyrosine-protein phosphatase A, repeat 1; Receptor-type ...
 894-1170 5.19e-60

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: 207.95  E-value: 5.19e-60
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316060223  894 PVQLDDFEAYFKDMSKDSAYKFSLQFEELKSVGLDLTHDAADLPVNRPKNRYTNILPYDFSRVKLVSMHNDEGADYINAN 973
Cdd:cd14621      7 PLPVDKLEEEINRRMADDNKLFREEFNALPACPIQATCEAASKEENKEKNRYVNILPYDHSRVHLTPVEGVPDSDYINAS 86

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316060223  974 YIPGYRHSKEYIATQGPLPETRNDFWKMVLQQKSPIIVMLTQCNERRRVKCDHYWPftDEPV-MYGDISVEMLSEEGFPE 1052
Cdd:cd14621     87 FINGYQEKNKFIAAQGPKEETVNDFWRMIWEQNTATIVMVTNLKERKECKCAQYWP--DQGCwTYGNIRVSVEDVTVLVD 164

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316060223 1053 WIIRKFRLGYADETLD------VLHLNYTSWPDHGVPTVNAieSILQFVHIVRQQADRTKDPVIVHCSAGVGRTGTFMAL 1126
Cdd:cd14621    165 YTVRKFCIQQVGDVTNkkpqrlITQFHFTSWPDFGVPFTPI--GMLKFLKKVKNCNPQYAGAIVVHCSAGVGRTGTFIVI 242

                          250       260       270       280
                   ....*....|....*....|....*....|....*....|....
gi 1316060223 1127 DRLMQHIREHEFVDILGMVSDMRSHRLSMVQTEEQYVFIHQCVL 1170
Cdd:cd14621    243 DAMLDMMHAERKVDVYGFVSRIRAQRCQMVQTDMQYVFIYQALL 286
PTPc-N20_13 cd14538
catalytic domain of tyrosine-protein phosphatase non-receptor type 20 and type 13; ...
 969-1170 2.21e-59

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


Pssm-ID: 350386 [Multi-domain]  Cd Length: 207  Bit Score: 202.60  E-value: 2.21e-59
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316060223  969 YINANYI--PGYRHSKEYIATQGPLPETRNDFWKMVLQQKSPIIVMLTQCNERRRVKCDHYWP-FTDEPVM-YGDISVEM 1044
Cdd:cd14538      1 YINASHIriPVGGDTYHYIACQGPLPNTTGDFWQMVWEQKSEVIAMVTQDVEGGKVKCHRYWPdSLNKPLIcGGRLEVSL 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316060223 1045 LSEEGFPEWIIRKFRLGYAD--ETLDVLHLNYTSWPDHGVPtVNAIeSILQFVHIVRQQAdrTKDPVIVHCSAGVGRTGT 1122
Cdd:cd14538     81 EKYQSLQDFVIRRISLRDKEtgEVHHITHLNFTTWPDHGTP-QSAD-PLLRFIRYMRRIH--NSGPIVVHCSAGIGRTGV 156

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*...
gi 1316060223 1123 FMALDRLMQHIREHEFVDILGMVSDMRSHRLSMVQTEEQYVFIHQCVL 1170
Cdd:cd14538    157 LITIDVALGLIERDLPFDIQDIVKDLREQRQGMIQTKDQYIFCYKACL 204
R-PTP-S-2 cd14627
PTP-like domain of receptor-type tyrosine-protein phosphatase S, repeat 2; Receptor-type ...
 933-1170 3.22e-59

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: 205.74  E-value: 3.22e-59
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316060223  933 AADLPVNRPKNRYTNILPYDFSRVKLVSMHNDEGADYINANYIPGYRHSKEYIATQGPLPETRNDFWKMVLQQKSPIIVM 1012
Cdd:cd14627     47 SANLPCNKFKNRLVNIMPYETTRVCLQPIRGVEGSDYINASFIDGYRQQKAYIATQGPLAETTEDFWRMLWENNSTIVVM 126

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316060223 1013 LTQCNERRRVKCDHYWPfTDEPVMYGDISVEMLSEEGFPEWIIRKFRLGYA--DETLDVLHLNYTSWPDHGVPTVNaiES 1090
Cdd:cd14627    127 LTKLREMGREKCHQYWP-AERSARYQYFVVDPMAEYNMPQYILREFKVTDArdGQSRTVRQFQFTDWPEQGVPKSG--EG 203

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316060223 1091 ILQF---VHIVRQQADRtKDPVIVHCSAGVGRTGTFMALDRLMQHIREHEFVDILGMVSDMRSHRLSMVQTEEQYVFIHQ 1167
Cdd:cd14627    204 FIDFigqVHKTKEQFGQ-DGPISVHCSAGVGRTGVFITLSIVLERMRYEGVVDIFQTVKMLRTQRPAMVQTEDEYQFCYQ 282


                   ...
gi 1316060223 1168 CVL 1170
Cdd:cd14627    283 AAL 285
PTPc-N13 cd14597
catalytic domain of tyrosine-protein phosphatase non-receptor type 13; Tyrosine-protein ...
 939-1170 5.93e-59

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: 202.75  E-value: 5.93e-59
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316060223  939 NRPKNRYTNILPYDFSRVKLvsmhNDEGaDYINANYI--PGYRHSKEYIATQGPLPETRNDFWKMVLQQKSPIIVMLTQC 1016
Cdd:cd14597      3 NRKKNRYKNILPYDTTRVPL----GDEG-GYINASFIkmPVGDEEFVYIACQGPLPTTVADFWQMVWEQKSTVIAMMTQE 77

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316060223 1017 NERRRVKCDHYWPFT-DEPVMYGD---ISVEMLSE-EGFpewIIRKFRLG--YADETLDVLHLNYTSWPDHGVPtvNAIE 1089
Cdd:cd14597     78 VEGGKIKCQRYWPEIlGKTTMVDNrlqLTLVRMQQlKNF---VIRVLELEdiQTREVRHITHLNFTAWPDHDTP--SQPE 152

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316060223 1090 SILQFVHIVRQQadRTKDPVIVHCSAGVGRTGTFMALDRLMQHIREHEFVDILGMVSDMRSHRLSMVQTEEQYVFIHQCV 1169
Cdd:cd14597    153 QLLTFISYMRHI--HKSGPIITHCSAGIGRSGTLICIDVVLGLISKDLDFDISDIVRTMRLQRHGMVQTEDQYIFCYQVI 230


                   .
gi 1316060223 1170 L 1170
Cdd:cd14597    231 L 231
R-PTP-D-2 cd14628
PTP-like domain of receptor-type tyrosine-protein phosphatase D, repeat 2; Receptor-type ...
 933-1170 6.67e-59

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: 204.58  E-value: 6.67e-59
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316060223  933 AADLPVNRPKNRYTNILPYDFSRVKLVSMHNDEGADYINANYIPGYRHSKEYIATQGPLPETRNDFWKMVLQQKSPIIVM 1012
Cdd:cd14628     46 SANLPCNKFKNRLVNIMPYESTRVCLQPIRGVEGSDYINASFIDGYRQQKAYIATQGPLAETTEDFWRMLWEHNSTIVVM 125

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316060223 1013 LTQCNERRRVKCDHYWPfTDEPVMYGDISVEMLSEEGFPEWIIRKFRLGYA--DETLDVLHLNYTSWPDHGVPTVNaiES 1090
Cdd:cd14628    126 LTKLREMGREKCHQYWP-AERSARYQYFVVDPMAEYNMPQYILREFKVTDArdGQSRTVRQFQFTDWPEQGVPKSG--EG 202

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316060223 1091 ILQF---VHIVRQQADRtKDPVIVHCSAGVGRTGTFMALDRLMQHIREHEFVDILGMVSDMRSHRLSMVQTEEQYVFIHQ 1167
Cdd:cd14628    203 FIDFigqVHKTKEQFGQ-DGPISVHCSAGVGRTGVFITLSIVLERMRYEGVVDIFQTVKMLRTQRPAMVQTEDQYQFCYR 281


                   ...
gi 1316060223 1168 CVL 1170
Cdd:cd14628    282 AAL 284
R-PTPc-typeIIb-1 cd14555
catalytic domain of type IIb (or R2B) subfamily receptor-type tyrosine-protein phosphatases, ...
 969-1170 1.07e-58

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: 200.91  E-value: 1.07e-58
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316060223  969 YINANYIPGYRHSKEYIATQGPLPETRNDFWKMVLQQKSPIIVMLTQCNERRRVKCDHYWPftDEPVMYGDISVEMLSEE 1048
Cdd:cd14555      1 YINANYIDGYHRPNHYIATQGPMQETVYDFWRMVWQENSASIVMVTNLVEVGRVKCSRYWP--DDTEVYGDIKVTLVETE 78

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316060223 1049 GFPEWIIRKF---RLGYaDETLDVLHLNYTSWPDHGVPTvnAIESILQFVHIVRQQADRTKDPVIVHCSAGVGRTGTFMA 1125
Cdd:cd14555     79 PLAEYVVRTFaleRRGY-HEIREVRQFHFTGWPDHGVPY--HATGLLGFIRRVKASNPPSAGPIVVHCSAGAGRTGCYIV 155

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*
gi 1316060223 1126 LDRLMQHIREHEFVDILGMVSDMRSHRLSMVQTEEQYVFIHQCVL 1170
Cdd:cd14555    156 IDIMLDMAEREGVVDIYNCVKELRSRRVNMVQTEEQYIFIHDAIL 200
R-PTP-F-2 cd14629
PTP-like domain of receptor-type tyrosine-protein phosphatase F, repeat 2; Receptor-type ...
 933-1170 5.88e-58

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: 201.88  E-value: 5.88e-58
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316060223  933 AADLPVNRPKNRYTNILPYDFSRVKLVSMHNDEGADYINANYIPGYRHSKEYIATQGPLPETRNDFWKMVLQQKSPIIVM 1012
Cdd:cd14629     47 SANLPCNKFKNRLVNIMPYELTRVCLQPIRGVEGSDYINASFIDGYRQQKAYIATQGPLAETTEDFWRMLWEHNSTIVVM 126

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316060223 1013 LTQCNERRRVKCDHYWPfTDEPVMYGDISVEMLSEEGFPEWIIRKFRLGYA--DETLDVLHLNYTSWPDHGVPTVNaiES 1090
Cdd:cd14629    127 LTKLREMGREKCHQYWP-AERSARYQYFVVDPMAEYNMPQYILREFKVTDArdGQSRTIRQFQFTDWPEQGVPKTG--EG 203

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316060223 1091 ILQF---VHIVRQQADRtKDPVIVHCSAGVGRTGTFMALDRLMQHIREHEFVDILGMVSDMRSHRLSMVQTEEQYVFIHQ 1167
Cdd:cd14629    204 FIDFigqVHKTKEQFGQ-DGPITVHCSAGVGRTGVFITLSIVLERMRYEGVVDMFQTVKTLRTQRPAMVQTEDQYQLCYR 282


                   ...
gi 1316060223 1168 CVL 1170
Cdd:cd14629    283 AAL 285
PTPc-N22 cd14602
catalytic domain of tyrosine-protein phosphatase non-receptor type 22; Tyrosine-protein ...
 942-1170 1.32e-57

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: 198.91  E-value: 1.32e-57
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316060223  942 KNRYTNILPYDFSRVKLVSMHNDEGADYINANYIPGYRHSKEYIATQGPLPETRNDFWKMVLQQKSPIIVMLTQCNERRR 1021
Cdd:cd14602      1 KNRYKDILPYDHSRVELSLITSDEDSDYINANFIKGVYGPRAYIATQGPLSTTLLDFWRMIWEYSVLIIVMACMEFEMGK 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316060223 1022 VKCDHYWPFT-DEPVMYGDISVEMLSEEGFPEWIIRKFRLGYADETLDVLHLNYTSWPDHGVPTvnAIESILQFVHIVRQ 1100
Cdd:cd14602     81 KKCERYWAEPgEMQLEFGPFSVTCEAEKRKSDYIIRTLKVKFNSETRTIYQFHYKNWPDHDVPS--SIDPILELIWDVRC 158

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1316060223 1101 QADRTKDPVIVHCSAGVGRTGTFMALD---RLMQHIREHEFVDILGMVSDMRSHRLSMVQTEEQYVFIHQCVL 1170
Cdd:cd14602    159 YQEDDSVPICIHCSAGCGRTGVICAIDytwMLLKDGIIPENFSVFSLIQEMRTQRPSLVQTKEQYELVYNAVI 231
R-PTPc-K-1 cd14631
catalytic domain of receptor-type tyrosine-protein phosphatase K, repeat 1; Receptor-type ...
 955-1170 4.47e-57

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: 196.78  E-value: 4.47e-57
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316060223  955 RVKLVSMHNDEGADYINANYIPGYRHSKEYIATQGPLPETRNDFWKMVLQQKSPIIVMLTQCNERRRVKCDHYWPftDEP 1034
Cdd:cd14631      1 RVILQPVEDDPSSDYINANYIDGYQRPSHYIATQGPVHETVYDFWRMIWQEQSACIVMVTNLVEVGRVKCYKYWP--DDT 78

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316060223 1035 VMYGDISVEMLSEEGFPEWIIRKFRLGYA--DETLDVLHLNYTSWPDHGVPtVNAIeSILQFVHIVRQQADRTKDPVIVH 1112
Cdd:cd14631     79 EVYGDFKVTCVEMEPLAEYVVRTFTLERRgyNEIREVKQFHFTGWPDHGVP-YHAT-GLLSFIRRVKLSNPPSAGPIVVH 156

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 1316060223 1113 CSAGVGRTGTFMALDRLMQHIREHEFVDILGMVSDMRSHRLSMVQTEEQYVFIHQCVL 1170
Cdd:cd14631    157 CSAGAGRTGCYIVIDIMLDMAEREGVVDIYNCVKALRSRRINMVQTEEQYIFIHDAIL 214
R-PTPc-U-1 cd14632
catalytic domain of receptor-type tyrosine-protein phosphatase U, repeat 1; Receptor-type ...
 969-1170 1.00e-56

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: 195.27  E-value: 1.00e-56
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316060223  969 YINANYIPGYRHSKEYIATQGPLPETRNDFWKMVLQQKSPIIVMLTQCNERRRVKCDHYWPftDEPVMYGDISVEMLSEE 1048
Cdd:cd14632      1 YINANYIDGYHRSNHFIATQGPKQEMVYDFWRMVWQEHCSSIVMITKLVEVGRVKCSKYWP--DDSDTYGDIKITLLKTE 78

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316060223 1049 GFPEWIIRKF---RLGYADETlDVLHLNYTSWPDHGVPTvnAIESILQFVHIVRQQADRTKDPVIVHCSAGVGRTGTFMA 1125
Cdd:cd14632     79 TLAEYSVRTFaleRRGYSARH-EVKQFHFTSWPEHGVPY--HATGLLAFIRRVKASTPPDAGPVVVHCSAGAGRTGCYIV 155

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*
gi 1316060223 1126 LDRLMQHIREHEFVDILGMVSDMRSHRLSMVQTEEQYVFIHQCVL 1170
Cdd:cd14632    156 LDVMLDMAECEGVVDIYNCVKTLCSRRINMIQTEEQYIFIHDAIL 200
PTPc-N11 cd14605
catalytic domain of tyrosine-protein phosphatase non-receptor type 11; Tyrosine-protein ...
 939-1169 1.94e-56

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: 196.01  E-value: 1.94e-56
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316060223  939 NRPKNRYTNILPYDFSRVKLVSMH-NDEGADYINANYI-PGY-------RHSKEYIATQGPLPETRNDFWKMVLQQKSPI 1009
Cdd:cd14605      2 NKNKNRYKNILPFDHTRVVLHDGDpNEPVSDYINANIImPEFetkcnnsKPKKSYIATQGCLQNTVNDFWRMVFQENSRV 81

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316060223 1010 IVMLTQCNERRRVKCDHYWPftDEPVM--YGDISVEMLSEEGFPEWIIRKFRL---GYADETLDVLHLNYTSWPDHGVPT 1084
Cdd:cd14605     82 IVMTTKEVERGKSKCVKYWP--DEYALkeYGVMRVRNVKESAAHDYILRELKLskvGQGNTERTVWQYHFRTWPDHGVPS 159

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316060223 1085 VNAieSILQFVHIVRQQADRTKD--PVIVHCSAGVGRTGTFMALDRLMQHIREHEF---VDILGMVSDMRSHRLSMVQTE 1159
Cdd:cd14605    160 DPG--GVLDFLEEVHHKQESIMDagPVVVHCSAGIGRTGTFIVIDILIDIIREKGVdcdIDVPKTIQMVRSQRSGMVQTE 237

                          250
                   ....*....|
gi 1316060223 1160 EQYVFIHQCV 1169
Cdd:cd14605    238 AQYRFIYMAV 247
R-PTPc-R cd14611
catalytic domain of receptor-type tyrosine-protein phosphatase R; Receptor-type ...
 942-1167 8.43e-56

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: 193.21  E-value: 8.43e-56
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316060223  942 KNRYTNILPYDFSRVKLVSMH-NDEGADYINANYIPGYR-HSKEYIATQGPLPETRNDFWKMVLQQKSPIIVMLTQCNER 1019
Cdd:cd14611      2 KNRYKTILPNPHSRVCLKPKNsNDSLSTYINANYIRGYGgKEKAFIATQGPMINTVNDFWQMVWQEDSPVIVMITKLKEK 81

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316060223 1020 RRvKCDHYWPftDEPVMYGDISVEMLSEEGFPEWIIRKFRLGYADETLDVLHLNYTSWPDHGVPtvNAIESILQFVHIVR 1099
Cdd:cd14611     82 NE-KCVLYWP--EKRGIYGKVEVLVNSVKECDNYTIRNLTLKQGSQSRSVKHYWYTSWPDHKTP--DSAQPLLQLMLDVE 156

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316060223 1100 Q--QADRTKDPVIVHCSAGVGRTGTFMALDRLMQHIREHEFVDILGMVSDMRSHRLSMVQTEEQYVFIHQ 1167
Cdd:cd14611    157 EdrLASPGRGPVVVHCSAGIGRTGCFIATTIGCQQLKEEGVVDVLSIVCQLRVDRGGMVQTSEQYEFVHH 226
PTPc-N6 cd14606
catalytic domain of tyrosine-protein phosphatase non-receptor type 6; Tyrosine-protein ...
 937-1170 1.17e-55

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: 194.33  E-value: 1.17e-55
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316060223  937 PVNRPKNRYTNILPYDFSRVKLVSMHND-EGADYINANYI------PGyRHSKEYIATQGPLPETRNDFWKMVLQQKSPI 1009
Cdd:cd14606     16 PENKSKNRYKNILPFDHSRVILQGRDSNiPGSDYINANYVknqllgPD-ENAKTYIASQGCLEATVNDFWQMAWQENSRV 94

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316060223 1010 IVMLTQCNERRRVKCDHYWPFTDEPVMYGDISVEMLSEEGFPEWIIRKFRLGYADET---LDVLHLNYTSWPDHGVPTVN 1086
Cdd:cd14606     95 IVMTTREVEKGRNKCVPYWPEVGMQRAYGPYSVTNCGEHDTTEYKLRTLQVSPLDNGeliREIWHYQYLSWPDHGVPSEP 174

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316060223 1087 AieSILQFVHIV--RQQADRTKDPVIVHCSAGVGRTGTFMALDRLMQHIREHEF---VDILGMVSDMRSHRLSMVQTEEQ 1161
Cdd:cd14606    175 G--GVLSFLDQInqRQESLPHAGPIIVHCSAGIGRTGTIIVIDMLMENISTKGLdcdIDIQKTIQMVRAQRSGMVQTEAQ 252


                   ....*....
gi 1316060223 1162 YVFIHQCVL 1170
Cdd:cd14606    253 YKFIYVAIA 261
PTPc-N1_2 cd14545
catalytic domain of tyrosine-protein phosphatase non-receptor type 1 and type 2; ...
 942-1164 1.70e-55

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: 192.61  E-value: 1.70e-55
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316060223  942 KNRYTNILPYDFSRVKLVSmhNDEGADYINANYIPGYRHSKEYIATQGPLPETRNDFWKMVLQQKSPIIVMLTQCNERRR 1021
Cdd:cd14545      1 LNRYRDRDPYDHDRSRVKL--KQGDNDYINASLVEVEEAKRSYILTQGPLPNTSGHFWQMVWEQNSKAVIMLNKLMEKGQ 78

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316060223 1022 VKCDHYWPFTDEPVM---YGDISVEMLSEEGFPEWIIRKFRLG--YADETLDVLHLNYTSWPDHGVPTVNAieSILQFVH 1096
Cdd:cd14545     79 IKCAQYWPQGEGNAMifeDTGLKVTLLSEEDKSYYTVRTLELEnlKTQETREVLHFHYTTWPDFGVPESPA--AFLNFLQ 156

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1316060223 1097 IVRQQA--DRTKDPVIVHCSAGVGRTGTFMALDRLMQHIREHEF--VDILGMVSDMRSHRLSMVQTEEQYVF 1164
Cdd:cd14545    157 KVRESGslSSDVGPPVVHCSAGIGRSGTFCLVDTCLVLIEKGNPssVDVKKVLLEMRKYRMGLIQTPDQLRF 228
PTPc-N1 cd14608
catalytic domain of tyrosine-protein phosphatase non-receptor type 1; Tyrosine-protein ...
 919-1170 5.10e-55

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: 192.93  E-value: 5.10e-55
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316060223  919 FEELKSVGLDLTHDAADLPVNRPKNRYTNILPYDFSRVKLvsmhNDEGADYINANYIPGYRHSKEYIATQGPLPETRNDF 998
Cdd:cd14608      5 YQDIRHEASDFPCRVAKLPKNKNRNRYRDVSPFDHSRIKL----HQEDNDYINASLIKMEEAQRSYILTQGPLPNTCGHF 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316060223  999 WKMVLQQKSPIIVMLTQCNERRRVKCDHYWPFTDEPVMY---GDISVEMLSEEGFPEWIIRKFRLG--YADETLDVLHLN 1073
Cdd:cd14608     81 WEMVWEQKSRGVVMLNRVMEKGSLKCAQYWPQKEEKEMIfedTNLKLTLISEDIKSYYTVRQLELEnlTTQETREILHFH 160

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316060223 1074 YTSWPDHGVPTVNAieSILQFVHIVRQQADRTKD--PVIVHCSAGVGRTGTFMALDR---LMQHIREHEFVDILGMVSDM 1148
Cdd:cd14608    161 YTTWPDFGVPESPA--SFLNFLFKVRESGSLSPEhgPVVVHCSAGIGRSGTFCLADTcllLMDKRKDPSSVDIKKVLLEM 238

                          250       260
                   ....*....|....*....|..
gi 1316060223 1149 RSHRLSMVQTEEQYVFIHQCVL 1170
Cdd:cd14608    239 RKFRMGLIQTADQLRFSYLAVI 260
PTPc-N22_18_12 cd14542
catalytic domain of tyrosine-protein phosphatase non-receptor type 22, type 18 and type 12; ...
 969-1167 6.14e-55

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: 189.94  E-value: 6.14e-55
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316060223  969 YINANYIPGYRHSKEYIATQGPLPETRNDFWKMVLQQKSPIIVMltQCNERR--RVKCDHYWPFTDEPVM-YGDISVEML 1045
Cdd:cd14542      1 YINANFIKGVSGSKAYIATQGPLPNTVLDFWRMIWEYNVQVIVM--ACREFEmgKKKCERYWPEEGEEQLqFGPFKISLE 78

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316060223 1046 SEEGF-PEWIIRKFRLGYADETLDVLHLNYTSWPDHGVPTvnAIESILQFVHIVRQQADRTKDPVIVHCSAGVGRTGTFM 1124
Cdd:cd14542     79 KEKRVgPDFLIRTLKVTFQKESRTVYQFHYTAWPDHGVPS--SVDPILDLVRLVRDYQGSEDVPICVHCSAGCGRTGTIC 156

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*..
gi 1316060223 1125 ALD---RLMQ-HIREHEFvDILGMVSDMRSHRLSMVQTEEQYVFIHQ 1167
Cdd:cd14542    157 AIDyvwNLLKtGKIPEEF-SLFDLVREMRKQRPAMVQTKEQYELVYR 202
PTPc-N5 cd14613
catalytic domain of tyrosine-protein phosphatase non-receptor type 5; Tyrosine-protein ...
 935-1171 8.99e-55

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: 191.61  E-value: 8.99e-55
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316060223  935 DLPVNRPKNRYTNILPYDFSRVKLVSMHNDEG-ADYINANYIPGY-RHSKEYIATQGPLPETRNDFWKMVLQQKSPIIVM 1012
Cdd:cd14613     21 DIPGLVRKNRYKTILPNPHSRVCLTSPDQDDPlSSYINANYIRGYgGEEKVYIATQGPTVNTVGDFWRMVWQERSPIIVM 100

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316060223 1013 LTQCNERRRvKCDHYWPftDEPVMYGDISVEMLSEEGFPEWIIRKFRLGYADETLDVLHLNYTSWPDHGVP-TVNAIESI 1091
Cdd:cd14613    101 ITNIEEMNE-KCTEYWP--EEQVTYEGIEITVKQVIHADDYRLRLITLKSGGEERGLKHYWYTSWPDQKTPdNAPPLLQL 177

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316060223 1092 LQFVHIVRQQADRTKDPVIVHCSAGVGRTGTFMALDRLMQHIREHEFVDILGMVSDMRSHRLSMVQTEEQYVFIHQCVLL 1171
Cdd:cd14613    178 VQEVEEARQQAEPNCGPVIVHCSAGIGRTGCFIATSICCKQLRNEGVVDILRTTCQLRLDRGGMIQTCEQYQFVHHVLSL 257
R-PTP-C-2 cd14558
PTP-like domain of receptor-type tyrosine-protein phosphatase C, repeat 2; Receptor-type ...
 969-1166 1.43e-54

PTP-like domain of receptor-type tyrosine-protein phosphatase C, repeat 2; Receptor-type tyrosine-protein phosphatase C (PTPRC), also known as CD45, leukocyte common antigen (LCA) or GP180, belongs to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. PTPRC/CD45 is found in all nucleated hematopoietic cells and is an essential regulator of T- and B-cell antigen receptor signaling. It controls immune response, both positively and negatively, by dephosphorylating a number of signaling molecules such as the Src family kinases, the CD3zeta chain of TCY, and ZAP-70 kinase. Mutations in the human PTPRC/CD45 gene are associated with severe combined immunodeficiency (SCID) and multiple sclerosis. PTPRC/CD45 contains an extracellular receptor-like region with fibronectin type III (FN3) repeats, a short transmembrane segment, and a cytoplasmic region comprising of a membrane proximal catalytically active PTP domain (repeat 1 or D1) and a membrane distal catalytically impaired PTP-like domain (repeat 2, or D2). This model represents repeat 2.


Pssm-ID: 350406 [Multi-domain]  Cd Length: 203  Bit Score: 188.76  E-value: 1.43e-54
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316060223  969 YINANYIPGYRHSKEYIATQGPLPETRNDFWKMVLQQKSPIIVMLTQCNERRRVKCDHYWPftDEPVMYGDISVEMLSEE 1048
Cdd:cd14558      1 YINASFIDGYWGPKSLIATQGPLPDTIADFWQMIFQKKVKVIVMLTELKEGDQEQCAQYWG--DEKKTYGDIEVELKDTE 78

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316060223 1049 GFPEWIIRKFRLGYA--DETLDVLHLNYTSWPDHGVPT-----VNAIESILQFVHIVRQQADRTKdPVIVHCSAGVGRTG 1121
Cdd:cd14558     79 KSPTYTVRVFEITHLkrKDSRTVYQYQYHKWKGEELPEkpkdlVDMIKSIKQKLPYKNSKHGRSV-PIVVHCSDGSSRTG 157

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*
gi 1316060223 1122 TFMALDRLMQHIREHEFVDILGMVSDMRSHRLSMVQTEEQYVFIH 1166
Cdd:cd14558    158 IFCALWNLLESAETEKVVDVFQVVKALRKQRPGMVSTLEQYQFLY 202
R-PTPc-Z-1 cd17668
catalytic domain of receptor-type tyrosine-protein phosphatase Z, repeat 1; Receptor-type ...
 969-1166 2.41e-53

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: 185.57  E-value: 2.41e-53
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316060223  969 YINANYIPGYRHSKEYIATQGPLPETRNDFWKMVLQQKSPIIVMLTQCNERRRVKCDHYWPfTDEPVMYGDISVEMLSEE 1048
Cdd:cd17668      1 YINANYVDGYNKPKAYIAAQGPLKSTAEDFWRMIWEHNVEVIVMITNLVEKGRRKCDQYWP-ADGSEEYGNFLVTQKSVQ 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316060223 1049 GFPEWIIRKFRL-----------GYADETLdVLHLNYTSWPDHGVPTVNAieSILQFVHIVRQQADRTKDPVIVHCSAGV 1117
Cdd:cd17668     80 VLAYYTVRNFTLrntkikkgsqkGRPSGRV-VTQYHYTQWPDMGVPEYTL--PVLTFVRKASYAKRHAVGPVVVHCSAGV 156

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*....
gi 1316060223 1118 GRTGTFMALDRLMQHIREHEFVDILGMVSDMRSHRLSMVQTEEQYVFIH 1166
Cdd:cd17668    157 GRTGTYIVLDSMLQQIQHEGTVNIFGFLKHIRSQRNYLVQTEEQYVFIH 205
PTPc-N2 cd14607
catalytic domain of tyrosine-protein phosphatase non-receptor type 2; Tyrosine-protein ...
 921-1169 4.54e-53

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: 186.71  E-value: 4.54e-53
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316060223  921 ELKSVGLDLTHDAADLPVNRPKNRYTNILPYDFSRVKLVSMHNDegadYINANYIPGYRHSKEYIATQGPLPETRNDFWK 1000
Cdd:cd14607      6 EIRNESHDYPHRVAKYPENRNRNRYRDVSPYDHSRVKLQNTEND----YINASLVVIEEAQRSYILTQGPLPNTCCHFWL 81

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316060223 1001 MVLQQKSPIIVMLTQCNERRRVKCDHYWPFTDEPVMY---GDISVEMLSEEGFPEWIIRKFRLGYAD--ETLDVLHLNYT 1075
Cdd:cd14607     82 MVWQQKTKAVVMLNRIVEKDSVKCAQYWPTDEEEVLSfkeTGFSVKLLSEDVKSYYTVHLLQLENINsgETRTISHFHYT 161

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316060223 1076 SWPDHGVPTVNAieSILQFVHIVRQQADRTKD--PVIVHCSAGVGRTGTFMALDR---LMQHiREHEFVDILGMVSDMRS 1150
Cdd:cd14607    162 TWPDFGVPESPA--SFLNFLFKVRESGSLSPEhgPAVVHCSAGIGRSGTFSLVDTclvLMEK-KDPDSVDIKQVLLDMRK 238

                          250
                   ....*....|....*....
gi 1316060223 1151 HRLSMVQTEEQYVFIHQCV 1169
Cdd:cd14607    239 YRMGLIQTPDQLRFSYMAV 257
R-PTPc-A-2 cd14623
catalytic domain of receptor-type tyrosine-protein phosphatase A, repeat 2; Receptor-type ...
 944-1169 5.92e-52

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: 182.55  E-value: 5.92e-52
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316060223  944 RYTNILPYDFSRVKLVSMHNDEGADYINANYIPGYRHSKEYIATQGPLPETRNDFWKMVLQQKSPIIVMLTQCNERRRVK 1023
Cdd:cd14623      1 RVLQIIPYEFNRVIIPVKRGEENTDYVNASFIDGYRQKDSYIASQGPLQHTIEDFWRMIWEWKSCSIVMLTELEERGQEK 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316060223 1024 CDHYWPfTDEPVMYGDISVEMLSEEGFPEWIIRKFRLGYADE--TLDVLHLNYTSWPDHGVPT-----VNAIESILqfvh 1096
Cdd:cd14623     81 CAQYWP-SDGSVSYGDITIELKKEEECESYTVRDLLVTNTREnkSRQIRQFHFHGWPEVGIPSdgkgmINIIAAVQ---- 155

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1316060223 1097 ivRQQADRTKDPVIVHCSAGVGRTGTFMALDRLMQHIREHEFVDILGMVSDMRSHRLSMVQTEEQYVFIHQCV 1169
Cdd:cd14623    156 --KQQQQSGNHPITVHCSAGAGRTGTFCALSTVLERVKAEGILDVFQTVKSLRLQRPHMVQTLEQYEFCYKVV 226
PTPc-N4 cd14601
catalytic domain of tyrosine-protein phosphatase non-receptor type 4; Tyrosine-protein ...
 968-1175 2.10e-51

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: 180.14  E-value: 2.10e-51
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316060223  968 DYINANYI----PGYRHSKEYIATQGPLPETRNDFWKMVLQQKSPIIVMLTQCNERRRVKCDHYWPFTDEPVMYGDISVE 1043
Cdd:cd14601      1 DYINANYInmeiPSSSIINRYIACQGPLPNTCSDFWQMTWEQGSSMVVMLTTQVERGRVKCHQYWPEPSGSSSYGGFQVT 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316060223 1044 MLSEEGFPEWIIRKFRLGY--ADETLDVLHLNYTSWPDHGVPTVNAieSILQFVHIVRQQADRTKDPVIVHCSAGVGRTG 1121
Cdd:cd14601     81 CHSEEGNPAYVFREMTLTNleKNESRPLTQIQYIAWPDHGVPDDSS--DFLDFVCLVRNKRAGKDEPVVVHCSAGIGRTG 158

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....
gi 1316060223 1122 TFMALDRLMQHIREHEFVDILGMVSDMRSHRLSMVQTEEQYVFIHQCVLLMWQK 1175
Cdd:cd14601    159 VLITMETAMCLIECNQPVYPLDIVRTMRDQRAMMIQTPSQYRFVCEAILKVYEE 212
R-PTPc-A-E-1 cd14551
catalytic domain of receptor-type tyrosine-protein phosphatase A and E, repeat 1; ...
 969-1167 3.43e-51

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: 179.34  E-value: 3.43e-51
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316060223  969 YINANYIPGYRHSKEYIATQGPLPETRNDFWKMVLQQKSPIIVMLTQCNERRRVKCDHYWPFTDEPVmYGDISVEMLSEE 1048
Cdd:cd14551      1 YINASYIDGYQEKNKFIAAQGPKDETVNDFWRMIWEQGSATIVMVTNLKERKEKKCSQYWPDQGCWT-YGNLRVRVEDTV 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316060223 1049 GFPEWIIRKFRLGYADETLD------VLHLNYTSWPDHGVPTVNAieSILQFVHIVRQQADRTKDPVIVHCSAGVGRTGT 1122
Cdd:cd14551     80 VLVDYTTRKFCIQKVNRGIGekrvrlVTQFHFTSWPDFGVPFTPI--GMLKFLKKVKSANPPRAGPIVVHCSAGVGRTGT 157

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*
gi 1316060223 1123 FMALDRLMQHIREHEFVDILGMVSDMRSHRLSMVQTEEQYVFIHQ 1167
Cdd:cd14551    158 FIVIDAMLDMMHAEGKVDVFGFVSRIRQQRSQMVQTDMQYVFIYQ 202
R-PTPc-A-E-2 cd14552
catalytic domain of receptor-type tyrosine-protein phosphatase A and E, repeat 2; ...
 969-1169 7.11e-50

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: 175.54  E-value: 7.11e-50
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316060223  969 YINANYIPGYRHSKEYIATQGPLPETRNDFWKMVLQQKSPIIVMLTQCNERRRVKCDHYWPfTDEPVMYGDISVEMLSEE 1048
Cdd:cd14552      1 YINASFIDGYRQKDAYIATQGPLDHTVEDFWRMIWEWKSCSIVMLTEIKERSQNKCAQYWP-EDGSVSSGDITVELKDQT 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316060223 1049 GFPEWIIRKFRL--GYADETLDVLHLNYTSWPDHGVPTvNAIESILQFVHIVRQQADRTKDPVIVHCSAGVGRTGTFMAL 1126
Cdd:cd14552     80 DYEDYTLRDFLVtkGKGGSTRTVRQFHFHGWPEVGIPD-NGKGMIDLIAAVQKQQQQSGNHPITVHCSAGAGRTGTFCAL 158

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|...
gi 1316060223 1127 DRLMQHIREHEFVDILGMVSDMRSHRLSMVQTEEQYVFIHQCV 1169
Cdd:cd14552    159 STVLERVKAEGVLDVFQVVKSLRLQRPHMVQTLEQYEFCYKVV 201
R-PTPc-E-2 cd14622
catalytic domain of receptor-type tyrosine-protein phosphatase E, repeat 2; Receptor-type ...
 968-1169 2.69e-49

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: 174.04  E-value: 2.69e-49
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316060223  968 DYINANYIPGYRHSKEYIATQGPLPETRNDFWKMVLQQKSPIIVMLTQCNERRRVKCDHYWPfTDEPVMYGDISVEMLSE 1047
Cdd:cd14622      1 DYINASFIDGYRQKDYFIATQGPLAHTVEDFWRMVWEWKCHTIVMLTELQEREQEKCVQYWP-SEGSVTHGEITIEIKND 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316060223 1048 EGFPEWIIRKFRLGYADE--TLDVLHLNYTSWPDHGVPTVNaiESILQFVHIVRQQADRTKD-PVIVHCSAGVGRTGTFM 1124
Cdd:cd14622     80 TLLETISIRDFLVTYNQEkqTRLVRQFHFHGWPEIGIPAEG--KGMIDLIAAVQKQQQQTGNhPIVVHCSAGAGRTGTFI 157

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*
gi 1316060223 1125 ALDRLMQHIREHEFVDILGMVSDMRSHRLSMVQTEEQYVFIHQCV 1169
Cdd:cd14622    158 ALSNILERVKAEGLLDVFQTVKSLRLQRPHMVQTLEQYEFCYRVV 202
PTPc-N20 cd14596
catalytic domain of tyrosine-protein phosphatase non-receptor type 20; Tyrosine-protein ...
 969-1170 2.50e-48

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: 171.08  E-value: 2.50e-48
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316060223  969 YINANYIPGYRHSKE--YIATQGPLPETRNDFWKMVLQQKSPIIVMLTQCNERRRVKCDHYWPFT-DEPVMYGDISVEML 1045
Cdd:cd14596      1 YINASYITMPVGEEElfYIATQGPLPSTIDDFWQMVWENRSDVIAMMTREVERGKVKCHRYWPETlQEPMELENYQLRLE 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316060223 1046 SEEGFPEWIIRKFRL--GYADETLDVLHLNYTSWPDHGVPtvNAIESILQFVHIVRqqADRTKDPVIVHCSAGVGRTGTF 1123
Cdd:cd14596     81 NYQALQYFIIRIIKLveKETGENRLIKHLQFTTWPDHGTP--QSSDQLVKFICYMR--KVHNTGPIVVHCSAGIGRAGVL 156

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*..
gi 1316060223 1124 MALDRLMQHIREHEFVDILGMVSDMRSHRLSMVQTEEQYVFIHQCVL 1170
Cdd:cd14596    157 ICVDVLLSLIEKDLSFNIKDIVREMRQQRYGMIQTKDQYLFCYKVVL 203
COG5599 COG5599
Protein tyrosine phosphatase [Signal transduction mechanisms];
920-1165 3.38e-47

Protein tyrosine phosphatase [Signal transduction mechanisms];


Pssm-ID: 444335 [Multi-domain]  Cd Length: 282  Bit Score: 170.66  E-value: 3.38e-47
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316060223  920 EELKSVGLDLTHDaaDLPVNRPKNRYTNILPYDFSRVKlvsmhndEGADYINANYIPGYRhSKEYIATQGPLPETRNDFW 999
Cdd:COG5599     25 NELAPSHNDPQYL--QNINGSPLNRFRDIQPYKETALR-------ANLGYLNANYIQVIG-NHRYIATQYPLEEQLEDFF 94

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316060223 1000 KMVLQQKSPIIVMLTQCNE--RRRVKCDHYWPFTDEpvmYG--DISVEMLSEEGFPEWI-IRKFRL---GYADETLDVLH 1071
Cdd:COG5599     95 QMLFDNNTPVLVVLASDDEisKPKVKMPVYFRQDGE---YGkyEVSSELTESIQLRDGIeARTYVLtikGTGQKKIEIPV 171

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316060223 1072 LNYTSWPDHGVPTVNAIESILQFVHIVRQQADRTKDPVIVHCSAGVGRTGTFMALDRLMQHIREHE--FVDILGMVSDMR 1149
Cdd:COG5599    172 LHVKNWPDHGAISAEALKNLADLIDKKEKIKDPDKLLPVVHCRAGVGRTGTLIACLALSKSINALVqiTLSVEEIVIDMR 251

                          250
                   ....*....|....*..
gi 1316060223 1150 SHR-LSMVQTEEQYVFI 1165
Cdd:COG5599    252 TSRnGGMVQTSEQLDVL 268
PTPc_plant_PTP1 cd17658
protein tyrosine phosphatase 1 from Arabidopsis thaliana and similar plant PTPs; Arabidopsis ...
 969-1166 5.20e-47

protein tyrosine phosphatase 1 from Arabidopsis thaliana and similar plant PTPs; Arabidopsis thaliana protein tyrosine phosphatase 1 (AtPTP1) belongs to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. AtPTP1 dephosphorylates and inhibits MAP kinase 6 (MPK6) in non-oxidative stress conditions. Together with MAP kinase phosphatase 1 (MKP1) it expresses salicylic acid (SA) and camalexin biosynthesis, and therefore, modulating defense response.


Pssm-ID: 350496 [Multi-domain]  Cd Length: 206  Bit Score: 167.26  E-value: 5.20e-47
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316060223  969 YINANYI--PGYRHSKEYIATQGPLPETRNDFWKMVLQQKSPIIVMLTQ-CNERRRVKCDHYWPFTD-EPVMYGDISVEM 1044
Cdd:cd17658      1 YINASLVetPASESLPKFIATQGPLPHTFEDFWEMVIQQRCPVIIMLTRlVDNYSTAKCADYFPAEEnESREFGRISVTN 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316060223 1045 LSEEGFPEWI-IRKFRLGY---ADETLDVLHLNYTSWPDHGVP-TVNAIESILQFVHIVRQQAdrtkDPVIVHCSAGVGR 1119
Cdd:cd17658     81 KKLKHSQHSItLRVLEVQYiesEEPPLSVLHIQYPEWPDHGVPkDTRSVRELLKRLYGIPPSA----GPIVVHCSAGIGR 156

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*....
gi 1316060223 1120 TGTFMALDRLMQHIREHEF--VDILGMVSDMRSHRLSMVQTEEQYVFIH 1166
Cdd:cd17658    157 TGAYCTIHNTIRRILEGDMsaVDLSKTVRKFRSQRIGMVQTQDQYIFCY 205
PTP-N23 cd14539
PTP-like domain of tyrosine-protein phosphatase non-receptor type 23; Tyrosine-protein ...
 969-1167 1.29e-45

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: 163.32  E-value: 1.29e-45
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316060223  969 YINANYIPGYR-HSKEYIATQGPLPETRNDFWKMVLQQKSPIIVMLTQCNERRRVKCDHYWPfTD--EPVMYGDISVEML 1045
Cdd:cd14539      1 YINASLIEDLTpYCPRFIATQAPLPGTAADFWLMVYEQQVSVIVMLVSEQENEKQKVHRYWP-TErgQALVYGAITVSLQ 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316060223 1046 SEEGFPEWIIRKFRLGYADETL--DVLHLNYTSWPDHGVPTvnAIESILQF---VHIVRQQADRTKDPVIVHCSAGVGRT 1120
Cdd:cd14539     80 SVRTTPTHVERIISIQHKDTRLsrSVVHLQFTTWPELGLPD--SPNPLLRFieeVHSHYLQQRSLQTPIVVHCSSGVGRT 157

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*...
gi 1316060223 1121 GTFMALDRLMQHIRE-HEFVDILGMVSDMRSHRLSMVQTEEQYVFIHQ 1167
Cdd:cd14539    158 GAFCLLYAAVQEIEAgNGIPDLPQLVRKMRQQRKYMLQEKEHLKFCYE 205
PTPc-N14 cd14599
catalytic domain of tyrosine-protein phosphatase non-receptor type 14; Tyrosine-protein ...
 918-1175 2.11e-44

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: 162.86  E-value: 2.11e-44
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316060223  918 QFEELKSVGLDLTHDAADLPVNRPKNRYTNILPYDFSRVKLV-SMHNDEGadYINANYIPGYRHSKE--YIATQGPLPET 994
Cdd:cd14599     17 EYEQIPKKKADGVFTTATLPENAERNRIREVVPYEENRVELVpTKENNTG--YINASHIKVTVGGEEwhYIATQGPLPHT 94

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316060223  995 RNDFWKMVLQQKSPIIVMLTQCNERRRVKCDHYWP---FTDEPVMYGDISV--EMLSEEGFPEWIIRKFRLGYADETLDV 1069
Cdd:cd14599     95 CHDFWQMVWEQGVNVIAMVTAEEEGGRSKSHRYWPklgSKHSSATYGKFKVttKFRTDSGCYATTGLKVKHLLSGQERTV 174

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316060223 1070 LHLNYTSWPDHGVPT-VNAIESILQFVHIVRQQADRTKD-------PVIVHCSAGVGRTGTFMaLDRLMQHIREH-EFVD 1140
Cdd:cd14599    175 WHLQYTDWPDHGCPEeVQGFLSYLEEIQSVRRHTNSMLDstkncnpPIVVHCSAGVGRTGVVI-LTELMIGCLEHnEKVE 253

                          250       260       270
                   ....*....|....*....|....*....|....*
gi 1316060223 1141 ILGMVSDMRSHRLSMVQTEEQYVFIHQcVLLMWQK 1175
Cdd:cd14599    254 VPVMLRHLREQRMFMIQTIAQYKFVYQ-VLIQFLK 287
PTPc-N21_14 cd14540
catalytic domain of tyrosine-protein phosphatase non-receptor type 21 and type 14; ...
 969-1170 4.90e-44

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: 159.16  E-value: 4.90e-44
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316060223  969 YINANYIPGYRHSKE--YIATQGPLPETRNDFWKMVLQQKSPIIVMLTQCNERRRVKCDHYWPFTD---EPVMYGDISVE 1043
Cdd:cd14540      1 YINASHITATVGGKQrfYIAAQGPLQNTVGDFWQMVWEQGVYLVVMVTAEEEGGREKCFRYWPTLGgehDALTFGEYKVS 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316060223 1044 MLSEEGFPEWIIRKFRLGY--ADETLDVLHLNYTSWPDHGVP-TVNAIESILQFVHIVR------QQADRTKDPVIVHCS 1114
Cdd:cd14540     81 TKFSVSSGCYTTTGLRVKHtlSGQSRTVWHLQYTDWPDHGCPeDVSGFLDFLEEINSVRrhtnqdVAGHNRNPPTLVHCS 160

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 1316060223 1115 AGVGRTGTFMALDRLMQHIREHEFVDILGMVSDMRSHRLSMVQTEEQYVFIHQCVL 1170
Cdd:cd14540    161 AGVGRTGVVILADLMLYCLDHNEELDIPRVLALLRHQRMLLVQTLAQYKFVYNVLI 216
R-PTP-N2 cd14610
PTP-like domain of receptor-type tyrosine-protein phosphatase N2; Receptor-type ...
 939-1164 1.68e-42

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: 157.14  E-value: 1.68e-42
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316060223  939 NRPKNRYTNILPYDFSRVKLVSMHNDEGADYINANYIPGYR-HSKEYIATQGPLPETRNDFWKMVLQQKSPIIVMLTQCN 1017
Cdd:cd14610     44 NVQKNRSLAVLPYDHSRIILKAENSHSHSDYINASPIMDHDpRNPAYIATQGPLPATVADFWQMVWESGCVVIVMLTPLA 123

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316060223 1018 ERRRVKCDHYWPftDEPV-MYGDISVEMLSEEGFPE-WIIRKFRLG--YADETLDVLHLNYTSWPDHGVPTvnAIESILQ 1093
Cdd:cd14610    124 ENGVKQCYHYWP--DEGSnLYHIYEVNLVSEHIWCEdFLVRSFYLKnlQTNETRTVTQFHFLSWNDQGVPA--STRSLLD 199

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1316060223 1094 FVHIVRQQADRTKDPVIVHCSAGVGRTGTF----MALDRLMQHIREhefVDILGMVSDMRSHRLSMVQTEEQYVF 1164
Cdd:cd14610    200 FRRKVNKCYRGRSCPIIVHCSDGAGRSGTYilidMVLNKMAKGAKE---IDIAATLEHLRDQRPGMVQTKEQFEF 271
R-PTP-N cd14609
PTP-like domain of receptor-type tyrosine-protein phosphatase N; Receptor-type ...
 932-1164 1.78e-42

PTP-like domain of receptor-type tyrosine-protein phosphatase N; Receptor-type tyrosine-protein phosphatase-like N (PTPRN or R-PTP-N), also called islet cell antigen 512 (ICA512) or PTP IA-2, belongs to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). It consists of a large ectodomain that contains a RESP18HD (regulated endocrine-specific protein 18 homology domain), followed by a transmembrane segment, and a single, catalytically-impaired, PTP domain. PTPRN is located in secretory granules of neuroendocrine cells and is involved in the generation, cargo storage, traffic, exocytosis and recycling of insulin secretory granules, as well as in beta-cell proliferation. It is a major autoantigen in type 1 diabetes and is involved in the regulation of insulin secretion.


Pssm-ID: 350457 [Multi-domain]  Cd Length: 281  Bit Score: 157.12  E-value: 1.78e-42
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316060223  932 DAADLPVNRPKNRYTNILPYDFSRVKLVSMHNDEGADYINANyiPGYRHSKE---YIATQGPLPETRNDFWKMVLQQKSP 1008
Cdd:cd14609     35 STAQGEANVKKNRNPDFVPYDHARIKLKAESNPSRSDYINAS--PIIEHDPRmpaYIATQGPLSHTIADFWQMVWENGCT 112

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316060223 1009 IIVMLTQCNERRRVKCDHYWPftDE-PVMYGDISVEMLSEEGFPE-WIIRKFRLG--YADETLDVLHLNYTSWPDHGVPT 1084
Cdd:cd14609    113 VIVMLTPLVEDGVKQCDRYWP--DEgSSLYHIYEVNLVSEHIWCEdFLVRSFYLKnvQTQETRTLTQFHFLSWPAEGIPS 190

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316060223 1085 vnAIESILQFVHIVRQQADRTKDPVIVHCSAGVGRTGTF----MALDRLMQHIREhefVDILGMVSDMRSHRLSMVQTEE 1160
Cdd:cd14609    191 --STRPLLDFRRKVNKCYRGRSCPIIVHCSDGAGRTGTYilidMVLNRMAKGVKE---IDIAATLEHVRDQRPGMVRTKD 265


                   ....
gi 1316060223 1161 QYVF 1164
Cdd:cd14609    266 QFEF 269
PHA02738 PHA02738
hypothetical protein; Provisional
 939-1169 1.92e-42

hypothetical protein; Provisional


Pssm-ID: 222923 [Multi-domain]  Cd Length: 320  Bit Score: 158.16  E-value: 1.92e-42
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316060223  939 NRPKNRYTNILPYDFSRVKLVSMHNDegADYINANYIPGYRHSKEYIATQGPLPETRNDFWKMVLQQKSPIIVMLTQCNE 1018
Cdd:PHA02738    49 NRKLNRYLDAVCFDHSRVILPAERNR--GDYINANYVDGFEYKKKFICGQAPTRQTCYDFYRMLWMEHVQIIVMLCKKKE 126

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316060223 1019 RRRVKCDHYWPFTDEPVM-YGDISVEMLSEEGFPEWIIRKFRLGYADE-TLDVLHLNYTSWPDHGVPtvNAIESILQFVH 1096
Cdd:PHA02738   127 NGREKCFPYWSDVEQGSIrFGKFKITTTQVETHPHYVKSTLLLTDGTSaTQTVTHFNFTAWPDHDVP--KNTSEFLNFVL 204

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316060223 1097 IVRQ-QADRTKD------------PVIVHCSAGVGRTGTFMALDRLMQHIREHEFVDILGMVSDMRSHRLSMVQTEEQYV 1163
Cdd:PHA02738   205 EVRQcQKELAQEslqighnrlqppPIVVHCNAGLGRTPCYCVVDISISRFDACATVSIPSIVSSIRNQRYYSLFIPFQYF 284


                   ....*.
gi 1316060223 1164 FIHQCV 1169
Cdd:PHA02738   285 FCYRAV 290
R-PTP-N-N2 cd14546
PTP-like domain of receptor-type tyrosine-protein phosphatase-like N and N2; Receptor-type ...
 969-1169 6.97e-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: 152.60  E-value: 6.97e-42
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316060223  969 YINANYIpgYRHSKE---YIATQGPLPETRNDFWKMVLQQKSPIIVMLTQCNERRRVKCDHYWPFTDEPVmYGDISVEML 1045
Cdd:cd14546      1 YINASTI--YDHDPRnpaYIATQGPLPHTIADFWQMIWEQGCVVIVMLTRLQENGVKQCARYWPEEGSEV-YHIYEVHLV 77

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316060223 1046 SEEGFPE-WIIRKFRLG--YADETLDVLHLNYTSWPDHGVPTvnAIESILQFVHIVRQQADRTKDPVIVHCSAGVGRTGT 1122
Cdd:cd14546     78 SEHIWCDdYLVRSFYLKnlQTSETRTVTQFHFLSWPDEGIPA--SAKPLLEFRRKVNKSYRGRSCPIVVHCSDGAGRTGT 155

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|.
gi 1316060223 1123 F----MALDRLMQHIREhefVDILGMVSDMRSHRLSMVQTEEQYVFIHQCV 1169
Cdd:cd14546    156 YilidMVLNRMAKGAKE---IDIAATLEHLRDQRPGMVKTKDQFEFVLTAV 203
PHA02742 PHA02742
protein tyrosine phosphatase; Provisional
 939-1170 7.38e-42

protein tyrosine phosphatase; Provisional


Pssm-ID: 165109 [Multi-domain]  Cd Length: 303  Bit Score: 155.93  E-value: 7.38e-42
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316060223  939 NRPKNRYTNILPYDFSRVKLVSmhNDEGADYINANYIPGYRHSKEYIATQGPLPETRNDFWKMVLQQKSPIIVMLTQCNE 1018
Cdd:PHA02742    52 NMKKCRYPDAPCFDRNRVILKI--EDGGDDFINASYVDGHNAKGRFICTQAPLEETALDFWQAIFQDQVRVIVMITKIME 129

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316060223 1019 RRRVKCDHYW-PFTDEPVMYGDISVEMLSEEGFPEWIIRKFRLGYAD--ETLDVLHLNYTSWPDHGVPTvnAIESILQFV 1095
Cdd:PHA02742   130 DGKEACYPYWmPHERGKATHGEFKIKTKKIKSFRNYAVTNLCLTDTNtgASLDIKHFAYEDWPHGGLPR--DPNKFLDFV 207

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316060223 1096 HIVRqQADRTKD------------PVIVHCSAGVGRTGTFMALDRLMQHIREHEFVDILGMVSDMRSHRLSMVQTEEQYV 1163
Cdd:PHA02742   208 LAVR-EADLKADvdikgenivkepPILVHCSAGLDRAGAFCAIDICISKYNERAIIPLLSIVRDLRKQRHNCLSLPQQYI 286


                   ....*..
gi 1316060223 1164 FIHQCVL 1170
Cdd:PHA02742   287 FCYFIVL 293
R-PTPc-typeIIb-2 cd14556
PTP domain of type IIb (or R2B) subfamily receptor-type tyrosine-protein phosphatases, repeat ...
 969-1167 1.32e-41

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: 151.79  E-value: 1.32e-41
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316060223  969 YINANYIPGYRHSKEYIATQGPLPETRNDFWKMVLQQKSPIIVMLTQCNERRRvKCDHYWPftdEPVM--YGDISVEMLS 1046
Cdd:cd14556      1 YINAALLDSYKQPAAFIVTQHPLPNTVTDFWRLVYDYGCTSIVMLNQLDPKDQ-SCPQYWP---DEGSgtYGPIQVEFVS 76

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316060223 1047 EEGFPEWIIRKFRL----GYADETLDVLHLNYTSWPDHGvPTVNAIESILQFVHIVRQ-QADRTKDPVIVHCSAGVGRTG 1121
Cdd:cd14556     77 TTIDEDVISRIFRLqnttRPQEGYRMVQQFQFLGWPRDR-DTPPSKRALLKLLSEVEKwQEQSGEGPIVVHCLNGVGRSG 155

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*.
gi 1316060223 1122 TFMALDRLMQHIREHEFVDILGMVSDMRSHRLSMVQTEEQYVFIHQ 1167
Cdd:cd14556    156 VFCAISSVCERIKVENVVDVFQAVKTLRNHRPNMVETEEQYKFCYD 201
PHA02747 PHA02747
protein tyrosine phosphatase; Provisional
 937-1166 4.33e-38

protein tyrosine phosphatase; Provisional


Pssm-ID: 165114 [Multi-domain]  Cd Length: 312  Bit Score: 145.14  E-value: 4.33e-38
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316060223  937 PVNRPKNRYTNILPYDFSRVKLVSmHNDEGADYINANYIPGYRHSKEYIATQGPLPETRNDFWKMVLQQKSPIIVMLTQC 1016
Cdd:PHA02747    49 PENQPKNRYWDIPCWDHNRVILDS-GGGSTSDYIHANWIDGFEDDKKFIATQGPFAETCADFWKAVWQEHCSIIVMLTPT 127

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316060223 1017 NERR-RVKCDHYW-PFTDEPVMYGDISVEMLSEEGFPEWIIRKFRL--GYADETLDVLHLNYTSWPDHGVPT--VNAIES 1090
Cdd:PHA02747   128 KGTNgEEKCYQYWcLNEDGNIDMEDFRIETLKTSVRAKYILTLIEItdKILKDSRKISHFQCSEWFEDETPSdhPDFIKF 207

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316060223 1091 IlQFVHIVRQQA-------DRTKDPVIVHCSAGVGRTGTFMALDRLMQHIREHEFVDILGMVSDMRSHRLSMVQTEEQYV 1163
Cdd:PHA02747   208 I-KIIDINRKKSgklfnpkDALLCPIVVHCSDGVGKTGIFCAVDICLNQLVKRKAICLAKTAEKIREQRHAGIMNFDDYL 286


                   ...
gi 1316060223 1164 FIH 1166
Cdd:PHA02747   287 FIQ 289
PTPc_motif smart00404
Protein tyrosine phosphatase, catalytic domain motif;
1069-1170 6.03e-37

Protein tyrosine phosphatase, catalytic domain motif;


Pssm-ID: 214649 [Multi-domain]  Cd Length: 105  Bit Score: 134.41  E-value: 6.03e-37
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316060223  1069 VLHLNYTSWPDHGVPTvnAIESILQFVHIVR--QQADRTKDPVIVHCSAGVGRTGTFMALDRLMQHIR-EHEFVDILGMV 1145
Cdd:smart00404    2 VKHYHYTGWPDHGVPE--SPDSILELLRAVKknLNQSESSGPVVVHCSAGVGRTGTFVAIDILLQQLEaEAGEVDIFDTV 79

                            90       100
                    ....*....|....*....|....*
gi 1316060223  1146 SDMRSHRLSMVQTEEQYVFIHQCVL 1170
Cdd:smart00404   80 KELRSQRPGMVQTEEQYLFLYRALL 104
PTPc_DSPc smart00012
Protein tyrosine phosphatase, catalytic domain, undefined specificity; Protein tyrosine ...
 1069-1170 6.03e-37

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: 134.41  E-value: 6.03e-37
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316060223  1069 VLHLNYTSWPDHGVPTvnAIESILQFVHIVR--QQADRTKDPVIVHCSAGVGRTGTFMALDRLMQHIR-EHEFVDILGMV 1145
Cdd:smart00012    2 VKHYHYTGWPDHGVPE--SPDSILELLRAVKknLNQSESSGPVVVHCSAGVGRTGTFVAIDILLQQLEaEAGEVDIFDTV 79

                            90       100
                    ....*....|....*....|....*
gi 1316060223  1146 SDMRSHRLSMVQTEEQYVFIHQCVL 1170
Cdd:smart00012   80 KELRSQRPGMVQTEEQYLFLYRALL 104
PTPc-N21 cd14598
catalytic domain of tyrosine-protein phosphatase non-receptor type 21; Tyrosine-protein ...
 969-1175 1.12e-36

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: 138.18  E-value: 1.12e-36
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316060223  969 YINANYIPGYRHSKE--YIATQGPLPETRNDFWKMVLQQKSPIIVMLTQCNERRRVKCDHYWPF---TDEPVMYG--DIS 1041
Cdd:cd14598      1 YINASHIKVTVGGKEwdYIATQGPLQNTCQDFWQMVWEQGVAIIAMVTAEEEGGREKSFRYWPRlgsRHNTVTYGrfKIT 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316060223 1042 VEMLSEEGFPEWIIRKFRLGYADETLDVLHLNYTSWPDHGVPT-VNAIESILQFVHIVRQQADRTKD------PVIVHCS 1114
Cdd:cd14598     81 TRFRTDSGCYATTGLKIKHLLTGQERTVWHLQYTDWPEHGCPEdLKGFLSYLEEIQSVRRHTNSTIDpkspnpPVLVHCS 160

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1316060223 1115 AGVGRTGTFMaLDRLMQHIREH-EFVDILGMVSDMRSHRLSMVQTEEQYVFIHQcVLLMWQK 1175
Cdd:cd14598    161 AGVGRTGVVI-LSEIMIACLEHnEMLDIPRVLDMLRQQRMMMVQTLSQYTFVYK-VLIQFLK 220
PHA02746 PHA02746
protein tyrosine phosphatase; Provisional
 937-1169 2.39e-36

protein tyrosine phosphatase; Provisional


Pssm-ID: 165113 [Multi-domain]  Cd Length: 323  Bit Score: 140.55  E-value: 2.39e-36
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316060223  937 PVNRPKNRYTNILPYDFSRV-------------------KLVSMHNDEGADYINANYIPGYRHSKEYIATQGPLPETRND 997
Cdd:PHA02746    49 KENLKKNRFHDIPCWDHSRVvinaheslkmfdvgdsdgkKIEVTSEDNAENYIHANFVDGFKEANKFICAQGPKEDTSED 128

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316060223  998 FWKMVLQQKSPIIVMLTQCnERRRVKCDHYWPF-TDEPVMYGDISVEMLseEGFPEWIIRKFRLGYADETLD----VLHL 1072
Cdd:PHA02746   129 FFKLISEHESQVIVSLTDI-DDDDEKCFELWTKeEDSELAFGRFVAKIL--DIIEELSFTKTRLMITDKISDtsreIHHF 205

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316060223 1073 NYTSWPDHGVPT-----VNAIESILQFVHIVRQQAD---RTKDPVIVHCSAGVGRTGTFMALDRLMQHIREHEFVDILGM 1144
Cdd:PHA02746   206 WFPDWPDNGIPTgmaefLELINKVNEEQAELIKQADndpQTLGPIVVHCSAGIGRAGTFCAIDNALEQLEKEKEVCLGEI 285

                          250       260
                   ....*....|....*....|....*
gi 1316060223 1145 VSDMRSHRLSMVQTEEQYVFIHQCV 1169
Cdd:PHA02746   286 VLKIRKQRHSSVFLPEQYAFCYKAL 310
R-PTP-Z-2 cd17669
catalytic domain of receptor-type tyrosine-protein phosphatase Z, repeat 2; Receptor-type ...
 969-1170 6.35e-30

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: 118.17  E-value: 6.35e-30
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316060223  969 YINANYIPGYRHSKEYIATQGPLPETRNDFWKMVLQQKSPIIVMLTQCNERRRVKCdHYWPFTDEPVMYGDISVEMLSEE 1048
Cdd:cd17669      1 YINASYIMGYYQSNEFIITQHPLLHTIKDFWRMIWDHNAQLIVMLPDGQNMAEDEF-VYWPNKDEPINCETFKVTLIAEE 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316060223 1049 GF-----PEWIIRKFRLGYA--DETLDVLHLNYTSWPDHGVPtvnaIESILQFVHIVRQQADRTKDPVIVHCSAGVGRTG 1121
Cdd:cd17669     80 HKclsneEKLIIQDFILEATqdDYVLEVRHFQCPKWPNPDSP----ISKTFELISIIKEEAANRDGPMIVHDEHGGVTAG 155

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*....
gi 1316060223 1122 TFMALDRLMQHIREHEFVDILGMVSDMRSHRLSMVQTEEQYVFIHQCVL 1170
Cdd:cd17669    156 TFCALTTLMHQLEKENSVDVYQVAKMINLMRPGVFTDIEQYQFLYKAIL 204
R5-PTP-2 cd14550
PTP-like domain of R5 subfamily receptor-type tyrosine-protein phosphatases, repeat 2; The R5 ...
 969-1167 1.08e-29

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: 117.42  E-value: 1.08e-29
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316060223  969 YINANYIPGYRHSKEYIATQGPLPETRNDFWKMVLQQKSPIIVMLTQCNERRRVKCdhYWPFTDEPVMYGDISVEMLSEE 1048
Cdd:cd14550      1 YINASYLQGYRRSNEFIITQHPLEHTIKDFWQMIWDHNSQTIVMLTDNELNEDEPI--YWPTKEKPLECETFKVTLSGED 78

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316060223 1049 -----GFPEWIIRKFRL--GYADETLDVLHLNYTSWPDHGVPtvnaIESILQFVHIVRQQADRTKDPVIVHCSAGVGRTG 1121
Cdd:cd14550     79 hsclsNEIRLIVRDFILesTQDDYVLEVRQFQCPSWPNPCSP----IHTVFELINTVQEWAQQRDGPIVVHDRYGGVQAA 154

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*.
gi 1316060223 1122 TFMALDRLMQHIREHEFVDILGMVSDMRSHRLSMVQTEEQYVFIHQ 1167
Cdd:cd14550    155 TFCALTTLHQQLEHESSVDVYQVAKLYHLMRPGVFTSKEDYQFLYK 200
R-PTPc-T-2 cd14634
PTP domain of receptor-type tyrosine-protein phosphatase T, repeat 2; Receptor-type ...
 969-1170 2.09e-29

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


Pssm-ID: 350482 [Multi-domain]  Cd Length: 206  Bit Score: 116.66  E-value: 2.09e-29
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316060223  969 YINANYIPGYRHSKEYIATQGPLPETRNDFWKMVLQQKSPIIVMLTQCNERRRvkCDHYWPfTDEPVMYGDISVEMLSEE 1048
Cdd:cd14634      1 YINAALMDSHKQPAAFIVTQHPLPNTVADFWRLVFDYNCSSVVMLNEMDAAQL--CMQYWP-EKTSCCYGPIQVEFVSAD 77

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316060223 1049 GFPEWIIRKFRLGYADETLD----VLHLNYTSWPDH--GVPTVNAIESILQFVHIVRQQADRTKDPVIVHCSAGVGRTGT 1122
Cdd:cd14634     78 IDEDIISRIFRICNMARPQDgyriVQHLQYIGWPAYrdTPPSKRSILKVVRRLEKWQEQYDGREGRTVVHCLNGGGRSGT 157

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*...
gi 1316060223 1123 FMALDRLMQHIREHEFVDILGMVSDMRSHRLSMVQTEEQYVFIHQCVL 1170
Cdd:cd14634    158 FCAICSVCEMIQQQNIIDVFHTVKTLRNNKSNMVETLEQYKFVYEVAL 205
R-PTPc-U-2 cd14637
PTP domain of receptor-type tyrosine-protein phosphatase U, repeat 2; Receptor-type ...
 969-1170 3.08e-27

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


Pssm-ID: 350485 [Multi-domain]  Cd Length: 207  Bit Score: 110.38  E-value: 3.08e-27
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316060223  969 YINANYIPGYRHSKEYIATQGPLPETRNDFWKMVLQQKSPIIVMLTQCNERRRV-KCDHYWPftdEPVM--YGDISVEML 1045
Cdd:cd14637      1 YINAALTDSYTRSAAFIVTLHPLQNTTTDFWRLVYDYGCTSVVMLNQLNQSNSAwPCLQYWP---EPGLqqYGPMEVEFV 77

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316060223 1046 SEEGFPEWIIRKFRLG----YADETLDVLHLNYTSWPDHGvPTVNAIESILQFVHIVRQ-QADRTKDPVIVHCSAGVGRT 1120
Cdd:cd14637     78 SGSADEDIVTRLFRVQnitrLQEGHLMVRHFQFLRWSAYR-DTPDSKKAFLHLLASVEKwQRESGEGRTVVHCLNGGGRS 156

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|
gi 1316060223 1121 GTFMALDRLMQHIREHEFVDILGMVSDMRSHRLSMVQTEEQYVFIHQCVL 1170
Cdd:cd14637    157 GTYCASAMILEMIRCHNIVDVFYAVKTLRNYKPNMVETLEQYRFCYEIAL 206
R-PTP-G-2 cd17670
PTP-like domain of receptor-type tyrosine-protein phosphatase G, repeat 2; Receptor-type ...
 969-1170 4.59e-27

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: 110.15  E-value: 4.59e-27
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316060223  969 YINANYIPGYRHSKEYIATQGPLPETRNDFWKMVLQQKSPIIVMLTQcNERRRVKCDHYWPFTDEPVMYGDISVEMLSEE 1048
Cdd:cd17670      1 YINASYIMGYYRSNEFIITQHPLPHTTKDFWRMIWDHNAQIIVMLPD-NQGLAEDEFVYWPSREESMNCEAFTVTLISKD 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316060223 1049 GF-----PEWIIRKFRLGYA--DETLDVLHLNYTSWPDHGVPtvnaIESILQFVHIVRQQADRTKDPVIVHCSAGVGRTG 1121
Cdd:cd17670     80 RLclsneEQIIIHDFILEATqdDYVLEVRHFQCPKWPNPDAP----ISSTFELINVIKEEALTRDGPTIVHDEFGAVSAG 155

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*....
gi 1316060223 1122 TFMALDRLMQHIREHEFVDILGMVSDMRSHRLSMVQTEEQYVFIHQCVL 1170
Cdd:cd17670    156 TLCALTTLSQQLENENAVDVYQVAKMINLMRPGVFTDIEQYQFLYKAML 204
R-PTPc-K-2 cd14636
PTP domain of receptor-type tyrosine-protein phosphatase K, repeat 2; Receptor-type ...
 969-1170 1.33e-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: 102.80  E-value: 1.33e-24
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316060223  969 YINANYIPGYRHSKEYIATQGPLPETRNDFWKMVLQQKSPIIVMLTQCNERRrvKCDHYWPfTDEPVMYGDISVEMLSEE 1048
Cdd:cd14636      1 YINAALMDSYRQPAAFIVTQHPLPNTVKDFWRLVYDYGCTSIVMLNEVDLAQ--GCPQYWP-EEGMLRYGPIQVECMSCS 77

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316060223 1049 GFPEWIIRKFRL--------GYadetLDVLHLNYTSWPDH-GVPTVNA--IESILQfVHIVRQQADRTKDPVIVHCSAGV 1117
Cdd:cd14636     78 MDCDVISRIFRIcnltrpqeGY----LMVQQFQYLGWASHrEVPGSKRsfLKLILQ-VEKWQEECDEGEGRTIIHCLNGG 152

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|...
gi 1316060223 1118 GRTGTFMALDRLMQHIREHEFVDILGMVSDMRSHRLSMVQTEEQYVFIHQCVL 1170
Cdd:cd14636    153 GRSGMFCAISIVCEMIKRQNVVDVFHAVKTLRNSKPNMVETPEQYRFCYDVAL 205
R-PTPc-M-2 cd14635
PTP domain of receptor-type tyrosine-protein phosphatase M, repeat 2; Receptor-type ...
 969-1170 5.93e-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: 95.14  E-value: 5.93e-22
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316060223  969 YINANYIPGYRHSKEYIATQGPLPETRNDFWKMVLQQKSPIIVMLTQCNERRRvkCDHYWPfTDEPVMYGDISVEMLSEE 1048
Cdd:cd14635      1 YINAALMDSYKQPSAFIVTQHPLPNTVKDFWRLVLDYHCTSIVMLNDVDPAQL--CPQYWP-ENGVHRHGPIQVEFVSAD 77

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316060223 1049 GFPEWIIRKFRLGYADETLD----VLHLNYTSWPDHGvPTVNAIESILQFVHIV---RQQADRTKDPVIVHCSAGVGRTG 1121
Cdd:cd14635     78 LEEDIISRIFRIYNAARPQDgyrmVQQFQFLGWPMYR-DTPVSKRSFLKLIRQVdkwQEEYNGGEGRTVVHCLNGGGRSG 156

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*....
gi 1316060223 1122 TFMALDRLMQHIREHEFVDILGMVSDMRSHRLSMVQTEEQYVFIHQCVL 1170
Cdd:cd14635    157 TFCAISIVCEMLRHQRAVDVFHAVKTLRNNKPNMVDLLDQYKFCYEVAL 205
PTP_YopH-like cd14559
YopH and related bacterial protein tyrosine phosphatases; Yersinia outer protein H (YopH) ...
 943-1163 5.00e-17

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: 81.68  E-value: 5.00e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316060223  943 NRYTNILpydfSRVKlvsmhNDEGADyINANYIP-GYRHSkeYIATQGPLPETRNDFWKMVLQQKSPIIVMLTQCNERRR 1021
Cdd:cd14559      1 NRFTNIQ----TRVS-----TPVGKN-LNANRVQiGNKNV--AIACQYPKNEQLEDHLKMLADNRTPCLVVLASNKDIQR 68

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316060223 1022 VKCDHYWPFTDEpvmYGDISV---EMLSEEGFPEWIIRKFRLGYADE----TLDVLHLnyTSWPDHGVPTVNAIESILQF 1094
Cdd:cd14559     69 KGLPPYFRQSGT---YGSVTVkskKTGKDELVDGLKADMYNLKITDGnktiTIPVVHV--TNWPDHTAISSEGLKELADL 143

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316060223 1095 VHIVRQ-----------QADRTKD---PVIvHCSAGVGRTGTFMALDRLMQHIREHEFVDIlgmVSDMRSHRLS-MVQTE 1159
Cdd:cd14559    144 VNKSAEekrnfykskgsSAINDKNkllPVI-HCRAGVGRTGQLAAAMELNKSPNNLSVEDI---VSDMRTSRNGkMVQKD 219


                   ....
gi 1316060223 1160 EQYV 1163
Cdd:cd14559    220 EQLD 223
CDC14 COG2453
Protein-tyrosine phosphatase [Signal transduction mechanisms];
1062-1167 6.68e-14

Protein-tyrosine phosphatase [Signal transduction mechanisms];


Pssm-ID: 441989 [Multi-domain]  Cd Length: 140  Bit Score: 70.00  E-value: 6.68e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316060223 1062 YADETLDVLHLNytsWPDHGVPTVNAIESILQFVHivrqQADRTKDPVIVHCSAGVGRTGTFMALDrLMQhiREHEFVDI 1141
Cdd:COG2453     43 LEEAGLEYLHLP---IPDFGAPDDEQLQEAVDFID----EALREGKKVLVHCRGGIGRTGTVAAAY-LVL--LGLSAEEA 112

                           90       100
                   ....*....|....*....|....*.
gi 1316060223 1142 LGMVsdmRSHRLSMVQTEEQYVFIHQ 1167
Cdd:COG2453    113 LARV---RAARPGAVETPAQRAFLER 135
PHA02740 PHA02740
protein tyrosine phosphatase; Provisional
 938-1167 1.09e-09

protein tyrosine phosphatase; Provisional


Pssm-ID: 165107 [Multi-domain]  Cd Length: 298  Bit Score: 61.14  E-value: 1.09e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316060223  938 VNRPK--NRYTNILPYDFSRVKLvsmHNDEGAdyINANYIPGYRHSKEYIATQGPLPETRNDFWKMVLQQKSPIIVMLTQ 1015
Cdd:PHA02740    50 ENKAKdeNLALHITRLLHRRIKL---FNDEKV--LDARFVDGYDFEQKFICIINLCEDACDKFLQALSDNKVQIIVLISR 124

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316060223 1016 CNERrrvKC-DHYWPFTDEPVM-YGDISVEMLSEEGFPEWIIRKFRL----GYADEtldVLHLNYTSWPDHGVPtvNAIE 1089
Cdd:PHA02740   125 HADK---KCfNQFWSLKEGCVItSDKFQIETLEIIIKPHFNLTLLSLtdkfGQAQK---ISHFQYTAWPADGFS--HDPD 196

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316060223 1090 SILQF--------VHIVRQQADRTKDPVIVHCSAGVGRTGTFMALDRLMQHIREHEFVDILGMVSDMRSHRLSMVQTEEQ 1161
Cdd:PHA02740   197 AFIDFfcniddlcADLEKHKADGKIAPIIIDCIDGISSSAVFCVFDICATEFDKTGMLSIANALKKVRQKKYGCMNCLDD 276


                   ....*.
gi 1316060223 1162 YVFIHQ 1167
Cdd:PHA02740   277 YVFCYH 282
PTP_DSP_cys cd14494
cys-based protein tyrosine phosphatase and dual-specificity phosphatase superfamily; This ...
 1080-1167 4.81e-09

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: 55.05  E-value: 4.81e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316060223 1080 HGVPT-VNAIESILQFVHIVRQQADRTKDPVIVHCSAGVGRTGTFMALDRLMQHIREHEfvDILGMVSDMRSHRlsMVQT 1158
Cdd:cd14494     29 LGVTTiVDLTLAMVDRFLEVLDQAEKPGEPVLVHCKAGVGRTGTLVACYLVLLGGMSAE--EAVRIVRLIRPGG--IPQT 104


                   ....*....
gi 1316060223 1159 EEQYVFIHQ 1167
Cdd:cd14494    105 IEQLDFLIK 113
DUSP23 cd14504
dual specificity phosphatase 23; Dual specificity phosphatase 23 (DUSP23), also known as ...
 1078-1167 3.23e-08

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


Pssm-ID: 350354 [Multi-domain]  Cd Length: 142  Bit Score: 53.82  E-value: 3.23e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316060223 1078 PDHGVPTvnaIESILQFVHIVrQQADRTKDPVIVHCSAGVGRTGTFMALdRLMQhireHEFVDILGMVSDMRSHRLSMVQ 1157
Cdd:cd14504     58 EDYTPPT---LEQIDEFLDIV-EEANAKNEAVLVHCLAGKGRTGTMLAC-YLVK----TGKISAVDAINEIRRIRPGSIE 128

                           90
                   ....*....|
gi 1316060223 1158 TEEQYVFIHQ 1167
Cdd:cd14504    129 TSEQEKFVIQ 138
CDC14_C cd14499
C-terminal dual-specificity phosphatase domain of CDC14 family proteins; The cell division ...
 1078-1132 1.36e-06

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


Pssm-ID: 350349 [Multi-domain]  Cd Length: 174  Bit Score: 49.76  E-value: 1.36e-06
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1316060223 1078 PDHGVPTvnaIESILQFVHIVrqqaDRTKDPVIVHCSAGVGRTGTFMALdRLMQH 1132
Cdd:cd14499     88 PDGSTPS---DDIVKKFLDIC----ENEKGAIAVHCKAGLGRTGTLIAC-YLMKH 134
fn3 pfam00041
Fibronectin type III domain;
730-802 5.71e-06

Fibronectin type III domain;


Pssm-ID: 394996 [Multi-domain]  Cd Length: 85  Bit Score: 45.48  E-value: 5.71e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316060223  730 PPRLLLAVNATHSSVTLLWSE----DGVVDYYQVLCRP---NWASKELKAGEPITStaqvLTVSGLVPSSSYNCSVTSFS 802
Cdd:pfam00041    2 APSNLTVTDVTSTSLTVSWTPppdgNGPITGYEVEYRPknsGEPWNEITVPGTTTS----VTLTGLKPGTEYEVRVQAVN 77
PTP_PTPDC1 cd14506
protein tyrosine phosphatase domain of PTP domain-containing protein 1; protein tyrosine ...
 1076-1166 5.90e-06

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: 48.50  E-value: 5.90e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316060223 1076 SWPDHGVPTVNAIESILQfvhiVRQQADRTKDPVIVHCSAGVGRTGTFMALdRLMQHIRehefvdilgMVSD-----MRS 1150
Cdd:cd14506     83 GWKDYGVPSLTTILDIVK----VMAFALQEGGKVAVHCHAGLGRTGVLIAC-YLVYALR---------MSADqairlVRS 148

                           90
                   ....*....|....*.
gi 1316060223 1151 HRLSMVQTEEQYVFIH 1166
Cdd:cd14506    149 KRPNSIQTRGQVLCVR 164
CDKN3-like cd14505
cyclin-dependent kinase inhibitor 3 and similar proteins; This family is composed of ...
 1067-1167 3.82e-05

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


Pssm-ID: 350355 [Multi-domain]  Cd Length: 163  Bit Score: 45.33  E-value: 3.82e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316060223 1067 LDVLHLnytSWPDHGVPTvnAIESILQFVHIVRQQADRTKDpVIVHCSAGVGRTGTFMA--LDRLMQHIREHEFVDILgm 1144
Cdd:cd14505     73 ITWHHL---PIPDGGVPS--DIAQWQELLEELLSALENGKK-VLIHCKGGLGRTGLIAAclLLELGDTLDPEQAIAAV-- 144

                           90       100
                   ....*....|....*....|...
gi 1316060223 1145 vsdmRSHRLSMVQTEEQYVFIHQ 1167
Cdd:cd14505    145 ----RALRPGAIQTPKQENFLHQ 163
PTPlike_phytase pfam14566
Inositol hexakisphosphate; Inositol hexakisphosphate, often called phytate, is found in ...
 1078-1130 1.03e-04

Inositol hexakisphosphate; Inositol hexakisphosphate, often called phytate, is found in abundance in seeds and acting as an inorganic phosphate reservoir. Phytases are phosphatases that hydrolyze phytate to less-phosphorylated myo-inositol derivatives and inorganic phosphate. The active-site sequence (HCXXGXGR) of the phytase identified from the gut micro-organizm Selenomonas ruminantium forms a loop (P loop) at the base of a substrate binding pocket that is characteriztic of protein tyrosine phosphatases (PTPs). The depth of this pocket is an important determinant of the substrate specificity of PTPs. In humans this enzyme is thought to aid bone mineralization and salvage the inositol moiety prior to apoptosis.


Pssm-ID: 464208 [Multi-domain]  Cd Length: 157  Bit Score: 43.84  E-value: 1.03e-04
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|...
gi 1316060223 1078 PDHGVPTVNAIEsilQFVHIVRQQADRTkdPVIVHCSAGVGRTGTFMALDRLM 1130
Cdd:pfam14566  109 TDEKAPLEEDFD---ALISIVKDAPEDT--ALVFNCQMGRGRTTTAMVIADLV 156
FN3 cd00063
Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein ...
 728-816 1.28e-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: 42.10  E-value: 1.28e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316060223  728 PAPPRLLLAVNATHSSVTLLWS----EDGVVDYYQVLCRPNWASKELKAGEPITSTAQVlTVSGLVPSSSYNCSVTSFSY 803
Cdd:cd00063      1 PSPPTNLRVTDVTSTSVTLSWTppedDGGPITGYVVEYREKGSGDWKEVEVTPGSETSY-TLTGLKPGTEYEFRVRAVNG 79

                           90
                   ....*....|....
gi 1316060223  804 SSASRPA-RITVTT 816
Cdd:cd00063     80 GGESPPSeSVTVTT 93
PRK15375 PRK15375
type III secretion system effector GTPase-activating protein SptP;
985-1172 1.34e-04

type III secretion system effector GTPase-activating protein SptP;


Pssm-ID: 185273 [Multi-domain]  Cd Length: 535  Bit Score: 45.95  E-value: 1.34e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316060223  985 IATQGPLPETRND----FWKMVLQQKSPIIVMLTQCNERRRVKCDHYW--PFTDEPVMYGDISVEMLSEEGFPEWIIRKF 1058
Cdd:PRK15375   335 VALAGSYPKNTPDaleaHMKMLLEKECSCLVVLTSEDQMQAKQLPPYFrgSYTFGEVHTNSQKVSSASQGEAIDQYNMQL 414

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316060223 1059 RLGYADETLDVLHLNytSWPDHG-VPTVNAIESILQFVHIVRQ-----QADRTKDPVIVHCSAGVGRTGTfMALDRLMQH 1132
Cdd:PRK15375   415 SCGEKRYTIPVLHVK--NWPDHQpLPSTDQLEYLADRVKNSNQngapgRSSSDKHLPMIHCLGGVGRTGT-MAAALVLKD 491

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|..
gi 1316060223 1133 IREHEFVDILGMVSDMRSHRlsMVQTEEQYVFIH--QCVLLM 1172
Cdd:PRK15375   492 NPHSNLEQVRADFRNSRNNR--MLEDASQFVQLKamQAQLLM 531
PTPLP-like cd14495
Protein tyrosine phosphatase-like domains of phytases and similar domains; This subfamily ...
 1078-1142 3.15e-04

Protein tyrosine phosphatase-like domains of phytases and similar domains; This subfamily contains the tandem protein tyrosine phosphatase (PTP)-like domains of protein tyrosine phosphatase-like phytases (PTPLPs) and similar domains including the PTP domain of Pseudomonas syringae tyrosine-protein phosphatase hopPtoD2. PTPLPs, also known as cysteine phytases, are one of four known classes of phytases, enzymes that degrade phytate (inositol hexakisphosphate [InsP(6)]) to less-phosphorylated myo-inositol derivatives. Phytate is the most abundant cellular inositol phosphate and plays important roles in a broad scope of cellular processes, including DNA repair, RNA processing and export, development, apoptosis, and pathogenicity. PTPLPs adopt a PTP fold, including the active-site signature sequence (CX5R(S/T)) and utilize a classical PTP reaction mechanism. However, these enzymes display no catalytic activity against classical PTP substrates due to several unique structural features that confer specificity for myo-inositol polyphosphates.


Pssm-ID: 350345  Cd Length: 278  Bit Score: 43.90  E-value: 3.15e-04
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1316060223 1078 PDHGVPTVNAIEsilQFVHIVRQ-QADRTkdpVIVHCSAGVGRTGTFMALDRLMQHIREHEFVDIL 1142
Cdd:cd14495    163 TDHVWPDDEEID---AFVAFYRSlPADAW---LHFHCRAGKGRTTTFMVMYDMLKNPKDVSFDDII 222
PTPMT1 cd14524
protein-tyrosine phosphatase mitochondrial 1; Protein-tyrosine phosphatase mitochondrial 1 or ...
 1079-1162 3.16e-04

protein-tyrosine phosphatase mitochondrial 1; Protein-tyrosine phosphatase mitochondrial 1 or PTP localized to the mitochondrion 1 (PTPMT1), also called phosphoinositide lipid phosphatase (PLIP), phosphatidylglycerophosphatase and protein-tyrosine phosphatase 1, or PTEN-like phosphatase, is a lipid phosphatase or phosphatidylglycerophosphatase (EC 3.1.3.27) which dephosphorylates phosphatidylglycerophosphate (PGP) to phosphatidylglycerol (PG). It is targeted to the mitochondrion by an N-terminal signal sequence and is found anchored to the matrix face of the inner membrane. It is essential for the biosynthesis of cardiolipin, a mitochondrial-specific phospholipid regulating the membrane integrity and activities of the organelle. PTPMT1 also plays a crucial role in hematopoietic stem cell (HSC) function, and has been shown to display activity toward phosphoprotein substrates.


Pssm-ID: 350374 [Multi-domain]  Cd Length: 149  Bit Score: 42.25  E-value: 3.16e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316060223 1079 DH-GVPTVNAIESILQFVHIVRQQADRtkdpVIVHCSAGVGRTGTfMALDRLMQHiREHEFVDILGMVSDMRSH---RLS 1154
Cdd:cd14524     65 DFtGVPSLEDLEKGVDFILKHREKGKS----VYVHCKAGRGRSAT-IVACYLIQH-KGWSPEEAQEFLRSKRPHillRLS 138


                   ....*...
gi 1316060223 1155 MVQTEEQY 1162
Cdd:cd14524    139 QREVLEEF 146
FN3 cd00063
Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein ...
 437-527 3.99e-04

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


Pssm-ID: 238020 [Multi-domain]  Cd Length: 93  Bit Score: 40.56  E-value: 3.99e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316060223  437 PQGVSVRLLDSSTAAVSWAPSAQNhNGSLVS-VLSTTCLKPSLSQRMENTYCSEensTSDIISNLTPGAQYRVVVYHTNG 515
Cdd:cd00063      4 PTNLRVTDVTSTSVTLSWTPPEDD-GGPITGyVVEYREKGSGDWKEVEVTPGSE---TSYTLTGLKPGTEYEFRVRAVNG 79

                           90
                   ....*....|..
gi 1316060223  516 PLTSPPSEPVII 527
Cdd:cd00063     80 GGESPPSESVTV 91
fn3 pfam00041
Fibronectin type III domain;
437-522 4.36e-04

Fibronectin type III domain;


Pssm-ID: 394996 [Multi-domain]  Cd Length: 85  Bit Score: 40.48  E-value: 4.36e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316060223  437 PQGVSVRLLDSSTAAVSWAPSAQnHNGSLVSVLSTtcLKPSLSQRMENTYCSEENSTSDIISNLTPGAQYRVVVYHTNGP 516
Cdd:pfam00041    3 PSNLTVTDVTSTSLTVSWTPPPD-GNGPITGYEVE--YRPKNSGEPWNEITVPGTTTSVTLTGLKPGTEYEVRVQAVNGG 79


                   ....*.
gi 1316060223  517 LTSPPS 522
Cdd:pfam00041   80 GEGPPS 85
FN3 cd00063
Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein ...
 531-631 5.34e-04

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


Pssm-ID: 238020 [Multi-domain]  Cd Length: 93  Bit Score: 40.17  E-value: 5.34e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316060223  531 PTGVRELAVYPLGPTAVVLSWQRP--YHVAFRKYILQTFffnpVTLASEWTTYYEIAATASviaTVRVTDLLPAWYYNFR 608
Cdd:cd00063      1 PSPPTNLRVTDVTSTSVTLSWTPPedDGGPITGYVVEYR----EKGSGDWKEVEVTPGSET---SYTLTGLKPGTEYEFR 73

                           90       100
                   ....*....|....*....|....*.
gi 1316060223  609 VSMVT---WGDPpltccdSSTVSFVT 631
Cdd:cd00063     74 VRAVNgggESPP------SESVTVTT 93
TpbA-like cd14529
bacterial protein tyrosine and dual-specificity phosphatases related to Pseudomonas aeruginosa ...
 1070-1126 5.49e-04

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


Pssm-ID: 350378 [Multi-domain]  Cd Length: 158  Bit Score: 41.98  E-value: 5.49e-04
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 1316060223 1070 LHLNYTSWPDH-GVPTVNAIESILQFVhiVRQQADRtkdPVIVHCSAGVGRTGTFMAL 1126
Cdd:cd14529     57 DGVKYVNLPLSaTRPTESDVQSFLLIM--DLKLAPG---PVLIHCKHGKDRTGLVSAL 109
FN3 smart00060
Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, ...
 531-613 6.63e-04

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


Pssm-ID: 214495 [Multi-domain]  Cd Length: 83  Bit Score: 39.91  E-value: 6.63e-04
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316060223   531 PTGVRELAVYPLGPTAVVLSWQRPYHVAFRKYILQtFFFNPVTLASEWTTYYEIAATASVIatvrVTDLLPAWYYNFRVS 610
Cdd:smart00060    1 PSPPSNLRVTDVTSTSVTLSWEPPPDDGITGYIVG-YRVEYREEGSEWKEVNVTPSSTSYT----LTGLKPGTEYEFRVR 75


                    ...
gi 1316060223   611 MVT 613
Cdd:smart00060   76 AVN 78
PTP_VSP_TPTE cd14510
protein tyrosine phosphatase-like catalytic domain of voltage-sensitive phosphatase ...
 1078-1122 7.32e-04

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


Pssm-ID: 350360 [Multi-domain]  Cd Length: 177  Bit Score: 41.96  E-value: 7.32e-04
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*..
gi 1316060223 1078 PDHGVPTVnaiESILQFVHIVRQ--QADRtKDPVIVHCSAGVGRTGT 1122
Cdd:cd14510     82 DDHNVPTL---DEMLSFTAEVREwmAADP-KNVVAIHCKGGKGRTGT 124
FN3 smart00060
Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, ...
 437-515 1.26e-03

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


Pssm-ID: 214495 [Multi-domain]  Cd Length: 83  Bit Score: 39.13  E-value: 1.26e-03
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316060223   437 PQGVSVRLLDSSTAAVSWAPSAQNHNGS-LVSVLSTTCLKPSLSQRMENTycseENSTSDIISNLTPGAQYRVVVYHTNG 515
Cdd:smart00060    4 PSNLRVTDVTSTSVTLSWEPPPDDGITGyIVGYRVEYREEGSEWKEVNVT----PSSTSYTLTGLKPGTEYEFRVRAVNG 79
FN3 COG3401
Fibronectin type 3 domain [General function prediction only];
261-612 1.55e-03

Fibronectin type 3 domain [General function prediction only];


Pssm-ID: 442628 [Multi-domain]  Cd Length: 603  Bit Score: 42.68  E-value: 1.55e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316060223  261 PTPRVSFNTTQNVTDSVAVGNGSRAEEEAEPQSYWLDPTEISPADRDEEFVNAVVSEYEDSNEPGSAM-AVPAEVPVLPT 339
Cdd:COG3401     69 TGGRAGTTSGVAAVAVAAAPPTATGLTTLTGSGSVGGATNTGLTSSDEVPSPAVGTATTATAVAGGAAtAGTYALGAGLY 148

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316060223  340 RLPPVLLELRWLPPRPPTSYDGFNVYIYRDGNSTEMATVDENTHEFFTELTEPGT-YRVQVTTLSSSGdcEARESSADTG 418
Cdd:COG3401    149 GVDGANASGTTASSVAGAGVVVSPDTSATAAVATTSLTVTSTTLVDGGGDIEPGTtYYYRVAATDTGG--ESAPSNEVSV 226

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316060223  419 FTFYLSPSgelleelreRPQGVSVRLLDSSTAAVSWAPSAQNH------------NGSLVSVlsttclkpslsqrmenty 486
Cdd:COG3401    227 TTPTTPPS---------APTGLTATADTPGSVTLSWDPVTESDatgyrvyrsnsgDGPFTKV------------------ 279

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316060223  487 cSEENSTSDIISNLTPGA--QYRVVVYHTNGpLTSPPSEP--VIIDIE-PTGVRELAVYPLGPTAVVLSWQRPYHVAFRK 561
Cdd:COG3401    280 -ATVTTTSYTDTGLTNGTtyYYRVTAVDAAG-NESAPSNVvsVTTDLTpPAAPSGLTATAVGSSSITLSWTASSDADVTG 357

                          330       340       350       360       370
                   ....*....|....*....|....*....|....*....|....*....|.
gi 1316060223  562 YILQtfffnpvTLASEWTTYYEIAATASViATVRVTDLLPAWYYNFRVSMV 612
Cdd:COG3401    358 YNVY-------RSTSGGGTYTKIAETVTT-TSYTDTGLTPGTTYYYKVTAV 400
FN3 smart00060
Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, ...
 728-802 1.66e-03

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


Pssm-ID: 214495 [Multi-domain]  Cd Length: 83  Bit Score: 38.75  E-value: 1.66e-03
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1316060223   728 PAPPRLLLAVNATHSSVTLLWS--EDGVVDYYQVLCRPNWASKELKAGE-PITSTAQVLTVSGLVPSSSYNCSVTSFS 802
Cdd:smart00060    1 PSPPSNLRVTDVTSTSVTLSWEppPDDGITGYIVGYRVEYREEGSEWKEvNVTPSSTSYTLTGLKPGTEYEFRVRAVN 78
FN3 COG3401
Fibronectin type 3 domain [General function prediction only];
579-818 3.85e-03

Fibronectin type 3 domain [General function prediction only];


Pssm-ID: 442628 [Multi-domain]  Cd Length: 603  Bit Score: 41.53  E-value: 3.85e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316060223  579 TTYYEIAATASVIATVRVTDLLPAWYYNFRVSMVTWGDPPLTCCDSSTVSFVTAPEAPH-ISSVDYSQGVLAVRWTygel 657
Cdd:COG3401    179 AVATTSLTVTSTTLVDGGGDIEPGTTYYYRVAATDTGGESAPSNEVSVTTPTTPPSAPTgLTATADTPGSVTLSWD---- 254

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316060223  658 fiDLSHSRMLHWQVEavGKKGPQRGYSV--DVTRNAMRASLpLPPGDIYNLTVTACTERSrNTSVP-NIIKLE-----PA 729
Cdd:COG3401    255 --PVTESDATGYRVY--RSNSGDGPFTKvaTVTTTSYTDTG-LTNGTTYYYRVTAVDAAG-NESAPsNVVSVTtdltpPA 328

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316060223  730 PPRLLLAVNATHSSVTLLW--SEDGVVDYYQVLCRPNWASKELKAGEPITSTAqvLTVSGLVPSSSYNCSVTSFS----Y 803
Cdd:COG3401    329 APSGLTATAVGSSSITLSWtaSSDADVTGYNVYRSTSGGGTYTKIAETVTTTS--YTDTGLTPGTTYYYKVTAVDaagnE 406

                          250
                   ....*....|....*
gi 1316060223  804 SSASRPARITVTTAA 818
Cdd:COG3401    407 SAPSEEVSATTASAA 421
 
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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