NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|998470296|gb|JAP69919|]
View 

putative receptor protein tyrosine phosphatase, partial [Ixodes ricinus]

Protein Classification

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

Name Accession Description Interval E-value
R5-PTPc-1 cd14549
catalytic domain of R5 subfamily receptor-type tyrosine-protein phosphatases, repeat 1; The R5 ...
688-889 1.31e-151

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: 453.35  E-value: 1.31e-151
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 998470296  688 YINANYIDGYHKSRAFIGTQGPLPATFDDYWRMVWEQRVCIIIMITNLVERGRRKCDMYWPKEGTETYGIIQVKLVQEIV 767
Cdd:cd14549     1 YINANYVDGYNKARAYIATQGPLPSTFDDFWRMVWEQNSAIIVMITNLVERGRRKCDQYWPKEGTETYGNIQVTLLSTEV 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 998470296  768 MATYTIRTFAIKNIKVKK--KQASERTVYQYHYTNWPDHGVPDHPLPVLSFVAKSSAANPPAAGPMIVHCSAGVGRTGTY 845
Cdd:cd14549    81 LATYTVRTFSLKNLKLKKvkGRSSERVVYQYHYTQWPDHGVPDYTLPVLSFVRKSSAANPPGAGPIVVHCSAGVGRTGTY 160
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....
gi 998470296  846 IVLDAMLRQMRQRQSVNVYGFLRHIRQQRNYLVQTEEQYVFIHD 889
Cdd:cd14549   161 IVIDSMLQQIQDKGTVNVFGFLKHIRTQRNYLVQTEEQYIFIHD 204
PTP_DSP_cys super family cl28904
cys-based protein tyrosine phosphatase and dual-specificity phosphatase superfamily; This ...
989-1197 1.82e-90

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 cd14550:

Pssm-ID: 475123 [Multi-domain]  Cd Length: 200  Bit Score: 289.99  E-value: 1.82e-90
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 998470296  989 YINATFLQGFNRLREFIVTQHPLMDTMADFWQMVWDHNSQTIVVLSVVDEKEH-PQFWPDTDEEQDYGSFKVKPTGESVA 1067
Cdd:cd14550     1 YINASYLQGYRRSNEFIITQHPLEHTIKDFWQMIWDHNSQTIVMLTDNELNEDePIYWPTKEKPLECETFKVTLSGEDHS 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 998470296 1068 PPVAEEKgalmpgegggLPSRDFILQSTQDDYELACRLLLCPGWPQSCSPLAKAFELVKEVgARQERDQNGPVVIVDRYG 1147
Cdd:cd14550    81 CLSNEIR----------LIVRDFILESTQDDYVLEVRQFQCPSWPNPCSPIHTVFELINTV-QEWAQQRDGPIVVHDRYG 149
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|
gi 998470296 1148 GTEAATFCCLSALYRQLEREKCVDVYMYAKLYHMRRPGIWKSQDDFLFLY 1197
Cdd:cd14550   150 GVQAATFCALTTLHQQLEHESSVDVYQVAKLYHLMRPGVFTSKEDYQFLY 199
FN3 COG3401
Fibronectin type 3 domain [General function prediction only];
196-438 1.62e-20

Fibronectin type 3 domain [General function prediction only];


:

Pssm-ID: 442628 [Multi-domain]  Cd Length: 603  Bit Score: 97.38  E-value: 1.62e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 998470296  196 VIGLKPFTVYSFRVLAVNAIGASKPSKEsFYMVTLREVPEgKPTIVHAQNTSSSSVRIQWTAPARHTIhgefEGYRItYR 275
Cdd:COG3401   196 GGDIEPGTTYYYRVAATDTGGESAPSNE-VSVTTPTTPPS-APTGLTATADTPGSVTLSWDPVTESDA----TGYRV-YR 268
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 998470296  276 prdRTQEESREIILRDSKQTQYTIRNLETFTQYLVSLQVFNPAGR--GPAVVVPVMTDEGVPSSPVNLTAVRVTDTTVRL 353
Cdd:COG3401   269 ---SNSGDGPFTKVATVTTTSYTDTGLTNGTTYYYRVTAVDAAGNesAPSNVVSVTTDLTPPAAPSGLTATAVGSSSITL 345
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 998470296  354 KWREPvrPNGVLQGYHVYfqpsRNGSSQQQRKTVSHPQPVEEYMLSGLKPFSFYDIWVKAFTQQHL-GESSNLLKVQTDV 432
Cdd:COG3401   346 SWTAS--SDADVTGYNVY----RSTSGGGTYTKIAETVTTTSYTDTGLTPGTTYYYKVTAVDAAGNeSAPSEEVSATTAS 419

                  ....*.
gi 998470296  433 QGPSAP 438
Cdd:COG3401   420 AASGES 425
PTP_DSP_cys super family cl28904
cys-based protein tyrosine phosphatase and dual-specificity phosphatase superfamily; This ...
907-1064 7.54e-17

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 cd14604:

Pssm-ID: 475123 [Multi-domain]  Cd Length: 297  Bit Score: 82.67  E-value: 7.54e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 998470296  907 LSRYVQSLQTAQVATTGAGDNEKSWSLLERqfKLVTMFKA-KDFNVVSAVKPCNKAKNRSLNLIPIESHRVHITPKPGID 985
Cdd:cd14604     6 LKKFIERVQAMKSTDHNGEDNFASDFMRLR--RLSTKYRTeKIYPTATGEKEENVKKNRYKDILPFDHSRVKLTLKTSSQ 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 998470296  986 GSDYINATFLQGFNRLREFIVTQHPLMDTMADFWQMVWDHNSQTIVVLSVVDE---KEHPQFWPDTDEEQ-DYGSFKVKP 1061
Cdd:cd14604    84 DSDYINANFIKGVYGPKAYIATQGPLANTVIDFWRMIWEYNVAIIVMACREFEmgrKKCERYWPLYGEEPmTFGPFRISC 163

                  ...
gi 998470296 1062 TGE 1064
Cdd:cd14604   164 EAE 166
FN3 cd00063
Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein ...
133-224 8.15e-17

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: 76.77  E-value: 8.15e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 998470296  133 PDPPGIPIVVGFTSRSVDLSWTSsPNSHHSVILHYIIHIRIGEKGDWDTMNKVMTsdNSTNFQVIGLKPFTVYSFRVLAV 212
Cdd:cd00063     1 PSPPTNLRVTDVTSTSVTLSWTP-PEDDGGPITGYVVEYREKGSGDWKEVEVTPG--SETSYTLTGLKPGTEYEFRVRAV 77
                          90
                  ....*....|..
gi 998470296  213 NAIGASKPSKES 224
Cdd:cd00063    78 NGGGESPPSESV 89
FN3 cd00063
Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein ...
435-511 9.38e-10

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: 56.74  E-value: 9.38e-10
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 998470296  435 PSAPVIVNLTCQSLDSLFLQWERPQTYYNRVDYYFVHYRSEEAWSFEEIAMAANDRLEHVmfIPNLTANTLYEVKVQ 511
Cdd:cd00063     1 PSPPTNLRVTDVTSTSVTLSWTPPEDDGGPITGYVVEYREKGSGDWKEVEVTPGSETSYT--LTGLKPGTEYEFRVR 75
IG_like smart00410
Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.
39-129 1.05e-06

Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.


:

Pssm-ID: 214653 [Multi-domain]  Cd Length: 85  Bit Score: 47.89  E-value: 1.05e-06
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 998470296     39 VRVGGNATLACPdlPPGAGPPrHLLWWKEDRRLIeATRDRVTVAPDagprvsllPGSSALVFRSVLTQDSGEYQCVVNNR 118
Cdd:smart00410    6 VKEGESVTLSCE--ASGSPPP-EVTWYKQGGKLL-AESGRFSVSRS--------GSTSTLTISNVTPEDSGTYTCAATNS 73
                            90
                    ....*....|..
gi 998470296    119 QG-RRGLVRLFV 129
Cdd:smart00410   74 SGsASSGTTLTV 85
 
Name Accession Description Interval E-value
R5-PTPc-1 cd14549
catalytic domain of R5 subfamily receptor-type tyrosine-protein phosphatases, repeat 1; The R5 ...
688-889 1.31e-151

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: 453.35  E-value: 1.31e-151
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 998470296  688 YINANYIDGYHKSRAFIGTQGPLPATFDDYWRMVWEQRVCIIIMITNLVERGRRKCDMYWPKEGTETYGIIQVKLVQEIV 767
Cdd:cd14549     1 YINANYVDGYNKARAYIATQGPLPSTFDDFWRMVWEQNSAIIVMITNLVERGRRKCDQYWPKEGTETYGNIQVTLLSTEV 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 998470296  768 MATYTIRTFAIKNIKVKK--KQASERTVYQYHYTNWPDHGVPDHPLPVLSFVAKSSAANPPAAGPMIVHCSAGVGRTGTY 845
Cdd:cd14549    81 LATYTVRTFSLKNLKLKKvkGRSSERVVYQYHYTQWPDHGVPDYTLPVLSFVRKSSAANPPGAGPIVVHCSAGVGRTGTY 160
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....
gi 998470296  846 IVLDAMLRQMRQRQSVNVYGFLRHIRQQRNYLVQTEEQYVFIHD 889
Cdd:cd14549   161 IVIDSMLQQIQDKGTVNVFGFLKHIRTQRNYLVQTEEQYIFIHD 204
PTPc smart00194
Protein tyrosine phosphatase, catalytic domain;
631-893 1.99e-120

Protein tyrosine phosphatase, catalytic domain;


Pssm-ID: 214550 [Multi-domain]  Cd Length: 259  Bit Score: 373.53  E-value: 1.99e-120
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 998470296    631 GFSREYETFQHCTDPDLTSSYSQLNENKPKNRYINIVAYDHTRVILKPIPGQkkSSDYINANYIDGYHKSRAFIGTQGPL 710
Cdd:smart00194    1 GLEEEFEKLDRLKPDDESCTVAAFPENRDKNRYKDVLPYDHTRVKLKPPPGE--GSDYINASYIDGPNGPKAYIATQGPL 78
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 998470296    711 PATFDDYWRMVWEQRVCIIIMITNLVERGRRKCDMYWPKEG--TETYGIIQVKLVQEIVMATYTIRTFAIKNIKVKKkqa 788
Cdd:smart00194   79 PSTVEDFWRMVWEQKVTVIVMLTELVEKGREKCAQYWPDEEgePLTYGDITVTLKSVEKVDDYTIRTLEVTNTGCSE--- 155
                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 998470296    789 sERTVYQYHYTNWPDHGVPDHPLPVLSFVAKSSAANPPAAGPMIVHCSAGVGRTGTYIVLDAMLRQMRQRQSVNVYGFLR 868
Cdd:smart00194  156 -TRTVTHYHYTNWPDHGVPESPESILDLIRAVRKSQSTSTGPIVVHCSAGVGRTGTFIAIDILLQQLEAGKEVDIFEIVK 234
                           250       260
                    ....*....|....*....|....*
gi 998470296    869 HIRQQRNYLVQTEEQYVFIHDALLE 893
Cdd:smart00194  235 ELRSQRPGMVQTEEQYIFLYRAILE 259
Y_phosphatase pfam00102
Protein-tyrosine phosphatase;
657-893 3.69e-110

Protein-tyrosine phosphatase;


Pssm-ID: 459674 [Multi-domain]  Cd Length: 234  Bit Score: 345.00  E-value: 3.69e-110
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 998470296   657 NKPKNRYINIVAYDHTRVILKPIPGQkksSDYINANYIDGYHKSRAFIGTQGPLPATFDDYWRMVWEQRVCIIIMITNLV 736
Cdd:pfam00102    1 NLEKNRYKDVLPYDHTRVKLTGDPGP---SDYINASYIDGYKKPKKYIATQGPLPNTVEDFWRMVWEEKVTIIVMLTELE 77
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 998470296   737 ERGRRKCDMYWP--KEGTETYGIIQVKLVQE-IVMATYTIRTFAIKNIKVKkkqaSERTVYQYHYTNWPDHGVPDHPLPV 813
Cdd:pfam00102   78 EKGREKCAQYWPeeEGESLEYGDFTVTLKKEkEDEKDYTVRTLEVSNGGSE----ETRTVKHFHYTGWPDHGVPESPNSL 153
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 998470296   814 LSFVAK-SSAANPPAAGPMIVHCSAGVGRTGTYIVLDAMLRQMRQRQSVNVYGFLRHIRQQRNYLVQTEEQYVFIHDALL 892
Cdd:pfam00102  154 LDLLRKvRKSSLDGRSGPIVVHCSAGIGRTGTFIAIDIALQQLEAEGEVDIFQIVKELRSQRPGMVQTLEQYIFLYDAIL 233

                   .
gi 998470296   893 E 893
Cdd:pfam00102  234 E 234
R5-PTP-2 cd14550
PTP-like domain of R5 subfamily receptor-type tyrosine-protein phosphatases, repeat 2; The R5 ...
989-1197 1.82e-90

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: 289.99  E-value: 1.82e-90
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 998470296  989 YINATFLQGFNRLREFIVTQHPLMDTMADFWQMVWDHNSQTIVVLSVVDEKEH-PQFWPDTDEEQDYGSFKVKPTGESVA 1067
Cdd:cd14550     1 YINASYLQGYRRSNEFIITQHPLEHTIKDFWQMIWDHNSQTIVMLTDNELNEDePIYWPTKEKPLECETFKVTLSGEDHS 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 998470296 1068 PPVAEEKgalmpgegggLPSRDFILQSTQDDYELACRLLLCPGWPQSCSPLAKAFELVKEVgARQERDQNGPVVIVDRYG 1147
Cdd:cd14550    81 CLSNEIR----------LIVRDFILESTQDDYVLEVRQFQCPSWPNPCSPIHTVFELINTV-QEWAQQRDGPIVVHDRYG 149
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|
gi 998470296 1148 GTEAATFCCLSALYRQLEREKCVDVYMYAKLYHMRRPGIWKSQDDFLFLY 1197
Cdd:cd14550   150 GVQAATFCALTTLHQQLEHESSVDVYQVAKLYHLMRPGVFTSKEDYQFLY 199
PTPc smart00194
Protein tyrosine phosphatase, catalytic domain;
933-1198 5.18e-55

Protein tyrosine phosphatase, catalytic domain;


Pssm-ID: 214550 [Multi-domain]  Cd Length: 259  Bit Score: 192.49  E-value: 5.18e-55
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 998470296    933 LLERQFKLVTMFKAKDFNVVSAVKPCNKAKNRSLNLIPIESHRVHITPKPGiDGSDYINATFLQGFNRLREFIVTQHPLM 1012
Cdd:smart00194    1 GLEEEFEKLDRLKPDDESCTVAAFPENRDKNRYKDVLPYDHTRVKLKPPPG-EGSDYINASYIDGPNGPKAYIATQGPLP 79
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 998470296   1013 DTMADFWQMVWDHNSQTIVVLSVVDEKEH---PQFWPDT-DEEQDYGSFKVKPTGESVAPpvaeekgalmpgeggGLPSR 1088
Cdd:smart00194   80 STVEDFWRMVWEQKVTVIVMLTELVEKGRekcAQYWPDEeGEPLTYGDITVTLKSVEKVD---------------DYTIR 144
                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 998470296   1089 DFILQSTQDDYELACRLLLCPGWPQSCSPL-AKAF-ELVKEVGARQErDQNGPVVIVDRYGGTEAATFCCLSALYRQLER 1166
Cdd:smart00194  145 TLEVTNTGCSETRTVTHYHYTNWPDHGVPEsPESIlDLIRAVRKSQS-TSTGPIVVHCSAGVGRTGTFIAIDILLQQLEA 223
                           250       260       270
                    ....*....|....*....|....*....|..
gi 998470296   1167 EKCVDVYMYAKLYHMRRPGIWKSQDDFLFLYR 1198
Cdd:smart00194  224 GKEVDIFEIVKELRSQRPGMVQTEEQYIFLYR 255
Y_phosphatase pfam00102
Protein-tyrosine phosphatase;
959-1198 2.97e-54

Protein-tyrosine phosphatase;


Pssm-ID: 459674 [Multi-domain]  Cd Length: 234  Bit Score: 189.38  E-value: 2.97e-54
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 998470296   959 NKAKNRSLNLIPIESHRVHITPKPGidGSDYINATFLQGFNRLREFIVTQHPLMDTMADFWQMVWDHNSQTIVVLSVVDE 1038
Cdd:pfam00102    1 NLEKNRYKDVLPYDHTRVKLTGDPG--PSDYINASYIDGYKKPKKYIATQGPLPNTVEDFWRMVWEEKVTIIVMLTELEE 78
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 998470296  1039 KEH---PQFWPDTDEE-QDYGSFKVKPTGEsvappVAEEKGALMpgeggglpsRDFILQSTQDDYELACRLLLCPGWPQS 1114
Cdd:pfam00102   79 KGRekcAQYWPEEEGEsLEYGDFTVTLKKE-----KEDEKDYTV---------RTLEVSNGGSEETRTVKHFHYTGWPDH 144
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 998470296  1115 CSPLAKA--FELVKEVGARQERDQNGPVVIVDRYGGTEAATFCCLSALYRQLEREKCVDVYMYAKLYHMRRPGIWKSQDD 1192
Cdd:pfam00102  145 GVPESPNslLDLLRKVRKSSLDGRSGPIVVHCSAGIGRTGTFIAIDIALQQLEAEGEVDIFQIVKELRSQRPGMVQTLEQ 224

                   ....*.
gi 998470296  1193 FLFLYR 1198
Cdd:pfam00102  225 YIFLYD 230
PHA02738 PHA02738
hypothetical protein; Provisional
650-902 1.26e-50

hypothetical protein; Provisional


Pssm-ID: 222923 [Multi-domain]  Cd Length: 320  Bit Score: 182.05  E-value: 1.26e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 998470296  650 SYSQLNENKPKNRYINIVAYDHTRVILkpiPGQKKSSDYINANYIDGYHKSRAFIGTQGPLPATFDDYWRMVWEQRVCII 729
Cdd:PHA02738   42 TFNAEKKNRKLNRYLDAVCFDHSRVIL---PAERNRGDYINANYVDGFEYKKKFICGQAPTRQTCYDFYRMLWMEHVQII 118
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 998470296  730 IMITNLVERGRRKCDMYWP--KEGTETYGIIQVKLVQEIVMATYTIRTfaiknIKVKKKQASERTVYQYHYTNWPDHGVP 807
Cdd:PHA02738  119 VMLCKKKENGREKCFPYWSdvEQGSIRFGKFKITTTQVETHPHYVKST-----LLLTDGTSATQTVTHFNFTAWPDHDVP 193
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 998470296  808 DHPLPVLSFV------AKSSAAN----------PPaagPMIVHCSAGVGRTGTYIVLDAMLRQMRQRQSVNVYGFLRHIR 871
Cdd:PHA02738  194 KNTSEFLNFVlevrqcQKELAQEslqighnrlqPP---PIVVHCNAGLGRTPCYCVVDISISRFDACATVSIPSIVSSIR 270
                         250       260       270
                  ....*....|....*....|....*....|.
gi 998470296  872 QQRNYLVQTEEQYVFIHDALLEAIDSGDTEV 902
Cdd:PHA02738  271 NQRYYSLFIPFQYFFCYRAVKRYVNLTVNKV 301
COG5599 COG5599
Protein tyrosine phosphatase [Signal transduction mechanisms];
651-887 4.23e-43

Protein tyrosine phosphatase [Signal transduction mechanisms];


Pssm-ID: 444335 [Multi-domain]  Cd Length: 282  Bit Score: 158.72  E-value: 4.23e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 998470296  651 YSQLNENKPKNRYINIVAYDHTRVilkpipgqKKSSDYINANYIDGYHKSRAfIGTQGPLPATFDDYWRMVWEQRVCIII 730
Cdd:COG5599    36 YLQNINGSPLNRFRDIQPYKETAL--------RANLGYLNANYIQVIGNHRY-IATQYPLEEQLEDFFQMLFDNNTPVLV 106
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 998470296  731 MITNLVERGRRKCDM--YWPKEGTETYGIIQVKLVQEIVMATytirTFAIKNIKVKKKQASE--RTVYQYHYTNWPDHGV 806
Cdd:COG5599   107 VLASDDEISKPKVKMpvYFRQDGEYGKYEVSSELTESIQLRD----GIEARTYVLTIKGTGQkkIEIPVLHVKNWPDHGA 182
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 998470296  807 PD----HPLpvLSFVAKSSAANPPAAGPMIVHCSAGVGRTGTYIVLDAMlRQMRQRQ---SVNVYGFLRHIRQQRNY-LV 878
Cdd:COG5599   183 ISaealKNL--ADLIDKKEKIKDPDKLLPVVHCRAGVGRTGTLIACLAL-SKSINALvqiTLSVEEIVIDMRTSRNGgMV 259

                  ....*....
gi 998470296  879 QTEEQYVFI 887
Cdd:COG5599   260 QTSEQLDVL 268
FN3 COG3401
Fibronectin type 3 domain [General function prediction only];
196-438 1.62e-20

Fibronectin type 3 domain [General function prediction only];


Pssm-ID: 442628 [Multi-domain]  Cd Length: 603  Bit Score: 97.38  E-value: 1.62e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 998470296  196 VIGLKPFTVYSFRVLAVNAIGASKPSKEsFYMVTLREVPEgKPTIVHAQNTSSSSVRIQWTAPARHTIhgefEGYRItYR 275
Cdd:COG3401   196 GGDIEPGTTYYYRVAATDTGGESAPSNE-VSVTTPTTPPS-APTGLTATADTPGSVTLSWDPVTESDA----TGYRV-YR 268
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 998470296  276 prdRTQEESREIILRDSKQTQYTIRNLETFTQYLVSLQVFNPAGR--GPAVVVPVMTDEGVPSSPVNLTAVRVTDTTVRL 353
Cdd:COG3401   269 ---SNSGDGPFTKVATVTTTSYTDTGLTNGTTYYYRVTAVDAAGNesAPSNVVSVTTDLTPPAAPSGLTATAVGSSSITL 345
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 998470296  354 KWREPvrPNGVLQGYHVYfqpsRNGSSQQQRKTVSHPQPVEEYMLSGLKPFSFYDIWVKAFTQQHL-GESSNLLKVQTDV 432
Cdd:COG3401   346 SWTAS--SDADVTGYNVY----RSTSGGGTYTKIAETVTTTSYTDTGLTPGTTYYYKVTAVDAAGNeSAPSEEVSATTAS 419

                  ....*.
gi 998470296  433 QGPSAP 438
Cdd:COG3401   420 AASGES 425
PTPc-N12 cd14604
catalytic domain of tyrosine-protein phosphatase non-receptor type 12; Tyrosine-protein ...
907-1064 7.54e-17

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: 82.67  E-value: 7.54e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 998470296  907 LSRYVQSLQTAQVATTGAGDNEKSWSLLERqfKLVTMFKA-KDFNVVSAVKPCNKAKNRSLNLIPIESHRVHITPKPGID 985
Cdd:cd14604     6 LKKFIERVQAMKSTDHNGEDNFASDFMRLR--RLSTKYRTeKIYPTATGEKEENVKKNRYKDILPFDHSRVKLTLKTSSQ 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 998470296  986 GSDYINATFLQGFNRLREFIVTQHPLMDTMADFWQMVWDHNSQTIVVLSVVDE---KEHPQFWPDTDEEQ-DYGSFKVKP 1061
Cdd:cd14604    84 DSDYINANFIKGVYGPKAYIATQGPLANTVIDFWRMIWEYNVAIIVMACREFEmgrKKCERYWPLYGEEPmTFGPFRISC 163

                  ...
gi 998470296 1062 TGE 1064
Cdd:cd14604   164 EAE 166
PHA02746 PHA02746
protein tyrosine phosphatase; Provisional
955-1172 7.92e-17

protein tyrosine phosphatase; Provisional


Pssm-ID: 165113 [Multi-domain]  Cd Length: 323  Bit Score: 83.15  E-value: 7.92e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 998470296  955 VKPCNKAKNRSLNLIPIESHRVHITPKPGI--------DG-----------SDYINATFLQGFNRLREFIVTQHPLMDTM 1015
Cdd:PHA02746   47 LKKENLKKNRFHDIPCWDHSRVVINAHESLkmfdvgdsDGkkievtsednaENYIHANFVDGFKEANKFICAQGPKEDTS 126
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 998470296 1016 ADFWQMVWDHNSQTIVVLSVVDEKEHPQF--W-PDTDEEQDYGSFKVKPTgesvapPVAEEKgalmpgeggGLPSRDFIL 1092
Cdd:PHA02746  127 EDFFKLISEHESQVIVSLTDIDDDDEKCFelWtKEEDSELAFGRFVAKIL------DIIEEL---------SFTKTRLMI 191
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 998470296 1093 QSTQDDYELACRLLLCPGWPQSCSP--LAKAFELVKEVGARQER---------DQNGPVVIVDRYGGTEAATFCCLSALY 1161
Cdd:PHA02746  192 TDKISDTSREIHHFWFPDWPDNGIPtgMAEFLELINKVNEEQAElikqadndpQTLGPIVVHCSAGIGRAGTFCAIDNAL 271
                         250
                  ....*....|.
gi 998470296 1162 RQLEREKCVDV 1172
Cdd:PHA02746  272 EQLEKEKEVCL 282
FN3 cd00063
Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein ...
133-224 8.15e-17

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: 76.77  E-value: 8.15e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 998470296  133 PDPPGIPIVVGFTSRSVDLSWTSsPNSHHSVILHYIIHIRIGEKGDWDTMNKVMTsdNSTNFQVIGLKPFTVYSFRVLAV 212
Cdd:cd00063     1 PSPPTNLRVTDVTSTSVTLSWTP-PEDDGGPITGYVVEYREKGSGDWKEVEVTPG--SETSYTLTGLKPGTEYEFRVRAV 77
                          90
                  ....*....|..
gi 998470296  213 NAIGASKPSKES 224
Cdd:cd00063    78 NGGGESPPSESV 89
FN3 cd00063
Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein ...
335-430 1.36e-15

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: 73.30  E-value: 1.36e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 998470296  335 PSSPVNLTAVRVTDTTVRLKWREPVRPNGVLQGYHVYFQPSRNGSSQQQRKTVShpqPVEEYMLSGLKPFSFYDIWVKAF 414
Cdd:cd00063     1 PSPPTNLRVTDVTSTSVTLSWTPPEDDGGPITGYVVEYREKGSGDWKEVEVTPG---SETSYTLTGLKPGTEYEFRVRAV 77
                          90
                  ....*....|....*.
gi 998470296  415 TQQHLGESSNLLKVQT 430
Cdd:cd00063    78 NGGGESPPSESVTVTT 93
fn3 pfam00041
Fibronectin type III domain;
236-322 1.21e-14

Fibronectin type III domain;


Pssm-ID: 394996 [Multi-domain]  Cd Length: 85  Bit Score: 70.14  E-value: 1.21e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 998470296   236 GKPTIVHAQNTSSSSVRIQWTAParHTIHGEFEGYRITYRPRDRTQEESREIILRDskQTQYTIRNLETFTQYLVSLQVF 315
Cdd:pfam00041    1 SAPSNLTVTDVTSTSLTVSWTPP--PDGNGPITGYEVEYRPKNSGEPWNEITVPGT--TTSVTLTGLKPGTEYEVRVQAV 76

                   ....*..
gi 998470296   316 NPAGRGP 322
Cdd:pfam00041   77 NGGGEGP 83
FN3 smart00060
Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, ...
133-218 1.34e-14

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: 70.34  E-value: 1.34e-14
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 998470296    133 PDPPGIPIVVGFTSRSVDLSWTSSPNSHHSvilHYIIHIRIGEKGDWDTMNKVMTSDNSTNFQVIGLKPFTVYSFRVLAV 212
Cdd:smart00060    1 PSPPSNLRVTDVTSTSVTLSWEPPPDDGIT---GYIVGYRVEYREEGSEWKEVNVTPSSTSYTLTGLKPGTEYEFRVRAV 77

                    ....*.
gi 998470296    213 NAIGAS 218
Cdd:smart00060   78 NGAGEG 83
FN3 smart00060
Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, ...
236-321 5.03e-14

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: 68.41  E-value: 5.03e-14
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 998470296    236 GKPTIVHAQNTSSSSVRIQWTAPArhtiHGEFEGYRITYRPRDRTQEESREIILRDSKQTQYTIRNLETFTQYLVSLQVF 315
Cdd:smart00060    2 SPPSNLRVTDVTSTSVTLSWEPPP----DDGITGYIVGYRVEYREEGSEWKEVNVTPSSTSYTLTGLKPGTEYEFRVRAV 77

                    ....*.
gi 998470296    316 NPAGRG 321
Cdd:smart00060   78 NGAGEG 83
fn3 pfam00041
Fibronectin type III domain;
134-221 7.62e-12

Fibronectin type III domain;


Pssm-ID: 394996 [Multi-domain]  Cd Length: 85  Bit Score: 62.43  E-value: 7.62e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 998470296   134 DPPGIPIVVGFTSRSVDLSWTSsPNSHHSVILHYIIHIRigEKGDWDTMNKVMTSDNSTNFQVIGLKPFTVYSFRVLAVN 213
Cdd:pfam00041    1 SAPSNLTVTDVTSTSLTVSWTP-PPDGNGPITGYEVEYR--PKNSGEPWNEITVPGTTTSVTLTGLKPGTEYEVRVQAVN 77

                   ....*...
gi 998470296   214 AIGASKPS 221
Cdd:pfam00041   78 GGGEGPPS 85
FN3 cd00063
Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein ...
435-511 9.38e-10

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: 56.74  E-value: 9.38e-10
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 998470296  435 PSAPVIVNLTCQSLDSLFLQWERPQTYYNRVDYYFVHYRSEEAWSFEEIAMAANDRLEHVmfIPNLTANTLYEVKVQ 511
Cdd:cd00063     1 PSPPTNLRVTDVTSTSVTLSWTPPEDDGGPITGYVVEYREKGSGDWKEVEVTPGSETSYT--LTGLKPGTEYEFRVR 75
FN3 smart00060
Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, ...
435-511 1.05e-06

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


Pssm-ID: 214495 [Multi-domain]  Cd Length: 83  Bit Score: 47.61  E-value: 1.05e-06
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 998470296    435 PSAPVIVNLTCQSLDSLFLQWERPQtyYNRVDYYFVHYRSEEAWSFEEIAMAANDRLEHVMFIPNLTANTLYEVKVQ 511
Cdd:smart00060    1 PSPPSNLRVTDVTSTSVTLSWEPPP--DDGITGYIVGYRVEYREEGSEWKEVNVTPSSTSYTLTGLKPGTEYEFRVR 75
IG_like smart00410
Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.
39-129 1.05e-06

Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.


Pssm-ID: 214653 [Multi-domain]  Cd Length: 85  Bit Score: 47.89  E-value: 1.05e-06
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 998470296     39 VRVGGNATLACPdlPPGAGPPrHLLWWKEDRRLIeATRDRVTVAPDagprvsllPGSSALVFRSVLTQDSGEYQCVVNNR 118
Cdd:smart00410    6 VKEGESVTLSCE--ASGSPPP-EVTWYKQGGKLL-AESGRFSVSRS--------GSTSTLTISNVTPEDSGTYTCAATNS 73
                            90
                    ....*....|..
gi 998470296    119 QG-RRGLVRLFV 129
Cdd:smart00410   74 SGsASSGTTLTV 85
ig pfam00047
Immunoglobulin domain; Members of the immunoglobulin superfamily are found in hundreds of ...
37-118 6.22e-06

Immunoglobulin domain; Members of the immunoglobulin superfamily are found in hundreds of proteins of different functions. Examples include antibodies, the giant muscle kinase titin and receptor tyrosine kinases. Immunoglobulin-like domains may be involved in protein-protein and protein-ligand interactions.


Pssm-ID: 395002  Cd Length: 86  Bit Score: 45.65  E-value: 6.22e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 998470296    37 LFVRVGGNATLACpdLPPGAGPPRHLLWWKEDRRLIEATRDRVTVAPDagprvsllpGSSALVFRSVLTQDSGEYQCVVN 116
Cdd:pfam00047    6 VTVLEGDSATLTC--SASTGSPGPDVTWSKEGGTLIESLKVKHDNGRT---------TQSSLLISNVTKEDAGTYTCVVN 74

                   ..
gi 998470296   117 NR 118
Cdd:pfam00047   75 NP 76
fn3 pfam00041
Fibronectin type III domain;
436-515 1.74e-05

Fibronectin type III domain;


Pssm-ID: 394996 [Multi-domain]  Cd Length: 85  Bit Score: 44.33  E-value: 1.74e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 998470296   436 SAPVIVNLTCQSLDSLFLQWERPQTYYNRVDYYFVHYRseEAWSFEEIAMAANDRLEHVMFIPNLTANTLYEVKVQGATR 515
Cdd:pfam00041    1 SAPSNLTVTDVTSTSLTVSWTPPPDGNGPITGYEVEYR--PKNSGEPWNEITVPGTTTSVTLTGLKPGTEYEVRVQAVNG 78
Ig cd00096
Immunoglobulin domain; The members here are composed of the immunoglobulin (Ig) domain found ...
45-122 1.14e-04

Immunoglobulin domain; The members here are composed of the immunoglobulin (Ig) domain found in the Ig superfamily. The Ig superfamily is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. Members of this group are components of immunoglobulin, neuroglia, cell surface glycoproteins, including T-cell receptors, CD2, CD4, CD8, and membrane glycoproteins, including butyrophilin and chondroitin sulfate proteoglycan core protein. A predominant feature of most Ig domains is a disulfide bridge connecting the two beta-sheets with a tryptophan residue packed against the disulfide bond. Ig superfamily (IgSF) domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. Typically, the V-set domains have A, B, E, and D strands in one sheet and A', G, F, C, C' and C" in the other. The structures in C1-set are smaller than those in the V-set; they have one beta sheet that is formed by strands A, B, E, and D and the other by strands G, F, C, and C'. Moreover, a C1-set Ig domain contains a short C' strand (three residues) and lacks A' and C" strand. Unlike other Ig domain sets, C2-set structures do not have a D strand. Like the V-set Ig domains, members of the I-set have a discontinuous A strand, but lack a C" strand.


Pssm-ID: 409353 [Multi-domain]  Cd Length: 70  Bit Score: 41.55  E-value: 1.14e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 998470296   45 ATLACPdlpPGAGPPRHLLWWKEDRRLIEATRDRVtvapdagprvSLLPGSSALVFRSVLTQDSGEYQCVVNNRQGRR 122
Cdd:cd00096     1 VTLTCS---ASGNPPPTITWYKNGKPLPPSSRDSR----------RSELGNGTLTISNVTLEDSGTYTCVASNSAGGS 65
COG3979 COG3979
Chitodextrinase [Carbohydrate transport and metabolism];
133-216 2.90e-04

Chitodextrinase [Carbohydrate transport and metabolism];


Pssm-ID: 443178 [Multi-domain]  Cd Length: 369  Bit Score: 44.76  E-value: 2.90e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 998470296  133 PDPPGIPIVVGFTSRSVDLSWTSSPNShhSVILHYIIHirigEKGDwdtmnKVMTSDNSTNFQVIGLKPFTVYSFRVLAV 212
Cdd:COG3979     3 PTAPTGLTASNVTSSSVSLSWDASTDN--VGVTGYDVY----RGGD-----QVATVTGLTAWTVTGLTPGTEYTFTVGAC 71

                  ....
gi 998470296  213 NAIG 216
Cdd:COG3979    72 DAAG 75
 
Name Accession Description Interval E-value
R5-PTPc-1 cd14549
catalytic domain of R5 subfamily receptor-type tyrosine-protein phosphatases, repeat 1; The R5 ...
688-889 1.31e-151

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: 453.35  E-value: 1.31e-151
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 998470296  688 YINANYIDGYHKSRAFIGTQGPLPATFDDYWRMVWEQRVCIIIMITNLVERGRRKCDMYWPKEGTETYGIIQVKLVQEIV 767
Cdd:cd14549     1 YINANYVDGYNKARAYIATQGPLPSTFDDFWRMVWEQNSAIIVMITNLVERGRRKCDQYWPKEGTETYGNIQVTLLSTEV 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 998470296  768 MATYTIRTFAIKNIKVKK--KQASERTVYQYHYTNWPDHGVPDHPLPVLSFVAKSSAANPPAAGPMIVHCSAGVGRTGTY 845
Cdd:cd14549    81 LATYTVRTFSLKNLKLKKvkGRSSERVVYQYHYTQWPDHGVPDYTLPVLSFVRKSSAANPPGAGPIVVHCSAGVGRTGTY 160
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....
gi 998470296  846 IVLDAMLRQMRQRQSVNVYGFLRHIRQQRNYLVQTEEQYVFIHD 889
Cdd:cd14549   161 IVIDSMLQQIQDKGTVNVFGFLKHIRTQRNYLVQTEEQYIFIHD 204
R-PTPc-G-1 cd17667
catalytic domain of receptor-type tyrosine-protein phosphatase G, repeat 1; Receptor-type ...
632-895 2.41e-135

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: 413.66  E-value: 2.41e-135
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 998470296  632 FSREYETFQHCT-DPDLTSSYSQLNENKPKNRYINIVAYDHTRVILKPIPGQ-KKSSDYINANYIDGYHKSRAFIGTQGP 709
Cdd:cd17667     1 FSEDFEEVQRCTaDMNITAEHSNHPDNKHKNRYINILAYDHSRVKLRPLPGKdSKHSDYINANYVDGYNKAKAYIATQGP 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 998470296  710 LPATFDDYWRMVWEQRVCIIIMITNLVERGRRKCDMYWPKEGTETYGIIQVKLVQEIVMATYTIRTFAIKNIKVKKKQA- 788
Cdd:cd17667    81 LKSTFEDFWRMIWEQNTGIIVMITNLVEKGRRKCDQYWPTENSEEYGNIIVTLKSTKIHACYTVRRFSIRNTKVKKGQKg 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 998470296  789 ------SERTVYQYHYTNWPDHGVPDHPLPVLSFVAKSSAANPPAAGPMIVHCSAGVGRTGTYIVLDAMLRQMRQRQSVN 862
Cdd:cd17667   161 npkgrqNERTVIQYHYTQWPDMGVPEYALPVLTFVRRSSAARTPEMGPVLVHCSAGVGRTGTYIVIDSMLQQIKDKSTVN 240
                         250       260       270
                  ....*....|....*....|....*....|...
gi 998470296  863 VYGFLRHIRQQRNYLVQTEEQYVFIHDALLEAI 895
Cdd:cd17667   241 VLGFLKHIRTQRNYLVQTEEQYIFIHDALLEAI 273
R-PTPc-LAR-1 cd14553
catalytic domain of LAR family receptor-type tyrosine-protein phosphatases, repeat 1; The LAR ...
657-897 2.00e-129

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: 396.38  E-value: 2.00e-129
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 998470296  657 NKPKNRYINIVAYDHTRVILKPIPGQKkSSDYINANYIDGYHKSRAFIGTQGPLPATFDDYWRMVWEQRVCIIIMITNLV 736
Cdd:cd14553     3 NKPKNRYANVIAYDHSRVILQPIEGVP-GSDYINANYCDGYRKQNAYIATQGPLPETFGDFWRMVWEQRSATIVMMTKLE 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 998470296  737 ERGRRKCDMYWPKEGTETYGIIQVKLVQEIVMATYTIRTFAIKNIKVKKKqaseRTVYQYHYTNWPDHGVPDHPLPVLSF 816
Cdd:cd14553    82 ERSRVKCDQYWPTRGTETYGLIQVTLLDTVELATYTVRTFALHKNGSSEK----REVRQFQFTAWPDHGVPEHPTPFLAF 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 998470296  817 VAKSSAANPPAAGPMIVHCSAGVGRTGTYIVLDAMLRQMRQRQSVNVYGFLRHIRQQRNYLVQTEEQYVFIHDALLEAID 896
Cdd:cd14553   158 LRRVKACNPPDAGPIVVHCSAGVGRTGCFIVIDSMLERIKHEKTVDIYGHVTCLRAQRNYMVQTEDQYIFIHDALLEAVT 237

                  .
gi 998470296  897 S 897
Cdd:cd14553   238 C 238
PTPc smart00194
Protein tyrosine phosphatase, catalytic domain;
631-893 1.99e-120

Protein tyrosine phosphatase, catalytic domain;


Pssm-ID: 214550 [Multi-domain]  Cd Length: 259  Bit Score: 373.53  E-value: 1.99e-120
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 998470296    631 GFSREYETFQHCTDPDLTSSYSQLNENKPKNRYINIVAYDHTRVILKPIPGQkkSSDYINANYIDGYHKSRAFIGTQGPL 710
Cdd:smart00194    1 GLEEEFEKLDRLKPDDESCTVAAFPENRDKNRYKDVLPYDHTRVKLKPPPGE--GSDYINASYIDGPNGPKAYIATQGPL 78
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 998470296    711 PATFDDYWRMVWEQRVCIIIMITNLVERGRRKCDMYWPKEG--TETYGIIQVKLVQEIVMATYTIRTFAIKNIKVKKkqa 788
Cdd:smart00194   79 PSTVEDFWRMVWEQKVTVIVMLTELVEKGREKCAQYWPDEEgePLTYGDITVTLKSVEKVDDYTIRTLEVTNTGCSE--- 155
                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 998470296    789 sERTVYQYHYTNWPDHGVPDHPLPVLSFVAKSSAANPPAAGPMIVHCSAGVGRTGTYIVLDAMLRQMRQRQSVNVYGFLR 868
Cdd:smart00194  156 -TRTVTHYHYTNWPDHGVPESPESILDLIRAVRKSQSTSTGPIVVHCSAGVGRTGTFIAIDILLQQLEAGKEVDIFEIVK 234
                           250       260
                    ....*....|....*....|....*
gi 998470296    869 HIRQQRNYLVQTEEQYVFIHDALLE 893
Cdd:smart00194  235 ELRSQRPGMVQTEEQYIFLYRAILE 259
R-PTPc-F-1 cd14626
catalytic domain of receptor-type tyrosine-protein phosphatase F, repeat 1; Receptor-type ...
615-895 1.51e-114

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: 358.58  E-value: 1.51e-114
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 998470296  615 SQWAKHVADLHADGDIGFSREYETFqhctDP--DLTSSYSQLNENKPKNRYINIVAYDHTRVILKPIPGQKkSSDYINAN 692
Cdd:cd14626     1 SDLADNIERLKANDGLKFSQEYESI----DPgqQFTWENSNLEVNKPKNRYANVIAYDHSRVILTSVDGVP-GSDYINAN 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 998470296  693 YIDGYHKSRAFIGTQGPLPATFDDYWRMVWEQRVCIIIMITNLVERGRRKCDMYWPKEGTETYGIIQVKLVQEIVMATYT 772
Cdd:cd14626    76 YIDGYRKQNAYIATQGPLPETLSDFWRMVWEQRTATIVMMTRLEEKSRVKCDQYWPIRGTETYGMIQVTLLDTVELATYS 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 998470296  773 IRTFAIKnikvKKKQASERTVYQYHYTNWPDHGVPDHPLPVLSFVAKSSAANPPAAGPMIVHCSAGVGRTGTYIVLDAML 852
Cdd:cd14626   156 VRTFALY----KNGSSEKREVRQFQFMAWPDHGVPEYPTPILAFLRRVKACNPPDAGPMVVHCSAGVGRTGCFIVIDAML 231
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|...
gi 998470296  853 RQMRQRQSVNVYGFLRHIRQQRNYLVQTEEQYVFIHDALLEAI 895
Cdd:cd14626   232 ERMKHEKTVDIYGHVTCMRSQRNYMVQTEDQYIFIHEALLEAA 274
Y_phosphatase pfam00102
Protein-tyrosine phosphatase;
657-893 3.69e-110

Protein-tyrosine phosphatase;


Pssm-ID: 459674 [Multi-domain]  Cd Length: 234  Bit Score: 345.00  E-value: 3.69e-110
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 998470296   657 NKPKNRYINIVAYDHTRVILKPIPGQkksSDYINANYIDGYHKSRAFIGTQGPLPATFDDYWRMVWEQRVCIIIMITNLV 736
Cdd:pfam00102    1 NLEKNRYKDVLPYDHTRVKLTGDPGP---SDYINASYIDGYKKPKKYIATQGPLPNTVEDFWRMVWEEKVTIIVMLTELE 77
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 998470296   737 ERGRRKCDMYWP--KEGTETYGIIQVKLVQE-IVMATYTIRTFAIKNIKVKkkqaSERTVYQYHYTNWPDHGVPDHPLPV 813
Cdd:pfam00102   78 EKGREKCAQYWPeeEGESLEYGDFTVTLKKEkEDEKDYTVRTLEVSNGGSE----ETRTVKHFHYTGWPDHGVPESPNSL 153
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 998470296   814 LSFVAK-SSAANPPAAGPMIVHCSAGVGRTGTYIVLDAMLRQMRQRQSVNVYGFLRHIRQQRNYLVQTEEQYVFIHDALL 892
Cdd:pfam00102  154 LDLLRKvRKSSLDGRSGPIVVHCSAGIGRTGTFIAIDIALQQLEAEGEVDIFQIVKELRSQRPGMVQTLEQYIFLYDAIL 233

                   .
gi 998470296   893 E 893
Cdd:pfam00102  234 E 234
R-PTPc-D-1 cd14624
catalytic domain of receptor-type tyrosine-protein phosphatase D, repeat 1; Receptor-type ...
609-899 3.27e-108

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: 341.71  E-value: 3.27e-108
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 998470296  609 YASVHVSQWAKHVADLHADGDIGFSREYETFqhctDP--DLTSSYSQLNENKPKNRYINIVAYDHTRVILKPIPGqKKSS 686
Cdd:cd14624     1 HPPIPILELADHIERLKANDNLKFSQEYESI----DPgqQFTWEHSNLEVNKPKNRYANVIAYDHSRVLLSAIEG-IPGS 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 998470296  687 DYINANYIDGYHKSRAFIGTQGPLPATFDDYWRMVWEQRVCIIIMITNLVERGRRKCDMYWPKEGTETYGIIQVKLVQEI 766
Cdd:cd14624    76 DYINANYIDGYRKQNAYIATQGALPETFGDFWRMIWEQRSATVVMMTKLEERSRVKCDQYWPSRGTETYGLIQVTLLDTV 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 998470296  767 VMATYTIRTFAIknikVKKKQASERTVYQYHYTNWPDHGVPDHPLPVLSFVAKSSAANPPAAGPMIVHCSAGVGRTGTYI 846
Cdd:cd14624   156 ELATYCVRTFAL----YKNGSSEKREVRQFQFTAWPDHGVPEHPTPFLAFLRRVKTCNPPDAGPMVVHCSAGVGRTGCFI 231
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|...
gi 998470296  847 VLDAMLRQMRQRQSVNVYGFLRHIRQQRNYLVQTEEQYVFIHDALLEAIDSGD 899
Cdd:cd14624   232 VIDAMLERIKHEKTVDIYGHVTLMRAQRNYMVQTEDQYIFIHDALLEAVTCGN 284
R-PTPc-S-1 cd14625
catalytic domain of receptor-type tyrosine-protein phosphatase S, repeat 1; Receptor-type ...
612-895 2.30e-107

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: 339.38  E-value: 2.30e-107
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 998470296  612 VHVSQWAKHVADLHADGDIGFSREYETFqhctDP--DLTSSYSQLNENKPKNRYINIVAYDHTRVILKPIPGqKKSSDYI 689
Cdd:cd14625     4 IPISELAEHTERLKANDNLKLSQEYESI----DPgqQFTWEHSNLEVNKPKNRYANVIAYDHSRVILQPIEG-IMGSDYI 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 998470296  690 NANYIDGYHKSRAFIGTQGPLPATFDDYWRMVWEQRVCIIIMITNLVERGRRKCDMYWPKEGTETYGIIQVKLVQEIVMA 769
Cdd:cd14625    79 NANYIDGYRKQNAYIATQGPLPETFGDFWRMVWEQRSATVVMMTKLEEKSRIKCDQYWPSRGTETYGMIQVTLLDTIELA 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 998470296  770 TYTIRTFAIKnikvKKKQASERTVYQYHYTNWPDHGVPDHPLPVLSFVAKSSAANPPAAGPMIVHCSAGVGRTGTYIVLD 849
Cdd:cd14625   159 TFCVRTFSLH----KNGSSEKREVRQFQFTAWPDHGVPEYPTPFLAFLRRVKTCNPPDAGPIVVHCSAGVGRTGCFIVID 234
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*.
gi 998470296  850 AMLRQMRQRQSVNVYGFLRHIRQQRNYLVQTEEQYVFIHDALLEAI 895
Cdd:cd14625   235 AMLERIKHEKTVDIYGHVTLMRSQRNYMVQTEDQYSFIHDALLEAV 280
R-PTPc-Z-1 cd17668
catalytic domain of receptor-type tyrosine-protein phosphatase Z, repeat 1; Receptor-type ...
688-892 7.75e-103

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: 324.24  E-value: 7.75e-103
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 998470296  688 YINANYIDGYHKSRAFIGTQGPLPATFDDYWRMVWEQRVCIIIMITNLVERGRRKCDMYWPKEGTETYGIIQVKLVQEIV 767
Cdd:cd17668     1 YINANYVDGYNKPKAYIAAQGPLKSTAEDFWRMIWEHNVEVIVMITNLVEKGRRKCDQYWPADGSEEYGNFLVTQKSVQV 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 998470296  768 MATYTIRTFAIKNIKVKKK----QASERTVYQYHYTNWPDHGVPDHPLPVLSFVAKSSAANPPAAGPMIVHCSAGVGRTG 843
Cdd:cd17668    81 LAYYTVRNFTLRNTKIKKGsqkgRPSGRVVTQYHYTQWPDMGVPEYTLPVLTFVRKASYAKRHAVGPVVVHCSAGVGRTG 160
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*....
gi 998470296  844 TYIVLDAMLRQMRQRQSVNVYGFLRHIRQQRNYLVQTEEQYVFIHDALL 892
Cdd:cd17668   161 TYIVLDSMLQQIQHEGTVNIFGFLKHIRSQRNYLVQTEEQYVFIHDALV 209
PTPc cd00047
catalytic domain of protein tyrosine phosphatases; Protein tyrosine phosphatases (PTP, EC 3.1. ...
688-889 5.51e-93

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: 296.89  E-value: 5.51e-93
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 998470296  688 YINANYIDGYHKSRAFIGTQGPLPATFDDYWRMVWEQRVCIIIMITNLVERGRRKCDMYWPKEG--TETYGIIQVKLVQE 765
Cdd:cd00047     1 YINASYIDGYRGPKEYIATQGPLPNTVEDFWRMVWEQKVSVIVMLTNLVEKGREKCERYWPEEGgkPLEYGDITVTLVSE 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 998470296  766 IVMATYTIRTFAIKNIKVKKkqasERTVYQYHYTNWPDHGVPDHPLPVLSFVAKSSAANPPAAGPMIVHCSAGVGRTGTY 845
Cdd:cd00047    81 EELSDYTIRTLELSPKGCSE----SREVTHLHYTGWPDHGVPSSPEDLLALVRRVRKEARKPNGPIVVHCSAGVGRTGTF 156
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....
gi 998470296  846 IVLDAMLRQMRQRQSVNVYGFLRHIRQQRNYLVQTEEQYVFIHD 889
Cdd:cd00047   157 IAIDILLERLEAEGEVDVFEIVKALRKQRPGMVQTLEQYEFIYE 200
R3-PTPc cd14548
catalytic domain of R3 subfamily receptor-type tyrosine-protein phosphatases and similar ...
662-888 1.88e-92

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: 296.57  E-value: 1.88e-92
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 998470296  662 RYINIVAYDHTRVILKPIPGQKkSSDYINANYIDGYHKSRAFIGTQGPLPATFDDYWRMVWEQRVCIIIMITNLVERGRR 741
Cdd:cd14548     1 RYTNILPYDHSRVKLIPINEEE-GSDYINANYIPGYNSPREFIATQGPLPGTKDDFWRMVWEQNSHTIVMLTQCMEKGRV 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 998470296  742 KCDMYWPKEGTET-YGIIQVKLVQEIVMATYTIRTFAIKNIkvkkkqASERTVYQYHYTNWPDHGVPDHPLPVLSFVAKS 820
Cdd:cd14548    80 KCDHYWPFDQDPVyYGDITVTMLSESVLPDWTIREFKLERG------DEVRSVRQFHFTAWPDHGVPEAPDSLLRFVRLV 153
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 998470296  821 SAANPPAAGPMIVHCSAGVGRTGTYIVLDAMLRQMRQRQSVNVYGFLRHIRQQRNYLVQTEEQYVFIH 888
Cdd:cd14548   154 RDYIKQEKGPTIVHCSAGVGRTGTFIALDRLLQQIESEDYVDIFGIVYDLRKHRPLMVQTEAQYIFLH 221
R5-PTP-2 cd14550
PTP-like domain of R5 subfamily receptor-type tyrosine-protein phosphatases, repeat 2; The R5 ...
989-1197 1.82e-90

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: 289.99  E-value: 1.82e-90
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 998470296  989 YINATFLQGFNRLREFIVTQHPLMDTMADFWQMVWDHNSQTIVVLSVVDEKEH-PQFWPDTDEEQDYGSFKVKPTGESVA 1067
Cdd:cd14550     1 YINASYLQGYRRSNEFIITQHPLEHTIKDFWQMIWDHNSQTIVMLTDNELNEDePIYWPTKEKPLECETFKVTLSGEDHS 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 998470296 1068 PPVAEEKgalmpgegggLPSRDFILQSTQDDYELACRLLLCPGWPQSCSPLAKAFELVKEVgARQERDQNGPVVIVDRYG 1147
Cdd:cd14550    81 CLSNEIR----------LIVRDFILESTQDDYVLEVRQFQCPSWPNPCSPIHTVFELINTV-QEWAQQRDGPIVVHDRYG 149
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|
gi 998470296 1148 GTEAATFCCLSALYRQLEREKCVDVYMYAKLYHMRRPGIWKSQDDFLFLY 1197
Cdd:cd14550   150 GVQAATFCALTTLHQQLEHESSVDVYQVAKLYHLMRPGVFTSKEDYQFLY 199
R-PTPc-M-1 cd14633
catalytic domain of receptor-type tyrosine-protein phosphatase M, repeat 1; Receptor-type ...
619-894 5.52e-85

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: 278.08  E-value: 5.52e-85
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 998470296  619 KHVADLHADGDIGFSREYETFQHCTDPDLTSSysQLNENKPKNRYINIVAYDHTRVILKPIPGQKkSSDYINANYIDGYH 698
Cdd:cd14633     4 QHITQMKCAEGYGFKEEYESFFEGQSAPWDSA--KKDENRMKNRYGNIIAYDHSRVRLQPIEGET-SSDYINGNYIDGYH 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 998470296  699 KSRAFIGTQGPLPATFDDYWRMVWEQRVCIIIMITNLVERGRRKCDMYWPKEgTETYGIIQVKLVQEIVMATYTIRTFAi 778
Cdd:cd14633    81 RPNHYIATQGPMQETIYDFWRMVWHENTASIIMVTNLVEVGRVKCCKYWPDD-TEIYKDIKVTLIETELLAEYVIRTFA- 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 998470296  779 knikVKKKQASE-RTVYQYHYTNWPDHGVPDHPLPVLSFVAKSSAANPPAAGPMIVHCSAGVGRTGTYIVLDAMLRQMRQ 857
Cdd:cd14633   159 ----VEKRGVHEiREIRQFHFTGWPDHGVPYHATGLLGFVRQVKSKSPPNAGPLVVHCSAGAGRTGCFIVIDIMLDMAER 234
                         250       260       270
                  ....*....|....*....|....*....|....*..
gi 998470296  858 RQSVNVYGFLRHIRQQRNYLVQTEEQYVFIHDALLEA 894
Cdd:cd14633   235 EGVVDIYNCVRELRSRRVNMVQTEEQYVFIHDAILEA 271
R-PTPc-A-1 cd14621
catalytic domain of receptor-type tyrosine-protein phosphatase A, repeat 1; Receptor-type ...
606-902 6.05e-85

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: 278.83  E-value: 6.05e-85
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 998470296  606 DSEYASVHVSQWAKHVADLHADGDIGFSREYETFQHCTDPDLTSSYSQlNENKPKNRYINIVAYDHTRVILKPIPGQKkS 685
Cdd:cd14621     2 NRKYPPLPVDKLEEEINRRMADDNKLFREEFNALPACPIQATCEAASK-EENKEKNRYVNILPYDHSRVHLTPVEGVP-D 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 998470296  686 SDYINANYIDGYHKSRAFIGTQGPLPATFDDYWRMVWEQRVCIIIMITNLVERGRRKCDMYWPKEGTETYGIIQVKLVQE 765
Cdd:cd14621    80 SDYINASFINGYQEKNKFIAAQGPKEETVNDFWRMIWEQNTATIVMVTNLKERKECKCAQYWPDQGCWTYGNIRVSVEDV 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 998470296  766 IVMATYTIRTFAIKNIKVKKKQASERTVYQYHYTNWPDHGVPDHPLPVLSFVAKSSAANPPAAGPMIVHCSAGVGRTGTY 845
Cdd:cd14621   160 TVLVDYTVRKFCIQQVGDVTNKKPQRLITQFHFTSWPDFGVPFTPIGMLKFLKKVKNCNPQYAGAIVVHCSAGVGRTGTF 239
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 998470296  846 IVLDAMLRQMRQRQSVNVYGFLRHIRQQRNYLVQTEEQYVFIHDALLEAIDSGDTEV 902
Cdd:cd14621   240 IVIDAMLDMMHAERKVDVYGFVSRIRAQRCQMVQTDMQYVFIYQALLEHYLYGDTEL 296
R-PTPc-E-1 cd14620
catalytic domain of receptor-type tyrosine-protein phosphatase E, repeat 1; Receptor-type ...
663-893 1.31e-82

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: 269.50  E-value: 1.31e-82
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 998470296  663 YINIVAYDHTRVILKPIPGQKkSSDYINANYIDGYHKSRAFIGTQGPLPATFDDYWRMVWEQRVCIIIMITNLVERGRRK 742
Cdd:cd14620     1 YPNILPYDHSRVILSQLDGIP-CSDYINASYIDGYKEKNKFIAAQGPKQETVNDFWRMVWEQKSATIVMLTNLKERKEEK 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 998470296  743 CDMYWPKEGTETYGIIQVKLVQEIVMATYTIRTFAIKNIKVKKKQASeRTVYQYHYTNWPDHGVPDHPLPVLSFVAKSSA 822
Cdd:cd14620    80 CYQYWPDQGCWTYGNIRVAVEDCVVLVDYTIRKFCIQPQLPDGCKAP-RLVTQLHFTSWPDFGVPFTPIGMLKFLKKVKS 158
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 998470296  823 ANPPAAGPMIVHCSAGVGRTGTYIVLDAMLRQMRQRQSVNVYGFLRHIRQQRNYLVQTEEQYVFIHDALLE 893
Cdd:cd14620   159 VNPVHAGPIVVHCSAGVGRTGTFIVIDAMIDMMHAEQKVDVFEFVSRIRNQRPQMVQTDMQYSFIYQALLE 229
R-PTPc-T-1 cd14630
catalytic domain of receptor-type tyrosine-protein phosphatase T, repeat 1; Receptor-type ...
655-894 1.42e-82

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: 269.59  E-value: 1.42e-82
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 998470296  655 NENKPKNRYINIVAYDHTRVILKPIPGQKKSsDYINANYIDGYHKSRAFIGTQGPLPATFDDYWRMVWEQRVCIIIMITN 734
Cdd:cd14630     1 DENRNKNRYGNIISYDHSRVRLQLLDGDPHS-DYINANYIDGYHRPRHYIATQGPMQETVKDFWRMIWQENSASVVMVTN 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 998470296  735 LVERGRRKCDMYWPKEgTETYGIIQVKLVQEIVMATYTIRTFAIKnikvKKKQASERTVYQYHYTNWPDHGVPDHPLPVL 814
Cdd:cd14630    80 LVEVGRVKCVRYWPDD-TEVYGDIKVTLIETEPLAEYVIRTFTVQ----KKGYHEIREIRQFHFTSWPDHGVPCYATGLL 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 998470296  815 SFVAKSSAANPPAAGPMIVHCSAGVGRTGTYIVLDAMLRQMRQRQSVNVYGFLRHIRQQRNYLVQTEEQYVFIHDALLEA 894
Cdd:cd14630   155 GFVRQVKFLNPPDAGPIVVHCSAGAGRTGCFIAIDIMLDMAENEGVVDIFNCVRELRAQRVNMVQTEEQYVFVHDAILEA 234
R-PTPc-typeIIb-1 cd14555
catalytic domain of type IIb (or R2B) subfamily receptor-type tyrosine-protein phosphatases, ...
688-894 1.58e-79

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: 259.85  E-value: 1.58e-79
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 998470296  688 YINANYIDGYHKSRAFIGTQGPLPATFDDYWRMVWEQRVCIIIMITNLVERGRRKCDMYWPkEGTETYGIIQVKLVQEIV 767
Cdd:cd14555     1 YINANYIDGYHRPNHYIATQGPMQETVYDFWRMVWQENSASIVMVTNLVEVGRVKCSRYWP-DDTEVYGDIKVTLVETEP 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 998470296  768 MATYTIRTFAIKnikvKKKQASERTVYQYHYTNWPDHGVPDHPLPVLSFVAKSSAANPPAAGPMIVHCSAGVGRTGTYIV 847
Cdd:cd14555    80 LAEYVVRTFALE----RRGYHEIREVRQFHFTGWPDHGVPYHATGLLGFIRRVKASNPPSAGPIVVHCSAGAGRTGCYIV 155
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*..
gi 998470296  848 LDAMLRQMRQRQSVNVYGFLRHIRQQRNYLVQTEEQYVFIHDALLEA 894
Cdd:cd14555   156 IDIMLDMAEREGVVDIYNCVKELRSRRVNMVQTEEQYIFIHDAILEA 202
PTPc-N9 cd14543
catalytic domain of tyrosine-protein phosphatase non-receptor type 9; Tyrosine-protein ...
631-888 2.03e-78

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: 259.60  E-value: 2.03e-78
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 998470296  631 GFSREYE---------TFQHctdpdltssySQLNENKPKNRYINIVAYDHTRVILKPIPGQKKSsDYINANYIDGYHKSR 701
Cdd:cd14543     4 GIYEEYEdirreppagTFLC----------SLAPANQEKNRYGDVLCLDQSRVKLPKRNGDERT-DYINANFMDGYKQKN 72
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 998470296  702 AFIGTQGPLPATFDDYWRMVWEQRVCIIIMITNLVERGRRKCDMYWPKEG--TETYGIIQVKLVQEIVMATYTIRTFAIK 779
Cdd:cd14543    73 AYIATQGPLPKTYSDFWRMVWEQKVLVIVMTTRVVERGRVKCGQYWPLEEgsSLRYGDLTVTNLSVENKEHYKKTTLEIH 152
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 998470296  780 NIKVKKKqaseRTVYQYHYTNWPDHGVPDHPLPVLSFVAK-----SSAANP--------PAAGPMIVHCSAGVGRTGTYI 846
Cdd:cd14543   153 NTETDES----RQVTHFQFTSWPDFGVPSSAAALLDFLGEvrqqqALAVKAmgdrwkghPPGPPIVVHCSAGIGRTGTFC 228
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|..
gi 998470296  847 VLDAMLRQMRQRQSVNVYGFLRHIRQQRNYLVQTEEQYVFIH 888
Cdd:cd14543   229 TLDICLSQLEDVGTLNVMQTVRRMRTQRAFSIQTPDQYYFCY 270
R-PTPc-H cd14619
catalytic domain of receptor-type tyrosine-protein phosphatase H; Receptor-type ...
661-895 3.17e-78

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: 257.51  E-value: 3.17e-78
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 998470296  661 NRYINIVAYDHTRVILKPIPgQKKSSDYINANYIDGYHKSRAFIGTQGPLPATFDDYWRMVWEQRVCIIIMITNLVERGR 740
Cdd:cd14619     1 NRFRNVLPYDWSRVPLKPIH-EEPGSDYINANYMPGYWSSQEFIATQGPLPQTVGDFWRMIWEQQSSTIVMLTNCMEAGR 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 998470296  741 RKCDMYWPKEGTE-TYGIIQVKLVQEIVMATYTIRTFAIKNikvkKKQASERTVYQYHYTNWPDHGVPDHPLPVLSF--V 817
Cdd:cd14619    80 VKCEHYWPLDYTPcTYGHLRVTVVSEEVMENWTVREFLLKQ----VEEQKTLSVRHFHFTAWPDHGVPSSTDTLLAFrrL 155
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 998470296  818 AKSSAANPPAAGPMIVHCSAGVGRTGTYIVLDAMLRQMRQRQSVNVYGFLRHIRQQRNYLVQTEEQYVFIHDALLEAI 895
Cdd:cd14619   156 LRQWLDQTMSGGPTVVHCSAGVGRTGTLIALDVLLQQLQSEGLLGPFSFVQKMRENRPLMVQTESQYVFLHQCILDFL 233
R-PTPc-J cd14615
catalytic domain of receptor-type tyrosine-protein phosphatase J; Receptor-type ...
661-893 1.26e-77

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


Pssm-ID: 350463 [Multi-domain]  Cd Length: 229  Bit Score: 255.51  E-value: 1.26e-77
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 998470296  661 NRYINIVAYDHTRVILKpIPGQKkSSDYINANYIDGYHKSRAFIGTQGPLPATFDDYWRMVWEQRVCIIIMITNLVERGR 740
Cdd:cd14615     1 NRYNNVLPYDISRVKLS-VQSHS-TDDYINANYMPGYNSKKEFIAAQGPLPNTVKDFWRMVWEKNVYAIVMLTKCVEQGR 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 998470296  741 RKCDMYWPKEGTETYGIIQVKLVQEIVMATYTIRTFAIKNIKVKKKqaseRTVYQYHYTNWPDHGVPDHPLPVLSF---V 817
Cdd:cd14615    79 TKCEEYWPSKQKKDYGDITVTMTSEIVLPEWTIRDFTVKNAQTNES----RTVRHFHFTSWPDHGVPETTDLLINFrhlV 154
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 998470296  818 AKSSAANPPaAGPMIVHCSAGVGRTGTYIVLDAMLRQMRQRQSVNVYGFLRHIRQQRNYLVQTEEQYVFIHDALLE 893
Cdd:cd14615   155 REYMKQNPP-NSPILVHCSAGVGRTGTFIAIDRLIYQIENENVVDVYGIVYDLRMHRPLMVQTEDQYVFLNQCALD 229
PTPc-N11_6 cd14544
catalytic domain of tyrosine-protein phosphatase non-receptor type 11 and type 6; ...
657-897 7.75e-77

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: 254.31  E-value: 7.75e-77
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 998470296  657 NKPKNRYINIVAYDHTRVILKPIPGQKKSSDYINANYI-------DGYHKSRAFIGTQGPLPATFDDYWRMVWEQRVCII 729
Cdd:cd14544     1 NKGKNRYKNILPFDHTRVILKDRDPNVPGSDYINANYIrnenegpTTDENAKTYIATQGCLENTVSDFWSMVWQENSRVI 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 998470296  730 IMITNLVERGRRKCDMYWPKEG-TETYGIIQVKLVQEIVMATYTIRTFaikNIKVKKKQASERTVYQYHYTNWPDHGVPD 808
Cdd:cd14544    81 VMTTKEVERGKNKCVRYWPDEGmQKQYGPYRVQNVSEHDTTDYTLREL---QVSKLDQGDPIREIWHYQYLSWPDHGVPS 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 998470296  809 HPLPVLSFV--AKSSAANPPAAGPMIVHCSAGVGRTGTYIVLDAMLRQMRQRQ---SVNVYGFLRHIRQQRNYLVQTEEQ 883
Cdd:cd14544   158 DPGGVLNFLedVNQRQESLPHAGPIVVHCSAGIGRTGTFIVIDMLLDQIKRKGldcDIDIQKTIQMVRSQRSGMVQTEAQ 237
                         250
                  ....*....|....
gi 998470296  884 YVFIHDALLEAIDS 897
Cdd:cd14544   238 YKFIYVAVAQYIET 251
R-PTPc-B cd14617
catalytic domain of receptor-type tyrosine-protein phosphatase B; Receptor-type ...
661-888 6.30e-76

catalytic domain of receptor-type tyrosine-protein phosphatase B; Receptor-type tyrosine-protein phosphatase B (PTPRB), also known as receptor-type tyrosine-protein phosphatase beta (R-PTP-beta) or vascular endothelial protein tyrosine phosphatase(VE-PTP), belongs to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. PTPRB/VE-PTP is a member of the R3 subfamily of receptor-type phosphotyrosine phosphatases (RPTP), characterized by a unique modular composition consisting of multiple extracellular fibronectin type III (FN3) repeats and a single (most RPTP subtypes have two) cytoplasmic catalytic PTP domain. It is expressed specifically in vascular endothelial cells and it plays an important role in blood vessel remodeling and angiogenesis.


Pssm-ID: 350465 [Multi-domain]  Cd Length: 228  Bit Score: 250.61  E-value: 6.30e-76
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 998470296  661 NRYINIVAYDHTRVILKPIPgQKKSSDYINANYIDGYHKSRAFIGTQGPLPATFDDYWRMVWEQRVCIIIMITNLVERGR 740
Cdd:cd14617     1 NRYNNILPYDSTRVKLSNVD-DDPCSDYINASYIPGNNFRREYIATQGPLPGTKDDFWKMVWEQNVHNIVMVTQCVEKGR 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 998470296  741 RKCDMYWPKEGTET-YGIIQVKLVQEIVMATYTIRTFAIKNikvKKKQASERTVYQYHYTNWPDHGVPDHPLPVLSFV-- 817
Cdd:cd14617    80 VKCDHYWPADQDSLyYGDLIVQMLSESVLPEWTIREFKICS---EEQLDAPRLVRHFHYTVWPDHGVPETTQSLIQFVrt 156
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 998470296  818 AKSSAANPPAAGPMIVHCSAGVGRTGTYIVLDAMLRQMRQRQSVNVYGFLRHIRQQRNYLVQTEEQYVFIH 888
Cdd:cd14617   157 VRDYINRTPGSGPTVVHCSAGVGRTGTFIALDRILQQLDSKDSVDIYGAVHDLRLHRVHMVQTECQYVYLH 227
R-PTPc-A-E-1 cd14551
catalytic domain of receptor-type tyrosine-protein phosphatase A and E, repeat 1; ...
688-888 6.64e-76

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: 249.83  E-value: 6.64e-76
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 998470296  688 YINANYIDGYHKSRAFIGTQGPLPATFDDYWRMVWEQRVCIIIMITNLVERGRRKCDMYWPKEGTETYGIIQVKLVQEIV 767
Cdd:cd14551     1 YINASYIDGYQEKNKFIAAQGPKDETVNDFWRMIWEQGSATIVMVTNLKERKEKKCSQYWPDQGCWTYGNLRVRVEDTVV 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 998470296  768 MATYTIRTFAIKNIKVKKKQASERTVYQYHYTNWPDHGVPDHPLPVLSFVAKSSAANPPAAGPMIVHCSAGVGRTGTYIV 847
Cdd:cd14551    81 LVDYTTRKFCIQKVNRGIGEKRVRLVTQFHFTSWPDFGVPFTPIGMLKFLKKVKSANPPRAGPIVVHCSAGVGRTGTFIV 160
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|.
gi 998470296  848 LDAMLRQMRQRQSVNVYGFLRHIRQQRNYLVQTEEQYVFIH 888
Cdd:cd14551   161 IDAMLDMMHAEGKVDVFGFVSRIRQQRSQMVQTDMQYVFIY 201
R-PTPc-U-1 cd14632
catalytic domain of receptor-type tyrosine-protein phosphatase U, repeat 1; Receptor-type ...
688-894 1.09e-75

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: 249.20  E-value: 1.09e-75
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 998470296  688 YINANYIDGYHKSRAFIGTQGPLPATFDDYWRMVWEQRVCIIIMITNLVERGRRKCDMYWPKEgTETYGIIQVKLVQEIV 767
Cdd:cd14632     1 YINANYIDGYHRSNHFIATQGPKQEMVYDFWRMVWQEHCSSIVMITKLVEVGRVKCSKYWPDD-SDTYGDIKITLLKTET 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 998470296  768 MATYTIRTFAIKnikvKKKQASERTVYQYHYTNWPDHGVPDHPLPVLSFVAKSSAANPPAAGPMIVHCSAGVGRTGTYIV 847
Cdd:cd14632    80 LAEYSVRTFALE----RRGYSARHEVKQFHFTSWPEHGVPYHATGLLAFIRRVKASTPPDAGPVVVHCSAGAGRTGCYIV 155
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*..
gi 998470296  848 LDAMLRQMRQRQSVNVYGFLRHIRQQRNYLVQTEEQYVFIHDALLEA 894
Cdd:cd14632   156 LDVMLDMAECEGVVDIYNCVKTLCSRRINMIQTEEQYIFIHDAILEA 202
R-PTPc-K-1 cd14631
catalytic domain of receptor-type tyrosine-protein phosphatase K, repeat 1; Receptor-type ...
673-894 4.19e-73

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: 242.23  E-value: 4.19e-73
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 998470296  673 RVILKPIPgQKKSSDYINANYIDGYHKSRAFIGTQGPLPATFDDYWRMVWEQRVCIIIMITNLVERGRRKCDMYWPkEGT 752
Cdd:cd14631     1 RVILQPVE-DDPSSDYINANYIDGYQRPSHYIATQGPVHETVYDFWRMIWQEQSACIVMVTNLVEVGRVKCYKYWP-DDT 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 998470296  753 ETYGIIQVKLVQEIVMATYTIRTFAIKnikvKKKQASERTVYQYHYTNWPDHGVPDHPLPVLSFVAKSSAANPPAAGPMI 832
Cdd:cd14631    79 EVYGDFKVTCVEMEPLAEYVVRTFTLE----RRGYNEIREVKQFHFTGWPDHGVPYHATGLLSFIRRVKLSNPPSAGPIV 154
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 998470296  833 VHCSAGVGRTGTYIVLDAMLRQMRQRQSVNVYGFLRHIRQQRNYLVQTEEQYVFIHDALLEA 894
Cdd:cd14631   155 VHCSAGAGRTGCYIVIDIMLDMAEREGVVDIYNCVKALRSRRINMVQTEEQYIFIHDAILEA 216
PTPc-KIM cd14547
catalytic domain of the kinase interaction motif (KIM) family of protein-tyrosine phosphatases; ...
661-888 1.80e-72

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: 240.76  E-value: 1.80e-72
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 998470296  661 NRYINIVAYDHTRVILKPIPGQKKSsDYINANYIDGY-HKSRAFIGTQGPLPATFDDYWRMVWEQRVCIIIMITNLVERg 739
Cdd:cd14547     1 NRYKTILPNEHSRVCLPSVDDDPLS-SYINANYIRGYdGEEKAYIATQGPLPNTVADFWRMVWQEKTPIIVMITNLTEA- 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 998470296  740 RRKCDMYWPKEGTETYGIIQVKLVQEIVMATYTIRTFAIKNikvkkkQASERTVYQYHYTNWPDHGVPDHPLPVLSFVAK 819
Cdd:cd14547    79 KEKCAQYWPEEENETYGDFEVTVQSVKETDGYTVRKLTLKY------GGEKRYLKHYWYTSWPDHKTPEAAQPLLSLVQE 152
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 998470296  820 --SSAANPPAAGPMIVHCSAGVGRTGTYIVLDAMLRQMRQRQSVNVYGFLRHIRQQRNYLVQTEEQYVFIH 888
Cdd:cd14547   153 veEARQTEPHRGPIVVHCSAGIGRTGCFIATSIGCQQLREEGVVDVLGIVCQLRLDRGGMVQTAEQYEFVH 223
R-PTPc-V cd14618
catalytic domain of receptor-type tyrosine-protein phosphatase V; Receptor-type ...
661-892 2.11e-72

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: 241.00  E-value: 2.11e-72
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 998470296  661 NRYINIVAYDHTRVILKPIPGQKKSsDYINANYIDGYHKSRAFIGTQGPLPATFDDYWRMVWEQRVCIIIMITNLVERGR 740
Cdd:cd14618     1 NRYPHVLPYDHSRVRLSQLGGEPHS-DYINANFIPGYTSPQEFIATQGPLKKTIEDFWRLVWEQQVCNIIMLTVGMENGR 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 998470296  741 RKCDMYWPKEGTE-TYGIIQVKLVQEIVMATYTIRTFAIKNIKVKKkqasERTVYQYHYTNWPDHGVPDHPLPVLSFV-- 817
Cdd:cd14618    80 VLCDHYWPSESTPvSYGHITVHLLAQSSEDEWTRREFKLWHEDLRK----ERRVKHLHYTAWPDHGIPESTSSLMAFRel 155
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 998470296  818 AKSSAANPPAAGPMIVHCSAGVGRTGTYIVLDAMLRQMRQRQSVNVYGFLRHIRQQRNYLVQTEEQYVFIHDALL 892
Cdd:cd14618   156 VREHVQATKGKGPTLVHCSAGVGRSGTFIALDRLLRQLKEEKVVDVFNTVYILRMHRYLMIQTLSQYIFLHSCIL 230
PTP_fungal cd18533
fungal protein tyrosine phosphatases; This subfamily contains Saccharomyces cerevisiae ...
688-889 3.47e-72

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: 239.46  E-value: 3.47e-72
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 998470296  688 YINANYID-GYHKSRAFIGTQGPLPATFDDYWRMVWEQRVCIIIMITNLVERGRRKCDMYWP-KEGTETYGIIQVKLVQ- 764
Cdd:cd18533     1 YINASYITlPGTSSKRYIATQGPLPATIGDFWKMIWQNNVGVIVMLTPLVENGREKCDQYWPsGEYEGEYGDLTVELVSe 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 998470296  765 -EIVMATYTIRTFaikniKVKKKQASERTVYQYHYTNWPDHGVPDHPLPV--LSFVAKSSAANPPAAGPMIVHCSAGVGR 841
Cdd:cd18533    81 eENDDGGFIVREF-----ELSKEDGKVKKVYHIQYKSWPDFGVPDSPEDLltLIKLKRELNDSASLDPPIIVHCSAGVGR 155
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 998470296  842 TGTYIVLDAMLRQM----RQRQSVN-----VYGFLRHIRQQRNYLVQTEEQYVFIHD 889
Cdd:cd18533   156 TGTFIALDSLLDELkrglSDSQDLEdsedpVYEIVNQLRKQRMSMVQTLRQYIFLYD 212
R-PTP-LAR-2 cd14554
PTP-like domain of the LAR family receptor-type tyrosine-protein phosphatases, repeat 2; The ...
657-892 1.08e-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: 239.35  E-value: 1.08e-71
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 998470296  657 NKPKNRYINIVAYDHTRVILKPIPGQKkSSDYINANYIDGYHKSRAFIGTQGPLPATFDDYWRMVWEQRVCIIIMITNLV 736
Cdd:cd14554     6 NKFKNRLVNILPYESTRVCLQPIRGVE-GSDYINASFIDGYRQRGAYIATQGPLAETTEDFWRMLWEHNSTIIVMLTKLR 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 998470296  737 ERGRRKCDMYWPKEGTETYGIIQVKLVQEIVMATYTIRTFAIKNIkvkkKQASERTVYQYHYTNWPDHGVPDHPLPVLSF 816
Cdd:cd14554    85 EMGREKCHQYWPAERSARYQYFVVDPMAEYNMPQYILREFKVTDA----RDGQSRTVRQFQFTDWPEQGVPKSGEGFIDF 160
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 998470296  817 VAK--SSAANPPAAGPMIVHCSAGVGRTGTYIVLDAMLRQMRQRQSVNVYGFLRHIRQQRNYLVQTEEQYVFIHDALL 892
Cdd:cd14554   161 IGQvhKTKEQFGQEGPITVHCSAGVGRTGVFITLSIVLERMRYEGVVDVFQTVKLLRTQRPAMVQTEDQYQFCYRAAL 238
R-PTPc-O cd14614
catalytic domain of receptor-type tyrosine-protein phosphatase O; Receptor-type ...
646-888 1.66e-67

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: 227.46  E-value: 1.66e-67
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 998470296  646 DLTSSYSQLNENKPKNRYINIVAYDHTRVILKPIpGQKKSSDYINANYIDGYHKSRAFIGTQGPLPATFDDYWRMVWEQR 725
Cdd:cd14614     1 DIPHFAADLPVNRCKNRYTNILPYDFSRVKLVSM-HEEEGSDYINANYIPGYNSPQEYIATQGPLPETRNDFWKMVLQQK 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 998470296  726 VCIIIMITNLVERGRRKCDMYWP-KEGTETYGIIQVKLVQEIVMATYTIRTFaikniKVKKKQASERtVYQYHYTNWPDH 804
Cdd:cd14614    80 SQIIVMLTQCNEKRRVKCDHYWPfTEEPVAYGDITVEMLSEEEQPDWAIREF-----RVSYADEVQD-VMHFNYTAWPDH 153
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 998470296  805 GVP--DHPLPVLSFVAKSSAANPPAAGPMIVHCSAGVGRTGTYIVLDAMLRQMRQRQSVNVYGFLRHIRQQRNYLVQTEE 882
Cdd:cd14614   154 GVPtaNAAESILQFVQMVRQQAVKSKGPMIIHCSAGVGRTGTFIALDRLLQHIRDHEFVDILGLVSEMRSYRMSMVQTEE 233

                  ....*.
gi 998470296  883 QYVFIH 888
Cdd:cd14614   234 QYIFIH 239
R-PTPc-C-1 cd14557
catalytic domain of receptor-type tyrosine-protein phosphatase C, repeat 1; Receptor-type ...
688-888 2.90e-67

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: 225.09  E-value: 2.90e-67
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 998470296  688 YINANYIDGYHKSRAFIGTQGPLPATFDDYWRMVWEQRVCIIIMITNLVERGRRKCDMYWP--KEGTETYGIIQVKLVQE 765
Cdd:cd14557     1 YINASYIDGFKEPRKYIAAQGPKDETVDDFWRMIWEQKSTVIVMVTRCEEGNRNKCAQYWPsmEEGSRAFGDVVVKINEE 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 998470296  766 IVMATYTIRTFAIKNikvKKKQASERTVYQYHYTNWPDHGVPDHPLPVLSFVAKSSAANPPAAGPMIVHCSAGVGRTGTY 845
Cdd:cd14557    81 KICPDYIIRKLNINN---KKEKGSGREVTHIQFTSWPDHGVPEDPHLLLKLRRRVNAFNNFFSGPIVVHCSAGVGRTGTY 157
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|...
gi 998470296  846 IVLDAMLRQMRQRQSVNVYGFLRHIRQQRNYLVQTEEQYVFIH 888
Cdd:cd14557   158 IGIDAMLEGLEAEGRVDVYGYVVKLRRQRCLMVQVEAQYILIH 200
PTPc-N11 cd14605
catalytic domain of tyrosine-protein phosphatase non-receptor type 11; Tyrosine-protein ...
656-897 5.35e-65

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: 220.66  E-value: 5.35e-65
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 998470296  656 ENKPKNRYINIVAYDHTRVILKPIPGQKKSSDYINANYIDGYHKS--------RAFIGTQGPLPATFDDYWRMVWEQRVC 727
Cdd:cd14605     1 ENKNKNRYKNILPFDHTRVVLHDGDPNEPVSDYINANIIMPEFETkcnnskpkKSYIATQGCLQNTVNDFWRMVFQENSR 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 998470296  728 IIIMITNLVERGRRKCDMYWPKE-GTETYGIIQVKLVQEIVMATYTIRTFAIKNIkvkKKQASERTVYQYHYTNWPDHGV 806
Cdd:cd14605    81 VIVMTTKEVERGKSKCVKYWPDEyALKEYGVMRVRNVKESAAHDYILRELKLSKV---GQGNTERTVWQYHFRTWPDHGV 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 998470296  807 PDHPLPVLSFV--AKSSAANPPAAGPMIVHCSAGVGRTGTYIVLDAMLRQMRQRQ---SVNVYGFLRHIRQQRNYLVQTE 881
Cdd:cd14605   158 PSDPGGVLDFLeeVHHKQESIMDAGPVVVHCSAGIGRTGTFIVIDILIDIIREKGvdcDIDVPKTIQMVRSQRSGMVQTE 237
                         250
                  ....*....|....*.
gi 998470296  882 EQYVFIHDALLEAIDS 897
Cdd:cd14605   238 AQYRFIYMAVQHYIET 253
R-PTP-N2 cd14610
PTP-like domain of receptor-type tyrosine-protein phosphatase N2; Receptor-type ...
634-897 1.47e-63

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: 218.00  E-value: 1.47e-63
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 998470296  634 REYETF-QHCTDPDlTSSYSQLNENKPKNRYINIVAYDHTRVILKpIPGQKKSSDYINANYI-DGYHKSRAFIGTQGPLP 711
Cdd:cd14610    21 KEWEALcAYQAEPN-ATNVAQREENVQKNRSLAVLPYDHSRIILK-AENSHSHSDYINASPImDHDPRNPAYIATQGPLP 98
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 998470296  712 ATFDDYWRMVWEQRVCIIIMITNLVERGRRKCDMYWPKEGTETYGIIQVKLVQE-IVMATYTIRTFAIKNIKVKKKqase 790
Cdd:cd14610    99 ATVADFWQMVWESGCVVIVMLTPLAENGVKQCYHYWPDEGSNLYHIYEVNLVSEhIWCEDFLVRSFYLKNLQTNET---- 174
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 998470296  791 RTVYQYHYTNWPDHGVPDHPLPVLSFVAKSSAANPPAAGPMIVHCSAGVGRTGTYIVLDAMLRQM-RQRQSVNVYGFLRH 869
Cdd:cd14610   175 RTVTQFHFLSWNDQGVPASTRSLLDFRRKVNKCYRGRSCPIIVHCSDGAGRSGTYILIDMVLNKMaKGAKEIDIAATLEH 254
                         250       260
                  ....*....|....*....|....*...
gi 998470296  870 IRQQRNYLVQTEEQYVFIHDALLEAIDS 897
Cdd:cd14610   255 LRDQRPGMVQTKEQFEFALTAVAEEVNA 282
PTPc-N6 cd14606
catalytic domain of tyrosine-protein phosphatase non-receptor type 6; Tyrosine-protein ...
653-897 4.04e-63

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: 215.90  E-value: 4.04e-63
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 998470296  653 QLNENKPKNRYINIVAYDHTRVILK----PIPGqkksSDYINANYIDGY-----HKSRAFIGTQGPLPATFDDYWRMVWE 723
Cdd:cd14606    14 QRPENKSKNRYKNILPFDHSRVILQgrdsNIPG----SDYINANYVKNQllgpdENAKTYIASQGCLEATVNDFWQMAWQ 89
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 998470296  724 QRVCIIIMITNLVERGRRKCDMYWPKEGTE-TYGIIQVKLVQEIVMATYTIRTFAIKNIKVKKKqasERTVYQYHYTNWP 802
Cdd:cd14606    90 ENSRVIVMTTREVEKGRNKCVPYWPEVGMQrAYGPYSVTNCGEHDTTEYKLRTLQVSPLDNGEL---IREIWHYQYLSWP 166
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 998470296  803 DHGVPDHPLPVLSFVAKSSAANP--PAAGPMIVHCSAGVGRTGTYIVLDAMLRQMRQRQ---SVNVYGFLRHIRQQRNYL 877
Cdd:cd14606   167 DHGVPSEPGGVLSFLDQINQRQEslPHAGPIIVHCSAGIGRTGTIIVIDMLMENISTKGldcDIDIQKTIQMVRAQRSGM 246
                         250       260
                  ....*....|....*....|
gi 998470296  878 VQTEEQYVFIHDALLEAIDS 897
Cdd:cd14606   247 VQTEAQYKFIYVAIAQFIET 266
R-PTP-D-2 cd14628
PTP-like domain of receptor-type tyrosine-protein phosphatase D, repeat 2; Receptor-type ...
657-899 1.89e-62

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: 214.98  E-value: 1.89e-62
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 998470296  657 NKPKNRYINIVAYDHTRVILKPIPGQKkSSDYINANYIDGYHKSRAFIGTQGPLPATFDDYWRMVWEQRVCIIIMITNLV 736
Cdd:cd14628    52 NKFKNRLVNIMPYESTRVCLQPIRGVE-GSDYINASFIDGYRQQKAYIATQGPLAETTEDFWRMLWEHNSTIVVMLTKLR 130
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 998470296  737 ERGRRKCDMYWPKEGTETYGIIQVKLVQEIVMATYTIRTFAIKNikvkKKQASERTVYQYHYTNWPDHGVPDHPLPVLSF 816
Cdd:cd14628   131 EMGREKCHQYWPAERSARYQYFVVDPMAEYNMPQYILREFKVTD----ARDGQSRTVRQFQFTDWPEQGVPKSGEGFIDF 206
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 998470296  817 VAKSSAANPPAA--GPMIVHCSAGVGRTGTYIVLDAMLRQMRQRQSVNVYGFLRHIRQQRNYLVQTEEQYVFIHDALLEA 894
Cdd:cd14628   207 IGQVHKTKEQFGqdGPISVHCSAGVGRTGVFITLSIVLERMRYEGVVDIFQTVKMLRTQRPAMVQTEDQYQFCYRAALEY 286

                  ....*
gi 998470296  895 IDSGD 899
Cdd:cd14628   287 LGSFD 291
R-PTP-S-2 cd14627
PTP-like domain of receptor-type tyrosine-protein phosphatase S, repeat 2; Receptor-type ...
657-897 5.63e-62

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: 213.44  E-value: 5.63e-62
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 998470296  657 NKPKNRYINIVAYDHTRVILKPIPGQKkSSDYINANYIDGYHKSRAFIGTQGPLPATFDDYWRMVWEQRVCIIIMITNLV 736
Cdd:cd14627    53 NKFKNRLVNIMPYETTRVCLQPIRGVE-GSDYINASFIDGYRQQKAYIATQGPLAETTEDFWRMLWENNSTIVVMLTKLR 131
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 998470296  737 ERGRRKCDMYWPKEGTETYGIIQVKLVQEIVMATYTIRTFAIKNikvkKKQASERTVYQYHYTNWPDHGVPDHPLPVLSF 816
Cdd:cd14627   132 EMGREKCHQYWPAERSARYQYFVVDPMAEYNMPQYILREFKVTD----ARDGQSRTVRQFQFTDWPEQGVPKSGEGFIDF 207
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 998470296  817 VAKSSAANPPAA--GPMIVHCSAGVGRTGTYIVLDAMLRQMRQRQSVNVYGFLRHIRQQRNYLVQTEEQYVFIHDALLEA 894
Cdd:cd14627   208 IGQVHKTKEQFGqdGPISVHCSAGVGRTGVFITLSIVLERMRYEGVVDIFQTVKMLRTQRPAMVQTEDEYQFCYQAALEY 287

                  ...
gi 998470296  895 IDS 897
Cdd:cd14627   288 LGS 290
PTPc-N22_18_12 cd14542
catalytic domain of tyrosine-protein phosphatase non-receptor type 22, type 18 and type 12; ...
688-888 5.11e-61

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: 207.28  E-value: 5.11e-61
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 998470296  688 YINANYIDGYHKSRAFIGTQGPLPATFDDYWRMVWEQRVCIIIMITNLVERGRRKCDMYWPKEGTE--TYGIIQVKLV-Q 764
Cdd:cd14542     1 YINANFIKGVSGSKAYIATQGPLPNTVLDFWRMIWEYNVQVIVMACREFEMGKKKCERYWPEEGEEqlQFGPFKISLEkE 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 998470296  765 EIVMATYTIRTFAIknikvkKKQASERTVYQYHYTNWPDHGVPDHPLPVLSFVAKSSAANPPAAGPMIVHCSAGVGRTGT 844
Cdd:cd14542    81 KRVGPDFLIRTLKV------TFQKESRTVYQFHYTAWPDHGVPSSVDPILDLVRLVRDYQGSEDVPICVHCSAGCGRTGT 154
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*...
gi 998470296  845 YIVLD----AMLRQMRQrQSVNVYGFLRHIRQQRNYLVQTEEQYVFIH 888
Cdd:cd14542   155 ICAIDyvwnLLKTGKIP-EEFSLFDLVREMRKQRPAMVQTKEQYELVY 201
R-PTP-N cd14609
PTP-like domain of receptor-type tyrosine-protein phosphatase N; Receptor-type ...
648-897 7.99e-61

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


Pssm-ID: 350457 [Multi-domain]  Cd Length: 281  Bit Score: 209.89  E-value: 7.99e-61
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 998470296  648 TSSYSQLNENKPKNRYINIVAYDHTRVILKpIPGQKKSSDYINAN-YIDGYHKSRAFIGTQGPLPATFDDYWRMVWEQRV 726
Cdd:cd14609    33 TCSTAQGEANVKKNRNPDFVPYDHARIKLK-AESNPSRSDYINASpIIEHDPRMPAYIATQGPLSHTIADFWQMVWENGC 111
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 998470296  727 CIIIMITNLVERGRRKCDMYWPKEGTETYGIIQVKLVQE-IVMATYTIRTFAIKNIKVKKKqaseRTVYQYHYTNWPDHG 805
Cdd:cd14609   112 TVIVMLTPLVEDGVKQCDRYWPDEGSSLYHIYEVNLVSEhIWCEDFLVRSFYLKNVQTQET----RTLTQFHFLSWPAEG 187
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 998470296  806 VPDHPLPVLSFVAKSSAANPPAAGPMIVHCSAGVGRTGTYIVLDAMLRQM-RQRQSVNVYGFLRHIRQQRNYLVQTEEQY 884
Cdd:cd14609   188 IPSSTRPLLDFRRKVNKCYRGRSCPIIVHCSDGAGRTGTYILIDMVLNRMaKGVKEIDIAATLEHVRDQRPGMVRTKDQF 267
                         250
                  ....*....|...
gi 998470296  885 VFIHDALLEAIDS 897
Cdd:cd14609   268 EFALTAVAEEVNA 280
PTPc-N18 cd14603
catalytic domain of tyrosine-protein phosphatase non-receptor type 18; Tyrosine-protein ...
656-893 3.30e-60

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: 207.76  E-value: 3.30e-60
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 998470296  656 ENKPKNRYINIVAYDHTRVILKPIPgQKKSSDYINANYIDGYHKSRAFIGTQGPLPATFDDYWRMVWEQRVCIIIMITNL 735
Cdd:cd14603    29 ENVKKNRYKDILPYDQTRVILSLLQ-EEGHSDYINANFIKGVDGSRAYIATQGPLSHTVLDFWRMIWQYGVKVILMACRE 107
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 998470296  736 VERGRRKCDMYWP-KEGTETYGIIQVKLVQEIVMATYTIrtfaIKNIKVKKKQASeRTVYQYHYTNWPDHGVPDHPLPVL 814
Cdd:cd14603   108 IEMGKKKCERYWAqEQEPLQTGPFTITLVKEKRLNEEVI----LRTLKVTFQKES-RSVSHFQYMAWPDHGIPDSPDCML 182
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 998470296  815 SFVAKSSAANPPAAGPMIVHCSAGVGRTGTYIVLDaMLRQMRQRQSV----NVYGFLRHIRQQRNYLVQTEEQYVFIHDA 890
Cdd:cd14603   183 AMIELARRLQGSGPEPLCVHCSAGCGRTGVICTVD-YVRQLLLTQRIppdfSIFDVVLEMRKQRPAAVQTEEQYEFLYHT 261

                  ...
gi 998470296  891 LLE 893
Cdd:cd14603   262 VAQ 264
R-PTP-F-2 cd14629
PTP-like domain of receptor-type tyrosine-protein phosphatase F, repeat 2; Receptor-type ...
657-897 5.10e-60

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: 208.04  E-value: 5.10e-60
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 998470296  657 NKPKNRYINIVAYDHTRVILKPIPGQKkSSDYINANYIDGYHKSRAFIGTQGPLPATFDDYWRMVWEQRVCIIIMITNLV 736
Cdd:cd14629    53 NKFKNRLVNIMPYELTRVCLQPIRGVE-GSDYINASFIDGYRQQKAYIATQGPLAETTEDFWRMLWEHNSTIVVMLTKLR 131
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 998470296  737 ERGRRKCDMYWPKEGTETYGIIQVKLVQEIVMATYTIRTFAIKNikvkKKQASERTVYQYHYTNWPDHGVPDHPLPVLSF 816
Cdd:cd14629   132 EMGREKCHQYWPAERSARYQYFVVDPMAEYNMPQYILREFKVTD----ARDGQSRTIRQFQFTDWPEQGVPKTGEGFIDF 207
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 998470296  817 VAKSSAANPPAA--GPMIVHCSAGVGRTGTYIVLDAMLRQMRQRQSVNVYGFLRHIRQQRNYLVQTEEQYVFIHDALLEA 894
Cdd:cd14629   208 IGQVHKTKEQFGqdGPITVHCSAGVGRTGVFITLSIVLERMRYEGVVDMFQTVKTLRTQRPAMVQTEDQYQLCYRAALEY 287

                  ...
gi 998470296  895 IDS 897
Cdd:cd14629   288 LGS 290
PTPc-N20_13 cd14538
catalytic domain of tyrosine-protein phosphatase non-receptor type 20 and type 13; ...
688-895 2.05e-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: 202.99  E-value: 2.05e-59
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 998470296  688 YINANYI------DGYHksraFIGTQGPLPATFDDYWRMVWEQRVCIIIMITNLVERGRRKCDMYWPKEGTET---YGII 758
Cdd:cd14538     1 YINASHIripvggDTYH----YIACQGPLPNTTGDFWQMVWEQKSEVIAMVTQDVEGGKVKCHRYWPDSLNKPlicGGRL 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 998470296  759 QVKLVQEIVMATYTIRTFAIKNIKVKKkqasERTVYQYHYTNWPDHGVPDHPLPVLSFV--AKSSAANppaaGPMIVHCS 836
Cdd:cd14538    77 EVSLEKYQSLQDFVIRRISLRDKETGE----VHHITHLNFTTWPDHGTPQSADPLLRFIryMRRIHNS----GPIVVHCS 148
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 998470296  837 AGVGRTGTYIVLDAMLRQMRQRQSVNVYGFLRHIRQQRNYLVQTEEQYVFIHDALLEAI 895
Cdd:cd14538   149 AGIGRTGVLITIDVALGLIERDLPFDIQDIVKDLREQRQGMIQTKDQYIFCYKACLEVL 207
R-PTPc-Q cd14616
catalytic domain of receptor-type tyrosine-protein phosphatase Q; Receptor-type ...
661-888 3.40e-59

catalytic domain of receptor-type tyrosine-protein phosphatase Q; Receptor-type tyrosine-protein phosphatase Q (PTPRQ or R-PTP-Q), also called phosphatidylinositol phosphatase PTPRQ, belongs to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. PTPRQ is a member of the R3 subfamily of receptor-type phosphotyrosine phosphatases (RPTP), characterized by a unique modular composition consisting of multiple extracellular fibronectin type III (FN3) repeats (18 in PTPRQ) and a single (most RPTP subtypes have two) cytoplasmic catalytic PTP domain. It displays low tyrosine-protein phosphatase activity; rather, it functions as a phosphatidylinositol phosphatase required for auditory processes. It regulates the levels of phosphatidylinositol 4,5-bisphosphate (PIP2) in the basal region of hair bundles. It can dephosphorylate a broad range of phosphatidylinositol phosphates, including phosphatidylinositol 3,4,5-trisphosphate and most phosphatidylinositol monophosphates and diphosphates.


Pssm-ID: 350464 [Multi-domain]  Cd Length: 224  Bit Score: 203.21  E-value: 3.40e-59
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 998470296  661 NRYINIVAYDHTRVILKPIPGQKkSSDYINANYIDGYHKSRAFIGTQGPLPATFDDYWRMVWEQRVCIIIMITNLVERGR 740
Cdd:cd14616     1 NRFPNIKPYNNNRVKLIADAGVP-GSDYINASYISGYLCPNEFIATQGPLPGTVGDFWRMVWETRAKTIVMLTQCFEKGR 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 998470296  741 RKCDMYWPKEG--TETYGIIQVKLVQEIVMATYTIRTFAIKnikvkkKQASERTVYQYHYTNWPDHGVPDHPLPVLSFVA 818
Cdd:cd14616    80 IRCHQYWPEDNkpVTVFGDIVITKLMEDVQIDWTIRDLKIE------RHGDYMMVRQCNFTSWPEHGVPESSAPLIHFVK 153
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 998470296  819 KSSAANPPAAGPMIVHCSAGVGRTGTYIVLDAMLRQMRQRQSVNVYGFLRHIRQQRNYLVQTEEQYVFIH 888
Cdd:cd14616   154 LVRASRAHDNTPMIVHCSAGVGRTGVFIALDHLTQHINDHDFVDIYGLVAELRSERMCMVQNLAQYIFLH 223
PTPc-N1_2 cd14545
catalytic domain of tyrosine-protein phosphatase non-receptor type 1 and type 2; ...
660-886 6.42e-59

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: 202.62  E-value: 6.42e-59
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 998470296  660 KNRYINIVAYDHTRVILKPipgQKKSSDYINANYIDGYHKSRAFIGTQGPLPATFDDYWRMVWEQRVCIIIMITNLVERG 739
Cdd:cd14545     1 LNRYRDRDPYDHDRSRVKL---KQGDNDYINASLVEVEEAKRSYILTQGPLPNTSGHFWQMVWEQNSKAVIMLNKLMEKG 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 998470296  740 RRKCDMYWPKEGTETYGI----IQVKLVQEIVMATYTIRTFAIKNIKVKKkqasERTVYQYHYTNWPDHGVPDHPLPVLS 815
Cdd:cd14545    78 QIKCAQYWPQGEGNAMIFedtgLKVTLLSEEDKSYYTVRTLELENLKTQE----TREVLHFHYTTWPDFGVPESPAAFLN 153
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 998470296  816 FVAK--SSAANPPAAGPMIVHCSAGVGRTGTYIVLDAMLRQMRQRQ--SVNVYGFLRHIRQQRNYLVQTEEQYVF 886
Cdd:cd14545   154 FLQKvrESGSLSSDVGPPVVHCSAGIGRSGTFCLVDTCLVLIEKGNpsSVDVKKVLLEMRKYRMGLIQTPDQLRF 228
PTPc-N7 cd14612
catalytic domain of tyrosine-protein phosphatase non-receptor type 7; Tyrosine-protein ...
660-891 6.95e-59

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


Pssm-ID: 350460 [Multi-domain]  Cd Length: 247  Bit Score: 203.14  E-value: 6.95e-59
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 998470296  660 KNRYINIVAYDHTRVILKPIPGQKKSSDYINANYIDGYH-KSRAFIGTQGPLPATFDDYWRMVWEQRVCIIIMITNLVER 738
Cdd:cd14612    18 KDRYKTILPNPQSRVCLRRAGSQEEEGSYINANYIRGYDgKEKAYIATQGPMLNTVSDFWEMVWQEECPIIVMITKLKEK 97
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 998470296  739 gRRKCDMYWPkEGTETYG--IIQVKLVQEIvmATYTIRTFAIKNikvkkkQASERTVYQYHYTNWPDHGVPDHPLPVLSF 816
Cdd:cd14612    98 -KEKCVHYWP-EKEGTYGrfEIRVQDMKEC--DGYTIRDLTIQL------EEESRSVKHYWFSSWPDHQTPESAGPLLRL 167
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 998470296  817 VAK-----SSAANPpaaGPMIVHCSAGVGRTGTYIVLDAMLRQMRQRQSVNVYGFLRHIRQQRNYLVQTEEQYVFIHDAL 891
Cdd:cd14612   168 VAEveesrQTAASP---GPIVVHCSAGIGRTGCFIATSIGCQQLKDTGKVDILGIVCQLRLDRGGMIQTSEQYQFLHHTL 244
PTPc-N22 cd14602
catalytic domain of tyrosine-protein phosphatase non-receptor type 22; Tyrosine-protein ...
660-893 8.32e-59

catalytic domain of tyrosine-protein phosphatase non-receptor type 22; Tyrosine-protein phosphatase non-receptor type 22 (PTPN22), also called lymphoid phosphatase (LyP), PEST-domain phosphatase (PEP), or hematopoietic cell protein-tyrosine phosphatase 70Z-PEP, belongs to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. PTPN22 is expressed in hematopoietic cells and it functions as a key regulator of immune homeostasis by inhibiting T-cell receptor signaling through the direct dephosphorylation of Src family kinases (Lck and Fyn), ITAMs of the TCRz/CD3 complex, and other signaling molecules. Mutations in the PTPN22 gene are associated with multiple connective tissue and autoimmune diseases including type 1 diabetes mellitus, rheumatoid arthritis, and systemic lupus erythematosus. PTPN22 contains an N-terminal catalytic PTP domain and four proline-rich regions at the C-terminus.


Pssm-ID: 350450 [Multi-domain]  Cd Length: 234  Bit Score: 202.38  E-value: 8.32e-59
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 998470296  660 KNRYINIVAYDHTRVILKPIPGQKkSSDYINANYIDGYHKSRAFIGTQGPLPATFDDYWRMVWEQRVCIIIMITNLVERG 739
Cdd:cd14602     1 KNRYKDILPYDHSRVELSLITSDE-DSDYINANFIKGVYGPRAYIATQGPLSTTLLDFWRMIWEYSVLIIVMACMEFEMG 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 998470296  740 RRKCDMYWPKEGTET--YGIIQVKLVQEIVMATYTIRTfaiknIKVKKKQASeRTVYQYHYTNWPDHGVPDHPLPVLSFV 817
Cdd:cd14602    80 KKKCERYWAEPGEMQleFGPFSVTCEAEKRKSDYIIRT-----LKVKFNSET-RTIYQFHYKNWPDHDVPSSIDPILELI 153
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 998470296  818 AKSSAANPPAAGPMIVHCSAGVGRTGTYIVLDAMLRQMRQR---QSVNVYGFLRHIRQQRNYLVQTEEQYVFIHDALLE 893
Cdd:cd14602   154 WDVRCYQEDDSVPICIHCSAGCGRTGVICAIDYTWMLLKDGiipENFSVFSLIQEMRTQRPSLVQTKEQYELVYNAVIE 232
PTPc-N12 cd14604
catalytic domain of tyrosine-protein phosphatase non-receptor type 12; Tyrosine-protein ...
656-891 1.70e-58

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: 204.01  E-value: 1.70e-58
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 998470296  656 ENKPKNRYINIVAYDHTRVILKpIPGQKKSSDYINANYIDGYHKSRAFIGTQGPLPATFDDYWRMVWEQRVCIIIMITNL 735
Cdd:cd14604    56 ENVKKNRYKDILPFDHSRVKLT-LKTSSQDSDYINANFIKGVYGPKAYIATQGPLANTVIDFWRMIWEYNVAIIVMACRE 134
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 998470296  736 VERGRRKCDMYWPKEGTE--TYGIIQVKLVQEIVMATYTIRTFAIKNikvkkkQASERTVYQYHYTNWPDHGVP---DHP 810
Cdd:cd14604   135 FEMGRKKCERYWPLYGEEpmTFGPFRISCEAEQARTDYFIRTLLLEF------QNETRRLYQFHYVNWPDHDVPssfDSI 208
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 998470296  811 LPVLSFVAKSSAANPPaagPMIVHCSAGVGRTGTYIVLD---AMLRQMRQRQSVNVYGFLRHIRQQRNYLVQTEEQYVFI 887
Cdd:cd14604   209 LDMISLMRKYQEHEDV---PICIHCSAGCGRTGAICAIDytwNLLKAGKIPEEFNVFNLIQEMRTQRHSAVQTKEQYELV 285

                  ....
gi 998470296  888 HDAL 891
Cdd:cd14604   286 HRAI 289
PTPc-N3_4 cd14541
catalytic domain of tyrosine-protein phosphatase non-receptor type 21 and type 14; ...
687-894 2.07e-58

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: 200.25  E-value: 2.07e-58
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 998470296  687 DYINANYID----GYHKSRAFIGTQGPLPATFDDYWRMVWEQRVCIIIMITNLVERGRRKCDMYWPKEG-TETYGIIQVK 761
Cdd:cd14541     1 DYINANYVNmeipGSGIVNRYIAAQGPLPNTCADFWQMVWEQKSTLIVMLTTLVERGRVKCHQYWPDLGeTMQFGNLQIT 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 998470296  762 LVQEIVMATYTIRTFAIKNIKVKKkqasERTVYQYHYTNWPDHGVPDHPLPVLSFVAKSSAANPPAAGPMIVHCSAGVGR 841
Cdd:cd14541    81 CVSEEVTPSFAFREFILTNTNTGE----ERHITQMQYLAWPDHGVPDDSSDFLDFVKRVRQNRVGMVEPTVVHCSAGIGR 156
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 998470296  842 TGTYIVLDAMLRQMRQRQSVNVYGFLRHIRQQRNYLVQTEEQYVFIHDALLEA 894
Cdd:cd14541   157 TGVLITMETAMCLIEANEPVYPLDIVRTMRDQRAMLIQTPSQYRFVCEAILRV 209
PTPc-N5 cd14613
catalytic domain of tyrosine-protein phosphatase non-receptor type 5; Tyrosine-protein ...
660-891 6.81e-58

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: 200.47  E-value: 6.81e-58
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 998470296  660 KNRYINIVAYDHTRVILKPIPGQKKSSDYINANYIDGY-HKSRAFIGTQGPLPATFDDYWRMVWEQRVCIIIMITNLVER 738
Cdd:cd14613    28 KNRYKTILPNPHSRVCLTSPDQDDPLSSYINANYIRGYgGEEKVYIATQGPTVNTVGDFWRMVWQERSPIIVMITNIEEM 107
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 998470296  739 GRrKCDMYWPKEGTeTYGIIQVKLVQEIVMATYTIRTFAIKnikvkkKQASERTVYQYHYTNWPDHGVPDHPLPVLSFVA 818
Cdd:cd14613   108 NE-KCTEYWPEEQV-TYEGIEITVKQVIHADDYRLRLITLK------SGGEERGLKHYWYTSWPDQKTPDNAPPLLQLVQ 179
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 998470296  819 KSSAAN---PPAAGPMIVHCSAGVGRTGTYIVLDAMLRQMRQRQSVNVYGFLRHIRQQRNYLVQTEEQYVFIHDAL 891
Cdd:cd14613   180 EVEEARqqaEPNCGPVIVHCSAGIGRTGCFIATSICCKQLRNEGVVDILRTTCQLRLDRGGMIQTCEQYQFVHHVL 255
R-PTPc-A-2 cd14623
catalytic domain of receptor-type tyrosine-protein phosphatase A, repeat 2; Receptor-type ...
662-893 1.06e-57

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: 199.12  E-value: 1.06e-57
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 998470296  662 RYINIVAYDHTRVILkPIPGQKKSSDYINANYIDGYHKSRAFIGTQGPLPATFDDYWRMVWEQRVCIIIMITNLVERGRR 741
Cdd:cd14623     1 RVLQIIPYEFNRVII-PVKRGEENTDYVNASFIDGYRQKDSYIASQGPLQHTIEDFWRMIWEWKSCSIVMLTELEERGQE 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 998470296  742 KCDMYWPKEGTETYGIIQVKLVQEIVMATYTIRTFAIKNIKVKKkqasERTVYQYHYTNWPDHGVPDHPLPVLSFVAKSS 821
Cdd:cd14623    80 KCAQYWPSDGSVSYGDITIELKKEEECESYTVRDLLVTNTRENK----SRQIRQFHFHGWPEVGIPSDGKGMINIIAAVQ 155
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 998470296  822 AANPPAAG-PMIVHCSAGVGRTGTYIVLDAMLRQMRQRQSVNVYGFLRHIRQQRNYLVQTEEQYVFIHDALLE 893
Cdd:cd14623   156 KQQQQSGNhPITVHCSAGAGRTGTFCALSTVLERVKAEGILDVFQTVKSLRLQRPHMVQTLEQYEFCYKVVQE 228
PTPc-N1 cd14608
catalytic domain of tyrosine-protein phosphatase non-receptor type 1; Tyrosine-protein ...
646-902 4.15e-57

catalytic domain of tyrosine-protein phosphatase non-receptor type 1; Tyrosine-protein phosphatase non-receptor type 1 (PTPN1), also called protein-tyrosine phosphatase 1B (PTP-1B), belongs to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. PTPN1/PTP-1B is the first PTP to be purified and characterized and is the prototypical intracellular PTP found in a wide variety of human tissues. It contains an N-terminal catalytic PTP domain, followed by two tandem proline-rich motifs that mediate interaction with SH3-domain-containing proteins, and a small hydrophobic stretch that localizes the enzyme to the endoplasmic reticulum (ER). It dephosphorylates and regulates the activity of a number of receptor tyrosine kinases, including the insulin receptor, the EGF receptor, and the PDGF receptor.


Pssm-ID: 350456 [Multi-domain]  Cd Length: 277  Bit Score: 199.10  E-value: 4.15e-57
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 998470296  646 DLTSSYSQLNENKPKNRYINIVAYDHTRVILkpipgQKKSSDYINANYIDGYHKSRAFIGTQGPLPATFDDYWRMVWEQR 725
Cdd:cd14608    14 DFPCRVAKLPKNKNRNRYRDVSPFDHSRIKL-----HQEDNDYINASLIKMEEAQRSYILTQGPLPNTCGHFWEMVWEQK 88
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 998470296  726 VCIIIMITNLVERGRRKCDMYWP-KEGTETY---GIIQVKLVQEIVMATYTIRTFAIKNIKVKKKqaseRTVYQYHYTNW 801
Cdd:cd14608    89 SRGVVMLNRVMEKGSLKCAQYWPqKEEKEMIfedTNLKLTLISEDIKSYYTVRQLELENLTTQET----REILHFHYTTW 164
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 998470296  802 PDHGVPDHPLPVLSFVAK--SSAANPPAAGPMIVHCSAGVGRTGTYIVLDAMLRQMRQRQ---SVNVYGFLRHIRQQRNY 876
Cdd:cd14608   165 PDFGVPESPASFLNFLFKvrESGSLSPEHGPVVVHCSAGIGRSGTFCLADTCLLLMDKRKdpsSVDIKKVLLEMRKFRMG 244
                         250       260
                  ....*....|....*....|....*...
gi 998470296  877 LVQTEEQYVFIHDALLEAID--SGDTEV 902
Cdd:cd14608   245 LIQTADQLRFSYLAVIEGAKfiMGDSSV 272
R-PTPc-A-E-2 cd14552
catalytic domain of receptor-type tyrosine-protein phosphatase A and E, repeat 2; ...
688-891 8.41e-57

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: 195.18  E-value: 8.41e-57
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 998470296  688 YINANYIDGYHKSRAFIGTQGPLPATFDDYWRMVWEQRVCIIIMITNLVERGRRKCDMYWPKEGTETYGIIQVKLVQEIV 767
Cdd:cd14552     1 YINASFIDGYRQKDAYIATQGPLDHTVEDFWRMIWEWKSCSIVMLTEIKERSQNKCAQYWPEDGSVSSGDITVELKDQTD 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 998470296  768 MATYTIRTFAIKNikvkKKQASERTVYQYHYTNWPDHGVPDHPLPVLSFVAKSSAANPPAA-GPMIVHCSAGVGRTGTYI 846
Cdd:cd14552    81 YEDYTLRDFLVTK----GKGGSTRTVRQFHFHGWPEVGIPDNGKGMIDLIAAVQKQQQQSGnHPITVHCSAGAGRTGTFC 156
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*
gi 998470296  847 VLDAMLRQMRQRQSVNVYGFLRHIRQQRNYLVQTEEQYVFIHDAL 891
Cdd:cd14552   157 ALSTVLERVKAEGVLDVFQVVKSLRLQRPHMVQTLEQYEFCYKVV 201
R-PTPc-R cd14611
catalytic domain of receptor-type tyrosine-protein phosphatase R; Receptor-type ...
660-888 2.71e-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: 194.75  E-value: 2.71e-56
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 998470296  660 KNRYINIVAYDHTRVILKPIPGQKKSSDYINANYIDGYH-KSRAFIGTQGPLPATFDDYWRMVWEQRVCIIIMITNLVER 738
Cdd:cd14611     2 KNRYKTILPNPHSRVCLKPKNSNDSLSTYINANYIRGYGgKEKAFIATQGPMINTVNDFWQMVWQEDSPVIVMITKLKEK 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 998470296  739 GRrKCDMYWPkEGTETYGIIQVKLVQEIVMATYTIRTFAIKNikvkkkQASERTVYQYHYTNWPDHGVPDHPLPVLSFV- 817
Cdd:cd14611    82 NE-KCVLYWP-EKRGIYGKVEVLVNSVKECDNYTIRNLTLKQ------GSQSRSVKHYWYTSWPDHKTPDSAQPLLQLMl 153
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 998470296  818 -AKSSAANPPAAGPMIVHCSAGVGRTGTYIVLDAMLRQMRQRQSVNVYGFLRHIRQQRNYLVQTEEQYVFIH 888
Cdd:cd14611   154 dVEEDRLASPGRGPVVVHCSAGIGRTGCFIATTIGCQQLKEEGVVDVLSIVCQLRVDRGGMVQTSEQYEFVH 225
R-PTP-N-N2 cd14546
PTP-like domain of receptor-type tyrosine-protein phosphatase-like N and N2; Receptor-type ...
688-896 3.25e-56

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: 193.81  E-value: 3.25e-56
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 998470296  688 YINANYI-DGYHKSRAFIGTQGPLPATFDDYWRMVWEQRVCIIIMITNLVERGRRKCDMYWPKEGTETYGIIQVKLVQE- 765
Cdd:cd14546     1 YINASTIyDHDPRNPAYIATQGPLPHTIADFWQMIWEQGCVVIVMLTRLQENGVKQCARYWPEEGSEVYHIYEVHLVSEh 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 998470296  766 IVMATYTIRTFAIKNIkvkkkQASE-RTVYQYHYTNWPDHGVPDHPLPVLSFVAKSSAANPPAAGPMIVHCSAGVGRTGT 844
Cdd:cd14546    81 IWCDDYLVRSFYLKNL-----QTSEtRTVTQFHFLSWPDEGIPASAKPLLEFRRKVNKSYRGRSCPIVVHCSDGAGRTGT 155
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 998470296  845 YIVLDAML-RQMRQRQSVNVYGFLRHIRQQRNYLVQTEEQYVFIHDALLEAID 896
Cdd:cd14546   156 YILIDMVLnRMAKGAKEIDIAATLEHLRDQRPGMVKTKDQFEFVLTAVAEEVN 208
PTPc-N13 cd14597
catalytic domain of tyrosine-protein phosphatase non-receptor type 13; Tyrosine-protein ...
656-892 5.87e-56

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: 194.28  E-value: 5.87e-56
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 998470296  656 ENKPKNRYINIVAYDHTRVILkpipGQKksSDYINANYIDGYHKSRAF--IGTQGPLPATFDDYWRMVWEQRVCIIIMIT 733
Cdd:cd14597     2 ENRKKNRYKNILPYDTTRVPL----GDE--GGYINASFIKMPVGDEEFvyIACQGPLPTTVADFWQMVWEQKSTVIAMMT 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 998470296  734 NLVERGRRKCDMYWPKEGTETYGI---IQVKLVQeivmaTYTIRTFAIKNIKVKKKQASE-RTVYQYHYTNWPDHGVPDH 809
Cdd:cd14597    76 QEVEGGKIKCQRYWPEILGKTTMVdnrLQLTLVR-----MQQLKNFVIRVLELEDIQTREvRHITHLNFTAWPDHDTPSQ 150
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 998470296  810 PLPVLSFVakSSAANPPAAGPMIVHCSAGVGRTGTYIVLDAMLRQMRQRQSVNVYGFLRHIRQQRNYLVQTEEQYVFIHD 889
Cdd:cd14597   151 PEQLLTFI--SYMRHIHKSGPIITHCSAGIGRSGTLICIDVVLGLISKDLDFDISDIVRTMRLQRHGMVQTEDQYIFCYQ 228

                  ...
gi 998470296  890 ALL 892
Cdd:cd14597   229 VIL 231
PTPc-N3 cd14600
catalytic domain of tyrosine-protein phosphatase non-receptor type 3; Tyrosine-protein ...
645-892 6.12e-56

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: 195.45  E-value: 6.12e-56
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 998470296  645 PDLTSSYSQLNENKPKNRYINIVAYDHTRVILKpipgqkKSSDYINANYID----GYHKSRAFIGTQGPLPATFDDYWRM 720
Cdd:cd14600    28 PGLAITCAKLPQNMDKNRYKDVLPYDATRVVLQ------GNEDYINASYVNmeipSANIVNKYIATQGPLPHTCAQFWQV 101
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 998470296  721 VWEQRVCIIIMITNLVERGRRKCDMYWPK-EGTETYGIIQVKLVQEIVMATYTIRTFAIKNIKVkkkqASERTVYQYHYT 799
Cdd:cd14600   102 VWEQKLSLIVMLTTLTERGRTKCHQYWPDpPDVMEYGGFRVQCHSEDCTIAYVFREMLLTNTQT----GEERTVTHLQYV 177
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 998470296  800 NWPDHGVPDHPLPVLSFVaKSSAANPPAAGPMIVHCSAGVGRTGTYIVLDAMLRQMRQRQSVNVYGFLRHIRQQRNYLVQ 879
Cdd:cd14600   178 AWPDHGVPDDSSDFLEFV-NYVRSKRVENEPVLVHCSAGIGRTGVLVTMETAMCLTERNQPVYPLDIVRKMRDQRAMMVQ 256
                         250
                  ....*....|...
gi 998470296  880 TEEQYVFIHDALL 892
Cdd:cd14600   257 TSSQYKFVCEAIL 269
R-PTP-Z-2 cd17669
catalytic domain of receptor-type tyrosine-protein phosphatase Z, repeat 2; Receptor-type ...
989-1198 2.83e-55

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: 190.98  E-value: 2.83e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 998470296  989 YINATFLQGFNRLREFIVTQHPLMDTMADFWQMVWDHNSQTIVVLSVVDEKEHPQF--WPDTDEEQDYGSFKVKPTGESV 1066
Cdd:cd17669     1 YINASYIMGYYQSNEFIITQHPLLHTIKDFWRMIWDHNAQLIVMLPDGQNMAEDEFvyWPNKDEPINCETFKVTLIAEEH 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 998470296 1067 APPVAEEKgalmpgegggLPSRDFILQSTQDDYELACRLLLCPGWPQSCSPLAKAFELVKEVgARQERDQNGPVVIVDRY 1146
Cdd:cd17669    81 KCLSNEEK----------LIIQDFILEATQDDYVLEVRHFQCPKWPNPDSPISKTFELISII-KEEAANRDGPMIVHDEH 149
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 998470296 1147 GGTEAATFCCLSALYRQLEREKCVDVYMYAKLYHMRRPGIWKSQDDFLFLYR 1198
Cdd:cd17669   150 GGVTAGTFCALTTLMHQLEKENSVDVYQVAKMINLMRPGVFTDIEQYQFLYK 201
PTPc-N21_14 cd14540
catalytic domain of tyrosine-protein phosphatase non-receptor type 21 and type 14; ...
688-893 3.83e-55

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: 191.13  E-value: 3.83e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 998470296  688 YINANYIDGY--HKSRAFIGTQGPLPATFDDYWRMVWEQRVCIIIMITNLVERGRRKCDMYWPKEG----TETYGIIQVK 761
Cdd:cd14540     1 YINASHITATvgGKQRFYIAAQGPLQNTVGDFWQMVWEQGVYLVVMVTAEEEGGREKCFRYWPTLGgehdALTFGEYKVS 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 998470296  762 LVQEIVMATYTIRTFAIKNIKVKKkqasERTVYQYHYTNWPDHGVPDHPLPVLSFVAK-----------SSAANPPAagP 830
Cdd:cd14540    81 TKFSVSSGCYTTTGLRVKHTLSGQ----SRTVWHLQYTDWPDHGCPEDVSGFLDFLEEinsvrrhtnqdVAGHNRNP--P 154
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 998470296  831 MIVHCSAGVGRTGTYIVLDAMLRQMRQRQSVNVYGFLRHIRQQRNYLVQTEEQYVFIHDALLE 893
Cdd:cd14540   155 TLVHCSAGVGRTGVVILADLMLYCLDHNEELDIPRVLALLRHQRMLLVQTLAQYKFVYNVLIQ 217
PTPc smart00194
Protein tyrosine phosphatase, catalytic domain;
933-1198 5.18e-55

Protein tyrosine phosphatase, catalytic domain;


Pssm-ID: 214550 [Multi-domain]  Cd Length: 259  Bit Score: 192.49  E-value: 5.18e-55
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 998470296    933 LLERQFKLVTMFKAKDFNVVSAVKPCNKAKNRSLNLIPIESHRVHITPKPGiDGSDYINATFLQGFNRLREFIVTQHPLM 1012
Cdd:smart00194    1 GLEEEFEKLDRLKPDDESCTVAAFPENRDKNRYKDVLPYDHTRVKLKPPPG-EGSDYINASYIDGPNGPKAYIATQGPLP 79
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 998470296   1013 DTMADFWQMVWDHNSQTIVVLSVVDEKEH---PQFWPDT-DEEQDYGSFKVKPTGESVAPpvaeekgalmpgeggGLPSR 1088
Cdd:smart00194   80 STVEDFWRMVWEQKVTVIVMLTELVEKGRekcAQYWPDEeGEPLTYGDITVTLKSVEKVD---------------DYTIR 144
                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 998470296   1089 DFILQSTQDDYELACRLLLCPGWPQSCSPL-AKAF-ELVKEVGARQErDQNGPVVIVDRYGGTEAATFCCLSALYRQLER 1166
Cdd:smart00194  145 TLEVTNTGCSETRTVTHYHYTNWPDHGVPEsPESIlDLIRAVRKSQS-TSTGPIVVHCSAGVGRTGTFIAIDILLQQLEA 223
                           250       260       270
                    ....*....|....*....|....*....|..
gi 998470296   1167 EKCVDVYMYAKLYHMRRPGIWKSQDDFLFLYR 1198
Cdd:smart00194  224 GKEVDIFEIVKELRSQRPGMVQTEEQYIFLYR 255
PTPc-N2 cd14607
catalytic domain of tyrosine-protein phosphatase non-receptor type 2; Tyrosine-protein ...
645-891 2.02e-54

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: 190.56  E-value: 2.02e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 998470296  645 PDLTSSYSQLNENKPKNRYINIVAYDHTRVILkpipgQKKSSDYINANYIDGYHKSRAFIGTQGPLPATFDDYWRMVWEQ 724
Cdd:cd14607    12 HDYPHRVAKYPENRNRNRYRDVSPYDHSRVKL-----QNTENDYINASLVVIEEAQRSYILTQGPLPNTCCHFWLMVWQQ 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 998470296  725 RVCIIIMITNLVERGRRKCDMYWPKEGTETYGI----IQVKLVQEIVMATYTIRTFAIKNIkvkkKQASERTVYQYHYTN 800
Cdd:cd14607    87 KTKAVVMLNRIVEKDSVKCAQYWPTDEEEVLSFketgFSVKLLSEDVKSYYTVHLLQLENI----NSGETRTISHFHYTT 162
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 998470296  801 WPDHGVPDHPLPVLSFVAK--SSAANPPAAGPMIVHCSAGVGRTGTYIVLDAMLRQMRQRQ--SVNVYGFLRHIRQQRNY 876
Cdd:cd14607   163 WPDFGVPESPASFLNFLFKvrESGSLSPEHGPAVVHCSAGIGRSGTFSLVDTCLVLMEKKDpdSVDIKQVLLDMRKYRMG 242
                         250
                  ....*....|....*
gi 998470296  877 LVQTEEQYVFIHDAL 891
Cdd:cd14607   243 LIQTPDQLRFSYMAV 257
PTPc-N14 cd14599
catalytic domain of tyrosine-protein phosphatase non-receptor type 14; Tyrosine-protein ...
635-893 2.87e-54

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: 191.36  E-value: 2.87e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 998470296  635 EYETFQHcTDPDLTSSYSQLNENKPKNRYINIVAYDHTRVILkpIPGQKKSSDYINANYI------DGYHksraFIGTQG 708
Cdd:cd14599    17 EYEQIPK-KKADGVFTTATLPENAERNRIREVVPYEENRVEL--VPTKENNTGYINASHIkvtvggEEWH----YIATQG 89
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 998470296  709 PLPATFDDYWRMVWEQRVCIIIMITNLVERGRRKCDMYWPKEGT----ETYGIIQVklvqeivmaTYTIRT----FAIKN 780
Cdd:cd14599    90 PLPHTCHDFWQMVWEQGVNVIAMVTAEEEGGRSKSHRYWPKLGSkhssATYGKFKV---------TTKFRTdsgcYATTG 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 998470296  781 IKVKKK-QASERTVYQYHYTNWPDHGVPDHPLPVLSFVAK--------------SSAANPPaagpMIVHCSAGVGRTGTY 845
Cdd:cd14599   161 LKVKHLlSGQERTVWHLQYTDWPDHGCPEEVQGFLSYLEEiqsvrrhtnsmldsTKNCNPP----IVVHCSAGVGRTGVV 236
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*...
gi 998470296  846 IVLDAMLRQMRQRQSVNVYGFLRHIRQQRNYLVQTEEQYVFIHDALLE 893
Cdd:cd14599   237 ILTELMIGCLEHNEKVEVPVMLRHLREQRMFMIQTIAQYKFVYQVLIQ 284
Y_phosphatase pfam00102
Protein-tyrosine phosphatase;
959-1198 2.97e-54

Protein-tyrosine phosphatase;


Pssm-ID: 459674 [Multi-domain]  Cd Length: 234  Bit Score: 189.38  E-value: 2.97e-54
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 998470296   959 NKAKNRSLNLIPIESHRVHITPKPGidGSDYINATFLQGFNRLREFIVTQHPLMDTMADFWQMVWDHNSQTIVVLSVVDE 1038
Cdd:pfam00102    1 NLEKNRYKDVLPYDHTRVKLTGDPG--PSDYINASYIDGYKKPKKYIATQGPLPNTVEDFWRMVWEEKVTIIVMLTELEE 78
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 998470296  1039 KEH---PQFWPDTDEE-QDYGSFKVKPTGEsvappVAEEKGALMpgeggglpsRDFILQSTQDDYELACRLLLCPGWPQS 1114
Cdd:pfam00102   79 KGRekcAQYWPEEEGEsLEYGDFTVTLKKE-----KEDEKDYTV---------RTLEVSNGGSEETRTVKHFHYTGWPDH 144
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 998470296  1115 CSPLAKA--FELVKEVGARQERDQNGPVVIVDRYGGTEAATFCCLSALYRQLEREKCVDVYMYAKLYHMRRPGIWKSQDD 1192
Cdd:pfam00102  145 GVPESPNslLDLLRKVRKSSLDGRSGPIVVHCSAGIGRTGTFIAIDIALQQLEAEGEVDIFQIVKELRSQRPGMVQTLEQ 224

                   ....*.
gi 998470296  1193 FLFLYR 1198
Cdd:pfam00102  225 YIFLYD 230
R-PTPc-E-2 cd14622
catalytic domain of receptor-type tyrosine-protein phosphatase E, repeat 2; Receptor-type ...
687-888 6.99e-51

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: 178.66  E-value: 6.99e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 998470296  687 DYINANYIDGYHKSRAFIGTQGPLPATFDDYWRMVWEQRVCIIIMITNLVERGRRKCDMYWPKEGTETYGIIQVKLVQEI 766
Cdd:cd14622     1 DYINASFIDGYRQKDYFIATQGPLAHTVEDFWRMVWEWKCHTIVMLTELQEREQEKCVQYWPSEGSVTHGEITIEIKNDT 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 998470296  767 VMATYTIRTFAIKNIKVKKKqaseRTVYQYHYTNWPDHGVPDHPLPVLSFVAKSSAANPPAAG-PMIVHCSAGVGRTGTY 845
Cdd:cd14622    81 LLETISIRDFLVTYNQEKQT----RLVRQFHFHGWPEIGIPAEGKGMIDLIAAVQKQQQQTGNhPIVVHCSAGAGRTGTF 156
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|...
gi 998470296  846 IVLDAMLRQMRQRQSVNVYGFLRHIRQQRNYLVQTEEQYVFIH 888
Cdd:cd14622   157 IALSNILERVKAEGLLDVFQTVKSLRLQRPHMVQTLEQYEFCY 199
PHA02738 PHA02738
hypothetical protein; Provisional
650-902 1.26e-50

hypothetical protein; Provisional


Pssm-ID: 222923 [Multi-domain]  Cd Length: 320  Bit Score: 182.05  E-value: 1.26e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 998470296  650 SYSQLNENKPKNRYINIVAYDHTRVILkpiPGQKKSSDYINANYIDGYHKSRAFIGTQGPLPATFDDYWRMVWEQRVCII 729
Cdd:PHA02738   42 TFNAEKKNRKLNRYLDAVCFDHSRVIL---PAERNRGDYINANYVDGFEYKKKFICGQAPTRQTCYDFYRMLWMEHVQII 118
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 998470296  730 IMITNLVERGRRKCDMYWP--KEGTETYGIIQVKLVQEIVMATYTIRTfaiknIKVKKKQASERTVYQYHYTNWPDHGVP 807
Cdd:PHA02738  119 VMLCKKKENGREKCFPYWSdvEQGSIRFGKFKITTTQVETHPHYVKST-----LLLTDGTSATQTVTHFNFTAWPDHDVP 193
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 998470296  808 DHPLPVLSFV------AKSSAAN----------PPaagPMIVHCSAGVGRTGTYIVLDAMLRQMRQRQSVNVYGFLRHIR 871
Cdd:PHA02738  194 KNTSEFLNFVlevrqcQKELAQEslqighnrlqPP---PIVVHCNAGLGRTPCYCVVDISISRFDACATVSIPSIVSSIR 270
                         250       260       270
                  ....*....|....*....|....*....|.
gi 998470296  872 QQRNYLVQTEEQYVFIHDALLEAIDSGDTEV 902
Cdd:PHA02738  271 NQRYYSLFIPFQYFFCYRAVKRYVNLTVNKV 301
R-PTP-C-2 cd14558
PTP-like domain of receptor-type tyrosine-protein phosphatase C, repeat 2; Receptor-type ...
688-889 1.85e-50

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


Pssm-ID: 350406 [Multi-domain]  Cd Length: 203  Bit Score: 177.20  E-value: 1.85e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 998470296  688 YINANYIDGYHKSRAFIGTQGPLPATFDDYWRMVWEQRVCIIIMITNLVERGRRKCDMYWPkEGTETYGIIQVKLVQEIV 767
Cdd:cd14558     1 YINASFIDGYWGPKSLIATQGPLPDTIADFWQMIFQKKVKVIVMLTELKEGDQEQCAQYWG-DEKKTYGDIEVELKDTEK 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 998470296  768 MATYTIRTFAIKNIKVKKkqasERTVYQYHYTNWPDHGVPDHPLPVLSFV------AKSSAANPPAAGPMIVHCSAGVGR 841
Cdd:cd14558    80 SPTYTVRVFEITHLKRKD----SRTVYQYQYHKWKGEELPEKPKDLVDMIksikqkLPYKNSKHGRSVPIVVHCSDGSSR 155
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*...
gi 998470296  842 TGTYIVLDAMLRQMRQRQSVNVYGFLRHIRQQRNYLVQTEEQYVFIHD 889
Cdd:cd14558   156 TGIFCALWNLLESAETEKVVDVFQVVKALRKQRPGMVSTLEQYQFLYD 203
PTPc-N4 cd14601
catalytic domain of tyrosine-protein phosphatase non-receptor type 4; Tyrosine-protein ...
687-896 3.14e-49

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: 173.98  E-value: 3.14e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 998470296  687 DYINANYIDGYHKS----RAFIGTQGPLPATFDDYWRMVWEQRVCIIIMITNLVERGRRKCDMYWPK-EGTETYGIIQVK 761
Cdd:cd14601     1 DYINANYINMEIPSssiiNRYIACQGPLPNTCSDFWQMTWEQGSSMVVMLTTQVERGRVKCHQYWPEpSGSSSYGGFQVT 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 998470296  762 LVQEIVMATYTIRTFAIKNIKVKKkqasERTVYQYHYTNWPDHGVPDHPLPVLSFVAKSSAANPPAAGPMIVHCSAGVGR 841
Cdd:cd14601    81 CHSEEGNPAYVFREMTLTNLEKNE----SRPLTQIQYIAWPDHGVPDDSSDFLDFVCLVRNKRAGKDEPVVVHCSAGIGR 156
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 998470296  842 TGTYIVLDAMLRQMRQRQSVNVYGFLRHIRQQRNYLVQTEEQYVFIHDALLEAID 896
Cdd:cd14601   157 TGVLITMETAMCLIECNQPVYPLDIVRTMRDQRAMMIQTPSQYRFVCEAILKVYE 211
PTPc-N20 cd14596
catalytic domain of tyrosine-protein phosphatase non-receptor type 20; Tyrosine-protein ...
688-895 6.37e-49

catalytic domain of tyrosine-protein phosphatase non-receptor type 20; Tyrosine-protein phosphatase non-receptor type 20 (PTPN20) belongs to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. Human PTPN20 is a widely expressed phosphatase with a dynamic subcellular distribution that is targeted to sites of actin polymerization.


Pssm-ID: 350444 [Multi-domain]  Cd Length: 207  Bit Score: 173.01  E-value: 6.37e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 998470296  688 YINANYIDGY--HKSRAFIGTQGPLPATFDDYWRMVWEQRVCIIIMITNLVERGRRKCDMYWPKEGTETYGI--IQVKLV 763
Cdd:cd14596     1 YINASYITMPvgEEELFYIATQGPLPSTIDDFWQMVWENRSDVIAMMTREVERGKVKCHRYWPETLQEPMELenYQLRLE 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 998470296  764 QEIVMATYTIRTFAIknikVKKKQASERTVYQYHYTNWPDHGVPDHPLPVLSFVAKSSAANppAAGPMIVHCSAGVGRTG 843
Cdd:cd14596    81 NYQALQYFIIRIIKL----VEKETGENRLIKHLQFTTWPDHGTPQSSDQLVKFICYMRKVH--NTGPIVVHCSAGIGRAG 154
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 998470296  844 TYIVLDAMLRQMRQRQSVNVYGFLRHIRQQRNYLVQTEEQYVFIHDALLEAI 895
Cdd:cd14596   155 VLICVDVLLSLIEKDLSFNIKDIVREMRQQRYGMIQTKDQYLFCYKVVLEVL 206
R-PTP-G-2 cd17670
PTP-like domain of receptor-type tyrosine-protein phosphatase G, repeat 2; Receptor-type ...
989-1198 8.83e-49

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: 172.56  E-value: 8.83e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 998470296  989 YINATFLQGFNRLREFIVTQHPLMDTMADFWQMVWDHNSQTIVVL---SVVDEKEHpQFWPDTDEEQDYGSFKVKPTGES 1065
Cdd:cd17670     1 YINASYIMGYYRSNEFIITQHPLPHTTKDFWRMIWDHNAQIIVMLpdnQGLAEDEF-VYWPSREESMNCEAFTVTLISKD 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 998470296 1066 VAPPVAEEKgalmpgegggLPSRDFILQSTQDDYELACRLLLCPGWPQSCSPLAKAFELVKeVGARQERDQNGPVVIVDR 1145
Cdd:cd17670    80 RLCLSNEEQ----------IIIHDFILEATQDDYVLEVRHFQCPKWPNPDAPISSTFELIN-VIKEEALTRDGPTIVHDE 148
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 998470296 1146 YGGTEAATFCCLSALYRQLEREKCVDVYMYAKLYHMRRPGIWKSQDDFLFLYR 1198
Cdd:cd17670   149 FGAVSAGTLCALTTLSQQLENENAVDVYQVAKMINLMRPGVFTDIEQYQFLYK 201
PHA02747 PHA02747
protein tyrosine phosphatase; Provisional
637-888 1.16e-46

protein tyrosine phosphatase; Provisional


Pssm-ID: 165114 [Multi-domain]  Cd Length: 312  Bit Score: 170.18  E-value: 1.16e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 998470296  637 ETFQHCTDP-DLTSSYSQLNENKPKNRYINIVAYDHTRVILKPipGQKKSSDYINANYIDGYHKSRAFIGTQGPLPATFD 715
Cdd:PHA02747   30 EHHQIILKPfDGLIANFEKPENQPKNRYWDIPCWDHNRVILDS--GGGSTSDYIHANWIDGFEDDKKFIATQGPFAETCA 107
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 998470296  716 DYWRMVWEQRVCIIIMIT-NLVERGRRKCDMYW-PKE-GTETYGIIQVKLVQEIVMATYTIRTFAIKNikvkKKQASERT 792
Cdd:PHA02747  108 DFWKAVWQEHCSIIVMLTpTKGTNGEEKCYQYWcLNEdGNIDMEDFRIETLKTSVRAKYILTLIEITD----KILKDSRK 183
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 998470296  793 VYQYHYTNWPDHGVP-DHP-----LPVLSFVAKSSAA--NPPAA--GPMIVHCSAGVGRTGTYIVLDAMLRQMRQRQSVN 862
Cdd:PHA02747  184 ISHFQCSEWFEDETPsDHPdfikfIKIIDINRKKSGKlfNPKDAllCPIVVHCSDGVGKTGIFCAVDICLNQLVKRKAIC 263
                         250       260
                  ....*....|....*....|....*.
gi 998470296  863 VYGFLRHIRQQRNYLVQTEEQYVFIH 888
Cdd:PHA02747  264 LAKTAEKIREQRHAGIMNFDDYLFIQ 289
PTP-N23 cd14539
PTP-like domain of tyrosine-protein phosphatase non-receptor type 23; Tyrosine-protein ...
688-889 2.11e-46

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


Pssm-ID: 350387 [Multi-domain]  Cd Length: 205  Bit Score: 165.63  E-value: 2.11e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 998470296  688 YINANYIDGYHKSRA-FIGTQGPLPATFDDYWRMVWEQRVCIIIMITNLVERGRRKCDMYWPKE--GTETYGIIQVKLVQ 764
Cdd:cd14539     1 YINASLIEDLTPYCPrFIATQAPLPGTAADFWLMVYEQQVSVIVMLVSEQENEKQKVHRYWPTErgQALVYGAITVSLQS 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 998470296  765 EIVMATYTIRTFAIKNikvkKKQASERTVYQYHYTNWPDHGVPDHPLPVLSF---VAKSSAANPPAAGPMIVHCSAGVGR 841
Cdd:cd14539    81 VRTTPTHVERIISIQH----KDTRLSRSVVHLQFTTWPELGLPDSPNPLLRFieeVHSHYLQQRSLQTPIVVHCSSGVGR 156
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*....
gi 998470296  842 TGTYIVLDAMLRQMRQ-RQSVNVYGFLRHIRQQRNYLVQTEEQYVFIHD 889
Cdd:cd14539   157 TGAFCLLYAAVQEIEAgNGIPDLPQLVRKMRQQRKYMLQEKEHLKFCYE 205
PHA02742 PHA02742
protein tyrosine phosphatase; Provisional
655-893 2.84e-46

protein tyrosine phosphatase; Provisional


Pssm-ID: 165109 [Multi-domain]  Cd Length: 303  Bit Score: 168.64  E-value: 2.84e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 998470296  655 NENKPKNRYINIVAYDHTRVILkpiPGQKKSSDYINANYIDGYHKSRAFIGTQGPLPATFDDYWRMVWEQRVCIIIMITN 734
Cdd:PHA02742   50 LKNMKKCRYPDAPCFDRNRVIL---KIEDGGDDFINASYVDGHNAKGRFICTQAPLEETALDFWQAIFQDQVRVIVMITK 126
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 998470296  735 LVERGRRKCDMYW-PKE-GTETYGIIQVKlvqeiVMATYTIRTFAIKNIKVKKKQ-ASERTVYQYHYTNWPDHGVPDHPL 811
Cdd:PHA02742  127 IMEDGKEACYPYWmPHErGKATHGEFKIK-----TKKIKSFRNYAVTNLCLTDTNtGASLDIKHFAYEDWPHGGLPRDPN 201
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 998470296  812 PVLSFV-----------AKSSAANPPAAGPMIVHCSAGVGRTGTYIVLDAMLRQMRQRQSVNVYGFLRHIRQQRNYLVQT 880
Cdd:PHA02742  202 KFLDFVlavreadlkadVDIKGENIVKEPPILVHCSAGLDRAGAFCAIDICISKYNERAIIPLLSIVRDLRKQRHNCLSL 281
                         250
                  ....*....|...
gi 998470296  881 EEQYVFIHDALLE 893
Cdd:PHA02742  282 PQQYIFCYFIVLI 294
PHA02746 PHA02746
protein tyrosine phosphatase; Provisional
648-895 1.64e-45

protein tyrosine phosphatase; Provisional


Pssm-ID: 165113 [Multi-domain]  Cd Length: 323  Bit Score: 167.13  E-value: 1.64e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 998470296  648 TSSYSQLNENKPKNRYINIVAYDHTRVILKP------------------IPGQKKSSDYINANYIDGYHKSRAFIGTQGP 709
Cdd:PHA02746   42 TTNHFLKKENLKKNRFHDIPCWDHSRVVINAheslkmfdvgdsdgkkieVTSEDNAENYIHANFVDGFKEANKFICAQGP 121
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 998470296  710 LPATFDDYWRMVWEQRVCIIIMITNlVERGRRKCDMYWPK-EGTE-TYGIIQVKLVQEIVMATYTIRTFAIKNikvkKKQ 787
Cdd:PHA02746  122 KEDTSEDFFKLISEHESQVIVSLTD-IDDDDEKCFELWTKeEDSElAFGRFVAKILDIIEELSFTKTRLMITD----KIS 196
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 998470296  788 ASERTVYQYHYTNWPDHGVPDHPLPVLSFVAK----------SSAANPPAAGPMIVHCSAGVGRTGTYIVLDAMLRQMRQ 857
Cdd:PHA02746  197 DTSREIHHFWFPDWPDNGIPTGMAEFLELINKvneeqaelikQADNDPQTLGPIVVHCSAGIGRAGTFCAIDNALEQLEK 276
                         250       260       270
                  ....*....|....*....|....*....|....*...
gi 998470296  858 RQSVNVYGFLRHIRQQRNYLVQTEEQYVFIHDALLEAI 895
Cdd:PHA02746  277 EKEVCLGEIVLKIRKQRHSSVFLPEQYAFCYKALKYAI 314
R-PTPc-typeIIb-2 cd14556
PTP domain of type IIb (or R2B) subfamily receptor-type tyrosine-protein phosphatases, repeat ...
688-889 5.45e-45

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: 161.42  E-value: 5.45e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 998470296  688 YINANYIDGYHKSRAFIGTQGPLPATFDDYWRMVWEQRVCIIIMItNLVERGRRKCDMYWPKEGTETYGIIQVKLVQEIV 767
Cdd:cd14556     1 YINAALLDSYKQPAAFIVTQHPLPNTVTDFWRLVYDYGCTSIVML-NQLDPKDQSCPQYWPDEGSGTYGPIQVEFVSTTI 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 998470296  768 MATYTIRTFAIKNIkvKKKQASERTVYQYHYTNWPDHG----VPDHPLPVLSFVAKSSAANppAAGPMIVHCSAGVGRTG 843
Cdd:cd14556    80 DEDVISRIFRLQNT--TRPQEGYRMVQQFQFLGWPRDRdtppSKRALLKLLSEVEKWQEQS--GEGPIVVHCLNGVGRSG 155
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*.
gi 998470296  844 TYIVLDAMLRQMRQRQSVNVYGFLRHIRQQRNYLVQTEEQYVFIHD 889
Cdd:cd14556   156 VFCAISSVCERIKVENVVDVFQAVKTLRNHRPNMVETEEQYKFCYD 201
PTPc_plant_PTP1 cd17658
protein tyrosine phosphatase 1 from Arabidopsis thaliana and similar plant PTPs; Arabidopsis ...
688-888 7.33e-45

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: 161.09  E-value: 7.33e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 998470296  688 YINANYI--DGYHKSRAFIGTQGPLPATFDDYWRMVWEQRVCIIIMITNLVERGRR-KCDMYWPKE--GTETYGIIQVKL 762
Cdd:cd17658     1 YINASLVetPASESLPKFIATQGPLPHTFEDFWEMVIQQRCPVIIMLTRLVDNYSTaKCADYFPAEenESREFGRISVTN 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 998470296  763 VQE-IVMATYTIRTFAIKNIKVkkkQASERTVYQYHYTNWPDHGVPDHPLPVLSFVAKSSAAnPPAAGPMIVHCSAGVGR 841
Cdd:cd17658    81 KKLkHSQHSITLRVLEVQYIES---EEPPLSVLHIQYPEWPDHGVPKDTRSVRELLKRLYGI-PPSAGPIVVHCSAGIGR 156
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*....
gi 998470296  842 TGTYIVLDAMLRQMRQ--RQSVNVYGFLRHIRQQRNYLVQTEEQYVFIH 888
Cdd:cd17658   157 TGAYCTIHNTIRRILEgdMSAVDLSKTVRKFRSQRIGMVQTQDQYIFCY 205
COG5599 COG5599
Protein tyrosine phosphatase [Signal transduction mechanisms];
651-887 4.23e-43

Protein tyrosine phosphatase [Signal transduction mechanisms];


Pssm-ID: 444335 [Multi-domain]  Cd Length: 282  Bit Score: 158.72  E-value: 4.23e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 998470296  651 YSQLNENKPKNRYINIVAYDHTRVilkpipgqKKSSDYINANYIDGYHKSRAfIGTQGPLPATFDDYWRMVWEQRVCIII 730
Cdd:COG5599    36 YLQNINGSPLNRFRDIQPYKETAL--------RANLGYLNANYIQVIGNHRY-IATQYPLEEQLEDFFQMLFDNNTPVLV 106
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 998470296  731 MITNLVERGRRKCDM--YWPKEGTETYGIIQVKLVQEIVMATytirTFAIKNIKVKKKQASE--RTVYQYHYTNWPDHGV 806
Cdd:COG5599   107 VLASDDEISKPKVKMpvYFRQDGEYGKYEVSSELTESIQLRD----GIEARTYVLTIKGTGQkkIEIPVLHVKNWPDHGA 182
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 998470296  807 PD----HPLpvLSFVAKSSAANPPAAGPMIVHCSAGVGRTGTYIVLDAMlRQMRQRQ---SVNVYGFLRHIRQQRNY-LV 878
Cdd:COG5599   183 ISaealKNL--ADLIDKKEKIKDPDKLLPVVHCRAGVGRTGTLIACLAL-SKSINALvqiTLSVEEIVIDMRTSRNGgMV 259

                  ....*....
gi 998470296  879 QTEEQYVFI 887
Cdd:COG5599   260 QTSEQLDVL 268
R-PTP-LAR-2 cd14554
PTP-like domain of the LAR family receptor-type tyrosine-protein phosphatases, repeat 2; The ...
957-1198 2.59e-42

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: 154.99  E-value: 2.59e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 998470296  957 PCNKAKNRSLNLIPIESHRVHITPKPGIDGSDYINATFLQGFNRLREFIVTQHPLMDTMADFWQMVWDHNSQTIVVLSVV 1036
Cdd:cd14554     4 PCNKFKNRLVNILPYESTRVCLQPIRGVEGSDYINASFIDGYRQRGAYIATQGPLAETTEDFWRMLWEHNSTIIVMLTKL 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 998470296 1037 DEKEHP---QFWPdTDEEQDYGSFKVKPTGESVAPPVAeekgalmpgeggglpSRDFILQSTQDDYELACRLLLCPGWPQ 1113
Cdd:cd14554    84 REMGREkchQYWP-AERSARYQYFVVDPMAEYNMPQYI---------------LREFKVTDARDGQSRTVRQFQFTDWPE 147
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 998470296 1114 SCSP-LAKAF-ELVKEV-GARQERDQNGPVVIVDRYGGTEAATFCCLSALYRQLEREKCVDVYMYAKLYHMRRPGIWKSQ 1190
Cdd:cd14554   148 QGVPkSGEGFiDFIGQVhKTKEQFGQEGPITVHCSAGVGRTGVFITLSIVLERMRYEGVVDVFQTVKLLRTQRPAMVQTE 227

                  ....*...
gi 998470296 1191 DDFLFLYR 1198
Cdd:cd14554   228 DQYQFCYR 235
PTPc-N21 cd14598
catalytic domain of tyrosine-protein phosphatase non-receptor type 21; Tyrosine-protein ...
688-893 1.60e-41

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: 152.05  E-value: 1.60e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 998470296  688 YINANYIDGY--HKSRAFIGTQGPLPATFDDYWRMVWEQRVCIIIMITNLVERGRRKCDMYWPKEG----TETYGIIQVk 761
Cdd:cd14598     1 YINASHIKVTvgGKEWDYIATQGPLQNTCQDFWQMVWEQGVAIIAMVTAEEEGGREKSFRYWPRLGsrhnTVTYGRFKI- 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 998470296  762 lvqeivmaTYTIRT----FAIKNIKVKK-KQASERTVYQYHYTNWPDHGVPDHPLPVLSFVAK--------SSAANPPAA 828
Cdd:cd14598    80 --------TTRFRTdsgcYATTGLKIKHlLTGQERTVWHLQYTDWPEHGCPEDLKGFLSYLEEiqsvrrhtNSTIDPKSP 151
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 998470296  829 G-PMIVHCSAGVGRTGTYIVLDAMLRQMRQRQSVNVYGFLRHIRQQRNYLVQTEEQYVFIHDALLE 893
Cdd:cd14598   152 NpPVLVHCSAGVGRTGVVILSEIMIACLEHNEMLDIPRVLDMLRQQRMMMVQTLSQYTFVYKVLIQ 217
R-PTP-D-2 cd14628
PTP-like domain of receptor-type tyrosine-protein phosphatase D, repeat 2; Receptor-type ...
900-1198 5.03e-41

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


Pssm-ID: 350476 [Multi-domain]  Cd Length: 292  Bit Score: 153.35  E-value: 5.03e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 998470296  900 TEVGVSQLSRYVQSLQTAQVATTGAGdnekswslLERQFKLVTMFKAKDFNVVSAVKPCNKAKNRSLNLIPIESHRVHIT 979
Cdd:cd14628     1 TEVPARNLYAYIQKLTQIETGENVTG--------MELEFKRLASSKAHTSRFISANLPCNKFKNRLVNIMPYESTRVCLQ 72
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 998470296  980 PKPGIDGSDYINATFLQGFNRLREFIVTQHPLMDTMADFWQMVWDHNSQTIVVLSVV----DEKEHpQFWPdTDEEQDYG 1055
Cdd:cd14628    73 PIRGVEGSDYINASFIDGYRQQKAYIATQGPLAETTEDFWRMLWEHNSTIVVMLTKLremgREKCH-QYWP-AERSARYQ 150
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 998470296 1056 SFKVKPTGESVAPPVAeekgalmpgeggglpSRDFILQSTQDDYELACRLLLCPGWPQSCSPLAKA--FELVKEVGARQE 1133
Cdd:cd14628   151 YFVVDPMAEYNMPQYI---------------LREFKVTDARDGQSRTVRQFQFTDWPEQGVPKSGEgfIDFIGQVHKTKE 215
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 998470296 1134 R-DQNGPVVIVDRYGGTEAATFCCLSALYRQLEREKCVDVYMYAKLYHMRRPGIWKSQDDFLFLYR 1198
Cdd:cd14628   216 QfGQDGPISVHCSAGVGRTGVFITLSIVLERMRYEGVVDIFQTVKMLRTQRPAMVQTEDQYQFCYR 281
PTPc cd00047
catalytic domain of protein tyrosine phosphatases; Protein tyrosine phosphatases (PTP, EC 3.1. ...
989-1198 1.17e-40

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: 148.97  E-value: 1.17e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 998470296  989 YINATFLQGFNRLREFIVTQHPLMDTMADFWQMVWDHNSQTIVVLSVVDEKEH---PQFWPD-TDEEQDYGSFKVKPTGE 1064
Cdd:cd00047     1 YINASYIDGYRGPKEYIATQGPLPNTVEDFWRMVWEQKVSVIVMLTNLVEKGRekcERYWPEeGGKPLEYGDITVTLVSE 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 998470296 1065 SVAPPVAEekgalmpgeggglpsRDFILQSTQDDYELACRLLLCPGW-----PQSCSPLAKAFELVKevgaRQERDQNGP 1139
Cdd:cd00047    81 EELSDYTI---------------RTLELSPKGCSESREVTHLHYTGWpdhgvPSSPEDLLALVRRVR----KEARKPNGP 141
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 998470296 1140 VVIVDRYGGTEAATFCCLSALYRQLEREKCVDVYMYAKLYHMRRPGIWKSQDDFLFLYR 1198
Cdd:cd00047   142 IVVHCSAGVGRTGTFIAIDILLERLEAEGEVDVFEIVKALRKQRPGMVQTLEQYEFIYE 200
PTPc_DSPc smart00012
Protein tyrosine phosphatase, catalytic domain, undefined specificity; Protein tyrosine ...
792-893 6.76e-40

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


Pssm-ID: 214469 [Multi-domain]  Cd Length: 105  Bit Score: 142.88  E-value: 6.76e-40
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 998470296    792 TVYQYHYTNWPDHGVPDHPLPVLSFVAKSSAANPPAA--GPMIVHCSAGVGRTGTYIVLDAMLRQMRQRQ-SVNVYGFLR 868
Cdd:smart00012    1 TVKHYHYTGWPDHGVPESPDSILELLRAVKKNLNQSEssGPVVVHCSAGVGRTGTFVAIDILLQQLEAEAgEVDIFDTVK 80
                            90       100
                    ....*....|....*....|....*
gi 998470296    869 HIRQQRNYLVQTEEQYVFIHDALLE 893
Cdd:smart00012   81 ELRSQRPGMVQTEEQYLFLYRALLE 105
PTPc_motif smart00404
Protein tyrosine phosphatase, catalytic domain motif;
792-893 6.76e-40

Protein tyrosine phosphatase, catalytic domain motif;


Pssm-ID: 214649 [Multi-domain]  Cd Length: 105  Bit Score: 142.88  E-value: 6.76e-40
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 998470296    792 TVYQYHYTNWPDHGVPDHPLPVLSFVAKSSAANPPAA--GPMIVHCSAGVGRTGTYIVLDAMLRQMRQRQ-SVNVYGFLR 868
Cdd:smart00404    1 TVKHYHYTGWPDHGVPESPDSILELLRAVKKNLNQSEssGPVVVHCSAGVGRTGTFVAIDILLQQLEAEAgEVDIFDTVK 80
                            90       100
                    ....*....|....*....|....*
gi 998470296    869 HIRQQRNYLVQTEEQYVFIHDALLE 893
Cdd:smart00404   81 ELRSQRPGMVQTEEQYLFLYRALLE 105
R-PTP-S-2 cd14627
PTP-like domain of receptor-type tyrosine-protein phosphatase S, repeat 2; Receptor-type ...
899-1198 1.56e-39

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: 148.73  E-value: 1.56e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 998470296  899 DTEVGVSQLSRYVQSLQTAQVATTGAGdnekswslLERQFKLVTMFKAKDFNVVSAVKPCNKAKNRSLNLIPIESHRVHI 978
Cdd:cd14627     1 NTEVPARNLYSYIQKLAQVEVGEHVTG--------MELEFKRLANSKAHTSRFISANLPCNKFKNRLVNIMPYETTRVCL 72
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 998470296  979 TPKPGIDGSDYINATFLQGFNRLREFIVTQHPLMDTMADFWQMVWDHNSQTIVVLSVV----DEKEHpQFWPdTDEEQDY 1054
Cdd:cd14627    73 QPIRGVEGSDYINASFIDGYRQQKAYIATQGPLAETTEDFWRMLWENNSTIVVMLTKLremgREKCH-QYWP-AERSARY 150
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 998470296 1055 GSFKVKPTGESVAPPVAeekgalmpgeggglpSRDFILQSTQDDYELACRLLLCPGWPQSCSPLAKA--FELVKEVGARQ 1132
Cdd:cd14627   151 QYFVVDPMAEYNMPQYI---------------LREFKVTDARDGQSRTVRQFQFTDWPEQGVPKSGEgfIDFIGQVHKTK 215
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 998470296 1133 ER-DQNGPVVIVDRYGGTEAATFCCLSALYRQLEREKCVDVYMYAKLYHMRRPGIWKSQDDFLFLYR 1198
Cdd:cd14627   216 EQfGQDGPISVHCSAGVGRTGVFITLSIVLERMRYEGVVDIFQTVKMLRTQRPAMVQTEDEYQFCYQ 282
R-PTP-F-2 cd14629
PTP-like domain of receptor-type tyrosine-protein phosphatase F, repeat 2; Receptor-type ...
900-1198 1.63e-38

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: 146.02  E-value: 1.63e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 998470296  900 TEVGVSQLSRYVQSLqtaqvattGAGDNEKSWSLLERQFKLVTMFKAKDFNVVSAVKPCNKAKNRSLNLIPIESHRVHIT 979
Cdd:cd14629     2 TEVPARNLYAHIQKL--------TQVPPGESVTAMELEFKLLANSKAHTSRFISANLPCNKFKNRLVNIMPYELTRVCLQ 73
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 998470296  980 PKPGIDGSDYINATFLQGFNRLREFIVTQHPLMDTMADFWQMVWDHNSQTIVVLSVV----DEKEHpQFWPdTDEEQDYG 1055
Cdd:cd14629    74 PIRGVEGSDYINASFIDGYRQQKAYIATQGPLAETTEDFWRMLWEHNSTIVVMLTKLremgREKCH-QYWP-AERSARYQ 151
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 998470296 1056 SFKVKPTGESVAPPVAeekgalmpgeggglpSRDFILQSTQDDYELACRLLLCPGWPQSCSP-LAKAF-ELVKEVGARQE 1133
Cdd:cd14629   152 YFVVDPMAEYNMPQYI---------------LREFKVTDARDGQSRTIRQFQFTDWPEQGVPkTGEGFiDFIGQVHKTKE 216
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 998470296 1134 R-DQNGPVVIVDRYGGTEAATFCCLSALYRQLEREKCVDVYMYAKLYHMRRPGIWKSQDDFLFLYR 1198
Cdd:cd14629   217 QfGQDGPITVHCSAGVGRTGVFITLSIVLERMRYEGVVDMFQTVKTLRTQRPAMVQTEDQYQLCYR 282
R-PTPc-typeIIb-2 cd14556
PTP domain of type IIb (or R2B) subfamily receptor-type tyrosine-protein phosphatases, repeat ...
989-1197 1.31e-36

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: 137.15  E-value: 1.31e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 998470296  989 YINATFLQGFNRLREFIVTQHPLMDTMADFWQMVWDHNSQTIVVLSVVDEKEH--PQFWPDtDEEQDYGSFKVKPTGESV 1066
Cdd:cd14556     1 YINAALLDSYKQPAAFIVTQHPLPNTVTDFWRLVYDYGCTSIVMLNQLDPKDQscPQYWPD-EGSGTYGPIQVEFVSTTI 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 998470296 1067 APPVAeekgalmpgeggglpSRDFILQST---QDDYELAcRLLLCPGWP--QSCSPLAKAF-ELVKEVGARQERDQNGPV 1140
Cdd:cd14556    80 DEDVI---------------SRIFRLQNTtrpQEGYRMV-QQFQFLGWPrdRDTPPSKRALlKLLSEVEKWQEQSGEGPI 143
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 998470296 1141 VIVDRYGGTEAATFCCLSALYRQLEREKCVDVYMYAKLYHMRRPGIWKSQDDFLFLY 1197
Cdd:cd14556   144 VVHCLNGVGRSGVFCAISSVCERIKVENVVDVFQAVKTLRNHRPNMVETEEQYKFCY 200
R-PTPc-A-2 cd14623
catalytic domain of receptor-type tyrosine-protein phosphatase A, repeat 2; Receptor-type ...
964-1198 5.65e-30

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: 119.38  E-value: 5.65e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 998470296  964 RSLNLIPIESHRVHITPKPGIDGSDYINATFLQGFNRLREFIVTQHPLMDTMADFWQMVWDHNSQTIVVLSVVDEKEH-- 1041
Cdd:cd14623     1 RVLQIIPYEFNRVIIPVKRGEENTDYVNASFIDGYRQKDSYIASQGPLQHTIEDFWRMIWEWKSCSIVMLTELEERGQek 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 998470296 1042 -PQFWPdTDEEQDYGSFKVKPTGESvappvaeekgalmpgEGGGLPSRDFILQSTQDDYELACRLLLCPGWPQSCSPL-- 1118
Cdd:cd14623    81 cAQYWP-SDGSVSYGDITIELKKEE---------------ECESYTVRDLLVTNTRENKSRQIRQFHFHGWPEVGIPSdg 144
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 998470296 1119 AKAFELVKEVGARQERDQNGPVVIVDRYGGTEAATFCCLSALYRQLEREKCVDVYMYAKLYHMRRPGIWKSQDDFLFLYR 1198
Cdd:cd14623   145 KGMINIIAAVQKQQQQSGNHPITVHCSAGAGRTGTFCALSTVLERVKAEGILDVFQTVKSLRLQRPHMVQTLEQYEFCYK 224
R3-PTPc cd14548
catalytic domain of R3 subfamily receptor-type tyrosine-protein phosphatases and similar ...
964-1197 1.06e-29

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: 118.23  E-value: 1.06e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 998470296  964 RSLNLIPIESHRVHITPKPGIDGSDYINATFLQGFNRLREFIVTQHPLMDTMADFWQMVWDHNSQTIVVLSVVDEK---- 1039
Cdd:cd14548     1 RYTNILPYDHSRVKLIPINEEEGSDYINANYIPGYNSPREFIATQGPLPGTKDDFWRMVWEQNSHTIVMLTQCMEKgrvk 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 998470296 1040 -EHpqFWPDTDEEQDYGSFKVKPTGESVAPPVAeekgalmpgeggglpSRDFILQSTQDDYELA-CRLLLCP--GWPQSC 1115
Cdd:cd14548    81 cDH--YWPFDQDPVYYGDITVTMLSESVLPDWT---------------IREFKLERGDEVRSVRqFHFTAWPdhGVPEAP 143
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 998470296 1116 SPLAKAFELVkevgaRQERDQN-GPVVIVDRYGGTEAATFCCLSALYRQLEREKCVDVymYAKLYHMR--RPGIWKSQDD 1192
Cdd:cd14548   144 DSLLRFVRLV-----RDYIKQEkGPTIVHCSAGVGRTGTFIALDRLLQQIESEDYVDI--FGIVYDLRkhRPLMVQTEAQ 216

                  ....*
gi 998470296 1193 FLFLY 1197
Cdd:cd14548   217 YIFLH 221
R-PTPc-T-2 cd14634
PTP domain of receptor-type tyrosine-protein phosphatase T, repeat 2; Receptor-type ...
688-893 1.32e-29

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


Pssm-ID: 350482 [Multi-domain]  Cd Length: 206  Bit Score: 117.43  E-value: 1.32e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 998470296  688 YINANYIDGYHKSRAFIGTQGPLPATFDDYWRMVWEQRVCIIIMITNLveRGRRKCDMYWPKEGTETYGIIQVKLVQEIV 767
Cdd:cd14634     1 YINAALMDSHKQPAAFIVTQHPLPNTVADFWRLVFDYNCSSVVMLNEM--DAAQLCMQYWPEKTSCCYGPIQVEFVSADI 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 998470296  768 MATYTIRTFAIKNIKvkKKQASERTVYQYHYTNWPDHgvPDHP------LPVLSFVAKSSAANPPAAGPMIVHCSAGVGR 841
Cdd:cd14634    79 DEDIISRIFRICNMA--RPQDGYRIVQHLQYIGWPAY--RDTPpskrsiLKVVRRLEKWQEQYDGREGRTVVHCLNGGGR 154
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 998470296  842 TGTYIVLDAMLRQMRQRQSVNVYGFLRHIRQQRNYLVQTEEQYVFIHDALLE 893
Cdd:cd14634   155 SGTFCAICSVCEMIQQQNIIDVFHTVKTLRNNKSNMVETLEQYKFVYEVALE 206
R-PTPc-LAR-1 cd14553
catalytic domain of LAR family receptor-type tyrosine-protein phosphatases, repeat 1; The LAR ...
957-1197 7.72e-29

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: 116.34  E-value: 7.72e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 998470296  957 PCNKAKNRSLNLIPIESHRVHITPKPGIDGSDYINATFLQGFNRLREFIVTQHPLMDTMADFWQMVWDHNSQTIVVLSVV 1036
Cdd:cd14553     1 EVNKPKNRYANVIAYDHSRVILQPIEGVPGSDYINANYCDGYRKQNAYIATQGPLPETFGDFWRMVWEQRSATIVMMTKL 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 998470296 1037 DEKEH---PQFWPDTDEEQdYGSFKVKPTgESVappvaeekgalmpgEGGGLPSRDFIL--QSTQDDYELacRLLLCPGW 1111
Cdd:cd14553    81 EERSRvkcDQYWPTRGTET-YGLIQVTLL-DTV--------------ELATYTVRTFALhkNGSSEKREV--RQFQFTAW 142
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 998470296 1112 -----PQSCSPLakaFELVKEVGARQERDQnGPVVIVDRYGGTEAATFCCLSALYRQLEREKCVDVYMYAKLYHMRRPGI 1186
Cdd:cd14553   143 pdhgvPEHPTPF---LAFLRRVKACNPPDA-GPIVVHCSAGVGRTGCFIVIDSMLERIKHEKTVDIYGHVTCLRAQRNYM 218
                         250
                  ....*....|.
gi 998470296 1187 WKSQDDFLFLY 1197
Cdd:cd14553   219 VQTEDQYIFIH 229
R-PTPc-K-2 cd14636
PTP domain of receptor-type tyrosine-protein phosphatase K, repeat 2; Receptor-type ...
688-893 2.15e-28

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: 113.97  E-value: 2.15e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 998470296  688 YINANYIDGYHKSRAFIGTQGPLPATFDDYWRMVWEQRVCIIIMITNL-VERGrrkCDMYWPKEGTETYGIIQVKLVQEI 766
Cdd:cd14636     1 YINAALMDSYRQPAAFIVTQHPLPNTVKDFWRLVYDYGCTSIVMLNEVdLAQG---CPQYWPEEGMLRYGPIQVECMSCS 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 998470296  767 VMATYTIRTFAIKNIkvKKKQASERTVYQYHYTNWPDH-GVPDHPLPVLSF---VAKSSAANPPAAGPMIVHCSAGVGRT 842
Cdd:cd14636    78 MDCDVISRIFRICNL--TRPQEGYLMVQQFQYLGWASHrEVPGSKRSFLKLilqVEKWQEECDEGEGRTIIHCLNGGGRS 155
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|.
gi 998470296  843 GTYIVLDAMLRQMRQRQSVNVYGFLRHIRQQRNYLVQTEEQYVFIHDALLE 893
Cdd:cd14636   156 GMFCAISIVCEMIKRQNVVDVFHAVKTLRNSKPNMVETPEQYRFCYDVALE 206
R-PTPc-U-2 cd14637
PTP domain of receptor-type tyrosine-protein phosphatase U, repeat 2; Receptor-type ...
688-893 5.22e-28

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: 112.69  E-value: 5.22e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 998470296  688 YINANYIDGYHKSRAFIGTQGPLPATFDDYWRMVWEQRVCIIIMITNLVERGRR-KCDMYWPKEGTETYGIIQVKLVQEI 766
Cdd:cd14637     1 YINAALTDSYTRSAAFIVTLHPLQNTTTDFWRLVYDYGCTSVVMLNQLNQSNSAwPCLQYWPEPGLQQYGPMEVEFVSGS 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 998470296  767 VMATYTIRTFAIKNIkvKKKQASERTVYQYHYTNW-PDHGVPDHP---LPVLSFVAKSSAANppAAGPMIVHCSAGVGRT 842
Cdd:cd14637    81 ADEDIVTRLFRVQNI--TRLQEGHLMVRHFQFLRWsAYRDTPDSKkafLHLLASVEKWQRES--GEGRTVVHCLNGGGRS 156
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|.
gi 998470296  843 GTYIVLDAMLRQMRQRQSVNVYGFLRHIRQQRNYLVQTEEQYVFIHDALLE 893
Cdd:cd14637   157 GTYCASAMILEMIRCHNIVDVFYAVKTLRNYKPNMVETLEQYRFCYEIALE 207
R-PTPc-A-E-2 cd14552
catalytic domain of receptor-type tyrosine-protein phosphatase A and E, repeat 2; ...
989-1198 2.24e-27

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: 110.82  E-value: 2.24e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 998470296  989 YINATFLQGFNRLREFIVTQHPLMDTMADFWQMVWDHNSQTIVVLSVVDEKEH---PQFWPdTDEEQDYGSFKVKPTGES 1065
Cdd:cd14552     1 YINASFIDGYRQKDAYIATQGPLDHTVEDFWRMIWEWKSCSIVMLTEIKERSQnkcAQYWP-EDGSVSSGDITVELKDQT 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 998470296 1066 vappvaeekgalmpgEGGGLPSRDFILQSTQDDYELACRLLLCPGWPQSCSPL-AKAF-ELVKEVGARQERDQNGPVVIV 1143
Cdd:cd14552    80 ---------------DYEDYTLRDFLVTKGKGGSTRTVRQFHFHGWPEVGIPDnGKGMiDLIAAVQKQQQQSGNHPITVH 144
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 998470296 1144 DRYGGTEAATFCCLSALYRQLEREKCVDVYMYAKLYHMRRPGIWKSQDDFLFLYR 1198
Cdd:cd14552   145 CSAGAGRTGTFCALSTVLERVKAEGVLDVFQVVKSLRLQRPHMVQTLEQYEFCYK 199
R-PTPc-H cd14619
catalytic domain of receptor-type tyrosine-protein phosphatase H; Receptor-type ...
963-1198 4.06e-27

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: 111.13  E-value: 4.06e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 998470296  963 NRSLNLIPIESHRVHITPKPGIDGSDYINATFLQGFNRLREFIVTQHPLMDTMADFWQMVWDHNSQTIVVLSVVDEK--- 1039
Cdd:cd14619     1 NRFRNVLPYDWSRVPLKPIHEEPGSDYINANYMPGYWSSQEFIATQGPLPQTVGDFWRMIWEQQSSTIVMLTNCMEAgrv 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 998470296 1040 EHPQFWPDTDEEQDYGSFKVKPTGESVAPpvaeekgalmpgeggGLPSRDFILQSTQDDYELACRLLLCPGWPQSCSPLA 1119
Cdd:cd14619    81 KCEHYWPLDYTPCTYGHLRVTVVSEEVME---------------NWTVREFLLKQVEEQKTLSVRHFHFTAWPDHGVPSS 145
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 998470296 1120 KAFELVKEVGARQERDQN---GPVVIVDRYGGTEAATFCCLSALYRQLEREKCVDVYMYAKLYHMRRPGIWKSQDDFLFL 1196
Cdd:cd14619   146 TDTLLAFRRLLRQWLDQTmsgGPTVVHCSAGVGRTGTLIALDVLLQQLQSEGLLGPFSFVQKMRENRPLMVQTESQYVFL 225

                  ..
gi 998470296 1197 YR 1198
Cdd:cd14619   226 HQ 227
R-PTPc-M-2 cd14635
PTP domain of receptor-type tyrosine-protein phosphatase M, repeat 2; Receptor-type ...
688-893 5.69e-27

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: 109.78  E-value: 5.69e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 998470296  688 YINANYIDGYHKSRAFIGTQGPLPATFDDYWRMVWEQRVCIIIMITNLveRGRRKCDMYWPKEGTETYGIIQVKLVQEIV 767
Cdd:cd14635     1 YINAALMDSYKQPSAFIVTQHPLPNTVKDFWRLVLDYHCTSIVMLNDV--DPAQLCPQYWPENGVHRHGPIQVEFVSADL 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 998470296  768 MATYTIRTFAIKNikVKKKQASERTVYQYHYTNWPDHgvPDHPLPVLSF------VAKSSAANPPAAGPMIVHCSAGVGR 841
Cdd:cd14635    79 EEDIISRIFRIYN--AARPQDGYRMVQQFQFLGWPMY--RDTPVSKRSFlklirqVDKWQEEYNGGEGRTVVHCLNGGGR 154
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 998470296  842 TGTYIVLDAMLRQMRQRQSVNVYGFLRHIRQQRNYLVQTEEQYVFIHDALLE 893
Cdd:cd14635   155 SGTFCAISIVCEMLRHQRAVDVFHAVKTLRNNKPNMVDLLDQYKFCYEVALE 206
R5-PTP-2 cd14550
PTP-like domain of R5 subfamily receptor-type tyrosine-protein phosphatases, repeat 2; The R5 ...
688-887 1.28e-26

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: 108.56  E-value: 1.28e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 998470296  688 YINANYIDGYHKSRAFIGTQGPLPATFDDYWRMVWEQRVCIIIMITNLVERGrrKCDMYWPKEGT----ETYGIIQV--K 761
Cdd:cd14550     1 YINASYLQGYRRSNEFIITQHPLEHTIKDFWQMIWDHNSQTIVMLTDNELNE--DEPIYWPTKEKplecETFKVTLSgeD 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 998470296  762 LVQEIVMATYTIRTFAIKNikvkKKQASERTVYQYHYTNWPDhgvPDHPL-PVLSFVAKSSAANPPAAGPMIVHCSAGVG 840
Cdd:cd14550    79 HSCLSNEIRLIVRDFILES----TQDDYVLEVRQFQCPSWPN---PCSPIhTVFELINTVQEWAQQRDGPIVVHDRYGGV 151
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*..
gi 998470296  841 RTGTYIVLDAMLRQMRQRQSVNVYGFLRHIRQQRNYLVQTEEQYVFI 887
Cdd:cd14550   152 QAATFCALTTLHQQLEHESSVDVYQVAKLYHLMRPGVFTSKEDYQFL 198
R-PTP-Z-2 cd17669
catalytic domain of receptor-type tyrosine-protein phosphatase Z, repeat 2; Receptor-type ...
688-892 1.68e-26

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: 108.54  E-value: 1.68e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 998470296  688 YINANYIDGYHKSRAFIGTQGPLPATFDDYWRMVWEQRVCIIIMITNLVERGRRKCdMYWP-KEGTETYGIIQVKLVQEI 766
Cdd:cd17669     1 YINASYIMGYYQSNEFIITQHPLLHTIKDFWRMIWDHNAQLIVMLPDGQNMAEDEF-VYWPnKDEPINCETFKVTLIAEE 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 998470296  767 VMATYTIRTFAIKNIKVKKKQASE-RTVYQYHYTNWPDhgvPDHPLPV---LSFVAKSSAANppAAGPMIVHCSAGVGRT 842
Cdd:cd17669    80 HKCLSNEEKLIIQDFILEATQDDYvLEVRHFQCPKWPN---PDSPISKtfeLISIIKEEAAN--RDGPMIVHDEHGGVTA 154
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|
gi 998470296  843 GTYIVLDAMLRQMRQRQSVNVYGFLRHIRQQRNYLVQTEEQYVFIHDALL 892
Cdd:cd17669   155 GTFCALTTLMHQLEKENSVDVYQVAKMINLMRPGVFTDIEQYQFLYKAIL 204
R-PTPc-E-2 cd14622
catalytic domain of receptor-type tyrosine-protein phosphatase E, repeat 2; Receptor-type ...
988-1198 3.31e-26

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: 107.40  E-value: 3.31e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 998470296  988 DYINATFLQGFNRLREFIVTQHPLMDTMADFWQMVWDHNSQTIVVLSVVDEKEHP---QFWPdTDEEQDYGSFKVKPTGE 1064
Cdd:cd14622     1 DYINASFIDGYRQKDYFIATQGPLAHTVEDFWRMVWEWKCHTIVMLTELQEREQEkcvQYWP-SEGSVTHGEITIEIKND 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 998470296 1065 SVAPPVAeekgalmpgeggglpSRDFILQSTQDDYELACRLLLCPGWPQSCSPL--AKAFELVKEVGARQERDQNGPVVI 1142
Cdd:cd14622    80 TLLETIS---------------IRDFLVTYNQEKQTRLVRQFHFHGWPEIGIPAegKGMIDLIAAVQKQQQQTGNHPIVV 144
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 998470296 1143 VDRYGGTEAATFCCLSALYRQLEREKCVDVYMYAKLYHMRRPGIWKSQDDFLFLYR 1198
Cdd:cd14622   145 HCSAGAGRTGTFIALSNILERVKAEGLLDVFQTVKSLRLQRPHMVQTLEQYEFCYR 200
R-PTPc-F-1 cd14626
catalytic domain of receptor-type tyrosine-protein phosphatase F, repeat 1; Receptor-type ...
959-1197 4.53e-26

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: 109.35  E-value: 4.53e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 998470296  959 NKAKNRSLNLIPIESHRVHITPKPGIDGSDYINATFLQGFNRLREFIVTQHPLMDTMADFWQMVWDHNSQTIVVLSVVDE 1038
Cdd:cd14626    41 NKPKNRYANVIAYDHSRVILTSVDGVPGSDYINANYIDGYRKQNAYIATQGPLPETLSDFWRMVWEQRTATIVMMTRLEE 120
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 998470296 1039 KEH---PQFWPDTDEEQdYGSFKVKptgesvappvaeekgALMPGEGGGLPSRDFILQSTQDDYELACRLLLCPGWPQSC 1115
Cdd:cd14626   121 KSRvkcDQYWPIRGTET-YGMIQVT---------------LLDTVELATYSVRTFALYKNGSSEKREVRQFQFMAWPDHG 184
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 998470296 1116 SP--LAKAFELVKEVGARQERDQnGPVVIVDRYGGTEAATFCCLSALYRQLEREKCVDVYMYAKLYHMRRPGIWKSQDDF 1193
Cdd:cd14626   185 VPeyPTPILAFLRRVKACNPPDA-GPMVVHCSAGVGRTGCFIVIDAMLERMKHEKTVDIYGHVTCMRSQRNYMVQTEDQY 263

                  ....
gi 998470296 1194 LFLY 1197
Cdd:cd14626   264 IFIH 267
R-PTPc-J cd14615
catalytic domain of receptor-type tyrosine-protein phosphatase J; Receptor-type ...
963-1198 8.62e-26

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: 107.21  E-value: 8.62e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 998470296  963 NRSLNLIPIESHRVHITpKPGIDGSDYINATFLQGFNRLREFIVTQHPLMDTMADFWQMVWDHNSQTIVVLSVVDEK--- 1039
Cdd:cd14615     1 NRYNNVLPYDISRVKLS-VQSHSTDDYINANYMPGYNSKKEFIAAQGPLPNTVKDFWRMVWEKNVYAIVMLTKCVEQgrt 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 998470296 1040 EHPQFWPdTDEEQDYGSFKVKPTGESVAPPvaeekgalmpgegggLPSRDFILQSTQDDYELACRLLLCPGWPQSCSP-- 1117
Cdd:cd14615    80 KCEEYWP-SKQKKDYGDITVTMTSEIVLPE---------------WTIRDFTVKNAQTNESRTVRHFHFTSWPDHGVPet 143
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 998470296 1118 ---LAKAFELVKEVgaRQERDQNGPVVIVDRYGGTEAATFCCLSALYRQLEREKCVDVYMYAKLYHMRRPGIWKSQDDFL 1194
Cdd:cd14615   144 tdlLINFRHLVREY--MKQNPPNSPILVHCSAGVGRTGTFIAIDRLIYQIENENVVDVYGIVYDLRMHRPLMVQTEDQYV 221

                  ....
gi 998470296 1195 FLYR 1198
Cdd:cd14615   222 FLNQ 225
R-PTPc-V cd14618
catalytic domain of receptor-type tyrosine-protein phosphatase V; Receptor-type ...
963-1197 1.81e-25

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: 106.18  E-value: 1.81e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 998470296  963 NRSLNLIPIESHRVHITPKPGIDGSDYINATFLQGFNRLREFIVTQHPLMDTMADFWQMVWDHNSQTIVVLSVVDEK--- 1039
Cdd:cd14618     1 NRYPHVLPYDHSRVRLSQLGGEPHSDYINANFIPGYTSPQEFIATQGPLKKTIEDFWRLVWEQQVCNIIMLTVGMENgrv 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 998470296 1040 --EHpqFWPDTDEEQDYGSFKVKPTGESvappVAEEkgalmpgegggLPSRDFILQSTQDDYELACRLLLCPGW-----P 1112
Cdd:cd14618    81 lcDH--YWPSESTPVSYGHITVHLLAQS----SEDE-----------WTRREFKLWHEDLRKERRVKHLHYTAWpdhgiP 143
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 998470296 1113 QSCSPLAKAFELVKEvgARQERDQNGPVVIVDRYGGTEAATFCCLSALYRQLEREKCVDVYMYAKLYHMRRPGIWKSQDD 1192
Cdd:cd14618   144 ESTSSLMAFRELVRE--HVQATKGKGPTLVHCSAGVGRSGTFIALDRLLRQLKEEKVVDVFNTVYILRMHRYLMIQTLSQ 221

                  ....*
gi 998470296 1193 FLFLY 1197
Cdd:cd14618   222 YIFLH 226
R-PTPc-S-1 cd14625
catalytic domain of receptor-type tyrosine-protein phosphatase S, repeat 1; Receptor-type ...
959-1197 7.08e-25

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: 105.95  E-value: 7.08e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 998470296  959 NKAKNRSLNLIPIESHRVHITPKPGIDGSDYINATFLQGFNRLREFIVTQHPLMDTMADFWQMVWDHNSQTIVVLSVVDE 1038
Cdd:cd14625    47 NKPKNRYANVIAYDHSRVILQPIEGIMGSDYINANYIDGYRKQNAYIATQGPLPETFGDFWRMVWEQRSATVVMMTKLEE 126
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 998470296 1039 KEH---PQFWPDTDEEQdYGSFKVKptgesvappvaeekgALMPGEGGGLPSRDFILQSTQDDYELACRLLLCPGWPQSC 1115
Cdd:cd14625   127 KSRikcDQYWPSRGTET-YGMIQVT---------------LLDTIELATFCVRTFSLHKNGSSEKREVRQFQFTAWPDHG 190
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 998470296 1116 SPLAKA--FELVKEVGARQERDQnGPVVIVDRYGGTEAATFCCLSALYRQLEREKCVDVYMYAKLYHMRRPGIWKSQDDF 1193
Cdd:cd14625   191 VPEYPTpfLAFLRRVKTCNPPDA-GPIVVHCSAGVGRTGCFIVIDAMLERIKHEKTVDIYGHVTLMRSQRNYMVQTEDQY 269

                  ....
gi 998470296 1194 LFLY 1197
Cdd:cd14625   270 SFIH 273
R-PTPc-O cd14614
catalytic domain of receptor-type tyrosine-protein phosphatase O; Receptor-type ...
948-1198 5.01e-24

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: 102.66  E-value: 5.01e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 998470296  948 DFNVVSAVKPCNKAKNRSLNLIPIESHRVHITPKPGIDGSDYINATFLQGFNRLREFIVTQHPLMDTMADFWQMVWDHNS 1027
Cdd:cd14614     1 DIPHFAADLPVNRCKNRYTNILPYDFSRVKLVSMHEEEGSDYINANYIPGYNSPQEYIATQGPLPETRNDFWKMVLQQKS 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 998470296 1028 QTIVVLSVVDEKEH---PQFWPDTDEEQDYGSFKVKPTGESVAPpvaeekgalmpgeggglpsrDFILQSTQDDYELACR 1104
Cdd:cd14614    81 QIIVMLTQCNEKRRvkcDHYWPFTEEPVAYGDITVEMLSEEEQP--------------------DWAIREFRVSYADEVQ 140
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 998470296 1105 LLL---CPGWPQSCSPLAKAFELVKEV--GARQERDQN-GPVVIVDRYGGTEAATFCCLSALYRQLEREKCVDVYMYAKL 1178
Cdd:cd14614   141 DVMhfnYTAWPDHGVPTANAAESILQFvqMVRQQAVKSkGPMIIHCSAGVGRTGTFIALDRLLQHIRDHEFVDILGLVSE 220
                         250       260
                  ....*....|....*....|
gi 998470296 1179 YHMRRPGIWKSQDDFLFLYR 1198
Cdd:cd14614   221 MRSYRMSMVQTEEQYIFIHQ 240
R-PTPc-G-1 cd17667
catalytic domain of receptor-type tyrosine-protein phosphatase G, repeat 1; Receptor-type ...
957-1197 6.72e-24

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: 102.81  E-value: 6.72e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 998470296  957 PCNKAKNRSLNLIPIESHRVHITPKPGIDG--SDYINATFLQGFNRLREFIVTQHPLMDTMADFWQMVWDHNSQTIVVLS 1034
Cdd:cd17667    25 PDNKHKNRYINILAYDHSRVKLRPLPGKDSkhSDYINANYVDGYNKAKAYIATQGPLKSTFEDFWRMIWEQNTGIIVMIT 104
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 998470296 1035 VVDEK---EHPQFWPdTDEEQDYGSFKVKPTGESVAP-----PVAEEKGALMPGEGGGLPSRDFILQSTQDDYElacrll 1106
Cdd:cd17667   105 NLVEKgrrKCDQYWP-TENSEEYGNIIVTLKSTKIHAcytvrRFSIRNTKVKKGQKGNPKGRQNERTVIQYHYT------ 177
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 998470296 1107 lcpGWPQSCSP--LAKAFELVKEVGARQERDQnGPVVIVDRYGGTEAATFCCLSALYRQLEREKCVDVYMYAKLYHMRRP 1184
Cdd:cd17667   178 ---QWPDMGVPeyALPVLTFVRRSSAARTPEM-GPVLVHCSAGVGRTGTYIVIDSMLQQIKDKSTVNVLGFLKHIRTQRN 253
                         250
                  ....*....|...
gi 998470296 1185 GIWKSQDDFLFLY 1197
Cdd:cd17667   254 YLVQTEEQYIFIH 266
R-PTPc-A-1 cd14621
catalytic domain of receptor-type tyrosine-protein phosphatase A, repeat 1; Receptor-type ...
953-1198 1.96e-23

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: 102.02  E-value: 1.96e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 998470296  953 SAVKPCNKAKNRSLNLIPIESHRVHITPKPGIDGSDYINATFLQGFNRLREFIVTQHPLMDTMADFWQMVWDHNSQTIVV 1032
Cdd:cd14621    46 AASKEENKEKNRYVNILPYDHSRVHLTPVEGVPDSDYINASFINGYQEKNKFIAAQGPKEETVNDFWRMIWEQNTATIVM 125
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 998470296 1033 LSVVDEKEH---PQFWPDTDeEQDYGSFKVKptgesvappvAEEKGALMpgeggGLPSRDFILQSTQDDYELACRLLLC- 1108
Cdd:cd14621   126 VTNLKERKEckcAQYWPDQG-CWTYGNIRVS----------VEDVTVLV-----DYTVRKFCIQQVGDVTNKKPQRLITq 189
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 998470296 1109 ---PGWPQSCSPLAK--AFELVKEVGARQERdQNGPVVIVDRYGGTEAATFCCLSALYRQLEREKCVDVYMYAKLYHMRR 1183
Cdd:cd14621   190 fhfTSWPDFGVPFTPigMLKFLKKVKNCNPQ-YAGAIVVHCSAGVGRTGTFIVIDAMLDMMHAERKVDVYGFVSRIRAQR 268
                         250
                  ....*....|....*
gi 998470296 1184 PGIWKSQDDFLFLYR 1198
Cdd:cd14621   269 CQMVQTDMQYVFIYQ 283
R-PTP-C-2 cd14558
PTP-like domain of receptor-type tyrosine-protein phosphatase C, repeat 2; Receptor-type ...
989-1197 2.32e-23

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: 99.39  E-value: 2.32e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 998470296  989 YINATFLQGFNRLREFIVTQHPLMDTMADFWQMVWDHNSQTIVVLSVV---DEKEHPQFWPdtDEEQDYGSFKVKPTGES 1065
Cdd:cd14558     1 YINASFIDGYWGPKSLIATQGPLPDTIADFWQMIFQKKVKVIVMLTELkegDQEQCAQYWG--DEKKTYGDIEVELKDTE 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 998470296 1066 VAPPVAEekgalmpgeggglpsRDFILQSTQDDYELACRLLLCPGW-----PQSCSPLAKAFELVKEVGA--RQERDQNG 1138
Cdd:cd14558    79 KSPTYTV---------------RVFEITHLKRKDSRTVYQYQYHKWkgeelPEKPKDLVDMIKSIKQKLPykNSKHGRSV 143
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 998470296 1139 PVVIVDRYGGTEAATFCCLSALYRQLEREKCVDVYMYAKLYHMRRPGIWKSQDDFLFLY 1197
Cdd:cd14558   144 PIVVHCSDGSSRTGIFCALWNLLESAETEKVVDVFQVVKALRKQRPGMVSTLEQYQFLY 202
R-PTPc-E-1 cd14620
catalytic domain of receptor-type tyrosine-protein phosphatase E, repeat 1; Receptor-type ...
967-1198 5.25e-22

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: 96.16  E-value: 5.25e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 998470296  967 NLIPIESHRVHITPKPGIDGSDYINATFLQGFNRLREFIVTQHPLMDTMADFWQMVWDHNSQTIVVLSVVDEKEHP---Q 1043
Cdd:cd14620     3 NILPYDHSRVILSQLDGIPCSDYINASYIDGYKEKNKFIAAQGPKQETVNDFWRMVWEQKSATIVMLTNLKERKEEkcyQ 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 998470296 1044 FWPDTDeEQDYGSFKVkptgesvappVAEEKGALMpgeggGLPSRDFILQSTQDDYELACRL---LLCPGWPQSCSPLA- 1119
Cdd:cd14620    83 YWPDQG-CWTYGNIRV----------AVEDCVVLV-----DYTIRKFCIQPQLPDGCKAPRLvtqLHFTSWPDFGVPFTp 146
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 998470296 1120 ----KAFELVKEVGARQErdqnGPVVIVDRYGGTEAATFCCLSALYRQLEREKCVDVYMYAKLYHMRRPGIWKSQDDFLF 1195
Cdd:cd14620   147 igmlKFLKKVKSVNPVHA----GPIVVHCSAGVGRTGTFIVIDAMIDMMHAEQKVDVFEFVSRIRNQRPQMVQTDMQYSF 222

                  ...
gi 998470296 1196 LYR 1198
Cdd:cd14620   223 IYQ 225
PTPc-N9 cd14543
catalytic domain of tyrosine-protein phosphatase non-receptor type 9; Tyrosine-protein ...
950-1059 5.51e-22

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: 97.05  E-value: 5.51e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 998470296  950 NVVSAVKPCNKAKNRSLNLIPIESHRVHITPKPGIDGSDYINATFLQGFNRLREFIVTQHPLMDTMADFWQMVWDHNSQT 1029
Cdd:cd14543    20 TFLCSLAPANQEKNRYGDVLCLDQSRVKLPKRNGDERTDYINANFMDGYKQKNAYIATQGPLPKTYSDFWRMVWEQKVLV 99
                          90       100       110
                  ....*....|....*....|....*....|....
gi 998470296 1030 IVVLSVVDE---KEHPQFWP-DTDEEQDYGSFKV 1059
Cdd:cd14543   100 IVMTTRVVErgrVKCGQYWPlEEGSSLRYGDLTV 133
R-PTPc-B cd14617
catalytic domain of receptor-type tyrosine-protein phosphatase B; Receptor-type ...
963-1173 7.01e-22

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: 95.76  E-value: 7.01e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 998470296  963 NRSLNLIPIESHRVHITPKPGIDGSDYINATFLQGFNRLREFIVTQHPLMDTMADFWQMVWDHNSQTIVVLSVVDEK--- 1039
Cdd:cd14617     1 NRYNNILPYDSTRVKLSNVDDDPCSDYINASYIPGNNFRREYIATQGPLPGTKDDFWKMVWEQNVHNIVMVTQCVEKgrv 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 998470296 1040 --EHpqFWPDTDEEQDYGSFKVKPTGESVAPPvaeekgalmpgegggLPSRDF-ILQSTQDDYELACRLLLCPGWPQSCS 1116
Cdd:cd14617    81 kcDH--YWPADQDSLYYGDLIVQMLSESVLPE---------------WTIREFkICSEEQLDAPRLVRHFHYTVWPDHGV 143
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 998470296 1117 P--LAKAFELVKEVGARQERDQN-GPVVIVDRYGGTEAATFCCLSALYRQLEREKCVDVY 1173
Cdd:cd14617   144 PetTQSLIQFVRTVRDYINRTPGsGPTVVHCSAGVGRTGTFIALDRILQQLDSKDSVDIY 203
R-PTPc-D-1 cd14624
catalytic domain of receptor-type tyrosine-protein phosphatase D, repeat 1; Receptor-type ...
959-1197 8.58e-22

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: 97.11  E-value: 8.58e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 998470296  959 NKAKNRSLNLIPIESHRVHITPKPGIDGSDYINATFLQGFNRLREFIVTQHPLMDTMADFWQMVWDHNSQTIVVLSVVDE 1038
Cdd:cd14624    47 NKPKNRYANVIAYDHSRVLLSAIEGIPGSDYINANYIDGYRKQNAYIATQGALPETFGDFWRMIWEQRSATVVMMTKLEE 126
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 998470296 1039 KEH---PQFWPDTDEEQdYGSFKVKptgesvappvaeekgALMPGEGGGLPSRDFILQSTQDDYELACRLLLCPGWPQSC 1115
Cdd:cd14624   127 RSRvkcDQYWPSRGTET-YGLIQVT---------------LLDTVELATYCVRTFALYKNGSSEKREVRQFQFTAWPDHG 190
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 998470296 1116 SPLAKA--FELVKEVGARQERDQnGPVVIVDRYGGTEAATFCCLSALYRQLEREKCVDVYMYAKLYHMRRPGIWKSQDDF 1193
Cdd:cd14624   191 VPEHPTpfLAFLRRVKTCNPPDA-GPMVVHCSAGVGRTGCFIVIDAMLERIKHEKTVDIYGHVTLMRAQRNYMVQTEDQY 269

                  ....
gi 998470296 1194 LFLY 1197
Cdd:cd14624   270 IFIH 273
R-PTPc-Q cd14616
catalytic domain of receptor-type tyrosine-protein phosphatase Q; Receptor-type ...
963-1173 1.41e-21

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: 94.59  E-value: 1.41e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 998470296  963 NRSLNLIPIESHRVHITPKPGIDGSDYINATFLQGFNRLREFIVTQHPLMDTMADFWQMVWDHNSQTIVVLSVVDEKEH- 1041
Cdd:cd14616     1 NRFPNIKPYNNNRVKLIADAGVPGSDYINASYISGYLCPNEFIATQGPLPGTVGDFWRMVWETRAKTIVMLTQCFEKGRi 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 998470296 1042 --PQFWPDTDEeqdygsfKVKPTGESVAPPVAEEKGAlmpgeggGLPSRDFILQStQDDYELA--CRLLLCP--GWPQSC 1115
Cdd:cd14616    81 rcHQYWPEDNK-------PVTVFGDIVITKLMEDVQI-------DWTIRDLKIER-HGDYMMVrqCNFTSWPehGVPESS 145
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 998470296 1116 SPLAKafeLVKEVGARQERDqNGPVVIVDRYGGTEAATFCCLSALYRQLEREKCVDVY 1173
Cdd:cd14616   146 APLIH---FVKLVRASRAHD-NTPMIVHCSAGVGRTGVFIALDHLTQHINDHDFVDIY 199
R-PTP-G-2 cd17670
PTP-like domain of receptor-type tyrosine-protein phosphatase G, repeat 2; Receptor-type ...
688-892 2.15e-21

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: 93.59  E-value: 2.15e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 998470296  688 YINANYIDGYHKSRAFIGTQGPLPATFDDYWRMVWEQRVCIIIMITNlvERGRRKCD-MYWP-KEGTETYGIIQVKLVQE 765
Cdd:cd17670     1 YINASYIMGYYRSNEFIITQHPLPHTTKDFWRMIWDHNAQIIVMLPD--NQGLAEDEfVYWPsREESMNCEAFTVTLISK 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 998470296  766 IVMATYTIRTFAIKNIKVKKKQASE-RTVYQYHYTNWPDhgvPDHPLPV---LSFVAKSSAANppAAGPMIVHCSAGVGR 841
Cdd:cd17670    79 DRLCLSNEEQIIIHDFILEATQDDYvLEVRHFQCPKWPN---PDAPISStfeLINVIKEEALT--RDGPTIVHDEFGAVS 153
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|.
gi 998470296  842 TGTYIVLDAMLRQMRQRQSVNVYGFLRHIRQQRNYLVQTEEQYVFIHDALL 892
Cdd:cd17670   154 AGTLCALTTLSQQLENENAVDVYQVAKMINLMRPGVFTDIEQYQFLYKAML 204
PTPc-KIM cd14547
catalytic domain of the kinase interaction motif (KIM) family of protein-tyrosine phosphatases; ...
963-1172 7.14e-21

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: 92.84  E-value: 7.14e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 998470296  963 NRSLNLIPIESHRVHITPKPGIDGSDYINATFLQGFNRLRE-FIVTQHPLMDTMADFWQMVWDHNSQTIVVLSVVDEKEH 1041
Cdd:cd14547     1 NRYKTILPNEHSRVCLPSVDDDPLSSYINANYIRGYDGEEKaYIATQGPLPNTVADFWRMVWQEKTPIIVMITNLTEAKE 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 998470296 1042 P--QFWPDTDEEQdYGSFKVkpTGESVAPPvaeekgalmpgEGGGLpsRDFILQSTQDDYElaCRLLLCPGWPQSCSP-L 1118
Cdd:cd14547    81 KcaQYWPEEENET-YGDFEV--TVQSVKET-----------DGYTV--RKLTLKYGGEKRY--LKHYWYTSWPDHKTPeA 142
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 998470296 1119 AKAF-ELVKEV-GARQERDQNGPVVI-----VDRYGGTEAATFCClsalyRQLEREKCVDV 1172
Cdd:cd14547   143 AQPLlSLVQEVeEARQTEPHRGPIVVhcsagIGRTGCFIATSIGC-----QQLREEGVVDV 198
FN3 COG3401
Fibronectin type 3 domain [General function prediction only];
196-438 1.62e-20

Fibronectin type 3 domain [General function prediction only];


Pssm-ID: 442628 [Multi-domain]  Cd Length: 603  Bit Score: 97.38  E-value: 1.62e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 998470296  196 VIGLKPFTVYSFRVLAVNAIGASKPSKEsFYMVTLREVPEgKPTIVHAQNTSSSSVRIQWTAPARHTIhgefEGYRItYR 275
Cdd:COG3401   196 GGDIEPGTTYYYRVAATDTGGESAPSNE-VSVTTPTTPPS-APTGLTATADTPGSVTLSWDPVTESDA----TGYRV-YR 268
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 998470296  276 prdRTQEESREIILRDSKQTQYTIRNLETFTQYLVSLQVFNPAGR--GPAVVVPVMTDEGVPSSPVNLTAVRVTDTTVRL 353
Cdd:COG3401   269 ---SNSGDGPFTKVATVTTTSYTDTGLTNGTTYYYRVTAVDAAGNesAPSNVVSVTTDLTPPAAPSGLTATAVGSSSITL 345
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 998470296  354 KWREPvrPNGVLQGYHVYfqpsRNGSSQQQRKTVSHPQPVEEYMLSGLKPFSFYDIWVKAFTQQHL-GESSNLLKVQTDV 432
Cdd:COG3401   346 SWTAS--SDADVTGYNVY----RSTSGGGTYTKIAETVTTTSYTDTGLTPGTTYYYKVTAVDAAGNeSAPSEEVSATTAS 419

                  ....*.
gi 998470296  433 QGPSAP 438
Cdd:COG3401   420 AASGES 425
R-PTPc-M-1 cd14633
catalytic domain of receptor-type tyrosine-protein phosphatase M, repeat 1; Receptor-type ...
953-1197 2.82e-20

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: 92.41  E-value: 2.82e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 998470296  953 SAVKPCNKAKNRSLNLIPIESHRVHITPKPGIDGSDYINATFLQGFNRLREFIVTQHPLMDTMADFWQMVWDHNSQTIVV 1032
Cdd:cd14633    34 SAKKDENRMKNRYGNIIAYDHSRVRLQPIEGETSSDYINGNYIDGYHRPNHYIATQGPMQETIYDFWRMVWHENTASIIM 113
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 998470296 1033 ---LSVVDEKEHPQFWPDTDEeqDYGSFKV-----KPTGESVAPPVAEEKgalmpgeggglpsrdfilQSTQDDYELacR 1104
Cdd:cd14633   114 vtnLVEVGRVKCCKYWPDDTE--IYKDIKVtlietELLAEYVIRTFAVEK------------------RGVHEIREI--R 171
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 998470296 1105 LLLCPGWPQSCSPLAKA--FELVKEVGARQERDQnGPVVIVDRYGGTEAATFCCLSALYRQLEREKCVDVYMYAKLYHMR 1182
Cdd:cd14633   172 QFHFTGWPDHGVPYHATglLGFVRQVKSKSPPNA-GPLVVHCSAGAGRTGCFIVIDIMLDMAEREGVVDIYNCVRELRSR 250
                         250
                  ....*....|....*
gi 998470296 1183 RPGIWKSQDDFLFLY 1197
Cdd:cd14633   251 RVNMVQTEEQYVFIH 265
PTPc-N11_6 cd14544
catalytic domain of tyrosine-protein phosphatase non-receptor type 11 and type 6; ...
959-1197 4.80e-20

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: 90.98  E-value: 4.80e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 998470296  959 NKAKNRSLNLIPIESHRVHITPK-PGIDGSDYINATFL-----QGFNRLRE--FIVTQHPLMDTMADFWQMVWDHNSQTI 1030
Cdd:cd14544     1 NKGKNRYKNILPFDHTRVILKDRdPNVPGSDYINANYIrneneGPTTDENAktYIATQGCLENTVSDFWSMVWQENSRVI 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 998470296 1031 VVLSVVDEKEHPQ---FWPDTDEEQDYGSFKVKPTGESVAPPVAEEKGALMPGEGGGLPSRDFILQSTQddyelacrlll 1107
Cdd:cd14544    81 VMTTKEVERGKNKcvrYWPDEGMQKQYGPYRVQNVSEHDTTDYTLRELQVSKLDQGDPIREIWHYQYLS----------- 149
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 998470296 1108 cpgWPQSCSPL--AKAFELVKEVGARQE-RDQNGPVVIVDRYGGTEAATFCCLSALYRQLERE--KC-VDVYMYAKLYHM 1181
Cdd:cd14544   150 ---WPDHGVPSdpGGVLNFLEDVNQRQEsLPHAGPIVVHCSAGIGRTGTFIVIDMLLDQIKRKglDCdIDIQKTIQMVRS 226
                         250
                  ....*....|....*.
gi 998470296 1182 RRPGIWKSQDDFLFLY 1197
Cdd:cd14544   227 QRSGMVQTEAQYKFIY 242
PTPc-N7 cd14612
catalytic domain of tyrosine-protein phosphatase non-receptor type 7; Tyrosine-protein ...
957-1198 7.97e-20

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: 90.28  E-value: 7.97e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 998470296  957 PCNKAKNRSLNLIPIESHRVHI-TPKPGIDGSDYINATFLQGFN-RLREFIVTQHPLMDTMADFWQMVWDHNSQTIVVLS 1034
Cdd:cd14612    13 PGHASKDRYKTILPNPQSRVCLrRAGSQEEEGSYINANYIRGYDgKEKAYIATQGPMLNTVSDFWEMVWQEECPIIVMIT 92
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 998470296 1035 VVDEKEHP--QFWPdtDEEQDYGSFKVKptgesvappVAEEKgalmpgEGGGLPSRDFILQstqddYELACRLL---LCP 1109
Cdd:cd14612    93 KLKEKKEKcvHYWP--EKEGTYGRFEIR---------VQDMK------ECDGYTIRDLTIQ-----LEEESRSVkhyWFS 150
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 998470296 1110 GW-----PQSCSPLakaFELVKEV-GARQERDQNGPVVI-----VDRYGGTEAATFCCLsalyrQLEREKCVDVYMYAKL 1178
Cdd:cd14612   151 SWpdhqtPESAGPL---LRLVAEVeESRQTAASPGPIVVhcsagIGRTGCFIATSIGCQ-----QLKDTGKVDILGIVCQ 222
                         250       260
                  ....*....|....*....|
gi 998470296 1179 YHMRRPGIWKSQDDFLFLYR 1198
Cdd:cd14612   223 LRLDRGGMIQTSEQYQFLHH 242
FN3 COG3401
Fibronectin type 3 domain [General function prediction only];
132-352 8.79e-20

Fibronectin type 3 domain [General function prediction only];


Pssm-ID: 442628 [Multi-domain]  Cd Length: 603  Bit Score: 95.07  E-value: 8.79e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 998470296  132 VPDPPGIPIVVGFTSRSVDLSWTSSPNSHhsvILHYIIHIRIGEKGDWDTMNKVmtsdNSTNFQVIGLKPFTVYSFRVLA 211
Cdd:COG3401   232 PPSAPTGLTATADTPGSVTLSWDPVTESD---ATGYRVYRSNSGDGPFTKVATV----TTTSYTDTGLTNGTTYYYRVTA 304
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 998470296  212 VNAIG-ASKPSKESFymVTLREVPEGKPTIVHAQNTSSSSVRIQWTAPArhtiHGEFEGYRItYRprDRTQEESREIILR 290
Cdd:COG3401   305 VDAAGnESAPSNVVS--VTTDLTPPAAPSGLTATAVGSSSITLSWTASS----DADVTGYNV-YR--STSGGGTYTKIAE 375
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 998470296  291 DSKQTQYTIRNLETFTQYLVSLQVFNPAGRGPAVVVPVMTDEGVPSSPVNLTAVRVTDTTVR 352
Cdd:COG3401   376 TVTTTSYTDTGLTPGTTYYYKVTAVDAAGNESAPSEEVSATTASAASGESLTASVDAVPLTD 437
R-PTPc-T-2 cd14634
PTP domain of receptor-type tyrosine-protein phosphatase T, repeat 2; Receptor-type ...
989-1197 6.11e-19

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: 86.61  E-value: 6.11e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 998470296  989 YINATFLQGFNRLREFIVTQHPLMDTMADFWQMVWDHNSQTIVVLSVVDEKEH-PQFWPDTdEEQDYGSFKVkptgESVA 1067
Cdd:cd14634     1 YINAALMDSHKQPAAFIVTQHPLPNTVADFWRLVFDYNCSSVVMLNEMDAAQLcMQYWPEK-TSCCYGPIQV----EFVS 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 998470296 1068 PPVAEEkgalmpgegggLPSRDFI---LQSTQDDYELACRLLLCpGWPQ-SCSPLAK--AFELVKEVGARQER--DQNGP 1139
Cdd:cd14634    76 ADIDED-----------IISRIFRicnMARPQDGYRIVQHLQYI-GWPAyRDTPPSKrsILKVVRRLEKWQEQydGREGR 143
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 998470296 1140 VVIVDRYGGTEAATFCCLSALYRQLEREKCVDVYMYAKLYHMRRPGIWKSQDDFLFLY 1197
Cdd:cd14634   144 TVVHCLNGGGRSGTFCAICSVCEMIQQQNIIDVFHTVKTLRNNKSNMVETLEQYKFVY 201
R-PTPc-T-1 cd14630
catalytic domain of receptor-type tyrosine-protein phosphatase T, repeat 1; Receptor-type ...
959-1197 7.88e-19

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: 87.00  E-value: 7.88e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 998470296  959 NKAKNRSLNLIPIESHRVHITPKPGIDGSDYINATFLQGFNRLREFIVTQHPLMDTMADFWQMVWDHNSQTIVV---LSV 1035
Cdd:cd14630     3 NRNKNRYGNIISYDHSRVRLQLLDGDPHSDYINANYIDGYHRPRHYIATQGPMQETVKDFWRMIWQENSASVVMvtnLVE 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 998470296 1036 VDEKEHPQFWPdtDEEQDYGSFKVKPTGESvapPVAEekgalmpgegggLPSRDFILQSTQDDYELACRLLLCPGWPQSC 1115
Cdd:cd14630    83 VGRVKCVRYWP--DDTEVYGDIKVTLIETE---PLAE------------YVIRTFTVQKKGYHEIREIRQFHFTSWPDHG 145
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 998470296 1116 SPLAKA--FELVKEVGARQERDQnGPVVIVDRYGGTEAATFCCLSALYRQLEREKCVDVYMYAKLYHMRRPGIWKSQDDF 1193
Cdd:cd14630   146 VPCYATglLGFVRQVKFLNPPDA-GPIVVHCSAGAGRTGCFIAIDIMLDMAENEGVVDIFNCVRELRAQRVNMVQTEEQY 224

                  ....
gi 998470296 1194 LFLY 1197
Cdd:cd14630   225 VFVH 228
PHA02740 PHA02740
protein tyrosine phosphatase; Provisional
646-891 1.17e-18

protein tyrosine phosphatase; Provisional


Pssm-ID: 165107 [Multi-domain]  Cd Length: 298  Bit Score: 88.10  E-value: 1.17e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 998470296  646 DLTSSYSQLNENKPK--NRYINIVAYDHTRVILKpipgqkKSSDYINANYIDGYHKSRAFIGTQGPLPATFDDYWRMVWE 723
Cdd:PHA02740   40 DEANKACAQAENKAKdeNLALHITRLLHRRIKLF------NDEKVLDARFVDGYDFEQKFICIINLCEDACDKFLQALSD 113
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 998470296  724 QRVCIIIMITNLVErgrRKC-DMYWP-KEGT-ETYGIIQVKLVQEIVMATYTIRTFAIKNikvkkKQASERTVYQYHYTN 800
Cdd:PHA02740  114 NKVQIIVLISRHAD---KKCfNQFWSlKEGCvITSDKFQIETLEIIIKPHFNLTLLSLTD-----KFGQAQKISHFQYTA 185
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 998470296  801 WPDHGVPDHPLPVLSFV--AKSSAAN------PPAAGPMIVHCSAGVGRTGTYIVLDAMLRQMRQRQSVNVYGFLRHIRQ 872
Cdd:PHA02740  186 WPADGFSHDPDAFIDFFcnIDDLCADlekhkaDGKIAPIIIDCIDGISSSAVFCVFDICATEFDKTGMLSIANALKKVRQ 265
                         250
                  ....*....|....*....
gi 998470296  873 QRNYLVQTEEQYVFIHDAL 891
Cdd:PHA02740  266 KKYGCMNCLDDYVFCYHLI 284
R-PTPc-M-2 cd14635
PTP domain of receptor-type tyrosine-protein phosphatase M, repeat 2; Receptor-type ...
989-1197 1.44e-18

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: 85.51  E-value: 1.44e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 998470296  989 YINATFLQGFNRLREFIVTQHPLMDTMADFWQMVWDHNSQTIVVLSVVDEKEH-PQFWPDTDEEQdYGSFKVkptgESVA 1067
Cdd:cd14635     1 YINAALMDSYKQPSAFIVTQHPLPNTVKDFWRLVLDYHCTSIVMLNDVDPAQLcPQYWPENGVHR-HGPIQV----EFVS 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 998470296 1068 PPVAEEkgalmpgegggLPSRDFILQST---QDDYELACRLLLCpGWPQ-SCSPLAKA--FELVKEVGARQERDQNGP-- 1139
Cdd:cd14635    76 ADLEED-----------IISRIFRIYNAarpQDGYRMVQQFQFL-GWPMyRDTPVSKRsfLKLIRQVDKWQEEYNGGEgr 143
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 998470296 1140 VVIVDRYGGTEAATFCCLSALYRQLEREKCVDVYMYAKLYHMRRPGIWKSQDDFLFLY 1197
Cdd:cd14635   144 TVVHCLNGGGRSGTFCAISIVCEMLRHQRAVDVFHAVKTLRNNKPNMVDLLDQYKFCY 201
R5-PTPc-1 cd14549
catalytic domain of R5 subfamily receptor-type tyrosine-protein phosphatases, repeat 1; The R5 ...
989-1183 1.54e-18

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: 85.48  E-value: 1.54e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 998470296  989 YINATFLQGFNRLREFIVTQHPLMDTMADFWQMVWDHNSQTIVVLSVVDEK---EHPQFWPdTDEEQDYGSFKVKPTGES 1065
Cdd:cd14549     1 YINANYVDGYNKARAYIATQGPLPSTFDDFWRMVWEQNSAIIVMITNLVERgrrKCDQYWP-KEGTETYGNIQVTLLSTE 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 998470296 1066 VAPPVAEEKGALMPGEGGGLPSRDFILQSTQDDYElacrlllcpGWPQSCSP--LAKAFELVKEVgARQERDQNGPVVI- 1142
Cdd:cd14549    80 VLATYTVRTFSLKNLKLKKVKGRSSERVVYQYHYT---------QWPDHGVPdyTLPVLSFVRKS-SAANPPGAGPIVVh 149
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*
gi 998470296 1143 ----VDRYGgteaaTFCCLSALYRQLEREKCVDVYMYakLYHMRR 1183
Cdd:cd14549   150 csagVGRTG-----TYIVIDSMLQQIQDKGTVNVFGF--LKHIRT 187
PTPc-N11 cd14605
catalytic domain of tyrosine-protein phosphatase non-receptor type 11; Tyrosine-protein ...
959-1197 2.99e-18

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: 85.84  E-value: 2.99e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 998470296  959 NKAKNRSLNLIPIESHRVHITP-KPGIDGSDYINATFLQGFNRL--------REFIVTQHPLMDTMADFWQMVWDHNSQT 1029
Cdd:cd14605     2 NKNKNRYKNILPFDHTRVVLHDgDPNEPVSDYINANIIMPEFETkcnnskpkKSYIATQGCLQNTVNDFWRMVFQENSRV 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 998470296 1030 IVVLSVVDEKEHPQ---FWPDTDEEQDYGSFKVKPTGESvappvaeekgalmpgeggglPSRDFIL------QSTQDDYE 1100
Cdd:cd14605    82 IVMTTKEVERGKSKcvkYWPDEYALKEYGVMRVRNVKES--------------------AAHDYILrelklsKVGQGNTE 141
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 998470296 1101 LACRLLLCPGWPQSCSPL--AKAFELVKEVGARQER-DQNGPVVIVDRYGGTEAATFCCLSALYrQLEREK---C-VDVY 1173
Cdd:cd14605   142 RTVWQYHFRTWPDHGVPSdpGGVLDFLEEVHHKQESiMDAGPVVVHCSAGIGRTGTFIVIDILI-DIIREKgvdCdIDVP 220
                         250       260
                  ....*....|....*....|....
gi 998470296 1174 MYAKLYHMRRPGIWKSQDDFLFLY 1197
Cdd:cd14605   221 KTIQMVRSQRSGMVQTEAQYRFIY 244
PTPc-N18 cd14603
catalytic domain of tyrosine-protein phosphatase non-receptor type 18; Tyrosine-protein ...
944-1065 6.19e-18

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: 85.26  E-value: 6.19e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 998470296  944 FKAKD-FNVVSAVKPCNKAKNRSLNLIPIESHRVHITPKPGIDGSDYINATFLQGFNRLREFIVTQHPLMDTMADFWQMV 1022
Cdd:cd14603    14 FKADYvCSTVAGGRKENVKKNRYKDILPYDQTRVILSLLQEEGHSDYINANFIKGVDGSRAYIATQGPLSHTVLDFWRMI 93
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 998470296 1023 WDHNSQTIVVlsVVDEKEHPQ-----FWPDTDEEQDYGSFKVKPTGES 1065
Cdd:cd14603    94 WQYGVKVILM--ACREIEMGKkkcerYWAQEQEPLQTGPFTITLVKEK 139
R-PTP-N cd14609
PTP-like domain of receptor-type tyrosine-protein phosphatase N; Receptor-type ...
926-1195 6.24e-18

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: 85.47  E-value: 6.24e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 998470296  926 DNEKSWSLLERQFKLVTMFKAKDFNVVSAVKPCNKAKNRSLNLIPIESHRVHITPKPGIDGSDYINA-TFLQGFNRLREF 1004
Cdd:cd14609     9 DHLRNRDRLAKEWQALCAYQAEPNTCSTAQGEANVKKNRNPDFVPYDHARIKLKAESNPSRSDYINAsPIIEHDPRMPAY 88
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 998470296 1005 IVTQHPLMDTMADFWQMVWDHNSQTIVVLSVVDE---KEHPQFWPDtDEEQDYGSFKVKPTGESVAppvaeekgalmpge 1081
Cdd:cd14609    89 IATQGPLSHTIADFWQMVWENGCTVIVMLTPLVEdgvKQCDRYWPD-EGSSLYHIYEVNLVSEHIW-------------- 153
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 998470296 1082 ggglpSRDFILQS-------TQDDYELA-CRLLLCP--GWPQSCSPLakaFELVKEVGaRQERDQNGPVVIVDRYGGTEA 1151
Cdd:cd14609   154 -----CEDFLVRSfylknvqTQETRTLTqFHFLSWPaeGIPSSTRPL---LDFRRKVN-KCYRGRSCPIIVHCSDGAGRT 224
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*..
gi 998470296 1152 ATFCCLS-ALYRQLEREKCVDVymYAKLYHMR--RPGIWKSQDDFLF 1195
Cdd:cd14609   225 GTYILIDmVLNRMAKGVKEIDI--AATLEHVRdqRPGMVRTKDQFEF 269
PTPc-N3_4 cd14541
catalytic domain of tyrosine-protein phosphatase non-receptor type 21 and type 14; ...
988-1143 8.57e-18

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: 83.53  E-value: 8.57e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 998470296  988 DYINATF----LQGFNRLREFIVTQHPLMDTMADFWQMVWDHNSQTIVVLSVVDE----KEHpQFWPDTDEEQDYGSFKV 1059
Cdd:cd14541     1 DYINANYvnmeIPGSGIVNRYIAAQGPLPNTCADFWQMVWEQKSTLIVMLTTLVErgrvKCH-QYWPDLGETMQFGNLQI 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 998470296 1060 KPTGESVAPPVAEekgalmpgeggglpsRDFILQSTQDDYELACRLLLCPGWPQSCSPL-AKAF-ELVKEVgaRQERDQN 1137
Cdd:cd14541    80 TCVSEEVTPSFAF---------------REFILTNTNTGEERHITQMQYLAWPDHGVPDdSSDFlDFVKRV--RQNRVGM 142

                  ....*.
gi 998470296 1138 GPVVIV 1143
Cdd:cd14541   143 VEPTVV 148
R-PTPc-Z-1 cd17668
catalytic domain of receptor-type tyrosine-protein phosphatase Z, repeat 1; Receptor-type ...
989-1197 1.07e-17

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: 83.10  E-value: 1.07e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 998470296  989 YINATFLQGFNRLREFIVTQHPLMDTMADFWQMVWDHNSQTIVVLSVVDEK---EHPQFWPdTDEEQDYGSFKVKPTGES 1065
Cdd:cd17668     1 YINANYVDGYNKPKAYIAAQGPLKSTAEDFWRMIWEHNVEVIVMITNLVEKgrrKCDQYWP-ADGSEEYGNFLVTQKSVQ 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 998470296 1066 VAP-----PVAEEKGALMPGEGGGLPSRDFILQ--STQddyelacrlllcpgWPQSCSP--LAKAFELVKEVGARQeRDQ 1136
Cdd:cd17668    80 VLAyytvrNFTLRNTKIKKGSQKGRPSGRVVTQyhYTQ--------------WPDMGVPeyTLPVLTFVRKASYAK-RHA 144
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 998470296 1137 NGPVVIVDRYGGTEAATFCCLSALYRQLEREKCVDVYMYAKLYHMRRPGIWKSQDDFLFLY 1197
Cdd:cd17668   145 VGPVVVHCSAGVGRTGTYIVLDSMLQQIQHEGTVNIFGFLKHIRSQRNYLVQTEEQYVFIH 205
PTPc-N3 cd14600
catalytic domain of tyrosine-protein phosphatase non-receptor type 3; Tyrosine-protein ...
951-1142 1.85e-17

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: 84.13  E-value: 1.85e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 998470296  951 VVSAVKPCNKAKNRSLNLIPIESHRVHITpkpgiDGSDYINATFLQ----GFNRLREFIVTQHPLMDTMADFWQMVWDHN 1026
Cdd:cd14600    32 ITCAKLPQNMDKNRYKDVLPYDATRVVLQ-----GNEDYINASYVNmeipSANIVNKYIATQGPLPHTCAQFWQVVWEQK 106
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 998470296 1027 SQTIVVLSVVDE----KEHpQFWPDTDEEQDYGSFKVKPTGESVappvaeekgalmpgeGGGLPSRDFILQSTQDDYELA 1102
Cdd:cd14600   107 LSLIVMLTTLTErgrtKCH-QYWPDPPDVMEYGGFRVQCHSEDC---------------TIAYVFREMLLTNTQTGEERT 170
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|..
gi 998470296 1103 CRLLLCPGWPQSCSP--LAKAFELVKEVgaRQERDQNGPVVI 1142
Cdd:cd14600   171 VTHLQYVAWPDHGVPddSSDFLEFVNYV--RSKRVENEPVLV 210
PTPc-N6 cd14606
catalytic domain of tyrosine-protein phosphatase non-receptor type 6; Tyrosine-protein ...
956-1064 3.77e-17

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: 83.01  E-value: 3.77e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 998470296  956 KPCNKAKNRSLNLIPIESHRVHITPK-PGIDGSDYINATFLQgfNRL-------REFIVTQHPLMDTMADFWQMVWDHNS 1027
Cdd:cd14606    15 RPENKSKNRYKNILPFDHSRVILQGRdSNIPGSDYINANYVK--NQLlgpdenaKTYIASQGCLEATVNDFWQMAWQENS 92
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 998470296 1028 QTIVVLSVVDEKEHPQ---FWPDTDEEQDYGSFKVKPTGE 1064
Cdd:cd14606    93 RVIVMTTREVEKGRNKcvpYWPEVGMQRAYGPYSVTNCGE 132
PTPc-N12 cd14604
catalytic domain of tyrosine-protein phosphatase non-receptor type 12; Tyrosine-protein ...
907-1064 7.54e-17

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: 82.67  E-value: 7.54e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 998470296  907 LSRYVQSLQTAQVATTGAGDNEKSWSLLERqfKLVTMFKA-KDFNVVSAVKPCNKAKNRSLNLIPIESHRVHITPKPGID 985
Cdd:cd14604     6 LKKFIERVQAMKSTDHNGEDNFASDFMRLR--RLSTKYRTeKIYPTATGEKEENVKKNRYKDILPFDHSRVKLTLKTSSQ 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 998470296  986 GSDYINATFLQGFNRLREFIVTQHPLMDTMADFWQMVWDHNSQTIVVLSVVDE---KEHPQFWPDTDEEQ-DYGSFKVKP 1061
Cdd:cd14604    84 DSDYINANFIKGVYGPKAYIATQGPLANTVIDFWRMIWEYNVAIIVMACREFEmgrKKCERYWPLYGEEPmTFGPFRISC 163

                  ...
gi 998470296 1062 TGE 1064
Cdd:cd14604   164 EAE 166
PHA02746 PHA02746
protein tyrosine phosphatase; Provisional
955-1172 7.92e-17

protein tyrosine phosphatase; Provisional


Pssm-ID: 165113 [Multi-domain]  Cd Length: 323  Bit Score: 83.15  E-value: 7.92e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 998470296  955 VKPCNKAKNRSLNLIPIESHRVHITPKPGI--------DG-----------SDYINATFLQGFNRLREFIVTQHPLMDTM 1015
Cdd:PHA02746   47 LKKENLKKNRFHDIPCWDHSRVVINAHESLkmfdvgdsDGkkievtsednaENYIHANFVDGFKEANKFICAQGPKEDTS 126
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 998470296 1016 ADFWQMVWDHNSQTIVVLSVVDEKEHPQF--W-PDTDEEQDYGSFKVKPTgesvapPVAEEKgalmpgeggGLPSRDFIL 1092
Cdd:PHA02746  127 EDFFKLISEHESQVIVSLTDIDDDDEKCFelWtKEEDSELAFGRFVAKIL------DIIEEL---------SFTKTRLMI 191
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 998470296 1093 QSTQDDYELACRLLLCPGWPQSCSP--LAKAFELVKEVGARQER---------DQNGPVVIVDRYGGTEAATFCCLSALY 1161
Cdd:PHA02746  192 TDKISDTSREIHHFWFPDWPDNGIPtgMAEFLELINKVNEEQAElikqadndpQTLGPIVVHCSAGIGRAGTFCAIDNAL 271
                         250
                  ....*....|.
gi 998470296 1162 RQLEREKCVDV 1172
Cdd:PHA02746  272 EQLEKEKEVCL 282
FN3 cd00063
Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein ...
133-224 8.15e-17

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: 76.77  E-value: 8.15e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 998470296  133 PDPPGIPIVVGFTSRSVDLSWTSsPNSHHSVILHYIIHIRIGEKGDWDTMNKVMTsdNSTNFQVIGLKPFTVYSFRVLAV 212
Cdd:cd00063     1 PSPPTNLRVTDVTSTSVTLSWTP-PEDDGGPITGYVVEYREKGSGDWKEVEVTPG--SETSYTLTGLKPGTEYEFRVRAV 77
                          90
                  ....*....|..
gi 998470296  213 NAIGASKPSKES 224
Cdd:cd00063    78 NGGGESPPSESV 89
R-PTPc-C-1 cd14557
catalytic domain of receptor-type tyrosine-protein phosphatase C, repeat 1; Receptor-type ...
989-1182 2.84e-16

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: 78.72  E-value: 2.84e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 998470296  989 YINATFLQGFNRLREFIVTQHPLMDTMADFWQMVWDHNSQTIVVLSVVDEKEH---PQFWPDTDEEQD-YGSFKVKPTGE 1064
Cdd:cd14557     1 YINASYIDGFKEPRKYIAAQGPKDETVDDFWRMIWEQKSTVIVMVTRCEEGNRnkcAQYWPSMEEGSRaFGDVVVKINEE 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 998470296 1065 SVAPPVAEEKGALMPG-EGGGLPSRDFILQSTQDDYelacrlllcpGWPQSCSPLAKafeLVKEVGARQERdQNGPVVIV 1143
Cdd:cd14557    81 KICPDYIIRKLNINNKkEKGSGREVTHIQFTSWPDH----------GVPEDPHLLLK---LRRRVNAFNNF-FSGPIVVH 146
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|
gi 998470296 1144 DRYGGTEAATFCCLSALYRQLEREKCVDVYMY-AKLYHMR 1182
Cdd:cd14557   147 CSAGVGRTGTYIGIDAMLEGLEAEGRVDVYGYvVKLRRQR 186
PTPc-N1 cd14608
catalytic domain of tyrosine-protein phosphatase non-receptor type 1; Tyrosine-protein ...
945-1197 3.12e-16

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: 80.45  E-value: 3.12e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 998470296  945 KAKDFNVVSAVKPCNKAKNRSLNLIPIESHRVhitpKPGIDGSDYINATFLQGFNRLREFIVTQHPLMDTMADFWQMVWD 1024
Cdd:cd14608    11 EASDFPCRVAKLPKNKNRNRYRDVSPFDHSRI----KLHQEDNDYINASLIKMEEAQRSYILTQGPLPNTCGHFWEMVWE 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 998470296 1025 HNSQTIVVLSVVDEK---EHPQFWPDTDEEQ---DYGSFKVKPTGESVAPPVAeekgalmpgeggglpSRDFILQ--STQ 1096
Cdd:cd14608    87 QKSRGVVMLNRVMEKgslKCAQYWPQKEEKEmifEDTNLKLTLISEDIKSYYT---------------VRQLELEnlTTQ 151
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 998470296 1097 DDYE-LACRLLLCP--GWPQSCSPLAKAFELVKEVGARQErdQNGPVVIVDRYGGTEAATFCCL-SALYRQLEREKCVDV 1172
Cdd:cd14608   152 ETREiLHFHYTTWPdfGVPESPASFLNFLFKVRESGSLSP--EHGPVVVHCSAGIGRSGTFCLAdTCLLLMDKRKDPSSV 229
                         250       260
                  ....*....|....*....|....*..
gi 998470296 1173 YMYAKLYHMR--RPGIWKSQDDFLFLY 1197
Cdd:cd14608   230 DIKKVLLEMRkfRMGLIQTADQLRFSY 256
PHA02747 PHA02747
protein tyrosine phosphatase; Provisional
953-1196 3.44e-16

protein tyrosine phosphatase; Provisional


Pssm-ID: 165114 [Multi-domain]  Cd Length: 312  Bit Score: 81.20  E-value: 3.44e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 998470296  953 SAVKPCNKAKNRSLNLIPIESHRVHITPKPGiDGSDYINATFLQGFNRLREFIVTQHPLMDTMADFWQMVWDHNSQTIVV 1032
Cdd:PHA02747   45 NFEKPENQPKNRYWDIPCWDHNRVILDSGGG-STSDYIHANWIDGFEDDKKFIATQGPFAETCADFWKAVWQEHCSIIVM 123
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 998470296 1033 LS----VVDEKEHPQFW-PDTDEEQDYGSFKVKPTGESVAPPVAeekgalmpgegggLPSRDFILQSTQDDYELAcrLLL 1107
Cdd:PHA02747  124 LTptkgTNGEEKCYQYWcLNEDGNIDMEDFRIETLKTSVRAKYI-------------LTLIEITDKILKDSRKIS--HFQ 188
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 998470296 1108 CPGWPQSCSP--------LAKAFELVKEVGARQERDQNG---PVVIVDRYGGTEAATFCCLSALYRQLEREKCVDVYMYA 1176
Cdd:PHA02747  189 CSEWFEDETPsdhpdfikFIKIIDINRKKSGKLFNPKDAllcPIVVHCSDGVGKTGIFCAVDICLNQLVKRKAICLAKTA 268
                         250       260
                  ....*....|....*....|.
gi 998470296 1177 -KLYHMRRPGIwKSQDDFLFL 1196
Cdd:PHA02747  269 eKIREQRHAGI-MNFDDYLFI 288
R-PTPc-typeIIb-1 cd14555
catalytic domain of type IIb (or R2B) subfamily receptor-type tyrosine-protein phosphatases, ...
989-1197 3.52e-16

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: 78.42  E-value: 3.52e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 998470296  989 YINATFLQGFNRLREFIVTQHPLMDTMADFWQMVWDHNSQTIVV---LSVVDEKEHPQFWPDTDEEqdYGSFKV-----K 1060
Cdd:cd14555     1 YINANYIDGYHRPNHYIATQGPMQETVYDFWRMVWQENSASIVMvtnLVEVGRVKCSRYWPDDTEV--YGDIKVtlvetE 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 998470296 1061 PTGESVAppvaeekgalmpgeggglpsRDFILQSTQDDYELACRLLLCPGWPQSCSPLAKA--FELVKEVGARQERDQnG 1138
Cdd:cd14555    79 PLAEYVV--------------------RTFALERRGYHEIREVRQFHFTGWPDHGVPYHATglLGFIRRVKASNPPSA-G 137
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 998470296 1139 PVVIVDRYGGTEAATFCCLSALYRQLEREKCVDVYMYAKLYHMRRPGIWKSQDDFLFLY 1197
Cdd:cd14555   138 PIVVHCSAGAGRTGCYIVIDIMLDMAEREGVVDIYNCVKELRSRRVNMVQTEEQYIFIH 196
PTPc-N5 cd14613
catalytic domain of tyrosine-protein phosphatase non-receptor type 5; Tyrosine-protein ...
962-1197 3.93e-16

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: 79.91  E-value: 3.93e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 998470296  962 KNRSLNLIPIESHRVH-ITPKPGIDGSDYINATFLQGFN-RLREFIVTQHPLMDTMADFWQMVWDHNSQTIVVLSVVDEK 1039
Cdd:cd14613    28 KNRYKTILPNPHSRVClTSPDQDDPLSSYINANYIRGYGgEEKVYIATQGPTVNTVGDFWRMVWQERSPIIVMITNIEEM 107
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 998470296 1040 EHP--QFWPdtDEEQDYGSFKVkptgeSVAPPVAEEKGALmpgeggglpsRDFILQSTQDDYELacRLLLCPGWPQSCSP 1117
Cdd:cd14613   108 NEKctEYWP--EEQVTYEGIEI-----TVKQVIHADDYRL----------RLITLKSGGEERGL--KHYWYTSWPDQKTP 168
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 998470296 1118 --LAKAFELVKEV--GARQERDQNGPVVIVDRYGGTEAATFCCLSALYRQLEREKCVDVYMYAKLYHMRRPGIWKSQDDF 1193
Cdd:cd14613   169 dnAPPLLQLVQEVeeARQQAEPNCGPVIVHCSAGIGRTGCFIATSICCKQLRNEGVVDILRTTCQLRLDRGGMIQTCEQY 248

                  ....
gi 998470296 1194 LFLY 1197
Cdd:cd14613   249 QFVH 252
R-PTPc-K-2 cd14636
PTP domain of receptor-type tyrosine-protein phosphatase K, repeat 2; Receptor-type ...
989-1197 4.17e-16

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: 78.53  E-value: 4.17e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 998470296  989 YINATFLQGFNRLREFIVTQHPLMDTMADFWQMVWDHNSQTIVVLSVVDEKEH-PQFWPDTDEEQdYGSFKVKPTGESVA 1067
Cdd:cd14636     1 YINAALMDSYRQPAAFIVTQHPLPNTVKDFWRLVYDYGCTSIVMLNEVDLAQGcPQYWPEEGMLR-YGPIQVECMSCSMD 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 998470296 1068 PPVAeekgalmpgeggglpSRDFI---LQSTQDDYeLACRLLLCPGWPQSCS-PLAKA--FELVKEVGARQER--DQNGP 1139
Cdd:cd14636    80 CDVI---------------SRIFRicnLTRPQEGY-LMVQQFQYLGWASHREvPGSKRsfLKLILQVEKWQEEcdEGEGR 143
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 998470296 1140 VVIVDRYGGTEAATFCCLSALYRQLEREKCVDVYMYAKLYHMRRPGIWKSQDDFLFLY 1197
Cdd:cd14636   144 TIIHCLNGGGRSGMFCAISIVCEMIKRQNVVDVFHAVKTLRNSKPNMVETPEQYRFCY 201
R-PTP-N2 cd14610
PTP-like domain of receptor-type tyrosine-protein phosphatase N2; Receptor-type ...
926-1195 7.23e-16

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: 79.72  E-value: 7.23e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 998470296  926 DNEKSWSLLERQFKLVTMFKAKDFNVVSAVKPCNKAKNRSLNLIPIESHRVHITPKPGIDGSDYINATFLQGFN-RLREF 1004
Cdd:cd14610    11 DHLKNKNRLEKEWEALCAYQAEPNATNVAQREENVQKNRSLAVLPYDHSRIILKAENSHSHSDYINASPIMDHDpRNPAY 90
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 998470296 1005 IVTQHPLMDTMADFWQMVWDHNSQTIVVLSVVDE---KEHPQFWPDTDEEQdYGSFKVKPTGESVAppvAEEkgalmpge 1081
Cdd:cd14610    91 IATQGPLPATVADFWQMVWESGCVVIVMLTPLAEngvKQCYHYWPDEGSNL-YHIYEVNLVSEHIW---CED-------- 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 998470296 1082 gggLPSRDFILQSTQDDYELACRLLLCPGW-----PQSCSPLakaFELVKEVGaRQERDQNGPVVIVDRYGGTEAATFCC 1156
Cdd:cd14610   159 ---FLVRSFYLKNLQTNETRTVTQFHFLSWndqgvPASTRSL---LDFRRKVN-KCYRGRSCPIIVHCSDGAGRSGTYIL 231
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|..
gi 998470296 1157 LSALYRQLER-EKCVDVymYAKLYHMR--RPGIWKSQDDFLF 1195
Cdd:cd14610   232 IDMVLNKMAKgAKEIDI--AATLEHLRdqRPGMVQTKEQFEF 271
R-PTPc-K-1 cd14631
catalytic domain of receptor-type tyrosine-protein phosphatase K, repeat 1; Receptor-type ...
975-1197 8.59e-16

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: 77.75  E-value: 8.59e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 998470296  975 RVHITPKPGIDGSDYINATFLQGFNRLREFIVTQHPLMDTMADFWQMVWDHNSQTIVVLSVVDEKEHP---QFWPDTDEE 1051
Cdd:cd14631     1 RVILQPVEDDPSSDYINANYIDGYQRPSHYIATQGPVHETVYDFWRMIWQEQSACIVMVTNLVEVGRVkcyKYWPDDTEV 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 998470296 1052 qdYGSFKV-----KPTGESVAppvaeekgalmpgeggglpsRDFILQSTQDDYELACRLLLCPGWPQSCSPLAKA--FEL 1124
Cdd:cd14631    81 --YGDFKVtcvemEPLAEYVV--------------------RTFTLERRGYNEIREVKQFHFTGWPDHGVPYHATglLSF 138
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 998470296 1125 VKEVGARQERDQnGPVVIVDRYGGTEAATFCCLSALYRQLEREKCVDVYMYAKLYHMRRPGIWKSQDDFLFLY 1197
Cdd:cd14631   139 IRRVKLSNPPSA-GPIVVHCSAGAGRTGCYIVIDIMLDMAEREGVVDIYNCVKALRSRRINMVQTEEQYIFIH 210
FN3 cd00063
Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein ...
335-430 1.36e-15

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: 73.30  E-value: 1.36e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 998470296  335 PSSPVNLTAVRVTDTTVRLKWREPVRPNGVLQGYHVYFQPSRNGSSQQQRKTVShpqPVEEYMLSGLKPFSFYDIWVKAF 414
Cdd:cd00063     1 PSPPTNLRVTDVTSTSVTLSWTPPEDDGGPITGYVVEYREKGSGDWKEVEVTPG---SETSYTLTGLKPGTEYEFRVRAV 77
                          90
                  ....*....|....*.
gi 998470296  415 TQQHLGESSNLLKVQT 430
Cdd:cd00063    78 NGGGESPPSESVTVTT 93
R-PTPc-U-2 cd14637
PTP domain of receptor-type tyrosine-protein phosphatase U, repeat 2; Receptor-type ...
989-1197 1.61e-15

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: 76.87  E-value: 1.61e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 998470296  989 YINATFLQGFNRLREFIVTQHPLMDTMADFWQMVWDHNSQTIVVLSVVDEKEHP----QFWPDTDEEQdYGSFKVkptgE 1064
Cdd:cd14637     1 YINAALTDSYTRSAAFIVTLHPLQNTTTDFWRLVYDYGCTSVVMLNQLNQSNSAwpclQYWPEPGLQQ-YGPMEV----E 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 998470296 1065 SVAPPVAEEkgalmpgegggLPSRDFILQST---QDDYELACRLLLCPGWPQSCSPLAK-AF-ELVKEVGARQERDQNGP 1139
Cdd:cd14637    76 FVSGSADED-----------IVTRLFRVQNItrlQEGHLMVRHFQFLRWSAYRDTPDSKkAFlHLLASVEKWQRESGEGR 144
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 998470296 1140 VVIVDRYGGTEAATFCCLSALYRQLEREKCVDVYMYAKLYHMRRPGIWKSQDDFLFLY 1197
Cdd:cd14637   145 TVVHCLNGGGRSGTYCASAMILEMIRCHNIVDVFYAVKTLRNYKPNMVETLEQYRFCY 202
R-PTPc-U-1 cd14632
catalytic domain of receptor-type tyrosine-protein phosphatase U, repeat 1; Receptor-type ...
989-1197 2.21e-15

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: 76.24  E-value: 2.21e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 998470296  989 YINATFLQGFNRLREFIVTQHPLMDTMADFWQMVWDHNSQTIVVLSVVDE---KEHPQFWPDTDEEqdYGSFKVK-PTGE 1064
Cdd:cd14632     1 YINANYIDGYHRSNHFIATQGPKQEMVYDFWRMVWQEHCSSIVMITKLVEvgrVKCSKYWPDDSDT--YGDIKITlLKTE 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 998470296 1065 SVAPPVAeekgalmpgeggglpsRDFILQSTQDDYELACRLLLCPGWPQSCSPLAKA--FELVKEVGARQERDQnGPVVI 1142
Cdd:cd14632    79 TLAEYSV----------------RTFALERRGYSARHEVKQFHFTSWPEHGVPYHATglLAFIRRVKASTPPDA-GPVVV 141
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 998470296 1143 VDRYGGTEAATFCCLSALYRQLEREKCVDVYMYAKLYHMRRPGIWKSQDDFLFLY 1197
Cdd:cd14632   142 HCSAGAGRTGCYIVLDVMLDMAECEGVVDIYNCVKTLCSRRINMIQTEEQYIFIH 196
PTP_YopH-like cd14559
YopH and related bacterial protein tyrosine phosphatases; Yersinia outer protein H (YopH) ...
689-885 3.24e-15

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: 76.28  E-value: 3.24e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 998470296  689 INANYIDGYHKSRAfIGTQGPLPATFDDYWRMVWEQRVCIIIMITNLVERGRRKCDMYWpkEGTETYGIIQVKlvQEIVM 768
Cdd:cd14559    18 LNANRVQIGNKNVA-IACQYPKNEQLEDHLKMLADNRTPCLVVLASNKDIQRKGLPPYF--RQSGTYGSVTVK--SKKTG 92
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 998470296  769 ATYTIRTFAIKNIKVKKKQASER-TVYQYHYTNWPDHG-VPDHPLPVLS--------------FVAKSSAANPPAAGPMI 832
Cdd:cd14559    93 KDELVDGLKADMYNLKITDGNKTiTIPVVHVTNWPDHTaISSEGLKELAdlvnksaeekrnfyKSKGSSAINDKNKLLPV 172
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....
gi 998470296  833 VHCSAGVGRTGTYIvldAMLRQMRQRQSVNVYGFLRHIRQQRN-YLVQTEEQYV 885
Cdd:cd14559   173 IHCRAGVGRTGQLA---AAMELNKSPNNLSVEDIVSDMRTSRNgKMVQKDEQLD 223
FN3 cd00063
Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein ...
236-330 6.39e-15

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: 71.37  E-value: 6.39e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 998470296  236 GKPTIVHAQNTSSSSVRIQWTAPArhTIHGEFEGYRITYRPRDrtQEESREIILRDSKQTQYTIRNLETFTQYLVSLQVF 315
Cdd:cd00063     2 SPPTNLRVTDVTSTSVTLSWTPPE--DDGGPITGYVVEYREKG--SGDWKEVEVTPGSETSYTLTGLKPGTEYEFRVRAV 77
                          90
                  ....*....|....*.
gi 998470296  316 NPAGRG-PAVVVPVMT 330
Cdd:cd00063    78 NGGGESpPSESVTVTT 93
fn3 pfam00041
Fibronectin type III domain;
236-322 1.21e-14

Fibronectin type III domain;


Pssm-ID: 394996 [Multi-domain]  Cd Length: 85  Bit Score: 70.14  E-value: 1.21e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 998470296   236 GKPTIVHAQNTSSSSVRIQWTAParHTIHGEFEGYRITYRPRDRTQEESREIILRDskQTQYTIRNLETFTQYLVSLQVF 315
Cdd:pfam00041    1 SAPSNLTVTDVTSTSLTVSWTPP--PDGNGPITGYEVEYRPKNSGEPWNEITVPGT--TTSVTLTGLKPGTEYEVRVQAV 76

                   ....*..
gi 998470296   316 NPAGRGP 322
Cdd:pfam00041   77 NGGGEGP 83
FN3 smart00060
Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, ...
133-218 1.34e-14

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: 70.34  E-value: 1.34e-14
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 998470296    133 PDPPGIPIVVGFTSRSVDLSWTSSPNSHHSvilHYIIHIRIGEKGDWDTMNKVMTSDNSTNFQVIGLKPFTVYSFRVLAV 212
Cdd:smart00060    1 PSPPSNLRVTDVTSTSVTLSWEPPPDDGIT---GYIVGYRVEYREEGSEWKEVNVTPSSTSYTLTGLKPGTEYEFRVRAV 77

                    ....*.
gi 998470296    213 NAIGAS 218
Cdd:smart00060   78 NGAGEG 83
R-PTPc-A-E-1 cd14551
catalytic domain of receptor-type tyrosine-protein phosphatase A and E, repeat 1; ...
989-1198 1.37e-14

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: 73.79  E-value: 1.37e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 998470296  989 YINATFLQGFNRLREFIVTQHPLMDTMADFWQMVWDHNSQTIVVLSVVDEKEH---PQFWPDTDEEQdYGSFKVKptges 1065
Cdd:cd14551     1 YINASYIDGYQEKNKFIAAQGPKDETVNDFWRMIWEQGSATIVMVTNLKERKEkkcSQYWPDQGCWT-YGNLRVR----- 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 998470296 1066 vappvAEEKGALMpgeggGLPSRDFILQSTQDDY-ELACRL---LLCPGWPQ---SCSPLAKAFELVKEVGARQERDqnG 1138
Cdd:cd14551    75 -----VEDTVVLV-----DYTTRKFCIQKVNRGIgEKRVRLvtqFHFTSWPDfgvPFTPIGMLKFLKKVKSANPPRA--G 142
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 998470296 1139 PVVIVDRYGGTEAATFCCLSALYRQLEREKCVDVYMYAKLYHMRRPGIWKSQDDFLFLYR 1198
Cdd:cd14551   143 PIVVHCSAGVGRTGTFIVIDAMLDMMHAEGKVDVFGFVSRIRQQRSQMVQTDMQYVFIYQ 202
PTP_fungal cd18533
fungal protein tyrosine phosphatases; This subfamily contains Saccharomyces cerevisiae ...
989-1197 1.40e-14

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: 74.21  E-value: 1.40e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 998470296  989 YINATFLQ-GFNRLREFIVTQHPLMDTMADFWQMVWdhNSQTIVVLSVVDEKEHP-----QFWPDTDEEQDYGSFKVKpt 1062
Cdd:cd18533     1 YINASYITlPGTSSKRYIATQGPLPATIGDFWKMIW--QNNVGVIVMLTPLVENGrekcdQYWPSGEYEGEYGDLTVE-- 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 998470296 1063 gesvappVAEEKGalmpGEGGGLPSRDFILQStqDDYELACRL-LLCPGWPQSCSPLAKA--FELVKEVGARQERDQNGP 1139
Cdd:cd18533    77 -------LVSEEE----NDDGGFIVREFELSK--EDGKVKKVYhIQYKSWPDFGVPDSPEdlLTLIKLKRELNDSASLDP 143
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 998470296 1140 VVIVD------RYGgteaaTFCCLSALYRQLER--------EKCVDVyMYAKLYHMR--RPGIWKSQDDFLFLY 1197
Cdd:cd18533   144 PIIVHcsagvgRTG-----TFIALDSLLDELKRglsdsqdlEDSEDP-VYEIVNQLRkqRMSMVQTLRQYIFLY 211
R-PTPc-R cd14611
catalytic domain of receptor-type tyrosine-protein phosphatase R; Receptor-type ...
962-1197 1.88e-14

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: 74.18  E-value: 1.88e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 998470296  962 KNRSLNLIPIESHRVHITPKPGIDG-SDYINATFLQGF-NRLREFIVTQHPLMDTMADFWQMVWDHNSQTIVVLSVVDEK 1039
Cdd:cd14611     2 KNRYKTILPNPHSRVCLKPKNSNDSlSTYINANYIRGYgGKEKAFIATQGPMINTVNDFWQMVWQEDSPVIVMITKLKEK 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 998470296 1040 EHP--QFWPdtDEEQDYGsfKVKPTGESVAPPVAEEKGALMPGEGGGLPSRDFILQSTQDDYELacrlllcpgwPQSCSP 1117
Cdd:cd14611    82 NEKcvLYWP--EKRGIYG--KVEVLVNSVKECDNYTIRNLTLKQGSQSRSVKHYWYTSWPDHKT----------PDSAQP 147
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 998470296 1118 LAKAFELVKEvgARQERDQNGPVVI-----VDRYGGTEAATFCClsalyRQLEREKCVDVYMYAKLYHMRRPGIWKSQDD 1192
Cdd:cd14611   148 LLQLMLDVEE--DRLASPGRGPVVVhcsagIGRTGCFIATTIGC-----QQLKEEGVVDVLSIVCQLRVDRGGMVQTSEQ 220

                  ....*
gi 998470296 1193 FLFLY 1197
Cdd:cd14611   221 YEFVH 225
PTPc_motif smart00404
Protein tyrosine phosphatase, catalytic domain motif;
1103-1198 2.68e-14

Protein tyrosine phosphatase, catalytic domain motif;


Pssm-ID: 214649 [Multi-domain]  Cd Length: 105  Bit Score: 70.08  E-value: 2.68e-14
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 998470296   1103 CRLLLCPGW-----PQSCSPLAKAFELVKEVgaRQERDQNGPVVIVDRYGGTEAATFCCLSALYRQLERE-KCVDVYMYA 1176
Cdd:smart00404    2 VKHYHYTGWpdhgvPESPDSILELLRAVKKN--LNQSESSGPVVVHCSAGVGRTGTFVAIDILLQQLEAEaGEVDIFDTV 79
                            90       100
                    ....*....|....*....|..
gi 998470296   1177 KLYHMRRPGIWKSQDDFLFLYR 1198
Cdd:smart00404   80 KELRSQRPGMVQTEEQYLFLYR 101
PTPc_DSPc smart00012
Protein tyrosine phosphatase, catalytic domain, undefined specificity; Protein tyrosine ...
1103-1198 2.68e-14

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: 70.08  E-value: 2.68e-14
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 998470296   1103 CRLLLCPGW-----PQSCSPLAKAFELVKEVgaRQERDQNGPVVIVDRYGGTEAATFCCLSALYRQLERE-KCVDVYMYA 1176
Cdd:smart00012    2 VKHYHYTGWpdhgvPESPDSILELLRAVKKN--LNQSESSGPVVVHCSAGVGRTGTFVAIDILLQQLEAEaGEVDIFDTV 79
                            90       100
                    ....*....|....*....|..
gi 998470296   1177 KLYHMRRPGIWKSQDDFLFLYR 1198
Cdd:smart00012   80 KELRSQRPGMVQTEEQYLFLYR 101
fn3 pfam00041
Fibronectin type III domain;
336-423 3.61e-14

Fibronectin type III domain;


Pssm-ID: 394996 [Multi-domain]  Cd Length: 85  Bit Score: 68.98  E-value: 3.61e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 998470296   336 SSPVNLTAVRVTDTTVRLKWREPVRPNGVLQGYHVYFQPSRNGSSQQQRKTVSHPqpvEEYMLSGLKPFSFYDIWVKAFT 415
Cdd:pfam00041    1 SAPSNLTVTDVTSTSLTVSWTPPPDGNGPITGYEVEYRPKNSGEPWNEITVPGTT---TSVTLTGLKPGTEYEVRVQAVN 77

                   ....*...
gi 998470296   416 QQHLGESS 423
Cdd:pfam00041   78 GGGEGPPS 85
PTPc-N13 cd14597
catalytic domain of tyrosine-protein phosphatase non-receptor type 13; Tyrosine-protein ...
959-1048 3.64e-14

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: 73.33  E-value: 3.64e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 998470296  959 NKAKNRSLNLIPIESHRVHItpkpGIDGsDYINATFLQGFNRLREF--IVTQHPLMDTMADFWQMVWDHNSQTIVVLS-- 1034
Cdd:cd14597     3 NRKKNRYKNILPYDTTRVPL----GDEG-GYINASFIKMPVGDEEFvyIACQGPLPTTVADFWQMVWEQKSTVIAMMTqe 77
                          90
                  ....*....|....*
gi 998470296 1035 VVDEKEHPQ-FWPDT 1048
Cdd:cd14597    78 VEGGKIKCQrYWPEI 92
FN3 smart00060
Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, ...
236-321 5.03e-14

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: 68.41  E-value: 5.03e-14
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 998470296    236 GKPTIVHAQNTSSSSVRIQWTAPArhtiHGEFEGYRITYRPRDRTQEESREIILRDSKQTQYTIRNLETFTQYLVSLQVF 315
Cdd:smart00060    2 SPPSNLRVTDVTSTSVTLSWEPPP----DDGITGYIVGYRVEYREEGSEWKEVNVTPSSTSYTLTGLKPGTEYEFRVRAV 77

                    ....*.
gi 998470296    316 NPAGRG 321
Cdd:smart00060   78 NGAGEG 83
PTPc-N1_2 cd14545
catalytic domain of tyrosine-protein phosphatase non-receptor type 1 and type 2; ...
962-1060 5.20e-14

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: 72.81  E-value: 5.20e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 998470296  962 KNRSLNLIPIESHRVHITPkpgiDGSDYINATFLQGFNRLREFIVTQHPLMDTMADFWQMVWDHNSQTIVVLSVVDEKEH 1041
Cdd:cd14545     3 RYRDRDPYDHDRSRVKLKQ----GDNDYINASLVEVEEAKRSYILTQGPLPNTSGHFWQMVWEQNSKAVIMLNKLMEKGQ 78
                          90       100
                  ....*....|....*....|....*.
gi 998470296 1042 P---QFWPdTDEEQDY----GSFKVK 1060
Cdd:cd14545    79 IkcaQYWP-QGEGNAMifedTGLKVT 103
PTPc-N2 cd14607
catalytic domain of tyrosine-protein phosphatase non-receptor type 2; Tyrosine-protein ...
945-1197 8.86e-14

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: 72.69  E-value: 8.86e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 998470296  945 KAKDFNVVSAVKPCNKAKNRSLNLIPIESHRVHITPKPgidgSDYINATFLQGFNRLREFIVTQHPLMDTMADFWQMVWD 1024
Cdd:cd14607    10 ESHDYPHRVAKYPENRNRNRYRDVSPYDHSRVKLQNTE----NDYINASLVVIEEAQRSYILTQGPLPNTCCHFWLMVWQ 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 998470296 1025 HNSQTIVVLSVVDEKEH---PQFWPDTDEE----QDYGsFKVKPTGESVAPPVAEEKGALMPGEGGGLPSRDFILQSTQD 1097
Cdd:cd14607    86 QKTKAVVMLNRIVEKDSvkcAQYWPTDEEEvlsfKETG-FSVKLLSEDVKSYYTVHLLQLENINSGETRTISHFHYTTWP 164
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 998470296 1098 DYelacrlllcpGWPQSCSPLAKAFELVKEVGARQErdQNGPVVIVDRYGGTEAATFCCLSALYRQLEREKCVDVYMYAK 1177
Cdd:cd14607   165 DF----------GVPESPASFLNFLFKVRESGSLSP--EHGPAVVHCSAGIGRSGTFSLVDTCLVLMEKKDPDSVDIKQV 232
                         250       260
                  ....*....|....*....|..
gi 998470296 1178 LYHMR--RPGIWKSQDDFLFLY 1197
Cdd:cd14607   233 LLDMRkyRMGLIQTPDQLRFSY 254
PHA02742 PHA02742
protein tyrosine phosphatase; Provisional
959-1060 9.59e-14

protein tyrosine phosphatase; Provisional


Pssm-ID: 165109 [Multi-domain]  Cd Length: 303  Bit Score: 73.50  E-value: 9.59e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 998470296  959 NKAKNRSLNLIPIESHRVHITPKPGidGSDYINATFLQGFNRLREFIVTQHPLMDTMADFWQMVWDHNSQTIVVLSVVDE 1038
Cdd:PHA02742   52 NMKKCRYPDAPCFDRNRVILKIEDG--GDDFINASYVDGHNAKGRFICTQAPLEETALDFWQAIFQDQVRVIVMITKIME 129
                          90       100
                  ....*....|....*....|....*.
gi 998470296 1039 KE----HPQFWPDTDEEQDYGSFKVK 1060
Cdd:PHA02742  130 DGkeacYPYWMPHERGKATHGEFKIK 155
FN3 COG3401
Fibronectin type 3 domain [General function prediction only];
292-510 1.23e-13

Fibronectin type 3 domain [General function prediction only];


Pssm-ID: 442628 [Multi-domain]  Cd Length: 603  Bit Score: 75.42  E-value: 1.23e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 998470296  292 SKQTQYTIRNLETFTQYLVSLQVFNPAGRG-PAVVVPVMTDEGVPSSPVNLTAVRVTDTTVRLKWREPvrPNGVLQGYHV 370
Cdd:COG3401   189 STTLVDGGGDIEPGTTYYYRVAATDTGGESaPSNEVSVTTPTTPPSAPTGLTATADTPGSVTLSWDPV--TESDATGYRV 266
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 998470296  371 YfqpsRNGSSQQQRKTVSHPQpVEEYMLSGLKPFSFYDIWVKAFTQQHL-GESSNLLKVQTDVQGPSAPVIVNLTCQSLD 449
Cdd:COG3401   267 Y----RSNSGDGPFTKVATVT-TTSYTDTGLTNGTTYYYRVTAVDAAGNeSAPSNVVSVTTDLTPPAAPSGLTATAVGSS 341
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 998470296  450 SLFLQWErpQTYYNRVDYYFVHYRSEEAWSFEEIAMAANDrlehVMFI-PNLTANTLYEVKV 510
Cdd:COG3401   342 SITLSWT--ASSDADVTGYNVYRSTSGGGTYTKIAETVTT----TSYTdTGLTPGTTYYYKV 397
R-PTP-N-N2 cd14546
PTP-like domain of receptor-type tyrosine-protein phosphatase-like N and N2; Receptor-type ...
989-1197 2.32e-13

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: 70.55  E-value: 2.32e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 998470296  989 YINATFLQGFN-RLREFIVTQHPLMDTMADFWQMVWDHNSQTIVVLSVVDEKEHPQ---FWPDTDEEQdYGSFKVKPTGE 1064
Cdd:cd14546     1 YINASTIYDHDpRNPAYIATQGPLPHTIADFWQMIWEQGCVVIVMLTRLQENGVKQcarYWPEEGSEV-YHIYEVHLVSE 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 998470296 1065 SVAppvaeekgalmpgeggglpSRDFILQS-------TQDDYELACRLLLcpGWPQSCSPL-AKAF-ELVKEVGaRQERD 1135
Cdd:cd14546    80 HIW-------------------CDDYLVRSfylknlqTSETRTVTQFHFL--SWPDEGIPAsAKPLlEFRRKVN-KSYRG 137
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 998470296 1136 QNGPVVIVDRYGGTEAATFCCLS-ALYRQLEREKCVDVymYAKLYHMR--RPGIWKSQDDFLFLY 1197
Cdd:cd14546   138 RSCPIVVHCSDGAGRTGTYILIDmVLNRMAKGAKEIDI--AATLEHLRdqRPGMVKTKDQFEFVL 200
PTPc-N14 cd14599
catalytic domain of tyrosine-protein phosphatase non-receptor type 14; Tyrosine-protein ...
953-1059 4.20e-13

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: 71.18  E-value: 4.20e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 998470296  953 SAVKPCNKAKNRSLNLIPIESHRVHITPKPGiDGSDYINATFLQGFNRLRE--FIVTQHPLMDTMADFWQMVWDHNSQTI 1030
Cdd:cd14599    32 TATLPENAERNRIREVVPYEENRVELVPTKE-NNTGYINASHIKVTVGGEEwhYIATQGPLPHTCHDFWQMVWEQGVNVI 110
                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 998470296 1031 VVLSVVDE----KEHpQFWPDTDEEQD---YGSFKV 1059
Cdd:cd14599   111 AMVTAEEEggrsKSH-RYWPKLGSKHSsatYGKFKV 145
PTPc-N22 cd14602
catalytic domain of tyrosine-protein phosphatase non-receptor type 22; Tyrosine-protein ...
962-1197 5.36e-13

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: 69.87  E-value: 5.36e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 998470296  962 KNRSLNLIPIESHRVHITPKPGIDGSDYINATFLQGFNRLREFIVTQHPLMDTMADFWQMVWDHNSQTIVVLSVVDE--- 1038
Cdd:cd14602     1 KNRYKDILPYDHSRVELSLITSDEDSDYINANFIKGVYGPRAYIATQGPLSTTLLDFWRMIWEYSVLIIVMACMEFEmgk 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 998470296 1039 KEHPQFWPDTDEEQ-DYGSFKVKPTGEsvappvaEEKGalmpgeggglpsrDFILQSTQDDYELACRLLL---CPGWPQS 1114
Cdd:cd14602    81 KKCERYWAEPGEMQlEFGPFSVTCEAE-------KRKS-------------DYIIRTLKVKFNSETRTIYqfhYKNWPDH 140
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 998470296 1115 CSP--LAKAFELVKEVGARQErDQNGPVVIVDRYGGTEAATFCCLSALYRQLER---EKCVDVYMYAKLYHMRRPGIWKS 1189
Cdd:cd14602   141 DVPssIDPILELIWDVRCYQE-DDSVPICIHCSAGCGRTGVICAIDYTWMLLKDgiiPENFSVFSLIQEMRTQRPSLVQT 219

                  ....*...
gi 998470296 1190 QDDFLFLY 1197
Cdd:cd14602   220 KEQYELVY 227
FN3 smart00060
Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, ...
335-420 1.32e-12

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: 64.56  E-value: 1.32e-12
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 998470296    335 PSSPVNLTAVRVTDTTVRLKWREPVRPNGVlqGYHVYFQPSRNGSSQQQrKTVSHPQPVEEYMLSGLKPFSFYDIWVKAF 414
Cdd:smart00060    1 PSPPSNLRVTDVTSTSVTLSWEPPPDDGIT--GYIVGYRVEYREEGSEW-KEVNVTPSSTSYTLTGLKPGTEYEFRVRAV 77

                    ....*.
gi 998470296    415 TQQHLG 420
Cdd:smart00060   78 NGAGEG 83
PHA02738 PHA02738
hypothetical protein; Provisional
959-1062 1.59e-12

hypothetical protein; Provisional


Pssm-ID: 222923 [Multi-domain]  Cd Length: 320  Bit Score: 69.95  E-value: 1.59e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 998470296  959 NKAKNRSLNLIPIESHRVhITPKPGIDGsDYINATFLQGFNRLREFIVTQHPLMDTMADFWQMVWDHNSQTIVVLSVVDE 1038
Cdd:PHA02738   49 NRKLNRYLDAVCFDHSRV-ILPAERNRG-DYINANYVDGFEYKKKFICGQAPTRQTCYDFYRMLWMEHVQIIVMLCKKKE 126
                          90       100
                  ....*....|....*....|....*...
gi 998470296 1039 KEHPQ---FWPDTDEEQ-DYGSFKVKPT 1062
Cdd:PHA02738  127 NGREKcfpYWSDVEQGSiRFGKFKITTT 154
PTPc_plant_PTP1 cd17658
protein tyrosine phosphatase 1 from Arabidopsis thaliana and similar plant PTPs; Arabidopsis ...
989-1197 1.81e-12

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: 67.87  E-value: 1.81e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 998470296  989 YINATFLQ--GFNRLREFIVTQHPLMDTMADFWQMVWDHNSQTIVVL-SVVD----EKEHPQFWPDTDEEQDYGSFKVKP 1061
Cdd:cd17658     1 YINASLVEtpASESLPKFIATQGPLPHTFEDFWEMVIQQRCPVIIMLtRLVDnystAKCADYFPAEENESREFGRISVTN 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 998470296 1062 TGESVAppvaeekgalmpgeGGGLPSRDFILQSTQDDYELACRL-LLCPGWPQSCSPLAKAF--ELVKEVgaRQERDQNG 1138
Cdd:cd17658    81 KKLKHS--------------QHSITLRVLEVQYIESEEPPLSVLhIQYPEWPDHGVPKDTRSvrELLKRL--YGIPPSAG 144
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 998470296 1139 PVVIVDRYGGTEAATFCCLS-ALYRQLERE-KCVDVYMYAKLYHMRRPGIWKSQDDFLFLY 1197
Cdd:cd17658   145 PIVVHCSAGIGRTGAYCTIHnTIRRILEGDmSAVDLSKTVRKFRSQRIGMVQTQDQYIFCY 205
fn3 pfam00041
Fibronectin type III domain;
134-221 7.62e-12

Fibronectin type III domain;


Pssm-ID: 394996 [Multi-domain]  Cd Length: 85  Bit Score: 62.43  E-value: 7.62e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 998470296   134 DPPGIPIVVGFTSRSVDLSWTSsPNSHHSVILHYIIHIRigEKGDWDTMNKVMTSDNSTNFQVIGLKPFTVYSFRVLAVN 213
Cdd:pfam00041    1 SAPSNLTVTDVTSTSLTVSWTP-PPDGNGPITGYEVEYR--PKNSGEPWNEITVPGTTTSVTLTGLKPGTEYEVRVQAVN 77

                   ....*...
gi 998470296   214 AIGASKPS 221
Cdd:pfam00041   78 GGGEGPPS 85
PTPc-N22_18_12 cd14542
catalytic domain of tyrosine-protein phosphatase non-receptor type 22, type 18 and type 12; ...
989-1065 5.06e-11

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: 63.60  E-value: 5.06e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 998470296  989 YINATFLQGFNRLREFIVTQHPLMDTMADFWQMVWDHNSQTIVVlsVVDEKEH-----PQFWPDTDEEQ-DYGSFKVKPT 1062
Cdd:cd14542     1 YINANFIKGVSGSKAYIATQGPLPNTVLDFWRMIWEYNVQVIVM--ACREFEMgkkkcERYWPEEGEEQlQFGPFKISLE 78

                  ...
gi 998470296 1063 GES 1065
Cdd:cd14542    79 KEK 81
PTPc-N4 cd14601
catalytic domain of tyrosine-protein phosphatase non-receptor type 4; Tyrosine-protein ...
988-1059 7.68e-11

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: 63.04  E-value: 7.68e-11
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 998470296  988 DYINATFLQ----GFNRLREFIVTQHPLMDTMADFWQMVWDHNSQTIVVLSVVDEK---EHPQFWPDTDEEQDYGSFKV 1059
Cdd:cd14601     1 DYINANYINmeipSSSIINRYIACQGPLPNTCSDFWQMTWEQGSSMVVMLTTQVERgrvKCHQYWPEPSGSSSYGGFQV 79
FN3 cd00063
Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein ...
435-511 9.38e-10

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: 56.74  E-value: 9.38e-10
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 998470296  435 PSAPVIVNLTCQSLDSLFLQWERPQTYYNRVDYYFVHYRSEEAWSFEEIAMAANDRLEHVmfIPNLTANTLYEVKVQ 511
Cdd:cd00063     1 PSPPTNLRVTDVTSTSVTLSWTPPEDDGGPITGYVVEYREKGSGDWKEVEVTPGSETSYT--LTGLKPGTEYEFRVR 75
PTPc-N21_14 cd14540
catalytic domain of tyrosine-protein phosphatase non-receptor type 21 and type 14; ...
989-1059 1.72e-09

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: 59.39  E-value: 1.72e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 998470296  989 YINA---TFLQGfNRLREFIVTQHPLMDTMADFWQMVWDHNSQTIVVLSVVDEKEHP---QFWPDTDEEQD---YGSFKV 1059
Cdd:cd14540     1 YINAshiTATVG-GKQRFYIAAQGPLQNTVGDFWQMVWEQGVYLVVMVTAEEEGGREkcfRYWPTLGGEHDaltFGEYKV 79
FN3 COG3401
Fibronectin type 3 domain [General function prediction only];
133-280 2.83e-09

Fibronectin type 3 domain [General function prediction only];


Pssm-ID: 442628 [Multi-domain]  Cd Length: 603  Bit Score: 61.17  E-value: 2.83e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 998470296  133 PDPPGIPIVVGFTSRSVDLSWTSSPNSHhsvILHYIIHIRIGEKGDWDtmnKVMTSDNSTNFQVIGLKPFTVYSFRVLAV 212
Cdd:COG3401   327 PAAPSGLTATAVGSSSITLSWTASSDAD---VTGYNVYRSTSGGGTYT---KIAETVTTTSYTDTGLTPGTTYYYKVTAV 400
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 998470296  213 NAIG-ASKPSKESFYMVTLREVPEGK---PTIVHAQNTSSSSVRIQWTAPARHTIHGEFEGYRITYRPRDRT 280
Cdd:COG3401   401 DAAGnESAPSEEVSATTASAASGESLtasVDAVPLTDVAGATAAASAASNPGVSAAVLADGGDTGNAVPFTT 472
PTPc-N20 cd14596
catalytic domain of tyrosine-protein phosphatase non-receptor type 20; Tyrosine-protein ...
989-1048 1.31e-08

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: 56.29  E-value: 1.31e-08
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 998470296  989 YINATFLQGFNRLRE--FIVTQHPLMDTMADFWQMVWDHNSQTIVVLSVVDE----KEHpQFWPDT 1048
Cdd:cd14596     1 YINASYITMPVGEEElfYIATQGPLPSTIDDFWQMVWENRSDVIAMMTREVErgkvKCH-RYWPET 65
PTP-N23 cd14539
PTP-like domain of tyrosine-protein phosphatase non-receptor type 23; Tyrosine-protein ...
989-1165 1.75e-08

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: 56.24  E-value: 1.75e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 998470296  989 YINATFLQGFNRLR-EFIVTQHPLMDTMADFWQMVWDHNSQTIVVL---SVVDEKEHPQFWP-DTDEEQDYGSFKVKPTG 1063
Cdd:cd14539     1 YINASLIEDLTPYCpRFIATQAPLPGTAADFWLMVYEQQVSVIVMLvseQENEKQKVHRYWPtERGQALVYGAITVSLQS 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 998470296 1064 ESVAPPVAEEkgalmpgeggglpsrdfILQSTQDDYELACRL--LLCPGWPQSCSPLAKA--FELVKEVGA--RQERDQN 1137
Cdd:cd14539    81 VRTTPTHVER-----------------IISIQHKDTRLSRSVvhLQFTTWPELGLPDSPNplLRFIEEVHShyLQQRSLQ 143
                         170       180       190
                  ....*....|....*....|....*....|...
gi 998470296 1138 GPVVI-----VDRYGgteaaTFCCLSALYRQLE 1165
Cdd:cd14539   144 TPIVVhcssgVGRTG-----AFCLLYAAVQEIE 171
PTPc-N20_13 cd14538
catalytic domain of tyrosine-protein phosphatase non-receptor type 20 and type 13; ...
989-1059 2.34e-08

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: 55.84  E-value: 2.34e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 998470296  989 YINATFLQ---GFNRLReFIVTQHPLMDTMADFWQMVWDHNSQTIVVLSVVDE----KEHpQFWPDTDEEQD--YGSFKV 1059
Cdd:cd14538     1 YINASHIRipvGGDTYH-YIACQGPLPNTTGDFWQMVWEQKSEVIAMVTQDVEggkvKCH-RYWPDSLNKPLicGGRLEV 78
PHA02740 PHA02740
protein tyrosine phosphatase; Provisional
954-1045 2.19e-07

protein tyrosine phosphatase; Provisional


Pssm-ID: 165107 [Multi-domain]  Cd Length: 298  Bit Score: 54.20  E-value: 2.19e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 998470296  954 AVKPCNKAKNR------SLNLIPIESHRVHITPKPGIdgsdyINATFLQGFNRLREFIVTQHPLMDTMADFWQMVWDHNS 1027
Cdd:PHA02740   42 ANKACAQAENKakdenlALHITRLLHRRIKLFNDEKV-----LDARFVDGYDFEQKFICIINLCEDACDKFLQALSDNKV 116
                          90
                  ....*....|....*....
gi 998470296 1028 QTIVVLS-VVDEKEHPQFW 1045
Cdd:PHA02740  117 QIIVLISrHADKKCFNQFW 135
CDC14 COG2453
Protein-tyrosine phosphatase [Signal transduction mechanisms];
795-889 1.01e-06

Protein-tyrosine phosphatase [Signal transduction mechanisms];


Pssm-ID: 441989 [Multi-domain]  Cd Length: 140  Bit Score: 49.58  E-value: 1.01e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 998470296  795 QYHYTNWPDHGVPDHP--LPVLSFVAKSSAANPPAAgpmiVHCSAGVGRTGTYIVLDAMLRQMRQRQSvnvygfLRHIRQ 872
Cdd:COG2453    49 EYLHLPIPDFGAPDDEqlQEAVDFIDEALREGKKVL----VHCRGGIGRTGTVAAAYLVLLGLSAEEA------LARVRA 118
                          90
                  ....*....|....*..
gi 998470296  873 QRNYLVQTEEQYVFIHD 889
Cdd:COG2453   119 ARPGAVETPAQRAFLER 135
FN3 smart00060
Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, ...
435-511 1.05e-06

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


Pssm-ID: 214495 [Multi-domain]  Cd Length: 83  Bit Score: 47.61  E-value: 1.05e-06
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 998470296    435 PSAPVIVNLTCQSLDSLFLQWERPQtyYNRVDYYFVHYRSEEAWSFEEIAMAANDRLEHVMFIPNLTANTLYEVKVQ 511
Cdd:smart00060    1 PSPPSNLRVTDVTSTSVTLSWEPPP--DDGITGYIVGYRVEYREEGSEWKEVNVTPSSTSYTLTGLKPGTEYEFRVR 75
IG_like smart00410
Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.
39-129 1.05e-06

Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.


Pssm-ID: 214653 [Multi-domain]  Cd Length: 85  Bit Score: 47.89  E-value: 1.05e-06
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 998470296     39 VRVGGNATLACPdlPPGAGPPrHLLWWKEDRRLIeATRDRVTVAPDagprvsllPGSSALVFRSVLTQDSGEYQCVVNNR 118
Cdd:smart00410    6 VKEGESVTLSCE--ASGSPPP-EVTWYKQGGKLL-AESGRFSVSRS--------GSTSTLTISNVTPEDSGTYTCAATNS 73
                            90
                    ....*....|..
gi 998470296    119 QG-RRGLVRLFV 129
Cdd:smart00410   74 SGsASSGTTLTV 85
PTP_DSP_cys cd14494
cys-based protein tyrosine phosphatase and dual-specificity phosphatase superfamily; This ...
829-889 1.45e-06

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


Pssm-ID: 350344 [Multi-domain]  Cd Length: 113  Bit Score: 48.11  E-value: 1.45e-06
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 998470296  829 GPMIVHCSAGVGRTGTYIVLDAMLRQMRqrqsvNVYGFLRHIRQQR-NYLVQTEEQYVFIHD 889
Cdd:cd14494    57 EPVLVHCKAGVGRTGTLVACYLVLLGGM-----SAEEAVRIVRLIRpGGIPQTIEQLDFLIK 113
PTPc-N21 cd14598
catalytic domain of tyrosine-protein phosphatase non-receptor type 21; Tyrosine-protein ...
989-1059 2.09e-06

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: 50.36  E-value: 2.09e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 998470296  989 YINATFLQGFNRLRE--FIVTQHPLMDTMADFWQMVWDhnsQTIVVLSVVDEKEHP------QFWPDTDEEQD---YGSF 1057
Cdd:cd14598     1 YINASHIKVTVGGKEwdYIATQGPLQNTCQDFWQMVWE---QGVAIIAMVTAEEEGgreksfRYWPRLGSRHNtvtYGRF 77

                  ..
gi 998470296 1058 KV 1059
Cdd:cd14598    78 KI 79
ig pfam00047
Immunoglobulin domain; Members of the immunoglobulin superfamily are found in hundreds of ...
37-118 6.22e-06

Immunoglobulin domain; Members of the immunoglobulin superfamily are found in hundreds of proteins of different functions. Examples include antibodies, the giant muscle kinase titin and receptor tyrosine kinases. Immunoglobulin-like domains may be involved in protein-protein and protein-ligand interactions.


Pssm-ID: 395002  Cd Length: 86  Bit Score: 45.65  E-value: 6.22e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 998470296    37 LFVRVGGNATLACpdLPPGAGPPRHLLWWKEDRRLIEATRDRVTVAPDagprvsllpGSSALVFRSVLTQDSGEYQCVVN 116
Cdd:pfam00047    6 VTVLEGDSATLTC--SASTGSPGPDVTWSKEGGTLIESLKVKHDNGRT---------TQSSLLISNVTKEDAGTYTCVVN 74

                   ..
gi 998470296   117 NR 118
Cdd:pfam00047   75 NP 76
fn3 pfam00041
Fibronectin type III domain;
436-515 1.74e-05

Fibronectin type III domain;


Pssm-ID: 394996 [Multi-domain]  Cd Length: 85  Bit Score: 44.33  E-value: 1.74e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 998470296   436 SAPVIVNLTCQSLDSLFLQWERPQTYYNRVDYYFVHYRseEAWSFEEIAMAANDRLEHVMFIPNLTANTLYEVKVQGATR 515
Cdd:pfam00041    1 SAPSNLTVTDVTSTSLTVSWTPPPDGNGPITGYEVEYR--PKNSGEPWNEITVPGTTTSVTLTGLKPGTEYEVRVQAVNG 78
Ig_3 pfam13927
Immunoglobulin domain; This family contains immunoglobulin-like domains.
39-117 4.41e-05

Immunoglobulin domain; This family contains immunoglobulin-like domains.


Pssm-ID: 464046 [Multi-domain]  Cd Length: 78  Bit Score: 42.94  E-value: 4.41e-05
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 998470296    39 VRVGGNATLACPdlppGAGPPRHLLWWKEDRRLIEATRDRvtvapdagpRVSLLPGSSALVFRSVLTQDSGEYQCVVNN 117
Cdd:pfam13927   13 VREGETVTLTCE----ATGSPPPTITWYKNGEPISSGSTR---------SRSLSGSNSTLTISNVTRSDAGTYTCVASN 78
Ig cd00096
Immunoglobulin domain; The members here are composed of the immunoglobulin (Ig) domain found ...
45-122 1.14e-04

Immunoglobulin domain; The members here are composed of the immunoglobulin (Ig) domain found in the Ig superfamily. The Ig superfamily is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. Members of this group are components of immunoglobulin, neuroglia, cell surface glycoproteins, including T-cell receptors, CD2, CD4, CD8, and membrane glycoproteins, including butyrophilin and chondroitin sulfate proteoglycan core protein. A predominant feature of most Ig domains is a disulfide bridge connecting the two beta-sheets with a tryptophan residue packed against the disulfide bond. Ig superfamily (IgSF) domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. Typically, the V-set domains have A, B, E, and D strands in one sheet and A', G, F, C, C' and C" in the other. The structures in C1-set are smaller than those in the V-set; they have one beta sheet that is formed by strands A, B, E, and D and the other by strands G, F, C, and C'. Moreover, a C1-set Ig domain contains a short C' strand (three residues) and lacks A' and C" strand. Unlike other Ig domain sets, C2-set structures do not have a D strand. Like the V-set Ig domains, members of the I-set have a discontinuous A strand, but lack a C" strand.


Pssm-ID: 409353 [Multi-domain]  Cd Length: 70  Bit Score: 41.55  E-value: 1.14e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 998470296   45 ATLACPdlpPGAGPPRHLLWWKEDRRLIEATRDRVtvapdagprvSLLPGSSALVFRSVLTQDSGEYQCVVNNRQGRR 122
Cdd:cd00096     1 VTLTCS---ASGNPPPTITWYKNGKPLPPSSRDSR----------RSELGNGTLTISNVTLEDSGTYTCVASNSAGGS 65
IgI_2_Robo cd05724
Second immunoglobulin (Ig)-like domain in Robo (roundabout) receptors; member of the I-set of ...
39-122 1.57e-04

Second immunoglobulin (Ig)-like domain in Robo (roundabout) receptors; member of the I-set of Ig superfamily (IgSF) domains; The members here are composed of the second immunoglobulin (Ig)-like domain in Robo (roundabout) receptors. Robo receptors play a role in the development of the central nervous system (CNS), and are receptors of the Slit protein. Slit is a repellant secreted by the neural cells in the midline. Slit acts through Robo to prevent most neurons from crossing the midline from either side. Three mammalian Robo homologs (Robo1, Robo2, and Robo3), and three mammalian Slit homologs (Slit-1,Slit-2, Slit-3), have been identified. Commissural axons, which cross the midline, express low levels of Robo; longitudinal axons, which avoid the midline, express high levels of Robo. Robo1, Robo2, and Robo3 are expressed by commissural neurons in the vertebrate spinal cord and Slit-1, Slit-2, Slit-3 are expressed at the ventral midline. Robo-3 is a divergent member of the Robo family which instead of being a positive regulator of Slit responsiveness, antagonizes Slit responsiveness in precrossing axons. The Slit-Robo interaction is mediated by the second leucine-rich repeat (LRR) domain of Slit and the two N-terminal Ig domains of Robo, Ig1 and Ig2. The primary Robo binding site for Slit-2 has been shown by surface plasmon resonance experiments and mutational analysis to be the Ig1 domain, while the Ig2 domain has been proposed to harbor a weak secondary binding site. This group belongs to the I-set of IgSF domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand, but lack a C" strand.


Pssm-ID: 409389 [Multi-domain]  Cd Length: 87  Bit Score: 41.62  E-value: 1.57e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 998470296   39 VRVGGNATLACPdlPPGAGPPRHLLWWKEDRRLIeatrdrvtvapDAGPRVSLLPGSSaLVFRSVLTQDSGEYQCVVNNR 118
Cdd:cd05724     9 VAVGEMAVLECS--PPRGHPEPTVSWRKDGQPLN-----------LDNERVRIVDDGN-LLIAEARKSDEGTYKCVATNM 74

                  ....
gi 998470296  119 QGRR 122
Cdd:cd05724    75 VGER 78
PTP_PTPDC1 cd14506
protein tyrosine phosphatase domain of PTP domain-containing protein 1; protein tyrosine ...
790-889 1.91e-04

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


Pssm-ID: 350356 [Multi-domain]  Cd Length: 206  Bit Score: 43.88  E-value: 1.91e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 998470296  790 ERTVYQYHYtNWPDHGVPdhPLPVLSFVAKSSAANPPAAGPMIVHCSAGVGRTGTYI--VLDAMLRqMRQRQSVnvygfl 867
Cdd:cd14506    74 RAGIYFYNF-GWKDYGVP--SLTTILDIVKVMAFALQEGGKVAVHCHAGLGRTGVLIacYLVYALR-MSADQAI------ 143
                          90       100
                  ....*....|....*....|..
gi 998470296  868 RHIRQQRNYLVQTEEQYVFIHD 889
Cdd:cd14506   144 RLVRSKRPNSIQTRGQVLCVRE 165
DUSP23 cd14504
dual specificity phosphatase 23; Dual specificity phosphatase 23 (DUSP23), also known as ...
797-887 1.97e-04

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


Pssm-ID: 350354 [Multi-domain]  Cd Length: 142  Bit Score: 42.65  E-value: 1.97e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 998470296  797 HYTNWPDHGVPDHPLPV--------------LSFVAKSSAANPPAAgpmiVHCSAGVGRTGTyiVLDAMLRQMRQRQSVN 862
Cdd:cd14504    41 PEHSDTCPGLRYHHIPIedytpptleqidefLDIVEEANAKNEAVL----VHCLAGKGRTGT--MLACYLVKTGKISAVD 114
                          90       100
                  ....*....|....*....|....*
gi 998470296  863 VygfLRHIRQQRNYLVQTEEQYVFI 887
Cdd:cd14504   115 A---INEIRRIRPGSIETSEQEKFV 136
COG3979 COG3979
Chitodextrinase [Carbohydrate transport and metabolism];
133-216 2.90e-04

Chitodextrinase [Carbohydrate transport and metabolism];


Pssm-ID: 443178 [Multi-domain]  Cd Length: 369  Bit Score: 44.76  E-value: 2.90e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 998470296  133 PDPPGIPIVVGFTSRSVDLSWTSSPNShhSVILHYIIHirigEKGDwdtmnKVMTSDNSTNFQVIGLKPFTVYSFRVLAV 212
Cdd:COG3979     3 PTAPTGLTASNVTSSSVSLSWDASTDN--VGVTGYDVY----RGGD-----QVATVTGLTAWTVTGLTPGTEYTFTVGAC 71

                  ....
gi 998470296  213 NAIG 216
Cdd:COG3979    72 DAAG 75
DSPc smart00195
Dual specificity phosphatase, catalytic domain;
829-873 5.27e-04

Dual specificity phosphatase, catalytic domain;


Pssm-ID: 214551 [Multi-domain]  Cd Length: 138  Bit Score: 41.50  E-value: 5.27e-04
                            10        20        30        40
                    ....*....|....*....|....*....|....*....|....*
gi 998470296    829 GPMIVHCSAGVGRTGTYIVldAMLRQMRQRQSVNVYGFLRHIRQQ 873
Cdd:smart00195   79 GKVLVHCQAGVSRSATLII--AYLMKTRNMSLNDAYDFVKDRRPI 121
IgI_5_Robo cd20952
Fifth Ig-like domain of Roundabout (Robo) homolog 1/2, and similar domains; a member of the ...
39-120 1.66e-03

Fifth Ig-like domain of Roundabout (Robo) homolog 1/2, and similar domains; a member of the I-set of IgSF domains; The members here are composed of the fifth Ig-like domain of Roundabout (Robo) homolog 1/2 and similar domains. Robo receptors play a role in the development of the central nervous system (CNS), and are receptors of Slit protein. Slit is a repellant secreted by the neural cells in the midline. Slit acts through Robo to prevent most neurons from crossing the midline from either side. Three mammalian Robo homologs (Robo1, -2, and -3), and three mammalian Slit homologs (Slit-1,-2, -3), have been identified. Commissural axons, which cross the midline, express low levels of Robo; longitudinal axons, which avoid the midline, express high levels of Robo. Robo1, -2, and -3 are expressed by commissural neurons in the vertebrate spinal cord and Slits 1, -2, -3 are expressed at the ventral midline. Robo-3 is a divergent member of the Robo family which instead of being a positive regulator of slit responsiveness, antagonizes slit responsiveness in precrossing axons. The Slit-Robo interaction is mediated by the second leucine-rich repeat (LRR) domain of Slit and the two N-terminal Ig domains of Robo, Ig1 and Ig2. The primary Robo binding site for Slit2 has been shown by surface plasmon resonance experiments and mutational analysis to be is the Ig1 domain, while the Ig2 domain has been proposed to harbor a weak secondary binding site. The fifth Ig-like domain of Robo 1 and 2 is a member of the I-set Ig domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand but lack a C" strand. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors


Pssm-ID: 409544 [Multi-domain]  Cd Length: 87  Bit Score: 38.63  E-value: 1.66e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 998470296   39 VRVGGNATLACPdlppGAGPPRHLLWWKEDRRLIeatrdrvtvaPDAGPRVSLLPGSSaLVFRSVLTQDSGEYQCVVNNR 118
Cdd:cd20952    11 VAVGGTVVLNCQ----ATGEPVPTISWLKDGVPL----------LGKDERITTLENGS-LQIKGAEKSDTGEYTCVALNL 75

                  ..
gi 998470296  119 QG 120
Cdd:cd20952    76 SG 77
COG4733 COG4733
Phage-related protein, tail protein J [Mobilome: prophages, transposons];
133-355 1.92e-03

Phage-related protein, tail protein J [Mobilome: prophages, transposons];


Pssm-ID: 443767 [Multi-domain]  Cd Length: 978  Bit Score: 42.62  E-value: 1.92e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 998470296  133 PDPPGIPIVVGFTSR-------SVDLSWTSSPNShhsviLHYIIHIRIGEkGDWdtmNKVMTSDnSTNFQVIGLKPfTVY 205
Cdd:COG4733   531 WPPVNVTTSESLSVVaqgtavtTLTVSWDAPAGA-----VAYEVEWRRDD-GNW---VSVPRTS-GTSFEVPGIYA-GDY 599
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 998470296  206 SFRVLAVNAIG-ASKPSKESFYMVTLREVPEGKPTIVHAQNtSSSSVRIQWTAPArhtiHGEFEGYRITYRPRDrtQEES 284
Cdd:COG4733   600 EVRVRAINALGvSSAWAASSETTVTGKTAPPPAPTGLTATG-GLGGITLSWSFPV----DADTLRTEIRYSTTG--DWAS 672
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 998470296  285 REIILRDSKQTQYTIRNLETFTQYLVSLQVFNPAGRGPAVVVPVMTDEGVPSSPVNLT-AVRVTDTTVRLKW 355
Cdd:COG4733   673 ATVAQALYPGNTYTLAGLKAGQTYYYRARAVDRSGNVSAWWVSGQASADAAGILDAITgQILETELGQELDA 744
PTPLP-like cd14495
Protein tyrosine phosphatase-like domains of phytases and similar domains; This subfamily ...
779-853 3.40e-03

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: 40.82  E-value: 3.40e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 998470296  779 KNIKVKKKQASERTVYQ--YHYTNW--PDHGVPDhPLPVLSFVAksSAANPPAAGPMIVHCSAGVGRTGTYIVLDAMLR 853
Cdd:cd14495   136 KTVKVESVRTEEELVKKkgAHYVRIaaTDHVWPD-DEEIDAFVA--FYRSLPADAWLHFHCRAGKGRTTTFMVMYDMLK 211
COG4733 COG4733
Phage-related protein, tail protein J [Mobilome: prophages, transposons];
88-216 4.01e-03

Phage-related protein, tail protein J [Mobilome: prophages, transposons];


Pssm-ID: 443767 [Multi-domain]  Cd Length: 978  Bit Score: 41.47  E-value: 4.01e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 998470296   88 RVSLLPGSSALVFRSVLTQDSGEYQCV-----------------------VNNRQGRRGL----VRLFVQDVPDPPgiPI 140
Cdd:COG4733   555 TVSWDAPAGAVAYEVEWRRDDGNWVSVprtsgtsfevpgiyagdyevrvrAINALGVSSAwaasSETTVTGKTAPP--PA 632
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 998470296  141 VVGFTS----RSVDLSWTSSPNSHhsvILHYIihIRIGEKGDWDTMNKVMTSDNSTNFQVIGLKPFTVYSFRVLAVNAIG 216
Cdd:COG4733   633 PTGLTAtgglGGITLSWSFPVDAD---TLRTE--IRYSTTGDWASATVAQALYPGNTYTLAGLKAGQTYYYRARAVDRSG 707
 
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.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH