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Conserved domains on  [gi|1622828204|ref|XP_014976209|]
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receptor-type tyrosine-protein phosphatase C isoform X1 [Macaca mulatta]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
R-PTPc-C-1 cd14557
catalytic domain of receptor-type tyrosine-protein phosphatase C, repeat 1; Receptor-type ...
 711-911 1.15e-149

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: 449.66  E-value: 1.15e-149
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622828204  711 YINASYIDGFKEPRKYIAAQGPRDETVDDFWRMIWEQKATVIVMVTRCEEGNRNKCAEYWPSMEEGTRAFGDVVVKINQH 790
Cdd:cd14557      1 YINASYIDGFKEPRKYIAAQGPKDETVDDFWRMIWEQKSTVIVMVTRCEEGNRNKCAQYWPSMEEGSRAFGDVVVKINEE 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622828204  791 KRCPDYIIQKLNIVNKKEKATGREVTHIQFTSWPDHGVPEDPHLLLKLRRRVNAFSNFFSGPIVVHCSAGVGRTGTYIGI 870
Cdd:cd14557     81 KICPDYIIRKLNINNKKEKGSGREVTHIQFTSWPDHGVPEDPHLLLKLRRRVNAFNNFFSGPIVVHCSAGVGRTGTYIGI 160

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|.
gi 1622828204  871 DAMLEGLEAENKVDVYGYVVKLRRQRCLMVQVEAQYILIHQ 911
Cdd:cd14557    161 DAMLEGLEAEGRVDVYGYVVKLRRQRCLMVQVEAQYILIHQ 201
R-PTP-C-2 cd14558
PTP-like domain of receptor-type tyrosine-protein phosphatase C, repeat 2; Receptor-type ...
 1021-1227 1.05e-127

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: 391.76  E-value: 1.05e-127
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622828204 1021 YINASFIMSYWKPEVMIAAQGPLKETIGDFWQMIFQRKVKVIVMLTELKHGDQEICAQYWGEGKQTYGDIEVDMKDTNKS 1100
Cdd:cd14558      1 YINASFIDGYWGPKSLIATQGPLPDTIADFWQMIFQKKVKVIVMLTELKEGDQEQCAQYWGDEKKTYGDIEVELKDTEKS 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622828204 1101 STYTLRVFELRHSKRKDSRTVYQYQYTNWSVEQLPAEPKELVSLIQVLKEKLPQKNSsegnKHHKSTPLLIHCRDGSQQT 1180
Cdd:cd14558     81 PTYTVRVFEITHLKRKDSRTVYQYQYHKWKGEELPEKPKDLVDMIKSIKQKLPYKNS----KHGRSVPIVVHCSDGSSRT 156

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*..
gi 1622828204 1181 GIFCALLNLLESAETEEVVDIFQVVKALRKARPGMVSTFEQYQFLYD 1227
Cdd:cd14558    157 GIFCALWNLLESAETEKVVDVFQVVKALRKQRPGMVSTLEQYQFLYD 203
CD45 pfam12567
Leukocyte receptor CD45; This family of proteins is found in eukaryotes. Proteins in this ...
 237-300 3.33e-24

Leukocyte receptor CD45; This family of proteins is found in eukaryotes. Proteins in this family are typically between 77 and 1130 amino acids in length. The family is found in association with pfam00041. CD45 plays a critical role in T-cell receptor (TCR)-mediated signaling. CD45 interacts with SKAP55 which is a transcriptional activator of IL-2.


:

Pssm-ID: 432641  Cd Length: 59  Bit Score: 96.67  E-value: 3.33e-24
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1622828204  237 VDYLYNNKTKLFTAKLNVNENVECTNNNhthniCTNNEVLNLPECKEMNVFVSHNSCTDRHKEL 300
Cdd:pfam12567    1 VEYTYNSENKSFTAKLNVNDNVECENND-----CENNELHNLQECEQINVSISHNSCTSPNKIL 59
DUF5585 super family cl39316
Family of unknown function (DUF5585); This is a family of unknown function found in chordata.
 24-237 5.89e-11

Family of unknown function (DUF5585); This is a family of unknown function found in chordata.


The actual alignment was detected with superfamily member pfam17823:

Pssm-ID: 465521 [Multi-domain]  Cd Length: 506  Bit Score: 66.52  E-value: 5.89e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622828204   24 TGQGSTLSPTGRRTTKMPSVPLSSDPLPTHTTAF--SPASISERENDFSETTPSLSSDNTSTHVSP----DSLDNASAFN 97
Cdd:pfam17823  116 AAAASSSPSSAAQSLPAAIAALPSEAFSAPRAAAcrANASAAPRAAIAAASAPHAASPAPRTAASSttaaSSTTAASSAP 195

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622828204   98 TTGVSSALTPHLPThadSQTPSTGTDTQTPSGS---AANTTLSPTPRSNDISDVPGERSTASTFPT------------DP 162
Cdd:pfam17823  196 TTAASSAPATLTPA---RGISTAATATGHPAAGtalAAVGNSSPAAGTVTAAVGTVTPAALATLAAaagtvasaagtiNM 272

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622828204  163 ISPLATTLIPAR----NSSAALPARTSN-----TTITANTSVSYLNASETTTPSPSGST--------VISTPTIATTTSK 225
Cdd:pfam17823  273 GDPHARRLSPAKhmpsDTMARNPAAPMGaqaqgPIIQVSTDQPVHNTAGEPTPSPSNTTlepntpksVASTNLAVVTTTK 352

                          250
                   ....*....|...
gi 1622828204  226 PTCAEKYA-TIPV 237
Cdd:pfam17823  353 AQAKEPSAsPVPV 365
PTP_N pfam12453
Protein tyrosine phosphatase N terminal; This domain family is found in eukaryotes, and is ...
 7-32 1.15e-06

Protein tyrosine phosphatase N terminal; This domain family is found in eukaryotes, and is approximately 30 amino acids in length. The family is found in association with pfam00041. There is a single completely conserved residue L that may be functionally important. This family consists of various protein tyrosine phosphatase haematopoietic receptors, e.g. CD45, which dephosphorylate growth stimulating proteins. This limits growth signalling in haematopoietic cells.


:

Pssm-ID: 403599  Cd Length: 26  Bit Score: 45.99  E-value: 1.15e-06
                           10        20
                   ....*....|....*....|....*.
gi 1622828204    7 LKLLAFVFAFLDTEVFVTGQGSTLSP 32
Cdd:pfam12453    1 LKLLAFGFAFLDTEVFVTGESLTSST 26
fn3 pfam00041
Fibronectin type III domain;
398-467 2.96e-06

Fibronectin type III domain;


:

Pssm-ID: 394996 [Multi-domain]  Cd Length: 85  Bit Score: 46.64  E-value: 2.96e-06
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1622828204  398 GQPQNVVCRHEDAHQGVITWNPP---QRSFHNFTLCYVSK---TAKKCLSLDKHLTTYHLQNLKPYTNYSLSLHAY 467
Cdd:pfam00041    1 SAPSNLTVTDVTSTSLTVSWTPPpdgNGPITGYEVEYRPKnsgEPWNEITVPGTTTSVTLTGLKPGTEYEVRVQAV 76
FN3 cd00063
Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein ...
 490-570 2.47e-04

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


:

Pssm-ID: 238020 [Multi-domain]  Cd Length: 93  Bit Score: 41.33  E-value: 2.47e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622828204  490 PSQVQNMIVS-TSDNSMRVKCEAPRDVNGPTELYLLEVEAGN----TLVRNLSQSECDFSVNNLQYSTYYNLKAYYHNGK 564
Cdd:cd00063      1 PSPPTNLRVTdVTSTSVTLSWTPPEDDGGPITGYVVEYREKGsgdwKEVEVTPGSETSYTLTGLKPGTEYEFRVRAVNGG 80


                   ....*.
gi 1622828204  565 YSGEPV 570
Cdd:cd00063     81 GESPPS 86
 
Name Accession Description Interval E-value
R-PTPc-C-1 cd14557
catalytic domain of receptor-type tyrosine-protein phosphatase C, repeat 1; Receptor-type ...
 711-911 1.15e-149

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: 449.66  E-value: 1.15e-149
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622828204  711 YINASYIDGFKEPRKYIAAQGPRDETVDDFWRMIWEQKATVIVMVTRCEEGNRNKCAEYWPSMEEGTRAFGDVVVKINQH 790
Cdd:cd14557      1 YINASYIDGFKEPRKYIAAQGPKDETVDDFWRMIWEQKSTVIVMVTRCEEGNRNKCAQYWPSMEEGSRAFGDVVVKINEE 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622828204  791 KRCPDYIIQKLNIVNKKEKATGREVTHIQFTSWPDHGVPEDPHLLLKLRRRVNAFSNFFSGPIVVHCSAGVGRTGTYIGI 870
Cdd:cd14557     81 KICPDYIIRKLNINNKKEKGSGREVTHIQFTSWPDHGVPEDPHLLLKLRRRVNAFNNFFSGPIVVHCSAGVGRTGTYIGI 160

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|.
gi 1622828204  871 DAMLEGLEAENKVDVYGYVVKLRRQRCLMVQVEAQYILIHQ 911
Cdd:cd14557    161 DAMLEGLEAEGRVDVYGYVVKLRRQRCLMVQVEAQYILIHQ 201
R-PTP-C-2 cd14558
PTP-like domain of receptor-type tyrosine-protein phosphatase C, repeat 2; Receptor-type ...
 1021-1227 1.05e-127

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: 391.76  E-value: 1.05e-127
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622828204 1021 YINASFIMSYWKPEVMIAAQGPLKETIGDFWQMIFQRKVKVIVMLTELKHGDQEICAQYWGEGKQTYGDIEVDMKDTNKS 1100
Cdd:cd14558      1 YINASFIDGYWGPKSLIATQGPLPDTIADFWQMIFQKKVKVIVMLTELKEGDQEQCAQYWGDEKKTYGDIEVELKDTEKS 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622828204 1101 STYTLRVFELRHSKRKDSRTVYQYQYTNWSVEQLPAEPKELVSLIQVLKEKLPQKNSsegnKHHKSTPLLIHCRDGSQQT 1180
Cdd:cd14558     81 PTYTVRVFEITHLKRKDSRTVYQYQYHKWKGEELPEKPKDLVDMIKSIKQKLPYKNS----KHGRSVPIVVHCSDGSSRT 156

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*..
gi 1622828204 1181 GIFCALLNLLESAETEEVVDIFQVVKALRKARPGMVSTFEQYQFLYD 1227
Cdd:cd14558    157 GIFCALWNLLESAETEKVVDVFQVVKALRKQRPGMVSTLEQYQFLYD 203
PTPc smart00194
Protein tyrosine phosphatase, catalytic domain;
656-915 2.87e-111

Protein tyrosine phosphatase, catalytic domain;


Pssm-ID: 214550 [Multi-domain]  Cd Length: 259  Bit Score: 349.65  E-value: 2.87e-111
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622828204   656 LFLAEFQSIPRVFS-KFPIKEARKPFNQNKNRYVDILPYDYNRVELSEINGDaGSNYINASYIDGFKEPRKYIAAQGPRD 734
Cdd:smart00194    1 GLEEEFEKLDRLKPdDESCTVAAFPENRDKNRYKDVLPYDHTRVKLKPPPGE-GSDYINASYIDGPNGPKAYIATQGPLP 79

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622828204   735 ETVDDFWRMIWEQKATVIVMVTRCEEGNRNKCAEYWPSMEEGTRAFGDVVVKINQHKRCPDYIIQKLNIVNKKEKATgRE 814
Cdd:smart00194   80 STVEDFWRMVWEQKVTVIVMLTELVEKGREKCAQYWPDEEGEPLTYGDITVTLKSVEKVDDYTIRTLEVTNTGCSET-RT 158

                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622828204   815 VTHIQFTSWPDHGVPEDPHLLLKLRRRVNAFSNFFSGPIVVHCSAGVGRTGTYIGIDAMLEGLEAENKVDVYGYVVKLRR 894
Cdd:smart00194  159 VTHYHYTNWPDHGVPESPESILDLIRAVRKSQSTSTGPIVVHCSAGVGRTGTFIAIDILLQQLEAGKEVDIFEIVKELRS 238

                           250       260
                    ....*....|....*....|.
gi 1622828204   895 QRCLMVQVEAQYILIHQALVE 915
Cdd:smart00194  239 QRPGMVQTEEQYIFLYRAILE 259
Y_phosphatase pfam00102
Protein-tyrosine phosphatase;
681-915 3.23e-107

Protein-tyrosine phosphatase;


Pssm-ID: 459674 [Multi-domain]  Cd Length: 234  Bit Score: 337.68  E-value: 3.23e-107
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622828204  681 NQNKNRYVDILPYDYNRVELSEINGDagSNYINASYIDGFKEPRKYIAAQGPRDETVDDFWRMIWEQKATVIVMVTRCEE 760
Cdd:pfam00102    1 NLEKNRYKDVLPYDHTRVKLTGDPGP--SDYINASYIDGYKKPKKYIATQGPLPNTVEDFWRMVWEEKVTIIVMLTELEE 78

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622828204  761 GNRNKCAEYWPSMEEGTRAFGDVVVKI-NQHKRCPDYIIQKLNIVNKKEKATgREVTHIQFTSWPDHGVPEDPHLLLKLR 839
Cdd:pfam00102   79 KGREKCAQYWPEEEGESLEYGDFTVTLkKEKEDEKDYTVRTLEVSNGGSEET-RTVKHFHYTGWPDHGVPESPNSLLDLL 157

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1622828204  840 RRVNAFSN-FFSGPIVVHCSAGVGRTGTYIGIDAMLEGLEAENKVDVYGYVVKLRRQRCLMVQVEAQYILIHQALVE 915
Cdd:pfam00102  158 RKVRKSSLdGRSGPIVVHCSAGIGRTGTFIAIDIALQQLEAEGEVDIFQIVKELRSQRPGMVQTLEQYIFLYDAILE 234
PTPc smart00194
Protein tyrosine phosphatase, catalytic domain;
948-1230 8.22e-93

Protein tyrosine phosphatase, catalytic domain;


Pssm-ID: 214550 [Multi-domain]  Cd Length: 259  Bit Score: 299.57  E-value: 8.22e-93
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622828204   948 LEAEFQRLPSYRSW-RTQHIGNQEENKNKNRNSNVIPYDYNRVPLKHELEmskesdhdsdessdddsdseEPSKYINASF 1026
Cdd:smart00194    2 LEEEFEKLDRLKPDdESCTVAAFPENRDKNRYKDVLPYDHTRVKLKPPPG--------------------EGSDYINASY 61

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622828204  1027 IMSYWKPEVMIAAQGPLKETIGDFWQMIFQRKVKVIVMLTELKHGDQEICAQYW---GEGKQTYGDIEVDMKDTNKSSTY 1103
Cdd:smart00194   62 IDGPNGPKAYIATQGPLPSTVEDFWRMVWEQKVTVIVMLTELVEKGREKCAQYWpdeEGEPLTYGDITVTLKSVEKVDDY 141

                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622828204  1104 TLRVFELRHSKRKDSRTVYQYQYTNWSVEQLPAEPKELVSLIQVLKEKLPqknssegnkhHKSTPLLIHCRDGSQQTGIF 1183
Cdd:smart00194  142 TIRTLEVTNTGCSETRTVTHYHYTNWPDHGVPESPESILDLIRAVRKSQS----------TSTGPIVVHCSAGVGRTGTF 211

                           250       260       270       280
                    ....*....|....*....|....*....|....*....|....*..
gi 1622828204  1184 CALLNLLESAETEEVVDIFQVVKALRKARPGMVSTFEQYQFLYDIIA 1230
Cdd:smart00194  212 IAIDILLQQLEAGKEVDIFEIVKELRSQRPGMVQTEEQYIFLYRAIL 258
Y_phosphatase pfam00102
Protein-tyrosine phosphatase;
972-1230 1.17e-83

Protein-tyrosine phosphatase;


Pssm-ID: 459674 [Multi-domain]  Cd Length: 234  Bit Score: 272.96  E-value: 1.17e-83
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622828204  972 NKNKNRNSNVIPYDYNRVPLKHElemskesdhdsdessdddsdsEEPSKYINASFIMSYWKPEVMIAAQGPLKETIGDFW 1051
Cdd:pfam00102    1 NLEKNRYKDVLPYDHTRVKLTGD---------------------PGPSDYINASYIDGYKKPKKYIATQGPLPNTVEDFW 59

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622828204 1052 QMIFQRKVKVIVMLTELKHGDQEICAQYW---GEGKQTYGDIEVDMKDTNK-SSTYTLRVFELRHSKRKDSRTVYQYQYT 1127
Cdd:pfam00102   60 RMVWEEKVTIIVMLTELEEKGREKCAQYWpeeEGESLEYGDFTVTLKKEKEdEKDYTVRTLEVSNGGSEETRTVKHFHYT 139

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622828204 1128 NWSVEQLPAEPKELVSLIQVLkeklpqKNSSEGNKHHkstPLLIHCRDGSQQTGIFCALLNLLESAETEEVVDIFQVVKA 1207
Cdd:pfam00102  140 GWPDHGVPESPNSLLDLLRKV------RKSSLDGRSG---PIVVHCSAGIGRTGTFIAIDIALQQLEAEGEVDIFQIVKE 210

                          250       260
                   ....*....|....*....|...
gi 1622828204 1208 LRKARPGMVSTFEQYQFLYDIIA 1230
Cdd:pfam00102  211 LRSQRPGMVQTLEQYIFLYDAIL 233
PHA02746 PHA02746
protein tyrosine phosphatase; Provisional
 678-913 1.73e-51

protein tyrosine phosphatase; Provisional


Pssm-ID: 165113 [Multi-domain]  Cd Length: 323  Bit Score: 184.46  E-value: 1.73e-51
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622828204  678 KPFNQNKNRYVDILPYDYNRVELSE-------------------INGDAGSNYINASYIDGFKEPRKYIAAQGPRDETVD 738
Cdd:PHA02746    48 KKENLKKNRFHDIPCWDHSRVVINAheslkmfdvgdsdgkkievTSEDNAENYIHANFVDGFKEANKFICAQGPKEDTSE 127

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622828204  739 DFWRMIWEQKATVIVMVTRCEEGNRnKCAEYWPSMEEGTRAFGDVVVKINQHKRCPDYIIQKLNIVNKKEKaTGREVTHI 818
Cdd:PHA02746   128 DFFKLISEHESQVIVSLTDIDDDDE-KCFELWTKEEDSELAFGRFVAKILDIIEELSFTKTRLMITDKISD-TSREIHHF 205

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622828204  819 QFTSWPDHGVPEDPHLLLKLRRRVNA----------FSNFFSGPIVVHCSAGVGRTGTYIGIDAMLEGLEAENKVDVYGY 888
Cdd:PHA02746   206 WFPDWPDNGIPTGMAEFLELINKVNEeqaelikqadNDPQTLGPIVVHCSAGIGRAGTFCAIDNALEQLEKEKEVCLGEI 285

                          250       260
                   ....*....|....*....|....*
gi 1622828204  889 VVKLRRQRCLMVQVEAQYILIHQAL 913
Cdd:PHA02746   286 VLKIRKQRHSSVFLPEQYAFCYKAL 310
COG5599 COG5599
Protein tyrosine phosphatase [Signal transduction mechanisms];
684-909 1.31e-39

Protein tyrosine phosphatase [Signal transduction mechanisms];


Pssm-ID: 444335 [Multi-domain]  Cd Length: 282  Bit Score: 148.70  E-value: 1.31e-39
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622828204  684 KNRYVDILPYDYNRVElseINGdagsNYINASYIDGfKEPRKYIAAQGPRDETVDDFWRMIWEQKATVIVMVTRCEEG-- 761
Cdd:COG5599     45 LNRFRDIQPYKETALR---ANL----GYLNANYIQV-IGNHRYIATQYPLEEQLEDFFQMLFDNNTPVLVVLASDDEIsk 116

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622828204  762 NRNKCAEYWPsmEEGTRAFGDVVVKINQHKRCPDYIIQKLNIVNKKEKA-TGREVTHIQFTSWPDHGVP--EDPHLLLKL 838
Cdd:COG5599    117 PKVKMPVYFR--QDGEYGKYEVSSELTESIQLRDGIEARTYVLTIKGTGqKKIEIPVLHVKNWPDHGAIsaEALKNLADL 194

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1622828204  839 RRRVNAFSNFFSGPIVVHCSAGVGRTGTYIGIDAMLEGLEAEN--KVDVYGYVVKLRRQR-CLMVQVEAQYILI 909
Cdd:COG5599    195 IDKKEKIKDPDKLLPVVHCRAGVGRTGTLIACLALSKSINALVqiTLSVEEIVIDMRTSRnGGMVQTSEQLDVL 268
PHA02747 PHA02747
protein tyrosine phosphatase; Provisional
 971-1225 5.02e-34

protein tyrosine phosphatase; Provisional


Pssm-ID: 165114 [Multi-domain]  Cd Length: 312  Bit Score: 133.59  E-value: 5.02e-34
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622828204  971 ENKNKNRNSNVIPYDYNRVPLKhelemskesdhdsdessdddSDSEEPSKYINASFIMSYWKPEVMIAAQGPLKETIGDF 1050
Cdd:PHA02747    50 ENQPKNRYWDIPCWDHNRVILD--------------------SGGGSTSDYIHANWIDGFEDDKKFIATQGPFAETCADF 109

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622828204 1051 WQMIFQRKVKVIVMLTELKHGD-QEICAQYWG---EGKQTYGDIEVDMKDTNKSSTYTLRVFELRHSKRKDSRTVYQYQY 1126
Cdd:PHA02747   110 WKAVWQEHCSIIVMLTPTKGTNgEEKCYQYWClneDGNIDMEDFRIETLKTSVRAKYILTLIEITDKILKDSRKISHFQC 189

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622828204 1127 TNWSVEQLPAEPKELVSLIQVLKEKLPQKNSSEGNKHHKSTPLLIHCRDGSQQTGIFCALLNLLESAETEEVVDIFQVVK 1206
Cdd:PHA02747   190 SEWFEDETPSDHPDFIKFIKIIDINRKKSGKLFNPKDALLCPIVVHCSDGVGKTGIFCAVDICLNQLVKRKAICLAKTAE 269

                          250
                   ....*....|....*....
gi 1622828204 1207 ALRKARPGMVSTFEQYQFL 1225
Cdd:PHA02747   270 KIREQRHAGIMNFDDYLFI 288
COG5599 COG5599
Protein tyrosine phosphatase [Signal transduction mechanisms];
963-1231 1.72e-29

Protein tyrosine phosphatase [Signal transduction mechanisms];


Pssm-ID: 444335 [Multi-domain]  Cd Length: 282  Bit Score: 119.43  E-value: 1.72e-29
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622828204  963 TQHIGNQEeNKNKNRNSNVIPYDYNRVplkhelemskesdhdsdessdddsdsEEPSKYINASFIMSYwKPEVMIAAQGP 1042
Cdd:COG5599     34 PQYLQNIN-GSPLNRFRDIQPYKETAL--------------------------RANLGYLNANYIQVI-GNHRYIATQYP 85

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622828204 1043 LKETIGDFWQMIFQRKVKVIVMLTELKHGDQEI--CAQYWGEgKQTYGDIEVDMKDTNK---SSTYTLRVFEL-RHSKRK 1116
Cdd:COG5599     86 LEEQLEDFFQMLFDNNTPVLVVLASDDEISKPKvkMPVYFRQ-DGEYGKYEVSSELTESiqlRDGIEARTYVLtIKGTGQ 164

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622828204 1117 DSRTVYQYQYTNW------SVEQLpaepKELVSLI-QVLKEKLPQKNssegnkhhkstPLLIHCRDGSQQTGIFCALLNL 1189
Cdd:COG5599    165 KKIEIPVLHVKNWpdhgaiSAEAL----KNLADLIdKKEKIKDPDKL-----------LPVVHCRAGVGRTGTLIACLAL 229

                          250       260       270       280
                   ....*....|....*....|....*....|....*....|....*
gi 1622828204 1190 LES--AETEEVVDIFQVVKALRKAR-PGMVSTFEQYQFLYDIIAS 1231
Cdd:COG5599    230 SKSinALVQITLSVEEIVIDMRTSRnGGMVQTSEQLDVLVKLAEQ 274
CD45 pfam12567
Leukocyte receptor CD45; This family of proteins is found in eukaryotes. Proteins in this ...
 237-300 3.33e-24

Leukocyte receptor CD45; This family of proteins is found in eukaryotes. Proteins in this family are typically between 77 and 1130 amino acids in length. The family is found in association with pfam00041. CD45 plays a critical role in T-cell receptor (TCR)-mediated signaling. CD45 interacts with SKAP55 which is a transcriptional activator of IL-2.


Pssm-ID: 432641  Cd Length: 59  Bit Score: 96.67  E-value: 3.33e-24
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1622828204  237 VDYLYNNKTKLFTAKLNVNENVECTNNNhthniCTNNEVLNLPECKEMNVFVSHNSCTDRHKEL 300
Cdd:pfam12567    1 VEYTYNSENKSFTAKLNVNDNVECENND-----CENNELHNLQECEQINVSISHNSCTSPNKIL 59
DUF5585 pfam17823
Family of unknown function (DUF5585); This is a family of unknown function found in chordata.
 24-237 5.89e-11

Family of unknown function (DUF5585); This is a family of unknown function found in chordata.


Pssm-ID: 465521 [Multi-domain]  Cd Length: 506  Bit Score: 66.52  E-value: 5.89e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622828204   24 TGQGSTLSPTGRRTTKMPSVPLSSDPLPTHTTAF--SPASISERENDFSETTPSLSSDNTSTHVSP----DSLDNASAFN 97
Cdd:pfam17823  116 AAAASSSPSSAAQSLPAAIAALPSEAFSAPRAAAcrANASAAPRAAIAAASAPHAASPAPRTAASSttaaSSTTAASSAP 195

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622828204   98 TTGVSSALTPHLPThadSQTPSTGTDTQTPSGS---AANTTLSPTPRSNDISDVPGERSTASTFPT------------DP 162
Cdd:pfam17823  196 TTAASSAPATLTPA---RGISTAATATGHPAAGtalAAVGNSSPAAGTVTAAVGTVTPAALATLAAaagtvasaagtiNM 272

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622828204  163 ISPLATTLIPAR----NSSAALPARTSN-----TTITANTSVSYLNASETTTPSPSGST--------VISTPTIATTTSK 225
Cdd:pfam17823  273 GDPHARRLSPAKhmpsDTMARNPAAPMGaqaqgPIIQVSTDQPVHNTAGEPTPSPSNTTlepntpksVASTNLAVVTTTK 352

                          250
                   ....*....|...
gi 1622828204  226 PTCAEKYA-TIPV 237
Cdd:pfam17823  353 AQAKEPSAsPVPV 365
PHA03255 PHA03255
BDLF3; Provisional
 81-227 1.27e-08

BDLF3; Provisional


Pssm-ID: 165513 [Multi-domain]  Cd Length: 234  Bit Score: 57.22  E-value: 1.27e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622828204   81 TSTHVSPdsldnASAFNTTGVSSALTPHlPTHADSQTPSTGTDTQTPS------GSAANTTLSPTPrsndisdvpGERST 154
Cdd:PHA03255    25 TSSGSST-----ASAGNVTGTTAVTTPS-PSASGPSTNQSTTLTTTSApitttaILSTNTTTVTST---------GTTVT 89

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622828204  155 ASTFPTDPISPLATTLIPARNSSA-------ALPARTSNTTITANTSVSYLNASETTTPSPSGSTVISTPTIATTTSKPT 227
Cdd:PHA03255    90 PVPTTSNASTINVTTKVTAQNITAteagtgtSTGVTSNVTTRSSSTTSATTRITNATTLAPTLSSKGTSNATKTTAELPT 169
Chi1 COG3469
Chitinase [Carbohydrate transport and metabolism];
24-227 4.10e-08

Chitinase [Carbohydrate transport and metabolism];


Pssm-ID: 442692 [Multi-domain]  Cd Length: 534  Bit Score: 57.46  E-value: 4.10e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622828204   24 TGQGSTLSPTGRRTTKMPSVPLSSDPLPTHTTAFSPASISERENDFSETTPSLSSDNTSTHVSPDSLDNASAFNTTGVSS 103
Cdd:COG3469     15 ASATAVTLLGAAATAASVTLTAATATTVVSTTGSVVVAASGSAGSGTGTTAASSTAATSSTTSTTATATAAAAAATSTSA 94

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622828204  104 ALTPHLPTHADSQTPSTGTDTQTPSGSAANTTLSPTPRSNDISDVPGERSTASTFPTDPISPLATTliparnsSAALPAR 183
Cdd:COG3469     95 TLVATSTASGANTGTSTVTTTSTGAGSVTSTTSSTAGSTTTSGASATSSAGSTTTTTTVSGTETAT-------GGTTTTS 167

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....
gi 1622828204  184 TSNTTITANTSVSYLNASETTTPSPSGSTviSTPTIATTTSKPT 227
Cdd:COG3469    168 TTTTTTSASTTPSATTTATATTASGATTP--SATTTATTTGPPT 209
PTP_N pfam12453
Protein tyrosine phosphatase N terminal; This domain family is found in eukaryotes, and is ...
 7-32 1.15e-06

Protein tyrosine phosphatase N terminal; This domain family is found in eukaryotes, and is approximately 30 amino acids in length. The family is found in association with pfam00041. There is a single completely conserved residue L that may be functionally important. This family consists of various protein tyrosine phosphatase haematopoietic receptors, e.g. CD45, which dephosphorylate growth stimulating proteins. This limits growth signalling in haematopoietic cells.


Pssm-ID: 403599  Cd Length: 26  Bit Score: 45.99  E-value: 1.15e-06
                           10        20
                   ....*....|....*....|....*.
gi 1622828204    7 LKLLAFVFAFLDTEVFVTGQGSTLSP 32
Cdd:pfam12453    1 LKLLAFGFAFLDTEVFVTGESLTSST 26
fn3 pfam00041
Fibronectin type III domain;
398-467 2.96e-06

Fibronectin type III domain;


Pssm-ID: 394996 [Multi-domain]  Cd Length: 85  Bit Score: 46.64  E-value: 2.96e-06
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1622828204  398 GQPQNVVCRHEDAHQGVITWNPP---QRSFHNFTLCYVSK---TAKKCLSLDKHLTTYHLQNLKPYTNYSLSLHAY 467
Cdd:pfam00041    1 SAPSNLTVTDVTSTSLTVSWTPPpdgNGPITGYEVEYRPKnsgEPWNEITVPGTTTSVTLTGLKPGTEYEVRVQAV 76
FN3 cd00063
Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein ...
 397-467 4.30e-06

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


Pssm-ID: 238020 [Multi-domain]  Cd Length: 93  Bit Score: 46.34  E-value: 4.30e-06
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1622828204  397 PGQPQNVVCRHEDAHQGVITWNPPQRS---FHNFTLCYVSKTAKKCLSLDKHL---TTYHLQNLKPYTNYSLSLHAY 467
Cdd:cd00063      1 PSPPTNLRVTDVTSTSVTLSWTPPEDDggpITGYVVEYREKGSGDWKEVEVTPgseTSYTLTGLKPGTEYEFRVRAV 77
FN3 smart00060
Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, ...
 397-467 1.31e-04

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


Pssm-ID: 214495 [Multi-domain]  Cd Length: 83  Bit Score: 41.83  E-value: 1.31e-04
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1622828204   397 PGQPQNVVCRHEDAHQGVITWNPPQRSFHN-----FTLCYVSKTAK-KCLSLDKHLTTYHLQNLKPYTNYSLSLHAY 467
Cdd:smart00060    1 PSPPSNLRVTDVTSTSVTLSWEPPPDDGITgyivgYRVEYREEGSEwKEVNVTPSSTSYTLTGLKPGTEYEFRVRAV 77
FN3 cd00063
Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein ...
 490-570 2.47e-04

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


Pssm-ID: 238020 [Multi-domain]  Cd Length: 93  Bit Score: 41.33  E-value: 2.47e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622828204  490 PSQVQNMIVS-TSDNSMRVKCEAPRDVNGPTELYLLEVEAGN----TLVRNLSQSECDFSVNNLQYSTYYNLKAYYHNGK 564
Cdd:cd00063      1 PSPPTNLRVTdVTSTSVTLSWTPPEDDGGPITGYVVEYREKGsgdwKEVEVTPGSETSYTLTGLKPGTEYEFRVRAVNGG 80


                   ....*.
gi 1622828204  565 YSGEPV 570
Cdd:cd00063     81 GESPPS 86
fn3 pfam00041
Fibronectin type III domain;
491-569 1.23e-03

Fibronectin type III domain;


Pssm-ID: 394996 [Multi-domain]  Cd Length: 85  Bit Score: 39.32  E-value: 1.23e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622828204  491 SQVQNMIVS-TSDNSMRVKCEAPRDVNGPTELYLLEVEAGNT----LVRNLSQSECDFSVNNLQYSTYYNLKAYYHNGKY 565
Cdd:pfam00041    1 SAPSNLTVTdVTSTSLTVSWTPPPDGNGPITGYEVEYRPKNSgepwNEITVPGTTTSVTLTGLKPGTEYEVRVQAVNGGG 80


                   ....
gi 1622828204  566 SGEP 569
Cdd:pfam00041   81 EGPP 84
 
Name Accession Description Interval E-value
R-PTPc-C-1 cd14557
catalytic domain of receptor-type tyrosine-protein phosphatase C, repeat 1; Receptor-type ...
 711-911 1.15e-149

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: 449.66  E-value: 1.15e-149
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622828204  711 YINASYIDGFKEPRKYIAAQGPRDETVDDFWRMIWEQKATVIVMVTRCEEGNRNKCAEYWPSMEEGTRAFGDVVVKINQH 790
Cdd:cd14557      1 YINASYIDGFKEPRKYIAAQGPKDETVDDFWRMIWEQKSTVIVMVTRCEEGNRNKCAQYWPSMEEGSRAFGDVVVKINEE 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622828204  791 KRCPDYIIQKLNIVNKKEKATGREVTHIQFTSWPDHGVPEDPHLLLKLRRRVNAFSNFFSGPIVVHCSAGVGRTGTYIGI 870
Cdd:cd14557     81 KICPDYIIRKLNINNKKEKGSGREVTHIQFTSWPDHGVPEDPHLLLKLRRRVNAFNNFFSGPIVVHCSAGVGRTGTYIGI 160

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|.
gi 1622828204  871 DAMLEGLEAENKVDVYGYVVKLRRQRCLMVQVEAQYILIHQ 911
Cdd:cd14557    161 DAMLEGLEAEGRVDVYGYVVKLRRQRCLMVQVEAQYILIHQ 201
R-PTP-C-2 cd14558
PTP-like domain of receptor-type tyrosine-protein phosphatase C, repeat 2; Receptor-type ...
 1021-1227 1.05e-127

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: 391.76  E-value: 1.05e-127
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622828204 1021 YINASFIMSYWKPEVMIAAQGPLKETIGDFWQMIFQRKVKVIVMLTELKHGDQEICAQYWGEGKQTYGDIEVDMKDTNKS 1100
Cdd:cd14558      1 YINASFIDGYWGPKSLIATQGPLPDTIADFWQMIFQKKVKVIVMLTELKEGDQEQCAQYWGDEKKTYGDIEVELKDTEKS 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622828204 1101 STYTLRVFELRHSKRKDSRTVYQYQYTNWSVEQLPAEPKELVSLIQVLKEKLPQKNSsegnKHHKSTPLLIHCRDGSQQT 1180
Cdd:cd14558     81 PTYTVRVFEITHLKRKDSRTVYQYQYHKWKGEELPEKPKDLVDMIKSIKQKLPYKNS----KHGRSVPIVVHCSDGSSRT 156

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*..
gi 1622828204 1181 GIFCALLNLLESAETEEVVDIFQVVKALRKARPGMVSTFEQYQFLYD 1227
Cdd:cd14558    157 GIFCALWNLLESAETEKVVDVFQVVKALRKQRPGMVSTLEQYQFLYD 203
PTPc smart00194
Protein tyrosine phosphatase, catalytic domain;
656-915 2.87e-111

Protein tyrosine phosphatase, catalytic domain;


Pssm-ID: 214550 [Multi-domain]  Cd Length: 259  Bit Score: 349.65  E-value: 2.87e-111
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622828204   656 LFLAEFQSIPRVFS-KFPIKEARKPFNQNKNRYVDILPYDYNRVELSEINGDaGSNYINASYIDGFKEPRKYIAAQGPRD 734
Cdd:smart00194    1 GLEEEFEKLDRLKPdDESCTVAAFPENRDKNRYKDVLPYDHTRVKLKPPPGE-GSDYINASYIDGPNGPKAYIATQGPLP 79

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622828204   735 ETVDDFWRMIWEQKATVIVMVTRCEEGNRNKCAEYWPSMEEGTRAFGDVVVKINQHKRCPDYIIQKLNIVNKKEKATgRE 814
Cdd:smart00194   80 STVEDFWRMVWEQKVTVIVMLTELVEKGREKCAQYWPDEEGEPLTYGDITVTLKSVEKVDDYTIRTLEVTNTGCSET-RT 158

                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622828204   815 VTHIQFTSWPDHGVPEDPHLLLKLRRRVNAFSNFFSGPIVVHCSAGVGRTGTYIGIDAMLEGLEAENKVDVYGYVVKLRR 894
Cdd:smart00194  159 VTHYHYTNWPDHGVPESPESILDLIRAVRKSQSTSTGPIVVHCSAGVGRTGTFIAIDILLQQLEAGKEVDIFEIVKELRS 238

                           250       260
                    ....*....|....*....|.
gi 1622828204   895 QRCLMVQVEAQYILIHQALVE 915
Cdd:smart00194  239 QRPGMVQTEEQYIFLYRAILE 259
Y_phosphatase pfam00102
Protein-tyrosine phosphatase;
681-915 3.23e-107

Protein-tyrosine phosphatase;


Pssm-ID: 459674 [Multi-domain]  Cd Length: 234  Bit Score: 337.68  E-value: 3.23e-107
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622828204  681 NQNKNRYVDILPYDYNRVELSEINGDagSNYINASYIDGFKEPRKYIAAQGPRDETVDDFWRMIWEQKATVIVMVTRCEE 760
Cdd:pfam00102    1 NLEKNRYKDVLPYDHTRVKLTGDPGP--SDYINASYIDGYKKPKKYIATQGPLPNTVEDFWRMVWEEKVTIIVMLTELEE 78

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622828204  761 GNRNKCAEYWPSMEEGTRAFGDVVVKI-NQHKRCPDYIIQKLNIVNKKEKATgREVTHIQFTSWPDHGVPEDPHLLLKLR 839
Cdd:pfam00102   79 KGREKCAQYWPEEEGESLEYGDFTVTLkKEKEDEKDYTVRTLEVSNGGSEET-RTVKHFHYTGWPDHGVPESPNSLLDLL 157

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1622828204  840 RRVNAFSN-FFSGPIVVHCSAGVGRTGTYIGIDAMLEGLEAENKVDVYGYVVKLRRQRCLMVQVEAQYILIHQALVE 915
Cdd:pfam00102  158 RKVRKSSLdGRSGPIVVHCSAGIGRTGTFIAIDIALQQLEAEGEVDIFQIVKELRSQRPGMVQTLEQYIFLYDAILE 234
R-PTPc-LAR-1 cd14553
catalytic domain of LAR family receptor-type tyrosine-protein phosphatases, repeat 1; The LAR ...
 681-915 2.14e-97

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: 311.25  E-value: 2.14e-97
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622828204  681 NQNKNRYVDILPYDYNRVELSEINGDAGSNYINASYIDGFKEPRKYIAAQGPRDETVDDFWRMIWEQKATVIVMVTRCEE 760
Cdd:cd14553      3 NKPKNRYANVIAYDHSRVILQPIEGVPGSDYINANYCDGYRKQNAYIATQGPLPETFGDFWRMVWEQRSATIVMMTKLEE 82

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622828204  761 GNRNKCAEYWPSmeEGTRAFGDVVVKINQHKRCPDYIIQKLNIVNKKEKATgREVTHIQFTSWPDHGVPEDPHLLLKLRR 840
Cdd:cd14553     83 RSRVKCDQYWPT--RGTETYGLIQVTLLDTVELATYTVRTFALHKNGSSEK-REVRQFQFTAWPDHGVPEHPTPFLAFLR 159

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1622828204  841 RVNAFSNFFSGPIVVHCSAGVGRTGTYIGIDAMLEGLEAENKVDVYGYVVKLRRQRCLMVQVEAQYILIHQALVE 915
Cdd:cd14553    160 RVKACNPPDAGPIVVHCSAGVGRTGCFIVIDSMLERIKHEKTVDIYGHVTCLRAQRNYMVQTEDQYIFIHDALLE 234
PTPc cd00047
catalytic domain of protein tyrosine phosphatases; Protein tyrosine phosphatases (PTP, EC 3.1. ...
 711-911 2.13e-95

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: 304.21  E-value: 2.13e-95
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622828204  711 YINASYIDGFKEPRKYIAAQGPRDETVDDFWRMIWEQKATVIVMVTRCEEGNRNKCAEYWPSMEEGTRAFGDVVVKINQH 790
Cdd:cd00047      1 YINASYIDGYRGPKEYIATQGPLPNTVEDFWRMVWEQKVSVIVMLTNLVEKGREKCERYWPEEGGKPLEYGDITVTLVSE 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622828204  791 KRCPDYIIQKLNIVNKKEKATgREVTHIQFTSWPDHGVPEDPHLLLKLRRRVNAFSNFFSGPIVVHCSAGVGRTGTYIGI 870
Cdd:cd00047     81 EELSDYTIRTLELSPKGCSES-REVTHLHYTGWPDHGVPSSPEDLLALVRRVRKEARKPNGPIVVHCSAGVGRTGTFIAI 159

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|.
gi 1622828204  871 DAMLEGLEAENKVDVYGYVVKLRRQRCLMVQVEAQYILIHQ 911
Cdd:cd00047    160 DILLERLEAEGEVDVFEIVKALRKQRPGMVQTLEQYEFIYE 200
R3-PTPc cd14548
catalytic domain of R3 subfamily receptor-type tyrosine-protein phosphatases and similar ...
 686-911 8.18e-93

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: 298.11  E-value: 8.18e-93
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622828204  686 RYVDILPYDYNRVELSEINGDAGSNYINASYIDGFKEPRKYIAAQGPRDETVDDFWRMIWEQKATVIVMVTRCEEGNRNK 765
Cdd:cd14548      1 RYTNILPYDHSRVKLIPINEEEGSDYINANYIPGYNSPREFIATQGPLPGTKDDFWRMVWEQNSHTIVMLTQCMEKGRVK 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622828204  766 CAEYWPSMEEGTrAFGDVVVKINQHKRCPDYIIQKLNIVNKKEKatgREVTHIQFTSWPDHGVPEDPHLLLKLRRRVNAF 845
Cdd:cd14548     81 CDHYWPFDQDPV-YYGDITVTMLSESVLPDWTIREFKLERGDEV---RSVRQFHFTAWPDHGVPEAPDSLLRFVRLVRDY 156

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1622828204  846 SNFFSGPIVVHCSAGVGRTGTYIGIDAMLEGLEAENKVDVYGYVVKLRRQRCLMVQVEAQYILIHQ 911
Cdd:cd14548    157 IKQEKGPTIVHCSAGVGRTGTFIALDRLLQQIESEDYVDIFGIVYDLRKHRPLMVQTEAQYIFLHQ 222
PTPc smart00194
Protein tyrosine phosphatase, catalytic domain;
948-1230 8.22e-93

Protein tyrosine phosphatase, catalytic domain;


Pssm-ID: 214550 [Multi-domain]  Cd Length: 259  Bit Score: 299.57  E-value: 8.22e-93
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622828204   948 LEAEFQRLPSYRSW-RTQHIGNQEENKNKNRNSNVIPYDYNRVPLKHELEmskesdhdsdessdddsdseEPSKYINASF 1026
Cdd:smart00194    2 LEEEFEKLDRLKPDdESCTVAAFPENRDKNRYKDVLPYDHTRVKLKPPPG--------------------EGSDYINASY 61

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622828204  1027 IMSYWKPEVMIAAQGPLKETIGDFWQMIFQRKVKVIVMLTELKHGDQEICAQYW---GEGKQTYGDIEVDMKDTNKSSTY 1103
Cdd:smart00194   62 IDGPNGPKAYIATQGPLPSTVEDFWRMVWEQKVTVIVMLTELVEKGREKCAQYWpdeEGEPLTYGDITVTLKSVEKVDDY 141

                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622828204  1104 TLRVFELRHSKRKDSRTVYQYQYTNWSVEQLPAEPKELVSLIQVLKEKLPqknssegnkhHKSTPLLIHCRDGSQQTGIF 1183
Cdd:smart00194  142 TIRTLEVTNTGCSETRTVTHYHYTNWPDHGVPESPESILDLIRAVRKSQS----------TSTGPIVVHCSAGVGRTGTF 211

                           250       260       270       280
                    ....*....|....*....|....*....|....*....|....*..
gi 1622828204  1184 CALLNLLESAETEEVVDIFQVVKALRKARPGMVSTFEQYQFLYDIIA 1230
Cdd:smart00194  212 IAIDILLQQLEAGKEVDIFEIVKELRSQRPGMVQTEEQYIFLYRAIL 258
R-PTPc-A-1 cd14621
catalytic domain of receptor-type tyrosine-protein phosphatase A, repeat 1; Receptor-type ...
 636-924 4.31e-89

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: 290.77  E-value: 4.31e-89
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622828204  636 PIHADILLETYKRKIADEGRLFLAEFQSIPRVFSKFPIKEARKPFNQNKNRYVDILPYDYNRVELSEINGDAGSNYINAS 715
Cdd:cd14621      7 PLPVDKLEEEINRRMADDNKLFREEFNALPACPIQATCEAASKEENKEKNRYVNILPYDHSRVHLTPVEGVPDSDYINAS 86

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622828204  716 YIDGFKEPRKYIAAQGPRDETVDDFWRMIWEQKATVIVMVTRCEEGNRNKCAEYWPsmEEGTRAFGDVVVKINQHKRCPD 795
Cdd:cd14621     87 FINGYQEKNKFIAAQGPKEETVNDFWRMIWEQNTATIVMVTNLKERKECKCAQYWP--DQGCWTYGNIRVSVEDVTVLVD 164

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622828204  796 YIIQKL------NIVNKKEKatgREVTHIQFTSWPDHGVPEDPHLLLKLRRRVNAFSNFFSGPIVVHCSAGVGRTGTYIG 869
Cdd:cd14621    165 YTVRKFciqqvgDVTNKKPQ---RLITQFHFTSWPDFGVPFTPIGMLKFLKKVKNCNPQYAGAIVVHCSAGVGRTGTFIV 241

                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1622828204  870 IDAMLEGLEAENKVDVYGYVVKLRRQRCLMVQVEAQYILIHQALVEYNQFGETEV 924
Cdd:cd14621    242 IDAMLDMMHAERKVDVYGFVSRIRAQRCQMVQTDMQYVFIYQALLEHYLYGDTEL 296
Y_phosphatase pfam00102
Protein-tyrosine phosphatase;
972-1230 1.17e-83

Protein-tyrosine phosphatase;


Pssm-ID: 459674 [Multi-domain]  Cd Length: 234  Bit Score: 272.96  E-value: 1.17e-83
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622828204  972 NKNKNRNSNVIPYDYNRVPLKHElemskesdhdsdessdddsdsEEPSKYINASFIMSYWKPEVMIAAQGPLKETIGDFW 1051
Cdd:pfam00102    1 NLEKNRYKDVLPYDHTRVKLTGD---------------------PGPSDYINASYIDGYKKPKKYIATQGPLPNTVEDFW 59

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622828204 1052 QMIFQRKVKVIVMLTELKHGDQEICAQYW---GEGKQTYGDIEVDMKDTNK-SSTYTLRVFELRHSKRKDSRTVYQYQYT 1127
Cdd:pfam00102   60 RMVWEEKVTIIVMLTELEEKGREKCAQYWpeeEGESLEYGDFTVTLKKEKEdEKDYTVRTLEVSNGGSEETRTVKHFHYT 139

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622828204 1128 NWSVEQLPAEPKELVSLIQVLkeklpqKNSSEGNKHHkstPLLIHCRDGSQQTGIFCALLNLLESAETEEVVDIFQVVKA 1207
Cdd:pfam00102  140 GWPDHGVPESPNSLLDLLRKV------RKSSLDGRSG---PIVVHCSAGIGRTGTFIAIDIALQQLEAEGEVDIFQIVKE 210

                          250       260
                   ....*....|....*....|...
gi 1622828204 1208 LRKARPGMVSTFEQYQFLYDIIA 1230
Cdd:pfam00102  211 LRSQRPGMVQTLEQYIFLYDAIL 233
R5-PTPc-1 cd14549
catalytic domain of R5 subfamily receptor-type tyrosine-protein phosphatases, repeat 1; The R5 ...
 711-910 2.51e-83

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: 270.76  E-value: 2.51e-83
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622828204  711 YINASYIDGFKEPRKYIAAQGPRDETVDDFWRMIWEQKATVIVMVTRCEEGNRNKCAEYWPSmeEGTRAFGDVVVKINQH 790
Cdd:cd14549      1 YINANYVDGYNKARAYIATQGPLPSTFDDFWRMVWEQNSAIIVMITNLVERGRRKCDQYWPK--EGTETYGNIQVTLLST 78

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622828204  791 KRCPDYIIQKLNIVNKKEK-----ATGREVTHIQFTSWPDHGVPEDPHLLLKLRRRVNAFSNFFSGPIVVHCSAGVGRTG 865
Cdd:cd14549     79 EVLATYTVRTFSLKNLKLKkvkgrSSERVVYQYHYTQWPDHGVPDYTLPVLSFVRKSSAANPPGAGPIVVHCSAGVGRTG 158

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*
gi 1622828204  866 TYIGIDAMLEGLEAENKVDVYGYVVKLRRQRCLMVQVEAQYILIH 910
Cdd:cd14549    159 TYIVIDSMLQQIQDKGTVNVFGFLKHIRTQRNYLVQTEEQYIFIH 203
R-PTPc-E-1 cd14620
catalytic domain of receptor-type tyrosine-protein phosphatase E, repeat 1; Receptor-type ...
 687-915 6.02e-81

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: 265.27  E-value: 6.02e-81
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622828204  687 YVDILPYDYNRVELSEINGDAGSNYINASYIDGFKEPRKYIAAQGPRDETVDDFWRMIWEQKATVIVMVTRCEEGNRNKC 766
Cdd:cd14620      1 YPNILPYDHSRVILSQLDGIPCSDYINASYIDGYKEKNKFIAAQGPKQETVNDFWRMVWEQKSATIVMLTNLKERKEEKC 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622828204  767 AEYWPsmEEGTRAFGDVVVKINQHKRCPDYIIQKLNIVNKKEKAT--GREVTHIQFTSWPDHGVPEDPHLLLKLRRRVNA 844
Cdd:cd14620     81 YQYWP--DQGCWTYGNIRVAVEDCVVLVDYTIRKFCIQPQLPDGCkaPRLVTQLHFTSWPDFGVPFTPIGMLKFLKKVKS 158

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1622828204  845 FSNFFSGPIVVHCSAGVGRTGTYIGIDAMLEGLEAENKVDVYGYVVKLRRQRCLMVQVEAQYILIHQALVE 915
Cdd:cd14620    159 VNPVHAGPIVVHCSAGVGRTGTFIVIDAMIDMMHAEQKVDVFEFVSRIRNQRPQMVQTDMQYSFIYQALLE 229
PTPc-N9 cd14543
catalytic domain of tyrosine-protein phosphatase non-receptor type 9; Tyrosine-protein ...
 676-910 1.92e-80

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: 265.38  E-value: 1.92e-80
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622828204  676 ARKPFNQNKNRYVDILPYDYNRVELSEINGDAGSNYINASYIDGFKEPRKYIAAQGPRDETVDDFWRMIWEQKATVIVMV 755
Cdd:cd14543     24 SLAPANQEKNRYGDVLCLDQSRVKLPKRNGDERTDYINANFMDGYKQKNAYIATQGPLPKTYSDFWRMVWEQKVLVIVMT 103

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622828204  756 TRCEEGNRNKCAEYWPSMEEGTRAFGDVVVkINQHKRC-PDYIIQKLNIVNKKEKATgREVTHIQFTSWPDHGVPEDPHL 834
Cdd:cd14543    104 TRVVERGRVKCGQYWPLEEGSSLRYGDLTV-TNLSVENkEHYKKTTLEIHNTETDES-RQVTHFQFTSWPDFGVPSSAAA 181

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622828204  835 LL--------KLRRRVNAFSNFFSG-----PIVVHCSAGVGRTGTYIGIDAMLEGLEAENKVDVYGYVVKLRRQRCLMVQ 901
Cdd:cd14543    182 LLdflgevrqQQALAVKAMGDRWKGhppgpPIVVHCSAGIGRTGTFCTLDICLSQLEDVGTLNVMQTVRRMRTQRAFSIQ 261


                   ....*....
gi 1622828204  902 VEAQYILIH 910
Cdd:cd14543    262 TPDQYYFCY 270
R-PTPc-F-1 cd14626
catalytic domain of receptor-type tyrosine-protein phosphatase F, repeat 1; Receptor-type ...
 642-915 2.40e-80

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: 265.36  E-value: 2.40e-80
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622828204  642 LLETYKRKIADEGRLFLAEFQSI-PRvfSKFPIKEARKPFNQNKNRYVDILPYDYNRVELSEINGDAGSNYINASYIDGF 720
Cdd:cd14626      3 LADNIERLKANDGLKFSQEYESIdPG--QQFTWENSNLEVNKPKNRYANVIAYDHSRVILTSVDGVPGSDYINANYIDGY 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622828204  721 KEPRKYIAAQGPRDETVDDFWRMIWEQKATVIVMVTRCEEGNRNKCAEYWPSmeEGTRAFGDVVVKINQHKRCPDYIIQK 800
Cdd:cd14626     81 RKQNAYIATQGPLPETLSDFWRMVWEQRTATIVMMTRLEEKSRVKCDQYWPI--RGTETYGMIQVTLLDTVELATYSVRT 158

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622828204  801 LNiVNKKEKATGREVTHIQFTSWPDHGVPEDPHLLLKLRRRVNAFSNFFSGPIVVHCSAGVGRTGTYIGIDAMLEGLEAE 880
Cdd:cd14626    159 FA-LYKNGSSEKREVRQFQFMAWPDHGVPEYPTPILAFLRRVKACNPPDAGPMVVHCSAGVGRTGCFIVIDAMLERMKHE 237

                          250       260       270
                   ....*....|....*....|....*....|....*
gi 1622828204  881 NKVDVYGYVVKLRRQRCLMVQVEAQYILIHQALVE 915
Cdd:cd14626    238 KTVDIYGHVTCMRSQRNYMVQTEDQYIFIHEALLE 272
PTPc cd00047
catalytic domain of protein tyrosine phosphatases; Protein tyrosine phosphatases (PTP, EC 3.1. ...
 1021-1227 1.23e-79

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: 260.30  E-value: 1.23e-79
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622828204 1021 YINASFIMSYWKPEVMIAAQGPLKETIGDFWQMIFQRKVKVIVMLTELKHGDQEICAQYW---GEGKQTYGDIEVDMKDT 1097
Cdd:cd00047      1 YINASYIDGYRGPKEYIATQGPLPNTVEDFWRMVWEQKVSVIVMLTNLVEKGREKCERYWpeeGGKPLEYGDITVTLVSE 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622828204 1098 NKSSTYTLRVFELRHSKRKDSRTVYQYQYTNWSVEQLPAEPKELVSLIQVLKEKLPQKNSsegnkhhkstPLLIHCRDGS 1177
Cdd:cd00047     81 EELSDYTIRTLELSPKGCSESREVTHLHYTGWPDHGVPSSPEDLLALVRRVRKEARKPNG----------PIVVHCSAGV 150

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|
gi 1622828204 1178 QQTGIFCALLNLLESAETEEVVDIFQVVKALRKARPGMVSTFEQYQFLYD 1227
Cdd:cd00047    151 GRTGTFIAIDILLERLEAEGEVDVFEIVKALRKQRPGMVQTLEQYEFIYE 200
R-PTPc-H cd14619
catalytic domain of receptor-type tyrosine-protein phosphatase H; Receptor-type ...
 685-916 9.07e-77

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: 253.66  E-value: 9.07e-77
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622828204  685 NRYVDILPYDYNRVELSEINGDAGSNYINASYIDGFKEPRKYIAAQGPRDETVDDFWRMIWEQKATVIVMVTRCEEGNRN 764
Cdd:cd14619      1 NRFRNVLPYDWSRVPLKPIHEEPGSDYINANYMPGYWSSQEFIATQGPLPQTVGDFWRMIWEQQSSTIVMLTNCMEAGRV 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622828204  765 KCAEYWPsMEEGTRAFGDVVVKINQHKRCPDYIIQKLNIVNKKEKATgREVTHIQFTSWPDHGVPEDPHLLLKLRRRVNA 844
Cdd:cd14619     81 KCEHYWP-LDYTPCTYGHLRVTVVSEEVMENWTVREFLLKQVEEQKT-LSVRHFHFTAWPDHGVPSSTDTLLAFRRLLRQ 158

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1622828204  845 F--SNFFSGPIVVHCSAGVGRTGTYIGIDAMLEGLEAENKVDVYGYVVKLRRQRCLMVQVEAQYILIHQALVEY 916
Cdd:cd14619    159 WldQTMSGGPTVVHCSAGVGRTGTLIALDVLLQQLQSEGLLGPFSFVQKMRENRPLMVQTESQYVFLHQCILDF 232
R-PTPc-A-E-1 cd14551
catalytic domain of receptor-type tyrosine-protein phosphatase A and E, repeat 1; ...
 711-911 3.93e-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: 250.60  E-value: 3.93e-76
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622828204  711 YINASYIDGFKEPRKYIAAQGPRDETVDDFWRMIWEQKATVIVMVTRCEEGNRNKCAEYWPsmEEGTRAFGDVVVKINQH 790
Cdd:cd14551      1 YINASYIDGYQEKNKFIAAQGPKDETVNDFWRMIWEQGSATIVMVTNLKERKEKKCSQYWP--DQGCWTYGNLRVRVEDT 78

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622828204  791 KRCPDYIIQKLnIVNKKEKATG----REVTHIQFTSWPDHGVPEDPHLLLKLRRRVNAFSNFFSGPIVVHCSAGVGRTGT 866
Cdd:cd14551     79 VVLVDYTTRKF-CIQKVNRGIGekrvRLVTQFHFTSWPDFGVPFTPIGMLKFLKKVKSANPPRAGPIVVHCSAGVGRTGT 157

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*
gi 1622828204  867 YIGIDAMLEGLEAENKVDVYGYVVKLRRQRCLMVQVEAQYILIHQ 911
Cdd:cd14551    158 FIVIDAMLDMMHAEGKVDVFGFVSRIRQQRSQMVQTDMQYVFIYQ 202
R-PTPc-B cd14617
catalytic domain of receptor-type tyrosine-protein phosphatase B; Receptor-type ...
 685-911 8.11e-75

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: 247.91  E-value: 8.11e-75
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622828204  685 NRYVDILPYDYNRVELSEINGDAGSNYINASYIDGFKEPRKYIAAQGPRDETVDDFWRMIWEQKATVIVMVTRCEEGNRN 764
Cdd:cd14617      1 NRYNNILPYDSTRVKLSNVDDDPCSDYINASYIPGNNFRREYIATQGPLPGTKDDFWKMVWEQNVHNIVMVTQCVEKGRV 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622828204  765 KCAEYWPsMEEGTRAFGDVVVKINQHKRCPDYIIQKLNIVNKKEKATGREVTHIQFTSWPDHGVPEDPHLLLKLRRRVNA 844
Cdd:cd14617     81 KCDHYWP-ADQDSLYYGDLIVQMLSESVLPEWTIREFKICSEEQLDAPRLVRHFHYTVWPDHGVPETTQSLIQFVRTVRD 159

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1622828204  845 FSNFF--SGPIVVHCSAGVGRTGTYIGIDAMLEGLEAENKVDVYGYVVKLRRQRCLMVQVEAQYILIHQ 911
Cdd:cd14617    160 YINRTpgSGPTVVHCSAGVGRTGTFIALDRILQQLDSKDSVDIYGAVHDLRLHRVHMVQTECQYVYLHQ 228
R-PTPc-J cd14615
catalytic domain of receptor-type tyrosine-protein phosphatase J; Receptor-type ...
 685-911 3.21e-74

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: 246.27  E-value: 3.21e-74
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622828204  685 NRYVDILPYDYNRVELSeINGDAGSNYINASYIDGFKEPRKYIAAQGPRDETVDDFWRMIWEQKATVIVMVTRCEEGNRN 764
Cdd:cd14615      1 NRYNNVLPYDISRVKLS-VQSHSTDDYINANYMPGYNSKKEFIAAQGPLPNTVKDFWRMVWEKNVYAIVMLTKCVEQGRT 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622828204  765 KCAEYWPSmeEGTRAFGDVVVKINQHKRCPDYIIQKLNIVNKKEkATGREVTHIQFTSWPDHGVPEDPHLLLKLRRRVNA 844
Cdd:cd14615     80 KCEEYWPS--KQKKDYGDITVTMTSEIVLPEWTIRDFTVKNAQT-NESRTVRHFHFTSWPDHGVPETTDLLINFRHLVRE 156

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1622828204  845 FS--NFFSGPIVVHCSAGVGRTGTYIGIDAMLEGLEAENKVDVYGYVVKLRRQRCLMVQVEAQYILIHQ 911
Cdd:cd14615    157 YMkqNPPNSPILVHCSAGVGRTGTFIAIDRLIYQIENENVVDVYGIVYDLRMHRPLMVQTEDQYVFLNQ 225
R-PTPc-S-1 cd14625
catalytic domain of receptor-type tyrosine-protein phosphatase S, repeat 1; Receptor-type ...
 636-915 1.11e-72

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: 243.85  E-value: 1.11e-72
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622828204  636 PIHADILLETYKRKIADEGRLFLAEFQSIPRvFSKFPIKEARKPFNQNKNRYVDILPYDYNRVELSEINGDAGSNYINAS 715
Cdd:cd14625      3 PIPISELAEHTERLKANDNLKLSQEYESIDP-GQQFTWEHSNLEVNKPKNRYANVIAYDHSRVILQPIEGIMGSDYINAN 81

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622828204  716 YIDGFKEPRKYIAAQGPRDETVDDFWRMIWEQKATVIVMVTRCEEGNRNKCAEYWPSmeEGTRAFGDVVVKINQHKRCPD 795
Cdd:cd14625     82 YIDGYRKQNAYIATQGPLPETFGDFWRMVWEQRSATVVMMTKLEEKSRIKCDQYWPS--RGTETYGMIQVTLLDTIELAT 159

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622828204  796 YIIQKLNIvNKKEKATGREVTHIQFTSWPDHGVPEDPHLLLKLRRRVNAFSNFFSGPIVVHCSAGVGRTGTYIGIDAMLE 875
Cdd:cd14625    160 FCVRTFSL-HKNGSSEKREVRQFQFTAWPDHGVPEYPTPFLAFLRRVKTCNPPDAGPIVVHCSAGVGRTGCFIVIDAMLE 238

                          250       260       270       280
                   ....*....|....*....|....*....|....*....|
gi 1622828204  876 GLEAENKVDVYGYVVKLRRQRCLMVQVEAQYILIHQALVE 915
Cdd:cd14625    239 RIKHEKTVDIYGHVTLMRSQRNYMVQTEDQYSFIHDALLE 278
R-PTPc-D-1 cd14624
catalytic domain of receptor-type tyrosine-protein phosphatase D, repeat 1; Receptor-type ...
 636-915 1.36e-72

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: 243.87  E-value: 1.36e-72
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622828204  636 PIHADILLETYKRKIADEGRLFLAEFQSIPRvFSKFPIKEARKPFNQNKNRYVDILPYDYNRVELSEINGDAGSNYINAS 715
Cdd:cd14624      3 PIPILELADHIERLKANDNLKFSQEYESIDP-GQQFTWEHSNLEVNKPKNRYANVIAYDHSRVLLSAIEGIPGSDYINAN 81

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622828204  716 YIDGFKEPRKYIAAQGPRDETVDDFWRMIWEQKATVIVMVTRCEEGNRNKCAEYWPSmeEGTRAFGDVVVKINQHKRCPD 795
Cdd:cd14624     82 YIDGYRKQNAYIATQGALPETFGDFWRMIWEQRSATVVMMTKLEERSRVKCDQYWPS--RGTETYGLIQVTLLDTVELAT 159

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622828204  796 YIIQKLNIVnKKEKATGREVTHIQFTSWPDHGVPEDPHLLLKLRRRVNAFSNFFSGPIVVHCSAGVGRTGTYIGIDAMLE 875
Cdd:cd14624    160 YCVRTFALY-KNGSSEKREVRQFQFTAWPDHGVPEHPTPFLAFLRRVKTCNPPDAGPMVVHCSAGVGRTGCFIVIDAMLE 238

                          250       260       270       280
                   ....*....|....*....|....*....|....*....|
gi 1622828204  876 GLEAENKVDVYGYVVKLRRQRCLMVQVEAQYILIHQALVE 915
Cdd:cd14624    239 RIKHEKTVDIYGHVTLMRAQRNYMVQTEDQYIFIHDALLE 278
PTPc-KIM cd14547
catalytic domain of the kinase interaction motif (KIM) family of protein-tyrosine phosphatases; ...
 685-911 3.16e-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: 240.38  E-value: 3.16e-72
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622828204  685 NRYVDILPYDYNRVELSEINGDAGSNYINASYIDGFK-EPRKYIAAQGPRDETVDDFWRMIWEQKATVIVMVTRCEEGNR 763
Cdd:cd14547      1 NRYKTILPNEHSRVCLPSVDDDPLSSYINANYIRGYDgEEKAYIATQGPLPNTVADFWRMVWQEKTPIIVMITNLTEAKE 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622828204  764 nKCAEYWPsMEEGTRaFGDVVVKINQHKRCPDYIIQKLNIVNKKEKatgREVTHIQFTSWPDHGVPEDPHLLLKLRRRVN 843
Cdd:cd14547     81 -KCAQYWP-EEENET-YGDFEVTVQSVKETDGYTVRKLTLKYGGEK---RYLKHYWYTSWPDHKTPEAAQPLLSLVQEVE 154

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622828204  844 --AFSNFFSGPIVVHCSAGVGRTGTYIGIDAMLEGLEAENKVDVYGYVVKLRRQRCLMVQVEAQYILIHQ 911
Cdd:cd14547    155 eaRQTEPHRGPIVVHCSAGIGRTGCFIATSIGCQQLREEGVVDVLGIVCQLRLDRGGMVQTAEQYEFVHR 224
R-PTPc-O cd14614
catalytic domain of receptor-type tyrosine-protein phosphatase O; Receptor-type ...
 676-911 4.83e-72

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: 240.56  E-value: 4.83e-72
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622828204  676 ARKPFNQNKNRYVDILPYDYNRVELSEINGDAGSNYINASYIDGFKEPRKYIAAQGPRDETVDDFWRMIWEQKATVIVMV 755
Cdd:cd14614      7 ADLPVNRCKNRYTNILPYDFSRVKLVSMHEEEGSDYINANYIPGYNSPQEYIATQGPLPETRNDFWKMVLQQKSQIIVML 86

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622828204  756 TRCEEGNRNKCAEYWPSMEEGTrAFGDVVVKINQHKRCPDYIIQKLNIVNKKEKatgREVTHIQFTSWPDHGVP--EDPH 833
Cdd:cd14614     87 TQCNEKRRVKCDHYWPFTEEPV-AYGDITVEMLSEEEQPDWAIREFRVSYADEV---QDVMHFNYTAWPDHGVPtaNAAE 162

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1622828204  834 LLLKLRRRVNAFSNFFSGPIVVHCSAGVGRTGTYIGIDAMLEGLEAENKVDVYGYVVKLRRQRCLMVQVEAQYILIHQ 911
Cdd:cd14614    163 SILQFVQMVRQQAVKSKGPMIIHCSAGVGRTGTFIALDRLLQHIRDHEFVDILGLVSEMRSYRMSMVQTEEQYIFIHQ 240
R-PTPc-G-1 cd17667
catalytic domain of receptor-type tyrosine-protein phosphatase G, repeat 1; Receptor-type ...
 657-915 7.93e-71

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: 238.40  E-value: 7.93e-71
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622828204  657 FLAEFQSIPRVFSKFPI--KEARKPFNQNKNRYVDILPYDYNRVELSEINGDAG--SNYINASYIDGFKEPRKYIAAQGP 732
Cdd:cd17667      1 FSEDFEEVQRCTADMNItaEHSNHPDNKHKNRYINILAYDHSRVKLRPLPGKDSkhSDYINANYVDGYNKAKAYIATQGP 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622828204  733 RDETVDDFWRMIWEQKATVIVMVTRCEEGNRNKCAEYWPSmeEGTRAFGDVVVKINQHKRCPDYIIQKLNIVNKKEK--- 809
Cdd:cd17667     81 LKSTFEDFWRMIWEQNTGIIVMITNLVEKGRRKCDQYWPT--ENSEEYGNIIVTLKSTKIHACYTVRRFSIRNTKVKkgq 158

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622828204  810 ---ATGRE----VTHIQFTSWPDHGVPEDPHLLLKLRRRVNAFSNFFSGPIVVHCSAGVGRTGTYIGIDAMLEGLEAENK 882
Cdd:cd17667    159 kgnPKGRQnertVIQYHYTQWPDMGVPEYALPVLTFVRRSSAARTPEMGPVLVHCSAGVGRTGTYIVIDSMLQQIKDKST 238

                          250       260       270
                   ....*....|....*....|....*....|...
gi 1622828204  883 VDVYGYVVKLRRQRCLMVQVEAQYILIHQALVE 915
Cdd:cd17667    239 VNVLGFLKHIRTQRNYLVQTEEQYIFIHDALLE 271
R-PTPc-T-1 cd14630
catalytic domain of receptor-type tyrosine-protein phosphatase T, repeat 1; Receptor-type ...
 681-915 1.58e-70

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: 236.08  E-value: 1.58e-70
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622828204  681 NQNKNRYVDILPYDYNRVELSEINGDAGSNYINASYIDGFKEPRKYIAAQGPRDETVDDFWRMIWEQKATVIVMVTRCEE 760
Cdd:cd14630      3 NRNKNRYGNIISYDHSRVRLQLLDGDPHSDYINANYIDGYHRPRHYIATQGPMQETVKDFWRMIWQENSASVVMVTNLVE 82

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622828204  761 GNRNKCAEYWPsmeEGTRAFGDVVVKINQHKRCPDYIIQKLNiVNKKEKATGREVTHIQFTSWPDHGVPEDPHLLLKLRR 840
Cdd:cd14630     83 VGRVKCVRYWP---DDTEVYGDIKVTLIETEPLAEYVIRTFT-VQKKGYHEIREIRQFHFTSWPDHGVPCYATGLLGFVR 158

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1622828204  841 RVNAFSNFFSGPIVVHCSAGVGRTGTYIGIDAMLEGLEAENKVDVYGYVVKLRRQRCLMVQVEAQYILIHQALVE 915
Cdd:cd14630    159 QVKFLNPPDAGPIVVHCSAGAGRTGCFIAIDIMLDMAENEGVVDIFNCVRELRAQRVNMVQTEEQYVFVHDAILE 233
R-PTP-LAR-2 cd14554
PTP-like domain of the LAR family receptor-type tyrosine-protein phosphatases, repeat 2; The ...
 676-912 6.38e-69

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: 231.64  E-value: 6.38e-69
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622828204  676 ARKPFNQNKNRYVDILPYDYNRVELSEINGDAGSNYINASYIDGFKEPRKYIAAQGPRDETVDDFWRMIWEQKATVIVMV 755
Cdd:cd14554      1 ANLPCNKFKNRLVNILPYESTRVCLQPIRGVEGSDYINASFIDGYRQRGAYIATQGPLAETTEDFWRMLWEHNSTIIVML 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622828204  756 TRCEEGNRNKCAEYWPSmEEGTRAFGDVVVKINQHKRcPDYIIQKLNIVNKKEKaTGREVTHIQFTSWPDHGVPEDPHLL 835
Cdd:cd14554     81 TKLREMGREKCHQYWPA-ERSARYQYFVVDPMAEYNM-PQYILREFKVTDARDG-QSRTVRQFQFTDWPEQGVPKSGEGF 157

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1622828204  836 LKLRRRV-NAFSNF-FSGPIVVHCSAGVGRTGTYIGIDAMLEGLEAENKVDVYGYVVKLRRQRCLMVQVEAQYILIHQA 912
Cdd:cd14554    158 IDFIGQVhKTKEQFgQEGPITVHCSAGVGRTGVFITLSIVLERMRYEGVVDVFQTVKLLRTQRPAMVQTEDQYQFCYRA 236
PTPc-N11_6 cd14544
catalytic domain of tyrosine-protein phosphatase non-receptor type 11 and type 6; ...
 681-916 7.28e-69

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: 231.97  E-value: 7.28e-69
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622828204  681 NQNKNRYVDILPYDYNRVELSEINGD-AGSNYINASYI-------DGFKEPRKYIAAQGPRDETVDDFWRMIWEQKATVI 752
Cdd:cd14544      1 NKGKNRYKNILPFDHTRVILKDRDPNvPGSDYINANYIrnenegpTTDENAKTYIATQGCLENTVSDFWSMVWQENSRVI 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622828204  753 VMVTRCEEGNRNKCAEYWPSmEEGTRAFGDVVVKINQHKRCPDYIIQKLNIVNKKEKATGREVTHIQFTSWPDHGVPEDP 832
Cdd:cd14544     81 VMTTKEVERGKNKCVRYWPD-EGMQKQYGPYRVQNVSEHDTTDYTLRELQVSKLDQGDPIREIWHYQYLSWPDHGVPSDP 159

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622828204  833 HLLLKLRRRVNAFSNFF--SGPIVVHCSAGVGRTGTYIGIDAMLE-----GLEAEnkVDVYGYVVKLRRQRCLMVQVEAQ 905
Cdd:cd14544    160 GGVLNFLEDVNQRQESLphAGPIVVHCSAGIGRTGTFIVIDMLLDqikrkGLDCD--IDIQKTIQMVRSQRSGMVQTEAQ 237

                          250
                   ....*....|.
gi 1622828204  906 YILIHQALVEY 916
Cdd:cd14544    238 YKFIYVAVAQY 248
PTP_fungal cd18533
fungal protein tyrosine phosphatases; This subfamily contains Saccharomyces cerevisiae ...
 711-911 6.96e-67

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: 224.44  E-value: 6.96e-67
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622828204  711 YINASYID-GFKEPRKYIAAQGPRDETVDDFWRMIWEQKATVIVMVTRCEEGNRNKCAEYWPSmEEGTRAFGDVVVKINQ 789
Cdd:cd18533      1 YINASYITlPGTSSKRYIATQGPLPATIGDFWKMIWQNNVGVIVMLTPLVENGREKCDQYWPS-GEYEGEYGDLTVELVS 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622828204  790 HKRCPDYIIQKLNIVNKKEKATGREVTHIQFTSWPDHGVPEDPHLLLKLRRRVNA--FSNFFSGPIVVHCSAGVGRTGTY 867
Cdd:cd18533     80 EEENDDGGFIVREFELSKEDGKVKKVYHIQYKSWPDFGVPDSPEDLLTLIKLKRElnDSASLDPPIIVHCSAGVGRTGTF 159

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|...
gi 1622828204  868 IGIDAMLEGLEA--------ENKVD-VYGYVVKLRRQRCLMVQVEAQYILIHQ 911
Cdd:cd18533    160 IALDSLLDELKRglsdsqdlEDSEDpVYEIVNQLRKQRMSMVQTLRQYIFLYD 212
R-PTPc-M-1 cd14633
catalytic domain of receptor-type tyrosine-protein phosphatase M, repeat 1; Receptor-type ...
 640-915 2.07e-66

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: 225.69  E-value: 2.07e-66
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622828204  640 DILLETYKRKIAdEGRLFLAEFQSIPRVFSKfPIKEARKPFNQNKNRYVDILPYDYNRVELSEINGDAGSNYINASYIDG 719
Cdd:cd14633      1 DLLQHITQMKCA-EGYGFKEEYESFFEGQSA-PWDSAKKDENRMKNRYGNIIAYDHSRVRLQPIEGETSSDYINGNYIDG 78

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622828204  720 FKEPRKYIAAQGPRDETVDDFWRMIWEQKATVIVMVTRCEEGNRNKCAEYWPsmeEGTRAFGDVVVKINQHKRCPDYIIQ 799
Cdd:cd14633     79 YHRPNHYIATQGPMQETIYDFWRMVWHENTASIIMVTNLVEVGRVKCCKYWP---DDTEIYKDIKVTLIETELLAEYVIR 155

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622828204  800 KLnIVNKKEKATGREVTHIQFTSWPDHGVPEDPHLLLKLRRRVNAFSNFFSGPIVVHCSAGVGRTGTYIGIDAMLEGLEA 879
Cdd:cd14633    156 TF-AVEKRGVHEIREIRQFHFTGWPDHGVPYHATGLLGFVRQVKSKSPPNAGPLVVHCSAGAGRTGCFIVIDIMLDMAER 234

                          250       260       270
                   ....*....|....*....|....*....|....*.
gi 1622828204  880 ENKVDVYGYVVKLRRQRCLMVQVEAQYILIHQALVE 915
Cdd:cd14633    235 EGVVDIYNCVRELRSRRVNMVQTEEQYVFIHDAILE 270
R-PTPc-V cd14618
catalytic domain of receptor-type tyrosine-protein phosphatase V; Receptor-type ...
 685-914 4.18e-66

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: 223.28  E-value: 4.18e-66
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622828204  685 NRYVDILPYDYNRVELSEINGDAGSNYINASYIDGFKEPRKYIAAQGPRDETVDDFWRMIWEQKATVIVMVTRCEEGNRN 764
Cdd:cd14618      1 NRYPHVLPYDHSRVRLSQLGGEPHSDYINANFIPGYTSPQEFIATQGPLKKTIEDFWRLVWEQQVCNIIMLTVGMENGRV 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622828204  765 KCAEYWPSmEEGTRAFGDVVVKINQHKRCPDYIIQKLNIVNKKEKATgREVTHIQFTSWPDHGVPEDPHLLLKLRRRVNA 844
Cdd:cd14618     81 LCDHYWPS-ESTPVSYGHITVHLLAQSSEDEWTRREFKLWHEDLRKE-RRVKHLHYTAWPDHGIPESTSSLMAFRELVRE 158

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1622828204  845 F--SNFFSGPIVVHCSAGVGRTGTYIGIDAMLEGLEAENKVDVYGYVVKLRRQRCLMVQVEAQYILIHQALV 914
Cdd:cd14618    159 HvqATKGKGPTLVHCSAGVGRSGTFIALDRLLRQLKEEKVVDVFNTVYILRMHRYLMIQTLSQYIFLHSCIL 230
R-PTPc-Z-1 cd17668
catalytic domain of receptor-type tyrosine-protein phosphatase Z, repeat 1; Receptor-type ...
 711-914 4.74e-64

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: 216.38  E-value: 4.74e-64
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622828204  711 YINASYIDGFKEPRKYIAAQGPRDETVDDFWRMIWEQKATVIVMVTRCEEGNRNKCAEYWPSmeEGTRAFGDVVVKINQH 790
Cdd:cd17668      1 YINANYVDGYNKPKAYIAAQGPLKSTAEDFWRMIWEHNVEVIVMITNLVEKGRRKCDQYWPA--DGSEEYGNFLVTQKSV 78

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622828204  791 KRCPDYIIQKLNIVN-------KKEKATGREVTHIQFTSWPDHGVPEDPHLLLKLRRRVNAFSNFFSGPIVVHCSAGVGR 863
Cdd:cd17668     79 QVLAYYTVRNFTLRNtkikkgsQKGRPSGRVVTQYHYTQWPDMGVPEYTLPVLTFVRKASYAKRHAVGPVVVHCSAGVGR 158

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|.
gi 1622828204  864 TGTYIGIDAMLEGLEAENKVDVYGYVVKLRRQRCLMVQVEAQYILIHQALV 914
Cdd:cd17668    159 TGTYIVLDSMLQQIQHEGTVNIFGFLKHIRSQRNYLVQTEEQYVFIHDALV 209
R-PTPc-Q cd14616
catalytic domain of receptor-type tyrosine-protein phosphatase Q; Receptor-type ...
 685-911 7.95e-64

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


Pssm-ID: 350464 [Multi-domain]  Cd Length: 224  Bit Score: 216.31  E-value: 7.95e-64
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622828204  685 NRYVDILPYDYNRVELSEINGDAGSNYINASYIDGFKEPRKYIAAQGPRDETVDDFWRMIWEQKATVIVMVTRCEEGNRN 764
Cdd:cd14616      1 NRFPNIKPYNNNRVKLIADAGVPGSDYINASYISGYLCPNEFIATQGPLPGTVGDFWRMVWETRAKTIVMLTQCFEKGRI 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622828204  765 KCAEYWPSMEEGTRAFGDVVVKINQHKRCPDYIIQKLNIVNKKEKATgreVTHIQFTSWPDHGVPEDPHLLLKLRRRVNA 844
Cdd:cd14616     81 RCHQYWPEDNKPVTVFGDIVITKLMEDVQIDWTIRDLKIERHGDYMM---VRQCNFTSWPEHGVPESSAPLIHFVKLVRA 157

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1622828204  845 FSNFFSGPIVVHCSAGVGRTGTYIGIDAMLEGLEAENKVDVYGYVVKLRRQRCLMVQVEAQYILIHQ 911
Cdd:cd14616    158 SRAHDNTPMIVHCSAGVGRTGVFIALDHLTQHINDHDFVDIYGLVAELRSERMCMVQNLAQYIFLHQ 224
R-PTPc-typeIIb-1 cd14555
catalytic domain of type IIb (or R2B) subfamily receptor-type tyrosine-protein phosphatases, ...
 711-915 4.38e-63

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: 213.63  E-value: 4.38e-63
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622828204  711 YINASYIDGFKEPRKYIAAQGPRDETVDDFWRMIWEQKATVIVMVTRCEEGNRNKCAEYWPsmeEGTRAFGDVVVKINQH 790
Cdd:cd14555      1 YINANYIDGYHRPNHYIATQGPMQETVYDFWRMVWQENSASIVMVTNLVEVGRVKCSRYWP---DDTEVYGDIKVTLVET 77

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622828204  791 KRCPDYIIQKLNiVNKKEKATGREVTHIQFTSWPDHGVPEDPHLLLKLRRRVNAFSNFFSGPIVVHCSAGVGRTGTYIGI 870
Cdd:cd14555     78 EPLAEYVVRTFA-LERRGYHEIREVRQFHFTGWPDHGVPYHATGLLGFIRRVKASNPPSAGPIVVHCSAGAGRTGCYIVI 156

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*
gi 1622828204  871 DAMLEGLEAENKVDVYGYVVKLRRQRCLMVQVEAQYILIHQALVE 915
Cdd:cd14555    157 DIMLDMAEREGVVDIYNCVKELRSRRVNMVQTEEQYIFIHDAILE 201
PTPc-N6 cd14606
catalytic domain of tyrosine-protein phosphatase non-receptor type 6; Tyrosine-protein ...
 674-916 1.03e-61

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: 212.05  E-value: 1.03e-61
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622828204  674 KEARKPFNQNKNRYVDILPYDYNRVELSeiNGDA---GSNYINASYID----GFKEPRK-YIAAQGPRDETVDDFWRMIW 745
Cdd:cd14606     11 LEGQRPENKSKNRYKNILPFDHSRVILQ--GRDSnipGSDYINANYVKnqllGPDENAKtYIASQGCLEATVNDFWQMAW 88

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622828204  746 EQKATVIVMVTRCEEGNRNKCAEYWPSMeEGTRAFGDVVVKINQHKRCPDYIIQKLNIVNKKEKATGREVTHIQFTSWPD 825
Cdd:cd14606     89 QENSRVIVMTTREVEKGRNKCVPYWPEV-GMQRAYGPYSVTNCGEHDTTEYKLRTLQVSPLDNGELIREIWHYQYLSWPD 167

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622828204  826 HGVPEDPHLLLKLRRRVNAFSNFF--SGPIVVHCSAGVGRTGTYIGIDAMLEGLEAEN---KVDVYGYVVKLRRQRCLMV 900
Cdd:cd14606    168 HGVPSEPGGVLSFLDQINQRQESLphAGPIIVHCSAGIGRTGTIIVIDMLMENISTKGldcDIDIQKTIQMVRAQRSGMV 247

                          250
                   ....*....|....*.
gi 1622828204  901 QVEAQYILIHQALVEY 916
Cdd:cd14606    248 QTEAQYKFIYVAIAQF 263
PTPc-N20_13 cd14538
catalytic domain of tyrosine-protein phosphatase non-receptor type 20 and type 13; ...
 711-915 6.79e-61

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: 207.23  E-value: 6.79e-61
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622828204  711 YINASYI--DGFKEPRKYIAAQGPRDETVDDFWRMIWEQKATVIVMVTRCEEGNRNKCAEYWP-SMEEGTRAFGDVVVKI 787
Cdd:cd14538      1 YINASHIriPVGGDTYHYIACQGPLPNTTGDFWQMVWEQKSEVIAMVTQDVEGGKVKCHRYWPdSLNKPLICGGRLEVSL 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622828204  788 NQHKRCPDYIIQKLNIvnkKEKATG--REVTHIQFTSWPDHGVPEDPHLLLKLRRRVNAFSNffSGPIVVHCSAGVGRTG 865
Cdd:cd14538     81 EKYQSLQDFVIRRISL---RDKETGevHHITHLNFTTWPDHGTPQSADPLLRFIRYMRRIHN--SGPIVVHCSAGIGRTG 155

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|
gi 1622828204  866 TYIGIDAMLEGLEAENKVDVYGYVVKLRRQRCLMVQVEAQYILIHQALVE 915
Cdd:cd14538    156 VLITIDVALGLIERDLPFDIQDIVKDLREQRQGMIQTKDQYIFCYKACLE 205
R-PTP-S-2 cd14627
PTP-like domain of receptor-type tyrosine-protein phosphatase S, repeat 2; Receptor-type ...
 676-916 7.56e-61

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: 210.36  E-value: 7.56e-61
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622828204  676 ARKPFNQNKNRYVDILPYDYNRVELSEINGDAGSNYINASYIDGFKEPRKYIAAQGPRDETVDDFWRMIWEQKATVIVMV 755
Cdd:cd14627     48 ANLPCNKFKNRLVNIMPYETTRVCLQPIRGVEGSDYINASFIDGYRQQKAYIATQGPLAETTEDFWRMLWENNSTIVVML 127

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622828204  756 TRCEEGNRNKCAEYWPSmeEGTRAFGDVVVKINQHKRCPDYIIQKLNIVNKKEkATGREVTHIQFTSWPDHGVPEDPHLL 835
Cdd:cd14627    128 TKLREMGREKCHQYWPA--ERSARYQYFVVDPMAEYNMPQYILREFKVTDARD-GQSRTVRQFQFTDWPEQGVPKSGEGF 204

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622828204  836 LKLRRRVNAFSNFF--SGPIVVHCSAGVGRTGTYIGIDAMLEGLEAENKVDVYGYVVKLRRQRCLMVQVEAQYILIHQAL 913
Cdd:cd14627    205 IDFIGQVHKTKEQFgqDGPISVHCSAGVGRTGVFITLSIVLERMRYEGVVDIFQTVKMLRTQRPAMVQTEDEYQFCYQAA 284


                   ...
gi 1622828204  914 VEY 916
Cdd:cd14627    285 LEY 287
R-PTP-D-2 cd14628
PTP-like domain of receptor-type tyrosine-protein phosphatase D, repeat 2; Receptor-type ...
 676-916 1.23e-60

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: 209.97  E-value: 1.23e-60
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622828204  676 ARKPFNQNKNRYVDILPYDYNRVELSEINGDAGSNYINASYIDGFKEPRKYIAAQGPRDETVDDFWRMIWEQKATVIVMV 755
Cdd:cd14628     47 ANLPCNKFKNRLVNIMPYESTRVCLQPIRGVEGSDYINASFIDGYRQQKAYIATQGPLAETTEDFWRMLWEHNSTIVVML 126

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622828204  756 TRCEEGNRNKCAEYWPSmeEGTRAFGDVVVKINQHKRCPDYIIQKLNIVNKKEkATGREVTHIQFTSWPDHGVPEDPHLL 835
Cdd:cd14628    127 TKLREMGREKCHQYWPA--ERSARYQYFVVDPMAEYNMPQYILREFKVTDARD-GQSRTVRQFQFTDWPEQGVPKSGEGF 203

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622828204  836 LKLRRRVNAFSNFF--SGPIVVHCSAGVGRTGTYIGIDAMLEGLEAENKVDVYGYVVKLRRQRCLMVQVEAQYILIHQAL 913
Cdd:cd14628    204 IDFIGQVHKTKEQFgqDGPISVHCSAGVGRTGVFITLSIVLERMRYEGVVDIFQTVKMLRTQRPAMVQTEDQYQFCYRAA 283


                   ...
gi 1622828204  914 VEY 916
Cdd:cd14628    284 LEY 286
R-PTP-F-2 cd14629
PTP-like domain of receptor-type tyrosine-protein phosphatase F, repeat 2; Receptor-type ...
 676-916 1.99e-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: 209.20  E-value: 1.99e-60
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622828204  676 ARKPFNQNKNRYVDILPYDYNRVELSEINGDAGSNYINASYIDGFKEPRKYIAAQGPRDETVDDFWRMIWEQKATVIVMV 755
Cdd:cd14629     48 ANLPCNKFKNRLVNIMPYELTRVCLQPIRGVEGSDYINASFIDGYRQQKAYIATQGPLAETTEDFWRMLWEHNSTIVVML 127

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622828204  756 TRCEEGNRNKCAEYWPSmeEGTRAFGDVVVKINQHKRCPDYIIQKLNIVNKKEkATGREVTHIQFTSWPDHGVPEDPHLL 835
Cdd:cd14629    128 TKLREMGREKCHQYWPA--ERSARYQYFVVDPMAEYNMPQYILREFKVTDARD-GQSRTIRQFQFTDWPEQGVPKTGEGF 204

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622828204  836 LKLRRRVNAFSNFF--SGPIVVHCSAGVGRTGTYIGIDAMLEGLEAENKVDVYGYVVKLRRQRCLMVQVEAQYILIHQAL 913
Cdd:cd14629    205 IDFIGQVHKTKEQFgqDGPITVHCSAGVGRTGVFITLSIVLERMRYEGVVDMFQTVKTLRTQRPAMVQTEDQYQLCYRAA 284


                   ...
gi 1622828204  914 VEY 916
Cdd:cd14629    285 LEY 287
R-PTPc-K-1 cd14631
catalytic domain of receptor-type tyrosine-protein phosphatase K, repeat 1; Receptor-type ...
 697-915 2.26e-60

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: 206.41  E-value: 2.26e-60
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622828204  697 RVELSEINGDAGSNYINASYIDGFKEPRKYIAAQGPRDETVDDFWRMIWEQKATVIVMVTRCEEGNRNKCAEYWPsmeEG 776
Cdd:cd14631      1 RVILQPVEDDPSSDYINANYIDGYQRPSHYIATQGPVHETVYDFWRMIWQEQSACIVMVTNLVEVGRVKCYKYWP---DD 77

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622828204  777 TRAFGDVVVKINQHKRCPDYIIQKLNIvNKKEKATGREVTHIQFTSWPDHGVPEDPHLLLKLRRRVNAFSNFFSGPIVVH 856
Cdd:cd14631     78 TEVYGDFKVTCVEMEPLAEYVVRTFTL-ERRGYNEIREVKQFHFTGWPDHGVPYHATGLLSFIRRVKLSNPPSAGPIVVH 156

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 1622828204  857 CSAGVGRTGTYIGIDAMLEGLEAENKVDVYGYVVKLRRQRCLMVQVEAQYILIHQALVE 915
Cdd:cd14631    157 CSAGAGRTGCYIVIDIMLDMAEREGVVDIYNCVKALRSRRINMVQTEEQYIFIHDAILE 215
PTPc-N7 cd14612
catalytic domain of tyrosine-protein phosphatase non-receptor type 7; Tyrosine-protein ...
 679-916 1.16e-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: 205.45  E-value: 1.16e-59
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622828204  679 PFNQNKNRYVDILPYDYNRVEL-SEINGDAGSNYINASYIDGFK-EPRKYIAAQGPRDETVDDFWRMIWEQKATVIVMVT 756
Cdd:cd14612     13 PGHASKDRYKTILPNPQSRVCLrRAGSQEEEGSYINANYIRGYDgKEKAYIATQGPMLNTVSDFWEMVWQEECPIIVMIT 92

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622828204  757 RCEEGNRnKCAEYWPSmEEGTraFGDVVVKINQHKRCPDYIIQKLNIVNKKEKatgREVTHIQFTSWPDHGVPEDPHLLL 836
Cdd:cd14612     93 KLKEKKE-KCVHYWPE-KEGT--YGRFEIRVQDMKECDGYTIRDLTIQLEEES---RSVKHYWFSSWPDHQTPESAGPLL 165

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622828204  837 KL-----RRRVNAFSnffSGPIVVHCSAGVGRTGTYIGIDAMLEGLEAENKVDVYGYVVKLRRQRCLMVQVEAQYILIHQ 911
Cdd:cd14612    166 RLvaeveESRQTAAS---PGPIVVHCSAGIGRTGCFIATSIGCQQLKDTGKVDILGIVCQLRLDRGGMIQTSEQYQFLHH 242


                   ....*
gi 1622828204  912 ALVEY 916
Cdd:cd14612    243 TLALY 247
R-PTPc-A-E-2 cd14552
catalytic domain of receptor-type tyrosine-protein phosphatase A and E, repeat 2; ...
 1021-1229 3.77e-58

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


Pssm-ID: 350400 [Multi-domain]  Cd Length: 202  Bit Score: 199.42  E-value: 3.77e-58
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622828204 1021 YINASFIMSYWKPEVMIAAQGPLKETIGDFWQMIFQRKVKVIVMLTELKHGDQEICAQYW-GEGKQTYGDIEVDMKDTNK 1099
Cdd:cd14552      1 YINASFIDGYRQKDAYIATQGPLDHTVEDFWRMIWEWKSCSIVMLTEIKERSQNKCAQYWpEDGSVSSGDITVELKDQTD 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622828204 1100 SSTYTLRVFELRHSKRKDSRTVYQYQYTNWSVEQLPAEPKELVSLIQVLkeklpQKNSSEGNKHhkstPLLIHCRDGSQQ 1179
Cdd:cd14552     81 YEDYTLRDFLVTKGKGGSTRTVRQFHFHGWPEVGIPDNGKGMIDLIAAV-----QKQQQQSGNH----PITVHCSAGAGR 151

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|
gi 1622828204 1180 TGIFCALLNLLESAETEEVVDIFQVVKALRKARPGMVSTFEQYQFLYDII 1229
Cdd:cd14552    152 TGTFCALSTVLERVKAEGVLDVFQVVKSLRLQRPHMVQTLEQYEFCYKVV 201
R-PTPc-U-1 cd14632
catalytic domain of receptor-type tyrosine-protein phosphatase U, repeat 1; Receptor-type ...
 711-915 1.07e-57

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: 197.97  E-value: 1.07e-57
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622828204  711 YINASYIDGFKEPRKYIAAQGPRDETVDDFWRMIWEQKATVIVMVTRCEEGNRNKCAEYWPsmeEGTRAFGDVVVKINQH 790
Cdd:cd14632      1 YINANYIDGYHRSNHFIATQGPKQEMVYDFWRMVWQEHCSSIVMITKLVEVGRVKCSKYWP---DDSDTYGDIKITLLKT 77

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622828204  791 KRCPDYIIQKLNIvNKKEKATGREVTHIQFTSWPDHGVPEDPHLLLKLRRRVNAFSNFFSGPIVVHCSAGVGRTGTYIGI 870
Cdd:cd14632     78 ETLAEYSVRTFAL-ERRGYSARHEVKQFHFTSWPEHGVPYHATGLLAFIRRVKASTPPDAGPVVVHCSAGAGRTGCYIVL 156

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*
gi 1622828204  871 DAMLEGLEAENKVDVYGYVVKLRRQRCLMVQVEAQYILIHQALVE 915
Cdd:cd14632    157 DVMLDMAECEGVVDIYNCVKTLCSRRINMIQTEEQYIFIHDAILE 201
R-PTPc-A-2 cd14623
catalytic domain of receptor-type tyrosine-protein phosphatase A, repeat 2; Receptor-type ...
 686-915 1.46e-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: 198.73  E-value: 1.46e-57
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622828204  686 RYVDILPYDYNRVELSEINGDAGSNYINASYIDGFKEPRKYIAAQGPRDETVDDFWRMIWEQKATVIVMVTRCEEGNRNK 765
Cdd:cd14623      1 RVLQIIPYEFNRVIIPVKRGEENTDYVNASFIDGYRQKDSYIASQGPLQHTIEDFWRMIWEWKSCSIVMLTELEERGQEK 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622828204  766 CAEYWPSmeEGTRAFGDVVVKINQHKRCPDYIIQKLNIVNKKEKATgREVTHIQFTSWPDHGVPEDP----HLLLKLRRR 841
Cdd:cd14623     81 CAQYWPS--DGSVSYGDITIELKKEEECESYTVRDLLVTNTRENKS-RQIRQFHFHGWPEVGIPSDGkgmiNIIAAVQKQ 157

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1622828204  842 VNAFSNFfsgPIVVHCSAGVGRTGTYIGIDAMLEGLEAENKVDVYGYVVKLRRQRCLMVQVEAQYILIHQALVE 915
Cdd:cd14623    158 QQQSGNH---PITVHCSAGAGRTGTFCALSTVLERVKAEGILDVFQTVKSLRLQRPHMVQTLEQYEFCYKVVQE 228
PTPc-N21_14 cd14540
catalytic domain of tyrosine-protein phosphatase non-receptor type 21 and type 14; ...
 711-916 1.54e-57

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: 198.06  E-value: 1.54e-57
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622828204  711 YINASYID---GFKEpRKYIAAQGPRDETVDDFWRMIWEQKATVIVMVTRCEEGNRNKCAEYWPSM--EEGTRAFGD--V 783
Cdd:cd14540      1 YINASHITatvGGKQ-RFYIAAQGPLQNTVGDFWQMVWEQGVYLVVMVTAEEEGGREKCFRYWPTLggEHDALTFGEykV 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622828204  784 VVKINQHKRCpdYIIQKLNIVNKKEKaTGREVTHIQFTSWPDHGVPEDPHLLL-------KLRRRVNAFS--NFFSGPIV 854
Cdd:cd14540     80 STKFSVSSGC--YTTTGLRVKHTLSG-QSRTVWHLQYTDWPDHGCPEDVSGFLdfleeinSVRRHTNQDVagHNRNPPTL 156

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1622828204  855 VHCSAGVGRTGTYIGIDAMLEGLEAENKVDVYGYVVKLRRQRCLMVQVEAQYILIHQALVEY 916
Cdd:cd14540    157 VHCSAGVGRTGVVILADLMLYCLDHNEELDIPRVLALLRHQRMLLVQTLAQYKFVYNVLIQY 218
PTPc-N11 cd14605
catalytic domain of tyrosine-protein phosphatase non-receptor type 11; Tyrosine-protein ...
 681-916 2.16e-57

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: 199.09  E-value: 2.16e-57
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622828204  681 NQNKNRYVDILPYDYNRVELSEinGDA---GSNYINASYI--------DGFKEPRKYIAAQGPRDETVDDFWRMIWEQKA 749
Cdd:cd14605      2 NKNKNRYKNILPFDHTRVVLHD--GDPnepVSDYINANIImpefetkcNNSKPKKSYIATQGCLQNTVNDFWRMVFQENS 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622828204  750 TVIVMVTRCEEGNRNKCAEYWPSmEEGTRAFGDVVVKINQHKRCPDYIIQKLNIVNKKEKATGREVTHIQFTSWPDHGVP 829
Cdd:cd14605     80 RVIVMTTKEVERGKSKCVKYWPD-EYALKEYGVMRVRNVKESAAHDYILRELKLSKVGQGNTERTVWQYHFRTWPDHGVP 158

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622828204  830 EDPHLLLKLRRRVNAFSNFFS--GPIVVHCSAGVGRTGTYIGIDAMLEGLEAEN---KVDVYGYVVKLRRQRCLMVQVEA 904
Cdd:cd14605    159 SDPGGVLDFLEEVHHKQESIMdaGPVVVHCSAGIGRTGTFIVIDILIDIIREKGvdcDIDVPKTIQMVRSQRSGMVQTEA 238

                          250
                   ....*....|..
gi 1622828204  905 QYILIHQALVEY 916
Cdd:cd14605    239 QYRFIYMAVQHY 250
PTPc-N18 cd14603
catalytic domain of tyrosine-protein phosphatase non-receptor type 18; Tyrosine-protein ...
 681-915 3.71e-57

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: 198.90  E-value: 3.71e-57
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622828204  681 NQNKNRYVDILPYDYNRVELSEINGDAGSNYINASYIDGFKEPRKYIAAQGPRDETVDDFWRMIWEQKATVIVMVTRCEE 760
Cdd:cd14603     30 NVKKNRYKDILPYDQTRVILSLLQEEGHSDYINANFIKGVDGSRAYIATQGPLSHTVLDFWRMIWQYGVKVILMACREIE 109

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622828204  761 GNRNKCAEYWPSMEEgTRAFGD-VVVKINQHKRCPDYIIQKLNIVNKKEKatgREVTHIQFTSWPDHGVPEDPHLLLKLR 839
Cdd:cd14603    110 MGKKKCERYWAQEQE-PLQTGPfTITLVKEKRLNEEVILRTLKVTFQKES---RSVSHFQYMAWPDHGIPDSPDCMLAMI 185

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1622828204  840 RRVNAFSNFFSGPIVVHCSAGVGRTGTYIGIDAMLEGLEAEN---KVDVYGYVVKLRRQRCLMVQVEAQYILIHQALVE 915
Cdd:cd14603    186 ELARRLQGSGPEPLCVHCSAGCGRTGVICTVDYVRQLLLTQRippDFSIFDVVLEMRKQRPAAVQTEEQYEFLYHTVAQ 264
PTPc-N13 cd14597
catalytic domain of tyrosine-protein phosphatase non-receptor type 13; Tyrosine-protein ...
 681-914 8.94e-57

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: 196.59  E-value: 8.94e-57
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622828204  681 NQNKNRYVDILPYDYNRVELSEINGdagsnYINASYID---GfKEPRKYIAAQGPRDETVDDFWRMIWEQKATVIVMVTR 757
Cdd:cd14597      3 NRKKNRYKNILPYDTTRVPLGDEGG-----YINASFIKmpvG-DEEFVYIACQGPLPTTVADFWQMVWEQKSTVIAMMTQ 76

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622828204  758 CEEGNRNKCAEYWPSMEEGTRAFGD----VVVKINQHKrcpDYIIQKLNIVNKKEKATgREVTHIQFTSWPDHGVPEDPH 833
Cdd:cd14597     77 EVEGGKIKCQRYWPEILGKTTMVDNrlqlTLVRMQQLK---NFVIRVLELEDIQTREV-RHITHLNFTAWPDHDTPSQPE 152

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622828204  834 LLLKL---RRRVNAfsnffSGPIVVHCSAGVGRTGTYIGIDAMLEGLEAENKVDVYGYVVKLRRQRCLMVQVEAQYILIH 910
Cdd:cd14597    153 QLLTFisyMRHIHK-----SGPIITHCSAGIGRSGTLICIDVVLGLISKDLDFDISDIVRTMRLQRHGMVQTEDQYIFCY 227


                   ....
gi 1622828204  911 QALV 914
Cdd:cd14597    228 QVIL 231
PTPc-N22_18_12 cd14542
catalytic domain of tyrosine-protein phosphatase non-receptor type 22, type 18 and type 12; ...
 711-911 4.42e-56

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: 193.41  E-value: 4.42e-56
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622828204  711 YINASYIDGFKEPRKYIAAQGPRDETVDDFWRMIWEQKATVIVMVTRCEEGNRNKCAEYWPSMEEGTRAFGDVVVK-INQ 789
Cdd:cd14542      1 YINANFIKGVSGSKAYIATQGPLPNTVLDFWRMIWEYNVQVIVMACREFEMGKKKCERYWPEEGEEQLQFGPFKISlEKE 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622828204  790 HKRCPDYIIQKLNIVNKKEKatgREVTHIQFTSWPDHGVPEDPHLLLKLRRRVNAFSNFFSGPIVVHCSAGVGRTGTYIG 869
Cdd:cd14542     81 KRVGPDFLIRTLKVTFQKES---RTVYQFHYTAWPDHGVPSSVDPILDLVRLVRDYQGSEDVPICVHCSAGCGRTGTICA 157

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*.
gi 1622828204  870 ID----AMLEGLEAENkVDVYGYVVKLRRQRCLMVQVEAQYILIHQ 911
Cdd:cd14542    158 IDyvwnLLKTGKIPEE-FSLFDLVREMRKQRPAMVQTKEQYELVYR 202
PTPc-N1_2 cd14545
catalytic domain of tyrosine-protein phosphatase non-receptor type 1 and type 2; ...
 684-905 6.09e-56

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: 194.15  E-value: 6.09e-56
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622828204  684 KNRYVDILPYDYNRVELSEINGDagSNYINASYIDGFKEPRKYIAAQGPRDETVDDFWRMIWEQKATVIVMVTRCEEGNR 763
Cdd:cd14545      1 LNRYRDRDPYDHDRSRVKLKQGD--NDYINASLVEVEEAKRSYILTQGPLPNTSGHFWQMVWEQNSKAVIMLNKLMEKGQ 78

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622828204  764 NKCAEYWPSMEEGTRAFGDVVVKIN--QHKRCPDYIIQKLNIVNKKEKATgREVTHIQFTSWPDHGVPEDP----HLLLK 837
Cdd:cd14545     79 IKCAQYWPQGEGNAMIFEDTGLKVTllSEEDKSYYTVRTLELENLKTQET-REVLHFHYTTWPDFGVPESPaaflNFLQK 157

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622828204  838 LRRRVNAFSNFfsGPIVVHCSAGVGRTGTYIGIDAMLEGLEAEN--KVDVYGYVVKLRRQRCLMVQVEAQ 905
Cdd:cd14545    158 VRESGSLSSDV--GPPVVHCSAGIGRSGTFCLVDTCLVLIEKGNpsSVDVKKVLLEMRKYRMGLIQTPDQ 225
R-PTPc-A-E-2 cd14552
catalytic domain of receptor-type tyrosine-protein phosphatase A and E, repeat 2; ...
 711-914 6.79e-56

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


Pssm-ID: 350400 [Multi-domain]  Cd Length: 202  Bit Score: 192.87  E-value: 6.79e-56
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622828204  711 YINASYIDGFKEPRKYIAAQGPRDETVDDFWRMIWEQKATVIVMVTRCEEGNRNKCAEYWPsmEEGTRAFGDVVVKINQH 790
Cdd:cd14552      1 YINASFIDGYRQKDAYIATQGPLDHTVEDFWRMIWEWKSCSIVMLTEIKERSQNKCAQYWP--EDGSVSSGDITVELKDQ 78

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622828204  791 KRCPDYIIQKLNIVNKKEKATgREVTHIQFTSWPDHGVPEDP----HLLLKLRRRVNAFSNffsGPIVVHCSAGVGRTGT 866
Cdd:cd14552     79 TDYEDYTLRDFLVTKGKGGST-RTVRQFHFHGWPEVGIPDNGkgmiDLIAAVQKQQQQSGN---HPITVHCSAGAGRTGT 154

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*...
gi 1622828204  867 YIGIDAMLEGLEAENKVDVYGYVVKLRRQRCLMVQVEAQYILIHQALV 914
Cdd:cd14552    155 FCALSTVLERVKAEGVLDVFQVVKSLRLQRPHMVQTLEQYEFCYKVVQ 202
PTPc-N14 cd14599
catalytic domain of tyrosine-protein phosphatase non-receptor type 14; Tyrosine-protein ...
 644-916 6.41e-55

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: 193.29  E-value: 6.41e-55
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622828204  644 ETYKRKIaDEGRLFlAEFQSIPRVFSKFPIKEARKPFNQNKNRYVDILPYDYNRVELSEiNGDAGSNYINASYIDGF--K 721
Cdd:cd14599      3 KTLERKL-EEGMVF-TEYEQIPKKKADGVFTTATLPENAERNRIREVVPYEENRVELVP-TKENNTGYINASHIKVTvgG 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622828204  722 EPRKYIAAQGPRDETVDDFWRMIWEQKATVIVMVTRCEEGNRNKCAEYWPSM--EEGTRAFGDVVVKINQHKRCPDYIIQ 799
Cdd:cd14599     80 EEWHYIATQGPLPHTCHDFWQMVWEQGVNVIAMVTAEEEGGRSKSHRYWPKLgsKHSSATYGKFKVTTKFRTDSGCYATT 159

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622828204  800 KLNIvnkKEKATGREVT--HIQFTSWPDHGVPEDPHLLLK-------LRRRVNAF---SNFFSGPIVVHCSAGVGRTGTY 867
Cdd:cd14599    160 GLKV---KHLLSGQERTvwHLQYTDWPDHGCPEEVQGFLSyleeiqsVRRHTNSMldsTKNCNPPIVVHCSAGVGRTGVV 236

                          250       260       270       280
                   ....*....|....*....|....*....|....*....|....*....
gi 1622828204  868 IGIDAMLEGLEAENKVDVYGYVVKLRRQRCLMVQVEAQYILIHQALVEY 916
Cdd:cd14599    237 ILTELMIGCLEHNEKVEVPVMLRHLREQRMFMIQTIAQYKFVYQVLIQF 285
R3-PTPc cd14548
catalytic domain of R3 subfamily receptor-type tyrosine-protein phosphatases and similar ...
 977-1226 4.37e-54

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: 188.33  E-value: 4.37e-54
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622828204  977 RNSNVIPYDYNRVPLK--HELEMSKesdhdsdessdddsdseepskYINASFIMSYWKPEVMIAAQGPLKETIGDFWQMI 1054
Cdd:cd14548      1 RYTNILPYDHSRVKLIpiNEEEGSD---------------------YINANYIPGYNSPREFIATQGPLPGTKDDFWRMV 59

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622828204 1055 FQRKVKVIVMLTELKHGDQEICAQYWGEGKQ--TYGDIEVDMKDTNKSSTYTLRVFELRHskRKDSRTVYQYQYTNWSVE 1132
Cdd:cd14548     60 WEQNSHTIVMLTQCMEKGRVKCDHYWPFDQDpvYYGDITVTMLSESVLPDWTIREFKLER--GDEVRSVRQFHFTAWPDH 137

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622828204 1133 QLPAEPKELVSLIQVLKEKLPQKNssegnkhhksTPLLIHCRDGSQQTGIFCALLNLLESAETEEVVDIFQVVKALRKAR 1212
Cdd:cd14548    138 GVPEAPDSLLRFVRLVRDYIKQEK----------GPTIVHCSAGVGRTGTFIALDRLLQQIESEDYVDIFGIVYDLRKHR 207

                          250
                   ....*....|....
gi 1622828204 1213 PGMVSTFEQYQFLY 1226
Cdd:cd14548    208 PLMVQTEAQYIFLH 221
PTPc-N3_4 cd14541
catalytic domain of tyrosine-protein phosphatase non-receptor type 21 and type 14; ...
 711-906 6.77e-54

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: 187.54  E-value: 6.77e-54
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622828204  711 YINASYID----GFKEPRKYIAAQGPRDETVDDFWRMIWEQKATVIVMVTRCEEGNRNKCAEYWPSMEEgTRAFGDVVVK 786
Cdd:cd14541      2 YINANYVNmeipGSGIVNRYIAAQGPLPNTCADFWQMVWEQKSTLIVMLTTLVERGRVKCHQYWPDLGE-TMQFGNLQIT 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622828204  787 INQHKRCPDYIIQKLNIVNKKEKATgREVTHIQFTSWPDHGVPEDPHLLLKLRRRVNAFSNFFSGPIVVHCSAGVGRTGT 866
Cdd:cd14541     81 CVSEEVTPSFAFREFILTNTNTGEE-RHITQMQYLAWPDHGVPDDSSDFLDFVKRVRQNRVGMVEPTVVHCSAGIGRTGV 159

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|
gi 1622828204  867 YIGIDAMLEGLEAENKVDVYGYVVKLRRQRCLMVQVEAQY 906
Cdd:cd14541    160 LITMETAMCLIEANEPVYPLDIVRTMRDQRAMLIQTPSQY 199
R-PTP-C-2 cd14558
PTP-like domain of receptor-type tyrosine-protein phosphatase C, repeat 2; Receptor-type ...
 711-906 7.32e-54

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


Pssm-ID: 350406 [Multi-domain]  Cd Length: 203  Bit Score: 186.83  E-value: 7.32e-54
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622828204  711 YINASYIDGFKEPRKYIAAQGPRDETVDDFWRMIWEQKATVIVMVTRCEEGNRNKCAEYWPsmeEGTRAFGDVVVKINQH 790
Cdd:cd14558      1 YINASFIDGYWGPKSLIATQGPLPDTIADFWQMIFQKKVKVIVMLTELKEGDQEQCAQYWG---DEKKTYGDIEVELKDT 77

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622828204  791 KRCPDYIIQKLNIVNKKEKATgREVTHIQFTSWPDHGVPEDPHLLLKLRRRV------NAFSNFFSGPIVVHCSAGVGRT 864
Cdd:cd14558     78 EKSPTYTVRVFEITHLKRKDS-RTVYQYQYHKWKGEELPEKPKDLVDMIKSIkqklpyKNSKHGRSVPIVVHCSDGSSRT 156

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|..
gi 1622828204  865 GTYIGIDAMLEGLEAENKVDVYGYVVKLRRQRCLMVQVEAQY 906
Cdd:cd14558    157 GIFCALWNLLESAETEKVVDVFQVVKALRKQRPGMVSTLEQY 198
PTPc-N22 cd14602
catalytic domain of tyrosine-protein phosphatase non-receptor type 22; Tyrosine-protein ...
 684-915 8.75e-54

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: 188.13  E-value: 8.75e-54
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622828204  684 KNRYVDILPYDYNRVELSEINGDAGSNYINASYIDGFKEPRKYIAAQGPRDETVDDFWRMIWEQKATVIVMVTRCEEGNR 763
Cdd:cd14602      1 KNRYKDILPYDHSRVELSLITSDEDSDYINANFIKGVYGPRAYIATQGPLSTTLLDFWRMIWEYSVLIIVMACMEFEMGK 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622828204  764 NKCAEYWPSMEEGTRAFGDVVVKINQHKRCPDYIIQKLNIVNKKEKatgREVTHIQFTSWPDHGVPEDPHLLLKLRRRVN 843
Cdd:cd14602     81 KKCERYWAEPGEMQLEFGPFSVTCEAEKRKSDYIIRTLKVKFNSET---RTIYQFHYKNWPDHDVPSSIDPILELIWDVR 157

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1622828204  844 AFSNFFSGPIVVHCSAGVGRTGTYIGID----AMLEGLEAENkVDVYGYVVKLRRQRCLMVQVEAQYILIHQALVE 915
Cdd:cd14602    158 CYQEDDSVPICIHCSAGCGRTGVICAIDytwmLLKDGIIPEN-FSVFSLIQEMRTQRPSLVQTKEQYELVYNAVIE 232
R-PTPc-A-2 cd14623
catalytic domain of receptor-type tyrosine-protein phosphatase A, repeat 2; Receptor-type ...
 977-1229 9.10e-54

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: 187.56  E-value: 9.10e-54
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622828204  977 RNSNVIPYDYNRV--PLKHELEMSKesdhdsdessdddsdseepskYINASFIMSYWKPEVMIAAQGPLKETIGDFWQMI 1054
Cdd:cd14623      1 RVLQIIPYEFNRViiPVKRGEENTD---------------------YVNASFIDGYRQKDSYIASQGPLQHTIEDFWRMI 59

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622828204 1055 FQRKVKVIVMLTELKHGDQEICAQYW-GEGKQTYGDIEVDMKDTNKSSTYTLRVFELRHSKRKDSRTVYQYQYTNWSVEQ 1133
Cdd:cd14623     60 WEWKSCSIVMLTELEERGQEKCAQYWpSDGSVSYGDITIELKKEEECESYTVRDLLVTNTRENKSRQIRQFHFHGWPEVG 139

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622828204 1134 LPAEPKELVSLIQVLkeklpQKNSSEGNKHhkstPLLIHCRDGSQQTGIFCALLNLLESAETEEVVDIFQVVKALRKARP 1213
Cdd:cd14623    140 IPSDGKGMINIIAAV-----QKQQQQSGNH----PITVHCSAGAGRTGTFCALSTVLERVKAEGILDVFQTVKSLRLQRP 210

                          250
                   ....*....|....*.
gi 1622828204 1214 GMVSTFEQYQFLYDII 1229
Cdd:cd14623    211 HMVQTLEQYEFCYKVV 226
PTPc-N12 cd14604
catalytic domain of tyrosine-protein phosphatase non-receptor type 12; Tyrosine-protein ...
 657-915 1.73e-53

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: 189.37  E-value: 1.73e-53
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622828204  657 FLAEFQSIPRVFSKF------PIKEARKPFNQNKNRYVDILPYDYNRVELSEINGDAGSNYINASYIDGFKEPRKYIAAQ 730
Cdd:cd14604     27 FASDFMRLRRLSTKYrtekiyPTATGEKEENVKKNRYKDILPFDHSRVKLTLKTSSQDSDYINANFIKGVYGPKAYIATQ 106

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622828204  731 GPRDETVDDFWRMIWEQKATVIVMVTRCEEGNRNKCAEYWPSMEEGTRAFGDVVVKINQHKRCPDYIIQKLNIVNKKEKa 810
Cdd:cd14604    107 GPLANTVIDFWRMIWEYNVAIIVMACREFEMGRKKCERYWPLYGEEPMTFGPFRISCEAEQARTDYFIRTLLLEFQNET- 185

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622828204  811 tgREVTHIQFTSWPDHGVPEDPHLLLKLRRRVNAFSNFFSGPIVVHCSAGVGRTGTYIGIDAMLEGLEA---ENKVDVYG 887
Cdd:cd14604    186 --RRLYQFHYVNWPDHDVPSSFDSILDMISLMRKYQEHEDVPICIHCSAGCGRTGAICAIDYTWNLLKAgkiPEEFNVFN 263

                          250       260
                   ....*....|....*....|....*...
gi 1622828204  888 YVVKLRRQRCLMVQVEAQYILIHQALVE 915
Cdd:cd14604    264 LIQEMRTQRHSAVQTKEQYELVHRAIAQ 291
R-PTPc-E-2 cd14622
catalytic domain of receptor-type tyrosine-protein phosphatase E, repeat 2; Receptor-type ...
 1021-1229 2.56e-53

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


Pssm-ID: 350470 [Multi-domain]  Cd Length: 205  Bit Score: 185.59  E-value: 2.56e-53
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622828204 1021 YINASFIMSYWKPEVMIAAQGPLKETIGDFWQMIFQRKVKVIVMLTELKHGDQEICAQYW-GEGKQTYGDIEVDMKDTNK 1099
Cdd:cd14622      2 YINASFIDGYRQKDYFIATQGPLAHTVEDFWRMVWEWKCHTIVMLTELQEREQEKCVQYWpSEGSVTHGEITIEIKNDTL 81

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622828204 1100 SSTYTLRVFELRHSKRKDSRTVYQYQYTNWSVEQLPAEPKELVSLIQVLkeklpQKNSSEGNKHhkstPLLIHCRDGSQQ 1179
Cdd:cd14622     82 LETISIRDFLVTYNQEKQTRLVRQFHFHGWPEIGIPAEGKGMIDLIAAV-----QKQQQQTGNH----PIVVHCSAGAGR 152

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|
gi 1622828204 1180 TGIFCALLNLLESAETEEVVDIFQVVKALRKARPGMVSTFEQYQFLYDII 1229
Cdd:cd14622    153 TGTFIALSNILERVKAEGLLDVFQTVKSLRLQRPHMVQTLEQYEFCYRVV 202
R5-PTPc-1 cd14549
catalytic domain of R5 subfamily receptor-type tyrosine-protein phosphatases, repeat 1; The R5 ...
 1021-1227 2.73e-53

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: 185.25  E-value: 2.73e-53
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622828204 1021 YINASFIMSYWKPEVMIAAQGPLKETIGDFWQMIFQRKVKVIVMLTELKHGDQEICAQYW-GEGKQTYGDIEVDMKDTNK 1099
Cdd:cd14549      1 YINANYVDGYNKARAYIATQGPLPSTFDDFWRMVWEQNSAIIVMITNLVERGRRKCDQYWpKEGTETYGNIQVTLLSTEV 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622828204 1100 SSTYTLRVFELRHSK------RKDSRTVYQYQYTNWSVEQLPAEPKELVSLIQvlkeklpqkNSSEGNKHHkSTPLLIHC 1173
Cdd:cd14549     81 LATYTVRTFSLKNLKlkkvkgRSSERVVYQYHYTQWPDHGVPDYTLPVLSFVR---------KSSAANPPG-AGPIVVHC 150

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....
gi 1622828204 1174 RDGSQQTGIFCALLNLLESAETEEVVDIFQVVKALRKARPGMVSTFEQYQFLYD 1227
Cdd:cd14549    151 SAGVGRTGTYIVIDSMLQQIQDKGTVNVFGFLKHIRTQRNYLVQTEEQYIFIHD 204
PTPc-N1 cd14608
catalytic domain of tyrosine-protein phosphatase non-receptor type 1; Tyrosine-protein ...
 661-924 4.57e-53

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: 187.54  E-value: 4.57e-53
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622828204  661 FQSIPRVFSKFPIKEARKPFNQNKNRYVDILPYDYNRVELSEINGDagsnYINASYIDGFKEPRKYIAAQGPRDETVDDF 740
Cdd:cd14608      5 YQDIRHEASDFPCRVAKLPKNKNRNRYRDVSPFDHSRIKLHQEDND----YINASLIKMEEAQRSYILTQGPLPNTCGHF 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622828204  741 WRMIWEQKATVIVMVTRCEEGNRNKCAEYWPSMEEGTRAFGDVVVKIN--QHKRCPDYIIQKLNIVNKKEKATgREVTHI 818
Cdd:cd14608     81 WEMVWEQKSRGVVMLNRVMEKGSLKCAQYWPQKEEKEMIFEDTNLKLTliSEDIKSYYTVRQLELENLTTQET-REILHF 159

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622828204  819 QFTSWPDHGVPEDP----HLLLKLRRrvNAFSNFFSGPIVVHCSAGVGRTGTYIGIDA---MLEGLEAENKVDVYGYVVK 891
Cdd:cd14608    160 HYTTWPDFGVPESPasflNFLFKVRE--SGSLSPEHGPVVVHCSAGIGRSGTFCLADTcllLMDKRKDPSSVDIKKVLLE 237

                          250       260       270
                   ....*....|....*....|....*....|....*
gi 1622828204  892 LRRQRCLMVQVEAQYILIHQALVEYNQF--GETEV 924
Cdd:cd14608    238 MRKFRMGLIQTADQLRFSYLAVIEGAKFimGDSSV 272
PTPc-N3 cd14600
catalytic domain of tyrosine-protein phosphatase non-receptor type 3; Tyrosine-protein ...
 658-914 1.10e-52

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: 186.21  E-value: 1.10e-52
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622828204  658 LAEFQSIPRVFSKFPIKEARKPFNQNKNRYVDILPYDYNRVELSEingdaGSNYINASYID----GFKEPRKYIAAQGPR 733
Cdd:cd14600     17 LIQFEQLYRKKPGLAITCAKLPQNMDKNRYKDVLPYDATRVVLQG-----NEDYINASYVNmeipSANIVNKYIATQGPL 91

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622828204  734 DETVDDFWRMIWEQKATVIVMVTRCEEGNRNKCAEYWPSMEEgTRAFGDVVVKINQHKRCPDYIIQKLNIVNKKekaTGR 813
Cdd:cd14600     92 PHTCAQFWQVVWEQKLSLIVMLTTLTERGRTKCHQYWPDPPD-VMEYGGFRVQCHSEDCTIAYVFREMLLTNTQ---TGE 167

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622828204  814 E--VTHIQFTSWPDHGVPEDPHLLLKLRRRVNAfSNFFSGPIVVHCSAGVGRTGTYIGIDAMLEGLEAENKVDVYGYVVK 891
Cdd:cd14600    168 ErtVTHLQYVAWPDHGVPDDSSDFLEFVNYVRS-KRVENEPVLVHCSAGIGRTGVLVTMETAMCLTERNQPVYPLDIVRK 246

                          250       260
                   ....*....|....*....|...
gi 1622828204  892 LRRQRCLMVQVEAQYILIHQALV 914
Cdd:cd14600    247 MRDQRAMMVQTSSQYKFVCEAIL 269
PTP_fungal cd18533
fungal protein tyrosine phosphatases; This subfamily contains Saccharomyces cerevisiae ...
 1021-1227 1.77e-52

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: 183.22  E-value: 1.77e-52
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622828204 1021 YINASFI-MSYWKPEVMIAAQGPLKETIGDFWQMIFQRKVKVIVMLTELKHGDQEICAQYW--GEGKQTYGDIEVDM--K 1095
Cdd:cd18533      1 YINASYItLPGTSSKRYIATQGPLPATIGDFWKMIWQNNVGVIVMLTPLVENGREKCDQYWpsGEYEGEYGDLTVELvsE 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622828204 1096 DTNKSSTYTLRVFELRHSKRKdSRTVYQYQYTNWSVEQLPAEPKELVSLIQVLKEKLpqknssegNKHHKSTPLLIHCRD 1175
Cdd:cd18533     81 EENDDGGFIVREFELSKEDGK-VKKVYHIQYKSWPDFGVPDSPEDLLTLIKLKRELN--------DSASLDPPIIVHCSA 151

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1622828204 1176 GSQQTGIFCAL---LNLLE-----SAETEEVVD-IFQVVKALRKARPGMVSTFEQYQFLYD 1227
Cdd:cd18533    152 GVGRTGTFIALdslLDELKrglsdSQDLEDSEDpVYEIVNQLRKQRMSMVQTLRQYIFLYD 212
R-PTPc-R cd14611
catalytic domain of receptor-type tyrosine-protein phosphatase R; Receptor-type ...
 684-911 1.79e-52

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: 183.97  E-value: 1.79e-52
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622828204  684 KNRYVDILPYDYNRVELSEIN-GDAGSNYINASYIDGFK-EPRKYIAAQGPRDETVDDFWRMIWEQKATVIVMVTRCEEG 761
Cdd:cd14611      2 KNRYKTILPNPHSRVCLKPKNsNDSLSTYINANYIRGYGgKEKAFIATQGPMINTVNDFWQMVWQEDSPVIVMITKLKEK 81

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622828204  762 NRnKCAEYWPsmeEGTRAFGDVVVKINQHKRCPDYIIQKLNIvnkKEKATGREVTHIQFTSWPDHGVPEDPHLLLKLRRR 841
Cdd:cd14611     82 NE-KCVLYWP---EKRGIYGKVEVLVNSVKECDNYTIRNLTL---KQGSQSRSVKHYWYTSWPDHKTPDSAQPLLQLMLD 154

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1622828204  842 V--NAFSNFFSGPIVVHCSAGVGRTGTYIGIDAMLEGLEAENKVDVYGYVVKLRRQRCLMVQVEAQYILIHQ 911
Cdd:cd14611    155 VeeDRLASPGRGPVVVHCSAGIGRTGCFIATTIGCQQLKEEGVVDVLSIVCQLRVDRGGMVQTSEQYEFVHH 226
PTPc-N5 cd14613
catalytic domain of tyrosine-protein phosphatase non-receptor type 5; Tyrosine-protein ...
 659-916 3.88e-52

catalytic domain of tyrosine-protein phosphatase non-receptor type 5; Tyrosine-protein phosphatase non-receptor type 5 (PTPN5), also called striatum-enriched protein-tyrosine phosphatase (STEP) or neural-specific PTP, belongs to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. PTPN5/STEP is a kinase interaction motif (KIM)-PTP, characterized by the presence of a 16-amino-acid KIM that binds specifically to members of the MAPK (mitogen-activated protein kinase) family. It is a CNS-enriched protein that regulates key signaling proteins required for synaptic strengthening, as well as NMDA and AMPA receptor trafficking. PTPN5 is implicated in multiple neurologic and neuropsychiatric disorders, such as Alzheimer's disease, Parkinson's disease, schizophrenia, and fragile X syndrome.


Pssm-ID: 350461 [Multi-domain]  Cd Length: 258  Bit Score: 184.30  E-value: 3.88e-52
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622828204  659 AEFQSIPRVFSKfPiKEARKPFNQNKNRYVDILPYDYNRVEL-SEINGDAGSNYINASYIDGF-KEPRKYIAAQGPRDET 736
Cdd:cd14613      5 AEFFEIPMNFVD-P-KEYDIPGLVRKNRYKTILPNPHSRVCLtSPDQDDPLSSYINANYIRGYgGEEKVYIATQGPTVNT 82

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622828204  737 VDDFWRMIWEQKATVIVMVTRCEEGNRnKCAEYWPsmeEGTRAFGDVVVKINQHKRCPDYiiqKLNIVNKKEKATGREVT 816
Cdd:cd14613     83 VGDFWRMVWQERSPIIVMITNIEEMNE-KCTEYWP---EEQVTYEGIEITVKQVIHADDY---RLRLITLKSGGEERGLK 155

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622828204  817 HIQFTSWPDHGVPEDPHLLLKLRRRVNAF---SNFFSGPIVVHCSAGVGRTGTYIGIDAMLEGLEAENKVDVYGYVVKLR 893
Cdd:cd14613    156 HYWYTSWPDQKTPDNAPPLLQLVQEVEEArqqAEPNCGPVIVHCSAGIGRTGCFIATSICCKQLRNEGVVDILRTTCQLR 235

                          250       260
                   ....*....|....*....|...
gi 1622828204  894 RQRCLMVQVEAQYILIHQALVEY 916
Cdd:cd14613    236 LDRGGMIQTCEQYQFVHHVLSLY 258
PHA02746 PHA02746
protein tyrosine phosphatase; Provisional
 678-913 1.73e-51

protein tyrosine phosphatase; Provisional


Pssm-ID: 165113 [Multi-domain]  Cd Length: 323  Bit Score: 184.46  E-value: 1.73e-51
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622828204  678 KPFNQNKNRYVDILPYDYNRVELSE-------------------INGDAGSNYINASYIDGFKEPRKYIAAQGPRDETVD 738
Cdd:PHA02746    48 KKENLKKNRFHDIPCWDHSRVVINAheslkmfdvgdsdgkkievTSEDNAENYIHANFVDGFKEANKFICAQGPKEDTSE 127

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622828204  739 DFWRMIWEQKATVIVMVTRCEEGNRnKCAEYWPSMEEGTRAFGDVVVKINQHKRCPDYIIQKLNIVNKKEKaTGREVTHI 818
Cdd:PHA02746   128 DFFKLISEHESQVIVSLTDIDDDDE-KCFELWTKEEDSELAFGRFVAKILDIIEELSFTKTRLMITDKISD-TSREIHHF 205

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622828204  819 QFTSWPDHGVPEDPHLLLKLRRRVNA----------FSNFFSGPIVVHCSAGVGRTGTYIGIDAMLEGLEAENKVDVYGY 888
Cdd:PHA02746   206 WFPDWPDNGIPTGMAEFLELINKVNEeqaelikqadNDPQTLGPIVVHCSAGIGRAGTFCAIDNALEQLEKEKEVCLGEI 285

                          250       260
                   ....*....|....*....|....*
gi 1622828204  889 VVKLRRQRCLMVQVEAQYILIHQAL 913
Cdd:PHA02746   286 VLKIRKQRHSSVFLPEQYAFCYKAL 310
R-PTP-N-N2 cd14546
PTP-like domain of receptor-type tyrosine-protein phosphatase-like N and N2; Receptor-type ...
 711-925 1.92e-51

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: 180.33  E-value: 1.92e-51
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622828204  711 YINASYIDGfKEPRK--YIAAQGPRDETVDDFWRMIWEQKATVIVMVTRCEEGNRNKCAEYWPsmEEGTRAFGDVVVK-I 787
Cdd:cd14546      1 YINASTIYD-HDPRNpaYIATQGPLPHTIADFWQMIWEQGCVVIVMLTRLQENGVKQCARYWP--EEGSEVYHIYEVHlV 77

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622828204  788 NQHKRCPDYIIQKLNIVNKKEKATgREVTHIQFTSWPDHGVPEDPHLLLKLRRRVNAFSNFFSGPIVVHCSAGVGRTGTY 867
Cdd:cd14546     78 SEHIWCDDYLVRSFYLKNLQTSET-RTVTQFHFLSWPDEGIPASAKPLLEFRRKVNKSYRGRSCPIVVHCSDGAGRTGTY 156

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 1622828204  868 IGIDAMLEGLEAENK-VDVYGYVVKLRRQRCLMVQVEAQYILIHQALVEynqfgetEVN 925
Cdd:cd14546    157 ILIDMVLNRMAKGAKeIDIAATLEHLRDQRPGMVKTKDQFEFVLTAVAE-------EVN 208
R-PTPc-LAR-1 cd14553
catalytic domain of LAR family receptor-type tyrosine-protein phosphatases, repeat 1; The LAR ...
 970-1229 2.13e-51

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: 181.44  E-value: 2.13e-51
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622828204  970 EENKNKNRNSNVIPYDYNRVPLKhelemskesdhdsdessddDSDSEEPSKYINASFIMSYWKPEVMIAAQGPLKETIGD 1049
Cdd:cd14553      1 EVNKPKNRYANVIAYDHSRVILQ-------------------PIEGVPGSDYINANYCDGYRKQNAYIATQGPLPETFGD 61

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622828204 1050 FWQMIFQRKVKVIVMLTELKHGDQEICAQYW-GEGKQTYGDIEVDMKDTNKSSTYTLRVFELRHSKRKDSRTVYQYQYTN 1128
Cdd:cd14553     62 FWRMVWEQRSATIVMMTKLEERSRVKCDQYWpTRGTETYGLIQVTLLDTVELATYTVRTFALHKNGSSEKREVRQFQFTA 141

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622828204 1129 WSVEQLPAEPKELVSLIQVLKEKLPQknssegnkhhKSTPLLIHCRDGSQQTGIFCALLNLLESAETEEVVDIFQVVKAL 1208
Cdd:cd14553    142 WPDHGVPEHPTPFLAFLRRVKACNPP----------DAGPIVVHCSAGVGRTGCFIVIDSMLERIKHEKTVDIYGHVTCL 211

                          250       260
                   ....*....|....*....|.
gi 1622828204 1209 RKARPGMVSTFEQYQFLYDII 1229
Cdd:cd14553    212 RAQRNYMVQTEDQYIFIHDAL 232
R-PTP-LAR-2 cd14554
PTP-like domain of the LAR family receptor-type tyrosine-protein phosphatases, repeat 2; The ...
 972-1226 4.02e-51

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: 180.41  E-value: 4.02e-51
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622828204  972 NKNKNRNSNVIPYDYNRVPLK--HELEMSkesdhdsdessdddsdseepsKYINASFIMSYWKPEVMIAAQGPLKETIGD 1049
Cdd:cd14554      6 NKFKNRLVNILPYESTRVCLQpiRGVEGS---------------------DYINASFIDGYRQRGAYIATQGPLAETTED 64

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622828204 1050 FWQMIFQRKVKVIVMLTELKHGDQEICAQYW-GEGKQTYGDIEVDMKDTNKSSTYTLRVFELRHSKRKDSRTVYQYQYTN 1128
Cdd:cd14554     65 FWRMLWEHNSTIIVMLTKLREMGREKCHQYWpAERSARYQYFVVDPMAEYNMPQYILREFKVTDARDGQSRTVRQFQFTD 144

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622828204 1129 WSVEQLPAEPKELVSLI-QVLKEKlpQKNSSEGnkhhkstPLLIHCRDGSQQTGIFCALLNLLESAETEEVVDIFQVVKA 1207
Cdd:cd14554    145 WPEQGVPKSGEGFIDFIgQVHKTK--EQFGQEG-------PITVHCSAGVGRTGVFITLSIVLERMRYEGVVDVFQTVKL 215

                          250
                   ....*....|....*....
gi 1622828204 1208 LRKARPGMVSTFEQYQFLY 1226
Cdd:cd14554    216 LRTQRPAMVQTEDQYQFCY 234
R-PTP-N2 cd14610
PTP-like domain of receptor-type tyrosine-protein phosphatase N2; Receptor-type ...
 676-915 9.24e-51

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: 181.02  E-value: 9.24e-51
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622828204  676 ARKPFNQNKNRYVDILPYDYNRVELSEINGDAGSNYINASYIDGfKEPRK--YIAAQGPRDETVDDFWRMIWEQKATVIV 753
Cdd:cd14610     39 AQREENVQKNRSLAVLPYDHSRIILKAENSHSHSDYINASPIMD-HDPRNpaYIATQGPLPATVADFWQMVWESGCVVIV 117

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622828204  754 MVTRCEEGNRNKCAEYWPsmEEGTRAFGDVVVK-INQHKRCPDYIIQKLNIVNKKEKATgREVTHIQFTSWPDHGVPEDP 832
Cdd:cd14610    118 MLTPLAENGVKQCYHYWP--DEGSNLYHIYEVNlVSEHIWCEDFLVRSFYLKNLQTNET-RTVTQFHFLSWNDQGVPAST 194

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622828204  833 HLLLKLRRRVNAFSNFFSGPIVVHCSAGVGRTGTYIGIDAMLEGL-EAENKVDVYGYVVKLRRQRCLMVQVEAQYILIHQ 911
Cdd:cd14610    195 RSLLDFRRKVNKCYRGRSCPIIVHCSDGAGRSGTYILIDMVLNKMaKGAKEIDIAATLEHLRDQRPGMVQTKEQFEFALT 274


                   ....
gi 1622828204  912 ALVE 915
Cdd:cd14610    275 AVAE 278
R-PTPc-typeIIb-2 cd14556
PTP domain of type IIb (or R2B) subfamily receptor-type tyrosine-protein phosphatases, repeat ...
 1021-1227 6.67e-50

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: 175.67  E-value: 6.67e-50
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622828204 1021 YINASFIMSYWKPEVMIAAQGPLKETIGDFWQMIFQRKVKVIVMLTELKHGDQEiCAQYWGE-GKQTYGDIEVDMKDTNK 1099
Cdd:cd14556      1 YINAALLDSYKQPAAFIVTQHPLPNTVTDFWRLVYDYGCTSIVMLNQLDPKDQS-CPQYWPDeGSGTYGPIQVEFVSTTI 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622828204 1100 SSTYTLRVFELRHSKR--KDSRTVYQYQYTNWSVEQL-PAEPKELVSLIQVLkEKLpQKNSSEGnkhhkstPLLIHCRDG 1176
Cdd:cd14556     80 DEDVISRIFRLQNTTRpqEGYRMVQQFQFLGWPRDRDtPPSKRALLKLLSEV-EKW-QEQSGEG-------PIVVHCLNG 150

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|.
gi 1622828204 1177 SQQTGIFCALLNLLESAETEEVVDIFQVVKALRKARPGMVSTFEQYQFLYD 1227
Cdd:cd14556    151 VGRSGVFCAISSVCERIKVENVVDVFQAVKTLRNHRPNMVETEEQYKFCYD 201
R-PTP-N cd14609
PTP-like domain of receptor-type tyrosine-protein phosphatase N; Receptor-type ...
 658-915 3.76e-49

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: 176.38  E-value: 3.76e-49
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622828204  658 LAEFQSIPRVFSKfpikeARKPFNQNKNRYVDILPYDYNRVELSEINGDAGSNYINASYIDGfKEPR--KYIAAQGPRDE 735
Cdd:cd14609     24 LCAYQAEPNTCST-----AQGEANVKKNRNPDFVPYDHARIKLKAESNPSRSDYINASPIIE-HDPRmpAYIATQGPLSH 97

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622828204  736 TVDDFWRMIWEQKATVIVMVTRCEEGNRNKCAEYWPsmEEGTRAFGDVVVK-INQHKRCPDYIIQKLNIVNKKEKATgRE 814
Cdd:cd14609     98 TIADFWQMVWENGCTVIVMLTPLVEDGVKQCDRYWP--DEGSSLYHIYEVNlVSEHIWCEDFLVRSFYLKNVQTQET-RT 174

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622828204  815 VTHIQFTSWPDHGVPEDPHLLLKLRRRVNAFSNFFSGPIVVHCSAGVGRTGTYIGIDAMLEGL-EAENKVDVYGYVVKLR 893
Cdd:cd14609    175 LTQFHFLSWPAEGIPSSTRPLLDFRRKVNKCYRGRSCPIIVHCSDGAGRTGTYILIDMVLNRMaKGVKEIDIAATLEHVR 254

                          250       260
                   ....*....|....*....|..
gi 1622828204  894 RQRCLMVQVEAQYILIHQALVE 915
Cdd:cd14609    255 DQRPGMVRTKDQFEFALTAVAE 276
PTPc-N20 cd14596
catalytic domain of tyrosine-protein phosphatase non-receptor type 20; Tyrosine-protein ...
 711-915 6.04e-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: 6.04e-49
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622828204  711 YINASYID---GFKEpRKYIAAQGPRDETVDDFWRMIWEQKATVIVMVTRCEEGNRNKCAEYWPSMEEGTRAFGDVVVKI 787
Cdd:cd14596      1 YINASYITmpvGEEE-LFYIATQGPLPSTIDDFWQMVWENRSDVIAMMTREVERGKVKCHRYWPETLQEPMELENYQLRL 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622828204  788 NQHKRCPDYIIQKLNIVNkKEKATGREVTHIQFTSWPDHGVPEDPHLLLKLRRRVNAFSNffSGPIVVHCSAGVGRTGTY 867
Cdd:cd14596     80 ENYQALQYFIIRIIKLVE-KETGENRLIKHLQFTTWPDHGTPQSSDQLVKFICYMRKVHN--TGPIVVHCSAGIGRAGVL 156

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*...
gi 1622828204  868 IGIDAMLEGLEAENKVDVYGYVVKLRRQRCLMVQVEAQYILIHQALVE 915
Cdd:cd14596    157 ICVDVLLSLIEKDLSFNIKDIVREMRQQRYGMIQTKDQYLFCYKVVLE 204
R-PTPc-H cd14619
catalytic domain of receptor-type tyrosine-protein phosphatase H; Receptor-type ...
 976-1229 7.65e-49

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: 173.92  E-value: 7.65e-49
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622828204  976 NRNSNVIPYDYNRVPLK--HELEMSKesdhdsdessdddsdseepskYINASFIMSYWKPEVMIAAQGPLKETIGDFWQM 1053
Cdd:cd14619      1 NRFRNVLPYDWSRVPLKpiHEEPGSD---------------------YINANYMPGYWSSQEFIATQGPLPQTVGDFWRM 59

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622828204 1054 IFQRKVKVIVMLTELKHGDQEICAQYWGEGKQ--TYGDIEVDMKDTNKSSTYTLRVFELRHSKRKDSRTVYQYQYTNWSV 1131
Cdd:cd14619     60 IWEQQSSTIVMLTNCMEAGRVKCEHYWPLDYTpcTYGHLRVTVVSEEVMENWTVREFLLKQVEEQKTLSVRHFHFTAWPD 139

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622828204 1132 EQLPAEPKELVSLIQVLKEKLPQKNSsegnkhhkSTPLLIHCRDGSQQTGIFCALLNLLESAETEEVVDIFQVVKALRKA 1211
Cdd:cd14619    140 HGVPSSTDTLLAFRRLLRQWLDQTMS--------GGPTVVHCSAGVGRTGTLIALDVLLQQLQSEGLLGPFSFVQKMREN 211

                          250
                   ....*....|....*...
gi 1622828204 1212 RPGMVSTFEQYQFLYDII 1229
Cdd:cd14619    212 RPLMVQTESQYVFLHQCI 229
R-PTP-S-2 cd14627
PTP-like domain of receptor-type tyrosine-protein phosphatase S, repeat 2; Receptor-type ...
 922-1226 8.41e-49

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: 175.69  E-value: 8.41e-49
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622828204  922 TEVNLSELHPYLHNMKKRDPPSEPSPLEAEFQRLPSYRSWRTQHI-GNQEENKNKNRNSNVIPYDYNRVPLKhelemske 1000
Cdd:cd14627      2 TEVPARNLYSYIQKLAQVEVGEHVTGMELEFKRLANSKAHTSRFIsANLPCNKFKNRLVNIMPYETTRVCLQ-------- 73

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622828204 1001 sdhdsdessddDSDSEEPSKYINASFIMSYWKPEVMIAAQGPLKETIGDFWQMIFQRKVKVIVMLTELKHGDQEICAQYW 1080
Cdd:cd14627     74 -----------PIRGVEGSDYINASFIDGYRQQKAYIATQGPLAETTEDFWRMLWENNSTIVVMLTKLREMGREKCHQYW 142

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622828204 1081 -GEGKQTYGDIEVDMKDTNKSSTYTLRVFELRHSKRKDSRTVYQYQYTNWSVEQLPAEPKELVSLI-QVLKEKlpqknss 1158
Cdd:cd14627    143 pAERSARYQYFVVDPMAEYNMPQYILREFKVTDARDGQSRTVRQFQFTDWPEQGVPKSGEGFIDFIgQVHKTK------- 215

                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1622828204 1159 egNKHHKSTPLLIHCRDGSQQTGIFCALLNLLESAETEEVVDIFQVVKALRKARPGMVSTFEQYQFLY 1226
Cdd:cd14627    216 --EQFGQDGPISVHCSAGVGRTGVFITLSIVLERMRYEGVVDIFQTVKMLRTQRPAMVQTEDEYQFCY 281
R-PTPc-E-2 cd14622
catalytic domain of receptor-type tyrosine-protein phosphatase E, repeat 2; Receptor-type ...
 710-916 8.73e-49

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


Pssm-ID: 350470 [Multi-domain]  Cd Length: 205  Bit Score: 172.50  E-value: 8.73e-49
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622828204  710 NYINASYIDGFKEPRKYIAAQGPRDETVDDFWRMIWEQKATVIVMVTRCEEGNRNKCAEYWPSmeEGTRAFGDVVVKINQ 789
Cdd:cd14622      1 DYINASFIDGYRQKDYFIATQGPLAHTVEDFWRMVWEWKCHTIVMLTELQEREQEKCVQYWPS--EGSVTHGEITIEIKN 78

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622828204  790 HKRCPDYIIQKLNIVNKKEKATgREVTHIQFTSWPDHGVPEDPH----LLLKLRRRVNAFSNffsGPIVVHCSAGVGRTG 865
Cdd:cd14622     79 DTLLETISIRDFLVTYNQEKQT-RLVRQFHFHGWPEIGIPAEGKgmidLIAAVQKQQQQTGN---HPIVVHCSAGAGRTG 154

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|.
gi 1622828204  866 TYIGIDAMLEGLEAENKVDVYGYVVKLRRQRCLMVQVEAQYILIHQALVEY 916
Cdd:cd14622    155 TFIALSNILERVKAEGLLDVFQTVKSLRLQRPHMVQTLEQYEFCYRVVQDF 205
R-PTP-D-2 cd14628
PTP-like domain of receptor-type tyrosine-protein phosphatase D, repeat 2; Receptor-type ...
 922-1226 2.56e-48

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: 174.53  E-value: 2.56e-48
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622828204  922 TEVNLSELHPYLHNMKKRDPPSEPSPLEAEFQRLPSYRSWRTQHI-GNQEENKNKNRNSNVIPYDYNRVPLKhelemske 1000
Cdd:cd14628      1 TEVPARNLYAYIQKLTQIETGENVTGMELEFKRLASSKAHTSRFIsANLPCNKFKNRLVNIMPYESTRVCLQ-------- 72

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622828204 1001 sdhdsdessddDSDSEEPSKYINASFIMSYWKPEVMIAAQGPLKETIGDFWQMIFQRKVKVIVMLTELKHGDQEICAQYW 1080
Cdd:cd14628     73 -----------PIRGVEGSDYINASFIDGYRQQKAYIATQGPLAETTEDFWRMLWEHNSTIVVMLTKLREMGREKCHQYW 141

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622828204 1081 -GEGKQTYGDIEVDMKDTNKSSTYTLRVFELRHSKRKDSRTVYQYQYTNWSVEQLPAEPKELVSLI-QVLKEKlpqknss 1158
Cdd:cd14628    142 pAERSARYQYFVVDPMAEYNMPQYILREFKVTDARDGQSRTVRQFQFTDWPEQGVPKSGEGFIDFIgQVHKTK------- 214

                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1622828204 1159 egNKHHKSTPLLIHCRDGSQQTGIFCALLNLLESAETEEVVDIFQVVKALRKARPGMVSTFEQYQFLY 1226
Cdd:cd14628    215 --EQFGQDGPISVHCSAGVGRTGVFITLSIVLERMRYEGVVDIFQTVKMLRTQRPAMVQTEDQYQFCY 280
PTPc-N9 cd14543
catalytic domain of tyrosine-protein phosphatase non-receptor type 9; Tyrosine-protein ...
 972-1226 4.60e-48

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: 172.93  E-value: 4.60e-48
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622828204  972 NKNKNRNSNVIPYDYNRVPLKHELEmskesdhdsdessdddsdsEEPSKYINASFIMSYWKPEVMIAAQGPLKETIGDFW 1051
Cdd:cd14543     29 NQEKNRYGDVLCLDQSRVKLPKRNG-------------------DERTDYINANFMDGYKQKNAYIATQGPLPKTYSDFW 89

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622828204 1052 QMIFQRKVKVIVMLTELKHGDQEICAQYW---GEGKQTYGDIEVDMKDTNKSSTYTLRVFELRHSKRKDSRTVYQYQYTN 1128
Cdd:cd14543     90 RMVWEQKVLVIVMTTRVVERGRVKCGQYWpleEGSSLRYGDLTVTNLSVENKEHYKKTTLEIHNTETDESRQVTHFQFTS 169

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622828204 1129 WSVEQLPAEPKELVSLIQVLKEKLPQKNSSEGN---KHHKSTPLLIHCRDGSQQTGIFCALLNLLESAETEEVVDIFQVV 1205
Cdd:cd14543    170 WPDFGVPSSAAALLDFLGEVRQQQALAVKAMGDrwkGHPPGPPIVVHCSAGIGRTGTFCTLDICLSQLEDVGTLNVMQTV 249

                          250       260
                   ....*....|....*....|.
gi 1622828204 1206 KALRKARPGMVSTFEQYQFLY 1226
Cdd:cd14543    250 RRMRTQRAFSIQTPDQYYFCY 270
PTPc-N2 cd14607
catalytic domain of tyrosine-protein phosphatase non-receptor type 2; Tyrosine-protein ...
 669-905 6.05e-48

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: 172.07  E-value: 6.05e-48
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622828204  669 SKFPIKEARKPFNQNKNRYVDILPYDYNRVELSEINGDagsnYINASYIDGFKEPRKYIAAQGPRDETVDDFWRMIWEQK 748
Cdd:cd14607     12 HDYPHRVAKYPENRNRNRYRDVSPYDHSRVKLQNTEND----YINASLVVIEEAQRSYILTQGPLPNTCCHFWLMVWQQK 87

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622828204  749 ATVIVMVTRCEEGNRNKCAEYWPSMEEGTRAFGDV--VVKINQHKRCPDYIIQKLNIVNKKEKATgREVTHIQFTSWPDH 826
Cdd:cd14607     88 TKAVVMLNRIVEKDSVKCAQYWPTDEEEVLSFKETgfSVKLLSEDVKSYYTVHLLQLENINSGET-RTISHFHYTTWPDF 166

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622828204  827 GVPEDP----HLLLKLRRrvNAFSNFFSGPIVVHCSAGVGRTGTYIGIDAMLEGLEAEN--KVDVYGYVVKLRRQRCLMV 900
Cdd:cd14607    167 GVPESPasflNFLFKVRE--SGSLSPEHGPAVVHCSAGIGRSGTFSLVDTCLVLMEKKDpdSVDIKQVLLDMRKYRMGLI 244


                   ....*
gi 1622828204  901 QVEAQ 905
Cdd:cd14607    245 QTPDQ 249
PTPc_plant_PTP1 cd17658
protein tyrosine phosphatase 1 from Arabidopsis thaliana and similar plant PTPs; Arabidopsis ...
 711-910 2.01e-47

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


Pssm-ID: 350496 [Multi-domain]  Cd Length: 206  Bit Score: 168.80  E-value: 2.01e-47
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622828204  711 YINASYI--DGFKEPRKYIAAQGPRDETVDDFWRMIWEQKATVIVMVTRCEEGNR-NKCAEYWPSMEEGTRAFGDVVVKI 787
Cdd:cd17658      1 YINASLVetPASESLPKFIATQGPLPHTFEDFWEMVIQQRCPVIIMLTRLVDNYStAKCADYFPAEENESREFGRISVTN 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622828204  788 NQHKrCPDYIIQKLNI-VNKKE-KATGREVTHIQFTSWPDHGVPEDPHLLLKLRRRVNAFSNFFsGPIVVHCSAGVGRTG 865
Cdd:cd17658     81 KKLK-HSQHSITLRVLeVQYIEsEEPPLSVLHIQYPEWPDHGVPKDTRSVRELLKRLYGIPPSA-GPIVVHCSAGIGRTG 158

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|
gi 1622828204  866 TYIGID----AMLEG-LEAenkVDVYGYVVKLRRQRCLMVQVEAQYILIH 910
Cdd:cd17658    159 AYCTIHntirRILEGdMSA---VDLSKTVRKFRSQRIGMVQTQDQYIFCY 205
PHA02747 PHA02747
protein tyrosine phosphatase; Provisional
 673-910 3.54e-47

protein tyrosine phosphatase; Provisional


Pssm-ID: 165114 [Multi-domain]  Cd Length: 312  Bit Score: 171.72  E-value: 3.54e-47
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622828204  673 IKEARKPFNQNKNRYVDILPYDYNRVELsEINGDAGSNYINASYIDGFKEPRKYIAAQGPRDETVDDFWRMIWEQKATVI 752
Cdd:PHA02747    43 IANFEKPENQPKNRYWDIPCWDHNRVIL-DSGGGSTSDYIHANWIDGFEDDKKFIATQGPFAETCADFWKAVWQEHCSII 121

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622828204  753 VMVTRCEEGN-RNKCAEYWPSMEEGTRAFGDVVVKINQHKRCPDYIIQKLNIVNKKEKaTGREVTHIQFTSWPDHGVPED 831
Cdd:PHA02747   122 VMLTPTKGTNgEEKCYQYWCLNEDGNIDMEDFRIETLKTSVRAKYILTLIEITDKILK-DSRKISHFQCSEWFEDETPSD 200

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622828204  832 PHLLLKL-----RRRVNAFSNFFS-----GPIVVHCSAGVGRTGTYIGIDAMLEGLEAENKVDVYGYVVKLRRQRCLMVQ 901
Cdd:PHA02747   201 HPDFIKFikiidINRKKSGKLFNPkdallCPIVVHCSDGVGKTGIFCAVDICLNQLVKRKAICLAKTAEKIREQRHAGIM 280


                   ....*....
gi 1622828204  902 VEAQYILIH 910
Cdd:PHA02747   281 NFDDYLFIQ 289
R-PTPc-V cd14618
catalytic domain of receptor-type tyrosine-protein phosphatase V; Receptor-type ...
 976-1229 1.01e-46

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: 167.43  E-value: 1.01e-46
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622828204  976 NRNSNVIPYDYNRVPLKhelEMSKESDHdsdessdddsdseepsKYINASFIMSYWKPEVMIAAQGPLKETIGDFWQMIF 1055
Cdd:cd14618      1 NRYPHVLPYDHSRVRLS---QLGGEPHS----------------DYINANFIPGYTSPQEFIATQGPLKKTIEDFWRLVW 61

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622828204 1056 QRKVKVIVMLTELKHGDQEICAQYWGEGKQ--TYGDIEVDMKDTNKSSTYTLRVFELRHSKRKDSRTVYQYQYTNWSVEQ 1133
Cdd:cd14618     62 EQQVCNIIMLTVGMENGRVLCDHYWPSESTpvSYGHITVHLLAQSSEDEWTRREFKLWHEDLRKERRVKHLHYTAWPDHG 141

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622828204 1134 LPAEPKELVSLIQVLKEKLpqkNSSEGnkhhkSTPLLIHCRDGSQQTGIFCALLNLLESAETEEVVDIFQVVKALRKARP 1213
Cdd:cd14618    142 IPESTSSLMAFRELVREHV---QATKG-----KGPTLVHCSAGVGRSGTFIALDRLLRQLKEEKVVDVFNTVYILRMHRY 213

                          250
                   ....*....|....*.
gi 1622828204 1214 GMVSTFEQYQFLYDII 1229
Cdd:cd14618    214 LMIQTLSQYIFLHSCI 229
R-PTP-F-2 cd14629
PTP-like domain of receptor-type tyrosine-protein phosphatase F, repeat 2; Receptor-type ...
 922-1226 9.07e-46

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: 167.21  E-value: 9.07e-46
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622828204  922 TEVNLSELHPYLHNMKKRDPPSEPSPLEAEFQRLPSYRSWRTQHI-GNQEENKNKNRNSNVIPYDYNRVPLKhelemske 1000
Cdd:cd14629      2 TEVPARNLYAHIQKLTQVPPGESVTAMELEFKLLANSKAHTSRFIsANLPCNKFKNRLVNIMPYELTRVCLQ-------- 73

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622828204 1001 sdhdsdessddDSDSEEPSKYINASFIMSYWKPEVMIAAQGPLKETIGDFWQMIFQRKVKVIVMLTELKHGDQEICAQYW 1080
Cdd:cd14629     74 -----------PIRGVEGSDYINASFIDGYRQQKAYIATQGPLAETTEDFWRMLWEHNSTIVVMLTKLREMGREKCHQYW 142

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622828204 1081 -GEGKQTYGDIEVDMKDTNKSSTYTLRVFELRHSKRKDSRTVYQYQYTNWSVEQLPAEPKELVSLI-QVLKEKlpqknss 1158
Cdd:cd14629    143 pAERSARYQYFVVDPMAEYNMPQYILREFKVTDARDGQSRTIRQFQFTDWPEQGVPKTGEGFIDFIgQVHKTK------- 215

                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1622828204 1159 egNKHHKSTPLLIHCRDGSQQTGIFCALLNLLESAETEEVVDIFQVVKALRKARPGMVSTFEQYQFLY 1226
Cdd:cd14629    216 --EQFGQDGPITVHCSAGVGRTGVFITLSIVLERMRYEGVVDMFQTVKTLRTQRPAMVQTEDQYQLCY 281
PTPc-KIM cd14547
catalytic domain of the kinase interaction motif (KIM) family of protein-tyrosine phosphatases; ...
 1021-1226 9.10e-46

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: 164.49  E-value: 9.10e-46
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622828204 1021 YINASFIMSY-WKPEVMIAAQGPLKETIGDFWQMIFQRKVKVIVMLTELKHGDQEiCAQYWGEGK-QTYGDIEVDMKDTN 1098
Cdd:cd14547     27 YINANYIRGYdGEEKAYIATQGPLPNTVADFWRMVWQEKTPIIVMITNLTEAKEK-CAQYWPEEEnETYGDFEVTVQSVK 105

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622828204 1099 KSSTYTLRVFELRHskRKDSRTVYQYQYTNWSVEQLPAEPKELVSLIQVLkEKLPQKNSSEGnkhhkstPLLIHCRDGSQ 1178
Cdd:cd14547    106 ETDGYTVRKLTLKY--GGEKRYLKHYWYTSWPDHKTPEAAQPLLSLVQEV-EEARQTEPHRG-------PIVVHCSAGIG 175

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*...
gi 1622828204 1179 QTGIFCALLNLLESAETEEVVDIFQVVKALRKARPGMVSTFEQYQFLY 1226
Cdd:cd14547    176 RTGCFIATSIGCQQLREEGVVDVLGIVCQLRLDRGGMVQTAEQYEFVH 223
R-PTPc-T-1 cd14630
catalytic domain of receptor-type tyrosine-protein phosphatase T, repeat 1; Receptor-type ...
 970-1229 1.70e-45

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: 164.43  E-value: 1.70e-45
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622828204  970 EENKNKNRNSNVIPYDYNRVPLKhelemskesdhdsdessddDSDSEEPSKYINASFIMSYWKPEVMIAAQGPLKETIGD 1049
Cdd:cd14630      1 DENRNKNRYGNIISYDHSRVRLQ-------------------LLDGDPHSDYINANYIDGYHRPRHYIATQGPMQETVKD 61

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622828204 1050 FWQMIFQRKVKVIVMLTELKHGDQEICAQYWGEGKQTYGDIEVDMKDTNKSSTYTLRVFELRHSKRKDSRTVYQYQYTNW 1129
Cdd:cd14630     62 FWRMIWQENSASVVMVTNLVEVGRVKCVRYWPDDTEVYGDIKVTLIETEPLAEYVIRTFTVQKKGYHEIREIRQFHFTSW 141

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622828204 1130 SVEQLPAEPKELVSLIQVLKEKLPQknssegnkhhKSTPLLIHCRDGSQQTGIFCALLNLLESAETEEVVDIFQVVKALR 1209
Cdd:cd14630    142 PDHGVPCYATGLLGFVRQVKFLNPP----------DAGPIVVHCSAGAGRTGCFIAIDIMLDMAENEGVVDIFNCVRELR 211

                          250       260
                   ....*....|....*....|
gi 1622828204 1210 KARPGMVSTFEQYQFLYDII 1229
Cdd:cd14630    212 AQRVNMVQTEEQYVFVHDAI 231
R-PTPc-J cd14615
catalytic domain of receptor-type tyrosine-protein phosphatase J; Receptor-type ...
 976-1225 3.14e-45

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: 163.06  E-value: 3.14e-45
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622828204  976 NRNSNVIPYDYNRVPLKHElemskesdhdsdessdddsdSEEPSKYINASFIMSYWKPEVMIAAQGPLKETIGDFWQMIF 1055
Cdd:cd14615      1 NRYNNVLPYDISRVKLSVQ--------------------SHSTDDYINANYMPGYNSKKEFIAAQGPLPNTVKDFWRMVW 60

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622828204 1056 QRKVKVIVMLTELKHGDQEICAQYW-GEGKQTYGDIEVDMKDTNKSSTYTLRVFELRHSKRKDSRTVYQYQYTNWSVEQL 1134
Cdd:cd14615     61 EKNVYAIVMLTKCVEQGRTKCEEYWpSKQKKDYGDITVTMTSEIVLPEWTIRDFTVKNAQTNESRTVRHFHFTSWPDHGV 140

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622828204 1135 PAEPKELVSLIQVLKEKLPQknssegnkHHKSTPLLIHCRDGSQQTGIFCALLNLLESAETEEVVDIFQVVKALRKARPG 1214
Cdd:cd14615    141 PETTDLLINFRHLVREYMKQ--------NPPNSPILVHCSAGVGRTGTFIAIDRLIYQIENENVVDVYGIVYDLRMHRPL 212

                          250
                   ....*....|.
gi 1622828204 1215 MVSTFEQYQFL 1225
Cdd:cd14615    213 MVQTEDQYVFL 223
R-PTPc-F-1 cd14626
catalytic domain of receptor-type tyrosine-protein phosphatase F, repeat 1; Receptor-type ...
 968-1227 5.31e-45

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: 164.44  E-value: 5.31e-45
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622828204  968 NQEENKNKNRNSNVIPYDYNRVPLkhelemskesdhdsdessdDDSDSEEPSKYINASFIMSYWKPEVMIAAQGPLKETI 1047
Cdd:cd14626     37 NLEVNKPKNRYANVIAYDHSRVIL-------------------TSVDGVPGSDYINANYIDGYRKQNAYIATQGPLPETL 97

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622828204 1048 GDFWQMIFQRKVKVIVMLTELKHGDQEICAQYW-GEGKQTYGDIEVDMKDTNKSSTYTLRVFELRHSKRKDSRTVYQYQY 1126
Cdd:cd14626     98 SDFWRMVWEQRTATIVMMTRLEEKSRVKCDQYWpIRGTETYGMIQVTLLDTVELATYSVRTFALYKNGSSEKREVRQFQF 177

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622828204 1127 TNWSVEQLPAEPKELVSLIQVLKEKLPQknssegnkhhKSTPLLIHCRDGSQQTGIFCALLNLLESAETEEVVDIFQVVK 1206
Cdd:cd14626    178 MAWPDHGVPEYPTPILAFLRRVKACNPP----------DAGPMVVHCSAGVGRTGCFIVIDAMLERMKHEKTVDIYGHVT 247

                          250       260
                   ....*....|....*....|.
gi 1622828204 1207 ALRKARPGMVSTFEQYQFLYD 1227
Cdd:cd14626    248 CMRSQRNYMVQTEDQYIFIHE 268
PTP-N23 cd14539
PTP-like domain of tyrosine-protein phosphatase non-receptor type 23; Tyrosine-protein ...
 711-911 1.28e-43

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: 157.55  E-value: 1.28e-43
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622828204  711 YINASYIDGFKE--PRkYIAAQGPRDETVDDFWRMIWEQKATVIVMVTRCEEGNRNKCAEYWPSMEEGTRAFGDVVVKIN 788
Cdd:cd14539      1 YINASLIEDLTPycPR-FIATQAPLPGTAADFWLMVYEQQVSVIVMLVSEQENEKQKVHRYWPTERGQALVYGAITVSLQ 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622828204  789 QHKRCPDYIIQKLNIVNKKEKATgREVTHIQFTSWPDHGVPEDPHLLLKLRRRVNAFSNFFSG---PIVVHCSAGVGRTG 865
Cdd:cd14539     80 SVRTTPTHVERIISIQHKDTRLS-RSVVHLQFTTWPELGLPDSPNPLLRFIEEVHSHYLQQRSlqtPIVVHCSSGVGRTG 158

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*...
gi 1622828204  866 TY-IGIDAMLEgLEAENKV-DVYGYVVKLRRQRCLMVQVEAQYILIHQ 911
Cdd:cd14539    159 AFcLLYAAVQE-IEAGNGIpDLPQLVRKMRQQRKYMLQEKEHLKFCYE 205
PTPc-N4 cd14601
catalytic domain of tyrosine-protein phosphatase non-receptor type 4; Tyrosine-protein ...
 710-915 2.41e-43

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: 157.03  E-value: 2.41e-43
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622828204  710 NYINASYID----GFKEPRKYIAAQGPRDETVDDFWRMIWEQKATVIVMVTRCEEGNRNKCAEYWPSMeEGTRAFGDVVV 785
Cdd:cd14601      1 DYINANYINmeipSSSIINRYIACQGPLPNTCSDFWQMTWEQGSSMVVMLTTQVERGRVKCHQYWPEP-SGSSSYGGFQV 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622828204  786 KINQHKRCPDYIIQKLNIVNkKEKATGREVTHIQFTSWPDHGVPEDPHLLLKLRRRVNAFSNFFSGPIVVHCSAGVGRTG 865
Cdd:cd14601     80 TCHSEEGNPAYVFREMTLTN-LEKNESRPLTQIQYIAWPDHGVPDDSSDFLDFVCLVRNKRAGKDEPVVVHCSAGIGRTG 158

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|
gi 1622828204  866 TYIGIDAMLEGLEAENKVDVYGYVVKLRRQRCLMVQVEAQYILIHQALVE 915
Cdd:cd14601    159 VLITMETAMCLIECNQPVYPLDIVRTMRDQRAMMIQTPSQYRFVCEAILK 208
PTPc-N21 cd14598
catalytic domain of tyrosine-protein phosphatase non-receptor type 21; Tyrosine-protein ...
 711-916 2.72e-43

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: 157.44  E-value: 2.72e-43
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622828204  711 YINASYID---GFKEpRKYIAAQGPRDETVDDFWRMIWEQKATVIVMVTRCEEGNRNKCAEYWPSM--EEGTRAFGDVVV 785
Cdd:cd14598      1 YINASHIKvtvGGKE-WDYIATQGPLQNTCQDFWQMVWEQGVAIIAMVTAEEEGGREKSFRYWPRLgsRHNTVTYGRFKI 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622828204  786 KINQHKRCPDYIIQKLNIvnkKEKATGREVT--HIQFTSWPDHGVPEDPHLLL-------KLRRRVNAFSNFFSG--PIV 854
Cdd:cd14598     80 TTRFRTDSGCYATTGLKI---KHLLTGQERTvwHLQYTDWPEHGCPEDLKGFLsyleeiqSVRRHTNSTIDPKSPnpPVL 156

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1622828204  855 VHCSAGVGRTGTYIGIDAMLEGLEAENKVDVYGYVVKLRRQRCLMVQVEAQYILIHQALVEY 916
Cdd:cd14598    157 VHCSAGVGRTGVVILSEIMIACLEHNEMLDIPRVLDMLRQQRMMMVQTLSQYTFVYKVLIQF 218
PHA02738 PHA02738
hypothetical protein; Provisional
 681-924 3.66e-43

hypothetical protein; Provisional


Pssm-ID: 222923 [Multi-domain]  Cd Length: 320  Bit Score: 160.48  E-value: 3.66e-43
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622828204  681 NQNKNRYVDILPYDYNRVEL-SEINGdagSNYINASYIDGFKEPRKYIAAQGPRDETVDDFWRMIWEQKATVIVMVTRCE 759
Cdd:PHA02738    49 NRKLNRYLDAVCFDHSRVILpAERNR---GDYINANYVDGFEYKKKFICGQAPTRQTCYDFYRMLWMEHVQIIVMLCKKK 125

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622828204  760 EGNRNKCAEYWPSMEEGTRAFGDVVVKINQHKRCPDYIIQKLNIVNKKEkATgREVTHIQFTSWPDHGVPEDPHLLLKLR 839
Cdd:PHA02738   126 ENGREKCFPYWSDVEQGSIRFGKFKITTTQVETHPHYVKSTLLLTDGTS-AT-QTVTHFNFTAWPDHDVPKNTSEFLNFV 203

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622828204  840 RRV---------NAFSN----FFSGPIVVHCSAGVGRTGTYIGIDAMLEGLEAENKVDVYGYVVKLRRQRCLMVQVEAQY 906
Cdd:PHA02738   204 LEVrqcqkelaqESLQIghnrLQPPPIVVHCNAGLGRTPCYCVVDISISRFDACATVSIPSIVSSIRNQRYYSLFIPFQY 283

                          250
                   ....*....|....*...
gi 1622828204  907 ILIHQALVEYNQFGETEV 924
Cdd:PHA02738   284 FFCYRAVKRYVNLTVNKV 301
R-PTPc-typeIIb-1 cd14555
catalytic domain of type IIb (or R2B) subfamily receptor-type tyrosine-protein phosphatases, ...
 1021-1229 3.76e-43

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: 156.23  E-value: 3.76e-43
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622828204 1021 YINASFIMSYWKPEVMIAAQGPLKETIGDFWQMIFQRKVKVIVMLTELKHGDQEICAQYWGEGKQTYGDIEVDMKDTNKS 1100
Cdd:cd14555      1 YINANYIDGYHRPNHYIATQGPMQETVYDFWRMVWQENSASIVMVTNLVEVGRVKCSRYWPDDTEVYGDIKVTLVETEPL 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622828204 1101 STYTLRVFELRHSKRKDSRTVYQYQYTNWSVEQLPAEPKELVSLIQVLKEKLPQknssegnkhhKSTPLLIHCRDGSQQT 1180
Cdd:cd14555     81 AEYVVRTFALERRGYHEIREVRQFHFTGWPDHGVPYHATGLLGFIRRVKASNPP----------SAGPIVVHCSAGAGRT 150

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*....
gi 1622828204 1181 GIFCALLNLLESAETEEVVDIFQVVKALRKARPGMVSTFEQYQFLYDII 1229
Cdd:cd14555    151 GCYIVIDIMLDMAEREGVVDIYNCVKELRSRRVNMVQTEEQYIFIHDAI 199
R-PTPc-S-1 cd14625
catalytic domain of receptor-type tyrosine-protein phosphatase S, repeat 1; Receptor-type ...
 924-1229 6.71e-43

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: 158.33  E-value: 6.71e-43
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622828204  924 VNLSELHPYLHNMKKRDPPSepspLEAEFQRLPSYRSWRTQHiGNQEENKNKNRNSNVIPYDYNRVPLKhelemskesdh 1003
Cdd:cd14625      4 IPISELAEHTERLKANDNLK----LSQEYESIDPGQQFTWEH-SNLEVNKPKNRYANVIAYDHSRVILQ----------- 67

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622828204 1004 dsdessddDSDSEEPSKYINASFIMSYWKPEVMIAAQGPLKETIGDFWQMIFQRKVKVIVMLTELKHGDQEICAQYW-GE 1082
Cdd:cd14625     68 --------PIEGIMGSDYINANYIDGYRKQNAYIATQGPLPETFGDFWRMVWEQRSATVVMMTKLEEKSRIKCDQYWpSR 139

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622828204 1083 GKQTYGDIEVDMKDTNKSSTYTLRVFELRHSKRKDSRTVYQYQYTNWSVEQLPAEPKELVSLIQVLKEKLPQknssegnk 1162
Cdd:cd14625    140 GTETYGMIQVTLLDTIELATFCVRTFSLHKNGSSEKREVRQFQFTAWPDHGVPEYPTPFLAFLRRVKTCNPP-------- 211

                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1622828204 1163 hhKSTPLLIHCRDGSQQTGIFCALLNLLESAETEEVVDIFQVVKALRKARPGMVSTFEQYQFLYDII 1229
Cdd:cd14625    212 --DAGPIVVHCSAGVGRTGCFIVIDAMLERIKHEKTVDIYGHVTLMRSQRNYMVQTEDQYSFIHDAL 276
PHA02742 PHA02742
protein tyrosine phosphatase; Provisional
 671-916 1.04e-42

protein tyrosine phosphatase; Provisional


Pssm-ID: 165109 [Multi-domain]  Cd Length: 303  Bit Score: 158.63  E-value: 1.04e-42
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622828204  671 FPIKEARKPFNQNKNRYVDILPYDYNRVELSEINGdaGSNYINASYIDGFKEPRKYIAAQGPRDETVDDFWRMIWEQKAT 750
Cdd:PHA02742    42 FSCNESLELKNMKKCRYPDAPCFDRNRVILKIEDG--GDDFINASYVDGHNAKGRFICTQAPLEETALDFWQAIFQDQVR 119

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622828204  751 VIVMVTRCEEGNRNKCAEYWPSMEEGTRAFGDVVVKINQHKRCPDYIIQKLNIVNKKeKATGREVTHIQFTSWPDHGVPE 830
Cdd:PHA02742   120 VIVMITKIMEDGKEACYPYWMPHERGKATHGEFKIKTKKIKSFRNYAVTNLCLTDTN-TGASLDIKHFAYEDWPHGGLPR 198

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622828204  831 DP-----------HLLLKLRRRVNAFSNFFSGPIVVHCSAGVGRTGTYIGIDAMLEGLEAENKVDVYGYVVKLRRQRCLM 899
Cdd:PHA02742   199 DPnkfldfvlavrEADLKADVDIKGENIVKEPPILVHCSAGLDRAGAFCAIDICISKYNERAIIPLLSIVRDLRKQRHNC 278

                          250
                   ....*....|....*..
gi 1622828204  900 VQVEAQYILIHQALVEY 916
Cdd:PHA02742   279 LSLPQQYIFCYFIVLIF 295
PTPc-N12 cd14604
catalytic domain of tyrosine-protein phosphatase non-receptor type 12; Tyrosine-protein ...
 933-1236 1.53e-42

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: 157.79  E-value: 1.53e-42
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622828204  933 LHNMKKRDPPSEPSpLEAEFQRLPSYRS-WRTQHI-----GNQEENKNKNRNSNVIPYDYNRVPLKHELEmskesdhdsd 1006
Cdd:cd14604     13 VQAMKSTDHNGEDN-FASDFMRLRRLSTkYRTEKIyptatGEKEENVKKNRYKDILPFDHSRVKLTLKTS---------- 81

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622828204 1007 essdddsdsEEPSKYINASFIMSYWKPEVMIAAQGPLKETIGDFWQMIFQRKVKVIVMLT-ELKHGDQEiCAQYW---GE 1082
Cdd:cd14604     82 ---------SQDSDYINANFIKGVYGPKAYIATQGPLANTVIDFWRMIWEYNVAIIVMACrEFEMGRKK-CERYWplyGE 151

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622828204 1083 GKQTYGDIEVDMKDTNKSSTYTLRVFELRHskRKDSRTVYQYQYTNWSVEQLPAEPKELVSLIQVLKEklpqknssegNK 1162
Cdd:cd14604    152 EPMTFGPFRISCEAEQARTDYFIRTLLLEF--QNETRRLYQFHYVNWPDHDVPSSFDSILDMISLMRK----------YQ 219

                          250       260       270       280       290       300       310
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1622828204 1163 HHKSTPLLIHCRDGSQQTGIFCAL---LNLLESAETEEVVDIFQVVKALRKARPGMVSTFEQYQFLYDIIASTYPAQ 1236
Cdd:cd14604    220 EHEDVPICIHCSAGCGRTGAICAIdytWNLLKAGKIPEEFNVFNLIQEMRTQRHSAVQTKEQYELVHRAIAQLFEKQ 296
R-PTPc-G-1 cd17667
catalytic domain of receptor-type tyrosine-protein phosphatase G, repeat 1; Receptor-type ...
 951-1227 1.55e-42

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: 157.12  E-value: 1.55e-42
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622828204  951 EFQRLPSYRSWRTQHiGNQEENKNKNRNSNVIPYDYNRVPLKhelemskesdhdsdessDDDSDSEEPSKYINASFIMSY 1030
Cdd:cd17667      7 EVQRCTADMNITAEH-SNHPDNKHKNRYINILAYDHSRVKLR-----------------PLPGKDSKHSDYINANYVDGY 68

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622828204 1031 WKPEVMIAAQGPLKETIGDFWQMIFQRKVKVIVMLTELKHGDQEICAQYW-GEGKQTYGDIEVDMKDTNKSSTYTLRVFE 1109
Cdd:cd17667     69 NKAKAYIATQGPLKSTFEDFWRMIWEQNTGIIVMITNLVEKGRRKCDQYWpTENSEEYGNIIVTLKSTKIHACYTVRRFS 148

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622828204 1110 LRHSK-----------RKDSRTVYQYQYTNWSVEQLPAEPKELVSLIQvlkeklpqknSSEGNKHHKSTPLLIHCRDGSQ 1178
Cdd:cd17667    149 IRNTKvkkgqkgnpkgRQNERTVIQYHYTQWPDMGVPEYALPVLTFVR----------RSSAARTPEMGPVLVHCSAGVG 218

                          250       260       270       280
                   ....*....|....*....|....*....|....*....|....*....
gi 1622828204 1179 QTGIFCALLNLLESAETEEVVDIFQVVKALRKARPGMVSTFEQYQFLYD 1227
Cdd:cd17667    219 RTGTYIVIDSMLQQIKDKSTVNVLGFLKHIRTQRNYLVQTEEQYIFIHD 267
R-PTP-N-N2 cd14546
PTP-like domain of receptor-type tyrosine-protein phosphatase-like N and N2; Receptor-type ...
 1021-1230 2.88e-41

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: 151.06  E-value: 2.88e-41
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622828204 1021 YINASFIMSYwKPE--VMIAAQGPLKETIGDFWQMIFQRKVKVIVMLTELKHGDQEICAQYW-GEGKQTYGDIEVDM-KD 1096
Cdd:cd14546      1 YINASTIYDH-DPRnpAYIATQGPLPHTIADFWQMIWEQGCVVIVMLTRLQENGVKQCARYWpEEGSEVYHIYEVHLvSE 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622828204 1097 TNKSSTYTLRVFELRHSKRKDSRTVYQYQYTNWSVEQLPAEPKELVSliqvLKEKLpqknssegNK--HHKSTPLLIHCR 1174
Cdd:cd14546     80 HIWCDDYLVRSFYLKNLQTSETRTVTQFHFLSWPDEGIPASAKPLLE----FRRKV--------NKsyRGRSCPIVVHCS 147

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 1622828204 1175 DGSQQTGIFCAL---LNLLESAETEevVDIFQVVKALRKARPGMVSTFEQYQFLYDIIA 1230
Cdd:cd14546    148 DGAGRTGTYILIdmvLNRMAKGAKE--IDIAATLEHLRDQRPGMVKTKDQFEFVLTAVA 204
R-PTPc-M-1 cd14633
catalytic domain of receptor-type tyrosine-protein phosphatase M, repeat 1; Receptor-type ...
 969-1229 3.33e-41

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: 153.27  E-value: 3.33e-41
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622828204  969 QEENKNKNRNSNVIPYDYNRVPLKhelemskesdhdsdessddDSDSEEPSKYINASFIMSYWKPEVMIAAQGPLKETIG 1048
Cdd:cd14633     37 KDENRMKNRYGNIIAYDHSRVRLQ-------------------PIEGETSSDYINGNYIDGYHRPNHYIATQGPMQETIY 97

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622828204 1049 DFWQMIFQRKVKVIVMLTELKHGDQEICAQYWGEGKQTYGDIEVDMKDTNKSSTYTLRVFELRHSKRKDSRTVYQYQYTN 1128
Cdd:cd14633     98 DFWRMVWHENTASIIMVTNLVEVGRVKCCKYWPDDTEIYKDIKVTLIETELLAEYVIRTFAVEKRGVHEIREIRQFHFTG 177

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622828204 1129 WSVEQLPAEPKELVSLIQVLKEKLPQknssegnkhhKSTPLLIHCRDGSQQTGIFCALLNLLESAETEEVVDIFQVVKAL 1208
Cdd:cd14633    178 WPDHGVPYHATGLLGFVRQVKSKSPP----------NAGPLVVHCSAGAGRTGCFIVIDIMLDMAEREGVVDIYNCVREL 247

                          250       260
                   ....*....|....*....|.
gi 1622828204 1209 RKARPGMVSTFEQYQFLYDII 1229
Cdd:cd14633    248 RSRRVNMVQTEEQYVFIHDAI 268
R-PTPc-A-1 cd14621
catalytic domain of receptor-type tyrosine-protein phosphatase A, repeat 1; Receptor-type ...
 951-1233 5.02e-41

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: 153.64  E-value: 5.02e-41
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622828204  951 EFQRLPSYRSWRTQHIGNQEENKNKNRNSNVIPYDYNRVPLkhelemskesdhdsdessdDDSDSEEPSKYINASFIMSY 1030
Cdd:cd14621     31 EFNALPACPIQATCEAASKEENKEKNRYVNILPYDHSRVHL-------------------TPVEGVPDSDYINASFINGY 91

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622828204 1031 WKPEVMIAAQGPLKETIGDFWQMIFQRKVKVIVMLTELKHGDQEICAQYW-GEGKQTYGDIEVDMKDTNKSSTYTLRVFE 1109
Cdd:cd14621     92 QEKNKFIAAQGPKEETVNDFWRMIWEQNTATIVMVTNLKERKECKCAQYWpDQGCWTYGNIRVSVEDVTVLVDYTVRKFC 171

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622828204 1110 LRH----SKRKDSRTVYQYQYTNWSVEQLPAEPKELVSLIQVLKEKLPQknssegnkhhKSTPLLIHCRDGSQQTGIFCA 1185
Cdd:cd14621    172 IQQvgdvTNKKPQRLITQFHFTSWPDFGVPFTPIGMLKFLKKVKNCNPQ----------YAGAIVVHCSAGVGRTGTFIV 241

                          250       260       270       280
                   ....*....|....*....|....*....|....*....|....*...
gi 1622828204 1186 LLNLLESAETEEVVDIFQVVKALRKARPGMVSTFEQYQFLYDIIASTY 1233
Cdd:cd14621    242 IDAMLDMMHAERKVDVYGFVSRIRAQRCQMVQTDMQYVFIYQALLEHY 289
R-PTPc-Z-1 cd17668
catalytic domain of receptor-type tyrosine-protein phosphatase Z, repeat 1; Receptor-type ...
 1021-1227 6.22e-41

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: 150.13  E-value: 6.22e-41
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622828204 1021 YINASFIMSYWKPEVMIAAQGPLKETIGDFWQMIFQRKVKVIVMLTELKHGDQEICAQYW-GEGKQTYGDIEVDMKDTNK 1099
Cdd:cd17668      1 YINANYVDGYNKPKAYIAAQGPLKSTAEDFWRMIWEHNVEVIVMITNLVEKGRRKCDQYWpADGSEEYGNFLVTQKSVQV 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622828204 1100 SSTYTLRVFELRHSK--------RKDSRTVYQYQYTNWSVEQLPAEPKELVSLIQvlkeklpqknSSEGNKHHKSTPLLI 1171
Cdd:cd17668     81 LAYYTVRNFTLRNTKikkgsqkgRPSGRVVTQYHYTQWPDMGVPEYTLPVLTFVR----------KASYAKRHAVGPVVV 150

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 1622828204 1172 HCRDGSQQTGIFCALLNLLESAETEEVVDIFQVVKALRKARPGMVSTFEQYQFLYD 1227
Cdd:cd17668    151 HCSAGVGRTGTYIVLDSMLQQIQHEGTVNIFGFLKHIRSQRNYLVQTEEQYVFIHD 206
R-PTPc-A-E-1 cd14551
catalytic domain of receptor-type tyrosine-protein phosphatase A and E, repeat 1; ...
 1021-1226 1.02e-40

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: 149.29  E-value: 1.02e-40
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622828204 1021 YINASFIMSYWKPEVMIAAQGPLKETIGDFWQMIFQRKVKVIVMLTELKHGDQEICAQYW-GEGKQTYGDIEVDMKDTNK 1099
Cdd:cd14551      1 YINASYIDGYQEKNKFIAAQGPKDETVNDFWRMIWEQGSATIVMVTNLKERKEKKCSQYWpDQGCWTYGNLRVRVEDTVV 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622828204 1100 SSTYTLRVFELRH----SKRKDSRTVYQYQYTNWSVEQLPAEPKELVSLIQVLKEKLPQKNSsegnkhhkstPLLIHCRD 1175
Cdd:cd14551     81 LVDYTTRKFCIQKvnrgIGEKRVRLVTQFHFTSWPDFGVPFTPIGMLKFLKKVKSANPPRAG----------PIVVHCSA 150

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|.
gi 1622828204 1176 GSQQTGIFCALLNLLESAETEEVVDIFQVVKALRKARPGMVSTFEQYQFLY 1226
Cdd:cd14551    151 GVGRTGTFIVIDAMLDMMHAEGKVDVFGFVSRIRQQRSQMVQTDMQYVFIY 201
R-PTPc-O cd14614
catalytic domain of receptor-type tyrosine-protein phosphatase O; Receptor-type ...
 972-1226 1.12e-40

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: 150.81  E-value: 1.12e-40
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622828204  972 NKNKNRNSNVIPYDYNRVPL--KHELEMSKesdhdsdessdddsdseepskYINASFIMSYWKPEVMIAAQGPLKETIGD 1049
Cdd:cd14614     12 NRCKNRYTNILPYDFSRVKLvsMHEEEGSD---------------------YINANYIPGYNSPQEYIATQGPLPETRND 70

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622828204 1050 FWQMIFQRKVKVIVMLTELKHGDQEICAQYW--GEGKQTYGDIEVDMKDTNKSSTYTLRVFELRHSkrKDSRTVYQYQYT 1127
Cdd:cd14614     71 FWKMVLQQKSQIIVMLTQCNEKRRVKCDHYWpfTEEPVAYGDITVEMLSEEEQPDWAIREFRVSYA--DEVQDVMHFNYT 148

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622828204 1128 NWSVEQLPA--EPKELVSLIQVLKEklpQKNSSEGnkhhkstPLLIHCRDGSQQTGIFCALLNLLESAETEEVVDIFQVV 1205
Cdd:cd14614    149 AWPDHGVPTanAAESILQFVQMVRQ---QAVKSKG-------PMIIHCSAGVGRTGTFIALDRLLQHIRDHEFVDILGLV 218

                          250       260
                   ....*....|....*....|.
gi 1622828204 1206 KALRKARPGMVSTFEQYQFLY 1226
Cdd:cd14614    219 SEMRSYRMSMVQTEEQYIFIH 239
R-PTP-N2 cd14610
PTP-like domain of receptor-type tyrosine-protein phosphatase N2; Receptor-type ...
 926-1230 1.20e-40

PTP-like domain of receptor-type tyrosine-protein phosphatase N2; Receptor-type tyrosine-protein phosphatase N2 (PTPRN2 or R-PTP-N2), also called islet cell autoantigen-related protein (IAR), ICAAR, phogrin, or IA-2beta, belongs to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). It consists of a large ectodomain that contains a RESP18HD (regulated endocrine-specific protein 18 homology domain), followed by a transmembrane segment, and a single, catalytically-impaired, PTP domain. It is mainly expressed in neuropeptidergic neurons and peptide-secreting endocrine cells, including insulin-producing pancreatic beta-cells. It may function as a phosphatidylinositol phosphatase to regulate insulin secretion. It is also required for normal accumulation of the neurotransmitters norepinephrine, dopamine and serotonin in the brain.


Pssm-ID: 350458 [Multi-domain]  Cd Length: 283  Bit Score: 152.13  E-value: 1.20e-40
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622828204  926 LSELHPYLHNmKKRdppsepspLEAEFQRLPSYRSW-RTQHIGNQEENKNKNRNSNVIPYDYNRVPLKHELEMSKEsdhd 1004
Cdd:cd14610      6 LSYMEDHLKN-KNR--------LEKEWEALCAYQAEpNATNVAQREENVQKNRSLAVLPYDHSRIILKAENSHSHS---- 72

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622828204 1005 sdessdddsdseepsKYINASFIMSYwKPE--VMIAAQGPLKETIGDFWQMIFQRKVKVIVMLTELKHGDQEICAQYW-G 1081
Cdd:cd14610     73 ---------------DYINASPIMDH-DPRnpAYIATQGPLPATVADFWQMVWESGCVVIVMLTPLAENGVKQCYHYWpD 136

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622828204 1082 EGKQTYGDIEVDMKDTNK-SSTYTLRVFELRHSKRKDSRTVYQYQYTNWSVEQLPAEPKELVSliqvLKEKLpqknsseg 1160
Cdd:cd14610    137 EGSNLYHIYEVNLVSEHIwCEDFLVRSFYLKNLQTNETRTVTQFHFLSWNDQGVPASTRSLLD----FRRKV-------- 204

                          250       260       270       280       290       300       310
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1622828204 1161 NKHH--KSTPLLIHCRDGSQQTGIFCAL-LNLLESAETEEVVDIFQVVKALRKARPGMVSTFEQYQFLYDIIA 1230
Cdd:cd14610    205 NKCYrgRSCPIIVHCSDGAGRSGTYILIdMVLNKMAKGAKEIDIAATLEHLRDQRPGMVQTKEQFEFALTAVA 277
R-PTPc-C-1 cd14557
catalytic domain of receptor-type tyrosine-protein phosphatase C, repeat 1; Receptor-type ...
 1021-1226 1.27e-40

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: 148.82  E-value: 1.27e-40
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622828204 1021 YINASFIMSYWKPEVMIAAQGPLKETIGDFWQMIFQRKVKVIVMLTELKHGDQEICAQYW---GEGKQTYGDIEVDMKDT 1097
Cdd:cd14557      1 YINASYIDGFKEPRKYIAAQGPKDETVDDFWRMIWEQKSTVIVMVTRCEEGNRNKCAQYWpsmEEGSRAFGDVVVKINEE 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622828204 1098 NKSSTYTLRVFELRHSKRKDS-RTVYQYQYTNWSVEQLPAEPKELVsliqvlkeKLPQKNSSEGNKHhkSTPLLIHCRDG 1176
Cdd:cd14557     81 KICPDYIIRKLNINNKKEKGSgREVTHIQFTSWPDHGVPEDPHLLL--------KLRRRVNAFNNFF--SGPIVVHCSAG 150

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|
gi 1622828204 1177 SQQTGIFCALLNLLESAETEEVVDIFQVVKALRKARPGMVSTFEQYQFLY 1226
Cdd:cd14557    151 VGRTGTYIGIDAMLEGLEAEGRVDVYGYVVKLRRQRCLMVQVEAQYILIH 200
R-PTPc-D-1 cd14624
catalytic domain of receptor-type tyrosine-protein phosphatase D, repeat 1; Receptor-type ...
 951-1229 2.00e-40

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: 151.42  E-value: 2.00e-40
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622828204  951 EFQRLPSYRSWRTQHiGNQEENKNKNRNSNVIPYDYNRVPLKhelemskesdhdsdessddDSDSEEPSKYINASFIMSY 1030
Cdd:cd14624     27 EYESIDPGQQFTWEH-SNLEVNKPKNRYANVIAYDHSRVLLS-------------------AIEGIPGSDYINANYIDGY 86

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622828204 1031 WKPEVMIAAQGPLKETIGDFWQMIFQRKVKVIVMLTELKHGDQEICAQYW-GEGKQTYGDIEVDMKDTNKSSTYTLRVFE 1109
Cdd:cd14624     87 RKQNAYIATQGALPETFGDFWRMIWEQRSATVVMMTKLEERSRVKCDQYWpSRGTETYGLIQVTLLDTVELATYCVRTFA 166

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622828204 1110 LRHSKRKDSRTVYQYQYTNWSVEQLPAEPKELVSLIQVLKEKLPQknssegnkhhKSTPLLIHCRDGSQQTGIFCALLNL 1189
Cdd:cd14624    167 LYKNGSSEKREVRQFQFTAWPDHGVPEHPTPFLAFLRRVKTCNPP----------DAGPMVVHCSAGVGRTGCFIVIDAM 236

                          250       260       270       280
                   ....*....|....*....|....*....|....*....|
gi 1622828204 1190 LESAETEEVVDIFQVVKALRKARPGMVSTFEQYQFLYDII 1229
Cdd:cd14624    237 LERIKHEKTVDIYGHVTLMRAQRNYMVQTEDQYIFIHDAL 276
R-PTPc-U-1 cd14632
catalytic domain of receptor-type tyrosine-protein phosphatase U, repeat 1; Receptor-type ...
 1021-1229 4.06e-40

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: 147.51  E-value: 4.06e-40
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622828204 1021 YINASFIMSYWKPEVMIAAQGPLKETIGDFWQMIFQRKVKVIVMLTELKHGDQEICAQYWGEGKQTYGDIEVDMKDTNKS 1100
Cdd:cd14632      1 YINANYIDGYHRSNHFIATQGPKQEMVYDFWRMVWQEHCSSIVMITKLVEVGRVKCSKYWPDDSDTYGDIKITLLKTETL 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622828204 1101 STYTLRVFELRHSKRKDSRTVYQYQYTNWSVEQLPAEPKELVSLIQVLKEKLPQknssegnkhhKSTPLLIHCRDGSQQT 1180
Cdd:cd14632     81 AEYSVRTFALERRGYSARHEVKQFHFTSWPEHGVPYHATGLLAFIRRVKASTPP----------DAGPVVVHCSAGAGRT 150

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*....
gi 1622828204 1181 GIFCALLNLLESAETEEVVDIFQVVKALRKARPGMVSTFEQYQFLYDII 1229
Cdd:cd14632    151 GCYIVLDVMLDMAECEGVVDIYNCVKTLCSRRINMIQTEEQYIFIHDAI 199
R-PTPc-typeIIb-2 cd14556
PTP domain of type IIb (or R2B) subfamily receptor-type tyrosine-protein phosphatases, repeat ...
 711-911 5.57e-40

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: 147.17  E-value: 5.57e-40
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622828204  711 YINASYIDGFKEPRKYIAAQGPRDETVDDFWRMIWEQKATVIVMVTRCEEGNRNkCAEYWPsmEEGTRAFGDVVVKINQH 790
Cdd:cd14556      1 YINAALLDSYKQPAAFIVTQHPLPNTVTDFWRLVYDYGCTSIVMLNQLDPKDQS-CPQYWP--DEGSGTYGPIQVEFVST 77

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622828204  791 KRCPDYIIQKLNIVNKKEKATG-REVTHIQFTSWPDHG-VPEDPHLLLKLRRRVNA-FSNFFSGPIVVHCSAGVGRTGTY 867
Cdd:cd14556     78 TIDEDVISRIFRLQNTTRPQEGyRMVQQFQFLGWPRDRdTPPSKRALLKLLSEVEKwQEQSGEGPIVVHCLNGVGRSGVF 157

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....
gi 1622828204  868 IGIDAMLEGLEAENKVDVYGYVVKLRRQRCLMVQVEAQYILIHQ 911
Cdd:cd14556    158 CAISSVCERIKVENVVDVFQAVKTLRNHRPNMVETEEQYKFCYD 201
PTPc-N22_18_12 cd14542
catalytic domain of tyrosine-protein phosphatase non-receptor type 22, type 18 and type 12; ...
 1021-1226 1.23e-39

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: 146.03  E-value: 1.23e-39
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622828204 1021 YINASFIMSYWKPEVMIAAQGPLKETIGDFWQMIFQRKVKVIVMLTELKHGDQEICAQYW---GEGKQTYGDIEVDM-KD 1096
Cdd:cd14542      1 YINANFIKGVSGSKAYIATQGPLPNTVLDFWRMIWEYNVQVIVMACREFEMGKKKCERYWpeeGEEQLQFGPFKISLeKE 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622828204 1097 TNKSSTYTLRVFELRHSkrKDSRTVYQYQYTNWSVEQLPAEPKELVSLIQVLKEKlpqknssegnKHHKSTPLLIHCRDG 1176
Cdd:cd14542     81 KRVGPDFLIRTLKVTFQ--KESRTVYQFHYTAWPDHGVPSSVDPILDLVRLVRDY----------QGSEDVPICVHCSAG 148

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|...
gi 1622828204 1177 SQQTGIFCAL---LNLLESAETEEVVDIFQVVKALRKARPGMVSTFEQYQFLY 1226
Cdd:cd14542    149 CGRTGTICAIdyvWNLLKTGKIPEEFSLFDLVREMRKQRPAMVQTKEQYELVY 201
R-PTPc-K-1 cd14631
catalytic domain of receptor-type tyrosine-protein phosphatase K, repeat 1; Receptor-type ...
 1021-1229 1.24e-39

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: 146.70  E-value: 1.24e-39
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622828204 1021 YINASFIMSYWKPEVMIAAQGPLKETIGDFWQMIFQRKVKVIVMLTELKHGDQEICAQYWGEGKQTYGDIEVDMKDTNKS 1100
Cdd:cd14631     15 YINANYIDGYQRPSHYIATQGPVHETVYDFWRMIWQEQSACIVMVTNLVEVGRVKCYKYWPDDTEVYGDFKVTCVEMEPL 94

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622828204 1101 STYTLRVFELRHSKRKDSRTVYQYQYTNWSVEQLPAEPKELVSLIQVLKEKLPQknssegnkhhKSTPLLIHCRDGSQQT 1180
Cdd:cd14631     95 AEYVVRTFTLERRGYNEIREVKQFHFTGWPDHGVPYHATGLLSFIRRVKLSNPP----------SAGPIVVHCSAGAGRT 164

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*....
gi 1622828204 1181 GIFCALLNLLESAETEEVVDIFQVVKALRKARPGMVSTFEQYQFLYDII 1229
Cdd:cd14631    165 GCYIVIDIMLDMAEREGVVDIYNCVKALRSRRINMVQTEEQYIFIHDAI 213
COG5599 COG5599
Protein tyrosine phosphatase [Signal transduction mechanisms];
684-909 1.31e-39

Protein tyrosine phosphatase [Signal transduction mechanisms];


Pssm-ID: 444335 [Multi-domain]  Cd Length: 282  Bit Score: 148.70  E-value: 1.31e-39
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622828204  684 KNRYVDILPYDYNRVElseINGdagsNYINASYIDGfKEPRKYIAAQGPRDETVDDFWRMIWEQKATVIVMVTRCEEG-- 761
Cdd:COG5599     45 LNRFRDIQPYKETALR---ANL----GYLNANYIQV-IGNHRYIATQYPLEEQLEDFFQMLFDNNTPVLVVLASDDEIsk 116

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622828204  762 NRNKCAEYWPsmEEGTRAFGDVVVKINQHKRCPDYIIQKLNIVNKKEKA-TGREVTHIQFTSWPDHGVP--EDPHLLLKL 838
Cdd:COG5599    117 PKVKMPVYFR--QDGEYGKYEVSSELTESIQLRDGIEARTYVLTIKGTGqKKIEIPVLHVKNWPDHGAIsaEALKNLADL 194

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1622828204  839 RRRVNAFSNFFSGPIVVHCSAGVGRTGTYIGIDAMLEGLEAEN--KVDVYGYVVKLRRQR-CLMVQVEAQYILI 909
Cdd:COG5599    195 IDKKEKIKDPDKLLPVVHCRAGVGRTGTLIACLALSKSINALVqiTLSVEEIVIDMRTSRnGGMVQTSEQLDVL 268
R-PTPc-E-1 cd14620
catalytic domain of receptor-type tyrosine-protein phosphatase E, repeat 1; Receptor-type ...
 980-1226 1.31e-39

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: 147.01  E-value: 1.31e-39
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622828204  980 NVIPYDYNRVPLKHelemskesdhdsdessdddSDSEEPSKYINASFIMSYWKPEVMIAAQGPLKETIGDFWQMIFQRKV 1059
Cdd:cd14620      3 NILPYDHSRVILSQ-------------------LDGIPCSDYINASYIDGYKEKNKFIAAQGPKQETVNDFWRMVWEQKS 63

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622828204 1060 KVIVMLTELKHGDQEICAQYWGE-GKQTYGDIEVDMKDTNKSSTYTLRVFELR---HSKRKDSRTVYQYQYTNWSVEQLP 1135
Cdd:cd14620     64 ATIVMLTNLKERKEEKCYQYWPDqGCWTYGNIRVAVEDCVVLVDYTIRKFCIQpqlPDGCKAPRLVTQLHFTSWPDFGVP 143

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622828204 1136 AEPkelVSLIQVLKeKLPQKNSSEGNkhhkstPLLIHCRDGSQQTGIFCALLNLLESAETEEVVDIFQVVKALRKARPGM 1215
Cdd:cd14620    144 FTP---IGMLKFLK-KVKSVNPVHAG------PIVVHCSAGVGRTGTFIVIDAMIDMMHAEQKVDVFEFVSRIRNQRPQM 213

                          250
                   ....*....|.
gi 1622828204 1216 VSTFEQYQFLY 1226
Cdd:cd14620    214 VQTDMQYSFIY 224
PTPc-N18 cd14603
catalytic domain of tyrosine-protein phosphatase non-receptor type 18; Tyrosine-protein ...
 963-1233 6.53e-39

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: 146.51  E-value: 6.53e-39
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622828204  963 TQHIGNQEENKNKNRNSNVIPYDYNRV---PLKHELEmskesdhdsdessdddsdseepSKYINASFIMSYWKPEVMIAA 1039
Cdd:cd14603     21 STVAGGRKENVKKNRYKDILPYDQTRVilsLLQEEGH----------------------SDYINANFIKGVDGSRAYIAT 78

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622828204 1040 QGPLKETIGDFWQMIFQRKVKVIVM-LTELKHGDQEiCAQYWGEGKQT--YGDIEV-DMKDTNKSSTYTLRVfeLRHSKR 1115
Cdd:cd14603     79 QGPLSHTVLDFWRMIWQYGVKVILMaCREIEMGKKK-CERYWAQEQEPlqTGPFTItLVKEKRLNEEVILRT--LKVTFQ 155

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622828204 1116 KDSRTVYQYQYTNWSVEQLPAEPKELVSLIQVLKEKlpQKNSSEgnkhhkstPLLIHCRDGSQQTGIFCAL---LNLLES 1192
Cdd:cd14603    156 KESRSVSHFQYMAWPDHGIPDSPDCMLAMIELARRL--QGSGPE--------PLCVHCSAGCGRTGVICTVdyvRQLLLT 225

                          250       260       270       280
                   ....*....|....*....|....*....|....*....|.
gi 1622828204 1193 AETEEVVDIFQVVKALRKARPGMVSTFEQYQFLYDIIASTY 1233
Cdd:cd14603    226 QRIPPDFSIFDVVLEMRKQRPAAVQTEEQYEFLYHTVAQMF 266
PTPc-N7 cd14612
catalytic domain of tyrosine-protein phosphatase non-receptor type 7; Tyrosine-protein ...
 975-1230 7.83e-39

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: 145.36  E-value: 7.83e-39
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622828204  975 KNRNSNVIPYDYNRVPLKHElemskesdhdsdessdddSDSEEPSKYINASFIMSY-WKPEVMIAAQGPLKETIGDFWQM 1053
Cdd:cd14612     18 KDRYKTILPNPQSRVCLRRA------------------GSQEEEGSYINANYIRGYdGKEKAYIATQGPMLNTVSDFWEM 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622828204 1054 IFQRKVKVIVMLTELKHGdQEICAQYWGEGKQTYGDIEVDMKDTNKSSTYTLRVFELRHSkrKDSRTVYQYQYTNWSVEQ 1133
Cdd:cd14612     80 VWQEECPIIVMITKLKEK-KEKCVHYWPEKEGTYGRFEIRVQDMKECDGYTIRDLTIQLE--EESRSVKHYWFSSWPDHQ 156

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622828204 1134 LPAEPKELVSLIQVLKEKlPQKNSSEGnkhhkstPLLIHCRDGSQQTGIFCALLNLLESAETEEVVDIFQVVKALRKARP 1213
Cdd:cd14612    157 TPESAGPLLRLVAEVEES-RQTAASPG-------PIVVHCSAGIGRTGCFIATSIGCQQLKDTGKVDILGIVCQLRLDRG 228

                          250
                   ....*....|....*..
gi 1622828204 1214 GMVSTFEQYQFLYDIIA 1230
Cdd:cd14612    229 GMIQTSEQYQFLHHTLA 245
R-PTPc-Q cd14616
catalytic domain of receptor-type tyrosine-protein phosphatase Q; Receptor-type ...
 976-1226 9.42e-39

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: 144.28  E-value: 9.42e-39
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622828204  976 NRNSNVIPYDYNRVPLKHElemskesdhdsdessdddsDSEEPSKYINASFIMSYWKPEVMIAAQGPLKETIGDFWQMIF 1055
Cdd:cd14616      1 NRFPNIKPYNNNRVKLIAD-------------------AGVPGSDYINASYISGYLCPNEFIATQGPLPGTVGDFWRMVW 61

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622828204 1056 QRKVKVIVMLTELKHGDQEICAQYWGEGKQ---TYGDIEVDMKDTNKSSTYTLRvfELRHSKRKDSRTVYQYQYTNWSVE 1132
Cdd:cd14616     62 ETRAKTIVMLTQCFEKGRIRCHQYWPEDNKpvtVFGDIVITKLMEDVQIDWTIR--DLKIERHGDYMMVRQCNFTSWPEH 139

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622828204 1133 QLPAEPKELVSLIQVLKeklpqknsseGNKHHKSTPLLIHCRDGSQQTGIFCALLNLLESAETEEVVDIFQVVKALRKAR 1212
Cdd:cd14616    140 GVPESSAPLIHFVKLVR----------ASRAHDNTPMIVHCSAGVGRTGVFIALDHLTQHINDHDFVDIYGLVAELRSER 209

                          250
                   ....*....|....
gi 1622828204 1213 PGMVSTFEQYQFLY 1226
Cdd:cd14616    210 MCMVQNLAQYIFLH 223
PTPc-N13 cd14597
catalytic domain of tyrosine-protein phosphatase non-receptor type 13; Tyrosine-protein ...
 970-1229 1.87e-38

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: 143.82  E-value: 1.87e-38
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622828204  970 EENKNKNRNSNVIPYDYNRVPLKHElemskesdhdsdessdddsdseepSKYINASFI-MSYWKPE-VMIAAQGPLKETI 1047
Cdd:cd14597      1 KENRKKNRYKNILPYDTTRVPLGDE------------------------GGYINASFIkMPVGDEEfVYIACQGPLPTTV 56

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622828204 1048 GDFWQMIFQRKVKVIVMLTELKHGDQEICAQYWGE--GKQTYGD--IEVDMKDTNKSSTYTLRVFELRHSKRKDSRTVYQ 1123
Cdd:cd14597     57 ADFWQMVWEQKSTVIAMMTQEVEGGKIKCQRYWPEilGKTTMVDnrLQLTLVRMQQLKNFVIRVLELEDIQTREVRHITH 136

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622828204 1124 YQYTNWSVEQLPAEPKELVSLIQVLkeklpqknssegnKH-HKSTPLLIHCRDGSQQTGIFCALLNLLESAETEEVVDIF 1202
Cdd:cd14597    137 LNFTAWPDHDTPSQPEQLLTFISYM-------------RHiHKSGPIITHCSAGIGRSGTLICIDVVLGLISKDLDFDIS 203

                          250       260
                   ....*....|....*....|....*..
gi 1622828204 1203 QVVKALRKARPGMVSTFEQYQFLYDII 1229
Cdd:cd14597    204 DIVRTMRLQRHGMVQTEDQYIFCYQVI 230
PTPc_motif smart00404
Protein tyrosine phosphatase, catalytic domain motif;
814-915 8.17e-38

Protein tyrosine phosphatase, catalytic domain motif;


Pssm-ID: 214649 [Multi-domain]  Cd Length: 105  Bit Score: 137.10  E-value: 8.17e-38
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622828204   814 EVTHIQFTSWPDHGVPEDPHLLLKLRRRVNAFSNF--FSGPIVVHCSAGVGRTGTYIGIDAMLEGLEAE-NKVDVYGYVV 890
Cdd:smart00404    1 TVKHYHYTGWPDHGVPESPDSILELLRAVKKNLNQseSSGPVVVHCSAGVGRTGTFVAIDILLQQLEAEaGEVDIFDTVK 80

                            90       100
                    ....*....|....*....|....*
gi 1622828204   891 KLRRQRCLMVQVEAQYILIHQALVE 915
Cdd:smart00404   81 ELRSQRPGMVQTEEQYLFLYRALLE 105
PTPc_DSPc smart00012
Protein tyrosine phosphatase, catalytic domain, undefined specificity; Protein tyrosine ...
 814-915 8.17e-38

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: 137.10  E-value: 8.17e-38
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622828204   814 EVTHIQFTSWPDHGVPEDPHLLLKLRRRVNAFSNF--FSGPIVVHCSAGVGRTGTYIGIDAMLEGLEAE-NKVDVYGYVV 890
Cdd:smart00012    1 TVKHYHYTGWPDHGVPESPDSILELLRAVKKNLNQseSSGPVVVHCSAGVGRTGTFVAIDILLQQLEAEaGEVDIFDTVK 80

                            90       100
                    ....*....|....*....|....*
gi 1622828204   891 KLRRQRCLMVQVEAQYILIHQALVE 915
Cdd:smart00012   81 ELRSQRPGMVQTEEQYLFLYRALLE 105
PTPc-N5 cd14613
catalytic domain of tyrosine-protein phosphatase non-receptor type 5; Tyrosine-protein ...
 975-1230 1.06e-37

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: 142.69  E-value: 1.06e-37
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622828204  975 KNRNSNVIPYDYNRVPLKHELEmskesdhdsdessdddsdSEEPSKYINASFIMSYWKPE-VMIAAQGPLKETIGDFWQM 1053
Cdd:cd14613     28 KNRYKTILPNPHSRVCLTSPDQ------------------DDPLSSYINANYIRGYGGEEkVYIATQGPTVNTVGDFWRM 89

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622828204 1054 IFQRKVKVIVMLTELKHGDqEICAQYWGEGKQTYGDIEVDMKDTNKSSTYTLRVFELRhsKRKDSRTVYQYQYTNWSVEQ 1133
Cdd:cd14613     90 VWQERSPIIVMITNIEEMN-EKCTEYWPEEQVTYEGIEITVKQVIHADDYRLRLITLK--SGGEERGLKHYWYTSWPDQK 166

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622828204 1134 LPAEPKELVSLIQVLKEKLPQKNSSEGnkhhkstPLLIHCRDGSQQTGIFCALLNLLESAETEEVVDIFQVVKALRKARP 1213
Cdd:cd14613    167 TPDNAPPLLQLVQEVEEARQQAEPNCG-------PVIVHCSAGIGRTGCFIATSICCKQLRNEGVVDILRTTCQLRLDRG 239

                          250
                   ....*....|....*..
gi 1622828204 1214 GMVSTFEQYQFLYDIIA 1230
Cdd:cd14613    240 GMIQTCEQYQFVHHVLS 256
R-PTP-N cd14609
PTP-like domain of receptor-type tyrosine-protein phosphatase N; Receptor-type ...
 948-1230 1.13e-37

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: 143.25  E-value: 1.13e-37
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622828204  948 LEAEFQRLPSYRSW-RTQHIGNQEENKNKNRNSNVIPYDYNRVPLKHELEMSKEsdhdsdessdddsdseepsKYINASF 1026
Cdd:cd14609     17 LAKEWQALCAYQAEpNTCSTAQGEANVKKNRNPDFVPYDHARIKLKAESNPSRS-------------------DYINASP 77

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622828204 1027 IMSYwKPEV--MIAAQGPLKETIGDFWQMIFQRKVKVIVMLTELKHGDQEICAQYW-GEGKQTYGDIEVDMKDTNK-SST 1102
Cdd:cd14609     78 IIEH-DPRMpaYIATQGPLSHTIADFWQMVWENGCTVIVMLTPLVEDGVKQCDRYWpDEGSSLYHIYEVNLVSEHIwCED 156

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622828204 1103 YTLRVFELRHSKRKDSRTVYQYQYTNWSVEQLPAEPKELVSliqvLKEKLpqknssegNKHH--KSTPLLIHCRDGSQQT 1180
Cdd:cd14609    157 FLVRSFYLKNVQTQETRTLTQFHFLSWPAEGIPSSTRPLLD----FRRKV--------NKCYrgRSCPIIVHCSDGAGRT 224

                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|...
gi 1622828204 1181 GIFCAL---LNLLESAETEevVDIFQVVKALRKARPGMVSTFEQYQFLYDIIA 1230
Cdd:cd14609    225 GTYILIdmvLNRMAKGVKE--IDIAATLEHVRDQRPGMVRTKDQFEFALTAVA 275
PTPc-N22 cd14602
catalytic domain of tyrosine-protein phosphatase non-receptor type 22; Tyrosine-protein ...
 975-1229 3.11e-37

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: 140.36  E-value: 3.11e-37
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622828204  975 KNRNSNVIPYDYNRVPLkhelemskesdhdsdessdDDSDSEEPSKYINASFIMSYWKPEVMIAAQGPLKETIGDFWQMI 1054
Cdd:cd14602      1 KNRYKDILPYDHSRVEL-------------------SLITSDEDSDYINANFIKGVYGPRAYIATQGPLSTTLLDFWRMI 61

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622828204 1055 FQRKVKVIVM-LTELKHGDQEiCAQYW---GEGKQTYGDIEVDMKDTNKSSTYTLRVfeLRHSKRKDSRTVYQYQYTNWS 1130
Cdd:cd14602     62 WEYSVLIIVMaCMEFEMGKKK-CERYWaepGEMQLEFGPFSVTCEAEKRKSDYIIRT--LKVKFNSETRTIYQFHYKNWP 138

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622828204 1131 VEQLPAEPKELVSLIQVLKEKlpqknssegnKHHKSTPLLIHCRDGSQQTGIFCAL---LNLLESAETEEVVDIFQVVKA 1207
Cdd:cd14602    139 DHDVPSSIDPILELIWDVRCY----------QEDDSVPICIHCSAGCGRTGVICAIdytWMLLKDGIIPENFSVFSLIQE 208

                          250       260
                   ....*....|....*....|..
gi 1622828204 1208 LRKARPGMVSTFEQYQFLYDII 1229
Cdd:cd14602    209 MRTQRPSLVQTKEQYELVYNAV 230
PTPc-N11_6 cd14544
catalytic domain of tyrosine-protein phosphatase non-receptor type 11 and type 6; ...
 972-1226 4.23e-37

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: 140.68  E-value: 4.23e-37
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622828204  972 NKNKNRNSNVIPYDYNRVPLKhelemskesdhdsdessdDDSDSEEPSKYINASFIMS-------YWKPEVMIAAQGPLK 1044
Cdd:cd14544      1 NKGKNRYKNILPFDHTRVILK------------------DRDPNVPGSDYINANYIRNenegpttDENAKTYIATQGCLE 62

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622828204 1045 ETIGDFWQMIFQRKVKVIVMLTELKHGDQEICAQYW---GEGKQtYGDIEVDMKDTNKSSTYTLRVFELRHSKRKDS-RT 1120
Cdd:cd14544     63 NTVSDFWSMVWQENSRVIVMTTKEVERGKNKCVRYWpdeGMQKQ-YGPYRVQNVSEHDTTDYTLRELQVSKLDQGDPiRE 141

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622828204 1121 VYQYQYTNWSVEQLPAEPKELVSLIQVLKEKLPQKNSsegnkhhkSTPLLIHCRDGSQQTGIFCALLNLLESAETEEV-- 1198
Cdd:cd14544    142 IWHYQYLSWPDHGVPSDPGGVLNFLEDVNQRQESLPH--------AGPIVVHCSAGIGRTGTFIVIDMLLDQIKRKGLdc 213

                          250       260
                   ....*....|....*....|....*....
gi 1622828204 1199 -VDIFQVVKALRKARPGMVSTFEQYQFLY 1226
Cdd:cd14544    214 dIDIQKTIQMVRSQRSGMVQTEAQYKFIY 242
PTPc-N20_13 cd14538
catalytic domain of tyrosine-protein phosphatase non-receptor type 20 and type 13; ...
 1021-1229 4.25e-37

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: 139.05  E-value: 4.25e-37
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622828204 1021 YINASFI--------MSYwkpevmIAAQGPLKETIGDFWQMIFQRKVKVIVMLTELKHGDQEICAQYWGEGKQT----YG 1088
Cdd:cd14538      1 YINASHIripvggdtYHY------IACQGPLPNTTGDFWQMVWEQKSEVIAMVTQDVEGGKVKCHRYWPDSLNKplicGG 74

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622828204 1089 DIEVDMKDTNKSSTYTLRVFELRHSKRKDSRTVYQYQYTNWSVEQLPAEPKELVSLIQVLKeklpqknssegnKHHKSTP 1168
Cdd:cd14538     75 RLEVSLEKYQSLQDFVIRRISLRDKETGEVHHITHLNFTTWPDHGTPQSADPLLRFIRYMR------------RIHNSGP 142

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1622828204 1169 LLIHCRDGSQQTGIFCALLNLLESAETEEVVDIFQVVKALRKARPGMVSTFEQYQFLYDII 1229
Cdd:cd14538    143 IVVHCSAGIGRTGVLITIDVALGLIERDLPFDIQDIVKDLREQRQGMIQTKDQYIFCYKAC 203
PTPc-N21_14 cd14540
catalytic domain of tyrosine-protein phosphatase non-receptor type 21 and type 14; ...
 1021-1226 4.73e-37

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: 139.13  E-value: 4.73e-37
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622828204 1021 YINASFImsywKPEV------MIAAQGPLKETIGDFWQMIFQRKVKVIVMLTELKHGDQEICAQYW-----GEGKQTYGD 1089
Cdd:cd14540      1 YINASHI----TATVggkqrfYIAAQGPLQNTVGDFWQMVWEQGVYLVVMVTAEEEGGREKCFRYWptlggEHDALTFGE 76

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622828204 1090 IEVDMKDTNKSSTYTLRVFELRHSKRKDSRTVYQYQYTNWSVEQLPAEPKELVSLIQVLKEkLPQKNSSEGNKHHKSTPL 1169
Cdd:cd14540     77 YKVSTKFSVSSGCYTTTGLRVKHTLSGQSRTVWHLQYTDWPDHGCPEDVSGFLDFLEEINS-VRRHTNQDVAGHNRNPPT 155

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 1622828204 1170 LIHCRDGSQQTG--IFCALlnLLESAETEEVVDIFQVVKALRKARPGMVSTFEQYQFLY 1226
Cdd:cd14540    156 LVHCSAGVGRTGvvILADL--MLYCLDHNEELDIPRVLALLRHQRMLLVQTLAQYKFVY 212
PTPc-N11 cd14605
catalytic domain of tyrosine-protein phosphatase non-receptor type 11; Tyrosine-protein ...
 971-1226 2.22e-36

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: 138.61  E-value: 2.22e-36
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622828204  971 ENKNKNRNSNVIPYDYNRVPLkHELEMSKESDhdsdessdddsdseepsKYINASFIMSYW-------KPE-VMIAAQGP 1042
Cdd:cd14605      1 ENKNKNRYKNILPFDHTRVVL-HDGDPNEPVS-----------------DYINANIIMPEFetkcnnsKPKkSYIATQGC 62

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622828204 1043 LKETIGDFWQMIFQRKVKVIVMLT-ELKHGDQEiCAQYWGE--GKQTYGDIEVDMKDTNKSSTYTLRvfELRHSK---RK 1116
Cdd:cd14605     63 LQNTVNDFWRMVFQENSRVIVMTTkEVERGKSK-CVKYWPDeyALKEYGVMRVRNVKESAAHDYILR--ELKLSKvgqGN 139

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622828204 1117 DSRTVYQYQYTNWSVEQLPAEPKELVSLIQVLKEKlpQKNSSEGNkhhkstPLLIHCRDGSQQTGIFCA---LLNLLESA 1193
Cdd:cd14605    140 TERTVWQYHFRTWPDHGVPSDPGGVLDFLEEVHHK--QESIMDAG------PVVVHCSAGIGRTGTFIVidiLIDIIREK 211

                          250       260       270
                   ....*....|....*....|....*....|...
gi 1622828204 1194 ETEEVVDIFQVVKALRKARPGMVSTFEQYQFLY 1226
Cdd:cd14605    212 GVDCDIDVPKTIQMVRSQRSGMVQTEAQYRFIY 244
R-PTPc-R cd14611
catalytic domain of receptor-type tyrosine-protein phosphatase R; Receptor-type ...
 975-1226 2.26e-36

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: 137.74  E-value: 2.26e-36
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622828204  975 KNRNSNVIPYDYNRVPLKhelemskesdhdsdessdDDSDSEEPSKYINASFIMSYW-KPEVMIAAQGPLKETIGDFWQM 1053
Cdd:cd14611      2 KNRYKTILPNPHSRVCLK------------------PKNSNDSLSTYINANYIRGYGgKEKAFIATQGPMINTVNDFWQM 63

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622828204 1054 IFQRKVKVIVMLTELKHGDqEICAQYWGEGKQTYGDIEVDMKDTNKSSTYTLRVFELRHSKRkdSRTVYQYQYTNWSVEQ 1133
Cdd:cd14611     64 VWQEDSPVIVMITKLKEKN-EKCVLYWPEKRGIYGKVEVLVNSVKECDNYTIRNLTLKQGSQ--SRSVKHYWYTSWPDHK 140

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622828204 1134 LPAEPKELVSLIQVLKEKlPQKNSSEGnkhhkstPLLIHCRDGSQQTGIFCALLNLLESAETEEVVDIFQVVKALRKARP 1213
Cdd:cd14611    141 TPDSAQPLLQLMLDVEED-RLASPGRG-------PVVVHCSAGIGRTGCFIATTIGCQQLKEEGVVDVLSIVCQLRVDRG 212

                          250
                   ....*....|...
gi 1622828204 1214 GMVSTFEQYQFLY 1226
Cdd:cd14611    213 GMVQTSEQYEFVH 225
PTP-N23 cd14539
PTP-like domain of tyrosine-protein phosphatase non-receptor type 23; Tyrosine-protein ...
 1021-1227 2.57e-35

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: 133.66  E-value: 2.57e-35
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622828204 1021 YINASFI--MSYWKPEVmIAAQGPLKETIGDFWQMIFQRKVKVIVMLTelkhGDQEICAQ----YWGEGK---QTYGDIE 1091
Cdd:cd14539      1 YINASLIedLTPYCPRF-IATQAPLPGTAADFWLMVYEQQVSVIVMLV----SEQENEKQkvhrYWPTERgqaLVYGAIT 75

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622828204 1092 VDMKDTNKSSTYTLRVFELRHSKRKDSRTVYQYQYTNWSVEQLPAEPKELVSLIQVLKEKLPQKNSSEgnkhhksTPLLI 1171
Cdd:cd14539     76 VSLQSVRTTPTHVERIISIQHKDTRLSRSVVHLQFTTWPELGLPDSPNPLLRFIEEVHSHYLQQRSLQ-------TPIVV 148

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 1622828204 1172 HCRDGSQQTGIFCALLN-LLESAETEEVVDIFQVVKALRKARPGMVSTFEQYQFLYD 1227
Cdd:cd14539    149 HCSSGVGRTGAFCLLYAaVQEIEAGNGIPDLPQLVRKMRQQRKYMLQEKEHLKFCYE 205
R-PTPc-T-2 cd14634
PTP domain of receptor-type tyrosine-protein phosphatase T, repeat 2; Receptor-type ...
 1021-1228 4.55e-35

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: 133.22  E-value: 4.55e-35
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622828204 1021 YINASFIMSYWKPEVMIAAQGPLKETIGDFWQMIFQRKVKVIVMLTELKHGdqEICAQYWGEGKQ-TYGDIEVDMKDTNK 1099
Cdd:cd14634      1 YINAALMDSHKQPAAFIVTQHPLPNTVADFWRLVFDYNCSSVVMLNEMDAA--QLCMQYWPEKTScCYGPIQVEFVSADI 78

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622828204 1100 SSTYTLRVFELRHSKRKDS--RTVYQYQYTNW-SVEQLPAEPKELVSLIQVLKEKLPQKNSSEGNKhhkstplLIHCRDG 1176
Cdd:cd14634     79 DEDIISRIFRICNMARPQDgyRIVQHLQYIGWpAYRDTPPSKRSILKVVRRLEKWQEQYDGREGRT-------VVHCLNG 151

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|..
gi 1622828204 1177 SQQTGIFCALLNLLESAETEEVVDIFQVVKALRKARPGMVSTFEQYQFLYDI 1228
Cdd:cd14634    152 GGRSGTFCAICSVCEMIQQQNIIDVFHTVKTLRNNKSNMVETLEQYKFVYEV 203
PTPc-N1_2 cd14545
catalytic domain of tyrosine-protein phosphatase non-receptor type 1 and type 2; ...
 975-1226 1.63e-34

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: 132.52  E-value: 1.63e-34
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622828204  975 KNRNSNVIPYDYNRVPLKHELEMSKesdhdsdessdddsdseepskYINASFIMSYWKPEVMIAAQGPLKETIGDFWQMI 1054
Cdd:cd14545      1 LNRYRDRDPYDHDRSRVKLKQGDND---------------------YINASLVEVEEAKRSYILTQGPLPNTSGHFWQMV 59

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622828204 1055 FQRKVKVIVMLTELKHGDQEICAQYWGEGKQTYGDIE-----VDMKDTNKSSTYTLRVFELRHSKRKDSRTVYQYQYTNW 1129
Cdd:cd14545     60 WEQNSKAVIMLNKLMEKGQIKCAQYWPQGEGNAMIFEdtglkVTLLSEEDKSYYTVRTLELENLKTQETREVLHFHYTTW 139

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622828204 1130 SVEQLPAEPKELVSLIQvlkeKLPQKNSSEGNKhhksTPLLIHCRDGSQQTGIFC---ALLNLLESAETEEvVDIFQVVK 1206
Cdd:cd14545    140 PDFGVPESPAAFLNFLQ----KVRESGSLSSDV----GPPVVHCSAGIGRSGTFClvdTCLVLIEKGNPSS-VDVKKVLL 210

                          250       260
                   ....*....|....*....|
gi 1622828204 1207 ALRKARPGMVSTFEQYQFLY 1226
Cdd:cd14545    211 EMRKYRMGLIQTPDQLRFSY 230
PTPc-N6 cd14606
catalytic domain of tyrosine-protein phosphatase non-receptor type 6; Tyrosine-protein ...
 964-1230 1.79e-34

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: 133.47  E-value: 1.79e-34
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622828204  964 QHIGNQEENKNKNRNSNVIPYDYNRVPLKhelemskesdhdsdessdDDSDSEEPSKYINASFIMSYW-----KPEVMIA 1038
Cdd:cd14606     10 RLEGQRPENKSKNRYKNILPFDHSRVILQ------------------GRDSNIPGSDYINANYVKNQLlgpdeNAKTYIA 71

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622828204 1039 AQGPLKETIGDFWQMIFQRKVKVIVMLT-ELKHGDQEiCAQYWGE--GKQTYGDIEVDMKDTNKSSTYTLRVFELRHSKR 1115
Cdd:cd14606     72 SQGCLEATVNDFWQMAWQENSRVIVMTTrEVEKGRNK-CVPYWPEvgMQRAYGPYSVTNCGEHDTTEYKLRTLQVSPLDN 150

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622828204 1116 KDS-RTVYQYQYTNWSVEQLPAEPKELVSL---IQVLKEKLPqknssegnkhhKSTPLLIHCRDGSQQTGIFCALLNLLE 1191
Cdd:cd14606    151 GELiREIWHYQYLSWPDHGVPSEPGGVLSFldqINQRQESLP-----------HAGPIIVHCSAGIGRTGTIIVIDMLME 219

                          250       260       270       280
                   ....*....|....*....|....*....|....*....|..
gi 1622828204 1192 SAETEEV---VDIFQVVKALRKARPGMVSTFEQYQFLYDIIA 1230
Cdd:cd14606    220 NISTKGLdcdIDIQKTIQMVRAQRSGMVQTEAQYKFIYVAIA 261
PHA02747 PHA02747
protein tyrosine phosphatase; Provisional
 971-1225 5.02e-34

protein tyrosine phosphatase; Provisional


Pssm-ID: 165114 [Multi-domain]  Cd Length: 312  Bit Score: 133.59  E-value: 5.02e-34
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622828204  971 ENKNKNRNSNVIPYDYNRVPLKhelemskesdhdsdessdddSDSEEPSKYINASFIMSYWKPEVMIAAQGPLKETIGDF 1050
Cdd:PHA02747    50 ENQPKNRYWDIPCWDHNRVILD--------------------SGGGSTSDYIHANWIDGFEDDKKFIATQGPFAETCADF 109

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622828204 1051 WQMIFQRKVKVIVMLTELKHGD-QEICAQYWG---EGKQTYGDIEVDMKDTNKSSTYTLRVFELRHSKRKDSRTVYQYQY 1126
Cdd:PHA02747   110 WKAVWQEHCSIIVMLTPTKGTNgEEKCYQYWClneDGNIDMEDFRIETLKTSVRAKYILTLIEITDKILKDSRKISHFQC 189

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622828204 1127 TNWSVEQLPAEPKELVSLIQVLKEKLPQKNSSEGNKHHKSTPLLIHCRDGSQQTGIFCALLNLLESAETEEVVDIFQVVK 1206
Cdd:PHA02747   190 SEWFEDETPSDHPDFIKFIKIIDINRKKSGKLFNPKDALLCPIVVHCSDGVGKTGIFCAVDICLNQLVKRKAICLAKTAE 269

                          250
                   ....*....|....*....
gi 1622828204 1207 ALRKARPGMVSTFEQYQFL 1225
Cdd:PHA02747   270 KIREQRHAGIMNFDDYLFI 288
PHA02746 PHA02746
protein tyrosine phosphatase; Provisional
 969-1229 5.20e-34

protein tyrosine phosphatase; Provisional


Pssm-ID: 165113 [Multi-domain]  Cd Length: 323  Bit Score: 134.00  E-value: 5.20e-34
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622828204  969 QEENKNKNRNSNVIPYDYNRVPLKHELEMSKESDHDSDESSDDDSDSEEPSKYINASFIMSYWKPEVMIAAQGPLKETIG 1048
Cdd:PHA02746    48 KKENLKKNRFHDIPCWDHSRVVINAHESLKMFDVGDSDGKKIEVTSEDNAENYIHANFVDGFKEANKFICAQGPKEDTSE 127

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622828204 1049 DFWQMIFQRKVKVIVMLTELKHgDQEICAQYWGEGKQ---TYGDIEVDMKDTNKSSTYTLRVFELRHSKRKDSRTVYQYQ 1125
Cdd:PHA02746   128 DFFKLISEHESQVIVSLTDIDD-DDEKCFELWTKEEDselAFGRFVAKILDIIEELSFTKTRLMITDKISDTSREIHHFW 206

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622828204 1126 YTNWSVEQLPAEPKELVSLIQVLKEKLPQKNSSEGNKHHKSTPLLIHCRDGSQQTGIFCALLNLLESAETEEVVDIFQVV 1205
Cdd:PHA02746   207 FPDWPDNGIPTGMAEFLELINKVNEEQAELIKQADNDPQTLGPIVVHCSAGIGRAGTFCAIDNALEQLEKEKEVCLGEIV 286

                          250       260
                   ....*....|....*....|....
gi 1622828204 1206 KALRKARPGMVSTFEQYQFLYDII 1229
Cdd:PHA02746   287 LKIRKQRHSSVFLPEQYAFCYKAL 310
R-PTPc-K-2 cd14636
PTP domain of receptor-type tyrosine-protein phosphatase K, repeat 2; Receptor-type ...
 1021-1228 6.25e-34

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: 129.76  E-value: 6.25e-34
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622828204 1021 YINASFIMSYWKPEVMIAAQGPLKETIGDFWQMIFQRKVKVIVMLTELKHgdQEICAQYW-GEGKQTYGDIEVDMKDTNK 1099
Cdd:cd14636      1 YINAALMDSYRQPAAFIVTQHPLPNTVKDFWRLVYDYGCTSIVMLNEVDL--AQGCPQYWpEEGMLRYGPIQVECMSCSM 78

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622828204 1100 SSTYTLRVFELRHSKRKDS--RTVYQYQYTNW-SVEQLPAEPKELVSLIqvLKEKLPQKNSSEGNKHhkstpLLIHCRDG 1176
Cdd:cd14636     79 DCDVISRIFRICNLTRPQEgyLMVQQFQYLGWaSHREVPGSKRSFLKLI--LQVEKWQEECDEGEGR-----TIIHCLNG 151

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|..
gi 1622828204 1177 SQQTGIFCALLNLLESAETEEVVDIFQVVKALRKARPGMVSTFEQYQFLYDI 1228
Cdd:cd14636    152 GGRSGMFCAISIVCEMIKRQNVVDVFHAVKTLRNSKPNMVETPEQYRFCYDV 203
PTPc_plant_PTP1 cd17658
protein tyrosine phosphatase 1 from Arabidopsis thaliana and similar plant PTPs; Arabidopsis ...
 1021-1226 1.07e-33

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: 129.12  E-value: 1.07e-33
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622828204 1021 YINASFIMSYWKPEV--MIAAQGPLKETIGDFWQMIFQRKVKVIVMLTELKHGDQEI-CAQYW---GEGKQTYGDIEVDM 1094
Cdd:cd17658      1 YINASLVETPASESLpkFIATQGPLPHTFEDFWEMVIQQRCPVIIMLTRLVDNYSTAkCADYFpaeENESREFGRISVTN 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622828204 1095 KDTNKSST-YTLRVFELRHSKRKDS-RTVYQYQYTNWSVEQLPAEPKELVSLIQVLKEKLPqknsSEGnkhhkstPLLIH 1172
Cdd:cd17658     81 KKLKHSQHsITLRVLEVQYIESEEPpLSVLHIQYPEWPDHGVPKDTRSVRELLKRLYGIPP----SAG-------PIVVH 149

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 1622828204 1173 CRDGSQQTGIFCALLNLLES--AETEEVVDIFQVVKALRKARPGMVSTFEQYQFLY 1226
Cdd:cd17658    150 CSAGIGRTGAYCTIHNTIRRilEGDMSAVDLSKTVRKFRSQRIGMVQTQDQYIFCY 205
R-PTPc-U-2 cd14637
PTP domain of receptor-type tyrosine-protein phosphatase U, repeat 2; Receptor-type ...
 1021-1228 1.01e-32

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


Pssm-ID: 350485 [Multi-domain]  Cd Length: 207  Bit Score: 126.56  E-value: 1.01e-32
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622828204 1021 YINASFIMSYWKPEVMIAAQGPLKETIGDFWQMIFQRKVKVIVMLTELKHGDQEI-CAQYWGE-GKQTYGDIEVDMKDTN 1098
Cdd:cd14637      1 YINAALTDSYTRSAAFIVTLHPLQNTTTDFWRLVYDYGCTSVVMLNQLNQSNSAWpCLQYWPEpGLQQYGPMEVEFVSGS 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622828204 1099 KSSTYTLRVFELRHSKR--KDSRTVYQYQYTNWSV-EQLPAEPKELVSLIQVLKEKlpQKNSSEGNKhhkstplLIHCRD 1175
Cdd:cd14637     81 ADEDIVTRLFRVQNITRlqEGHLMVRHFQFLRWSAyRDTPDSKKAFLHLLASVEKW--QRESGEGRT-------VVHCLN 151

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|...
gi 1622828204 1176 GSQQTGIFCALLNLLESAETEEVVDIFQVVKALRKARPGMVSTFEQYQFLYDI 1228
Cdd:cd14637    152 GGGRSGTYCASAMILEMIRCHNIVDVFYAVKTLRNYKPNMVETLEQYRFCYEI 204
PHA02742 PHA02742
protein tyrosine phosphatase; Provisional
 971-1229 1.39e-31

protein tyrosine phosphatase; Provisional


Pssm-ID: 165109 [Multi-domain]  Cd Length: 303  Bit Score: 126.27  E-value: 1.39e-31
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622828204  971 ENKN--KNRNSNVIPYDYNRVPLKHELEMSKesdhdsdessdddsdseepskYINASFIMSYWKPEVMIAAQGPLKETIG 1048
Cdd:PHA02742    49 ELKNmkKCRYPDAPCFDRNRVILKIEDGGDD---------------------FINASYVDGHNAKGRFICTQAPLEETAL 107

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622828204 1049 DFWQMIFQRKVKVIVMLTELKHGDQEICAQYWG---EGKQTYGDIEVDMKDTNKSSTYTLRVFELRHSKRKDSRTVYQYQ 1125
Cdd:PHA02742   108 DFWQAIFQDQVRVIVMITKIMEDGKEACYPYWMpheRGKATHGEFKIKTKKIKSFRNYAVTNLCLTDTNTGASLDIKHFA 187

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622828204 1126 YTNWSVEQLPAEPKELVSLIQVLKE-KLPQKNSSEGNKHHKSTPLLIHCRDGSQQTGIFCALLNLLESAETEEVVDIFQV 1204
Cdd:PHA02742   188 YEDWPHGGLPRDPNKFLDFVLAVREaDLKADVDIKGENIVKEPPILVHCSAGLDRAGAFCAIDICISKYNERAIIPLLSI 267

                          250       260
                   ....*....|....*....|....*
gi 1622828204 1205 VKALRKARPGMVSTFEQYQFLYDII 1229
Cdd:PHA02742   268 VRDLRKQRHNCLSLPQQYIFCYFIV 292
PTPc-N14 cd14599
catalytic domain of tyrosine-protein phosphatase non-receptor type 14; Tyrosine-protein ...
 951-1229 2.05e-31

catalytic domain of tyrosine-protein phosphatase non-receptor type 14; Tyrosine-protein phosphatase non-receptor type 14 (PTPN14), also called protein-tyrosine phosphatase pez, belongs to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. PTPN14 is a potential tumor suppressor and plays a regulatory role in the Hippo and Wnt/beta-catenin signaling pathways. It contains an N-terminal FERM domain and a C-terminal catalytic PTP domain, separated by a long intervening sequence.


Pssm-ID: 350447 [Multi-domain]  Cd Length: 287  Bit Score: 125.11  E-value: 2.05e-31
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622828204  951 EFQRLPSYRSWRTQHIGNQEENKNKNRNSNVIPYDYNRVPLKHELEmskesdhdsdessdddsdseEPSKYINASFIMSY 1030
Cdd:cd14599     17 EYEQIPKKKADGVFTTATLPENAERNRIREVVPYEENRVELVPTKE--------------------NNTGYINASHIKVT 76

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622828204 1031 WKPEV--MIAAQGPLKETIGDFWQMIFQRKVKVIVMLTELKHGDQEICAQYWGE-----GKQTYGDIEVDMKDTNKSSTY 1103
Cdd:cd14599     77 VGGEEwhYIATQGPLPHTCHDFWQMVWEQGVNVIAMVTAEEEGGRSKSHRYWPKlgskhSSATYGKFKVTTKFRTDSGCY 156

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622828204 1104 TLRVFELRHSKRKDSRTVYQYQYTNWSVEQLPAEPKELVSLIQVLKEKLPQKNSSEGNKHHKSTPLLIHCRDGSQQTGIF 1183
Cdd:cd14599    157 ATTGLKVKHLLSGQERTVWHLQYTDWPDHGCPEEVQGFLSYLEEIQSVRRHTNSMLDSTKNCNPPIVVHCSAGVGRTGVV 236

                          250       260       270       280
                   ....*....|....*....|....*....|....*....|....*.
gi 1622828204 1184 CALLNLLESAETEEVVDIFQVVKALRKARPGMVSTFEQYQFLYDII 1229
Cdd:cd14599    237 ILTELMIGCLEHNEKVEVPVMLRHLREQRMFMIQTIAQYKFVYQVL 282
PTPc-N2 cd14607
catalytic domain of tyrosine-protein phosphatase non-receptor type 2; Tyrosine-protein ...
 971-1226 2.56e-31

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: 123.92  E-value: 2.56e-31
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622828204  971 ENKNKNRNSNVIPYDYNRVPLKHelemskesdhdsdessdddsdseEPSKYINASFIMSYWKPEVMIAAQGPLKETIGDF 1050
Cdd:cd14607     23 ENRNRNRYRDVSPYDHSRVKLQN-----------------------TENDYINASLVVIEEAQRSYILTQGPLPNTCCHF 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622828204 1051 WQMIFQRKVKVIVMLTELKHGDQEICAQYW---GEGKQTYGD--IEVDMKDTNKSSTYTLRVFELRHSKRKDSRTVYQYQ 1125
Cdd:cd14607     80 WLMVWQQKTKAVVMLNRIVEKDSVKCAQYWptdEEEVLSFKEtgFSVKLLSEDVKSYYTVHLLQLENINSGETRTISHFH 159

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622828204 1126 YTNWSVEQLPAEPKELVSLIQVLKEklpqknssEGNKHHKSTPLLIHCRDGSQQTGIFCAL---LNLLESAETEEvVDIF 1202
Cdd:cd14607    160 YTTWPDFGVPESPASFLNFLFKVRE--------SGSLSPEHGPAVVHCSAGIGRSGTFSLVdtcLVLMEKKDPDS-VDIK 230

                          250       260
                   ....*....|....*....|....
gi 1622828204 1203 QVVKALRKARPGMVSTFEQYQFLY 1226
Cdd:cd14607    231 QVLLDMRKYRMGLIQTPDQLRFSY 254
PTPc-N1 cd14608
catalytic domain of tyrosine-protein phosphatase non-receptor type 1; Tyrosine-protein ...
 966-1226 3.33e-31

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: 124.37  E-value: 3.33e-31
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622828204  966 IGNQEENKNKNRNSNVIPYDYNRVPLKHElemskesdhdsdessdddsdseePSKYINASFIMSYWKPEVMIAAQGPLKE 1045
Cdd:cd14608     19 VAKLPKNKNRNRYRDVSPFDHSRIKLHQE-----------------------DNDYINASLIKMEEAQRSYILTQGPLPN 75

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622828204 1046 TIGDFWQMIFQRKVKVIVMLTELKHGDQEICAQYWGEGKQTygdiEVDMKDTN---------KSSTYTLRVFELRHSKRK 1116
Cdd:cd14608     76 TCGHFWEMVWEQKSRGVVMLNRVMEKGSLKCAQYWPQKEEK----EMIFEDTNlkltlisedIKSYYTVRQLELENLTTQ 151

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622828204 1117 DSRTVYQYQYTNWSVEQLPAEPKELVSLIQVLKEklpqknssEGNKHHKSTPLLIHCRDGSQQTGIFC---ALLNLLESA 1193
Cdd:cd14608    152 ETREILHFHYTTWPDFGVPESPASFLNFLFKVRE--------SGSLSPEHGPVVVHCSAGIGRSGTFCladTCLLLMDKR 223

                          250       260       270
                   ....*....|....*....|....*....|...
gi 1622828204 1194 ETEEVVDIFQVVKALRKARPGMVSTFEQYQFLY 1226
Cdd:cd14608    224 KDPSSVDIKKVLLEMRKFRMGLIQTADQLRFSY 256
R-PTPc-B cd14617
catalytic domain of receptor-type tyrosine-protein phosphatase B; Receptor-type ...
 976-1226 5.51e-31

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: 122.33  E-value: 5.51e-31
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622828204  976 NRNSNVIPYDYNRVPLKHelemskesdhdsdessdddSDSEEPSKYINASFIMSYWKPEVMIAAQGPLKETIGDFWQMIF 1055
Cdd:cd14617      1 NRYNNILPYDSTRVKLSN-------------------VDDDPCSDYINASYIPGNNFRREYIATQGPLPGTKDDFWKMVW 61

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622828204 1056 QRKVKVIVMLTELKHGDQEICAQYWGEGKQT--YGDIEVDMKDTNKSSTYTLRVFELRHSKRKDS-RTVYQYQYTNWSVE 1132
Cdd:cd14617     62 EQNVHNIVMVTQCVEKGRVKCDHYWPADQDSlyYGDLIVQMLSESVLPEWTIREFKICSEEQLDApRLVRHFHYTVWPDH 141

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622828204 1133 QLPAEPKELVSLIQVLKEKLpqknssegNKHHKSTPLLIHCRDGSQQTGIFCALLNLLESAETEEVVDIFQVVKALRKAR 1212
Cdd:cd14617    142 GVPETTQSLIQFVRTVRDYI--------NRTPGSGPTVVHCSAGVGRTGTFIALDRILQQLDSKDSVDIYGAVHDLRLHR 213

                          250
                   ....*....|....
gi 1622828204 1213 PGMVSTFEQYQFLY 1226
Cdd:cd14617    214 VHMVQTECQYVYLH 227
PTPc-N20 cd14596
catalytic domain of tyrosine-protein phosphatase non-receptor type 20; Tyrosine-protein ...
 1021-1229 1.09e-30

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: 120.62  E-value: 1.09e-30
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622828204 1021 YINASFIMSYWKPE--VMIAAQGPLKETIGDFWQMIFQRKVKVIVMLTELKHGDQEICAQYWGEGKQTYGDIE---VDMK 1095
Cdd:cd14596      1 YINASYITMPVGEEelFYIATQGPLPSTIDDFWQMVWENRSDVIAMMTREVERGKVKCHRYWPETLQEPMELEnyqLRLE 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622828204 1096 DTNKSSTYTLRVFELRHSKRKDSRTVYQYQYTNWSVEQLPAEPKELVSLIQVLKeklpqknssegnKHHKSTPLLIHCRD 1175
Cdd:cd14596     81 NYQALQYFIIRIIKLVEKETGENRLIKHLQFTTWPDHGTPQSSDQLVKFICYMR------------KVHNTGPIVVHCSA 148

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....
gi 1622828204 1176 GSQQTGIFCALLNLLESAETEEVVDIFQVVKALRKARPGMVSTFEQYQFLYDII 1229
Cdd:cd14596    149 GIGRAGVLICVDVLLSLIEKDLSFNIKDIVREMRQQRYGMIQTKDQYLFCYKVV 202
PTPc-N21 cd14598
catalytic domain of tyrosine-protein phosphatase non-receptor type 21; Tyrosine-protein ...
 1021-1229 3.01e-30

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: 119.69  E-value: 3.01e-30
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622828204 1021 YINASFIM-----SYWKpevMIAAQGPLKETIGDFWQMIFQRKVKVIVMLTELKHGDQEICAQYWG-----EGKQTYGDI 1090
Cdd:cd14598      1 YINASHIKvtvggKEWD---YIATQGPLQNTCQDFWQMVWEQGVAIIAMVTAEEEGGREKSFRYWPrlgsrHNTVTYGRF 77

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622828204 1091 EVDMKDTNKSSTYTLRVFELRHSKRKDSRTVYQYQYTNWSVEQLPAEPKELVSLIQVLKEKLPQKNSSEGNKHHKStPLL 1170
Cdd:cd14598     78 KITTRFRTDSGCYATTGLKIKHLLTGQERTVWHLQYTDWPEHGCPEDLKGFLSYLEEIQSVRRHTNSTIDPKSPNP-PVL 156

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 1622828204 1171 IHCRDGSQQTGIFCALLNLLESAETEEVVDIFQVVKALRKARPGMVSTFEQYQFLYDII 1229
Cdd:cd14598    157 VHCSAGVGRTGVVILSEIMIACLEHNEMLDIPRVLDMLRQQRMMMVQTLSQYTFVYKVL 215
PTPc_motif smart00404
Protein tyrosine phosphatase, catalytic domain motif;
1120-1231 3.42e-30

Protein tyrosine phosphatase, catalytic domain motif;


Pssm-ID: 214649 [Multi-domain]  Cd Length: 105  Bit Score: 115.53  E-value: 3.42e-30
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622828204  1120 TVYQYQYTNWSVEQLPAEPKELVSLIQVLKEKLPQKNSSegnkhhksTPLLIHCRDGSQQTGIFCALLNLLESAETE-EV 1198
Cdd:smart00404    1 TVKHYHYTGWPDHGVPESPDSILELLRAVKKNLNQSESS--------GPVVVHCSAGVGRTGTFVAIDILLQQLEAEaGE 72

                            90       100       110
                    ....*....|....*....|....*....|...
gi 1622828204  1199 VDIFQVVKALRKARPGMVSTFEQYQFLYDIIAS 1231
Cdd:smart00404   73 VDIFDTVKELRSQRPGMVQTEEQYLFLYRALLE 105
PTPc_DSPc smart00012
Protein tyrosine phosphatase, catalytic domain, undefined specificity; Protein tyrosine ...
 1120-1231 3.42e-30

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


Pssm-ID: 214469 [Multi-domain]  Cd Length: 105  Bit Score: 115.53  E-value: 3.42e-30
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622828204  1120 TVYQYQYTNWSVEQLPAEPKELVSLIQVLKEKLPQKNSSegnkhhksTPLLIHCRDGSQQTGIFCALLNLLESAETE-EV 1198
Cdd:smart00012    1 TVKHYHYTGWPDHGVPESPDSILELLRAVKKNLNQSESS--------GPVVVHCSAGVGRTGTFVAIDILLQQLEAEaGE 72

                            90       100       110
                    ....*....|....*....|....*....|...
gi 1622828204  1199 VDIFQVVKALRKARPGMVSTFEQYQFLYDIIAS 1231
Cdd:smart00012   73 VDIFDTVKELRSQRPGMVQTEEQYLFLYRALLE 105
R-PTPc-M-2 cd14635
PTP domain of receptor-type tyrosine-protein phosphatase M, repeat 2; Receptor-type ...
 1021-1228 4.76e-30

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: 118.64  E-value: 4.76e-30
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622828204 1021 YINASFIMSYWKPEVMIAAQGPLKETIGDFWQMIFQRKVKVIVMLTELKHGdqEICAQYWGE-GKQTYGDIEVDMKDTNK 1099
Cdd:cd14635      1 YINAALMDSYKQPSAFIVTQHPLPNTVKDFWRLVLDYHCTSIVMLNDVDPA--QLCPQYWPEnGVHRHGPIQVEFVSADL 78

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622828204 1100 SSTYTLRVFELRHSKRKDS--RTVYQYQYTNWSV-EQLPAEPKELVSLIQVLKEKLPQKNSSEGNKhhkstplLIHCRDG 1176
Cdd:cd14635     79 EEDIISRIFRIYNAARPQDgyRMVQQFQFLGWPMyRDTPVSKRSFLKLIRQVDKWQEEYNGGEGRT-------VVHCLNG 151

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|..
gi 1622828204 1177 SQQTGIFCALLNLLESAETEEVVDIFQVVKALRKARPGMVSTFEQYQFLYDI 1228
Cdd:cd14635    152 GGRSGTFCAISIVCEMLRHQRAVDVFHAVKTLRNNKPNMVDLLDQYKFCYEV 203
PTPc-N3_4 cd14541
catalytic domain of tyrosine-protein phosphatase non-receptor type 21 and type 14; ...
 1021-1233 5.36e-30

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: 118.59  E-value: 5.36e-30
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622828204 1021 YINASFI-MSYWKPEVM---IAAQGPLKETIGDFWQMIFQRKVKVIVMLTELKHGDQEICAQYW--GEGKQTYGDIEVDM 1094
Cdd:cd14541      2 YINANYVnMEIPGSGIVnryIAAQGPLPNTCADFWQMVWEQKSTLIVMLTTLVERGRVKCHQYWpdLGETMQFGNLQITC 81

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622828204 1095 KDTNKSSTYTLRVFELRHSKRKDSRTVYQYQYTNWSVEQLPAEPKELVSLIQVLKEklpqknssegNKHHKSTPLLIHCR 1174
Cdd:cd14541     82 VSEEVTPSFAFREFILTNTNTGEERHITQMQYLAWPDHGVPDDSSDFLDFVKRVRQ----------NRVGMVEPTVVHCS 151

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1622828204 1175 DGSQQTGIfcalLNLLESA----ETEEVVDIFQVVKALRKARPGMVSTFEQYQFLYDIIASTY 1233
Cdd:cd14541    152 AGIGRTGV----LITMETAmcliEANEPVYPLDIVRTMRDQRAMLIQTPSQYRFVCEAILRVY 210
R-PTPc-T-2 cd14634
PTP domain of receptor-type tyrosine-protein phosphatase T, repeat 2; Receptor-type ...
 711-915 5.92e-30

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: 118.59  E-value: 5.92e-30
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622828204  711 YINASYIDGFKEPRKYIAAQGPRDETVDDFWRMIWEQKATVIVMVTrcEEGNRNKCAEYWPsmEEGTRAFGDVVVKINQH 790
Cdd:cd14634      1 YINAALMDSHKQPAAFIVTQHPLPNTVADFWRLVFDYNCSSVVMLN--EMDAAQLCMQYWP--EKTSCCYGPIQVEFVSA 76

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622828204  791 KRCPDYIIQKLNIVNKKEKATG-REVTHIQFTSWPDH-GVPEDPHLLLKLRRRVNAFSNFF---SGPIVVHCSAGVGRTG 865
Cdd:cd14634     77 DIDEDIISRIFRICNMARPQDGyRIVQHLQYIGWPAYrDTPPSKRSILKVVRRLEKWQEQYdgrEGRTVVHCLNGGGRSG 156

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|
gi 1622828204  866 TYIGIDAMLEGLEAENKVDVYGYVVKLRRQRCLMVQVEAQYILIHQALVE 915
Cdd:cd14634    157 TFCAICSVCEMIQQQNIIDVFHTVKTLRNNKSNMVETLEQYKFVYEVALE 206
COG5599 COG5599
Protein tyrosine phosphatase [Signal transduction mechanisms];
963-1231 1.72e-29

Protein tyrosine phosphatase [Signal transduction mechanisms];


Pssm-ID: 444335 [Multi-domain]  Cd Length: 282  Bit Score: 119.43  E-value: 1.72e-29
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622828204  963 TQHIGNQEeNKNKNRNSNVIPYDYNRVplkhelemskesdhdsdessdddsdsEEPSKYINASFIMSYwKPEVMIAAQGP 1042
Cdd:COG5599     34 PQYLQNIN-GSPLNRFRDIQPYKETAL--------------------------RANLGYLNANYIQVI-GNHRYIATQYP 85

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622828204 1043 LKETIGDFWQMIFQRKVKVIVMLTELKHGDQEI--CAQYWGEgKQTYGDIEVDMKDTNK---SSTYTLRVFEL-RHSKRK 1116
Cdd:COG5599     86 LEEQLEDFFQMLFDNNTPVLVVLASDDEISKPKvkMPVYFRQ-DGEYGKYEVSSELTESiqlRDGIEARTYVLtIKGTGQ 164

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622828204 1117 DSRTVYQYQYTNW------SVEQLpaepKELVSLI-QVLKEKLPQKNssegnkhhkstPLLIHCRDGSQQTGIFCALLNL 1189
Cdd:COG5599    165 KKIEIPVLHVKNWpdhgaiSAEAL----KNLADLIdKKEKIKDPDKL-----------LPVVHCRAGVGRTGTLIACLAL 229

                          250       260       270       280
                   ....*....|....*....|....*....|....*....|....*
gi 1622828204 1190 LES--AETEEVVDIFQVVKALRKAR-PGMVSTFEQYQFLYDIIAS 1231
Cdd:COG5599    230 SKSinALVQITLSVEEIVIDMRTSRnGGMVQTSEQLDVLVKLAEQ 274
PTPc-N3 cd14600
catalytic domain of tyrosine-protein phosphatase non-receptor type 3; Tyrosine-protein ...
 969-1233 5.14e-29

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: 118.03  E-value: 5.14e-29
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622828204  969 QEENKNKNRNSNVIPYDYNRVPLKHElemskesdhdsdessdddsdseepSKYINASFI-MSYWKPEVM---IAAQGPLK 1044
Cdd:cd14600     37 LPQNMDKNRYKDVLPYDATRVVLQGN------------------------EDYINASYVnMEIPSANIVnkyIATQGPLP 92

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622828204 1045 ETIGDFWQMIFQRKVKVIVMLTELKHGDQEICAQYWGEGKQT--YGDIEVDMKDTNKSSTYTLRVFELRHSKRKDSRTVY 1122
Cdd:cd14600     93 HTCAQFWQVVWEQKLSLIVMLTTLTERGRTKCHQYWPDPPDVmeYGGFRVQCHSEDCTIAYVFREMLLTNTQTGEERTVT 172

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622828204 1123 QYQYTNWSVEQLPAEPKELVSLIQVLKEklpqknssegnKHHKSTPLLIHCRDGSQQTGIFCALLNLLESAETEEVVDIF 1202
Cdd:cd14600    173 HLQYVAWPDHGVPDDSSDFLEFVNYVRS-----------KRVENEPVLVHCSAGIGRTGVLVTMETAMCLTERNQPVYPL 241

                          250       260       270
                   ....*....|....*....|....*....|.
gi 1622828204 1203 QVVKALRKARPGMVSTFEQYQFLYDIIASTY 1233
Cdd:cd14600    242 DIVRKMRDQRAMMVQTSSQYKFVCEAILRVY 272
R5-PTP-2 cd14550
PTP-like domain of R5 subfamily receptor-type tyrosine-protein phosphatases, repeat 2; The R5 ...
 1021-1226 1.03e-28

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: 114.73  E-value: 1.03e-28
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622828204 1021 YINASFIMSYWKPEVMIAAQGPLKETIGDFWQMIFQRKVKVIVMLTELkHGDQEiCAQYW-GEGK----QTYGDIEVDMK 1095
Cdd:cd14550      1 YINASYLQGYRRSNEFIITQHPLEHTIKDFWQMIWDHNSQTIVMLTDN-ELNED-EPIYWpTKEKplecETFKVTLSGED 78

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622828204 1096 DTNKSST--YTLRVFELRHSKRKDSRTVYQYQYTNWSVEQLPaePKELVSLIQVLKEklpQKNSSEGnkhhkstPLLIHC 1173
Cdd:cd14550     79 HSCLSNEirLIVRDFILESTQDDYVLEVRQFQCPSWPNPCSP--IHTVFELINTVQE---WAQQRDG-------PIVVHD 146

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|...
gi 1622828204 1174 RDGSQQTGIFCALLNLLESAETEEVVDIFQVVKALRKARPGMVSTFEQYQFLY 1226
Cdd:cd14550    147 RYGGVQAATFCALTTLHQQLEHESSVDVYQVAKLYHLMRPGVFTSKEDYQFLY 199
R5-PTP-2 cd14550
PTP-like domain of R5 subfamily receptor-type tyrosine-protein phosphatases, repeat 2; The R5 ...
 711-897 2.20e-28

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: 113.57  E-value: 2.20e-28
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622828204  711 YINASYIDGFKEPRKYIAAQGPRDETVDDFWRMIWEQKATVIVMVTRCEEgnRNKCAEYWPSMEEGTRAFGDVVVKINQH 790
Cdd:cd14550      1 YINASYLQGYRRSNEFIITQHPLEHTIKDFWQMIWDHNSQTIVMLTDNEL--NEDEPIYWPTKEKPLECETFKVTLSGED 78

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622828204  791 KRC----PDYIIQKLNIVNKKEKATgREVTHIQFTSWPDHGVPedPHLLLKLRRRVNAFSNFFSGPIVVHCSAGVGRTGT 866
Cdd:cd14550     79 HSClsneIRLIVRDFILESTQDDYV-LEVRQFQCPSWPNPCSP--IHTVFELINTVQEWAQQRDGPIVVHDRYGGVQAAT 155

                          170       180       190
                   ....*....|....*....|....*....|...
gi 1622828204  867 YIGIDAMLEGLEAENKVDVYGYVV--KLRRQRC 897
Cdd:cd14550    156 FCALTTLHQQLEHESSVDVYQVAKlyHLMRPGV 188
R-PTP-Z-2 cd17669
catalytic domain of receptor-type tyrosine-protein phosphatase Z, repeat 2; Receptor-type ...
 1021-1229 8.61e-28

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: 112.01  E-value: 8.61e-28
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622828204 1021 YINASFIMSYWKPEVMIAAQGPLKETIGDFWQMIFQRKVKVIVMLTELKHGDQEICAqYWGEGKQ-------TYGDIEVD 1093
Cdd:cd17669      1 YINASYIMGYYQSNEFIITQHPLLHTIKDFWRMIWDHNAQLIVMLPDGQNMAEDEFV-YWPNKDEpincetfKVTLIAEE 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622828204 1094 MKDTNKSSTYTLRVFELRHSKRKDSRTVYQYQYTNWSVEQLPAEpkELVSLIQVLKEKLPQKNSsegnkhhkstPLLIHC 1173
Cdd:cd17669     80 HKCLSNEEKLIIQDFILEATQDDYVLEVRHFQCPKWPNPDSPIS--KTFELISIIKEEAANRDG----------PMIVHD 147

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 1622828204 1174 RDGSQQTGIFCALLNLLESAETEEVVDIFQVVKALRKARPGMVSTFEQYQFLYDII 1229
Cdd:cd17669    148 EHGGVTAGTFCALTTLMHQLEKENSVDVYQVAKMINLMRPGVFTDIEQYQFLYKAI 203
PTPc-N4 cd14601
catalytic domain of tyrosine-protein phosphatase non-receptor type 4; Tyrosine-protein ...
 1021-1233 9.10e-28

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: 112.35  E-value: 9.10e-28
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622828204 1021 YINASFI-MSYWKPEVM---IAAQGPLKETIGDFWQMIFQRKVKVIVMLTELKHGDQEICAQYWGE--GKQTYGDIEVDM 1094
Cdd:cd14601      2 YINANYInMEIPSSSIInryIACQGPLPNTCSDFWQMTWEQGSSMVVMLTTQVERGRVKCHQYWPEpsGSSSYGGFQVTC 81

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622828204 1095 KDTNKSSTYTLRVFELRHSKRKDSRTVYQYQYTNWSVEQLPAEPKELVSLIQVLKEKlpqknssegnKHHKSTPLLIHCR 1174
Cdd:cd14601     82 HSEEGNPAYVFREMTLTNLEKNESRPLTQIQYIAWPDHGVPDDSSDFLDFVCLVRNK----------RAGKDEPVVVHCS 151

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 1622828204 1175 DGSQQTGIFCALLNLLESAETEEVVDIFQVVKALRKARPGMVSTFEQYQFLYDIIASTY 1233
Cdd:cd14601    152 AGIGRTGVLITMETAMCLIECNQPVYPLDIVRTMRDQRAMMIQTPSQYRFVCEAILKVY 210
R-PTPc-M-2 cd14635
PTP domain of receptor-type tyrosine-protein phosphatase M, repeat 2; Receptor-type ...
 711-915 2.10e-26

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: 108.24  E-value: 2.10e-26
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622828204  711 YINASYIDGFKEPRKYIAAQGPRDETVDDFWRMIWEQKATVIVMVTRCEEGNRnkCAEYWPsmEEGTRAFGDVVVKINQH 790
Cdd:cd14635      1 YINAALMDSYKQPSAFIVTQHPLPNTVKDFWRLVLDYHCTSIVMLNDVDPAQL--CPQYWP--ENGVHRHGPIQVEFVSA 76

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622828204  791 KRCPDYIIQKLNIVNKKEKATG-REVTHIQFTSWPDH-GVPEDPHLLLKLRRRVNAFSNFF---SGPIVVHCSAGVGRTG 865
Cdd:cd14635     77 DLEEDIISRIFRIYNAARPQDGyRMVQQFQFLGWPMYrDTPVSKRSFLKLIRQVDKWQEEYnggEGRTVVHCLNGGGRSG 156

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|
gi 1622828204  866 TYIGIDAMLEGLEAENKVDVYGYVVKLRRQRCLMVQVEAQYILIHQALVE 915
Cdd:cd14635    157 TFCAISIVCEMLRHQRAVDVFHAVKTLRNNKPNMVDLLDQYKFCYEVALE 206
R-PTP-G-2 cd17670
PTP-like domain of receptor-type tyrosine-protein phosphatase G, repeat 2; Receptor-type ...
 1021-1231 1.53e-25

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: 105.92  E-value: 1.53e-25
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622828204 1021 YINASFIMSYWKPEVMIAAQGPLKETIGDFWQMIFQRKVKVIVMLTElKHGDQEICAQYWGEGKQ-------TYGDIEVD 1093
Cdd:cd17670      1 YINASYIMGYYRSNEFIITQHPLPHTTKDFWRMIWDHNAQIIVMLPD-NQGLAEDEFVYWPSREEsmnceafTVTLISKD 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622828204 1094 MKDTNKSSTYTLRVFELRHSKRKDSRTVYQYQYTNWSVEQLPAEpkELVSLIQVLKEKLPQKNSsegnkhhkstPLLIHC 1173
Cdd:cd17670     80 RLCLSNEEQIIIHDFILEATQDDYVLEVRHFQCPKWPNPDAPIS--STFELINVIKEEALTRDG----------PTIVHD 147

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 1622828204 1174 RDGSQQTGIFCALLNLLESAETEEVVDIFQVVKALRKARPGMVSTFEQYQFLYDIIAS 1231
Cdd:cd17670    148 EFGAVSAGTLCALTTLSQQLENENAVDVYQVAKMINLMRPGVFTDIEQYQFLYKAMLS 205
R-PTP-Z-2 cd17669
catalytic domain of receptor-type tyrosine-protein phosphatase Z, repeat 2; Receptor-type ...
 711-914 2.43e-24

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: 102.38  E-value: 2.43e-24
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622828204  711 YINASYIDGFKEPRKYIAAQGPRDETVDDFWRMIWEQKATVIVMVTRCEEGNRNKCAeYWPSMEEGTRAFGDVVVKINQH 790
Cdd:cd17669      1 YINASYIMGYYQSNEFIITQHPLLHTIKDFWRMIWDHNAQLIVMLPDGQNMAEDEFV-YWPNKDEPINCETFKVTLIAEE 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622828204  791 KRC----PDYIIQKLnIVNKKEKATGREVTHIQFTSWPDhgvPEDP-HLLLKLRRRVNAFSNFFSGPIVVHCSAGVGRTG 865
Cdd:cd17669     80 HKClsneEKLIIQDF-ILEATQDDYVLEVRHFQCPKWPN---PDSPiSKTFELISIIKEEAANRDGPMIVHDEHGGVTAG 155

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*....
gi 1622828204  866 TYIGIDAMLEGLEAENKVDVYGYVVKLRRQRCLMVQVEAQYILIHQALV 914
Cdd:cd17669    156 TFCALTTLMHQLEKENSVDVYQVAKMINLMRPGVFTDIEQYQFLYKAIL 204
CD45 pfam12567
Leukocyte receptor CD45; This family of proteins is found in eukaryotes. Proteins in this ...
 237-300 3.33e-24

Leukocyte receptor CD45; This family of proteins is found in eukaryotes. Proteins in this family are typically between 77 and 1130 amino acids in length. The family is found in association with pfam00041. CD45 plays a critical role in T-cell receptor (TCR)-mediated signaling. CD45 interacts with SKAP55 which is a transcriptional activator of IL-2.


Pssm-ID: 432641  Cd Length: 59  Bit Score: 96.67  E-value: 3.33e-24
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1622828204  237 VDYLYNNKTKLFTAKLNVNENVECTNNNhthniCTNNEVLNLPECKEMNVFVSHNSCTDRHKEL 300
Cdd:pfam12567    1 VEYTYNSENKSFTAKLNVNDNVECENND-----CENNELHNLQECEQINVSISHNSCTSPNKIL 59
R-PTPc-K-2 cd14636
PTP domain of receptor-type tyrosine-protein phosphatase K, repeat 2; Receptor-type ...
 711-915 5.88e-24

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


Pssm-ID: 350484 [Multi-domain]  Cd Length: 206  Bit Score: 101.26  E-value: 5.88e-24
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622828204  711 YINASYIDGFKEPRKYIAAQGPRDETVDDFWRMIWEQKATVIVMVTRCEEGnrNKCAEYWPsmEEGTRAFGDVVVKINQH 790
Cdd:cd14636      1 YINAALMDSYRQPAAFIVTQHPLPNTVKDFWRLVYDYGCTSIVMLNEVDLA--QGCPQYWP--EEGMLRYGPIQVECMSC 76

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622828204  791 KRCPDYIIQKLNIVNKKEKATGR-EVTHIQFTSWPDH-GVPEDPHLLLKLRRRVNAFS---NFFSGPIVVHCSAGVGRTG 865
Cdd:cd14636     77 SMDCDVISRIFRICNLTRPQEGYlMVQQFQYLGWASHrEVPGSKRSFLKLILQVEKWQeecDEGEGRTIIHCLNGGGRSG 156

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|
gi 1622828204  866 TYIGIDAMLEGLEAENKVDVYGYVVKLRRQRCLMVQVEAQYILIHQALVE 915
Cdd:cd14636    157 MFCAISIVCEMIKRQNVVDVFHAVKTLRNSKPNMVETPEQYRFCYDVALE 206
R-PTP-G-2 cd17670
PTP-like domain of receptor-type tyrosine-protein phosphatase G, repeat 2; Receptor-type ...
 711-914 1.21e-22

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: 97.44  E-value: 1.21e-22
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622828204  711 YINASYIDGFKEPRKYIAAQGPRDETVDDFWRMIWEQKATVIVMVTRcEEGNRNKCAEYWPSMEEGTRAFGDVVVKINQH 790
Cdd:cd17670      1 YINASYIMGYYRSNEFIITQHPLPHTTKDFWRMIWDHNAQIIVMLPD-NQGLAEDEFVYWPSREESMNCEAFTVTLISKD 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622828204  791 KRC---PDYIIQKLNIVNKKEKATGREVTHIQFTSWPDHGVPEDPHLLLKLRRRVNAFSNffSGPIVVHCSAGVGRTGTY 867
Cdd:cd17670     80 RLClsnEEQIIIHDFILEATQDDYVLEVRHFQCPKWPNPDAPISSTFELINVIKEEALTR--DGPTIVHDEFGAVSAGTL 157

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*..
gi 1622828204  868 IGIDAMLEGLEAENKVDVYGYVVKLRRQRCLMVQVEAQYILIHQALV 914
Cdd:cd17670    158 CALTTLSQQLENENAVDVYQVAKMINLMRPGVFTDIEQYQFLYKAML 204
PHA02738 PHA02738
hypothetical protein; Provisional
 969-1229 2.13e-21

hypothetical protein; Provisional


Pssm-ID: 222923 [Multi-domain]  Cd Length: 320  Bit Score: 96.92  E-value: 2.13e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622828204  969 QEENKNKNRNSNVIPYDYNRVPLKHElemskesdhdsdessdddsdsEEPSKYINASFIMSYWKPEVMIAAQGPLKETIG 1048
Cdd:PHA02738    46 EKKNRKLNRYLDAVCFDHSRVILPAE---------------------RNRGDYINANYVDGFEYKKKFICGQAPTRQTCY 104

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622828204 1049 DFWQMIFQRKVKVIVMLTELKHGDQEICAQYWGEGKQT---YGDIEVDMKDTNKSSTYTLRVFELRHSKRKdSRTVYQYQ 1125
Cdd:PHA02738   105 DFYRMLWMEHVQIIVMLCKKKENGREKCFPYWSDVEQGsirFGKFKITTTQVETHPHYVKSTLLLTDGTSA-TQTVTHFN 183

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622828204 1126 YTNWSVEQLPAEPKELVSLIQVLKE---KLPQKNSSEGNKHHKSTPLLIHCRDGSQQTGIFCALLNLLESAETEEVVDIF 1202
Cdd:PHA02738   184 FTAWPDHDVPKNTSEFLNFVLEVRQcqkELAQESLQIGHNRLQPPPIVVHCNAGLGRTPCYCVVDISISRFDACATVSIP 263

                          250       260
                   ....*....|....*....|....*..
gi 1622828204 1203 QVVKALRKARPGMVSTFEQYQFLYDII 1229
Cdd:PHA02738   264 SIVSSIRNQRYYSLFIPFQYFFCYRAV 290
R-PTPc-U-2 cd14637
PTP domain of receptor-type tyrosine-protein phosphatase U, repeat 2; Receptor-type ...
 711-915 1.34e-19

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: 88.43  E-value: 1.34e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622828204  711 YINASYIDGFKEPRKYIAAQGPRDETVDDFWRMIWEQKATVIVMVTRCEEGNRN-KCAEYWPsmEEGTRAFGDVVVKINQ 789
Cdd:cd14637      1 YINAALTDSYTRSAAFIVTLHPLQNTTTDFWRLVYDYGCTSVVMLNQLNQSNSAwPCLQYWP--EPGLQQYGPMEVEFVS 78

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622828204  790 HKRCPDYIIQKLNIVNKKEKATGR-EVTHIQFTSW-PDHGVPEDPHLLLKLRRRVNAF-SNFFSGPIVVHCSAGVGRTGT 866
Cdd:cd14637     79 GSADEDIVTRLFRVQNITRLQEGHlMVRHFQFLRWsAYRDTPDSKKAFLHLLASVEKWqRESGEGRTVVHCLNGGGRSGT 158

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*....
gi 1622828204  867 YIGIDAMLEGLEAENKVDVYGYVVKLRRQRCLMVQVEAQYILIHQALVE 915
Cdd:cd14637    159 YCASAMILEMIRCHNIVDVFYAVKTLRNYKPNMVETLEQYRFCYEIALE 207
PHA02740 PHA02740
protein tyrosine phosphatase; Provisional
 675-916 7.28e-18

protein tyrosine phosphatase; Provisional


Pssm-ID: 165107 [Multi-domain]  Cd Length: 298  Bit Score: 85.79  E-value: 7.28e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622828204  675 EARKPFNQNKNRYVD-ILPYDYNRVELSEINGDAGSNYINASYIDGFKEPRKYIAAQGPRDETVDDFWRMIWEQKATVIV 753
Cdd:PHA02740    41 EANKACAQAENKAKDeNLALHITRLLHRRIKLFNDEKVLDARFVDGYDFEQKFICIINLCEDACDKFLQALSDNKVQIIV 120

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622828204  754 MVTRCEEgnRNKCAEYWPSMEEGTRAFGDVVVKINQHKRCPDYIIQKLNIVNKKEKAtgREVTHIQFTSWPDHGVPEDPH 833
Cdd:PHA02740   121 LISRHAD--KKCFNQFWSLKEGCVITSDKFQIETLEIIIKPHFNLTLLSLTDKFGQA--QKISHFQYTAWPADGFSHDPD 196

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622828204  834 -----------LLLKLRRRvNAFSNFfsGPIVVHCSAGVGRTGTYIGIDAMLEGLEAENKVDVYGYVVKLRRQRCLMVQV 902
Cdd:PHA02740   197 afidffcniddLCADLEKH-KADGKI--APIIIDCIDGISSSAVFCVFDICATEFDKTGMLSIANALKKVRQKKYGCMNC 273

                          250
                   ....*....|....
gi 1622828204  903 EAQYILIHQALVEY 916
Cdd:PHA02740   274 LDDYVFCYHLIAAY 287
PTP_YopH-like cd14559
YopH and related bacterial protein tyrosine phosphatases; Yersinia outer protein H (YopH) ...
 712-906 1.52e-12

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: 68.58  E-value: 1.52e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622828204  712 INASYIDgFKEPRKYIAAQGPRDETVDDFWRMIWEQKATVIVMVTRCEEGNRNKCAEYWpsmeEGTRAFGDVVVKINQHK 791
Cdd:cd14559     18 LNANRVQ-IGNKNVAIACQYPKNEQLEDHLKMLADNRTPCLVVLASNKDIQRKGLPPYF----RQSGTYGSVTVKSKKTG 92

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622828204  792 rcPDYIIQKLNI------VNKKEKATGREVTHIqfTSWPDHGvPEDPHLLLKLRRRVN----------------AFSNFF 849
Cdd:cd14559     93 --KDELVDGLKAdmynlkITDGNKTITIPVVHV--TNWPDHT-AISSEGLKELADLVNksaeekrnfykskgssAINDKN 167

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 1622828204  850 SGPIVVHCSAGVGRTGTYIgidAMLEGLEAENKVDVYGYVVKLRRQRC-LMVQVEAQY 906
Cdd:cd14559    168 KLLPVIHCRAGVGRTGQLA---AAMELNKSPNNLSVEDIVSDMRTSRNgKMVQKDEQL 222
PHA02740 PHA02740
protein tyrosine phosphatase; Provisional
 1020-1230 1.36e-11

protein tyrosine phosphatase; Provisional


Pssm-ID: 165107 [Multi-domain]  Cd Length: 298  Bit Score: 66.91  E-value: 1.36e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622828204 1020 KYINASFIMSYWKPEVMIAAQGPLKETIGDFWQMIFQRKVKVIVMLTelKHGDQEICAQYWGEGKQTygdievdMKDTNK 1099
Cdd:PHA02740    77 KVLDARFVDGYDFEQKFICIINLCEDACDKFLQALSDNKVQIIVLIS--RHADKKCFNQFWSLKEGC-------VITSDK 147

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622828204 1100 SSTYTLRVFELRH---------SKRKDSRTVYQYQYTNWSVEQLPAEPKELVSLIQVLKEKLPQKNSSEGNKhhKSTPLL 1170
Cdd:PHA02740   148 FQIETLEIIIKPHfnltllsltDKFGQAQKISHFQYTAWPADGFSHDPDAFIDFFCNIDDLCADLEKHKADG--KIAPII 225

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622828204 1171 IHCRDGSQQTGIFCALLNLLESAETEEVVDIFQVVKALRKARPGMVSTFEQYQFLYDIIA 1230
Cdd:PHA02740   226 IDCIDGISSSAVFCVFDICATEFDKTGMLSIANALKKVRQKKYGCMNCLDDYVFCYHLIA 285
PTP_YopH-like cd14559
YopH and related bacterial protein tyrosine phosphatases; Yersinia outer protein H (YopH) ...
 1034-1225 4.70e-11

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: 64.34  E-value: 4.70e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622828204 1034 EVMIAAQGPLKETIGDFWQMIFQRKVKVIVMLTElkhgDQEICA----QYWGEGKqTYGDIEVDMKDTNKSS-------- 1101
Cdd:cd14559     29 NVAIACQYPKNEQLEDHLKMLADNRTPCLVVLAS----NKDIQRkglpPYFRQSG-TYGSVTVKSKKTGKDElvdglkad 103

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622828204 1102 TYTLRvfeLRHSKRKDSRTVYQYqyTNW------SVEQLpaepKELVSLIQVLKEK----LPQKNSSEGNKHHKSTPLlI 1171
Cdd:cd14559    104 MYNLK---ITDGNKTITIPVVHV--TNWpdhtaiSSEGL----KELADLVNKSAEEkrnfYKSKGSSAINDKNKLLPV-I 173

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1622828204 1172 HCRDGSQQTGIFCALLNLLESAETEEVVDIfqvVKALRKARPG-MVSTFEQYQFL 1225
Cdd:cd14559    174 HCRAGVGRTGQLAAAMELNKSPNNLSVEDI---VSDMRTSRNGkMVQKDEQLDTL 225
DUF5585 pfam17823
Family of unknown function (DUF5585); This is a family of unknown function found in chordata.
 24-237 5.89e-11

Family of unknown function (DUF5585); This is a family of unknown function found in chordata.


Pssm-ID: 465521 [Multi-domain]  Cd Length: 506  Bit Score: 66.52  E-value: 5.89e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622828204   24 TGQGSTLSPTGRRTTKMPSVPLSSDPLPTHTTAF--SPASISERENDFSETTPSLSSDNTSTHVSP----DSLDNASAFN 97
Cdd:pfam17823  116 AAAASSSPSSAAQSLPAAIAALPSEAFSAPRAAAcrANASAAPRAAIAAASAPHAASPAPRTAASSttaaSSTTAASSAP 195

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622828204   98 TTGVSSALTPHLPThadSQTPSTGTDTQTPSGS---AANTTLSPTPRSNDISDVPGERSTASTFPT------------DP 162
Cdd:pfam17823  196 TTAASSAPATLTPA---RGISTAATATGHPAAGtalAAVGNSSPAAGTVTAAVGTVTPAALATLAAaagtvasaagtiNM 272

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622828204  163 ISPLATTLIPAR----NSSAALPARTSN-----TTITANTSVSYLNASETTTPSPSGST--------VISTPTIATTTSK 225
Cdd:pfam17823  273 GDPHARRLSPAKhmpsDTMARNPAAPMGaqaqgPIIQVSTDQPVHNTAGEPTPSPSNTTlepntpksVASTNLAVVTTTK 352

                          250
                   ....*....|...
gi 1622828204  226 PTCAEKYA-TIPV 237
Cdd:pfam17823  353 AQAKEPSAsPVPV 365
Herpes_BLLF1 pfam05109
Herpes virus major outer envelope glycoprotein (BLLF1); This family consists of the BLLF1 ...
 52-236 1.47e-09

Herpes virus major outer envelope glycoprotein (BLLF1); This family consists of the BLLF1 viral late glycoprotein, also termed gp350/220. It is the most abundantly expressed glycoprotein in the viral envelope of the Herpesviruses and is the major antigen responsible for stimulating the production of neutralising antibodies in vivo.


Pssm-ID: 282904 [Multi-domain]  Cd Length: 886  Bit Score: 62.63  E-value: 1.47e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622828204   52 THTTAFSPASISerendfSETTPSLssdNTSTHVSPDSldnasafnTTGVSSalTPHLPTHAD---SQTPSTGT---DTQ 125
Cdd:pfam05109  416 THKVIFSKAPES------TTTSPTL---NTTGFAAPNT--------TTGLPS--STHVPTNLTapaSTGPTVSTadvTSP 476

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622828204  126 TPSGS---AANTTLSPTPRSNdisdvpgerSTASTFPtDPISPLATTLIPARNSSAALPARTSNT-TITANTSVSYLNAS 201
Cdd:pfam05109  477 TPAGTtsgASPVTPSPSPRDN---------GTESKAP-DMTSPTSAVTTPTPNATSPTPAVTTPTpNATSPTLGKTSPTS 546

                          170       180       190
                   ....*....|....*....|....*....|....*
gi 1622828204  202 ETTTPSPSGstviSTPTIATTTSKPTcaekyATIP 236
Cdd:pfam05109  547 AVTTPTPNA----TSPTPAVTTPTPN-----ATIP 572
DUF5585 pfam17823
Family of unknown function (DUF5585); This is a family of unknown function found in chordata.
 54-236 2.14e-09

Family of unknown function (DUF5585); This is a family of unknown function found in chordata.


Pssm-ID: 465521 [Multi-domain]  Cd Length: 506  Bit Score: 61.51  E-value: 2.14e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622828204   54 TTAFSPASISErendfSETTPSLSSDNTSTHVSPDSLDNASAFNTTGVSSALTPHLPTHADSQTPSTGTDTqTPSGSAAN 133
Cdd:pfam17823   64 TAAPAPVTLTK-----GTSAAHLNSTEVTAEHTPHGTDLSEPATREGAADGAASRALAAAASSSPSSAAQS-LPAAIAAL 137

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622828204  134 TTLSP-TPRsndiSDVPGERSTAStfptdPISPLATTLIPARNSSAALPARTSNTTITANTSVSYLNASETTTPSPSGST 212
Cdd:pfam17823  138 PSEAFsAPR----AAACRANASAA-----PRAAIAAASAPHAASPAPRTAASSTTAASSTTAASSAPTTAASSAPATLTP 208

                          170       180
                   ....*....|....*....|....
gi 1622828204  213 VISTPTIATTTSKPTCAEKYATIP 236
Cdd:pfam17823  209 ARGISTAATATGHPAAGTALAAVG 232
DUF5585 pfam17823
Family of unknown function (DUF5585); This is a family of unknown function found in chordata.
 42-227 4.57e-09

Family of unknown function (DUF5585); This is a family of unknown function found in chordata.


Pssm-ID: 465521 [Multi-domain]  Cd Length: 506  Bit Score: 60.74  E-value: 4.57e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622828204   42 SVPLSSdplpTHTTAFSPASI--------SERENDFSETTPSlsSDNTSTH----------VSPDSLDN---ASAFNTTG 100
Cdd:pfam17823   12 SLPLSE----SHAAPADPRHFvlnkmwngAGKQNASGDAVPR--ADNKSSEq*nfcaataaPAPVTLTKgtsAAHLNSTE 85

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622828204  101 VSSALTPHlpthadsqtpstGTDTQTP--SGSAANTTLS---PTPRSNDISDVPGERSTASTFPTDPISPLATTLIPARN 175
Cdd:pfam17823   86 VTAEHTPH------------GTDLSEPatREGAADGAASralAAAASSSPSSAAQSLPAAIAALPSEAFSAPRAAACRAN 153

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|..
gi 1622828204  176 SSAALPARTSNTTITANTSVSYLNASETTTPSPSGSTVISTPTIATTTSKPT 227
Cdd:pfam17823  154 ASAAPRAAIAAASAPHAASPAPRTAASSTTAASSTTAASSAPTTAASSAPAT 205
PHA03255 PHA03255
BDLF3; Provisional
 81-227 1.27e-08

BDLF3; Provisional


Pssm-ID: 165513 [Multi-domain]  Cd Length: 234  Bit Score: 57.22  E-value: 1.27e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622828204   81 TSTHVSPdsldnASAFNTTGVSSALTPHlPTHADSQTPSTGTDTQTPS------GSAANTTLSPTPrsndisdvpGERST 154
Cdd:PHA03255    25 TSSGSST-----ASAGNVTGTTAVTTPS-PSASGPSTNQSTTLTTTSApitttaILSTNTTTVTST---------GTTVT 89

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622828204  155 ASTFPTDPISPLATTLIPARNSSA-------ALPARTSNTTITANTSVSYLNASETTTPSPSGSTVISTPTIATTTSKPT 227
Cdd:PHA03255    90 PVPTTSNASTINVTTKVTAQNITAteagtgtSTGVTSNVTTRSSSTTSATTRITNATTLAPTLSSKGTSNATKTTAELPT 169
Herpes_BLLF1 pfam05109
Herpes virus major outer envelope glycoprotein (BLLF1); This family consists of the BLLF1 ...
 17-235 1.47e-08

Herpes virus major outer envelope glycoprotein (BLLF1); This family consists of the BLLF1 viral late glycoprotein, also termed gp350/220. It is the most abundantly expressed glycoprotein in the viral envelope of the Herpesviruses and is the major antigen responsible for stimulating the production of neutralising antibodies in vivo.


Pssm-ID: 282904 [Multi-domain]  Cd Length: 886  Bit Score: 59.54  E-value: 1.47e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622828204   17 LDTEVFVTGQGSTLSPTGRRTTKMPSVPLSS----------DPLPTHTTA-FSPA--SISERENDFSETTPSLSSDNTS- 82
Cdd:pfam05109  434 LNTTGFAAPNTTTGLPSSTHVPTNLTAPASTgptvstadvtSPTPAGTTSgASPVtpSPSPRDNGTESKAPDMTSPTSAv 513

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622828204   83 THVSPDSLDNASAFnTTGVSSALTPHL----PTHA------DSQTPSTGTDTQTPS------GSAANTTLSPTPRSNDIS 146
Cdd:pfam05109  514 TTPTPNATSPTPAV-TTPTPNATSPTLgktsPTSAvttptpNATSPTPAVTTPTPNatiptlGKTSPTSAVTTPTPNATS 592

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622828204  147 DVPGERS-----TASTFPTDPISPLATTliPARNSSAALPARTSNTTITANTSVSYL--NASETTTPSPSGSTVISTPTI 219
Cdd:pfam05109  593 PTVGETSpqantTNHTLGGTSSTPVVTS--PPKNATSAVTTGQHNITSSSTSSMSLRpsSISETLSPSTSDNSTSHMPLL 670

                          250
                   ....*....|....*.
gi 1622828204  220 atTTSKPTCAEKYATI 235
Cdd:pfam05109  671 --TSAHPTGGENITQV 684
Chi1 COG3469
Chitinase [Carbohydrate transport and metabolism];
24-227 4.10e-08

Chitinase [Carbohydrate transport and metabolism];


Pssm-ID: 442692 [Multi-domain]  Cd Length: 534  Bit Score: 57.46  E-value: 4.10e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622828204   24 TGQGSTLSPTGRRTTKMPSVPLSSDPLPTHTTAFSPASISERENDFSETTPSLSSDNTSTHVSPDSLDNASAFNTTGVSS 103
Cdd:COG3469     15 ASATAVTLLGAAATAASVTLTAATATTVVSTTGSVVVAASGSAGSGTGTTAASSTAATSSTTSTTATATAAAAAATSTSA 94

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622828204  104 ALTPHLPTHADSQTPSTGTDTQTPSGSAANTTLSPTPRSNDISDVPGERSTASTFPTDPISPLATTliparnsSAALPAR 183
Cdd:COG3469     95 TLVATSTASGANTGTSTVTTTSTGAGSVTSTTSSTAGSTTTSGASATSSAGSTTTTTTVSGTETAT-------GGTTTTS 167

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....
gi 1622828204  184 TSNTTITANTSVSYLNASETTTPSPSGSTviSTPTIATTTSKPT 227
Cdd:COG3469    168 TTTTTTSASTTPSATTTATATTASGATTP--SATTTATTTGPPT 209
DUF5585 pfam17823
Family of unknown function (DUF5585); This is a family of unknown function found in chordata.
 24-236 3.72e-07

Family of unknown function (DUF5585); This is a family of unknown function found in chordata.


Pssm-ID: 465521 [Multi-domain]  Cd Length: 506  Bit Score: 54.58  E-value: 3.72e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622828204   24 TGQGSTLS-PTGRR------TTKMPSVPLSSdplpthttafSPASISErendfseTTPSLSSDNTSTHVSPDSLDNASAF 96
Cdd:pfam17823   91 TPHGTDLSePATREgaadgaASRALAAAASS----------SPSSAAQ-------SLPAAIAALPSEAFSAPRAAACRAN 153

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622828204   97 NTTGVSSALTPHLPTHADSQTPSTGTDTQTPSGSAANTTLSPTprsndisdvPGERSTASTF-PTDPISPLAT-TLIPAr 174
Cdd:pfam17823  154 ASAAPRAAIAAASAPHAASPAPRTAASSTTAASSTTAASSAPT---------TAASSAPATLtPARGISTAATaTGHPA- 223

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1622828204  175 nSSAALpARTSNTTITANTSVSylnASETTTPSPSGSTVISTPTIATTTSKPTCAEKYATIP 236
Cdd:pfam17823  224 -AGTAL-AAVGNSSPAAGTVTA---AVGTVTPAALATLAAAAGTVASAAGTINMGDPHARRL 280
CDC14 COG2453
Protein-tyrosine phosphatase [Signal transduction mechanisms];
823-911 5.72e-07

Protein-tyrosine phosphatase [Signal transduction mechanisms];


Pssm-ID: 441989 [Multi-domain]  Cd Length: 140  Bit Score: 50.35  E-value: 5.72e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622828204  823 WPDHGVPEDPHL---LLKLRRRVNAfsnffSGPIVVHCSAGVGRTGTYIGIDAMLEGLEAENKVDvygyvvKLRRQRCLM 899
Cdd:COG2453     55 IPDFGAPDDEQLqeaVDFIDEALRE-----GKKVLVHCRGGIGRTGTVAAAYLVLLGLSAEEALA------RVRAARPGA 123

                           90
                   ....*....|..
gi 1622828204  900 VQVEAQYILIHQ 911
Cdd:COG2453    124 VETPAQRAFLER 135
PHA03255 PHA03255
BDLF3; Provisional
 115-252 1.10e-06

BDLF3; Provisional


Pssm-ID: 165513 [Multi-domain]  Cd Length: 234  Bit Score: 51.44  E-value: 1.10e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622828204  115 SQTPSTGTDTQTpSGSAANTTLSPTPRSNDISDVPGERSTASTFPTDPISPLATTLIPARNSSAALPARTSN-------T 187
Cdd:PHA03255    26 SSGSSTASAGNV-TGTTAVTTPSPSASGPSTNQSTTLTTTSAPITTTAILSTNTTTVTSTGTTVTPVPTTSNastinvtT 104

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1622828204  188 TITANTSVSYLNASETTTPSPSGSTVISTPTI-ATT------TSKPTCAEKYAtipvdylyNNKTKLfTAKL 252
Cdd:PHA03255   105 KVTAQNITATEAGTGTSTGVTSNVTTRSSSTTsATTritnatTLAPTLSSKGT--------SNATKT-TAEL 167
PTP_N pfam12453
Protein tyrosine phosphatase N terminal; This domain family is found in eukaryotes, and is ...
 7-32 1.15e-06

Protein tyrosine phosphatase N terminal; This domain family is found in eukaryotes, and is approximately 30 amino acids in length. The family is found in association with pfam00041. There is a single completely conserved residue L that may be functionally important. This family consists of various protein tyrosine phosphatase haematopoietic receptors, e.g. CD45, which dephosphorylate growth stimulating proteins. This limits growth signalling in haematopoietic cells.


Pssm-ID: 403599  Cd Length: 26  Bit Score: 45.99  E-value: 1.15e-06
                           10        20
                   ....*....|....*....|....*.
gi 1622828204    7 LKLLAFVFAFLDTEVFVTGQGSTLSP 32
Cdd:pfam12453    1 LKLLAFGFAFLDTEVFVTGESLTSST 26
Chi1 COG3469
Chitinase [Carbohydrate transport and metabolism];
72-237 1.46e-06

Chitinase [Carbohydrate transport and metabolism];


Pssm-ID: 442692 [Multi-domain]  Cd Length: 534  Bit Score: 52.45  E-value: 1.46e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622828204   72 TTPSLSSDNTSTHVSPDSLDNASAFNTTGVSSALTPHLPTHADS---QTPSTGTDTQTPSGSAANTTLSPTPRSNDISDV 148
Cdd:COG3469     32 VTLTAATATTVVSTTGSVVVAASGSAGSGTGTTAASSTAATSSTtstTATATAAAAAATSTSATLVATSTASGANTGTST 111

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622828204  149 PGERSTASTFPTDPISPLATTLIPARNSSAALPARTSNTTITANTSVSYLNASE--TTTPSPSGSTVISTPTIATTTSKP 226
Cdd:COG3469    112 VTTTSTGAGSVTSTTSSTAGSTTTSGASATSSAGSTTTTTTVSGTETATGGTTTtsTTTTTTSASTTPSATTTATATTAS 191

                          170
                   ....*....|.
gi 1622828204  227 TCAEKYATIPV 237
Cdd:COG3469    192 GATTPSATTTA 202
PHA03255 PHA03255
BDLF3; Provisional
 28-162 1.65e-06

BDLF3; Provisional


Pssm-ID: 165513 [Multi-domain]  Cd Length: 234  Bit Score: 50.67  E-value: 1.65e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622828204   28 STLSPTGRRTTKMPSVPLSSDPLPTHTTAFSPASISERENDFSETTPSLSSDNTSThvsPDSLDNASAFNTTGVSSALTP 107
Cdd:PHA03255    44 TTPSPSASGPSTNQSTTLTTTSAPITTTAILSTNTTTVTSTGTTVTPVPTTSNAST---INVTTKVTAQNITATEAGTGT 120

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1622828204  108 HLPTHADSQTPSTGTDTQTPSGSAAnTTLSPTPRSNDISDVpgERSTAStFPTDP 162
Cdd:PHA03255   121 STGVTSNVTTRSSSTTSATTRITNA-TTLAPTLSSKGTSNA--TKTTAE-LPTVP 171
CDKN3-like cd14505
cyclin-dependent kinase inhibitor 3 and similar proteins; This family is composed of ...
 1083-1227 2.16e-06

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


Pssm-ID: 350355 [Multi-domain]  Cd Length: 163  Bit Score: 49.18  E-value: 2.16e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622828204 1083 GKQTYGDIEVDMKDTNKSSTYTLRVF----ELRHSKRKDSRTVYQYQYTNWSveQLPAE----PKELVSLIQVLKEKLPQ 1154
Cdd:cd14505     25 FKDHRRDLQADLEELKDQGVDDVVTLctdgELEELGVPDLLEQYQQAGITWH--HLPIPdggvPSDIAQWQELLEELLSA 102

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1622828204 1155 KNSSEGnkhhkstpLLIHCRDGSQQTGIFCA--LLNLLESAETEevvdifQVVKALRKARPGMVSTFEQYQFLYD 1227
Cdd:cd14505    103 LENGKK--------VLIHCKGGLGRTGLIAAclLLELGDTLDPE------QAIAAVRALRPGAIQTPKQENFLHQ 163
fn3 pfam00041
Fibronectin type III domain;
398-467 2.96e-06

Fibronectin type III domain;


Pssm-ID: 394996 [Multi-domain]  Cd Length: 85  Bit Score: 46.64  E-value: 2.96e-06
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1622828204  398 GQPQNVVCRHEDAHQGVITWNPP---QRSFHNFTLCYVSK---TAKKCLSLDKHLTTYHLQNLKPYTNYSLSLHAY 467
Cdd:pfam00041    1 SAPSNLTVTDVTSTSLTVSWTPPpdgNGPITGYEVEYRPKnsgEPWNEITVPGTTTSVTLTGLKPGTEYEVRVQAV 76
PHA03255 PHA03255
BDLF3; Provisional
 58-212 3.73e-06

BDLF3; Provisional


Pssm-ID: 165513 [Multi-domain]  Cd Length: 234  Bit Score: 49.90  E-value: 3.73e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622828204   58 SPASISERENDFSETTPSLSSDNTSTH--------VSPDSLDNASAFNTTGVSSALT--PHLPTHADSQTPSTGTD--TQ 125
Cdd:PHA03255    30 STASAGNVTGTTAVTTPSPSASGPSTNqsttltttSAPITTTAILSTNTTTVTSTGTtvTPVPTTSNASTINVTTKvtAQ 109

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622828204  126 TPSGSAANTTLSPTPRSNDISdvpgeRSTASTFPTDPISPlATTLIPARNSSAalparTSNTTITantsvsylnASETTT 205
Cdd:PHA03255   110 NITATEAGTGTSTGVTSNVTT-----RSSSTTSATTRITN-ATTLAPTLSSKG-----TSNATKT---------TAELPT 169

                          170
                   ....*....|.
gi 1622828204  206 P----SPSGST 212
Cdd:PHA03255   170 VpderQPSLSY 180
FN3 cd00063
Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein ...
 397-467 4.30e-06

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


Pssm-ID: 238020 [Multi-domain]  Cd Length: 93  Bit Score: 46.34  E-value: 4.30e-06
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1622828204  397 PGQPQNVVCRHEDAHQGVITWNPPQRS---FHNFTLCYVSKTAKKCLSLDKHL---TTYHLQNLKPYTNYSLSLHAY 467
Cdd:cd00063      1 PSPPTNLRVTDVTSTSVTLSWTPPEDDggpITGYVVEYREKGSGDWKEVEVTPgseTSYTLTGLKPGTEYEFRVRAV 77
PRK10118 PRK10118
flagellar hook length control protein FliK;
45-237 2.99e-05

flagellar hook length control protein FliK;


Pssm-ID: 236652 [Multi-domain]  Cd Length: 408  Bit Score: 47.94  E-value: 2.99e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622828204   45 LSSDPLPTHTTAFSPASISERENDfseTTPSLSSDNTSthvspdSLdnasafnttgvsSALTPHLPtHADSQTPSTGTDT 124
Cdd:PRK10118   107 SSPLTPALKTSALAALSKNAQKDE---KADDLSDEDLA------SL------------SALFAMLP-GQDNTTPVADAPS 164

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622828204  125 QTpSGSAANTTLSPTPRSNDISDVPGERSTASTfpTDPISPLATTLIPARNSSAALparTSNTTITANTSVSylnASETT 204
Cdd:PRK10118   165 TV-LPAEKPTLLTKDMPSAPQDETHTLSSDEHE--KGLTSAQLTTAQPDDAPGTPA---QPLTPLAAEAQAK---AEVIS 235

                          170       180       190
                   ....*....|....*....|....*....|...
gi 1622828204  205 TPSPSGSTVISTPTIATTTSKPTcaekyATIPV 237
Cdd:PRK10118   236 TPSPVTAAASPTITPHQTQPLPT-----AAAPV 263
FN3 smart00060
Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, ...
 397-467 1.31e-04

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


Pssm-ID: 214495 [Multi-domain]  Cd Length: 83  Bit Score: 41.83  E-value: 1.31e-04
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1622828204   397 PGQPQNVVCRHEDAHQGVITWNPPQRSFHN-----FTLCYVSKTAK-KCLSLDKHLTTYHLQNLKPYTNYSLSLHAY 467
Cdd:smart00060    1 PSPPSNLRVTDVTSTSVTLSWEPPPDDGITgyivgYRVEYREEGSEwKEVNVTPSSTSYTLTGLKPGTEYEFRVRAV 77
PTP_DSP_cys cd14494
cys-based protein tyrosine phosphatase and dual-specificity phosphatase superfamily; This ...
 851-896 1.48e-04

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: 42.72  E-value: 1.48e-04
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*.
gi 1622828204  851 GPIVVHCSAGVGRTGTYIGIDAMLEGleaenKVDVYGYVVKLRRQR 896
Cdd:cd14494     57 EPVLVHCKAGVGRTGTLVACYLVLLG-----GMSAEEAVRIVRLIR 97
FN3 cd00063
Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein ...
 490-570 2.47e-04

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


Pssm-ID: 238020 [Multi-domain]  Cd Length: 93  Bit Score: 41.33  E-value: 2.47e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622828204  490 PSQVQNMIVS-TSDNSMRVKCEAPRDVNGPTELYLLEVEAGN----TLVRNLSQSECDFSVNNLQYSTYYNLKAYYHNGK 564
Cdd:cd00063      1 PSPPTNLRVTdVTSTSVTLSWTPPEDDGGPITGYVVEYREKGsgdwKEVEVTPGSETSYTLTGLKPGTEYEFRVRAVNGG 80


                   ....*.
gi 1622828204  565 YSGEPV 570
Cdd:cd00063     81 GESPPS 86
PTP_DSP_cys cd14494
cys-based protein tyrosine phosphatase and dual-specificity phosphatase superfamily; This ...
 1168-1227 3.22e-04

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: 41.57  E-value: 3.22e-04
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1622828204 1168 PLLIHCRDGSQQTGIFCALLNLLESAETeevvdIFQVVKALRKARPGMVS-TFEQYQFLYD 1227
Cdd:cd14494     58 PVLVHCKAGVGRTGTLVACYLVLLGGMS-----AEEAVRIVRLIRPGGIPqTIEQLDFLIK 113
PHA03307 PHA03307
transcriptional regulator ICP4; Provisional
 24-236 6.34e-04

transcriptional regulator ICP4; Provisional


Pssm-ID: 223039 [Multi-domain]  Cd Length: 1352  Bit Score: 44.39  E-value: 6.34e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622828204   24 TGQGSTLSPTGRRTTKMPSVPLSSDPLPTHTTAfSPASISErendfseTTPSLSSDNTSTHVSPDSLDNASAFNTTGVSS 103
Cdd:PHA03307    89 TWSLSTLAPASPAREGSPTPPGPSSPDPPPPTP-PPASPPP-------SPAPDLSEMLRPVGSPGPPPAASPPAAGASPA 160

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622828204  104 ALTPHLPTHADSQTPStgtdtqtPSGSAANTTLSPTPRSNDISDVPGERSTASTFPTDPISPLATTLIPARNSSAALPAR 183
Cdd:PHA03307   161 AVASDAASSRQAALPL-------SSPEETARAPSSPPAEPPPSTPPAAASPRPPRRSSPISASASSPAPAPGRSAADDAG 233

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 1622828204  184 TSNTTITANTSVSYLNASETTTPSPSGSTVISTPTIAT------TTSKPTCAEKYATIP 236
Cdd:PHA03307   234 ASSSDSSSSESSGCGWGPENECPLPRPAPITLPTRIWEasgwngPSSRPGPASSSSSPR 292
PHA03307 PHA03307
transcriptional regulator ICP4; Provisional
 26-232 8.96e-04

transcriptional regulator ICP4; Provisional


Pssm-ID: 223039 [Multi-domain]  Cd Length: 1352  Bit Score: 44.01  E-value: 8.96e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622828204   26 QGSTLSPTGRRTTKMPSVP-LSSDPLPTHTTAFSPasisERENDFSETTPSLSSDNTSTHVSPDSLDNASAFNT---TGV 101
Cdd:PHA03307   198 PPAAASPRPPRRSSPISASaSSPAPAPGRSAADDA----GASSSDSSSSESSGCGWGPENECPLPRPAPITLPTriwEAS 273

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622828204  102 SSALTPHLPTHADSQTPSTGTDTQTPSGSAANTTLSPTPRSNDISDVPGERSTASTFPTDPISPLATTLIPARNSSAALP 181
Cdd:PHA03307   274 GWNGPSSRPGPASSSSSPRERSPSPSPSSPGSGPAPSSPRASSSSSSSRESSSSSTSSSSESSRGAAVSPGPSPSRSPSP 353

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|.
gi 1622828204  182 ARTSNTTITANTSvsylNASETTTPSPSGSTVISTPTIATTtsKPTCAEKY 232
Cdd:PHA03307   354 SRPPPPADPSSPR----KRPRPSRAPSSPAASAGRPTRRRA--RAAVAGRA 398
fn3 pfam00041
Fibronectin type III domain;
491-569 1.23e-03

Fibronectin type III domain;


Pssm-ID: 394996 [Multi-domain]  Cd Length: 85  Bit Score: 39.32  E-value: 1.23e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622828204  491 SQVQNMIVS-TSDNSMRVKCEAPRDVNGPTELYLLEVEAGNT----LVRNLSQSECDFSVNNLQYSTYYNLKAYYHNGKY 565
Cdd:pfam00041    1 SAPSNLTVTdVTSTSLTVSWTPPPDGNGPITGYEVEYRPKNSgepwNEITVPGTTTSVTLTGLKPGTEYEVRVQAVNGGG 80


                   ....
gi 1622828204  566 SGEP 569
Cdd:pfam00041   81 EGPP 84
CDC14_C cd14499
C-terminal dual-specificity phosphatase domain of CDC14 family proteins; The cell division ...
 851-873 1.24e-03

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


Pssm-ID: 350349 [Multi-domain]  Cd Length: 174  Bit Score: 41.28  E-value: 1.24e-03
                           10        20
                   ....*....|....*....|...
gi 1622828204  851 GPIVVHCSAGVGRTGTYIGIDAM 873
Cdd:cd14499    110 GAIAVHCKAGLGRTGTLIACYLM 132
COG4935 COG4935
Regulatory P domain of the subtilisin-like proprotein convertases and other proteases ...
 11-224 2.32e-03

Regulatory P domain of the subtilisin-like proprotein convertases and other proteases [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 443962 [Multi-domain]  Cd Length: 641  Bit Score: 42.12  E-value: 2.32e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622828204   11 AFVFAFLDTEVFVTGQGSTLSPTGRRTTKMPSVPLSSdplpthTTAFSPASISERENDFSETTPSLSSDNTSTHVSPDSL 90
Cdd:COG4935    349 ASVVAGASGGGAGTAAAAGGGAAAAAAGGAAAAGAAA------GAAAGAAAGAAAAGGVASAAGAVGAGTAAGASATAAV 422

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622828204   91 DNASAFNTTGVSSALTPHLPTHADSQTPSTGTDTQTPSGSAANTTLSPTPRSNDISDVPGERSTASTFPTDPISPLATTL 170
Cdd:COG4935    423 STGAASGSSTTSSTGTTATATGLGGGADAGSTSTGTGSAAGAAGGTTTATSGLASSTTAAAAAAAAGLATTAAVAAGAAG 502

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....
gi 1622828204  171 IPARNSSAALPARTSNTTITANTSVSYLNASETTTPSPSGSTVISTPTIATTTS 224
Cdd:COG4935    503 AAAAAATAASVGGATGAAGTTNSTATFSNTTDVAIPDNGPAGVTSTITVSGGGA 556
CDC14 COG2453
Protein-tyrosine phosphatase [Signal transduction mechanisms];
1168-1228 2.44e-03

Protein-tyrosine phosphatase [Signal transduction mechanisms];


Pssm-ID: 441989 [Multi-domain]  Cd Length: 140  Bit Score: 39.57  E-value: 2.44e-03
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1622828204 1168 PLLIHCRDGSQQTGIFCALLNLLESAETEEVVdifqvvKALRKARPGMVSTFEQYQFLYDI 1228
Cdd:COG2453     82 KVLVHCRGGIGRTGTVAAAYLVLLGLSAEEAL------ARVRAARPGAVETPAQRAFLERF 136
TpbA-like cd14529
bacterial protein tyrosine and dual-specificity phosphatases related to Pseudomonas aeruginosa ...
 808-939 3.33e-03

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


Pssm-ID: 350378 [Multi-domain]  Cd Length: 158  Bit Score: 39.66  E-value: 3.33e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622828204  808 EKATGREVTHIQFTSWpdhgVPEDPHLLLKLRRRVNAFSNffsGPIVVHCSAGVGRTGTYIGIdamlegleaenkvdvYG 887
Cdd:cd14529     54 AKIDGVKYVNLPLSAT----RPTESDVQSFLLIMDLKLAP---GPVLIHCKHGKDRTGLVSAL---------------YR 111

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|..
gi 1622828204  888 YVVKLRRQrclmvQVEAQYILIHQALVEYNQFGETEVNLSELHPYLHNMKKR 939
Cdd:cd14529    112 IVYGGSKE-----EANEDYRLSNRHLEGLRSGIALDSKGGVKGRYLAAYFER 158
DUSP23 cd14504
dual specificity phosphatase 23; Dual specificity phosphatase 23 (DUSP23), also known as ...
 847-905 4.26e-03

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: 39.18  E-value: 4.26e-03
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1622828204  847 NFFSGPIVVHCSAGVGRTGT----YIGIDAMLEGLEAenkvdvygyVVKLRRQRCLMVQVEAQ 905
Cdd:cd14504     79 NAKNEAVLVHCLAGKGRTGTmlacYLVKTGKISAVDA---------INEIRRIRPGSIETSEQ 132
PTP_PTPDC1 cd14506
protein tyrosine phosphatase domain of PTP domain-containing protein 1; protein tyrosine ...
 822-868 5.81e-03

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


Pssm-ID: 350356 [Multi-domain]  Cd Length: 206  Bit Score: 39.64  E-value: 5.81e-03
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*..
gi 1622828204  822 SWPDHGVPEdPHLLLKLRRrVNAFSNFFSGPIVVHCSAGVGRTGTYI 868
Cdd:cd14506     83 GWKDYGVPS-LTTILDIVK-VMAFALQEGGKVAVHCHAGLGRTGVLI 127
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

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