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Conserved domains on  [gi|578801329|ref|XP_006711535|]
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receptor-type tyrosine-protein phosphatase C isoform X2 [Homo sapiens]

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 ...
 659-859 9.67e-150

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: 448.89  E-value: 9.67e-150
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578801329  659 YINASYIDGFKEPRKYIAAQGPRDETVDDFWRMIWEQKATVIVMVTRCEEGNRNKCAEYWPSMEEGTRAFGDVVVKINQH 738
Cdd:cd14557     1 YINASYIDGFKEPRKYIAAQGPKDETVDDFWRMIWEQKSTVIVMVTRCEEGNRNKCAQYWPSMEEGSRAFGDVVVKINEE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578801329  739 KRCPDYIIQKLNIVNKKEKATGREVTHIQFTSWPDHGVPEDPHLLLKLRRRVNAFSNFFSGPIVVHCSAGVGRTGTYIGI 818
Cdd:cd14557    81 KICPDYIIRKLNINNKKEKGSGREVTHIQFTSWPDHGVPEDPHLLLKLRRRVNAFNNFFSGPIVVHCSAGVGRTGTYIGI 160

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|.
gi 578801329  819 DAMLEGLEAENKVDVYGYVVKLRRQRCLMVQVEAQYILIHQ 859
Cdd:cd14557   161 DAMLEGLEAEGRVDVYGYVVKLRRQRCLMVQVEAQYILIHQ 201
R-PTP-C-2 cd14558
PTP-like domain of receptor-type tyrosine-protein phosphatase C, repeat 2; Receptor-type ...
 969-1175 2.74e-129

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: 394.84  E-value: 2.74e-129
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578801329  969 YINASFIMSYWKPEVMIAAQGPLKETIGDFWQMIFQRKVKVIVMLTELKHGDQEICAQYWGEGKQTYGDIEVDLKDTDKS 1048
Cdd:cd14558     1 YINASFIDGYWGPKSLIATQGPLPDTIADFWQMIFQKKVKVIVMLTELKEGDQEQCAQYWGDEKKTYGDIEVELKDTEKS 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578801329 1049 STYTLRVFELRHSKRKDSRTVYQYQYTNWSVEQLPAEPKELISMIQVVKQKLPQKNSsegnKHHKSTPLLIHCRDGSQQT 1128
Cdd:cd14558    81 PTYTVRVFEITHLKRKDSRTVYQYQYHKWKGEELPEKPKDLVDMIKSIKQKLPYKNS----KHGRSVPIVVHCSDGSSRT 156

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*..
gi 578801329 1129 GIFCALLNLLESAETEEVVDIFQVVKALRKARPGMVSTFEQYQFLYD 1175
Cdd:cd14558   157 GIFCALWNLLESAETEKVVDVFQVVKALRKQRPGMVSTLEQYQFLYD 203
CD45 pfam12567
Leukocyte receptor CD45; This family of proteins is found in eukaryotes. Proteins in this ...
 189-247 1.54e-29

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: 111.69  E-value: 1.54e-29
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 578801329   189 VDYLYNKETKLFTAKLNVNENVECGNNTCTNNEVHNLTECKNASVSISHNSCTAPDKTL 247
Cdd:pfam12567    1 VEYTYNSENKSFTAKLNVNDNVECENNDCENNELHNLQECEQINVSISHNSCTSPNKIL 59
PHA03255 super family cl31530
BDLF3; Provisional
 18-183 2.53e-10

BDLF3; Provisional


The actual alignment was detected with superfamily member PHA03255:

Pssm-ID: 165513 [Multi-domain]  Cd Length: 234  Bit Score: 62.23  E-value: 2.53e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578801329   18 DTEVFVTGQSPTP-SPTGLTTAKMPSVPLSSDPLP------THTTAFSPAstferendfseTTTSLSPDNTSTQVSPDSl 90
Cdd:PHA03255   19 ETSLIWTSSGSSTaSAGNVTGTTAVTTPSPSASGPstnqstTLTTTSAPI-----------TTTAILSTNTTTVTSTGT- 86

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578801329   91 dNASAFNTTgvSSVQTPHLPTHADSQT---PSAGTDTQTFSGSaanaklNPTPGSNAISDAYLNASETTTLSPSGSAVIS 167
Cdd:PHA03255   87 -TVTPVPTT--SNASTINVTTKVTAQNitaTEAGTGTSTGVTS------NVTTRSSSTTSATTRITNATTLAPTLSSKGT 157

                         170
                  ....*....|....*..
gi 578801329  168 TTTIATTPSKPTC-DEK 183
Cdd:PHA03255  158 SNATKTTAELPTVpDER 174
FN3 cd00063
Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein ...
 437-517 1.96e-09

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: 55.97  E-value: 1.96e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578801329  437 PSQVWNMTVSMTSDNSMHVKCRPPRDRNGPHERYHLEVEAGN----TLVRNESHKNCDFRVKDLQYSTDYTFKAYFHNGD 512
Cdd:cd00063     1 PSPPTNLRVTDVTSTSVTLSWTPPEDDGGPITGYVVEYREKGsgdwKEVEVTPGSETSYTLTGLKPGTEYEFRVRAVNGG 80


                  ....*
gi 578801329  513 YPGEP 517
Cdd:cd00063    81 GESPP 85
fn3 pfam00041
Fibronectin type III domain;
345-414 4.61e-05

Fibronectin type III domain;


:

Pssm-ID: 394996 [Multi-domain]  Cd Length: 85  Bit Score: 43.17  E-value: 4.61e-05
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 578801329   345 GEPQIIFCRSEAAHQGVITWNPP---QRSFHNFTLCYIKETEKDC---LNLDKNLIKYDLQNLKPYTKYVLSLHAY 414
Cdd:pfam00041    1 SAPSNLTVTDVTSTSLTVSWTPPpdgNGPITGYEVEYRPKNSGEPwneITVPGTTTSVTLTGLKPGTEYEVRVQAV 76
 
Name Accession Description Interval E-value
R-PTPc-C-1 cd14557
catalytic domain of receptor-type tyrosine-protein phosphatase C, repeat 1; Receptor-type ...
 659-859 9.67e-150

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: 448.89  E-value: 9.67e-150
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578801329  659 YINASYIDGFKEPRKYIAAQGPRDETVDDFWRMIWEQKATVIVMVTRCEEGNRNKCAEYWPSMEEGTRAFGDVVVKINQH 738
Cdd:cd14557     1 YINASYIDGFKEPRKYIAAQGPKDETVDDFWRMIWEQKSTVIVMVTRCEEGNRNKCAQYWPSMEEGSRAFGDVVVKINEE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578801329  739 KRCPDYIIQKLNIVNKKEKATGREVTHIQFTSWPDHGVPEDPHLLLKLRRRVNAFSNFFSGPIVVHCSAGVGRTGTYIGI 818
Cdd:cd14557    81 KICPDYIIRKLNINNKKEKGSGREVTHIQFTSWPDHGVPEDPHLLLKLRRRVNAFNNFFSGPIVVHCSAGVGRTGTYIGI 160

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|.
gi 578801329  819 DAMLEGLEAENKVDVYGYVVKLRRQRCLMVQVEAQYILIHQ 859
Cdd:cd14557   161 DAMLEGLEAEGRVDVYGYVVKLRRQRCLMVQVEAQYILIHQ 201
R-PTP-C-2 cd14558
PTP-like domain of receptor-type tyrosine-protein phosphatase C, repeat 2; Receptor-type ...
 969-1175 2.74e-129

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: 394.84  E-value: 2.74e-129
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578801329  969 YINASFIMSYWKPEVMIAAQGPLKETIGDFWQMIFQRKVKVIVMLTELKHGDQEICAQYWGEGKQTYGDIEVDLKDTDKS 1048
Cdd:cd14558     1 YINASFIDGYWGPKSLIATQGPLPDTIADFWQMIFQKKVKVIVMLTELKEGDQEQCAQYWGDEKKTYGDIEVELKDTEKS 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578801329 1049 STYTLRVFELRHSKRKDSRTVYQYQYTNWSVEQLPAEPKELISMIQVVKQKLPQKNSsegnKHHKSTPLLIHCRDGSQQT 1128
Cdd:cd14558    81 PTYTVRVFEITHLKRKDSRTVYQYQYHKWKGEELPEKPKDLVDMIKSIKQKLPYKNS----KHGRSVPIVVHCSDGSSRT 156

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*..
gi 578801329 1129 GIFCALLNLLESAETEEVVDIFQVVKALRKARPGMVSTFEQYQFLYD 1175
Cdd:cd14558   157 GIFCALWNLLESAETEKVVDVFQVVKALRKQRPGMVSTLEQYQFLYD 203
PTPc smart00194
Protein tyrosine phosphatase, catalytic domain;
604-863 2.98e-111

Protein tyrosine phosphatase, catalytic domain;


Pssm-ID: 214550 [Multi-domain]  Cd Length: 259  Bit Score: 348.88  E-value: 2.98e-111
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578801329    604 LFLAEFQSIPRVFS-KFPIKEARKPFNQNKNRYVDILPYDYNRVELSEINGDaGSNYINASYIDGFKEPRKYIAAQGPRD 682
Cdd:smart00194    1 GLEEEFEKLDRLKPdDESCTVAAFPENRDKNRYKDVLPYDHTRVKLKPPPGE-GSDYINASYIDGPNGPKAYIATQGPLP 79

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578801329    683 ETVDDFWRMIWEQKATVIVMVTRCEEGNRNKCAEYWPSMEEGTRAFGDVVVKINQHKRCPDYIIQKLNIVNKKEKATgRE 762
Cdd:smart00194   80 STVEDFWRMVWEQKVTVIVMLTELVEKGREKCAQYWPDEEGEPLTYGDITVTLKSVEKVDDYTIRTLEVTNTGCSET-RT 158

                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578801329    763 VTHIQFTSWPDHGVPEDPHLLLKLRRRVNAFSNFFSGPIVVHCSAGVGRTGTYIGIDAMLEGLEAENKVDVYGYVVKLRR 842
Cdd:smart00194  159 VTHYHYTNWPDHGVPESPESILDLIRAVRKSQSTSTGPIVVHCSAGVGRTGTFIAIDILLQQLEAGKEVDIFEIVKELRS 238

                           250       260
                    ....*....|....*....|.
gi 578801329    843 QRCLMVQVEAQYILIHQALVE 863
Cdd:smart00194  239 QRPGMVQTEEQYIFLYRAILE 259
Y_phosphatase pfam00102
Protein-tyrosine phosphatase;
629-863 3.45e-107

Protein-tyrosine phosphatase;


Pssm-ID: 459674 [Multi-domain]  Cd Length: 234  Bit Score: 336.91  E-value: 3.45e-107
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578801329   629 NQNKNRYVDILPYDYNRVELSEINGDagSNYINASYIDGFKEPRKYIAAQGPRDETVDDFWRMIWEQKATVIVMVTRCEE 708
Cdd:pfam00102    1 NLEKNRYKDVLPYDHTRVKLTGDPGP--SDYINASYIDGYKKPKKYIATQGPLPNTVEDFWRMVWEEKVTIIVMLTELEE 78

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578801329   709 GNRNKCAEYWPSMEEGTRAFGDVVVKI-NQHKRCPDYIIQKLNIVNKKEKATgREVTHIQFTSWPDHGVPEDPHLLLKLR 787
Cdd:pfam00102   79 KGREKCAQYWPEEEGESLEYGDFTVTLkKEKEDEKDYTVRTLEVSNGGSEET-RTVKHFHYTGWPDHGVPESPNSLLDLL 157

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 578801329   788 RRVNAFSN-FFSGPIVVHCSAGVGRTGTYIGIDAMLEGLEAENKVDVYGYVVKLRRQRCLMVQVEAQYILIHQALVE 863
Cdd:pfam00102  158 RKVRKSSLdGRSGPIVVHCSAGIGRTGTFIAIDIALQQLEAEGEVDIFQIVKELRSQRPGMVQTLEQYIFLYDAILE 234
PTPc smart00194
Protein tyrosine phosphatase, catalytic domain;
896-1178 2.64e-96

Protein tyrosine phosphatase, catalytic domain;


Pssm-ID: 214550 [Multi-domain]  Cd Length: 259  Bit Score: 308.43  E-value: 2.64e-96
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578801329    896 LEAEFQRLPSYRSW-RTQHIGNQEENKSKNRNSNVIPYDYNRVPLKHELEmskesehdsdessdddsdseEPSKYINASF 974
Cdd:smart00194    2 LEEEFEKLDRLKPDdESCTVAAFPENRDKNRYKDVLPYDHTRVKLKPPPG--------------------EGSDYINASY 61

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578801329    975 IMSYWKPEVMIAAQGPLKETIGDFWQMIFQRKVKVIVMLTELKHGDQEICAQYW---GEGKQTYGDIEVDLKDTDKSSTY 1051
Cdd:smart00194   62 IDGPNGPKAYIATQGPLPSTVEDFWRMVWEQKVTVIVMLTELVEKGREKCAQYWpdeEGEPLTYGDITVTLKSVEKVDDY 141

                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578801329   1052 TLRVFELRHSKRKDSRTVYQYQYTNWSVEQLPAEPKELISMIQVVKQKLPqknssegnkhHKSTPLLIHCRDGSQQTGIF 1131
Cdd:smart00194  142 TIRTLEVTNTGCSETRTVTHYHYTNWPDHGVPESPESILDLIRAVRKSQS----------TSTGPIVVHCSAGVGRTGTF 211

                           250       260       270       280
                    ....*....|....*....|....*....|....*....|....*..
gi 578801329   1132 CALLNLLESAETEEVVDIFQVVKALRKARPGMVSTFEQYQFLYDVIA 1178
Cdd:smart00194  212 IAIDILLQQLEAGKEVDIFEIVKELRSQRPGMVQTEEQYIFLYRAIL 258
Y_phosphatase pfam00102
Protein-tyrosine phosphatase;
920-1178 1.15e-85

Protein-tyrosine phosphatase;


Pssm-ID: 459674 [Multi-domain]  Cd Length: 234  Bit Score: 278.36  E-value: 1.15e-85
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578801329   920 NKSKNRNSNVIPYDYNRVPLKHElemskesehdsdessdddsdsEEPSKYINASFIMSYWKPEVMIAAQGPLKETIGDFW 999
Cdd:pfam00102    1 NLEKNRYKDVLPYDHTRVKLTGD---------------------PGPSDYINASYIDGYKKPKKYIATQGPLPNTVEDFW 59

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578801329  1000 QMIFQRKVKVIVMLTELKHGDQEICAQYW---GEGKQTYGDIEVDLKDTDK-SSTYTLRVFELRHSKRKDSRTVYQYQYT 1075
Cdd:pfam00102   60 RMVWEEKVTIIVMLTELEEKGREKCAQYWpeeEGESLEYGDFTVTLKKEKEdEKDYTVRTLEVSNGGSEETRTVKHFHYT 139

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578801329  1076 NWSVEQLPAEPKELISMIQVVKQKlpqknssegNKHHKSTPLLIHCRDGSQQTGIFCALLNLLESAETEEVVDIFQVVKA 1155
Cdd:pfam00102  140 GWPDHGVPESPNSLLDLLRKVRKS---------SLDGRSGPIVVHCSAGIGRTGTFIAIDIALQQLEAEGEVDIFQIVKE 210

                          250       260
                   ....*....|....*....|...
gi 578801329  1156 LRKARPGMVSTFEQYQFLYDVIA 1178
Cdd:pfam00102  211 LRSQRPGMVQTLEQYIFLYDAIL 233
PHA02746 PHA02746
protein tyrosine phosphatase; Provisional
 626-861 1.44e-51

protein tyrosine phosphatase; Provisional


Pssm-ID: 165113 [Multi-domain]  Cd Length: 323  Bit Score: 184.85  E-value: 1.44e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578801329  626 KPFNQNKNRYVDILPYDYNRVELSE-------------------INGDAGSNYINASYIDGFKEPRKYIAAQGPRDETVD 686
Cdd:PHA02746   48 KKENLKKNRFHDIPCWDHSRVVINAheslkmfdvgdsdgkkievTSEDNAENYIHANFVDGFKEANKFICAQGPKEDTSE 127

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578801329  687 DFWRMIWEQKATVIVMVTRCEEGNRnKCAEYWPSMEEGTRAFGDVVVKINQHKRCPDYIIQKLNIVNKKEKaTGREVTHI 766
Cdd:PHA02746  128 DFFKLISEHESQVIVSLTDIDDDDE-KCFELWTKEEDSELAFGRFVAKILDIIEELSFTKTRLMITDKISD-TSREIHHF 205

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578801329  767 QFTSWPDHGVPEDPHLLLKLRRRVNA----------FSNFFSGPIVVHCSAGVGRTGTYIGIDAMLEGLEAENKVDVYGY 836
Cdd:PHA02746  206 WFPDWPDNGIPTGMAEFLELINKVNEeqaelikqadNDPQTLGPIVVHCSAGIGRAGTFCAIDNALEQLEKEKEVCLGEI 285

                         250       260
                  ....*....|....*....|....*
gi 578801329  837 VVKLRRQRCLMVQVEAQYILIHQAL 861
Cdd:PHA02746  286 VLKIRKQRHSSVFLPEQYAFCYKAL 310
COG5599 COG5599
Protein tyrosine phosphatase [Signal transduction mechanisms];
632-857 6.75e-40

Protein tyrosine phosphatase [Signal transduction mechanisms];


Pssm-ID: 444335 [Multi-domain]  Cd Length: 282  Bit Score: 149.47  E-value: 6.75e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578801329  632 KNRYVDILPYDYNRVElseINGdagsNYINASYIDGfKEPRKYIAAQGPRDETVDDFWRMIWEQKATVIVMVTRCEEG-- 709
Cdd:COG5599    45 LNRFRDIQPYKETALR---ANL----GYLNANYIQV-IGNHRYIATQYPLEEQLEDFFQMLFDNNTPVLVVLASDDEIsk 116

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578801329  710 NRNKCAEYWPsmEEGTRAFGDVVVKINQHKRCPDYIIQKLNIVNKKEKA-TGREVTHIQFTSWPDHGVP--EDPHLLLKL 786
Cdd:COG5599   117 PKVKMPVYFR--QDGEYGKYEVSSELTESIQLRDGIEARTYVLTIKGTGqKKIEIPVLHVKNWPDHGAIsaEALKNLADL 194

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 578801329  787 RRRVNAFSNFFSGPIVVHCSAGVGRTGTYIGIDAMLEGLEAEN--KVDVYGYVVKLRRQR-CLMVQVEAQYILI 857
Cdd:COG5599   195 IDKKEKIKDPDKLLPVVHCRAGVGRTGTLIACLALSKSINALVqiTLSVEEIVIDMRTSRnGGMVQTSEQLDVL 268
PHA02747 PHA02747
protein tyrosine phosphatase; Provisional
 919-1173 5.94e-35

protein tyrosine phosphatase; Provisional


Pssm-ID: 165114 [Multi-domain]  Cd Length: 312  Bit Score: 136.28  E-value: 5.94e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578801329  919 ENKSKNRNSNVIPYDYNRVPLKhelemskesehdsdessdddSDSEEPSKYINASFIMSYWKPEVMIAAQGPLKETIGDF 998
Cdd:PHA02747   50 ENQPKNRYWDIPCWDHNRVILD--------------------SGGGSTSDYIHANWIDGFEDDKKFIATQGPFAETCADF 109

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578801329  999 WQMIFQRKVKVIVMLTELKHGD-QEICAQYWG---EGKQTYGDIEVDLKDTDKSSTYTLRVFELRHSKRKDSRTVYQYQY 1074
Cdd:PHA02747  110 WKAVWQEHCSIIVMLTPTKGTNgEEKCYQYWClneDGNIDMEDFRIETLKTSVRAKYILTLIEITDKILKDSRKISHFQC 189

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578801329 1075 TNWSVEQLPAEPKELISMIQVVKQKLPQKNSSEGNKHHKSTPLLIHCRDGSQQTGIFCALLNLLESAETEEVVDIFQVVK 1154
Cdd:PHA02747  190 SEWFEDETPSDHPDFIKFIKIIDINRKKSGKLFNPKDALLCPIVVHCSDGVGKTGIFCAVDICLNQLVKRKAICLAKTAE 269

                         250
                  ....*....|....*....
gi 578801329 1155 ALRKARPGMVSTFEQYQFL 1173
Cdd:PHA02747  270 KIREQRHAGIMNFDDYLFI 288
COG5599 COG5599
Protein tyrosine phosphatase [Signal transduction mechanisms];
911-1179 4.28e-30

Protein tyrosine phosphatase [Signal transduction mechanisms];


Pssm-ID: 444335 [Multi-domain]  Cd Length: 282  Bit Score: 121.35  E-value: 4.28e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578801329  911 TQHIGNQEeNKSKNRNSNVIPYDYNRVplkhelemskesehdsdessdddsdsEEPSKYINASFIMSYwKPEVMIAAQGP 990
Cdd:COG5599    34 PQYLQNIN-GSPLNRFRDIQPYKETAL--------------------------RANLGYLNANYIQVI-GNHRYIATQYP 85

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578801329  991 LKETIGDFWQMIFQRKVKVIVMLTELKHGDQEI--CAQYWGEgKQTYGDIEVDLKDTDK---SSTYTLRVFEL-RHSKRK 1064
Cdd:COG5599    86 LEEQLEDFFQMLFDNNTPVLVVLASDDEISKPKvkMPVYFRQ-DGEYGKYEVSSELTESiqlRDGIEARTYVLtIKGTGQ 164

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578801329 1065 DSRTVYQYQYTNWSVEQLPAePKELISMIQVVKQKLPQKNSSEGnkhhkstPLLIHCRDGSQQTGIFCALLNLLES--AE 1142
Cdd:COG5599   165 KKIEIPVLHVKNWPDHGAIS-AEALKNLADLIDKKEKIKDPDKL-------LPVVHCRAGVGRTGTLIACLALSKSinAL 236

                         250       260       270
                  ....*....|....*....|....*....|....*...
gi 578801329 1143 TEEVVDIFQVVKALRKAR-PGMVSTFEQYQFLYDVIAS 1179
Cdd:COG5599   237 VQITLSVEEIVIDMRTSRnGGMVQTSEQLDVLVKLAEQ 274
CD45 pfam12567
Leukocyte receptor CD45; This family of proteins is found in eukaryotes. Proteins in this ...
 189-247 1.54e-29

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: 111.69  E-value: 1.54e-29
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 578801329   189 VDYLYNKETKLFTAKLNVNENVECGNNTCTNNEVHNLTECKNASVSISHNSCTAPDKTL 247
Cdd:pfam12567    1 VEYTYNSENKSFTAKLNVNDNVECENNDCENNELHNLQECEQINVSISHNSCTSPNKIL 59
PHA03255 PHA03255
BDLF3; Provisional
 18-183 2.53e-10

BDLF3; Provisional


Pssm-ID: 165513 [Multi-domain]  Cd Length: 234  Bit Score: 62.23  E-value: 2.53e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578801329   18 DTEVFVTGQSPTP-SPTGLTTAKMPSVPLSSDPLP------THTTAFSPAstferendfseTTTSLSPDNTSTQVSPDSl 90
Cdd:PHA03255   19 ETSLIWTSSGSSTaSAGNVTGTTAVTTPSPSASGPstnqstTLTTTSAPI-----------TTTAILSTNTTTVTSTGT- 86

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578801329   91 dNASAFNTTgvSSVQTPHLPTHADSQT---PSAGTDTQTFSGSaanaklNPTPGSNAISDAYLNASETTTLSPSGSAVIS 167
Cdd:PHA03255   87 -TVTPVPTT--SNASTINVTTKVTAQNitaTEAGTGTSTGVTS------NVTTRSSSTTSATTRITNATTLAPTLSSKGT 157

                         170
                  ....*....|....*..
gi 578801329  168 TTTIATTPSKPTC-DEK 183
Cdd:PHA03255  158 SNATKTTAELPTVpDER 174
PTP_N pfam12453
Protein tyrosine phosphatase N terminal; This domain family is found in eukaryotes, and is ...
 7-32 2.55e-10

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: 56.40  E-value: 2.55e-10
                           10        20
                   ....*....|....*....|....*.
gi 578801329     7 LKLLAFGFAFLDTEVFVTGQSPTPSP 32
Cdd:pfam12453    1 LKLLAFGFAFLDTEVFVTGESLTSST 26
FN3 cd00063
Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein ...
 437-517 1.96e-09

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: 55.97  E-value: 1.96e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578801329  437 PSQVWNMTVSMTSDNSMHVKCRPPRDRNGPHERYHLEVEAGN----TLVRNESHKNCDFRVKDLQYSTDYTFKAYFHNGD 512
Cdd:cd00063     1 PSPPTNLRVTDVTSTSVTLSWTPPEDDGGPITGYVVEYREKGsgdwKEVEVTPGSETSYTLTGLKPGTEYEFRVRAVNGG 80


                  ....*
gi 578801329  513 YPGEP 517
Cdd:cd00063    81 GESPP 85
fn3 pfam00041
Fibronectin type III domain;
438-517 1.98e-06

Fibronectin type III domain;


Pssm-ID: 394996 [Multi-domain]  Cd Length: 85  Bit Score: 47.02  E-value: 1.98e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578801329   438 SQVWNMTVSMTSDNSMHVKCRPPRDRNGPHERYHLEVEAGN--------TLVRNESHkncdFRVKDLQYSTDYTFKAYFH 509
Cdd:pfam00041    1 SAPSNLTVTDVTSTSLTVSWTPPPDGNGPITGYEVEYRPKNsgepwneiTVPGTTTS----VTLTGLKPGTEYEVRVQAV 76


                   ....*...
gi 578801329   510 NGDYPGEP 517
Cdd:pfam00041   77 NGGGEGPP 84
Chi1 COG3469
Chitinase [Carbohydrate transport and metabolism];
10-179 2.64e-06

Chitinase [Carbohydrate transport and metabolism];


Pssm-ID: 442692 [Multi-domain]  Cd Length: 534  Bit Score: 51.68  E-value: 2.64e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578801329   10 LAFGFAFLDTEVFVTGQSPTPSPTGLTTAKMPSVPLSSDPLPTHTTAFSPASTferendfseTTTSLSPDNTSTQVSPDS 89
Cdd:COG3469    49 VVVAASGSAGSGTGTTAASSTAATSSTTSTTATATAAAAAATSTSATLVATST---------ASGANTGTSTVTTTSTGA 119

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578801329   90 LDNASAFNTTGVSSVQTPHLPTHADSQTPSAGTDTQTFSGSAANAKLNPTPGSNAISDAYLNASETTTLSPSGSAVISTT 169
Cdd:COG3469   120 GSVTSTTSSTAGSTTTSGASATSSAGSTTTTTTVSGTETATGGTTTTSTTTTTTSASTTPSATTTATATTASGATTPSAT 199

                         170
                  ....*....|
gi 578801329  170 TIATTPSKPT 179
Cdd:COG3469   200 TTATTTGPPT 209
fn3 pfam00041
Fibronectin type III domain;
345-414 4.61e-05

Fibronectin type III domain;


Pssm-ID: 394996 [Multi-domain]  Cd Length: 85  Bit Score: 43.17  E-value: 4.61e-05
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 578801329   345 GEPQIIFCRSEAAHQGVITWNPP---QRSFHNFTLCYIKETEKDC---LNLDKNLIKYDLQNLKPYTKYVLSLHAY 414
Cdd:pfam00041    1 SAPSNLTVTDVTSTSLTVSWTPPpdgNGPITGYEVEYRPKNSGEPwneITVPGTTTSVTLTGLKPGTEYEVRVQAV 76
FN3 smart00060
Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, ...
 437-512 8.20e-05

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


Pssm-ID: 214495 [Multi-domain]  Cd Length: 83  Bit Score: 42.22  E-value: 8.20e-05
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578801329    437 PSQVWNMTVSMTSDNSMHVKCRPPRDRNGPHERYHLEVE----AGNTLVRNESHKNCDFRVKDLQYSTDYTFK--AYFHN 510
Cdd:smart00060    1 PSPPSNLRVTDVTSTSVTLSWEPPPDDGITGYIVGYRVEyreeGSEWKEVNVTPSSTSYTLTGLKPGTEYEFRvrAVNGA 80


                    ..
gi 578801329    511 GD 512
Cdd:smart00060   81 GE 82
FN3 cd00063
Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein ...
 344-414 8.75e-05

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


Pssm-ID: 238020 [Multi-domain]  Cd Length: 93  Bit Score: 42.48  E-value: 8.75e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 578801329  344 PGEPQIIFCRSEAAHQGVITWNPPQRS---FHNFTLCYIKETEKDCLNLDKNLIK---YDLQNLKPYTKYVLSLHAY 414
Cdd:cd00063     1 PSPPTNLRVTDVTSTSVTLSWTPPEDDggpITGYVVEYREKGSGDWKEVEVTPGSetsYTLTGLKPGTEYEFRVRAV 77
FN3 smart00060
Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, ...
 344-414 4.24e-03

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


Pssm-ID: 214495 [Multi-domain]  Cd Length: 83  Bit Score: 37.59  E-value: 4.24e-03
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 578801329    344 PGEPQIIFCRSEAAHQGVITWNPPQRSFHN-FTLCYIKETEKDC-----LNLDKNLIKYDLQNLKPYTKYVLSLHAY 414
Cdd:smart00060    1 PSPPSNLRVTDVTSTSVTLSWEPPPDDGITgYIVGYRVEYREEGsewkeVNVTPSSTSYTLTGLKPGTEYEFRVRAV 77
 
Name Accession Description Interval E-value
R-PTPc-C-1 cd14557
catalytic domain of receptor-type tyrosine-protein phosphatase C, repeat 1; Receptor-type ...
 659-859 9.67e-150

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: 448.89  E-value: 9.67e-150
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578801329  659 YINASYIDGFKEPRKYIAAQGPRDETVDDFWRMIWEQKATVIVMVTRCEEGNRNKCAEYWPSMEEGTRAFGDVVVKINQH 738
Cdd:cd14557     1 YINASYIDGFKEPRKYIAAQGPKDETVDDFWRMIWEQKSTVIVMVTRCEEGNRNKCAQYWPSMEEGSRAFGDVVVKINEE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578801329  739 KRCPDYIIQKLNIVNKKEKATGREVTHIQFTSWPDHGVPEDPHLLLKLRRRVNAFSNFFSGPIVVHCSAGVGRTGTYIGI 818
Cdd:cd14557    81 KICPDYIIRKLNINNKKEKGSGREVTHIQFTSWPDHGVPEDPHLLLKLRRRVNAFNNFFSGPIVVHCSAGVGRTGTYIGI 160

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|.
gi 578801329  819 DAMLEGLEAENKVDVYGYVVKLRRQRCLMVQVEAQYILIHQ 859
Cdd:cd14557   161 DAMLEGLEAEGRVDVYGYVVKLRRQRCLMVQVEAQYILIHQ 201
R-PTP-C-2 cd14558
PTP-like domain of receptor-type tyrosine-protein phosphatase C, repeat 2; Receptor-type ...
 969-1175 2.74e-129

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: 394.84  E-value: 2.74e-129
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578801329  969 YINASFIMSYWKPEVMIAAQGPLKETIGDFWQMIFQRKVKVIVMLTELKHGDQEICAQYWGEGKQTYGDIEVDLKDTDKS 1048
Cdd:cd14558     1 YINASFIDGYWGPKSLIATQGPLPDTIADFWQMIFQKKVKVIVMLTELKEGDQEQCAQYWGDEKKTYGDIEVELKDTEKS 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578801329 1049 STYTLRVFELRHSKRKDSRTVYQYQYTNWSVEQLPAEPKELISMIQVVKQKLPQKNSsegnKHHKSTPLLIHCRDGSQQT 1128
Cdd:cd14558    81 PTYTVRVFEITHLKRKDSRTVYQYQYHKWKGEELPEKPKDLVDMIKSIKQKLPYKNS----KHGRSVPIVVHCSDGSSRT 156

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*..
gi 578801329 1129 GIFCALLNLLESAETEEVVDIFQVVKALRKARPGMVSTFEQYQFLYD 1175
Cdd:cd14558   157 GIFCALWNLLESAETEKVVDVFQVVKALRKQRPGMVSTLEQYQFLYD 203
PTPc smart00194
Protein tyrosine phosphatase, catalytic domain;
604-863 2.98e-111

Protein tyrosine phosphatase, catalytic domain;


Pssm-ID: 214550 [Multi-domain]  Cd Length: 259  Bit Score: 348.88  E-value: 2.98e-111
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578801329    604 LFLAEFQSIPRVFS-KFPIKEARKPFNQNKNRYVDILPYDYNRVELSEINGDaGSNYINASYIDGFKEPRKYIAAQGPRD 682
Cdd:smart00194    1 GLEEEFEKLDRLKPdDESCTVAAFPENRDKNRYKDVLPYDHTRVKLKPPPGE-GSDYINASYIDGPNGPKAYIATQGPLP 79

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578801329    683 ETVDDFWRMIWEQKATVIVMVTRCEEGNRNKCAEYWPSMEEGTRAFGDVVVKINQHKRCPDYIIQKLNIVNKKEKATgRE 762
Cdd:smart00194   80 STVEDFWRMVWEQKVTVIVMLTELVEKGREKCAQYWPDEEGEPLTYGDITVTLKSVEKVDDYTIRTLEVTNTGCSET-RT 158

                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578801329    763 VTHIQFTSWPDHGVPEDPHLLLKLRRRVNAFSNFFSGPIVVHCSAGVGRTGTYIGIDAMLEGLEAENKVDVYGYVVKLRR 842
Cdd:smart00194  159 VTHYHYTNWPDHGVPESPESILDLIRAVRKSQSTSTGPIVVHCSAGVGRTGTFIAIDILLQQLEAGKEVDIFEIVKELRS 238

                           250       260
                    ....*....|....*....|.
gi 578801329    843 QRCLMVQVEAQYILIHQALVE 863
Cdd:smart00194  239 QRPGMVQTEEQYIFLYRAILE 259
Y_phosphatase pfam00102
Protein-tyrosine phosphatase;
629-863 3.45e-107

Protein-tyrosine phosphatase;


Pssm-ID: 459674 [Multi-domain]  Cd Length: 234  Bit Score: 336.91  E-value: 3.45e-107
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578801329   629 NQNKNRYVDILPYDYNRVELSEINGDagSNYINASYIDGFKEPRKYIAAQGPRDETVDDFWRMIWEQKATVIVMVTRCEE 708
Cdd:pfam00102    1 NLEKNRYKDVLPYDHTRVKLTGDPGP--SDYINASYIDGYKKPKKYIATQGPLPNTVEDFWRMVWEEKVTIIVMLTELEE 78

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578801329   709 GNRNKCAEYWPSMEEGTRAFGDVVVKI-NQHKRCPDYIIQKLNIVNKKEKATgREVTHIQFTSWPDHGVPEDPHLLLKLR 787
Cdd:pfam00102   79 KGREKCAQYWPEEEGESLEYGDFTVTLkKEKEDEKDYTVRTLEVSNGGSEET-RTVKHFHYTGWPDHGVPESPNSLLDLL 157

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 578801329   788 RRVNAFSN-FFSGPIVVHCSAGVGRTGTYIGIDAMLEGLEAENKVDVYGYVVKLRRQRCLMVQVEAQYILIHQALVE 863
Cdd:pfam00102  158 RKVRKSSLdGRSGPIVVHCSAGIGRTGTFIAIDIALQQLEAEGEVDIFQIVKELRSQRPGMVQTLEQYIFLYDAILE 234
R-PTPc-LAR-1 cd14553
catalytic domain of LAR family receptor-type tyrosine-protein phosphatases, repeat 1; The LAR ...
 629-863 1.19e-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: 1.19e-97
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578801329  629 NQNKNRYVDILPYDYNRVELSEINGDAGSNYINASYIDGFKEPRKYIAAQGPRDETVDDFWRMIWEQKATVIVMVTRCEE 708
Cdd:cd14553     3 NKPKNRYANVIAYDHSRVILQPIEGVPGSDYINANYCDGYRKQNAYIATQGPLPETFGDFWRMVWEQRSATIVMMTKLEE 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578801329  709 GNRNKCAEYWPSmeEGTRAFGDVVVKINQHKRCPDYIIQKLNIVNKKEKATgREVTHIQFTSWPDHGVPEDPHLLLKLRR 788
Cdd:cd14553    83 RSRVKCDQYWPT--RGTETYGLIQVTLLDTVELATYTVRTFALHKNGSSEK-REVRQFQFTAWPDHGVPEHPTPFLAFLR 159

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 578801329  789 RVNAFSNFFSGPIVVHCSAGVGRTGTYIGIDAMLEGLEAENKVDVYGYVVKLRRQRCLMVQVEAQYILIHQALVE 863
Cdd:cd14553   160 RVKACNPPDAGPIVVHCSAGVGRTGCFIVIDSMLERIKHEKTVDIYGHVTCLRAQRNYMVQTEDQYIFIHDALLE 234
PTPc smart00194
Protein tyrosine phosphatase, catalytic domain;
896-1178 2.64e-96

Protein tyrosine phosphatase, catalytic domain;


Pssm-ID: 214550 [Multi-domain]  Cd Length: 259  Bit Score: 308.43  E-value: 2.64e-96
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578801329    896 LEAEFQRLPSYRSW-RTQHIGNQEENKSKNRNSNVIPYDYNRVPLKHELEmskesehdsdessdddsdseEPSKYINASF 974
Cdd:smart00194    2 LEEEFEKLDRLKPDdESCTVAAFPENRDKNRYKDVLPYDHTRVKLKPPPG--------------------EGSDYINASY 61

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578801329    975 IMSYWKPEVMIAAQGPLKETIGDFWQMIFQRKVKVIVMLTELKHGDQEICAQYW---GEGKQTYGDIEVDLKDTDKSSTY 1051
Cdd:smart00194   62 IDGPNGPKAYIATQGPLPSTVEDFWRMVWEQKVTVIVMLTELVEKGREKCAQYWpdeEGEPLTYGDITVTLKSVEKVDDY 141

                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578801329   1052 TLRVFELRHSKRKDSRTVYQYQYTNWSVEQLPAEPKELISMIQVVKQKLPqknssegnkhHKSTPLLIHCRDGSQQTGIF 1131
Cdd:smart00194  142 TIRTLEVTNTGCSETRTVTHYHYTNWPDHGVPESPESILDLIRAVRKSQS----------TSTGPIVVHCSAGVGRTGTF 211

                           250       260       270       280
                    ....*....|....*....|....*....|....*....|....*..
gi 578801329   1132 CALLNLLESAETEEVVDIFQVVKALRKARPGMVSTFEQYQFLYDVIA 1178
Cdd:smart00194  212 IAIDILLQQLEAGKEVDIFEIVKELRSQRPGMVQTEEQYIFLYRAIL 258
PTPc cd00047
catalytic domain of protein tyrosine phosphatases; Protein tyrosine phosphatases (PTP, EC 3.1. ...
 659-859 2.77e-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: 303.44  E-value: 2.77e-95
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578801329  659 YINASYIDGFKEPRKYIAAQGPRDETVDDFWRMIWEQKATVIVMVTRCEEGNRNKCAEYWPSMEEGTRAFGDVVVKINQH 738
Cdd:cd00047     1 YINASYIDGYRGPKEYIATQGPLPNTVEDFWRMVWEQKVSVIVMLTNLVEKGREKCERYWPEEGGKPLEYGDITVTLVSE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578801329  739 KRCPDYIIQKLNIVNKKEKATgREVTHIQFTSWPDHGVPEDPHLLLKLRRRVNAFSNFFSGPIVVHCSAGVGRTGTYIGI 818
Cdd:cd00047    81 EELSDYTIRTLELSPKGCSES-REVTHLHYTGWPDHGVPSSPEDLLALVRRVRKEARKPNGPIVVHCSAGVGRTGTFIAI 159

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|.
gi 578801329  819 DAMLEGLEAENKVDVYGYVVKLRRQRCLMVQVEAQYILIHQ 859
Cdd:cd00047   160 DILLERLEAEGEVDVFEIVKALRKQRPGMVQTLEQYEFIYE 200
R3-PTPc cd14548
catalytic domain of R3 subfamily receptor-type tyrosine-protein phosphatases and similar ...
 634-859 8.94e-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: 297.34  E-value: 8.94e-93
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578801329  634 RYVDILPYDYNRVELSEINGDAGSNYINASYIDGFKEPRKYIAAQGPRDETVDDFWRMIWEQKATVIVMVTRCEEGNRNK 713
Cdd:cd14548     1 RYTNILPYDHSRVKLIPINEEEGSDYINANYIPGYNSPREFIATQGPLPGTKDDFWRMVWEQNSHTIVMLTQCMEKGRVK 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578801329  714 CAEYWPSMEEGTrAFGDVVVKINQHKRCPDYIIQKLNIVNKKEKatgREVTHIQFTSWPDHGVPEDPHLLLKLRRRVNAF 793
Cdd:cd14548    81 CDHYWPFDQDPV-YYGDITVTMLSESVLPDWTIREFKLERGDEV---RSVRQFHFTAWPDHGVPEAPDSLLRFVRLVRDY 156

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 578801329  794 SNFFSGPIVVHCSAGVGRTGTYIGIDAMLEGLEAENKVDVYGYVVKLRRQRCLMVQVEAQYILIHQ 859
Cdd:cd14548   157 IKQEKGPTIVHCSAGVGRTGTFIALDRLLQQIESEDYVDIFGIVYDLRKHRPLMVQTEAQYIFLHQ 222
R-PTPc-A-1 cd14621
catalytic domain of receptor-type tyrosine-protein phosphatase A, repeat 1; Receptor-type ...
 584-872 4.93e-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: 290.00  E-value: 4.93e-89
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578801329  584 PIHADILLETYKRKIADEGRLFLAEFQSIPRVFSKFPIKEARKPFNQNKNRYVDILPYDYNRVELSEINGDAGSNYINAS 663
Cdd:cd14621     7 PLPVDKLEEEINRRMADDNKLFREEFNALPACPIQATCEAASKEENKEKNRYVNILPYDHSRVHLTPVEGVPDSDYINAS 86

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578801329  664 YIDGFKEPRKYIAAQGPRDETVDDFWRMIWEQKATVIVMVTRCEEGNRNKCAEYWPsmEEGTRAFGDVVVKINQHKRCPD 743
Cdd:cd14621    87 FINGYQEKNKFIAAQGPKEETVNDFWRMIWEQNTATIVMVTNLKERKECKCAQYWP--DQGCWTYGNIRVSVEDVTVLVD 164

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578801329  744 YIIQKL------NIVNKKEKatgREVTHIQFTSWPDHGVPEDPHLLLKLRRRVNAFSNFFSGPIVVHCSAGVGRTGTYIG 817
Cdd:cd14621   165 YTVRKFciqqvgDVTNKKPQ---RLITQFHFTSWPDFGVPFTPIGMLKFLKKVKNCNPQYAGAIVVHCSAGVGRTGTFIV 241

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 578801329  818 IDAMLEGLEAENKVDVYGYVVKLRRQRCLMVQVEAQYILIHQALVEYNQFGETEV 872
Cdd:cd14621   242 IDAMLDMMHAERKVDVYGFVSRIRAQRCQMVQTDMQYVFIYQALLEHYLYGDTEL 296
Y_phosphatase pfam00102
Protein-tyrosine phosphatase;
920-1178 1.15e-85

Protein-tyrosine phosphatase;


Pssm-ID: 459674 [Multi-domain]  Cd Length: 234  Bit Score: 278.36  E-value: 1.15e-85
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578801329   920 NKSKNRNSNVIPYDYNRVPLKHElemskesehdsdessdddsdsEEPSKYINASFIMSYWKPEVMIAAQGPLKETIGDFW 999
Cdd:pfam00102    1 NLEKNRYKDVLPYDHTRVKLTGD---------------------PGPSDYINASYIDGYKKPKKYIATQGPLPNTVEDFW 59

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578801329  1000 QMIFQRKVKVIVMLTELKHGDQEICAQYW---GEGKQTYGDIEVDLKDTDK-SSTYTLRVFELRHSKRKDSRTVYQYQYT 1075
Cdd:pfam00102   60 RMVWEEKVTIIVMLTELEEKGREKCAQYWpeeEGESLEYGDFTVTLKKEKEdEKDYTVRTLEVSNGGSEETRTVKHFHYT 139

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578801329  1076 NWSVEQLPAEPKELISMIQVVKQKlpqknssegNKHHKSTPLLIHCRDGSQQTGIFCALLNLLESAETEEVVDIFQVVKA 1155
Cdd:pfam00102  140 GWPDHGVPESPNSLLDLLRKVRKS---------SLDGRSGPIVVHCSAGIGRTGTFIAIDIALQQLEAEGEVDIFQIVKE 210

                          250       260
                   ....*....|....*....|...
gi 578801329  1156 LRKARPGMVSTFEQYQFLYDVIA 1178
Cdd:pfam00102  211 LRSQRPGMVQTLEQYIFLYDAIL 233
R5-PTPc-1 cd14549
catalytic domain of R5 subfamily receptor-type tyrosine-protein phosphatases, repeat 1; The R5 ...
 659-858 2.12e-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: 2.12e-83
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578801329  659 YINASYIDGFKEPRKYIAAQGPRDETVDDFWRMIWEQKATVIVMVTRCEEGNRNKCAEYWPSmeEGTRAFGDVVVKINQH 738
Cdd:cd14549     1 YINANYVDGYNKARAYIATQGPLPSTFDDFWRMVWEQNSAIIVMITNLVERGRRKCDQYWPK--EGTETYGNIQVTLLST 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578801329  739 KRCPDYIIQKLNIVNKKEK-----ATGREVTHIQFTSWPDHGVPEDPHLLLKLRRRVNAFSNFFSGPIVVHCSAGVGRTG 813
Cdd:cd14549    79 EVLATYTVRTFSLKNLKLKkvkgrSSERVVYQYHYTQWPDHGVPDYTLPVLSFVRKSSAANPPGAGPIVVHCSAGVGRTG 158

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*
gi 578801329  814 TYIGIDAMLEGLEAENKVDVYGYVVKLRRQRCLMVQVEAQYILIH 858
Cdd:cd14549   159 TYIVIDSMLQQIQDKGTVNVFGFLKHIRTQRNYLVQTEEQYIFIH 203
PTPc cd00047
catalytic domain of protein tyrosine phosphatases; Protein tyrosine phosphatases (PTP, EC 3.1. ...
 969-1175 5.32e-82

catalytic domain of protein tyrosine phosphatases; Protein tyrosine phosphatases (PTP, EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides; they regulate phosphotyrosine levels in signal transduction pathways. The depth of the active site cleft renders the enzyme specific for phosphorylated Tyr (pTyr) residues, instead of pSer or pThr. This family has a distinctive active site signature motif, HCSAGxGRxG, and are characterized as either transmembrane, receptor-like or non-transmembrane (soluble) PTPs. Receptor-like PTP domains tend to occur in two copies in the cytoplasmic region of the transmembrane proteins, only one copy may be active.


Pssm-ID: 350343 [Multi-domain]  Cd Length: 200  Bit Score: 266.46  E-value: 5.32e-82
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578801329  969 YINASFIMSYWKPEVMIAAQGPLKETIGDFWQMIFQRKVKVIVMLTELKHGDQEICAQYW---GEGKQTYGDIEVDLKDT 1045
Cdd:cd00047     1 YINASYIDGYRGPKEYIATQGPLPNTVEDFWRMVWEQKVSVIVMLTNLVEKGREKCERYWpeeGGKPLEYGDITVTLVSE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578801329 1046 DKSSTYTLRVFELRHSKRKDSRTVYQYQYTNWSVEQLPAEPKELISMIQVVKQKLPQKNSsegnkhhkstPLLIHCRDGS 1125
Cdd:cd00047    81 EELSDYTIRTLELSPKGCSESREVTHLHYTGWPDHGVPSSPEDLLALVRRVRKEARKPNG----------PIVVHCSAGV 150

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|
gi 578801329 1126 QQTGIFCALLNLLESAETEEVVDIFQVVKALRKARPGMVSTFEQYQFLYD 1175
Cdd:cd00047   151 GRTGTFIAIDILLERLEAEGEVDVFEIVKALRKQRPGMVQTLEQYEFIYE 200
R-PTPc-E-1 cd14620
catalytic domain of receptor-type tyrosine-protein phosphatase E, repeat 1; Receptor-type ...
 635-863 1.05e-80

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: 264.11  E-value: 1.05e-80
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578801329  635 YVDILPYDYNRVELSEINGDAGSNYINASYIDGFKEPRKYIAAQGPRDETVDDFWRMIWEQKATVIVMVTRCEEGNRNKC 714
Cdd:cd14620     1 YPNILPYDHSRVILSQLDGIPCSDYINASYIDGYKEKNKFIAAQGPKQETVNDFWRMVWEQKSATIVMLTNLKERKEEKC 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578801329  715 AEYWPsmEEGTRAFGDVVVKINQHKRCPDYIIQKLNIVNKKEKAT--GREVTHIQFTSWPDHGVPEDPHLLLKLRRRVNA 792
Cdd:cd14620    81 YQYWP--DQGCWTYGNIRVAVEDCVVLVDYTIRKFCIQPQLPDGCkaPRLVTQLHFTSWPDFGVPFTPIGMLKFLKKVKS 158

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 578801329  793 FSNFFSGPIVVHCSAGVGRTGTYIGIDAMLEGLEAENKVDVYGYVVKLRRQRCLMVQVEAQYILIHQALVE 863
Cdd:cd14620   159 VNPVHAGPIVVHCSAGVGRTGTFIVIDAMIDMMHAEQKVDVFEFVSRIRNQRPQMVQTDMQYSFIYQALLE 229
R-PTPc-F-1 cd14626
catalytic domain of receptor-type tyrosine-protein phosphatase F, repeat 1; Receptor-type ...
 590-863 1.16e-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: 266.13  E-value: 1.16e-80
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578801329  590 LLETYKRKIADEGRLFLAEFQSI-PRvfSKFPIKEARKPFNQNKNRYVDILPYDYNRVELSEINGDAGSNYINASYIDGF 668
Cdd:cd14626     3 LADNIERLKANDGLKFSQEYESIdPG--QQFTWENSNLEVNKPKNRYANVIAYDHSRVILTSVDGVPGSDYINANYIDGY 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578801329  669 KEPRKYIAAQGPRDETVDDFWRMIWEQKATVIVMVTRCEEGNRNKCAEYWPSmeEGTRAFGDVVVKINQHKRCPDYIIQK 748
Cdd:cd14626    81 RKQNAYIATQGPLPETLSDFWRMVWEQRTATIVMMTRLEEKSRVKCDQYWPI--RGTETYGMIQVTLLDTVELATYSVRT 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578801329  749 LNiVNKKEKATGREVTHIQFTSWPDHGVPEDPHLLLKLRRRVNAFSNFFSGPIVVHCSAGVGRTGTYIGIDAMLEGLEAE 828
Cdd:cd14626   159 FA-LYKNGSSEKREVRQFQFMAWPDHGVPEYPTPILAFLRRVKACNPPDAGPMVVHCSAGVGRTGCFIVIDAMLERMKHE 237

                         250       260       270
                  ....*....|....*....|....*....|....*
gi 578801329  829 NKVDVYGYVVKLRRQRCLMVQVEAQYILIHQALVE 863
Cdd:cd14626   238 KTVDIYGHVTCMRSQRNYMVQTEDQYIFIHEALLE 272
PTPc-N9 cd14543
catalytic domain of tyrosine-protein phosphatase non-receptor type 9; Tyrosine-protein ...
 624-858 1.32e-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: 265.77  E-value: 1.32e-80
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578801329  624 ARKPFNQNKNRYVDILPYDYNRVELSEINGDAGSNYINASYIDGFKEPRKYIAAQGPRDETVDDFWRMIWEQKATVIVMV 703
Cdd:cd14543    24 SLAPANQEKNRYGDVLCLDQSRVKLPKRNGDERTDYINANFMDGYKQKNAYIATQGPLPKTYSDFWRMVWEQKVLVIVMT 103

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578801329  704 TRCEEGNRNKCAEYWPSMEEGTRAFGDVVVkINQHKRC-PDYIIQKLNIVNKKEKATgREVTHIQFTSWPDHGVPEDPHL 782
Cdd:cd14543   104 TRVVERGRVKCGQYWPLEEGSSLRYGDLTV-TNLSVENkEHYKKTTLEIHNTETDES-RQVTHFQFTSWPDFGVPSSAAA 181

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578801329  783 LL--------KLRRRVNAFSNFFSG-----PIVVHCSAGVGRTGTYIGIDAMLEGLEAENKVDVYGYVVKLRRQRCLMVQ 849
Cdd:cd14543   182 LLdflgevrqQQALAVKAMGDRWKGhppgpPIVVHCSAGIGRTGTFCTLDICLSQLEDVGTLNVMQTVRRMRTQRAFSIQ 261


                  ....*....
gi 578801329  850 VEAQYILIH 858
Cdd:cd14543   262 TPDQYYFCY 270
R-PTPc-H cd14619
catalytic domain of receptor-type tyrosine-protein phosphatase H; Receptor-type ...
 633-864 4.47e-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: 254.43  E-value: 4.47e-77
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578801329  633 NRYVDILPYDYNRVELSEINGDAGSNYINASYIDGFKEPRKYIAAQGPRDETVDDFWRMIWEQKATVIVMVTRCEEGNRN 712
Cdd:cd14619     1 NRFRNVLPYDWSRVPLKPIHEEPGSDYINANYMPGYWSSQEFIATQGPLPQTVGDFWRMIWEQQSSTIVMLTNCMEAGRV 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578801329  713 KCAEYWPsMEEGTRAFGDVVVKINQHKRCPDYIIQKLNIVNKKEKATgREVTHIQFTSWPDHGVPEDPHLLLKLRRRVNA 792
Cdd:cd14619    81 KCEHYWP-LDYTPCTYGHLRVTVVSEEVMENWTVREFLLKQVEEQKT-LSVRHFHFTAWPDHGVPSSTDTLLAFRRLLRQ 158

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 578801329  793 F--SNFFSGPIVVHCSAGVGRTGTYIGIDAMLEGLEAENKVDVYGYVVKLRRQRCLMVQVEAQYILIHQALVEY 864
Cdd:cd14619   159 WldQTMSGGPTVVHCSAGVGRTGTLIALDVLLQQLQSEGLLGPFSFVQKMRENRPLMVQTESQYVFLHQCILDF 232
R-PTPc-A-E-1 cd14551
catalytic domain of receptor-type tyrosine-protein phosphatase A and E, repeat 1; ...
 659-859 8.96e-76

catalytic domain of receptor-type tyrosine-protein phosphatase A and E, repeat 1; Receptor-type tyrosine-protein phosphatase A (PTPRA) and E (PTPRE) belong to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. PTPRA and PTPRE share several functions including regulation of Src family kinases and voltage-gated potassium (Kv) channels. They both contain a small extracellular domain, a transmembrane segment, and an intracellular region containing two tandem catalytic PTP domains. This model represents the first catalytic PTP domain (repeat 1).


Pssm-ID: 350399 [Multi-domain]  Cd Length: 202  Bit Score: 249.44  E-value: 8.96e-76
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578801329  659 YINASYIDGFKEPRKYIAAQGPRDETVDDFWRMIWEQKATVIVMVTRCEEGNRNKCAEYWPsmEEGTRAFGDVVVKINQH 738
Cdd:cd14551     1 YINASYIDGYQEKNKFIAAQGPKDETVNDFWRMIWEQGSATIVMVTNLKERKEKKCSQYWP--DQGCWTYGNLRVRVEDT 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578801329  739 KRCPDYIIQKLnIVNKKEKATG----REVTHIQFTSWPDHGVPEDPHLLLKLRRRVNAFSNFFSGPIVVHCSAGVGRTGT 814
Cdd:cd14551    79 VVLVDYTTRKF-CIQKVNRGIGekrvRLVTQFHFTSWPDFGVPFTPIGMLKFLKKVKSANPPRAGPIVVHCSAGVGRTGT 157

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*
gi 578801329  815 YIGIDAMLEGLEAENKVDVYGYVVKLRRQRCLMVQVEAQYILIHQ 859
Cdd:cd14551   158 FIVIDAMLDMMHAEGKVDVFGFVSRIRQQRSQMVQTDMQYVFIYQ 202
R-PTPc-B cd14617
catalytic domain of receptor-type tyrosine-protein phosphatase B; Receptor-type ...
 633-859 6.91e-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: 6.91e-75
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578801329  633 NRYVDILPYDYNRVELSEINGDAGSNYINASYIDGFKEPRKYIAAQGPRDETVDDFWRMIWEQKATVIVMVTRCEEGNRN 712
Cdd:cd14617     1 NRYNNILPYDSTRVKLSNVDDDPCSDYINASYIPGNNFRREYIATQGPLPGTKDDFWKMVWEQNVHNIVMVTQCVEKGRV 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578801329  713 KCAEYWPsMEEGTRAFGDVVVKINQHKRCPDYIIQKLNIVNKKEKATGREVTHIQFTSWPDHGVPEDPHLLLKLRRRVNA 792
Cdd:cd14617    81 KCDHYWP-ADQDSLYYGDLIVQMLSESVLPEWTIREFKICSEEQLDAPRLVRHFHYTVWPDHGVPETTQSLIQFVRTVRD 159

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 578801329  793 FSNFF--SGPIVVHCSAGVGRTGTYIGIDAMLEGLEAENKVDVYGYVVKLRRQRCLMVQVEAQYILIHQ 859
Cdd:cd14617   160 YINRTpgSGPTVVHCSAGVGRTGTFIALDRILQQLDSKDSVDIYGAVHDLRLHRVHMVQTECQYVYLHQ 228
R-PTPc-J cd14615
catalytic domain of receptor-type tyrosine-protein phosphatase J; Receptor-type ...
 633-859 2.01e-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: 246.65  E-value: 2.01e-74
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578801329  633 NRYVDILPYDYNRVELSeINGDAGSNYINASYIDGFKEPRKYIAAQGPRDETVDDFWRMIWEQKATVIVMVTRCEEGNRN 712
Cdd:cd14615     1 NRYNNVLPYDISRVKLS-VQSHSTDDYINANYMPGYNSKKEFIAAQGPLPNTVKDFWRMVWEKNVYAIVMLTKCVEQGRT 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578801329  713 KCAEYWPSmeEGTRAFGDVVVKINQHKRCPDYIIQKLNIVNKKEkATGREVTHIQFTSWPDHGVPEDPHLLLKLRRRVNA 792
Cdd:cd14615    80 KCEEYWPS--KQKKDYGDITVTMTSEIVLPEWTIRDFTVKNAQT-NESRTVRHFHFTSWPDHGVPETTDLLINFRHLVRE 156

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 578801329  793 FS--NFFSGPIVVHCSAGVGRTGTYIGIDAMLEGLEAENKVDVYGYVVKLRRQRCLMVQVEAQYILIHQ 859
Cdd:cd14615   157 YMkqNPPNSPILVHCSAGVGRTGTFIAIDRLIYQIENENVVDVYGIVYDLRMHRPLMVQTEDQYVFLNQ 225
R-PTPc-S-1 cd14625
catalytic domain of receptor-type tyrosine-protein phosphatase S, repeat 1; Receptor-type ...
 584-863 9.10e-73

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: 244.23  E-value: 9.10e-73
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578801329  584 PIHADILLETYKRKIADEGRLFLAEFQSIPRvFSKFPIKEARKPFNQNKNRYVDILPYDYNRVELSEINGDAGSNYINAS 663
Cdd:cd14625     3 PIPISELAEHTERLKANDNLKLSQEYESIDP-GQQFTWEHSNLEVNKPKNRYANVIAYDHSRVILQPIEGIMGSDYINAN 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578801329  664 YIDGFKEPRKYIAAQGPRDETVDDFWRMIWEQKATVIVMVTRCEEGNRNKCAEYWPSmeEGTRAFGDVVVKINQHKRCPD 743
Cdd:cd14625    82 YIDGYRKQNAYIATQGPLPETFGDFWRMVWEQRSATVVMMTKLEEKSRIKCDQYWPS--RGTETYGMIQVTLLDTIELAT 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578801329  744 YIIQKLNIvNKKEKATGREVTHIQFTSWPDHGVPEDPHLLLKLRRRVNAFSNFFSGPIVVHCSAGVGRTGTYIGIDAMLE 823
Cdd:cd14625   160 FCVRTFSL-HKNGSSEKREVRQFQFTAWPDHGVPEYPTPFLAFLRRVKTCNPPDAGPIVVHCSAGVGRTGCFIVIDAMLE 238

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|
gi 578801329  824 GLEAENKVDVYGYVVKLRRQRCLMVQVEAQYILIHQALVE 863
Cdd:cd14625   239 RIKHEKTVDIYGHVTLMRSQRNYMVQTEDQYSFIHDALLE 278
R-PTPc-D-1 cd14624
catalytic domain of receptor-type tyrosine-protein phosphatase D, repeat 1; Receptor-type ...
 584-863 1.17e-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: 1.17e-72
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578801329  584 PIHADILLETYKRKIADEGRLFLAEFQSIPRvFSKFPIKEARKPFNQNKNRYVDILPYDYNRVELSEINGDAGSNYINAS 663
Cdd:cd14624     3 PIPILELADHIERLKANDNLKFSQEYESIDP-GQQFTWEHSNLEVNKPKNRYANVIAYDHSRVLLSAIEGIPGSDYINAN 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578801329  664 YIDGFKEPRKYIAAQGPRDETVDDFWRMIWEQKATVIVMVTRCEEGNRNKCAEYWPSmeEGTRAFGDVVVKINQHKRCPD 743
Cdd:cd14624    82 YIDGYRKQNAYIATQGALPETFGDFWRMIWEQRSATVVMMTKLEERSRVKCDQYWPS--RGTETYGLIQVTLLDTVELAT 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578801329  744 YIIQKLNIVnKKEKATGREVTHIQFTSWPDHGVPEDPHLLLKLRRRVNAFSNFFSGPIVVHCSAGVGRTGTYIGIDAMLE 823
Cdd:cd14624   160 YCVRTFALY-KNGSSEKREVRQFQFTAWPDHGVPEHPTPFLAFLRRVKTCNPPDAGPMVVHCSAGVGRTGCFIVIDAMLE 238

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|
gi 578801329  824 GLEAENKVDVYGYVVKLRRQRCLMVQVEAQYILIHQALVE 863
Cdd:cd14624   239 RIKHEKTVDIYGHVTLMRAQRNYMVQTEDQYIFIHDALLE 278
PTPc-KIM cd14547
catalytic domain of the kinase interaction motif (KIM) family of protein-tyrosine phosphatases; ...
 633-859 2.76e-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: 2.76e-72
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578801329  633 NRYVDILPYDYNRVELSEINGDAGSNYINASYIDGFK-EPRKYIAAQGPRDETVDDFWRMIWEQKATVIVMVTRCEEGNR 711
Cdd:cd14547     1 NRYKTILPNEHSRVCLPSVDDDPLSSYINANYIRGYDgEEKAYIATQGPLPNTVADFWRMVWQEKTPIIVMITNLTEAKE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578801329  712 nKCAEYWPsMEEGTRaFGDVVVKINQHKRCPDYIIQKLNIVNKKEKatgREVTHIQFTSWPDHGVPEDPHLLLKLRRRVN 791
Cdd:cd14547    81 -KCAQYWP-EEENET-YGDFEVTVQSVKETDGYTVRKLTLKYGGEK---RYLKHYWYTSWPDHKTPEAAQPLLSLVQEVE 154

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578801329  792 --AFSNFFSGPIVVHCSAGVGRTGTYIGIDAMLEGLEAENKVDVYGYVVKLRRQRCLMVQVEAQYILIHQ 859
Cdd:cd14547   155 eaRQTEPHRGPIVVHCSAGIGRTGCFIATSIGCQQLREEGVVDVLGIVCQLRLDRGGMVQTAEQYEFVHR 224
R-PTPc-O cd14614
catalytic domain of receptor-type tyrosine-protein phosphatase O; Receptor-type ...
 624-859 5.09e-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: 5.09e-72
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578801329  624 ARKPFNQNKNRYVDILPYDYNRVELSEINGDAGSNYINASYIDGFKEPRKYIAAQGPRDETVDDFWRMIWEQKATVIVMV 703
Cdd:cd14614     7 ADLPVNRCKNRYTNILPYDFSRVKLVSMHEEEGSDYINANYIPGYNSPQEYIATQGPLPETRNDFWKMVLQQKSQIIVML 86

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578801329  704 TRCEEGNRNKCAEYWPSMEEGTrAFGDVVVKINQHKRCPDYIIQKLNIVNKKEKatgREVTHIQFTSWPDHGVP--EDPH 781
Cdd:cd14614    87 TQCNEKRRVKCDHYWPFTEEPV-AYGDITVEMLSEEEQPDWAIREFRVSYADEV---QDVMHFNYTAWPDHGVPtaNAAE 162

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 578801329  782 LLLKLRRRVNAFSNFFSGPIVVHCSAGVGRTGTYIGIDAMLEGLEAENKVDVYGYVVKLRRQRCLMVQVEAQYILIHQ 859
Cdd:cd14614   163 SILQFVQMVRQQAVKSKGPMIIHCSAGVGRTGTFIALDRLLQHIRDHEFVDILGLVSEMRSYRMSMVQTEEQYIFIHQ 240
R-PTPc-G-1 cd17667
catalytic domain of receptor-type tyrosine-protein phosphatase G, repeat 1; Receptor-type ...
 605-863 4.68e-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: 238.78  E-value: 4.68e-71
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578801329  605 FLAEFQSIPRVFSKFPI--KEARKPFNQNKNRYVDILPYDYNRVELSEINGDAG--SNYINASYIDGFKEPRKYIAAQGP 680
Cdd:cd17667     1 FSEDFEEVQRCTADMNItaEHSNHPDNKHKNRYINILAYDHSRVKLRPLPGKDSkhSDYINANYVDGYNKAKAYIATQGP 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578801329  681 RDETVDDFWRMIWEQKATVIVMVTRCEEGNRNKCAEYWPSmeEGTRAFGDVVVKINQHKRCPDYIIQKLNIVNKKEK--- 757
Cdd:cd17667    81 LKSTFEDFWRMIWEQNTGIIVMITNLVEKGRRKCDQYWPT--ENSEEYGNIIVTLKSTKIHACYTVRRFSIRNTKVKkgq 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578801329  758 ---ATGRE----VTHIQFTSWPDHGVPEDPHLLLKLRRRVNAFSNFFSGPIVVHCSAGVGRTGTYIGIDAMLEGLEAENK 830
Cdd:cd17667   159 kgnPKGRQnertVIQYHYTQWPDMGVPEYALPVLTFVRRSSAARTPEMGPVLVHCSAGVGRTGTYIVIDSMLQQIKDKST 238

                         250       260       270
                  ....*....|....*....|....*....|...
gi 578801329  831 VDVYGYVVKLRRQRCLMVQVEAQYILIHQALVE 863
Cdd:cd17667   239 VNVLGFLKHIRTQRNYLVQTEEQYIFIHDALLE 271
R-PTPc-T-1 cd14630
catalytic domain of receptor-type tyrosine-protein phosphatase T, repeat 1; Receptor-type ...
 629-863 1.96e-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: 235.69  E-value: 1.96e-70
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578801329  629 NQNKNRYVDILPYDYNRVELSEINGDAGSNYINASYIDGFKEPRKYIAAQGPRDETVDDFWRMIWEQKATVIVMVTRCEE 708
Cdd:cd14630     3 NRNKNRYGNIISYDHSRVRLQLLDGDPHSDYINANYIDGYHRPRHYIATQGPMQETVKDFWRMIWQENSASVVMVTNLVE 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578801329  709 GNRNKCAEYWPsmeEGTRAFGDVVVKINQHKRCPDYIIQKLNiVNKKEKATGREVTHIQFTSWPDHGVPEDPHLLLKLRR 788
Cdd:cd14630    83 VGRVKCVRYWP---DDTEVYGDIKVTLIETEPLAEYVIRTFT-VQKKGYHEIREIRQFHFTSWPDHGVPCYATGLLGFVR 158

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 578801329  789 RVNAFSNFFSGPIVVHCSAGVGRTGTYIGIDAMLEGLEAENKVDVYGYVVKLRRQRCLMVQVEAQYILIHQALVE 863
Cdd:cd14630   159 QVKFLNPPDAGPIVVHCSAGAGRTGCFIAIDIMLDMAENEGVVDIFNCVRELRAQRVNMVQTEEQYVFVHDAILE 233
PTPc-N11_6 cd14544
catalytic domain of tyrosine-protein phosphatase non-receptor type 11 and type 6; ...
 629-864 6.37e-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: 6.37e-69
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578801329  629 NQNKNRYVDILPYDYNRVELSEINGD-AGSNYINASYI-------DGFKEPRKYIAAQGPRDETVDDFWRMIWEQKATVI 700
Cdd:cd14544     1 NKGKNRYKNILPFDHTRVILKDRDPNvPGSDYINANYIrnenegpTTDENAKTYIATQGCLENTVSDFWSMVWQENSRVI 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578801329  701 VMVTRCEEGNRNKCAEYWPSmEEGTRAFGDVVVKINQHKRCPDYIIQKLNIVNKKEKATGREVTHIQFTSWPDHGVPEDP 780
Cdd:cd14544    81 VMTTKEVERGKNKCVRYWPD-EGMQKQYGPYRVQNVSEHDTTDYTLRELQVSKLDQGDPIREIWHYQYLSWPDHGVPSDP 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578801329  781 HLLLKLRRRVNAFSNFF--SGPIVVHCSAGVGRTGTYIGIDAMLE-----GLEAEnkVDVYGYVVKLRRQRCLMVQVEAQ 853
Cdd:cd14544   160 GGVLNFLEDVNQRQESLphAGPIVVHCSAGIGRTGTFIVIDMLLDqikrkGLDCD--IDIQKTIQMVRSQRSGMVQTEAQ 237

                         250
                  ....*....|.
gi 578801329  854 YILIHQALVEY 864
Cdd:cd14544   238 YKFIYVAVAQY 248
R-PTP-LAR-2 cd14554
PTP-like domain of the LAR family receptor-type tyrosine-protein phosphatases, repeat 2; The ...
 624-860 8.09e-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: 231.26  E-value: 8.09e-69
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578801329  624 ARKPFNQNKNRYVDILPYDYNRVELSEINGDAGSNYINASYIDGFKEPRKYIAAQGPRDETVDDFWRMIWEQKATVIVMV 703
Cdd:cd14554     1 ANLPCNKFKNRLVNILPYESTRVCLQPIRGVEGSDYINASFIDGYRQRGAYIATQGPLAETTEDFWRMLWEHNSTIIVML 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578801329  704 TRCEEGNRNKCAEYWPSmEEGTRAFGDVVVKINQHKRcPDYIIQKLNIVNKKEKaTGREVTHIQFTSWPDHGVPEDPHLL 783
Cdd:cd14554    81 TKLREMGREKCHQYWPA-ERSARYQYFVVDPMAEYNM-PQYILREFKVTDARDG-QSRTVRQFQFTDWPEQGVPKSGEGF 157

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 578801329  784 LKLRRRV-NAFSNF-FSGPIVVHCSAGVGRTGTYIGIDAMLEGLEAENKVDVYGYVVKLRRQRCLMVQVEAQYILIHQA 860
Cdd:cd14554   158 IDFIGQVhKTKEQFgQEGPITVHCSAGVGRTGVFITLSIVLERMRYEGVVDVFQTVKLLRTQRPAMVQTEDQYQFCYRA 236
PTP_fungal cd18533
fungal protein tyrosine phosphatases; This subfamily contains Saccharomyces cerevisiae ...
 659-859 7.69e-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: 7.69e-67
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578801329  659 YINASYID-GFKEPRKYIAAQGPRDETVDDFWRMIWEQKATVIVMVTRCEEGNRNKCAEYWPSmEEGTRAFGDVVVKINQ 737
Cdd:cd18533     1 YINASYITlPGTSSKRYIATQGPLPATIGDFWKMIWQNNVGVIVMLTPLVENGREKCDQYWPS-GEYEGEYGDLTVELVS 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578801329  738 HKRCPDYIIQKLNIVNKKEKATGREVTHIQFTSWPDHGVPEDPHLLLKLRRRVNA--FSNFFSGPIVVHCSAGVGRTGTY 815
Cdd:cd18533    80 EEENDDGGFIVREFELSKEDGKVKKVYHIQYKSWPDFGVPDSPEDLLTLIKLKRElnDSASLDPPIIVHCSAGVGRTGTF 159

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 578801329  816 IGIDAMLEGLEA--------ENKVD-VYGYVVKLRRQRCLMVQVEAQYILIHQ 859
Cdd:cd18533   160 IALDSLLDELKRglsdsqdlEDSEDpVYEIVNQLRKQRMSMVQTLRQYIFLYD 212
R-PTPc-V cd14618
catalytic domain of receptor-type tyrosine-protein phosphatase V; Receptor-type ...
 633-862 3.97e-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: 3.97e-66
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578801329  633 NRYVDILPYDYNRVELSEINGDAGSNYINASYIDGFKEPRKYIAAQGPRDETVDDFWRMIWEQKATVIVMVTRCEEGNRN 712
Cdd:cd14618     1 NRYPHVLPYDHSRVRLSQLGGEPHSDYINANFIPGYTSPQEFIATQGPLKKTIEDFWRLVWEQQVCNIIMLTVGMENGRV 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578801329  713 KCAEYWPSmEEGTRAFGDVVVKINQHKRCPDYIIQKLNIVNKKEKATgREVTHIQFTSWPDHGVPEDPHLLLKLRRRVNA 792
Cdd:cd14618    81 LCDHYWPS-ESTPVSYGHITVHLLAQSSEDEWTRREFKLWHEDLRKE-RRVKHLHYTAWPDHGIPESTSSLMAFRELVRE 158

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 578801329  793 F--SNFFSGPIVVHCSAGVGRTGTYIGIDAMLEGLEAENKVDVYGYVVKLRRQRCLMVQVEAQYILIHQALV 862
Cdd:cd14618   159 HvqATKGKGPTLVHCSAGVGRSGTFIALDRLLRQLKEEKVVDVFNTVYILRMHRYLMIQTLSQYIFLHSCIL 230
R-PTPc-M-1 cd14633
catalytic domain of receptor-type tyrosine-protein phosphatase M, repeat 1; Receptor-type ...
 588-863 4.16e-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: 224.92  E-value: 4.16e-66
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578801329  588 DILLETYKRKIAdEGRLFLAEFQSIPRVFSKfPIKEARKPFNQNKNRYVDILPYDYNRVELSEINGDAGSNYINASYIDG 667
Cdd:cd14633     1 DLLQHITQMKCA-EGYGFKEEYESFFEGQSA-PWDSAKKDENRMKNRYGNIIAYDHSRVRLQPIEGETSSDYINGNYIDG 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578801329  668 FKEPRKYIAAQGPRDETVDDFWRMIWEQKATVIVMVTRCEEGNRNKCAEYWPsmeEGTRAFGDVVVKINQHKRCPDYIIQ 747
Cdd:cd14633    79 YHRPNHYIATQGPMQETIYDFWRMVWHENTASIIMVTNLVEVGRVKCCKYWP---DDTEIYKDIKVTLIETELLAEYVIR 155

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578801329  748 KLnIVNKKEKATGREVTHIQFTSWPDHGVPEDPHLLLKLRRRVNAFSNFFSGPIVVHCSAGVGRTGTYIGIDAMLEGLEA 827
Cdd:cd14633   156 TF-AVEKRGVHEIREIRQFHFTGWPDHGVPYHATGLLGFVRQVKSKSPPNAGPLVVHCSAGAGRTGCFIVIDIMLDMAER 234

                         250       260       270
                  ....*....|....*....|....*....|....*.
gi 578801329  828 ENKVDVYGYVVKLRRQRCLMVQVEAQYILIHQALVE 863
Cdd:cd14633   235 EGVVDIYNCVRELRSRRVNMVQTEEQYVFIHDAILE 270
R-PTPc-Z-1 cd17668
catalytic domain of receptor-type tyrosine-protein phosphatase Z, repeat 1; Receptor-type ...
 659-862 3.18e-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: 216.77  E-value: 3.18e-64
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578801329  659 YINASYIDGFKEPRKYIAAQGPRDETVDDFWRMIWEQKATVIVMVTRCEEGNRNKCAEYWPSmeEGTRAFGDVVVKINQH 738
Cdd:cd17668     1 YINANYVDGYNKPKAYIAAQGPLKSTAEDFWRMIWEHNVEVIVMITNLVEKGRRKCDQYWPA--DGSEEYGNFLVTQKSV 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578801329  739 KRCPDYIIQKLNIVN-------KKEKATGREVTHIQFTSWPDHGVPEDPHLLLKLRRRVNAFSNFFSGPIVVHCSAGVGR 811
Cdd:cd17668    79 QVLAYYTVRNFTLRNtkikkgsQKGRPSGRVVTQYHYTQWPDMGVPEYTLPVLTFVRKASYAKRHAVGPVVVHCSAGVGR 158

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|.
gi 578801329  812 TGTYIGIDAMLEGLEAENKVDVYGYVVKLRRQRCLMVQVEAQYILIHQALV 862
Cdd:cd17668   159 TGTYIVLDSMLQQIQHEGTVNIFGFLKHIRSQRNYLVQTEEQYVFIHDALV 209
R-PTPc-Q cd14616
catalytic domain of receptor-type tyrosine-protein phosphatase Q; Receptor-type ...
 633-859 1.09e-63

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: 215.93  E-value: 1.09e-63
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578801329  633 NRYVDILPYDYNRVELSEINGDAGSNYINASYIDGFKEPRKYIAAQGPRDETVDDFWRMIWEQKATVIVMVTRCEEGNRN 712
Cdd:cd14616     1 NRFPNIKPYNNNRVKLIADAGVPGSDYINASYISGYLCPNEFIATQGPLPGTVGDFWRMVWETRAKTIVMLTQCFEKGRI 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578801329  713 KCAEYWPSMEEGTRAFGDVVVKINQHKRCPDYIIQKLNIVNKKEKATgreVTHIQFTSWPDHGVPEDPHLLLKLRRRVNA 792
Cdd:cd14616    81 RCHQYWPEDNKPVTVFGDIVITKLMEDVQIDWTIRDLKIERHGDYMM---VRQCNFTSWPEHGVPESSAPLIHFVKLVRA 157

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 578801329  793 FSNFFSGPIVVHCSAGVGRTGTYIGIDAMLEGLEAENKVDVYGYVVKLRRQRCLMVQVEAQYILIHQ 859
Cdd:cd14616   158 SRAHDNTPMIVHCSAGVGRTGVFIALDHLTQHINDHDFVDIYGLVAELRSERMCMVQNLAQYIFLHQ 224
R-PTPc-typeIIb-1 cd14555
catalytic domain of type IIb (or R2B) subfamily receptor-type tyrosine-protein phosphatases, ...
 659-863 4.23e-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: 213.24  E-value: 4.23e-63
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578801329  659 YINASYIDGFKEPRKYIAAQGPRDETVDDFWRMIWEQKATVIVMVTRCEEGNRNKCAEYWPsmeEGTRAFGDVVVKINQH 738
Cdd:cd14555     1 YINANYIDGYHRPNHYIATQGPMQETVYDFWRMVWQENSASIVMVTNLVEVGRVKCSRYWP---DDTEVYGDIKVTLVET 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578801329  739 KRCPDYIIQKLNiVNKKEKATGREVTHIQFTSWPDHGVPEDPHLLLKLRRRVNAFSNFFSGPIVVHCSAGVGRTGTYIGI 818
Cdd:cd14555    78 EPLAEYVVRTFA-LERRGYHEIREVRQFHFTGWPDHGVPYHATGLLGFIRRVKASNPPSAGPIVVHCSAGAGRTGCYIVI 156

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*
gi 578801329  819 DAMLEGLEAENKVDVYGYVVKLRRQRCLMVQVEAQYILIHQALVE 863
Cdd:cd14555   157 DIMLDMAEREGVVDIYNCVKELRSRRVNMVQTEEQYIFIHDAILE 201
PTPc-N6 cd14606
catalytic domain of tyrosine-protein phosphatase non-receptor type 6; Tyrosine-protein ...
 622-864 9.80e-62

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: 9.80e-62
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578801329  622 KEARKPFNQNKNRYVDILPYDYNRVELSeiNGDA---GSNYINASYID----GFKEPRK-YIAAQGPRDETVDDFWRMIW 693
Cdd:cd14606    11 LEGQRPENKSKNRYKNILPFDHSRVILQ--GRDSnipGSDYINANYVKnqllGPDENAKtYIASQGCLEATVNDFWQMAW 88

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578801329  694 EQKATVIVMVTRCEEGNRNKCAEYWPSMeEGTRAFGDVVVKINQHKRCPDYIIQKLNIVNKKEKATGREVTHIQFTSWPD 773
Cdd:cd14606    89 QENSRVIVMTTREVEKGRNKCVPYWPEV-GMQRAYGPYSVTNCGEHDTTEYKLRTLQVSPLDNGELIREIWHYQYLSWPD 167

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578801329  774 HGVPEDPHLLLKLRRRVNAFSNFF--SGPIVVHCSAGVGRTGTYIGIDAMLEGLEAEN---KVDVYGYVVKLRRQRCLMV 848
Cdd:cd14606   168 HGVPSEPGGVLSFLDQINQRQESLphAGPIIVHCSAGIGRTGTIIVIDMLMENISTKGldcDIDIQKTIQMVRAQRSGMV 247

                         250
                  ....*....|....*.
gi 578801329  849 QVEAQYILIHQALVEY 864
Cdd:cd14606   248 QTEAQYKFIYVAIAQF 263
PTPc-N20_13 cd14538
catalytic domain of tyrosine-protein phosphatase non-receptor type 20 and type 13; ...
 659-863 6.41e-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: 6.41e-61
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578801329  659 YINASYI--DGFKEPRKYIAAQGPRDETVDDFWRMIWEQKATVIVMVTRCEEGNRNKCAEYWP-SMEEGTRAFGDVVVKI 735
Cdd:cd14538     1 YINASHIriPVGGDTYHYIACQGPLPNTTGDFWQMVWEQKSEVIAMVTQDVEGGKVKCHRYWPdSLNKPLICGGRLEVSL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578801329  736 NQHKRCPDYIIQKLNIvnkKEKATG--REVTHIQFTSWPDHGVPEDPHLLLKLRRRVNAFSNffSGPIVVHCSAGVGRTG 813
Cdd:cd14538    81 EKYQSLQDFVIRRISL---RDKETGevHHITHLNFTTWPDHGTPQSADPLLRFIRYMRRIHN--SGPIVVHCSAGIGRTG 155

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|
gi 578801329  814 TYIGIDAMLEGLEAENKVDVYGYVVKLRRQRCLMVQVEAQYILIHQALVE 863
Cdd:cd14538   156 VLITIDVALGLIERDLPFDIQDIVKDLREQRQGMIQTKDQYIFCYKACLE 205
R-PTP-S-2 cd14627
PTP-like domain of receptor-type tyrosine-protein phosphatase S, repeat 2; Receptor-type ...
 624-864 7.74e-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: 7.74e-61
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578801329  624 ARKPFNQNKNRYVDILPYDYNRVELSEINGDAGSNYINASYIDGFKEPRKYIAAQGPRDETVDDFWRMIWEQKATVIVMV 703
Cdd:cd14627    48 ANLPCNKFKNRLVNIMPYETTRVCLQPIRGVEGSDYINASFIDGYRQQKAYIATQGPLAETTEDFWRMLWENNSTIVVML 127

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578801329  704 TRCEEGNRNKCAEYWPSmeEGTRAFGDVVVKINQHKRCPDYIIQKLNIVNKKEkATGREVTHIQFTSWPDHGVPEDPHLL 783
Cdd:cd14627   128 TKLREMGREKCHQYWPA--ERSARYQYFVVDPMAEYNMPQYILREFKVTDARD-GQSRTVRQFQFTDWPEQGVPKSGEGF 204

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578801329  784 LKLRRRVNAFSNFF--SGPIVVHCSAGVGRTGTYIGIDAMLEGLEAENKVDVYGYVVKLRRQRCLMVQVEAQYILIHQAL 861
Cdd:cd14627   205 IDFIGQVHKTKEQFgqDGPISVHCSAGVGRTGVFITLSIVLERMRYEGVVDIFQTVKMLRTQRPAMVQTEDEYQFCYQAA 284


                  ...
gi 578801329  862 VEY 864
Cdd:cd14627   285 LEY 287
R-PTP-D-2 cd14628
PTP-like domain of receptor-type tyrosine-protein phosphatase D, repeat 2; Receptor-type ...
 624-864 1.35e-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: 209.59  E-value: 1.35e-60
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578801329  624 ARKPFNQNKNRYVDILPYDYNRVELSEINGDAGSNYINASYIDGFKEPRKYIAAQGPRDETVDDFWRMIWEQKATVIVMV 703
Cdd:cd14628    47 ANLPCNKFKNRLVNIMPYESTRVCLQPIRGVEGSDYINASFIDGYRQQKAYIATQGPLAETTEDFWRMLWEHNSTIVVML 126

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578801329  704 TRCEEGNRNKCAEYWPSmeEGTRAFGDVVVKINQHKRCPDYIIQKLNIVNKKEkATGREVTHIQFTSWPDHGVPEDPHLL 783
Cdd:cd14628   127 TKLREMGREKCHQYWPA--ERSARYQYFVVDPMAEYNMPQYILREFKVTDARD-GQSRTVRQFQFTDWPEQGVPKSGEGF 203

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578801329  784 LKLRRRVNAFSNFF--SGPIVVHCSAGVGRTGTYIGIDAMLEGLEAENKVDVYGYVVKLRRQRCLMVQVEAQYILIHQAL 861
Cdd:cd14628   204 IDFIGQVHKTKEQFgqDGPISVHCSAGVGRTGVFITLSIVLERMRYEGVVDIFQTVKMLRTQRPAMVQTEDQYQFCYRAA 283


                  ...
gi 578801329  862 VEY 864
Cdd:cd14628   284 LEY 286
R-PTP-F-2 cd14629
PTP-like domain of receptor-type tyrosine-protein phosphatase F, repeat 2; Receptor-type ...
 624-864 2.43e-60

PTP-like domain of receptor-type tyrosine-protein phosphatase F, repeat 2; Receptor-type tyrosine-protein phosphatase F (PTPRF), also known as leukocyte common antigen related (LAR), is the prototypical member of the LAR family of receptor-type tyrosine-protein phosphatases (RPTPs), which belong to the larger family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. PTPRF/LAR plays a role for LAR in cadherin complexes where it associates with and dephosphorylates beta-catenin, a pathway which may be critical for cadherin complex stability and cell-cell association. It also regulates focal adhesions through cyclin-dependent kinase-1 and is involved in axon guidance in the developing nervous system. It also functions in regulating insulin signaling. PTPRF contains an extracellular region with three immunoglobulin-like (Ig) domains and four to eight fibronectin type III (FN3) repeats (determined by alternative splicing), a single transmembrane domain, followed by an intracellular region with a membrane-proximal catalytic PTP domain (repeat 1, also called D1) and a membrane-distal non-catalytic PTP-like domain (repeat 2, also called D2). This model represents the non-catalytic PTP-like domain (repeat 2). Although described as non-catalytic, this domain contains the catalytic cysteine and the active site signature motif, HCSAGxGRxG.


Pssm-ID: 350477 [Multi-domain]  Cd Length: 291  Bit Score: 208.81  E-value: 2.43e-60
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578801329  624 ARKPFNQNKNRYVDILPYDYNRVELSEINGDAGSNYINASYIDGFKEPRKYIAAQGPRDETVDDFWRMIWEQKATVIVMV 703
Cdd:cd14629    48 ANLPCNKFKNRLVNIMPYELTRVCLQPIRGVEGSDYINASFIDGYRQQKAYIATQGPLAETTEDFWRMLWEHNSTIVVML 127

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578801329  704 TRCEEGNRNKCAEYWPSmeEGTRAFGDVVVKINQHKRCPDYIIQKLNIVNKKEkATGREVTHIQFTSWPDHGVPEDPHLL 783
Cdd:cd14629   128 TKLREMGREKCHQYWPA--ERSARYQYFVVDPMAEYNMPQYILREFKVTDARD-GQSRTIRQFQFTDWPEQGVPKTGEGF 204

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578801329  784 LKLRRRVNAFSNFF--SGPIVVHCSAGVGRTGTYIGIDAMLEGLEAENKVDVYGYVVKLRRQRCLMVQVEAQYILIHQAL 861
Cdd:cd14629   205 IDFIGQVHKTKEQFgqDGPITVHCSAGVGRTGVFITLSIVLERMRYEGVVDMFQTVKTLRTQRPAMVQTEDQYQLCYRAA 284


                  ...
gi 578801329  862 VEY 864
Cdd:cd14629   285 LEY 287
R-PTPc-K-1 cd14631
catalytic domain of receptor-type tyrosine-protein phosphatase K, repeat 1; Receptor-type ...
 645-863 2.45e-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: 206.02  E-value: 2.45e-60
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578801329  645 RVELSEINGDAGSNYINASYIDGFKEPRKYIAAQGPRDETVDDFWRMIWEQKATVIVMVTRCEEGNRNKCAEYWPsmeEG 724
Cdd:cd14631     1 RVILQPVEDDPSSDYINANYIDGYQRPSHYIATQGPVHETVYDFWRMIWQEQSACIVMVTNLVEVGRVKCYKYWP---DD 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578801329  725 TRAFGDVVVKINQHKRCPDYIIQKLNIvNKKEKATGREVTHIQFTSWPDHGVPEDPHLLLKLRRRVNAFSNFFSGPIVVH 804
Cdd:cd14631    78 TEVYGDFKVTCVEMEPLAEYVVRTFTL-ERRGYNEIREVKQFHFTGWPDHGVPYHATGLLSFIRRVKLSNPPSAGPIVVH 156

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 578801329  805 CSAGVGRTGTYIGIDAMLEGLEAENKVDVYGYVVKLRRQRCLMVQVEAQYILIHQALVE 863
Cdd:cd14631   157 CSAGAGRTGCYIVIDIMLDMAEREGVVDIYNCVKALRSRRINMVQTEEQYIFIHDAILE 215
PTPc-N7 cd14612
catalytic domain of tyrosine-protein phosphatase non-receptor type 7; Tyrosine-protein ...
 627-864 1.02e-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: 1.02e-59
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578801329  627 PFNQNKNRYVDILPYDYNRVEL-SEINGDAGSNYINASYIDGFK-EPRKYIAAQGPRDETVDDFWRMIWEQKATVIVMVT 704
Cdd:cd14612    13 PGHASKDRYKTILPNPQSRVCLrRAGSQEEEGSYINANYIRGYDgKEKAYIATQGPMLNTVSDFWEMVWQEECPIIVMIT 92

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578801329  705 RCEEGNRnKCAEYWPSmEEGTraFGDVVVKINQHKRCPDYIIQKLNIVNKKEKatgREVTHIQFTSWPDHGVPEDPHLLL 784
Cdd:cd14612    93 KLKEKKE-KCVHYWPE-KEGT--YGRFEIRVQDMKECDGYTIRDLTIQLEEES---RSVKHYWFSSWPDHQTPESAGPLL 165

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578801329  785 KL-----RRRVNAFSnffSGPIVVHCSAGVGRTGTYIGIDAMLEGLEAENKVDVYGYVVKLRRQRCLMVQVEAQYILIHQ 859
Cdd:cd14612   166 RLvaeveESRQTAAS---PGPIVVHCSAGIGRTGCFIATSIGCQQLKDTGKVDILGIVCQLRLDRGGMIQTSEQYQFLHH 242


                  ....*
gi 578801329  860 ALVEY 864
Cdd:cd14612   243 TLALY 247
R-PTPc-A-E-2 cd14552
catalytic domain of receptor-type tyrosine-protein phosphatase A and E, repeat 2; ...
 969-1177 1.47e-59

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: 203.27  E-value: 1.47e-59
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578801329  969 YINASFIMSYWKPEVMIAAQGPLKETIGDFWQMIFQRKVKVIVMLTELKHGDQEICAQYW-GEGKQTYGDIEVDLKDTDK 1047
Cdd:cd14552     1 YINASFIDGYRQKDAYIATQGPLDHTVEDFWRMIWEWKSCSIVMLTEIKERSQNKCAQYWpEDGSVSSGDITVELKDQTD 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578801329 1048 SSTYTLRVFELRHSKRKDSRTVYQYQYTNWSVEQLPAEPKELISMIQVVkqklpQKNSSEGNKHhkstPLLIHCRDGSQQ 1127
Cdd:cd14552    81 YEDYTLRDFLVTKGKGGSTRTVRQFHFHGWPEVGIPDNGKGMIDLIAAV-----QKQQQQSGNH----PITVHCSAGAGR 151

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|
gi 578801329 1128 TGIFCALLNLLESAETEEVVDIFQVVKALRKARPGMVSTFEQYQFLYDVI 1177
Cdd:cd14552   152 TGTFCALSTVLERVKAEGVLDVFQVVKSLRLQRPHMVQTLEQYEFCYKVV 201
R-PTPc-U-1 cd14632
catalytic domain of receptor-type tyrosine-protein phosphatase U, repeat 1; Receptor-type ...
 659-863 1.02e-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: 1.02e-57
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578801329  659 YINASYIDGFKEPRKYIAAQGPRDETVDDFWRMIWEQKATVIVMVTRCEEGNRNKCAEYWPsmeEGTRAFGDVVVKINQH 738
Cdd:cd14632     1 YINANYIDGYHRSNHFIATQGPKQEMVYDFWRMVWQEHCSSIVMITKLVEVGRVKCSKYWP---DDSDTYGDIKITLLKT 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578801329  739 KRCPDYIIQKLNIvNKKEKATGREVTHIQFTSWPDHGVPEDPHLLLKLRRRVNAFSNFFSGPIVVHCSAGVGRTGTYIGI 818
Cdd:cd14632    78 ETLAEYSVRTFAL-ERRGYSARHEVKQFHFTSWPEHGVPYHATGLLAFIRRVKASTPPDAGPVVVHCSAGAGRTGCYIVL 156

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*
gi 578801329  819 DAMLEGLEAENKVDVYGYVVKLRRQRCLMVQVEAQYILIHQALVE 863
Cdd:cd14632   157 DVMLDMAECEGVVDIYNCVKTLCSRRINMIQTEEQYIFIHDAILE 201
PTPc-N21_14 cd14540
catalytic domain of tyrosine-protein phosphatase non-receptor type 21 and type 14; ...
 659-864 1.46e-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: 1.46e-57
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578801329  659 YINASYID---GFKEpRKYIAAQGPRDETVDDFWRMIWEQKATVIVMVTRCEEGNRNKCAEYWPSM--EEGTRAFGD--V 731
Cdd:cd14540     1 YINASHITatvGGKQ-RFYIAAQGPLQNTVGDFWQMVWEQGVYLVVMVTAEEEGGREKCFRYWPTLggEHDALTFGEykV 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578801329  732 VVKINQHKRCpdYIIQKLNIVNKKEKaTGREVTHIQFTSWPDHGVPEDPHLLL-------KLRRRVNAFS--NFFSGPIV 802
Cdd:cd14540    80 STKFSVSSGC--YTTTGLRVKHTLSG-QSRTVWHLQYTDWPDHGCPEDVSGFLdfleeinSVRRHTNQDVagHNRNPPTL 156

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 578801329  803 VHCSAGVGRTGTYIGIDAMLEGLEAENKVDVYGYVVKLRRQRCLMVQVEAQYILIHQALVEY 864
Cdd:cd14540   157 VHCSAGVGRTGVVILADLMLYCLDHNEELDIPRVLALLRHQRMLLVQTLAQYKFVYNVLIQY 218
R-PTPc-A-2 cd14623
catalytic domain of receptor-type tyrosine-protein phosphatase A, repeat 2; Receptor-type ...
 634-863 1.57e-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: 198.35  E-value: 1.57e-57
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578801329  634 RYVDILPYDYNRVELSEINGDAGSNYINASYIDGFKEPRKYIAAQGPRDETVDDFWRMIWEQKATVIVMVTRCEEGNRNK 713
Cdd:cd14623     1 RVLQIIPYEFNRVIIPVKRGEENTDYVNASFIDGYRQKDSYIASQGPLQHTIEDFWRMIWEWKSCSIVMLTELEERGQEK 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578801329  714 CAEYWPSmeEGTRAFGDVVVKINQHKRCPDYIIQKLNIVNKKEKATgREVTHIQFTSWPDHGVPEDP----HLLLKLRRR 789
Cdd:cd14623    81 CAQYWPS--DGSVSYGDITIELKKEEECESYTVRDLLVTNTRENKS-RQIRQFHFHGWPEVGIPSDGkgmiNIIAAVQKQ 157

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 578801329  790 VNAFSNFfsgPIVVHCSAGVGRTGTYIGIDAMLEGLEAENKVDVYGYVVKLRRQRCLMVQVEAQYILIHQALVE 863
Cdd:cd14623   158 QQQSGNH---PITVHCSAGAGRTGTFCALSTVLERVKAEGILDVFQTVKSLRLQRPHMVQTLEQYEFCYKVVQE 228
PTPc-N11 cd14605
catalytic domain of tyrosine-protein phosphatase non-receptor type 11; Tyrosine-protein ...
 629-864 2.05e-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: 2.05e-57
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578801329  629 NQNKNRYVDILPYDYNRVELSEinGDA---GSNYINASYI--------DGFKEPRKYIAAQGPRDETVDDFWRMIWEQKA 697
Cdd:cd14605     2 NKNKNRYKNILPFDHTRVVLHD--GDPnepVSDYINANIImpefetkcNNSKPKKSYIATQGCLQNTVNDFWRMVFQENS 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578801329  698 TVIVMVTRCEEGNRNKCAEYWPSmEEGTRAFGDVVVKINQHKRCPDYIIQKLNIVNKKEKATGREVTHIQFTSWPDHGVP 777
Cdd:cd14605    80 RVIVMTTKEVERGKSKCVKYWPD-EYALKEYGVMRVRNVKESAAHDYILRELKLSKVGQGNTERTVWQYHFRTWPDHGVP 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578801329  778 EDPHLLLKLRRRVNAFSNFFS--GPIVVHCSAGVGRTGTYIGIDAMLEGLEAEN---KVDVYGYVVKLRRQRCLMVQVEA 852
Cdd:cd14605   159 SDPGGVLDFLEEVHHKQESIMdaGPVVVHCSAGIGRTGTFIVIDILIDIIREKGvdcDIDVPKTIQMVRSQRSGMVQTEA 238

                         250
                  ....*....|..
gi 578801329  853 QYILIHQALVEY 864
Cdd:cd14605   239 QYRFIYMAVQHY 250
PTPc-N18 cd14603
catalytic domain of tyrosine-protein phosphatase non-receptor type 18; Tyrosine-protein ...
 629-863 4.35e-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: 198.51  E-value: 4.35e-57
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578801329  629 NQNKNRYVDILPYDYNRVELSEINGDAGSNYINASYIDGFKEPRKYIAAQGPRDETVDDFWRMIWEQKATVIVMVTRCEE 708
Cdd:cd14603    30 NVKKNRYKDILPYDQTRVILSLLQEEGHSDYINANFIKGVDGSRAYIATQGPLSHTVLDFWRMIWQYGVKVILMACREIE 109

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578801329  709 GNRNKCAEYWPSMEEgTRAFGD-VVVKINQHKRCPDYIIQKLNIVNKKEKatgREVTHIQFTSWPDHGVPEDPHLLLKLR 787
Cdd:cd14603   110 MGKKKCERYWAQEQE-PLQTGPfTITLVKEKRLNEEVILRTLKVTFQKES---RSVSHFQYMAWPDHGIPDSPDCMLAMI 185

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 578801329  788 RRVNAFSNFFSGPIVVHCSAGVGRTGTYIGIDAMLEGLEAEN---KVDVYGYVVKLRRQRCLMVQVEAQYILIHQALVE 863
Cdd:cd14603   186 ELARRLQGSGPEPLCVHCSAGCGRTGVICTVDYVRQLLLTQRippDFSIFDVVLEMRKQRPAAVQTEEQYEFLYHTVAQ 264
PTPc-N13 cd14597
catalytic domain of tyrosine-protein phosphatase non-receptor type 13; Tyrosine-protein ...
 629-862 8.75e-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: 8.75e-57
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578801329  629 NQNKNRYVDILPYDYNRVELSEINGdagsnYINASYIdgfKEPRK-----YIAAQGPRDETVDDFWRMIWEQKATVIVMV 703
Cdd:cd14597     3 NRKKNRYKNILPYDTTRVPLGDEGG-----YINASFI---KMPVGdeefvYIACQGPLPTTVADFWQMVWEQKSTVIAMM 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578801329  704 TRCEEGNRNKCAEYWPSMEEGTRAFGD----VVVKINQHKrcpDYIIQKLNIVNKKEKATgREVTHIQFTSWPDHGVPED 779
Cdd:cd14597    75 TQEVEGGKIKCQRYWPEILGKTTMVDNrlqlTLVRMQQLK---NFVIRVLELEDIQTREV-RHITHLNFTAWPDHDTPSQ 150

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578801329  780 PHLLLKL---RRRVNAfsnffSGPIVVHCSAGVGRTGTYIGIDAMLEGLEAENKVDVYGYVVKLRRQRCLMVQVEAQYIL 856
Cdd:cd14597   151 PEQLLTFisyMRHIHK-----SGPIITHCSAGIGRSGTLICIDVVLGLISKDLDFDISDIVRTMRLQRHGMVQTEDQYIF 225


                  ....*.
gi 578801329  857 IHQALV 862
Cdd:cd14597   226 CYQVIL 231
PTPc-N22_18_12 cd14542
catalytic domain of tyrosine-protein phosphatase non-receptor type 22, type 18 and type 12; ...
 659-859 5.11e-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: 193.02  E-value: 5.11e-56
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578801329  659 YINASYIDGFKEPRKYIAAQGPRDETVDDFWRMIWEQKATVIVMVTRCEEGNRNKCAEYWPSMEEGTRAFGDVVVK-INQ 737
Cdd:cd14542     1 YINANFIKGVSGSKAYIATQGPLPNTVLDFWRMIWEYNVQVIVMACREFEMGKKKCERYWPEEGEEQLQFGPFKISlEKE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578801329  738 HKRCPDYIIQKLNIVNKKEKatgREVTHIQFTSWPDHGVPEDPHLLLKLRRRVNAFSNFFSGPIVVHCSAGVGRTGTYIG 817
Cdd:cd14542    81 KRVGPDFLIRTLKVTFQKES---RTVYQFHYTAWPDHGVPSSVDPILDLVRLVRDYQGSEDVPICVHCSAGCGRTGTICA 157

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*.
gi 578801329  818 ID----AMLEGLEAENkVDVYGYVVKLRRQRCLMVQVEAQYILIHQ 859
Cdd:cd14542   158 IDyvwnLLKTGKIPEE-FSLFDLVREMRKQRPAMVQTKEQYELVYR 202
PTPc-N1_2 cd14545
catalytic domain of tyrosine-protein phosphatase non-receptor type 1 and type 2; ...
 632-853 5.80e-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: 5.80e-56
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578801329  632 KNRYVDILPYDYNRVELSEINGDagSNYINASYIDGFKEPRKYIAAQGPRDETVDDFWRMIWEQKATVIVMVTRCEEGNR 711
Cdd:cd14545     1 LNRYRDRDPYDHDRSRVKLKQGD--NDYINASLVEVEEAKRSYILTQGPLPNTSGHFWQMVWEQNSKAVIMLNKLMEKGQ 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578801329  712 NKCAEYWPSMEEGTRAFGDVVVKIN--QHKRCPDYIIQKLNIVNKKEKATgREVTHIQFTSWPDHGVPEDP----HLLLK 785
Cdd:cd14545    79 IKCAQYWPQGEGNAMIFEDTGLKVTllSEEDKSYYTVRTLELENLKTQET-REVLHFHYTTWPDFGVPESPaaflNFLQK 157

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578801329  786 LRRRVNAFSNFfsGPIVVHCSAGVGRTGTYIGIDAMLEGLEAEN--KVDVYGYVVKLRRQRCLMVQVEAQ 853
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; ...
 659-862 6.47e-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: 6.47e-56
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578801329  659 YINASYIDGFKEPRKYIAAQGPRDETVDDFWRMIWEQKATVIVMVTRCEEGNRNKCAEYWPsmEEGTRAFGDVVVKINQH 738
Cdd:cd14552     1 YINASFIDGYRQKDAYIATQGPLDHTVEDFWRMIWEWKSCSIVMLTEIKERSQNKCAQYWP--EDGSVSSGDITVELKDQ 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578801329  739 KRCPDYIIQKLNIVNKKEKATgREVTHIQFTSWPDHGVPEDP----HLLLKLRRRVNAFSNffsGPIVVHCSAGVGRTGT 814
Cdd:cd14552    79 TDYEDYTLRDFLVTKGKGGST-RTVRQFHFHGWPEVGIPDNGkgmiDLIAAVQKQQQQSGN---HPITVHCSAGAGRTGT 154

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*...
gi 578801329  815 YIGIDAMLEGLEAENKVDVYGYVVKLRRQRCLMVQVEAQYILIHQALV 862
Cdd:cd14552   155 FCALSTVLERVKAEGVLDVFQVVKSLRLQRPHMVQTLEQYEFCYKVVQ 202
R-PTPc-A-2 cd14623
catalytic domain of receptor-type tyrosine-protein phosphatase A, repeat 2; Receptor-type ...
 925-1177 2.87e-55

catalytic domain of receptor-type tyrosine-protein phosphatase A, repeat 2; Receptor-type tyrosine-protein phosphatase A (PTPRA), also known as receptor-type tyrosine-protein phosphatase alpha (R-PTP-alpha), belongs to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. PTPRA is a positive regulator of Src and Src family kinases via dephosphorylation of the Src-inhibitory tyrosine 527. Thus, it affects transformation and tumorigenesis, inhibition of proliferation, cell cycle arrest, integrin signaling, neuronal differentiation and outgrowth, and ion channel activity. It is also involved in interleukin-1 signaling in fibroblasts through its interaction with the focal adhesion targeting domain of focal adhesion kinase. PTPRA comprises a small extracellular domain, a transmembrane segment, and an intracellular region containing two tandem catalytic PTP domains. This model represents the second PTP domain (repeat 2).


Pssm-ID: 350471 [Multi-domain]  Cd Length: 228  Bit Score: 191.80  E-value: 2.87e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578801329  925 RNSNVIPYDYNRV--PLKHELEmskesehdsdessdddsdseePSKYINASFIMSYWKPEVMIAAQGPLKETIGDFWQMI 1002
Cdd:cd14623     1 RVLQIIPYEFNRViiPVKRGEE---------------------NTDYVNASFIDGYRQKDSYIASQGPLQHTIEDFWRMI 59

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578801329 1003 FQRKVKVIVMLTELKHGDQEICAQYW-GEGKQTYGDIEVDLKDTDKSSTYTLRVFELRHSKRKDSRTVYQYQYTNWSVEQ 1081
Cdd:cd14623    60 WEWKSCSIVMLTELEERGQEKCAQYWpSDGSVSYGDITIELKKEEECESYTVRDLLVTNTRENKSRQIRQFHFHGWPEVG 139

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578801329 1082 LPAEPKELISMIQVVkqklpQKNSSEGNKHhkstPLLIHCRDGSQQTGIFCALLNLLESAETEEVVDIFQVVKALRKARP 1161
Cdd:cd14623   140 IPSDGKGMINIIAAV-----QKQQQQSGNH----PITVHCSAGAGRTGTFCALSTVLERVKAEGILDVFQTVKSLRLQRP 210

                         250
                  ....*....|....*.
gi 578801329 1162 GMVSTFEQYQFLYDVI 1177
Cdd:cd14623   211 HMVQTLEQYEFCYKVV 226
PTPc-N14 cd14599
catalytic domain of tyrosine-protein phosphatase non-receptor type 14; Tyrosine-protein ...
 592-864 5.53e-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: 5.53e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578801329  592 ETYKRKIaDEGRLFlAEFQSIPRVFSKFPIKEARKPFNQNKNRYVDILPYDYNRVELSEiNGDAGSNYINASYIDGF--K 669
Cdd:cd14599     3 KTLERKL-EEGMVF-TEYEQIPKKKADGVFTTATLPENAERNRIREVVPYEENRVELVP-TKENNTGYINASHIKVTvgG 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578801329  670 EPRKYIAAQGPRDETVDDFWRMIWEQKATVIVMVTRCEEGNRNKCAEYWPSM--EEGTRAFGD--VVVKINQHKRCpdYI 745
Cdd:cd14599    80 EEWHYIATQGPLPHTCHDFWQMVWEQGVNVIAMVTAEEEGGRSKSHRYWPKLgsKHSSATYGKfkVTTKFRTDSGC--YA 157

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578801329  746 IQKLNIvnkKEKATGREVT--HIQFTSWPDHGVPEDPHLLLK-------LRRRVNAF---SNFFSGPIVVHCSAGVGRTG 813
Cdd:cd14599   158 TTGLKV---KHLLSGQERTvwHLQYTDWPDHGCPEEVQGFLSyleeiqsVRRHTNSMldsTKNCNPPIVVHCSAGVGRTG 234

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|.
gi 578801329  814 TYIGIDAMLEGLEAENKVDVYGYVVKLRRQRCLMVQVEAQYILIHQALVEY 864
Cdd:cd14599   235 VVILTELMIGCLEHNEKVEVPVMLRHLREQRMFMIQTIAQYKFVYQVLIQF 285
R3-PTPc cd14548
catalytic domain of R3 subfamily receptor-type tyrosine-protein phosphatases and similar ...
 925-1174 7.54e-55

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: 190.64  E-value: 7.54e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578801329  925 RNSNVIPYDYNRVPLKhelemskesehdsdessddDSDSEEPSKYINASFIMSYWKPEVMIAAQGPLKETIGDFWQMIFQ 1004
Cdd:cd14548     1 RYTNILPYDHSRVKLI-------------------PINEEEGSDYINANYIPGYNSPREFIATQGPLPGTKDDFWRMVWE 61

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578801329 1005 RKVKVIVMLTELKHGDQEICAQYWGEGKQ--TYGDIEVDLKDTDKSSTYTLRVFELRHskRKDSRTVYQYQYTNWSVEQL 1082
Cdd:cd14548    62 QNSHTIVMLTQCMEKGRVKCDHYWPFDQDpvYYGDITVTMLSESVLPDWTIREFKLER--GDEVRSVRQFHFTAWPDHGV 139

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578801329 1083 PAEPKELISMIQVVKQKLPQKNssegnkhhksTPLLIHCRDGSQQTGIFCALLNLLESAETEEVVDIFQVVKALRKARPG 1162
Cdd:cd14548   140 PEAPDSLLRFVRLVRDYIKQEK----------GPTIVHCSAGVGRTGTFIALDRLLQQIESEDYVDIFGIVYDLRKHRPL 209

                         250
                  ....*....|..
gi 578801329 1163 MVSTFEQYQFLY 1174
Cdd:cd14548   210 MVQTEAQYIFLH 221
R5-PTPc-1 cd14549
catalytic domain of R5 subfamily receptor-type tyrosine-protein phosphatases, repeat 1; The R5 ...
 969-1175 1.43e-54

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: 189.10  E-value: 1.43e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578801329  969 YINASFIMSYWKPEVMIAAQGPLKETIGDFWQMIFQRKVKVIVMLTELKHGDQEICAQYW-GEGKQTYGDIEVDLKDTDK 1047
Cdd:cd14549     1 YINANYVDGYNKARAYIATQGPLPSTFDDFWRMVWEQNSAIIVMITNLVERGRRKCDQYWpKEGTETYGNIQVTLLSTEV 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578801329 1048 SSTYTLRVFELRHSK------RKDSRTVYQYQYTNWSVEQLPAEPKELISMIQvvkqklpqkNSSEGNKHHkSTPLLIHC 1121
Cdd:cd14549    81 LATYTVRTFSLKNLKlkkvkgRSSERVVYQYHYTQWPDHGVPDYTLPVLSFVR---------KSSAANPPG-AGPIVVHC 150

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....
gi 578801329 1122 RDGSQQTGIFCALLNLLESAETEEVVDIFQVVKALRKARPGMVSTFEQYQFLYD 1175
Cdd:cd14549   151 SAGVGRTGTYIVIDSMLQQIQDKGTVNVFGFLKHIRTQRNYLVQTEEQYIFIHD 204
R-PTPc-LAR-1 cd14553
catalytic domain of LAR family receptor-type tyrosine-protein phosphatases, repeat 1; The LAR ...
 918-1177 1.50e-54

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: 190.30  E-value: 1.50e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578801329  918 EENKSKNRNSNVIPYDYNRVPLKhelemskesehdsdessddDSDSEEPSKYINASFIMSYWKPEVMIAAQGPLKETIGD 997
Cdd:cd14553     1 EVNKPKNRYANVIAYDHSRVILQ-------------------PIEGVPGSDYINANYCDGYRKQNAYIATQGPLPETFGD 61

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578801329  998 FWQMIFQRKVKVIVMLTELKHGDQEICAQYW-GEGKQTYGDIEVDLKDTDKSSTYTLRVFELRHSKRKDSRTVYQYQYTN 1076
Cdd:cd14553    62 FWRMVWEQRSATIVMMTKLEERSRVKCDQYWpTRGTETYGLIQVTLLDTVELATYTVRTFALHKNGSSEKREVRQFQFTA 141

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578801329 1077 WSVEQLPAEPKELISMIQVVKQKLPQknssegnkhhKSTPLLIHCRDGSQQTGIFCALLNLLESAETEEVVDIFQVVKAL 1156
Cdd:cd14553   142 WPDHGVPEHPTPFLAFLRRVKACNPP----------DAGPIVVHCSAGVGRTGCFIVIDSMLERIKHEKTVDIYGHVTCL 211

                         250       260
                  ....*....|....*....|.
gi 578801329 1157 RKARPGMVSTFEQYQFLYDVI 1177
Cdd:cd14553   212 RAQRNYMVQTEDQYIFIHDAL 232
R-PTPc-E-2 cd14622
catalytic domain of receptor-type tyrosine-protein phosphatase E, repeat 2; Receptor-type ...
 969-1177 2.97e-54

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: 188.29  E-value: 2.97e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578801329  969 YINASFIMSYWKPEVMIAAQGPLKETIGDFWQMIFQRKVKVIVMLTELKHGDQEICAQYW-GEGKQTYGDIEVDLKDTDK 1047
Cdd:cd14622     2 YINASFIDGYRQKDYFIATQGPLAHTVEDFWRMVWEWKCHTIVMLTELQEREQEKCVQYWpSEGSVTHGEITIEIKNDTL 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578801329 1048 SSTYTLRVFELRHSKRKDSRTVYQYQYTNWSVEQLPAEPKELISMIQVVkqklpQKNSSEGNKHhkstPLLIHCRDGSQQ 1127
Cdd:cd14622    82 LETISIRDFLVTYNQEKQTRLVRQFHFHGWPEIGIPAEGKGMIDLIAAV-----QKQQQQTGNH----PIVVHCSAGAGR 152

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|
gi 578801329 1128 TGIFCALLNLLESAETEEVVDIFQVVKALRKARPGMVSTFEQYQFLYDVI 1177
Cdd:cd14622   153 TGTFIALSNILERVKAEGLLDVFQTVKSLRLQRPHMVQTLEQYEFCYRVV 202
PTPc-N3_4 cd14541
catalytic domain of tyrosine-protein phosphatase non-receptor type 21 and type 14; ...
 659-854 6.52e-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: 6.52e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578801329  659 YINASYID----GFKEPRKYIAAQGPRDETVDDFWRMIWEQKATVIVMVTRCEEGNRNKCAEYWPSMEEgTRAFGDVVVK 734
Cdd:cd14541     2 YINANYVNmeipGSGIVNRYIAAQGPLPNTCADFWQMVWEQKSTLIVMLTTLVERGRVKCHQYWPDLGE-TMQFGNLQIT 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578801329  735 INQHKRCPDYIIQKLNIVNKKEKATgREVTHIQFTSWPDHGVPEDPHLLLKLRRRVNAFSNFFSGPIVVHCSAGVGRTGT 814
Cdd:cd14541    81 CVSEEVTPSFAFREFILTNTNTGEE-RHITQMQYLAWPDHGVPDDSSDFLDFVKRVRQNRVGMVEPTVVHCSAGIGRTGV 159

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|
gi 578801329  815 YIGIDAMLEGLEAENKVDVYGYVVKLRRQRCLMVQVEAQY 854
Cdd:cd14541   160 LITMETAMCLIEANEPVYPLDIVRTMRDQRAMLIQTPSQY 199
PTPc-N22 cd14602
catalytic domain of tyrosine-protein phosphatase non-receptor type 22; Tyrosine-protein ...
 632-863 8.50e-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: 8.50e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578801329  632 KNRYVDILPYDYNRVELSEINGDAGSNYINASYIDGFKEPRKYIAAQGPRDETVDDFWRMIWEQKATVIVMVTRCEEGNR 711
Cdd:cd14602     1 KNRYKDILPYDHSRVELSLITSDEDSDYINANFIKGVYGPRAYIATQGPLSTTLLDFWRMIWEYSVLIIVMACMEFEMGK 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578801329  712 NKCAEYWPSMEEGTRAFGDVVVKINQHKRCPDYIIQKLNIVNKKEKatgREVTHIQFTSWPDHGVPEDPHLLLKLRRRVN 791
Cdd:cd14602    81 KKCERYWAEPGEMQLEFGPFSVTCEAEKRKSDYIIRTLKVKFNSET---RTIYQFHYKNWPDHDVPSSIDPILELIWDVR 157

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 578801329  792 AFSNFFSGPIVVHCSAGVGRTGTYIGID----AMLEGLEAENkVDVYGYVVKLRRQRCLMVQVEAQYILIHQALVE 863
Cdd:cd14602   158 CYQEDDSVPICIHCSAGCGRTGVICAIDytwmLLKDGIIPEN-FSVFSLIQEMRTQRPSLVQTKEQYELVYNAVIE 232
R-PTP-C-2 cd14558
PTP-like domain of receptor-type tyrosine-protein phosphatase C, repeat 2; Receptor-type ...
 659-854 1.21e-53

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: 186.44  E-value: 1.21e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578801329  659 YINASYIDGFKEPRKYIAAQGPRDETVDDFWRMIWEQKATVIVMVTRCEEGNRNKCAEYWPsmeEGTRAFGDVVVKINQH 738
Cdd:cd14558     1 YINASFIDGYWGPKSLIATQGPLPDTIADFWQMIFQKKVKVIVMLTELKEGDQEQCAQYWG---DEKKTYGDIEVELKDT 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578801329  739 KRCPDYIIQKLNIVNKKEKATgREVTHIQFTSWPDHGVPEDPHLLLKLRRRV------NAFSNFFSGPIVVHCSAGVGRT 812
Cdd:cd14558    78 EKSPTYTVRVFEITHLKRKDS-RTVYQYQYHKWKGEELPEKPKDLVDMIKSIkqklpyKNSKHGRSVPIVVHCSDGSSRT 156

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|..
gi 578801329  813 GTYIGIDAMLEGLEAENKVDVYGYVVKLRRQRCLMVQVEAQY 854
Cdd:cd14558   157 GIFCALWNLLESAETEKVVDVFQVVKALRKQRPGMVSTLEQY 198
PTPc-N12 cd14604
catalytic domain of tyrosine-protein phosphatase non-receptor type 12; Tyrosine-protein ...
 605-863 3.05e-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: 188.60  E-value: 3.05e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578801329  605 FLAEFQSIPRVFSKF------PIKEARKPFNQNKNRYVDILPYDYNRVELSEINGDAGSNYINASYIDGFKEPRKYIAAQ 678
Cdd:cd14604    27 FASDFMRLRRLSTKYrtekiyPTATGEKEENVKKNRYKDILPFDHSRVKLTLKTSSQDSDYINANFIKGVYGPKAYIATQ 106

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578801329  679 GPRDETVDDFWRMIWEQKATVIVMVTRCEEGNRNKCAEYWPSMEEGTRAFGDVVVKINQHKRCPDYIIQKLNIVNKKEKa 758
Cdd:cd14604   107 GPLANTVIDFWRMIWEYNVAIIVMACREFEMGRKKCERYWPLYGEEPMTFGPFRISCEAEQARTDYFIRTLLLEFQNET- 185

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578801329  759 tgREVTHIQFTSWPDHGVPEDPHLLLKLRRRVNAFSNFFSGPIVVHCSAGVGRTGTYIGIDAMLEGLEA---ENKVDVYG 835
Cdd:cd14604   186 --RRLYQFHYVNWPDHDVPSSFDSILDMISLMRKYQEHEDVPICIHCSAGCGRTGAICAIDYTWNLLKAgkiPEEFNVFN 263

                         250       260
                  ....*....|....*....|....*...
gi 578801329  836 YVVKLRRQRCLMVQVEAQYILIHQALVE 863
Cdd:cd14604   264 LIQEMRTQRHSAVQTKEQYELVHRAIAQ 291
PTPc-N1 cd14608
catalytic domain of tyrosine-protein phosphatase non-receptor type 1; Tyrosine-protein ...
 609-872 4.35e-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: 4.35e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578801329  609 FQSIPRVFSKFPIKEARKPFNQNKNRYVDILPYDYNRVELSEINGDagsnYINASYIDGFKEPRKYIAAQGPRDETVDDF 688
Cdd:cd14608     5 YQDIRHEASDFPCRVAKLPKNKNRNRYRDVSPFDHSRIKLHQEDND----YINASLIKMEEAQRSYILTQGPLPNTCGHF 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578801329  689 WRMIWEQKATVIVMVTRCEEGNRNKCAEYWPSMEEGTRAFGDVVVKIN--QHKRCPDYIIQKLNIVNKKEKATgREVTHI 766
Cdd:cd14608    81 WEMVWEQKSRGVVMLNRVMEKGSLKCAQYWPQKEEKEMIFEDTNLKLTliSEDIKSYYTVRQLELENLTTQET-REILHF 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578801329  767 QFTSWPDHGVPEDP----HLLLKLRRrvNAFSNFFSGPIVVHCSAGVGRTGTYIGIDA---MLEGLEAENKVDVYGYVVK 839
Cdd:cd14608   160 HYTTWPDFGVPESPasflNFLFKVRE--SGSLSPEHGPVVVHCSAGIGRSGTFCLADTcllLMDKRKDPSSVDIKKVLLE 237

                         250       260       270
                  ....*....|....*....|....*....|....*
gi 578801329  840 LRRQRCLMVQVEAQYILIHQALVEYNQF--GETEV 872
Cdd:cd14608   238 MRKFRMGLIQTADQLRFSYLAVIEGAKFimGDSSV 272
PTPc-N3 cd14600
catalytic domain of tyrosine-protein phosphatase non-receptor type 3; Tyrosine-protein ...
 606-862 7.86e-53

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: 186.59  E-value: 7.86e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578801329  606 LAEFQSIPRVFSKFPIKEARKPFNQNKNRYVDILPYDYNRVELSEingdaGSNYINASYID----GFKEPRKYIAAQGPR 681
Cdd:cd14600    17 LIQFEQLYRKKPGLAITCAKLPQNMDKNRYKDVLPYDATRVVLQG-----NEDYINASYVNmeipSANIVNKYIATQGPL 91

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578801329  682 DETVDDFWRMIWEQKATVIVMVTRCEEGNRNKCAEYWPSMEEgTRAFGDVVVKINQHKRCPDYIIQKLNIVNKKekaTGR 761
Cdd:cd14600    92 PHTCAQFWQVVWEQKLSLIVMLTTLTERGRTKCHQYWPDPPD-VMEYGGFRVQCHSEDCTIAYVFREMLLTNTQ---TGE 167

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578801329  762 E--VTHIQFTSWPDHGVPEDPHLLLKLRRRVNAfSNFFSGPIVVHCSAGVGRTGTYIGIDAMLEGLEAENKVDVYGYVVK 839
Cdd:cd14600   168 ErtVTHLQYVAWPDHGVPDDSSDFLEFVNYVRS-KRVENEPVLVHCSAGIGRTGVLVTMETAMCLTERNQPVYPLDIVRK 246

                         250       260
                  ....*....|....*....|...
gi 578801329  840 LRRQRCLMVQVEAQYILIHQALV 862
Cdd:cd14600   247 MRDQRAMMVQTSSQYKFVCEAIL 269
PTP_fungal cd18533
fungal protein tyrosine phosphatases; This subfamily contains Saccharomyces cerevisiae ...
 969-1175 8.19e-53

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: 184.37  E-value: 8.19e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578801329  969 YINASFI-MSYWKPEVMIAAQGPLKETIGDFWQMIFQRKVKVIVMLTELKHGDQEICAQYW--GEGKQTYGDIEVDL--K 1043
Cdd:cd18533     1 YINASYItLPGTSSKRYIATQGPLPATIGDFWKMIWQNNVGVIVMLTPLVENGREKCDQYWpsGEYEGEYGDLTVELvsE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578801329 1044 DTDKSSTYTLRVFELRHSKRKdSRTVYQYQYTNWSVEQLPAEPKELISMIQVVKQKLpqknssegNKHHKSTPLLIHCRD 1123
Cdd:cd18533    81 EENDDGGFIVREFELSKEDGK-VKKVYHIQYKSWPDFGVPDSPEDLLTLIKLKRELN--------DSASLDPPIIVHCSA 151

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 578801329 1124 GSQQTGIFCAL---LNLLE-----SAETEEVVD-IFQVVKALRKARPGMVSTFEQYQFLYD 1175
Cdd:cd18533   152 GVGRTGTFIALdslLDELKrglsdSQDLEDSEDpVYEIVNQLRKQRMSMVQTLRQYIFLYD 212
R-PTPc-R cd14611
catalytic domain of receptor-type tyrosine-protein phosphatase R; Receptor-type ...
 632-859 1.37e-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: 184.35  E-value: 1.37e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578801329  632 KNRYVDILPYDYNRVELSEIN-GDAGSNYINASYIDGFK-EPRKYIAAQGPRDETVDDFWRMIWEQKATVIVMVTRCEEG 709
Cdd:cd14611     2 KNRYKTILPNPHSRVCLKPKNsNDSLSTYINANYIRGYGgKEKAFIATQGPMINTVNDFWQMVWQEDSPVIVMITKLKEK 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578801329  710 NRnKCAEYWPsmeEGTRAFGDVVVKINQHKRCPDYIIQKLNIvnkKEKATGREVTHIQFTSWPDHGVPEDPHLLLKLRRR 789
Cdd:cd14611    82 NE-KCVLYWP---EKRGIYGKVEVLVNSVKECDNYTIRNLTL---KQGSQSRSVKHYWYTSWPDHKTPDSAQPLLQLMLD 154

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 578801329  790 V--NAFSNFFSGPIVVHCSAGVGRTGTYIGIDAMLEGLEAENKVDVYGYVVKLRRQRCLMVQVEAQYILIHQ 859
Cdd:cd14611   155 VeeDRLASPGRGPVVVHCSAGIGRTGCFIATTIGCQQLKEEGVVDVLSIVCQLRVDRGGMVQTSEQYEFVHH 226
PTPc-N5 cd14613
catalytic domain of tyrosine-protein phosphatase non-receptor type 5; Tyrosine-protein ...
 607-864 3.11e-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: 3.11e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578801329  607 AEFQSIPRVFSKfPiKEARKPFNQNKNRYVDILPYDYNRVEL-SEINGDAGSNYINASYIDGF-KEPRKYIAAQGPRDET 684
Cdd:cd14613     5 AEFFEIPMNFVD-P-KEYDIPGLVRKNRYKTILPNPHSRVCLtSPDQDDPLSSYINANYIRGYgGEEKVYIATQGPTVNT 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578801329  685 VDDFWRMIWEQKATVIVMVTRCEEGNRnKCAEYWPsmeEGTRAFGDVVVKINQHKRCPDYiiqKLNIVNKKEKATGREVT 764
Cdd:cd14613    83 VGDFWRMVWQERSPIIVMITNIEEMNE-KCTEYWP---EEQVTYEGIEITVKQVIHADDY---RLRLITLKSGGEERGLK 155

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578801329  765 HIQFTSWPDHGVPEDPHLLLKLRRRVNAF---SNFFSGPIVVHCSAGVGRTGTYIGIDAMLEGLEAENKVDVYGYVVKLR 841
Cdd:cd14613   156 HYWYTSWPDQKTPDNAPPLLQLVQEVEEArqqAEPNCGPVIVHCSAGIGRTGCFIATSICCKQLRNEGVVDILRTTCQLR 235

                         250       260
                  ....*....|....*....|...
gi 578801329  842 RQRCLMVQVEAQYILIHQALVEY 864
Cdd:cd14613   236 LDRGGMIQTCEQYQFVHHVLSLY 258
PHA02746 PHA02746
protein tyrosine phosphatase; Provisional
 626-861 1.44e-51

protein tyrosine phosphatase; Provisional


Pssm-ID: 165113 [Multi-domain]  Cd Length: 323  Bit Score: 184.85  E-value: 1.44e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578801329  626 KPFNQNKNRYVDILPYDYNRVELSE-------------------INGDAGSNYINASYIDGFKEPRKYIAAQGPRDETVD 686
Cdd:PHA02746   48 KKENLKKNRFHDIPCWDHSRVVINAheslkmfdvgdsdgkkievTSEDNAENYIHANFVDGFKEANKFICAQGPKEDTSE 127

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578801329  687 DFWRMIWEQKATVIVMVTRCEEGNRnKCAEYWPSMEEGTRAFGDVVVKINQHKRCPDYIIQKLNIVNKKEKaTGREVTHI 766
Cdd:PHA02746  128 DFFKLISEHESQVIVSLTDIDDDDE-KCFELWTKEEDSELAFGRFVAKILDIIEELSFTKTRLMITDKISD-TSREIHHF 205

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578801329  767 QFTSWPDHGVPEDPHLLLKLRRRVNA----------FSNFFSGPIVVHCSAGVGRTGTYIGIDAMLEGLEAENKVDVYGY 836
Cdd:PHA02746  206 WFPDWPDNGIPTGMAEFLELINKVNEeqaelikqadNDPQTLGPIVVHCSAGIGRAGTFCAIDNALEQLEKEKEVCLGEI 285

                         250       260
                  ....*....|....*....|....*
gi 578801329  837 VVKLRRQRCLMVQVEAQYILIHQAL 861
Cdd:PHA02746  286 VLKIRKQRHSSVFLPEQYAFCYKAL 310
PTPc-N9 cd14543
catalytic domain of tyrosine-protein phosphatase non-receptor type 9; Tyrosine-protein ...
 920-1174 1.64e-51

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: 182.56  E-value: 1.64e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578801329  920 NKSKNRNSNVIPYDYNRVPLKHELEmskesehdsdessdddsdsEEPSKYINASFIMSYWKPEVMIAAQGPLKETIGDFW 999
Cdd:cd14543    29 NQEKNRYGDVLCLDQSRVKLPKRNG-------------------DERTDYINANFMDGYKQKNAYIATQGPLPKTYSDFW 89

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578801329 1000 QMIFQRKVKVIVMLTELKHGDQEICAQYW---GEGKQTYGDIEVDLKDTDKSSTYTLRVFELRHSKRKDSRTVYQYQYTN 1076
Cdd:cd14543    90 RMVWEQKVLVIVMTTRVVERGRVKCGQYWpleEGSSLRYGDLTVTNLSVENKEHYKKTTLEIHNTETDESRQVTHFQFTS 169

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578801329 1077 WSVEQLPAEPKELISMIQVVKQKLPQKNSSEGN---KHHKSTPLLIHCRDGSQQTGIFCALLNLLESAETEEVVDIFQVV 1153
Cdd:cd14543   170 WPDFGVPSSAAALLDFLGEVRQQQALAVKAMGDrwkGHPPGPPIVVHCSAGIGRTGTFCTLDICLSQLEDVGTLNVMQTV 249

                         250       260
                  ....*....|....*....|.
gi 578801329 1154 KALRKARPGMVSTFEQYQFLY 1174
Cdd:cd14543   250 RRMRTQRAFSIQTPDQYYFCY 270
R-PTP-N-N2 cd14546
PTP-like domain of receptor-type tyrosine-protein phosphatase-like N and N2; Receptor-type ...
 659-873 1.82e-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: 1.82e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578801329  659 YINASYIDGfKEPRK--YIAAQGPRDETVDDFWRMIWEQKATVIVMVTRCEEGNRNKCAEYWPsmEEGTRAFGDVVVK-I 735
Cdd:cd14546     1 YINASTIYD-HDPRNpaYIATQGPLPHTIADFWQMIWEQGCVVIVMLTRLQENGVKQCARYWP--EEGSEVYHIYEVHlV 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578801329  736 NQHKRCPDYIIQKLNIVNKKEKATgREVTHIQFTSWPDHGVPEDPHLLLKLRRRVNAFSNFFSGPIVVHCSAGVGRTGTY 815
Cdd:cd14546    78 SEHIWCDDYLVRSFYLKNLQTSET-RTVTQFHFLSWPDEGIPASAKPLLEFRRKVNKSYRGRSCPIVVHCSDGAGRTGTY 156

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 578801329  816 IGIDAMLEGLEAENK-VDVYGYVVKLRRQRCLMVQVEAQYILIHQALVEynqfgetEVN 873
Cdd:cd14546   157 ILIDMVLNRMAKGAKeIDIAATLEHLRDQRPGMVKTKDQFEFVLTAVAE-------EVN 208
R-PTP-LAR-2 cd14554
PTP-like domain of the LAR family receptor-type tyrosine-protein phosphatases, repeat 2; The ...
 920-1174 3.65e-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: 3.65e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578801329  920 NKSKNRNSNVIPYDYNRVPLKhelemskesehdsdessddDSDSEEPSKYINASFIMSYWKPEVMIAAQGPLKETIGDFW 999
Cdd:cd14554     6 NKFKNRLVNILPYESTRVCLQ-------------------PIRGVEGSDYINASFIDGYRQRGAYIATQGPLAETTEDFW 66

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578801329 1000 QMIFQRKVKVIVMLTELKHGDQEICAQYW-GEGKQTYGDIEVDLKDTDKSSTYTLRVFELRHSKRKDSRTVYQYQYTNWS 1078
Cdd:cd14554    67 RMLWEHNSTIIVMLTKLREMGREKCHQYWpAERSARYQYFVVDPMAEYNMPQYILREFKVTDARDGQSRTVRQFQFTDWP 146

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578801329 1079 VEQLPAEPKELISMI-QVVKQKlpQKNSSEGnkhhkstPLLIHCRDGSQQTGIFCALLNLLESAETEEVVDIFQVVKALR 1157
Cdd:cd14554   147 EQGVPKSGEGFIDFIgQVHKTK--EQFGQEG-------PITVHCSAGVGRTGVFITLSIVLERMRYEGVVDVFQTVKLLR 217

                         250
                  ....*....|....*..
gi 578801329 1158 KARPGMVSTFEQYQFLY 1174
Cdd:cd14554   218 TQRPAMVQTEDQYQFCY 234
R-PTP-N2 cd14610
PTP-like domain of receptor-type tyrosine-protein phosphatase N2; Receptor-type ...
 624-863 8.80e-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: 8.80e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578801329  624 ARKPFNQNKNRYVDILPYDYNRVELSEINGDAGSNYINASYIDGfKEPRK--YIAAQGPRDETVDDFWRMIWEQKATVIV 701
Cdd:cd14610    39 AQREENVQKNRSLAVLPYDHSRIILKAENSHSHSDYINASPIMD-HDPRNpaYIATQGPLPATVADFWQMVWESGCVVIV 117

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578801329  702 MVTRCEEGNRNKCAEYWPsmEEGTRAFGDVVVK-INQHKRCPDYIIQKLNIVNKKEKATgREVTHIQFTSWPDHGVPEDP 780
Cdd:cd14610   118 MLTPLAENGVKQCYHYWP--DEGSNLYHIYEVNlVSEHIWCEDFLVRSFYLKNLQTNET-RTVTQFHFLSWNDQGVPAST 194

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578801329  781 HLLLKLRRRVNAFSNFFSGPIVVHCSAGVGRTGTYIGIDAMLEGL-EAENKVDVYGYVVKLRRQRCLMVQVEAQYILIHQ 859
Cdd:cd14610   195 RSLLDFRRKVNKCYRGRSCPIIVHCSDGAGRSGTYILIDMVLNKMaKGAKEIDIAATLEHLRDQRPGMVQTKEQFEFALT 274


                  ....
gi 578801329  860 ALVE 863
Cdd:cd14610   275 AVAE 278
R-PTPc-typeIIb-2 cd14556
PTP domain of type IIb (or R2B) subfamily receptor-type tyrosine-protein phosphatases, repeat ...
 969-1175 3.44e-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: 176.44  E-value: 3.44e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578801329  969 YINASFIMSYWKPEVMIAAQGPLKETIGDFWQMIFQRKVKVIVMLTELKHGDQEiCAQYWGE-GKQTYGDIEVDLKDTDK 1047
Cdd:cd14556     1 YINAALLDSYKQPAAFIVTQHPLPNTVTDFWRLVYDYGCTSIVMLNQLDPKDQS-CPQYWPDeGSGTYGPIQVEFVSTTI 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578801329 1048 SSTYTLRVFELRHSKR--KDSRTVYQYQYTNWSVEQL-PAEPKELISMIQVVKQKlpQKNSSEGnkhhkstPLLIHCRDG 1124
Cdd:cd14556    80 DEDVISRIFRLQNTTRpqEGYRMVQQFQFLGWPRDRDtPPSKRALLKLLSEVEKW--QEQSGEG-------PIVVHCLNG 150

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|.
gi 578801329 1125 SQQTGIFCALLNLLESAETEEVVDIFQVVKALRKARPGMVSTFEQYQFLYD 1175
Cdd:cd14556   151 VGRSGVFCAISSVCERIKVENVVDVFQAVKTLRNHRPNMVETEEQYKFCYD 201
R-PTPc-H cd14619
catalytic domain of receptor-type tyrosine-protein phosphatase H; Receptor-type ...
 924-1177 2.38e-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: 175.08  E-value: 2.38e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578801329  924 NRNSNVIPYDYNRVPLKhelemskesehdsdessddDSDSEEPSKYINASFIMSYWKPEVMIAAQGPLKETIGDFWQMIF 1003
Cdd:cd14619     1 NRFRNVLPYDWSRVPLK-------------------PIHEEPGSDYINANYMPGYWSSQEFIATQGPLPQTVGDFWRMIW 61

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578801329 1004 QRKVKVIVMLTELKHGDQEICAQYWGEGKQ--TYGDIEVDLKDTDKSSTYTLRVFELRHSKRKDSRTVYQYQYTNWSVEQ 1081
Cdd:cd14619    62 EQQSSTIVMLTNCMEAGRVKCEHYWPLDYTpcTYGHLRVTVVSEEVMENWTVREFLLKQVEEQKTLSVRHFHFTAWPDHG 141

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578801329 1082 LPAEPKELISMIQVVKQKLPQKNSsegnkhhkSTPLLIHCRDGSQQTGIFCALLNLLESAETEEVVDIFQVVKALRKARP 1161
Cdd:cd14619   142 VPSSTDTLLAFRRLLRQWLDQTMS--------GGPTVVHCSAGVGRTGTLIALDVLLQQLQSEGLLGPFSFVQKMRENRP 213

                         250
                  ....*....|....*.
gi 578801329 1162 GMVSTFEQYQFLYDVI 1177
Cdd:cd14619   214 LMVQTESQYVFLHQCI 229
R-PTP-S-2 cd14627
PTP-like domain of receptor-type tyrosine-protein phosphatase S, repeat 2; Receptor-type ...
 870-1174 2.43e-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: 177.23  E-value: 2.43e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578801329  870 TEVNLSELHPYLHNMKKRDPPSEPSPLEAEFQRLPSYRSWRTQHI-GNQEENKSKNRNSNVIPYDYNRVPLKhelemske 948
Cdd:cd14627     2 TEVPARNLYSYIQKLAQVEVGEHVTGMELEFKRLANSKAHTSRFIsANLPCNKFKNRLVNIMPYETTRVCLQ-------- 73

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578801329  949 sehdsdessddDSDSEEPSKYINASFIMSYWKPEVMIAAQGPLKETIGDFWQMIFQRKVKVIVMLTELKHGDQEICAQYW 1028
Cdd:cd14627    74 -----------PIRGVEGSDYINASFIDGYRQQKAYIATQGPLAETTEDFWRMLWENNSTIVVMLTKLREMGREKCHQYW 142

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578801329 1029 -GEGKQTYGDIEVDLKDTDKSSTYTLRVFELRHSKRKDSRTVYQYQYTNWSVEQLPAEPKELISMI-QVVKQKlpqknss 1106
Cdd:cd14627   143 pAERSARYQYFVVDPMAEYNMPQYILREFKVTDARDGQSRTVRQFQFTDWPEQGVPKSGEGFIDFIgQVHKTK------- 215

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 578801329 1107 egNKHHKSTPLLIHCRDGSQQTGIFCALLNLLESAETEEVVDIFQVVKALRKARPGMVSTFEQYQFLY 1174
Cdd:cd14627   216 --EQFGQDGPISVHCSAGVGRTGVFITLSIVLERMRYEGVVDIFQTVKMLRTQRPAMVQTEDEYQFCY 281
R-PTP-N cd14609
PTP-like domain of receptor-type tyrosine-protein phosphatase N; Receptor-type ...
 606-863 3.58e-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: 3.58e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578801329  606 LAEFQSIPRVFSKfpikeARKPFNQNKNRYVDILPYDYNRVELSEINGDAGSNYINASYIDGfKEPR--KYIAAQGPRDE 683
Cdd:cd14609    24 LCAYQAEPNTCST-----AQGEANVKKNRNPDFVPYDHARIKLKAESNPSRSDYINASPIIE-HDPRmpAYIATQGPLSH 97

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578801329  684 TVDDFWRMIWEQKATVIVMVTRCEEGNRNKCAEYWPsmEEGTRAFGDVVVK-INQHKRCPDYIIQKLNIVNKKEKATgRE 762
Cdd:cd14609    98 TIADFWQMVWENGCTVIVMLTPLVEDGVKQCDRYWP--DEGSSLYHIYEVNlVSEHIWCEDFLVRSFYLKNVQTQET-RT 174

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578801329  763 VTHIQFTSWPDHGVPEDPHLLLKLRRRVNAFSNFFSGPIVVHCSAGVGRTGTYIGIDAMLEGL-EAENKVDVYGYVVKLR 841
Cdd:cd14609   175 LTQFHFLSWPAEGIPSSTRPLLDFRRKVNKCYRGRSCPIIVHCSDGAGRTGTYILIDMVLNRMaKGVKEIDIAATLEHVR 254

                         250       260
                  ....*....|....*....|..
gi 578801329  842 RQRCLMVQVEAQYILIHQALVE 863
Cdd:cd14609   255 DQRPGMVRTKDQFEFALTAVAE 276
R-PTP-D-2 cd14628
PTP-like domain of receptor-type tyrosine-protein phosphatase D, repeat 2; Receptor-type ...
 870-1174 7.85e-49

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: 175.69  E-value: 7.85e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578801329  870 TEVNLSELHPYLHNMKKRDPPSEPSPLEAEFQRLPSYRSWRTQHI-GNQEENKSKNRNSNVIPYDYNRVPLKhelemske 948
Cdd:cd14628     1 TEVPARNLYAYIQKLTQIETGENVTGMELEFKRLASSKAHTSRFIsANLPCNKFKNRLVNIMPYESTRVCLQ-------- 72

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578801329  949 sehdsdessddDSDSEEPSKYINASFIMSYWKPEVMIAAQGPLKETIGDFWQMIFQRKVKVIVMLTELKHGDQEICAQYW 1028
Cdd:cd14628    73 -----------PIRGVEGSDYINASFIDGYRQQKAYIATQGPLAETTEDFWRMLWEHNSTIVVMLTKLREMGREKCHQYW 141

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578801329 1029 -GEGKQTYGDIEVDLKDTDKSSTYTLRVFELRHSKRKDSRTVYQYQYTNWSVEQLPAEPKELISMI-QVVKQKlpqknss 1106
Cdd:cd14628   142 pAERSARYQYFVVDPMAEYNMPQYILREFKVTDARDGQSRTVRQFQFTDWPEQGVPKSGEGFIDFIgQVHKTK------- 214

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 578801329 1107 egNKHHKSTPLLIHCRDGSQQTGIFCALLNLLESAETEEVVDIFQVVKALRKARPGMVSTFEQYQFLY 1174
Cdd:cd14628   215 --EQFGQDGPISVHCSAGVGRTGVFITLSIVLERMRYEGVVDIFQTVKMLRTQRPAMVQTEDQYQFCY 280
R-PTPc-E-2 cd14622
catalytic domain of receptor-type tyrosine-protein phosphatase E, repeat 2; Receptor-type ...
 658-864 8.34e-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: 8.34e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578801329  658 NYINASYIDGFKEPRKYIAAQGPRDETVDDFWRMIWEQKATVIVMVTRCEEGNRNKCAEYWPSmeEGTRAFGDVVVKINQ 737
Cdd:cd14622     1 DYINASFIDGYRQKDYFIATQGPLAHTVEDFWRMVWEWKCHTIVMLTELQEREQEKCVQYWPS--EGSVTHGEITIEIKN 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578801329  738 HKRCPDYIIQKLNIVNKKEKATgREVTHIQFTSWPDHGVPEDPH----LLLKLRRRVNAFSNffsGPIVVHCSAGVGRTG 813
Cdd:cd14622    79 DTLLETISIRDFLVTYNQEKQT-RLVRQFHFHGWPEIGIPAEGKgmidLIAAVQKQQQQTGN---HPIVVHCSAGAGRTG 154

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|.
gi 578801329  814 TYIGIDAMLEGLEAENKVDVYGYVVKLRRQRCLMVQVEAQYILIHQALVEY 864
Cdd:cd14622   155 TFIALSNILERVKAEGLLDVFQTVKSLRLQRPHMVQTLEQYEFCYRVVQDF 205
PTPc-N20 cd14596
catalytic domain of tyrosine-protein phosphatase non-receptor type 20; Tyrosine-protein ...
 659-863 9.45e-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: 172.24  E-value: 9.45e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578801329  659 YINASYID---GFKEpRKYIAAQGPRDETVDDFWRMIWEQKATVIVMVTRCEEGNRNKCAEYWPSMEEGTRAFGDVVVKI 735
Cdd:cd14596     1 YINASYITmpvGEEE-LFYIATQGPLPSTIDDFWQMVWENRSDVIAMMTREVERGKVKCHRYWPETLQEPMELENYQLRL 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578801329  736 NQHKRCPDYIIQKLNIVNkKEKATGREVTHIQFTSWPDHGVPEDPHLLLKLRRRVNAFSNffSGPIVVHCSAGVGRTGTY 815
Cdd:cd14596    80 ENYQALQYFIIRIIKLVE-KETGENRLIKHLQFTTWPDHGTPQSSDQLVKFICYMRKVHN--TGPIVVHCSAGIGRAGVL 156

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*...
gi 578801329  816 IGIDAMLEGLEAENKVDVYGYVVKLRRQRCLMVQVEAQYILIHQALVE 863
Cdd:cd14596   157 ICVDVLLSLIEKDLSFNIKDIVREMRQQRYGMIQTKDQYLFCYKVVLE 204
R-PTPc-V cd14618
catalytic domain of receptor-type tyrosine-protein phosphatase V; Receptor-type ...
 924-1177 4.46e-48

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: 171.28  E-value: 4.46e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578801329  924 NRNSNVIPYDYNRVPLKhelEMSKESEhdsdessdddsdseepSKYINASFIMSYWKPEVMIAAQGPLKETIGDFWQMIF 1003
Cdd:cd14618     1 NRYPHVLPYDHSRVRLS---QLGGEPH----------------SDYINANFIPGYTSPQEFIATQGPLKKTIEDFWRLVW 61

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578801329 1004 QRKVKVIVMLTELKHGDQEICAQYWGEGKQ--TYGDIEVDLKDTDKSSTYTLRVFELRHSKRKDSRTVYQYQYTNWSVEQ 1081
Cdd:cd14618    62 EQQVCNIIMLTVGMENGRVLCDHYWPSESTpvSYGHITVHLLAQSSEDEWTRREFKLWHEDLRKERRVKHLHYTAWPDHG 141

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578801329 1082 LPAEPKELISMIQVVKQKLpqkNSSEGnkhhkSTPLLIHCRDGSQQTGIFCALLNLLESAETEEVVDIFQVVKALRKARP 1161
Cdd:cd14618   142 IPESTSSLMAFRELVREHV---QATKG-----KGPTLVHCSAGVGRSGTFIALDRLLRQLKEEKVVDVFNTVYILRMHRY 213

                         250
                  ....*....|....*.
gi 578801329 1162 GMVSTFEQYQFLYDVI 1177
Cdd:cd14618   214 LMIQTLSQYIFLHSCI 229
PTPc-N2 cd14607
catalytic domain of tyrosine-protein phosphatase non-receptor type 2; Tyrosine-protein ...
 617-853 4.49e-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: 172.46  E-value: 4.49e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578801329  617 SKFPIKEARKPFNQNKNRYVDILPYDYNRVELSEINGDagsnYINASYIDGFKEPRKYIAAQGPRDETVDDFWRMIWEQK 696
Cdd:cd14607    12 HDYPHRVAKYPENRNRNRYRDVSPYDHSRVKLQNTEND----YINASLVVIEEAQRSYILTQGPLPNTCCHFWLMVWQQK 87

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578801329  697 ATVIVMVTRCEEGNRNKCAEYWPSMEEGTRAFGDV--VVKINQHKRCPDYIIQKLNIVNKKEKATgREVTHIQFTSWPDH 774
Cdd:cd14607    88 TKAVVMLNRIVEKDSVKCAQYWPTDEEEVLSFKETgfSVKLLSEDVKSYYTVHLLQLENINSGET-RTISHFHYTTWPDF 166

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578801329  775 GVPEDP----HLLLKLRRrvNAFSNFFSGPIVVHCSAGVGRTGTYIGIDAMLEGLEAEN--KVDVYGYVVKLRRQRCLMV 848
Cdd:cd14607   167 GVPESPasflNFLFKVRE--SGSLSPEHGPAVVHCSAGIGRSGTFSLVDTCLVLMEKKDpdSVDIKQVLLDMRKYRMGLI 244


                  ....*
gi 578801329  849 QVEAQ 853
Cdd:cd14607   245 QTPDQ 249
PTPc_plant_PTP1 cd17658
protein tyrosine phosphatase 1 from Arabidopsis thaliana and similar plant PTPs; Arabidopsis ...
 659-858 1.91e-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: 1.91e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578801329  659 YINASYI--DGFKEPRKYIAAQGPRDETVDDFWRMIWEQKATVIVMVTRCEEGNR-NKCAEYWPSMEEGTRAFGDVVVKI 735
Cdd:cd17658     1 YINASLVetPASESLPKFIATQGPLPHTFEDFWEMVIQQRCPVIIMLTRLVDNYStAKCADYFPAEENESREFGRISVTN 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578801329  736 NQHKrCPDYIIQKLNI-VNKKE-KATGREVTHIQFTSWPDHGVPEDPHLLLKLRRRVNAFSNFFsGPIVVHCSAGVGRTG 813
Cdd:cd17658    81 KKLK-HSQHSITLRVLeVQYIEsEEPPLSVLHIQYPEWPDHGVPKDTRSVRELLKRLYGIPPSA-GPIVVHCSAGIGRTG 158

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|
gi 578801329  814 TYIGID----AMLEG-LEAenkVDVYGYVVKLRRQRCLMVQVEAQYILIH 858
Cdd:cd17658   159 AYCTIHntirRILEGdMSA---VDLSKTVRKFRSQRIGMVQTQDQYIFCY 205
PHA02747 PHA02747
protein tyrosine phosphatase; Provisional
 621-858 2.15e-47

protein tyrosine phosphatase; Provisional


Pssm-ID: 165114 [Multi-domain]  Cd Length: 312  Bit Score: 172.49  E-value: 2.15e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578801329  621 IKEARKPFNQNKNRYVDILPYDYNRVELsEINGDAGSNYINASYIDGFKEPRKYIAAQGPRDETVDDFWRMIWEQKATVI 700
Cdd:PHA02747   43 IANFEKPENQPKNRYWDIPCWDHNRVIL-DSGGGSTSDYIHANWIDGFEDDKKFIATQGPFAETCADFWKAVWQEHCSII 121

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578801329  701 VMVTRCEEGN-RNKCAEYWPSMEEGTRAFGDVVVKINQHKRCPDYIIQKLNIVNKKEKaTGREVTHIQFTSWPDHGVPED 779
Cdd:PHA02747  122 VMLTPTKGTNgEEKCYQYWCLNEDGNIDMEDFRIETLKTSVRAKYILTLIEITDKILK-DSRKISHFQCSEWFEDETPSD 200

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578801329  780 PHLLLKL-----RRRVNAFSNFFS-----GPIVVHCSAGVGRTGTYIGIDAMLEGLEAENKVDVYGYVVKLRRQRCLMVQ 849
Cdd:PHA02747  201 HPDFIKFikiidINRKKSGKLFNPkdallCPIVVHCSDGVGKTGIFCAVDICLNQLVKRKAICLAKTAEKIREQRHAGIM 280


                  ....*....
gi 578801329  850 VEAQYILIH 858
Cdd:PHA02747  281 NFDDYLFIQ 289
R-PTPc-F-1 cd14626
catalytic domain of receptor-type tyrosine-protein phosphatase F, repeat 1; Receptor-type ...
 916-1177 1.36e-46

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: 168.68  E-value: 1.36e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578801329  916 NQEENKSKNRNSNVIPYDYNRVPLkhelemskesehdsdessdDDSDSEEPSKYINASFIMSYWKPEVMIAAQGPLKETI 995
Cdd:cd14626    37 NLEVNKPKNRYANVIAYDHSRVIL-------------------TSVDGVPGSDYINANYIDGYRKQNAYIATQGPLPETL 97

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578801329  996 GDFWQMIFQRKVKVIVMLTELKHGDQEICAQYW-GEGKQTYGDIEVDLKDTDKSSTYTLRVFELRHSKRKDSRTVYQYQY 1074
Cdd:cd14626    98 SDFWRMVWEQRTATIVMMTRLEEKSRVKCDQYWpIRGTETYGMIQVTLLDTVELATYSVRTFALYKNGSSEKREVRQFQF 177

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578801329 1075 TNWSVEQLPAEPKELISMIQVVKQKLPQknssegnkhhKSTPLLIHCRDGSQQTGIFCALLNLLESAETEEVVDIFQVVK 1154
Cdd:cd14626   178 MAWPDHGVPEYPTPILAFLRRVKACNPP----------DAGPMVVHCSAGVGRTGCFIVIDAMLERMKHEKTVDIYGHVT 247

                         250       260
                  ....*....|....*....|...
gi 578801329 1155 ALRKARPGMVSTFEQYQFLYDVI 1177
Cdd:cd14626   248 CMRSQRNYMVQTEDQYIFIHEAL 270
R-PTPc-T-1 cd14630
catalytic domain of receptor-type tyrosine-protein phosphatase T, repeat 1; Receptor-type ...
 918-1177 1.97e-46

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: 166.74  E-value: 1.97e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578801329  918 EENKSKNRNSNVIPYDYNRVPLKhELEMSKEsehdsdessdddsdseepSKYINASFIMSYWKPEVMIAAQGPLKETIGD 997
Cdd:cd14630     1 DENRNKNRYGNIISYDHSRVRLQ-LLDGDPH------------------SDYINANYIDGYHRPRHYIATQGPMQETVKD 61

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578801329  998 FWQMIFQRKVKVIVMLTELKHGDQEICAQYWGEGKQTYGDIEVDLKDTDKSSTYTLRVFELRHSKRKDSRTVYQYQYTNW 1077
Cdd:cd14630    62 FWRMIWQENSASVVMVTNLVEVGRVKCVRYWPDDTEVYGDIKVTLIETEPLAEYVIRTFTVQKKGYHEIREIRQFHFTSW 141

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578801329 1078 SVEQLPAEPKELISMIQVVKQKLPQknssegnkhhKSTPLLIHCRDGSQQTGIFCALLNLLESAETEEVVDIFQVVKALR 1157
Cdd:cd14630   142 PDHGVPCYATGLLGFVRQVKFLNPP----------DAGPIVVHCSAGAGRTGCFIAIDIMLDMAENEGVVDIFNCVRELR 211

                         250       260
                  ....*....|....*....|
gi 578801329 1158 KARPGMVSTFEQYQFLYDVI 1177
Cdd:cd14630   212 AQRVNMVQTEEQYVFVHDAI 231
R-PTP-F-2 cd14629
PTP-like domain of receptor-type tyrosine-protein phosphatase F, repeat 2; Receptor-type ...
 870-1174 3.15e-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: 168.37  E-value: 3.15e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578801329  870 TEVNLSELHPYLHNMKKRDPPSEPSPLEAEFQRLPSYRSWRTQHI-GNQEENKSKNRNSNVIPYDYNRVPLKhelemske 948
Cdd:cd14629     2 TEVPARNLYAHIQKLTQVPPGESVTAMELEFKLLANSKAHTSRFIsANLPCNKFKNRLVNIMPYELTRVCLQ-------- 73

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578801329  949 sehdsdessddDSDSEEPSKYINASFIMSYWKPEVMIAAQGPLKETIGDFWQMIFQRKVKVIVMLTELKHGDQEICAQYW 1028
Cdd:cd14629    74 -----------PIRGVEGSDYINASFIDGYRQQKAYIATQGPLAETTEDFWRMLWEHNSTIVVMLTKLREMGREKCHQYW 142

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578801329 1029 -GEGKQTYGDIEVDLKDTDKSSTYTLRVFELRHSKRKDSRTVYQYQYTNWSVEQLPAEPKELISMI-QVVKQKlpqknss 1106
Cdd:cd14629   143 pAERSARYQYFVVDPMAEYNMPQYILREFKVTDARDGQSRTIRQFQFTDWPEQGVPKTGEGFIDFIgQVHKTK------- 215

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 578801329 1107 egNKHHKSTPLLIHCRDGSQQTGIFCALLNLLESAETEEVVDIFQVVKALRKARPGMVSTFEQYQFLY 1174
Cdd:cd14629   216 --EQFGQDGPITVHCSAGVGRTGVFITLSIVLERMRYEGVVDMFQTVKTLRTQRPAMVQTEDQYQLCY 281
PTPc-KIM cd14547
catalytic domain of the kinase interaction motif (KIM) family of protein-tyrosine phosphatases; ...
 967-1174 4.78e-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: 165.26  E-value: 4.78e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578801329  967 SKYINASFIMSY-WKPEVMIAAQGPLKETIGDFWQMIFQRKVKVIVMLTELKHGDQEiCAQYWGEGK-QTYGDIEVDLKD 1044
Cdd:cd14547    25 SSYINANYIRGYdGEEKAYIATQGPLPNTVADFWRMVWQEKTPIIVMITNLTEAKEK-CAQYWPEEEnETYGDFEVTVQS 103

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578801329 1045 TDKSSTYTLRVFELRHskRKDSRTVYQYQYTNWSVEQLPAEPKELISMIQVVKQkLPQKNSSEGnkhhkstPLLIHCRDG 1124
Cdd:cd14547   104 VKETDGYTVRKLTLKY--GGEKRYLKHYWYTSWPDHKTPEAAQPLLSLVQEVEE-ARQTEPHRG-------PIVVHCSAG 173

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|
gi 578801329 1125 SQQTGIFCALLNLLESAETEEVVDIFQVVKALRKARPGMVSTFEQYQFLY 1174
Cdd:cd14547   174 IGRTGCFIATSIGCQQLREEGVVDVLGIVCQLRLDRGGMVQTAEQYEFVH 223
R-PTPc-J cd14615
catalytic domain of receptor-type tyrosine-protein phosphatase J; Receptor-type ...
 924-1173 1.13e-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: 164.60  E-value: 1.13e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578801329  924 NRNSNVIPYDYNRVPLKHElemskesehdsdessdddsdSEEPSKYINASFIMSYWKPEVMIAAQGPLKETIGDFWQMIF 1003
Cdd:cd14615     1 NRYNNVLPYDISRVKLSVQ--------------------SHSTDDYINANYMPGYNSKKEFIAAQGPLPNTVKDFWRMVW 60

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578801329 1004 QRKVKVIVMLTELKHGDQEICAQYW-GEGKQTYGDIEVDLKDTDKSSTYTLRVFELRHSKRKDSRTVYQYQYTNWSVEQL 1082
Cdd:cd14615    61 EKNVYAIVMLTKCVEQGRTKCEEYWpSKQKKDYGDITVTMTSEIVLPEWTIRDFTVKNAQTNESRTVRHFHFTSWPDHGV 140

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578801329 1083 PAEPKELISMIQVVKQKLPQknssegnkHHKSTPLLIHCRDGSQQTGIFCALLNLLESAETEEVVDIFQVVKALRKARPG 1162
Cdd:cd14615   141 PETTDLLINFRHLVREYMKQ--------NPPNSPILVHCSAGVGRTGTFIAIDRLIYQIENENVVDVYGIVYDLRMHRPL 212

                         250
                  ....*....|.
gi 578801329 1163 MVSTFEQYQFL 1173
Cdd:cd14615   213 MVQTEDQYVFL 223
R-PTPc-typeIIb-1 cd14555
catalytic domain of type IIb (or R2B) subfamily receptor-type tyrosine-protein phosphatases, ...
 969-1177 1.30e-44

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: 160.47  E-value: 1.30e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578801329  969 YINASFIMSYWKPEVMIAAQGPLKETIGDFWQMIFQRKVKVIVMLTELKHGDQEICAQYWGEGKQTYGDIEVDLKDTDKS 1048
Cdd:cd14555     1 YINANYIDGYHRPNHYIATQGPMQETVYDFWRMVWQENSASIVMVTNLVEVGRVKCSRYWPDDTEVYGDIKVTLVETEPL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578801329 1049 STYTLRVFELRHSKRKDSRTVYQYQYTNWSVEQLPAEPKELISMIQVVKQKLPQknssegnkhhKSTPLLIHCRDGSQQT 1128
Cdd:cd14555    81 AEYVVRTFALERRGYHEIREVRQFHFTGWPDHGVPYHATGLLGFIRRVKASNPP----------SAGPIVVHCSAGAGRT 150

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*....
gi 578801329 1129 GIFCALLNLLESAETEEVVDIFQVVKALRKARPGMVSTFEQYQFLYDVI 1177
Cdd:cd14555   151 GCYIVIDIMLDMAEREGVVDIYNCVKELRSRRVNMVQTEEQYIFIHDAI 199
R-PTPc-S-1 cd14625
catalytic domain of receptor-type tyrosine-protein phosphatase S, repeat 1; Receptor-type ...
 872-1177 1.31e-44

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: 163.34  E-value: 1.31e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578801329  872 VNLSELHPYLHNMKKRDPPSepspLEAEFQRLPSYRSWRTQHiGNQEENKSKNRNSNVIPYDYNRVPLKhelemskeseh 951
Cdd:cd14625     4 IPISELAEHTERLKANDNLK----LSQEYESIDPGQQFTWEH-SNLEVNKPKNRYANVIAYDHSRVILQ----------- 67

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578801329  952 dsdessddDSDSEEPSKYINASFIMSYWKPEVMIAAQGPLKETIGDFWQMIFQRKVKVIVMLTELKHGDQEICAQYW-GE 1030
Cdd:cd14625    68 --------PIEGIMGSDYINANYIDGYRKQNAYIATQGPLPETFGDFWRMVWEQRSATVVMMTKLEEKSRIKCDQYWpSR 139

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578801329 1031 GKQTYGDIEVDLKDTDKSSTYTLRVFELRHSKRKDSRTVYQYQYTNWSVEQLPAEPKELISMIQVVKQKLPQknssegnk 1110
Cdd:cd14625   140 GTETYGMIQVTLLDTIELATFCVRTFSLHKNGSSEKREVRQFQFTAWPDHGVPEYPTPFLAFLRRVKTCNPP-------- 211

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 578801329 1111 hhKSTPLLIHCRDGSQQTGIFCALLNLLESAETEEVVDIFQVVKALRKARPGMVSTFEQYQFLYDVI 1177
Cdd:cd14625   212 --DAGPIVVHCSAGVGRTGCFIVIDAMLERIKHEKTVDIYGHVTLMRSQRNYMVQTEDQYSFIHDAL 276
PTP-N23 cd14539
PTP-like domain of tyrosine-protein phosphatase non-receptor type 23; Tyrosine-protein ...
 659-859 9.89e-44

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: 157.93  E-value: 9.89e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578801329  659 YINASYIDGFKE--PRkYIAAQGPRDETVDDFWRMIWEQKATVIVMVTRCEEGNRNKCAEYWPSMEEGTRAFGDVVVKIN 736
Cdd:cd14539     1 YINASLIEDLTPycPR-FIATQAPLPGTAADFWLMVYEQQVSVIVMLVSEQENEKQKVHRYWPTERGQALVYGAITVSLQ 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578801329  737 QHKRCPDYIIQKLNIVNKKEKATgREVTHIQFTSWPDHGVPEDPHLLLKLRRRVNAFSNFFSG---PIVVHCSAGVGRTG 813
Cdd:cd14539    80 SVRTTPTHVERIISIQHKDTRLS-RSVVHLQFTTWPELGLPDSPNPLLRFIEEVHSHYLQQRSlqtPIVVHCSSGVGRTG 158

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*...
gi 578801329  814 TY-IGIDAMLEgLEAENKV-DVYGYVVKLRRQRCLMVQVEAQYILIHQ 859
Cdd:cd14539   159 AFcLLYAAVQE-IEAGNGIpDLPQLVRKMRQQRKYMLQEKEHLKFCYE 205
PTPc-N4 cd14601
catalytic domain of tyrosine-protein phosphatase non-receptor type 4; Tyrosine-protein ...
 658-863 1.63e-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: 157.41  E-value: 1.63e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578801329  658 NYINASYID----GFKEPRKYIAAQGPRDETVDDFWRMIWEQKATVIVMVTRCEEGNRNKCAEYWPSMeEGTRAFGDVVV 733
Cdd:cd14601     1 DYINANYINmeipSSSIINRYIACQGPLPNTCSDFWQMTWEQGSSMVVMLTTQVERGRVKCHQYWPEP-SGSSSYGGFQV 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578801329  734 KINQHKRCPDYIIQKLNIVNkKEKATGREVTHIQFTSWPDHGVPEDPHLLLKLRRRVNAFSNFFSGPIVVHCSAGVGRTG 813
Cdd:cd14601    80 TCHSEEGNPAYVFREMTLTN-LEKNESRPLTQIQYIAWPDHGVPDDSSDFLDFVCLVRNKRAGKDEPVVVHCSAGIGRTG 158

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|
gi 578801329  814 TYIGIDAMLEGLEAENKVDVYGYVVKLRRQRCLMVQVEAQYILIHQALVE 863
Cdd:cd14601   159 VLITMETAMCLIECNQPVYPLDIVRTMRDQRAMMIQTPSQYRFVCEAILK 208
PTPc-N12 cd14604
catalytic domain of tyrosine-protein phosphatase non-receptor type 12; Tyrosine-protein ...
 881-1184 2.36e-43

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: 160.10  E-value: 2.36e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578801329  881 LHNMKKRDPPSEPSpLEAEFQRLPSYRS-WRTQHI-----GNQEENKSKNRNSNVIPYDYNRVPLKheLEMSKESehdsd 954
Cdd:cd14604    13 VQAMKSTDHNGEDN-FASDFMRLRRLSTkYRTEKIyptatGEKEENVKKNRYKDILPFDHSRVKLT--LKTSSQD----- 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578801329  955 essdddsdseepSKYINASFIMSYWKPEVMIAAQGPLKETIGDFWQMIFQRKVKVIVMLT-ELKHGDQEiCAQYW---GE 1030
Cdd:cd14604    85 ------------SDYINANFIKGVYGPKAYIATQGPLANTVIDFWRMIWEYNVAIIVMACrEFEMGRKK-CERYWplyGE 151

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578801329 1031 GKQTYGDIEVDLKDTDKSSTYTLRVFELRHskRKDSRTVYQYQYTNWSVEQLPAEPKELISMIQVVKQklpqknssegNK 1110
Cdd:cd14604   152 EPMTFGPFRISCEAEQARTDYFIRTLLLEF--QNETRRLYQFHYVNWPDHDVPSSFDSILDMISLMRK----------YQ 219

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 578801329 1111 HHKSTPLLIHCRDGSQQTGIFCAL---LNLLESAETEEVVDIFQVVKALRKARPGMVSTFEQYQFLYDVIASTYPAQ 1184
Cdd:cd14604   220 EHEDVPICIHCSAGCGRTGAICAIdytWNLLKAGKIPEEFNVFNLIQEMRTQRHSAVQTKEQYELVHRAIAQLFEKQ 296
PTPc-N21 cd14598
catalytic domain of tyrosine-protein phosphatase non-receptor type 21; Tyrosine-protein ...
 659-864 2.60e-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: 2.60e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578801329  659 YINASYID---GFKEpRKYIAAQGPRDETVDDFWRMIWEQKATVIVMVTRCEEGNRNKCAEYWPSM--EEGTRAFGDVVV 733
Cdd:cd14598     1 YINASHIKvtvGGKE-WDYIATQGPLQNTCQDFWQMVWEQGVAIIAMVTAEEEGGREKSFRYWPRLgsRHNTVTYGRFKI 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578801329  734 KINQHKRCPDYIIQKLNIvnkKEKATGREVT--HIQFTSWPDHGVPEDPHLLL-------KLRRRVNAFSNFFSG--PIV 802
Cdd:cd14598    80 TTRFRTDSGCYATTGLKI---KHLLTGQERTvwHLQYTDWPEHGCPEDLKGFLsyleeiqSVRRHTNSTIDPKSPnpPVL 156

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 578801329  803 VHCSAGVGRTGTYIGIDAMLEGLEAENKVDVYGYVVKLRRQRCLMVQVEAQYILIHQALVEY 864
Cdd:cd14598   157 VHCSAGVGRTGVVILSEIMIACLEHNEMLDIPRVLDMLRQQRMMMVQTLSQYTFVYKVLIQF 218
PHA02738 PHA02738
hypothetical protein; Provisional
 629-872 3.44e-43

hypothetical protein; Provisional


Pssm-ID: 222923 [Multi-domain]  Cd Length: 320  Bit Score: 160.48  E-value: 3.44e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578801329  629 NQNKNRYVDILPYDYNRVEL-SEINGdagSNYINASYIDGFKEPRKYIAAQGPRDETVDDFWRMIWEQKATVIVMVTRCE 707
Cdd:PHA02738   49 NRKLNRYLDAVCFDHSRVILpAERNR---GDYINANYVDGFEYKKKFICGQAPTRQTCYDFYRMLWMEHVQIIVMLCKKK 125

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578801329  708 EGNRNKCAEYWPSMEEGTRAFGDVVVKINQHKRCPDYIIQKLNIVNKKEkATgREVTHIQFTSWPDHGVPEDPHLLLKLR 787
Cdd:PHA02738  126 ENGREKCFPYWSDVEQGSIRFGKFKITTTQVETHPHYVKSTLLLTDGTS-AT-QTVTHFNFTAWPDHDVPKNTSEFLNFV 203

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578801329  788 RRV---------NAFSN----FFSGPIVVHCSAGVGRTGTYIGIDAMLEGLEAENKVDVYGYVVKLRRQRCLMVQVEAQY 854
Cdd:PHA02738  204 LEVrqcqkelaqESLQIghnrLQPPPIVVHCNAGLGRTPCYCVVDISISRFDACATVSIPSIVSSIRNQRYYSLFIPFQY 283

                         250
                  ....*....|....*...
gi 578801329  855 ILIHQALVEYNQFGETEV 872
Cdd:PHA02738  284 FFCYRAVKRYVNLTVNKV 301
R-PTPc-G-1 cd17667
catalytic domain of receptor-type tyrosine-protein phosphatase G, repeat 1; Receptor-type ...
 899-1177 3.85e-43

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: 158.66  E-value: 3.85e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578801329  899 EFQRLPSYRSWRTQHiGNQEENKSKNRNSNVIPYDYNRVPLKhelemskesehdsdessDDDSDSEEPSKYINASFIMSY 978
Cdd:cd17667     7 EVQRCTADMNITAEH-SNHPDNKHKNRYINILAYDHSRVKLR-----------------PLPGKDSKHSDYINANYVDGY 68

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578801329  979 WKPEVMIAAQGPLKETIGDFWQMIFQRKVKVIVMLTELKHGDQEICAQYW-GEGKQTYGDIEVDLKDTDKSSTYTLRVFE 1057
Cdd:cd17667    69 NKAKAYIATQGPLKSTFEDFWRMIWEQNTGIIVMITNLVEKGRRKCDQYWpTENSEEYGNIIVTLKSTKIHACYTVRRFS 148

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578801329 1058 LRHSK-----------RKDSRTVYQYQYTNWSVEQLPAEPKELISMIqvvkqklpqKNSSEGNKHHKStPLLIHCRDGSQ 1126
Cdd:cd17667   149 IRNTKvkkgqkgnpkgRQNERTVIQYHYTQWPDMGVPEYALPVLTFV---------RRSSAARTPEMG-PVLVHCSAGVG 218

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|.
gi 578801329 1127 QTGIFCALLNLLESAETEEVVDIFQVVKALRKARPGMVSTFEQYQFLYDVI 1177
Cdd:cd17667   219 RTGTYIVIDSMLQQIKDKSTVNVLGFLKHIRTQRNYLVQTEEQYIFIHDAL 269
PHA02742 PHA02742
protein tyrosine phosphatase; Provisional
 619-864 5.50e-43

protein tyrosine phosphatase; Provisional


Pssm-ID: 165109 [Multi-domain]  Cd Length: 303  Bit Score: 159.40  E-value: 5.50e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578801329  619 FPIKEARKPFNQNKNRYVDILPYDYNRVELSEINGdaGSNYINASYIDGFKEPRKYIAAQGPRDETVDDFWRMIWEQKAT 698
Cdd:PHA02742   42 FSCNESLELKNMKKCRYPDAPCFDRNRVILKIEDG--GDDFINASYVDGHNAKGRFICTQAPLEETALDFWQAIFQDQVR 119

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578801329  699 VIVMVTRCEEGNRNKCAEYWPSMEEGTRAFGDVVVKINQHKRCPDYIIQKLNIVNKKeKATGREVTHIQFTSWPDHGVPE 778
Cdd:PHA02742  120 VIVMITKIMEDGKEACYPYWMPHERGKATHGEFKIKTKKIKSFRNYAVTNLCLTDTN-TGASLDIKHFAYEDWPHGGLPR 198

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578801329  779 DP-----------HLLLKLRRRVNAFSNFFSGPIVVHCSAGVGRTGTYIGIDAMLEGLEAENKVDVYGYVVKLRRQRCLM 847
Cdd:PHA02742  199 DPnkfldfvlavrEADLKADVDIKGENIVKEPPILVHCSAGLDRAGAFCAIDICISKYNERAIIPLLSIVRDLRKQRHNC 278

                         250
                  ....*....|....*..
gi 578801329  848 VQVEAQYILIHQALVEY 864
Cdd:PHA02742  279 LSLPQQYIFCYFIVLIF 295
R-PTPc-M-1 cd14633
catalytic domain of receptor-type tyrosine-protein phosphatase M, repeat 1; Receptor-type ...
 917-1177 1.22e-42

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: 157.13  E-value: 1.22e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578801329  917 QEENKSKNRNSNVIPYDYNRVPLKhELEMSKEsehdsdessdddsdseepSKYINASFIMSYWKPEVMIAAQGPLKETIG 996
Cdd:cd14633    37 KDENRMKNRYGNIIAYDHSRVRLQ-PIEGETS------------------SDYINGNYIDGYHRPNHYIATQGPMQETIY 97

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578801329  997 DFWQMIFQRKVKVIVMLTELKHGDQEICAQYWGEGKQTYGDIEVDLKDTDKSSTYTLRVFELRHSKRKDSRTVYQYQYTN 1076
Cdd:cd14633    98 DFWRMVWHENTASIIMVTNLVEVGRVKCCKYWPDDTEIYKDIKVTLIETELLAEYVIRTFAVEKRGVHEIREIRQFHFTG 177

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578801329 1077 WSVEQLPAEPKELISMIQVVKQKLPQknssegnkhhKSTPLLIHCRDGSQQTGIFCALLNLLESAETEEVVDIFQVVKAL 1156
Cdd:cd14633   178 WPDHGVPYHATGLLGFVRQVKSKSPP----------NAGPLVVHCSAGAGRTGCFIVIDIMLDMAEREGVVDIYNCVREL 247

                         250       260
                  ....*....|....*....|.
gi 578801329 1157 RKARPGMVSTFEQYQFLYDVI 1177
Cdd:cd14633   248 RSRRVNMVQTEEQYVFIHDAI 268
R-PTP-N2 cd14610
PTP-like domain of receptor-type tyrosine-protein phosphatase N2; Receptor-type ...
 874-1178 4.09e-42

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


Pssm-ID: 350458 [Multi-domain]  Cd Length: 283  Bit Score: 155.98  E-value: 4.09e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578801329  874 LSELHPYLHNmKKRdppsepspLEAEFQRLPSYRSW-RTQHIGNQEENKSKNRNSNVIPYDYNRVPLKHELEMSKesehd 952
Cdd:cd14610     6 LSYMEDHLKN-KNR--------LEKEWEALCAYQAEpNATNVAQREENVQKNRSLAVLPYDHSRIILKAENSHSH----- 71

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578801329  953 sdessdddsdseepSKYINASFIMSYwKPE--VMIAAQGPLKETIGDFWQMIFQRKVKVIVMLTELKHGDQEICAQYW-G 1029
Cdd:cd14610    72 --------------SDYINASPIMDH-DPRnpAYIATQGPLPATVADFWQMVWESGCVVIVMLTPLAENGVKQCYHYWpD 136

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578801329 1030 EGKQTYGDIEVDL-KDTDKSSTYTLRVFELRHSKRKDSRTVYQYQYTNWSVEQLPAEPKELISMIQVVkqklpqknsseg 1108
Cdd:cd14610   137 EGSNLYHIYEVNLvSEHIWCEDFLVRSFYLKNLQTNETRTVTQFHFLSWNDQGVPASTRSLLDFRRKV------------ 204

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 578801329 1109 NKHH--KSTPLLIHCRDGSQQTGIFCAL-LNLLESAETEEVVDIFQVVKALRKARPGMVSTFEQYQFLYDVIA 1178
Cdd:cd14610   205 NKCYrgRSCPIIVHCSDGAGRSGTYILIdMVLNKMAKGAKEIDIAATLEHLRDQRPGMVQTKEQFEFALTAVA 277
R-PTPc-A-1 cd14621
catalytic domain of receptor-type tyrosine-protein phosphatase A, repeat 1; Receptor-type ...
 899-1181 4.71e-42

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: 156.34  E-value: 4.71e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578801329  899 EFQRLPSYRSWRTQHIGNQEENKSKNRNSNVIPYDYNRVPLkhelemskesehdsdessdDDSDSEEPSKYINASFIMSY 978
Cdd:cd14621    31 EFNALPACPIQATCEAASKEENKEKNRYVNILPYDHSRVHL-------------------TPVEGVPDSDYINASFINGY 91

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578801329  979 WKPEVMIAAQGPLKETIGDFWQMIFQRKVKVIVMLTELKHGDQEICAQYW-GEGKQTYGDIEVDLKDTDKSSTYTLRVFE 1057
Cdd:cd14621    92 QEKNKFIAAQGPKEETVNDFWRMIWEQNTATIVMVTNLKERKECKCAQYWpDQGCWTYGNIRVSVEDVTVLVDYTVRKFC 171

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578801329 1058 LRH----SKRKDSRTVYQYQYTNWSVEQLPAEPKELISMIQVVKQKLPQknssegnkhhKSTPLLIHCRDGSQQTGIFCA 1133
Cdd:cd14621   172 IQQvgdvTNKKPQRLITQFHFTSWPDFGVPFTPIGMLKFLKKVKNCNPQ----------YAGAIVVHCSAGVGRTGTFIV 241

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*...
gi 578801329 1134 LLNLLESAETEEVVDIFQVVKALRKARPGMVSTFEQYQFLYDVIASTY 1181
Cdd:cd14621   242 IDAMLDMMHAERKVDVYGFVSRIRAQRCQMVQTDMQYVFIYQALLEHY 289
R-PTPc-D-1 cd14624
catalytic domain of receptor-type tyrosine-protein phosphatase D, repeat 1; Receptor-type ...
 899-1177 5.07e-42

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: 156.04  E-value: 5.07e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578801329  899 EFQRLPSYRSWRTQHiGNQEENKSKNRNSNVIPYDYNRVPLKhelemskesehdsdessddDSDSEEPSKYINASFIMSY 978
Cdd:cd14624    27 EYESIDPGQQFTWEH-SNLEVNKPKNRYANVIAYDHSRVLLS-------------------AIEGIPGSDYINANYIDGY 86

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578801329  979 WKPEVMIAAQGPLKETIGDFWQMIFQRKVKVIVMLTELKHGDQEICAQYW-GEGKQTYGDIEVDLKDTDKSSTYTLRVFE 1057
Cdd:cd14624    87 RKQNAYIATQGALPETFGDFWRMIWEQRSATVVMMTKLEERSRVKCDQYWpSRGTETYGLIQVTLLDTVELATYCVRTFA 166

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578801329 1058 LRHSKRKDSRTVYQYQYTNWSVEQLPAEPKELISMIQVVKQKLPQknssegnkhhKSTPLLIHCRDGSQQTGIFCALLNL 1137
Cdd:cd14624   167 LYKNGSSEKREVRQFQFTAWPDHGVPEHPTPFLAFLRRVKTCNPP----------DAGPMVVHCSAGVGRTGCFIVIDAM 236

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|
gi 578801329 1138 LESAETEEVVDIFQVVKALRKARPGMVSTFEQYQFLYDVI 1177
Cdd:cd14624   237 LERIKHEKTVDIYGHVTLMRAQRNYMVQTEDQYIFIHDAL 276
R-PTP-N-N2 cd14546
PTP-like domain of receptor-type tyrosine-protein phosphatase-like N and N2; Receptor-type ...
 969-1178 1.15e-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: 152.21  E-value: 1.15e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578801329  969 YINASFIMSYwKPE--VMIAAQGPLKETIGDFWQMIFQRKVKVIVMLTELKHGDQEICAQYW-GEGKQTYGDIEVDL-KD 1044
Cdd:cd14546     1 YINASTIYDH-DPRnpAYIATQGPLPHTIADFWQMIWEQGCVVIVMLTRLQENGVKQCARYWpEEGSEVYHIYEVHLvSE 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578801329 1045 TDKSSTYTLRVFELRHSKRKDSRTVYQYQYTNWSVEQLPAEPKELISMIQVVKQKLpqknssegnkHHKSTPLLIHCRDG 1124
Cdd:cd14546    80 HIWCDDYLVRSFYLKNLQTSETRTVTQFHFLSWPDEGIPASAKPLLEFRRKVNKSY----------RGRSCPIVVHCSDG 149

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 578801329 1125 SQQTGIFCAL---LNLLESAETEevVDIFQVVKALRKARPGMVSTFEQYQFLYDVIA 1178
Cdd:cd14546   150 AGRTGTYILIdmvLNRMAKGAKE--IDIAATLEHLRDQRPGMVKTKDQFEFVLTAVA 204
R-PTPc-U-1 cd14632
catalytic domain of receptor-type tyrosine-protein phosphatase U, repeat 1; Receptor-type ...
 969-1177 1.68e-41

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: 151.74  E-value: 1.68e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578801329  969 YINASFIMSYWKPEVMIAAQGPLKETIGDFWQMIFQRKVKVIVMLTELKHGDQEICAQYWGEGKQTYGDIEVDLKDTDKS 1048
Cdd:cd14632     1 YINANYIDGYHRSNHFIATQGPKQEMVYDFWRMVWQEHCSSIVMITKLVEVGRVKCSKYWPDDSDTYGDIKITLLKTETL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578801329 1049 STYTLRVFELRHSKRKDSRTVYQYQYTNWSVEQLPAEPKELISMIQVVKQKLPQknssegnkhhKSTPLLIHCRDGSQQT 1128
Cdd:cd14632    81 AEYSVRTFALERRGYSARHEVKQFHFTSWPEHGVPYHATGLLAFIRRVKASTPP----------DAGPVVVHCSAGAGRT 150

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*....
gi 578801329 1129 GIFCALLNLLESAETEEVVDIFQVVKALRKARPGMVSTFEQYQFLYDVI 1177
Cdd:cd14632   151 GCYIVLDVMLDMAECEGVVDIYNCVKTLCSRRINMIQTEEQYIFIHDAI 199
R-PTPc-O cd14614
catalytic domain of receptor-type tyrosine-protein phosphatase O; Receptor-type ...
 920-1174 1.73e-41

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: 153.12  E-value: 1.73e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578801329  920 NKSKNRNSNVIPYDYNRVPL--KHELEmskesehdsdessdddsdseePSKYINASFIMSYWKPEVMIAAQGPLKETIGD 997
Cdd:cd14614    12 NRCKNRYTNILPYDFSRVKLvsMHEEE---------------------GSDYINANYIPGYNSPQEYIATQGPLPETRND 70

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578801329  998 FWQMIFQRKVKVIVMLTELKHGDQEICAQYW--GEGKQTYGDIEVDLKDTDKSSTYTLRVFELRHSkrKDSRTVYQYQYT 1075
Cdd:cd14614    71 FWKMVLQQKSQIIVMLTQCNEKRRVKCDHYWpfTEEPVAYGDITVEMLSEEEQPDWAIREFRVSYA--DEVQDVMHFNYT 148

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578801329 1076 NWSVEQLPA--EPKELISMIQVVKQklpQKNSSEGnkhhkstPLLIHCRDGSQQTGIFCALLNLLESAETEEVVDIFQVV 1153
Cdd:cd14614   149 AWPDHGVPTanAAESILQFVQMVRQ---QAVKSKG-------PMIIHCSAGVGRTGTFIALDRLLQHIRDHEFVDILGLV 218

                         250       260
                  ....*....|....*....|.
gi 578801329 1154 KALRKARPGMVSTFEQYQFLY 1174
Cdd:cd14614   219 SEMRSYRMSMVQTEEQYIFIH 239
PTPc-N18 cd14603
catalytic domain of tyrosine-protein phosphatase non-receptor type 18; Tyrosine-protein ...
 911-1181 1.92e-41

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: 153.44  E-value: 1.92e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578801329  911 TQHIGNQEENKSKNRNSNVIPYDYNRV---PLKHELEmskesehdsdessdddsdseepSKYINASFIMSYWKPEVMIAA 987
Cdd:cd14603    21 STVAGGRKENVKKNRYKDILPYDQTRVilsLLQEEGH----------------------SDYINANFIKGVDGSRAYIAT 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578801329  988 QGPLKETIGDFWQMIFQRKVKVIVM-LTELKHGDQEiCAQYWGEGKQT--YGDIEV-DLKDTDKSSTYTLRVfeLRHSKR 1063
Cdd:cd14603    79 QGPLSHTVLDFWRMIWQYGVKVILMaCREIEMGKKK-CERYWAQEQEPlqTGPFTItLVKEKRLNEEVILRT--LKVTFQ 155

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578801329 1064 KDSRTVYQYQYTNWSVEQLPAEPKELISMIQVVKQKlpQKNSSEgnkhhkstPLLIHCRDGSQQTGIFCAL---LNLLES 1140
Cdd:cd14603   156 KESRSVSHFQYMAWPDHGIPDSPDCMLAMIELARRL--QGSGPE--------PLCVHCSAGCGRTGVICTVdyvRQLLLT 225

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|.
gi 578801329 1141 AETEEVVDIFQVVKALRKARPGMVSTFEQYQFLYDVIASTY 1181
Cdd:cd14603   226 QRIPPDFSIFDVVLEMRKQRPAAVQTEEQYEFLYHTVAQMF 266
R-PTPc-Z-1 cd17668
catalytic domain of receptor-type tyrosine-protein phosphatase Z, repeat 1; Receptor-type ...
 969-1177 2.28e-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: 151.28  E-value: 2.28e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578801329  969 YINASFIMSYWKPEVMIAAQGPLKETIGDFWQMIFQRKVKVIVMLTELKHGDQEICAQYW-GEGKQTYGDIEVDLKDTDK 1047
Cdd:cd17668     1 YINANYVDGYNKPKAYIAAQGPLKSTAEDFWRMIWEHNVEVIVMITNLVEKGRRKCDQYWpADGSEEYGNFLVTQKSVQV 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578801329 1048 SSTYTLRVFELRHSK--------RKDSRTVYQYQYTNWSVEQLPAEPKELISMIQvvkqklpqknSSEGNKHHKSTPLLI 1119
Cdd:cd17668    81 LAYYTVRNFTLRNTKikkgsqkgRPSGRVVTQYHYTQWPDMGVPEYTLPVLTFVR----------KASYAKRHAVGPVVV 150

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 578801329 1120 HCRDGSQQTGIFCALLNLLESAETEEVVDIFQVVKALRKARPGMVSTFEQYQFLYDVI 1177
Cdd:cd17668   151 HCSAGVGRTGTYIVLDSMLQQIQHEGTVNIFGFLKHIRSQRNYLVQTEEQYVFIHDAL 208
R-PTPc-A-E-1 cd14551
catalytic domain of receptor-type tyrosine-protein phosphatase A and E, repeat 1; ...
 969-1174 2.69e-41

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: 150.83  E-value: 2.69e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578801329  969 YINASFIMSYWKPEVMIAAQGPLKETIGDFWQMIFQRKVKVIVMLTELKHGDQEICAQYW-GEGKQTYGDIEVDLKDTDK 1047
Cdd:cd14551     1 YINASYIDGYQEKNKFIAAQGPKDETVNDFWRMIWEQGSATIVMVTNLKERKEKKCSQYWpDQGCWTYGNLRVRVEDTVV 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578801329 1048 SSTYTLRVFELRH----SKRKDSRTVYQYQYTNWSVEQLPAEPKELISMIQVVKQKLPQKNSsegnkhhkstPLLIHCRD 1123
Cdd:cd14551    81 LVDYTTRKFCIQKvnrgIGEKRVRLVTQFHFTSWPDFGVPFTPIGMLKFLKKVKSANPPRAG----------PIVVHCSA 150

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|.
gi 578801329 1124 GSQQTGIFCALLNLLESAETEEVVDIFQVVKALRKARPGMVSTFEQYQFLY 1174
Cdd:cd14551   151 GVGRTGTFIVIDAMLDMMHAEGKVDVFGFVSRIRQQRSQMVQTDMQYVFIY 201
R-PTPc-K-1 cd14631
catalytic domain of receptor-type tyrosine-protein phosphatase K, repeat 1; Receptor-type ...
 967-1177 3.41e-41

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: 151.33  E-value: 3.41e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578801329  967 SKYINASFIMSYWKPEVMIAAQGPLKETIGDFWQMIFQRKVKVIVMLTELKHGDQEICAQYWGEGKQTYGDIEVDLKDTD 1046
Cdd:cd14631    13 SDYINANYIDGYQRPSHYIATQGPVHETVYDFWRMIWQEQSACIVMVTNLVEVGRVKCYKYWPDDTEVYGDFKVTCVEME 92

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578801329 1047 KSSTYTLRVFELRHSKRKDSRTVYQYQYTNWSVEQLPAEPKELISMIQVVKQKLPQknssegnkhhKSTPLLIHCRDGSQ 1126
Cdd:cd14631    93 PLAEYVVRTFTLERRGYNEIREVKQFHFTGWPDHGVPYHATGLLSFIRRVKLSNPP----------SAGPIVVHCSAGAG 162

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|.
gi 578801329 1127 QTGIFCALLNLLESAETEEVVDIFQVVKALRKARPGMVSTFEQYQFLYDVI 1177
Cdd:cd14631   163 RTGCYIVIDIMLDMAEREGVVDIYNCVKALRSRRINMVQTEEQYIFIHDAI 213
R-PTPc-E-1 cd14620
catalytic domain of receptor-type tyrosine-protein phosphatase E, repeat 1; Receptor-type ...
 928-1177 7.60e-41

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: 150.48  E-value: 7.60e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578801329  928 NVIPYDYNRVPLKHelemskesehdsdessdddSDSEEPSKYINASFIMSYWKPEVMIAAQGPLKETIGDFWQMIFQRKV 1007
Cdd:cd14620     3 NILPYDHSRVILSQ-------------------LDGIPCSDYINASYIDGYKEKNKFIAAQGPKQETVNDFWRMVWEQKS 63

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578801329 1008 KVIVMLTELKHGDQEICAQYWGE-GKQTYGDIEVDLKDTDKSSTYTLRVFELR---HSKRKDSRTVYQYQYTNWSVEQLP 1083
Cdd:cd14620    64 ATIVMLTNLKERKEEKCYQYWPDqGCWTYGNIRVAVEDCVVLVDYTIRKFCIQpqlPDGCKAPRLVTQLHFTSWPDFGVP 143

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578801329 1084 AEPkelISMIQVVKqKLPQKNSSEGNkhhkstPLLIHCRDGSQQTGIFCALLNLLESAETEEVVDIFQVVKALRKARPGM 1163
Cdd:cd14620   144 FTP---IGMLKFLK-KVKSVNPVHAG------PIVVHCSAGVGRTGTFIVIDAMIDMMHAEQKVDVFEFVSRIRNQRPQM 213

                         250
                  ....*....|....
gi 578801329 1164 VSTFEQYQFLYDVI 1177
Cdd:cd14620   214 VQTDMQYSFIYQAL 227
R-PTPc-C-1 cd14557
catalytic domain of receptor-type tyrosine-protein phosphatase C, repeat 1; Receptor-type ...
 969-1174 1.06e-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: 149.21  E-value: 1.06e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578801329  969 YINASFIMSYWKPEVMIAAQGPLKETIGDFWQMIFQRKVKVIVMLTELKHGDQEICAQYW---GEGKQTYGDIEVDLKDT 1045
Cdd:cd14557     1 YINASYIDGFKEPRKYIAAQGPKDETVDDFWRMIWEQKSTVIVMVTRCEEGNRNKCAQYWpsmEEGSRAFGDVVVKINEE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578801329 1046 DKSSTYTLRVFELRHSKRKDS-RTVYQYQYTNWSVEQLPAEPKELIsmiqvvkqKLPQKNSSEGNKHhkSTPLLIHCRDG 1124
Cdd:cd14557    81 KICPDYIIRKLNINNKKEKGSgREVTHIQFTSWPDHGVPEDPHLLL--------KLRRRVNAFNNFF--SGPIVVHCSAG 150

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|
gi 578801329 1125 SQQTGIFCALLNLLESAETEEVVDIFQVVKALRKARPGMVSTFEQYQFLY 1174
Cdd:cd14557   151 VGRTGTYIGIDAMLEGLEAEGRVDVYGYVVKLRRQRCLMVQVEAQYILIH 200
R-PTPc-Q cd14616
catalytic domain of receptor-type tyrosine-protein phosphatase Q; Receptor-type ...
 924-1174 1.73e-40

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: 149.29  E-value: 1.73e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578801329  924 NRNSNVIPYDYNRVPLKHElemskesehdsdessdddsDSEEPSKYINASFIMSYWKPEVMIAAQGPLKETIGDFWQMIF 1003
Cdd:cd14616     1 NRFPNIKPYNNNRVKLIAD-------------------AGVPGSDYINASYISGYLCPNEFIATQGPLPGTVGDFWRMVW 61

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578801329 1004 QRKVKVIVMLTELKHGDQEICAQYWGEGKQ---TYGDIEVDLKDTDKSSTYTLRvfELRHSKRKDSRTVYQYQYTNWSVE 1080
Cdd:cd14616    62 ETRAKTIVMLTQCFEKGRIRCHQYWPEDNKpvtVFGDIVITKLMEDVQIDWTIR--DLKIERHGDYMMVRQCNFTSWPEH 139

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578801329 1081 QLPAEPKELISMIQVVKqklpqknsseGNKHHKSTPLLIHCRDGSQQTGIFCALLNLLESAETEEVVDIFQVVKALRKAR 1160
Cdd:cd14616   140 GVPESSAPLIHFVKLVR----------ASRAHDNTPMIVHCSAGVGRTGVFIALDHLTQHINDHDFVDIYGLVAELRSER 209

                         250
                  ....*....|....
gi 578801329 1161 PGMVSTFEQYQFLY 1174
Cdd:cd14616   210 MCMVQNLAQYIFLH 223
PTPc-N22_18_12 cd14542
catalytic domain of tyrosine-protein phosphatase non-receptor type 22, type 18 and type 12; ...
 969-1174 2.90e-40

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: 147.95  E-value: 2.90e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578801329  969 YINASFIMSYWKPEVMIAAQGPLKETIGDFWQMIFQRKVKVIVMLTELKHGDQEICAQYW---GEGKQTYGDIEVDL-KD 1044
Cdd:cd14542     1 YINANFIKGVSGSKAYIATQGPLPNTVLDFWRMIWEYNVQVIVMACREFEMGKKKCERYWpeeGEEQLQFGPFKISLeKE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578801329 1045 TDKSSTYTLRVFELRHSkrKDSRTVYQYQYTNWSVEQLPAEPKELISMIQVVKQKlpqknssegnKHHKSTPLLIHCRDG 1124
Cdd:cd14542    81 KRVGPDFLIRTLKVTFQ--KESRTVYQFHYTAWPDHGVPSSVDPILDLVRLVRDY----------QGSEDVPICVHCSAG 148

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 578801329 1125 SQQTGIFCAL---LNLLESAETEEVVDIFQVVKALRKARPGMVSTFEQYQFLY 1174
Cdd:cd14542   149 CGRTGTICAIdyvWNLLKTGKIPEEFSLFDLVREMRKQRPAMVQTKEQYELVY 201
R-PTPc-typeIIb-2 cd14556
PTP domain of type IIb (or R2B) subfamily receptor-type tyrosine-protein phosphatases, repeat ...
 659-859 5.81e-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: 146.78  E-value: 5.81e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578801329  659 YINASYIDGFKEPRKYIAAQGPRDETVDDFWRMIWEQKATVIVMVTRCEEGNRNkCAEYWPsmEEGTRAFGDVVVKINQH 738
Cdd:cd14556     1 YINAALLDSYKQPAAFIVTQHPLPNTVTDFWRLVYDYGCTSIVMLNQLDPKDQS-CPQYWP--DEGSGTYGPIQVEFVST 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578801329  739 KRCPDYIIQKLNIVNKKEKATG-REVTHIQFTSWPDHG-VPEDPHLLLKLRRRVNA-FSNFFSGPIVVHCSAGVGRTGTY 815
Cdd:cd14556    78 TIDEDVISRIFRLQNTTRPQEGyRMVQQFQFLGWPRDRdTPPSKRALLKLLSEVEKwQEQSGEGPIVVHCLNGVGRSGVF 157

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....
gi 578801329  816 IGIDAMLEGLEAENKVDVYGYVVKLRRQRCLMVQVEAQYILIHQ 859
Cdd:cd14556   158 CAISSVCERIKVENVVDVFQAVKTLRNHRPNMVETEEQYKFCYD 201
COG5599 COG5599
Protein tyrosine phosphatase [Signal transduction mechanisms];
632-857 6.75e-40

Protein tyrosine phosphatase [Signal transduction mechanisms];


Pssm-ID: 444335 [Multi-domain]  Cd Length: 282  Bit Score: 149.47  E-value: 6.75e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578801329  632 KNRYVDILPYDYNRVElseINGdagsNYINASYIDGfKEPRKYIAAQGPRDETVDDFWRMIWEQKATVIVMVTRCEEG-- 709
Cdd:COG5599    45 LNRFRDIQPYKETALR---ANL----GYLNANYIQV-IGNHRYIATQYPLEEQLEDFFQMLFDNNTPVLVVLASDDEIsk 116

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578801329  710 NRNKCAEYWPsmEEGTRAFGDVVVKINQHKRCPDYIIQKLNIVNKKEKA-TGREVTHIQFTSWPDHGVP--EDPHLLLKL 786
Cdd:COG5599   117 PKVKMPVYFR--QDGEYGKYEVSSELTESIQLRDGIEARTYVLTIKGTGqKKIEIPVLHVKNWPDHGAIsaEALKNLADL 194

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 578801329  787 RRRVNAFSNFFSGPIVVHCSAGVGRTGTYIGIDAMLEGLEAEN--KVDVYGYVVKLRRQR-CLMVQVEAQYILI 857
Cdd:COG5599   195 IDKKEKIKDPDKLLPVVHCRAGVGRTGTLIACLALSKSINALVqiTLSVEEIVIDMRTSRnGGMVQTSEQLDVL 268
PTPc-N7 cd14612
catalytic domain of tyrosine-protein phosphatase non-receptor type 7; Tyrosine-protein ...
 922-1178 2.27e-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: 146.90  E-value: 2.27e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578801329  922 SKNRNSNVIPYDYNRVPLKHElemskesehdsdessdddSDSEEPSKYINASFIMSY-WKPEVMIAAQGPLKETIGDFWQ 1000
Cdd:cd14612    17 SKDRYKTILPNPQSRVCLRRA------------------GSQEEEGSYINANYIRGYdGKEKAYIATQGPMLNTVSDFWE 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578801329 1001 MIFQRKVKVIVMLTELKHGdQEICAQYWGEGKQTYGDIEVDLKDTDKSSTYTLRVFELRHSkrKDSRTVYQYQYTNWSVE 1080
Cdd:cd14612    79 MVWQEECPIIVMITKLKEK-KEKCVHYWPEKEGTYGRFEIRVQDMKECDGYTIRDLTIQLE--EESRSVKHYWFSSWPDH 155

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578801329 1081 QLPAEPKELISMIQVVKQKlPQKNSSEGnkhhkstPLLIHCRDGSQQTGIFCALLNLLESAETEEVVDIFQVVKALRKAR 1160
Cdd:cd14612   156 QTPESAGPLLRLVAEVEES-RQTAASPG-------PIVVHCSAGIGRTGCFIATSIGCQQLKDTGKVDILGIVCQLRLDR 227

                         250
                  ....*....|....*...
gi 578801329 1161 PGMVSTFEQYQFLYDVIA 1178
Cdd:cd14612   228 GGMIQTSEQYQFLHHTLA 245
PTPc-N22 cd14602
catalytic domain of tyrosine-protein phosphatase non-receptor type 22; Tyrosine-protein ...
 923-1177 2.54e-39

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: 146.52  E-value: 2.54e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578801329  923 KNRNSNVIPYDYNRVPLKhelemskesehdsdessddDSDSEEPSKYINASFIMSYWKPEVMIAAQGPLKETIGDFWQMI 1002
Cdd:cd14602     1 KNRYKDILPYDHSRVELS-------------------LITSDEDSDYINANFIKGVYGPRAYIATQGPLSTTLLDFWRMI 61

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578801329 1003 FQRKVKVIVM-LTELKHGDQEiCAQYW---GEGKQTYGDIEVDLKDTDKSSTYTLRVfeLRHSKRKDSRTVYQYQYTNWS 1078
Cdd:cd14602    62 WEYSVLIIVMaCMEFEMGKKK-CERYWaepGEMQLEFGPFSVTCEAEKRKSDYIIRT--LKVKFNSETRTIYQFHYKNWP 138

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578801329 1079 VEQLPAEPKELISMIQVVKQKlpqknssegnKHHKSTPLLIHCRDGSQQTGIFCAL---LNLLESAETEEVVDIFQVVKA 1155
Cdd:cd14602   139 DHDVPSSIDPILELIWDVRCY----------QEDDSVPICIHCSAGCGRTGVICAIdytWMLLKDGIIPENFSVFSLIQE 208

                         250       260
                  ....*....|....*....|..
gi 578801329 1156 LRKARPGMVSTFEQYQFLYDVI 1177
Cdd:cd14602   209 MRTQRPSLVQTKEQYELVYNAV 230
R-PTP-N cd14609
PTP-like domain of receptor-type tyrosine-protein phosphatase N; Receptor-type ...
 896-1178 5.41e-39

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: 147.11  E-value: 5.41e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578801329  896 LEAEFQRLPSYRSW-RTQHIGNQEENKSKNRNSNVIPYDYNRVPLKHELEMSKesehdsdessdddsdseepSKYINASF 974
Cdd:cd14609    17 LAKEWQALCAYQAEpNTCSTAQGEANVKKNRNPDFVPYDHARIKLKAESNPSR-------------------SDYINASP 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578801329  975 IMSYwKPEV--MIAAQGPLKETIGDFWQMIFQRKVKVIVMLTELKHGDQEICAQYW-GEGKQTYGDIEVDL-KDTDKSST 1050
Cdd:cd14609    78 IIEH-DPRMpaYIATQGPLSHTIADFWQMVWENGCTVIVMLTPLVEDGVKQCDRYWpDEGSSLYHIYEVNLvSEHIWCED 156

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578801329 1051 YTLRVFELRHSKRKDSRTVYQYQYTNWSVEQLPAEPKELISMIQVVkqklpqknssegNKHH--KSTPLLIHCRDGSQQT 1128
Cdd:cd14609   157 FLVRSFYLKNVQTQETRTLTQFHFLSWPAEGIPSSTRPLLDFRRKV------------NKCYrgRSCPIIVHCSDGAGRT 224

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|...
gi 578801329 1129 GIFCAL---LNLLESAETEevVDIFQVVKALRKARPGMVSTFEQYQFLYDVIA 1178
Cdd:cd14609   225 GTYILIdmvLNRMAKGVKE--IDIAATLEHVRDQRPGMVRTKDQFEFALTAVA 275
PTPc-N13 cd14597
catalytic domain of tyrosine-protein phosphatase non-receptor type 13; Tyrosine-protein ...
 918-1177 7.43e-39

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: 144.97  E-value: 7.43e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578801329  918 EENKSKNRNSNVIPYDYNRVPLKHElemskesehdsdessdddsdseepSKYINASFI-MSYWKPE-VMIAAQGPLKETI 995
Cdd:cd14597     1 KENRKKNRYKNILPYDTTRVPLGDE------------------------GGYINASFIkMPVGDEEfVYIACQGPLPTTV 56

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578801329  996 GDFWQMIFQRKVKVIVMLTELKHGDQEICAQYWGE--GKQTYGD--IEVDLKDTDKSSTYTLRVFELRHSKRKDSRTVYQ 1071
Cdd:cd14597    57 ADFWQMVWEQKSTVIAMMTQEVEGGKIKCQRYWPEilGKTTMVDnrLQLTLVRMQQLKNFVIRVLELEDIQTREVRHITH 136

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578801329 1072 YQYTNWSVEQLPAEPKELISMIQVVKQKlpqknssegnkhHKSTPLLIHCRDGSQQTGIFCALLNLLESAETEEVVDIFQ 1151
Cdd:cd14597   137 LNFTAWPDHDTPSQPEQLLTFISYMRHI------------HKSGPIITHCSAGIGRSGTLICIDVVLGLISKDLDFDISD 204

                         250       260
                  ....*....|....*....|....*.
gi 578801329 1152 VVKALRKARPGMVSTFEQYQFLYDVI 1177
Cdd:cd14597   205 IVRTMRLQRHGMVQTEDQYIFCYQVI 230
PTPc-N5 cd14613
catalytic domain of tyrosine-protein phosphatase non-receptor type 5; Tyrosine-protein ...
 923-1178 1.72e-38

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: 144.62  E-value: 1.72e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578801329  923 KNRNSNVIPYDYNRVPLKHELEMSKEsehdsdessdddsdseepSKYINASFIMSYWKPE-VMIAAQGPLKETIGDFWQM 1001
Cdd:cd14613    28 KNRYKTILPNPHSRVCLTSPDQDDPL------------------SSYINANYIRGYGGEEkVYIATQGPTVNTVGDFWRM 89

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578801329 1002 IFQRKVKVIVMLTELKHGDqEICAQYWGEGKQTYGDIEVDLKDTDKSSTYTLRVFELRhsKRKDSRTVYQYQYTNWSVEQ 1081
Cdd:cd14613    90 VWQERSPIIVMITNIEEMN-EKCTEYWPEEQVTYEGIEITVKQVIHADDYRLRLITLK--SGGEERGLKHYWYTSWPDQK 166

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578801329 1082 LPAEPKELISMIQVVKQKLPQKNSSEGnkhhkstPLLIHCRDGSQQTGIFCALLNLLESAETEEVVDIFQVVKALRKARP 1161
Cdd:cd14613   167 TPDNAPPLLQLVQEVEEARQQAEPNCG-------PVIVHCSAGIGRTGCFIATSICCKQLRNEGVVDILRTTCQLRLDRG 239

                         250
                  ....*....|....*..
gi 578801329 1162 GMVSTFEQYQFLYDVIA 1178
Cdd:cd14613   240 GMIQTCEQYQFVHHVLS 256
PTPc_motif smart00404
Protein tyrosine phosphatase, catalytic domain motif;
762-863 7.84e-38

Protein tyrosine phosphatase, catalytic domain motif;


Pssm-ID: 214649 [Multi-domain]  Cd Length: 105  Bit Score: 137.10  E-value: 7.84e-38
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578801329    762 EVTHIQFTSWPDHGVPEDPHLLLKLRRRVNAFSNF--FSGPIVVHCSAGVGRTGTYIGIDAMLEGLEAE-NKVDVYGYVV 838
Cdd:smart00404    1 TVKHYHYTGWPDHGVPESPDSILELLRAVKKNLNQseSSGPVVVHCSAGVGRTGTFVAIDILLQQLEAEaGEVDIFDTVK 80

                            90       100
                    ....*....|....*....|....*
gi 578801329    839 KLRRQRCLMVQVEAQYILIHQALVE 863
Cdd:smart00404   81 ELRSQRPGMVQTEEQYLFLYRALLE 105
PTPc_DSPc smart00012
Protein tyrosine phosphatase, catalytic domain, undefined specificity; Protein tyrosine ...
 762-863 7.84e-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: 7.84e-38
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578801329    762 EVTHIQFTSWPDHGVPEDPHLLLKLRRRVNAFSNF--FSGPIVVHCSAGVGRTGTYIGIDAMLEGLEAE-NKVDVYGYVV 838
Cdd:smart00012    1 TVKHYHYTGWPDHGVPESPDSILELLRAVKKNLNQseSSGPVVVHCSAGVGRTGTFVAIDILLQQLEAEaGEVDIFDTVK 80

                            90       100
                    ....*....|....*....|....*
gi 578801329    839 KLRRQRCLMVQVEAQYILIHQALVE 863
Cdd:smart00012   81 ELRSQRPGMVQTEEQYLFLYRALLE 105
PTPc-N11_6 cd14544
catalytic domain of tyrosine-protein phosphatase non-receptor type 11 and type 6; ...
 920-1178 8.44e-38

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: 142.60  E-value: 8.44e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578801329  920 NKSKNRNSNVIPYDYNRVPLKhelemskesehdsdessdDDSDSEEPSKYINASFIMS-------YWKPEVMIAAQGPLK 992
Cdd:cd14544     1 NKGKNRYKNILPFDHTRVILK------------------DRDPNVPGSDYINANYIRNenegpttDENAKTYIATQGCLE 62

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578801329  993 ETIGDFWQMIFQRKVKVIVMLTELKHGDQEICAQYW---GEGKQtYGDIEV-DLKDTDKSStYTLRVFELRHSKRKDS-R 1067
Cdd:cd14544    63 NTVSDFWSMVWQENSRVIVMTTKEVERGKNKCVRYWpdeGMQKQ-YGPYRVqNVSEHDTTD-YTLRELQVSKLDQGDPiR 140

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578801329 1068 TVYQYQYTNWSVEQLPAEPKELISMIQVVKQKLPQKNSsegnkhhkSTPLLIHCRDGSQQTGIFCALLNLLESAETEEV- 1146
Cdd:cd14544   141 EIWHYQYLSWPDHGVPSDPGGVLNFLEDVNQRQESLPH--------AGPIVVHCSAGIGRTGTFIVIDMLLDQIKRKGLd 212

                         250       260       270
                  ....*....|....*....|....*....|....
gi 578801329 1147 --VDIFQVVKALRKARPGMVSTFEQYQFLYDVIA 1178
Cdd:cd14544   213 cdIDIQKTIQMVRSQRSGMVQTEAQYKFIYVAVA 246
PTPc-N21_14 cd14540
catalytic domain of tyrosine-protein phosphatase non-receptor type 21 and type 14; ...
 969-1177 1.10e-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: 141.05  E-value: 1.10e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578801329  969 YINASFImsywKPEV------MIAAQGPLKETIGDFWQMIFQRKVKVIVMLTELKHGDQEICAQYW-----GEGKQTYGD 1037
Cdd:cd14540     1 YINASHI----TATVggkqrfYIAAQGPLQNTVGDFWQMVWEQGVYLVVMVTAEEEGGREKCFRYWptlggEHDALTFGE 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578801329 1038 IEVDLKDTDKSSTYTLRVFELRHSKRKDSRTVYQYQYTNWSVEQLPAEPKELISMIQVVkQKLPQKNSSEGNKHHKSTPL 1117
Cdd:cd14540    77 YKVSTKFSVSSGCYTTTGLRVKHTLSGQSRTVWHLQYTDWPDHGCPEDVSGFLDFLEEI-NSVRRHTNQDVAGHNRNPPT 155

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 578801329 1118 LIHCRDGSQQTG--IFCALlnLLESAETEEVVDIFQVVKALRKARPGMVSTFEQYQFLYDVI 1177
Cdd:cd14540   156 LVHCSAGVGRTGvvILADL--MLYCLDHNEELDIPRVLALLRHQRMLLVQTLAQYKFVYNVL 215
R-PTPc-R cd14611
catalytic domain of receptor-type tyrosine-protein phosphatase R; Receptor-type ...
 922-1174 5.30e-37

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: 139.28  E-value: 5.30e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578801329  922 SKNRNSNVIPYDYNRVPLKhelemskesehdsdessdDDSDSEEPSKYINASFIMSYW-KPEVMIAAQGPLKETIGDFWQ 1000
Cdd:cd14611     1 TKNRYKTILPNPHSRVCLK------------------PKNSNDSLSTYINANYIRGYGgKEKAFIATQGPMINTVNDFWQ 62

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578801329 1001 MIFQRKVKVIVMLTELKHGDqEICAQYWGEGKQTYGDIEVDLKDTDKSSTYTLRVFELRHSKRkdSRTVYQYQYTNWSVE 1080
Cdd:cd14611    63 MVWQEDSPVIVMITKLKEKN-EKCVLYWPEKRGIYGKVEVLVNSVKECDNYTIRNLTLKQGSQ--SRSVKHYWYTSWPDH 139

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578801329 1081 QLPAEPKELISMIQVVKQKlPQKNSSEGnkhhkstPLLIHCRDGSQQTGIFCALLNLLESAETEEVVDIFQVVKALRKAR 1160
Cdd:cd14611   140 KTPDSAQPLLQLMLDVEED-RLASPGRG-------PVVVHCSAGIGRTGCFIATTIGCQQLKEEGVVDVLSIVCQLRVDR 211

                         250
                  ....*....|....
gi 578801329 1161 PGMVSTFEQYQFLY 1174
Cdd:cd14611   212 GGMVQTSEQYEFVH 225
PTPc-N20_13 cd14538
catalytic domain of tyrosine-protein phosphatase non-receptor type 20 and type 13; ...
 969-1177 1.24e-36

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: 137.51  E-value: 1.24e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578801329  969 YINASFI--------MSYwkpevmIAAQGPLKETIGDFWQMIFQRKVKVIVMLTELKHGDQEICAQYWGEGKQT----YG 1036
Cdd:cd14538     1 YINASHIripvggdtYHY------IACQGPLPNTTGDFWQMVWEQKSEVIAMVTQDVEGGKVKCHRYWPDSLNKplicGG 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578801329 1037 DIEVDLKDTDKSSTYTLRVFELRHSKRKDSRTVYQYQYTNWSVEQLPAEPKELISMIQVVKqklpqknssegnKHHKSTP 1116
Cdd:cd14538    75 RLEVSLEKYQSLQDFVIRRISLRDKETGEVHHITHLNFTTWPDHGTPQSADPLLRFIRYMR------------RIHNSGP 142

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 578801329 1117 LLIHCRDGSQQTGIFCALLNLLESAETEEVVDIFQVVKALRKARPGMVSTFEQYQFLYDVI 1177
Cdd:cd14538   143 IVVHCSAGIGRTGVLITIDVALGLIERDLPFDIQDIVKDLREQRQGMIQTKDQYIFCYKAC 203
PTPc-N6 cd14606
catalytic domain of tyrosine-protein phosphatase non-receptor type 6; Tyrosine-protein ...
 912-1178 1.38e-36

catalytic domain of tyrosine-protein phosphatase non-receptor type 6; Tyrosine-protein phosphatase non-receptor type 6 (PTPN6), also called SH2 domain-containing protein-tyrosine phosphatase 1 (SHP1 or SHP-1), belongs to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. PTPN6 expression is restricted mainly to hematopoietic and epithelial cells. It is an important regulator of hematopoietic cells, downregulating pathways that promote cell growth, survival, adhesion, and activation. It regulates glucose homeostasis by modulating insulin signalling in the liver and muscle, and it also negatively regulates bone resorption, affecting both the formation and the function of osteoclasts. PTPN6 contains two tandem SH2 domains, a catalytic PTP domain, and a C-terminal tail with regulatory properties.


Pssm-ID: 350454 [Multi-domain]  Cd Length: 266  Bit Score: 139.63  E-value: 1.38e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578801329  912 QHIGNQEENKSKNRNSNVIPYDYNRVPLKhelemskesehdsdessdDDSDSEEPSKYINASFIMSYW-----KPEVMIA 986
Cdd:cd14606    10 RLEGQRPENKSKNRYKNILPFDHSRVILQ------------------GRDSNIPGSDYINANYVKNQLlgpdeNAKTYIA 71

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578801329  987 AQGPLKETIGDFWQMIFQRKVKVIVMLT-ELKHGDQEiCAQYWGE--GKQTYGDIEVDLKDTDKSSTYTLRVFELRHSKR 1063
Cdd:cd14606    72 SQGCLEATVNDFWQMAWQENSRVIVMTTrEVEKGRNK-CVPYWPEvgMQRAYGPYSVTNCGEHDTTEYKLRTLQVSPLDN 150

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578801329 1064 KDS-RTVYQYQYTNWSVEQLPAEPKELISMIQVVKQK---LPqknssegnkhhKSTPLLIHCRDGSQQTGIFCALLNLLE 1139
Cdd:cd14606   151 GELiREIWHYQYLSWPDHGVPSEPGGVLSFLDQINQRqesLP-----------HAGPIIVHCSAGIGRTGTIIVIDMLME 219

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|..
gi 578801329 1140 SAETEEV---VDIFQVVKALRKARPGMVSTFEQYQFLYDVIA 1178
Cdd:cd14606   220 NISTKGLdcdIDIQKTIQMVRAQRSGMVQTEAQYKFIYVAIA 261
PTP-N23 cd14539
PTP-like domain of tyrosine-protein phosphatase non-receptor type 23; Tyrosine-protein ...
 969-1175 1.59e-36

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: 137.13  E-value: 1.59e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578801329  969 YINASFI--MSYWKPEVmIAAQGPLKETIGDFWQMIFQRKVKVIVMLTelkhGDQEICAQ----YWGEGK---QTYGDIE 1039
Cdd:cd14539     1 YINASLIedLTPYCPRF-IATQAPLPGTAADFWLMVYEQQVSVIVMLV----SEQENEKQkvhrYWPTERgqaLVYGAIT 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578801329 1040 VDLKDTDKSSTYTLRVFELRHSKRKDSRTVYQYQYTNWSVEQLPAEPKELISMIQVVKQKLPQKNSSEgnkhhksTPLLI 1119
Cdd:cd14539    76 VSLQSVRTTPTHVERIISIQHKDTRLSRSVVHLQFTTWPELGLPDSPNPLLRFIEEVHSHYLQQRSLQ-------TPIVV 148

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 578801329 1120 HCRDGSQQTGIFCALLN-LLESAETEEVVDIFQVVKALRKARPGMVSTFEQYQFLYD 1175
Cdd:cd14539   149 HCSSGVGRTGAFCLLYAaVQEIEAGNGIPDLPQLVRKMRQQRKYMLQEKEHLKFCYE 205
PTPc-N11 cd14605
catalytic domain of tyrosine-protein phosphatase non-receptor type 11; Tyrosine-protein ...
 919-1174 2.16e-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: 2.16e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578801329  919 ENKSKNRNSNVIPYDYNRVPLkHELEMSKESehdsdessdddsdseepSKYINASFIMSYW-------KPE-VMIAAQGP 990
Cdd:cd14605     1 ENKNKNRYKNILPFDHTRVVL-HDGDPNEPV-----------------SDYINANIIMPEFetkcnnsKPKkSYIATQGC 62

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578801329  991 LKETIGDFWQMIFQRKVKVIVMLT-ELKHGDQEiCAQYWGE--GKQTYGDIEV-DLKDTdKSSTYTLRvfELRHSK---R 1063
Cdd:cd14605    63 LQNTVNDFWRMVFQENSRVIVMTTkEVERGKSK-CVKYWPDeyALKEYGVMRVrNVKES-AAHDYILR--ELKLSKvgqG 138

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578801329 1064 KDSRTVYQYQYTNWSVEQLPAEPKELISMIQVVKQKlpQKNSSEGNkhhkstPLLIHCRDGSQQTGIFCA---LLNLLES 1140
Cdd:cd14605   139 NTERTVWQYHFRTWPDHGVPSDPGGVLDFLEEVHHK--QESIMDAG------PVVVHCSAGIGRTGTFIVidiLIDIIRE 210

                         250       260       270
                  ....*....|....*....|....*....|....
gi 578801329 1141 AETEEVVDIFQVVKALRKARPGMVSTFEQYQFLY 1174
Cdd:cd14605   211 KGVDCDIDVPKTIQMVRSQRSGMVQTEAQYRFIY 244
PTPc-N1_2 cd14545
catalytic domain of tyrosine-protein phosphatase non-receptor type 1 and type 2; ...
 923-1174 3.15e-36

catalytic domain of tyrosine-protein phosphatase non-receptor type 1 and type 2; Tyrosine-protein phosphatase non-receptor type 1 (PTPN1) type 2 (PTPN2) belong to the family of classical tyrosine-specific protein tyrosine phosphatases, (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. PTPN1 (or PTP-1B) is the first PTP to be purified and characterized and is the prototypical intracellular PTP found in a wide variety of human tissues. It dephosphorylates and regulates the activity of a number of receptor tyrosine kinases, including the insulin receptor, the EGF receptor, and the PDGF receptor. PTPN2 (or TCPTP), a tumor suppressor, dephosphorylates and inactivates EGFRs, Src family kinases, Janus-activated kinases (JAKs)-1 and -3, and signal transducer and activators of transcription (STATs)-1, -3 and -5, in a cell type and context-dependent manner.


Pssm-ID: 350393 [Multi-domain]  Cd Length: 231  Bit Score: 137.14  E-value: 3.15e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578801329  923 KNRNSNVIPYDYNRVPLKHELEmskesehdsdessdddsdseePSKYINASFIMSYWKPEVMIAAQGPLKETIGDFWQMI 1002
Cdd:cd14545     1 LNRYRDRDPYDHDRSRVKLKQG---------------------DNDYINASLVEVEEAKRSYILTQGPLPNTSGHFWQMV 59

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578801329 1003 FQRKVKVIVMLTELKHGDQEICAQYWGEGKQTYGDIE-----VDLKDTDKSSTYTLRVFELRHSKRKDSRTVYQYQYTNW 1077
Cdd:cd14545    60 WEQNSKAVIMLNKLMEKGQIKCAQYWPQGEGNAMIFEdtglkVTLLSEEDKSYYTVRTLELENLKTQETREVLHFHYTTW 139

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578801329 1078 SVEQLPAEPKELISMIQVVKqklpQKNSSEGNKhhksTPLLIHCRDGSQQTGIFC---ALLNLLESAETEEvVDIFQVVK 1154
Cdd:cd14545   140 PDFGVPESPAAFLNFLQKVR----ESGSLSSDV----GPPVVHCSAGIGRSGTFClvdTCLVLIEKGNPSS-VDVKKVLL 210

                         250       260
                  ....*....|....*....|
gi 578801329 1155 ALRKARPGMVSTFEQYQFLY 1174
Cdd:cd14545   211 EMRKYRMGLIQTPDQLRFSY 230
R-PTPc-T-2 cd14634
PTP domain of receptor-type tyrosine-protein phosphatase T, repeat 2; Receptor-type ...
 969-1176 1.42e-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: 134.76  E-value: 1.42e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578801329  969 YINASFIMSYWKPEVMIAAQGPLKETIGDFWQMIFQRKVKVIVMLTELKHGdqEICAQYWGEGKQ-TYGDIEVDLKDTDK 1047
Cdd:cd14634     1 YINAALMDSHKQPAAFIVTQHPLPNTVADFWRLVFDYNCSSVVMLNEMDAA--QLCMQYWPEKTScCYGPIQVEFVSADI 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578801329 1048 SSTYTLRVFELRHSKRKDS--RTVYQYQYTNW-SVEQLPAEPKELISMIQVVKQKLPQKNSSEGNKhhkstplLIHCRDG 1124
Cdd:cd14634    79 DEDIISRIFRICNMARPQDgyRIVQHLQYIGWpAYRDTPPSKRSILKVVRRLEKWQEQYDGREGRT-------VVHCLNG 151

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 578801329 1125 SQQTGIFCALLNLLESAETEEVVDIFQVVKALRKARPGMVSTFEQYQFLYDV 1176
Cdd:cd14634   152 GGRSGTFCAICSVCEMIQQQNIIDVFHTVKTLRNNKSNMVETLEQYKFVYEV 203
PHA02747 PHA02747
protein tyrosine phosphatase; Provisional
 919-1173 5.94e-35

protein tyrosine phosphatase; Provisional


Pssm-ID: 165114 [Multi-domain]  Cd Length: 312  Bit Score: 136.28  E-value: 5.94e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578801329  919 ENKSKNRNSNVIPYDYNRVPLKhelemskesehdsdessdddSDSEEPSKYINASFIMSYWKPEVMIAAQGPLKETIGDF 998
Cdd:PHA02747   50 ENQPKNRYWDIPCWDHNRVILD--------------------SGGGSTSDYIHANWIDGFEDDKKFIATQGPFAETCADF 109

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578801329  999 WQMIFQRKVKVIVMLTELKHGD-QEICAQYWG---EGKQTYGDIEVDLKDTDKSSTYTLRVFELRHSKRKDSRTVYQYQY 1074
Cdd:PHA02747  110 WKAVWQEHCSIIVMLTPTKGTNgEEKCYQYWClneDGNIDMEDFRIETLKTSVRAKYILTLIEITDKILKDSRKISHFQC 189

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578801329 1075 TNWSVEQLPAEPKELISMIQVVKQKLPQKNSSEGNKHHKSTPLLIHCRDGSQQTGIFCALLNLLESAETEEVVDIFQVVK 1154
Cdd:PHA02747  190 SEWFEDETPSDHPDFIKFIKIIDINRKKSGKLFNPKDALLCPIVVHCSDGVGKTGIFCAVDICLNQLVKRKAICLAKTAE 269

                         250
                  ....*....|....*....
gi 578801329 1155 ALRKARPGMVSTFEQYQFL 1173
Cdd:PHA02747  270 KIREQRHAGIMNFDDYLFI 288
PHA02746 PHA02746
protein tyrosine phosphatase; Provisional
 917-1177 1.04e-34

protein tyrosine phosphatase; Provisional


Pssm-ID: 165113 [Multi-domain]  Cd Length: 323  Bit Score: 135.93  E-value: 1.04e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578801329  917 QEENKSKNRNSNVIPYDYNRVPLKHELEMSKESEHDSDESSDDDSDSEEPSKYINASFIMSYWKPEVMIAAQGPLKETIG 996
Cdd:PHA02746   48 KKENLKKNRFHDIPCWDHSRVVINAHESLKMFDVGDSDGKKIEVTSEDNAENYIHANFVDGFKEANKFICAQGPKEDTSE 127

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578801329  997 DFWQMIFQRKVKVIVMLTELKHgDQEICAQYWGEGKQ---TYGDIEVDLKDTDKSSTYTLRVFELRHSKRKDSRTVYQYQ 1073
Cdd:PHA02746  128 DFFKLISEHESQVIVSLTDIDD-DDEKCFELWTKEEDselAFGRFVAKILDIIEELSFTKTRLMITDKISDTSREIHHFW 206

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578801329 1074 YTNWSVEQLPAEPKELISMIQVVKQKLPQKNSSEGNKHHKSTPLLIHCRDGSQQTGIFCALLNLLESAETEEVVDIFQVV 1153
Cdd:PHA02746  207 FPDWPDNGIPTGMAEFLELINKVNEEQAELIKQADNDPQTLGPIVVHCSAGIGRAGTFCAIDNALEQLEKEKEVCLGEIV 286

                         250       260
                  ....*....|....*....|....
gi 578801329 1154 KALRKARPGMVSTFEQYQFLYDVI 1177
Cdd:PHA02746  287 LKIRKQRHSSVFLPEQYAFCYKAL 310
R-PTPc-K-2 cd14636
PTP domain of receptor-type tyrosine-protein phosphatase K, repeat 2; Receptor-type ...
 969-1176 3.07e-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: 130.92  E-value: 3.07e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578801329  969 YINASFIMSYWKPEVMIAAQGPLKETIGDFWQMIFQRKVKVIVMLTELKHgdQEICAQYW-GEGKQTYGDIEVDLKDTDK 1047
Cdd:cd14636     1 YINAALMDSYRQPAAFIVTQHPLPNTVKDFWRLVYDYGCTSIVMLNEVDL--AQGCPQYWpEEGMLRYGPIQVECMSCSM 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578801329 1048 SSTYTLRVFELRHSKRKDS--RTVYQYQYTNW-SVEQLPAEPKELISMIQVVKQKLPQKNSSEGNKhhkstplLIHCRDG 1124
Cdd:cd14636    79 DCDVISRIFRICNLTRPQEgyLMVQQFQYLGWaSHREVPGSKRSFLKLILQVEKWQEECDEGEGRT-------IIHCLNG 151

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 578801329 1125 SQQTGIFCALLNLLESAETEEVVDIFQVVKALRKARPGMVSTFEQYQFLYDV 1176
Cdd:cd14636   152 GGRSGMFCAISIVCEMIKRQNVVDVFHAVKTLRNSKPNMVETPEQYRFCYDV 203
R-PTPc-U-2 cd14637
PTP domain of receptor-type tyrosine-protein phosphatase U, repeat 2; Receptor-type ...
 969-1176 2.94e-33

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: 128.10  E-value: 2.94e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578801329  969 YINASFIMSYWKPEVMIAAQGPLKETIGDFWQMIFQRKVKVIVMLTELKHGDQEI-CAQYWGE-GKQTYGDIEVDLKDTD 1046
Cdd:cd14637     1 YINAALTDSYTRSAAFIVTLHPLQNTTTDFWRLVYDYGCTSVVMLNQLNQSNSAWpCLQYWPEpGLQQYGPMEVEFVSGS 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578801329 1047 KSSTYTLRVFELRHSKR--KDSRTVYQYQYTNWSV-EQLPAEPKELISMIQVVKQKlpQKNSSEGNKhhkstplLIHCRD 1123
Cdd:cd14637    81 ADEDIVTRLFRVQNITRlqEGHLMVRHFQFLRWSAyRDTPDSKKAFLHLLASVEKW--QRESGEGRT-------VVHCLN 151

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 578801329 1124 GSQQTGIFCALLNLLESAETEEVVDIFQVVKALRKARPGMVSTFEQYQFLYDV 1176
Cdd:cd14637   152 GGGRSGTYCASAMILEMIRCHNIVDVFYAVKTLRNYKPNMVETLEQYRFCYEI 204
PTPc_plant_PTP1 cd17658
protein tyrosine phosphatase 1 from Arabidopsis thaliana and similar plant PTPs; Arabidopsis ...
 969-1174 1.11e-32

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: 126.04  E-value: 1.11e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578801329  969 YINASFIMSYWKPEV--MIAAQGPLKETIGDFWQMIFQRKVKVIVMLTELKHGDQEI-CAQYW---GEGKQTYGDIEVDL 1042
Cdd:cd17658     1 YINASLVETPASESLpkFIATQGPLPHTFEDFWEMVIQQRCPVIIMLTRLVDNYSTAkCADYFpaeENESREFGRISVTN 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578801329 1043 KDTDKSST-YTLRVFELRHSKRKDS-RTVYQYQYTNWSVEQLPAEPKELISMIQVVKQKLPqknsSEGnkhhkstPLLIH 1120
Cdd:cd17658    81 KKLKHSQHsITLRVLEVQYIESEEPpLSVLHIQYPEWPDHGVPKDTRSVRELLKRLYGIPP----SAG-------PIVVH 149

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 578801329 1121 CRDGSQQTGIFCALLNLLES--AETEEVVDIFQVVKALRKARPGMVSTFEQYQFLY 1174
Cdd:cd17658   150 CSAGIGRTGAYCTIHNTIRRilEGDMSAVDLSKTVRKFRSQRIGMVQTQDQYIFCY 205
PTPc-N14 cd14599
catalytic domain of tyrosine-protein phosphatase non-receptor type 14; Tyrosine-protein ...
 899-1177 1.22e-32

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: 128.96  E-value: 1.22e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578801329  899 EFQRLPSYRSWRTQHIGNQEENKSKNRNSNVIPYDYNRVPLKHELEmskesehdsdessdddsdseEPSKYINASFIMSY 978
Cdd:cd14599    17 EYEQIPKKKADGVFTTATLPENAERNRIREVVPYEENRVELVPTKE--------------------NNTGYINASHIKVT 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578801329  979 WKPEV--MIAAQGPLKETIGDFWQMIFQRKVKVIVMLTELKHGDQEICAQYWGE-----GKQTYGDIEVDLKDTDKSSTY 1051
Cdd:cd14599    77 VGGEEwhYIATQGPLPHTCHDFWQMVWEQGVNVIAMVTAEEEGGRSKSHRYWPKlgskhSSATYGKFKVTTKFRTDSGCY 156

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578801329 1052 TLRVFELRHSKRKDSRTVYQYQYTNWSVEQLPAEPKELISMIQVVKQKLPQKNSSEGNKHHKSTPLLIHCRDGSQQTGIF 1131
Cdd:cd14599   157 ATTGLKVKHLLSGQERTVWHLQYTDWPDHGCPEEVQGFLSYLEEIQSVRRHTNSMLDSTKNCNPPIVVHCSAGVGRTGVV 236

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*.
gi 578801329 1132 CALLNLLESAETEEVVDIFQVVKALRKARPGMVSTFEQYQFLYDVI 1177
Cdd:cd14599   237 ILTELMIGCLEHNEKVEVPVMLRHLREQRMFMIQTIAQYKFVYQVL 282
PTPc-N2 cd14607
catalytic domain of tyrosine-protein phosphatase non-receptor type 2; Tyrosine-protein ...
 919-1174 2.39e-32

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: 127.00  E-value: 2.39e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578801329  919 ENKSKNRNSNVIPYDYNRVPLKHelemskesehdsdessdddsdseEPSKYINASFIMSYWKPEVMIAAQGPLKETIGDF 998
Cdd:cd14607    23 ENRNRNRYRDVSPYDHSRVKLQN-----------------------TENDYINASLVVIEEAQRSYILTQGPLPNTCCHF 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578801329  999 WQMIFQRKVKVIVMLTELKHGDQEICAQYW---GEGKQTYGD--IEVDLKDTDKSSTYTLRVFELRHSKRKDSRTVYQYQ 1073
Cdd:cd14607    80 WLMVWQQKTKAVVMLNRIVEKDSVKCAQYWptdEEEVLSFKEtgFSVKLLSEDVKSYYTVHLLQLENINSGETRTISHFH 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578801329 1074 YTNWSVEQLPAEPKELISMIQVVKQklpqknssEGNKHHKSTPLLIHCRDGSQQTGIFCAL---LNLLESAETEEvVDIF 1150
Cdd:cd14607   160 YTTWPDFGVPESPASFLNFLFKVRE--------SGSLSPEHGPAVVHCSAGIGRSGTFSLVdtcLVLMEKKDPDS-VDIK 230

                         250       260
                  ....*....|....*....|....
gi 578801329 1151 QVVKALRKARPGMVSTFEQYQFLY 1174
Cdd:cd14607   231 QVLLDMRKYRMGLIQTPDQLRFSY 254
PTPc-N1 cd14608
catalytic domain of tyrosine-protein phosphatase non-receptor type 1; Tyrosine-protein ...
 914-1174 6.45e-32

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: 126.29  E-value: 6.45e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578801329  914 IGNQEENKSKNRNSNVIPYDYNRVPLKHElemskesehdsdessdddsdseePSKYINASFIMSYWKPEVMIAAQGPLKE 993
Cdd:cd14608    19 VAKLPKNKNRNRYRDVSPFDHSRIKLHQE-----------------------DNDYINASLIKMEEAQRSYILTQGPLPN 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578801329  994 TIGDFWQMIFQRKVKVIVMLTELKHGDQEICAQYW--GEGKQTY---GDIEVDLKDTDKSSTYTLRVFELRHSKRKDSRT 1068
Cdd:cd14608    76 TCGHFWEMVWEQKSRGVVMLNRVMEKGSLKCAQYWpqKEEKEMIfedTNLKLTLISEDIKSYYTVRQLELENLTTQETRE 155

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578801329 1069 VYQYQYTNWSVEQLPAEPKELISMIQVVKQklpqknssEGNKHHKSTPLLIHCRDGSQQTGIFC---ALLNLLESAETEE 1145
Cdd:cd14608   156 ILHFHYTTWPDFGVPESPASFLNFLFKVRE--------SGSLSPEHGPVVVHCSAGIGRSGTFCladTCLLLMDKRKDPS 227

                         250       260
                  ....*....|....*....|....*....
gi 578801329 1146 VVDIFQVVKALRKARPGMVSTFEQYQFLY 1174
Cdd:cd14608   228 SVDIKKVLLEMRKFRMGLIQTADQLRFSY 256
R-PTPc-B cd14617
catalytic domain of receptor-type tyrosine-protein phosphatase B; Receptor-type ...
 924-1174 8.40e-32

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: 124.65  E-value: 8.40e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578801329  924 NRNSNVIPYDYNRVPLKHelemskesehdsdessdddSDSEEPSKYINASFIMSYWKPEVMIAAQGPLKETIGDFWQMIF 1003
Cdd:cd14617     1 NRYNNILPYDSTRVKLSN-------------------VDDDPCSDYINASYIPGNNFRREYIATQGPLPGTKDDFWKMVW 61

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578801329 1004 QRKVKVIVMLTELKHGDQEICAQYWGEGKQT--YGDIEVDLKDTDKSSTYTLRVFELRHSKRKDS-RTVYQYQYTNWSVE 1080
Cdd:cd14617    62 EQNVHNIVMVTQCVEKGRVKCDHYWPADQDSlyYGDLIVQMLSESVLPEWTIREFKICSEEQLDApRLVRHFHYTVWPDH 141

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578801329 1081 QLPAEPKELISMIQVVKQKLpqknssegNKHHKSTPLLIHCRDGSQQTGIFCALLNLLESAETEEVVDIFQVVKALRKAR 1160
Cdd:cd14617   142 GVPETTQSLIQFVRTVRDYI--------NRTPGSGPTVVHCSAGVGRTGTFIALDRILQQLDSKDSVDIYGAVHDLRLHR 213

                         250
                  ....*....|....
gi 578801329 1161 PGMVSTFEQYQFLY 1174
Cdd:cd14617   214 VHMVQTECQYVYLH 227
PTPc-N3_4 cd14541
catalytic domain of tyrosine-protein phosphatase non-receptor type 21 and type 14; ...
 969-1181 8.48e-32

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: 123.98  E-value: 8.48e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578801329  969 YINASFI-MSYWKPEVM---IAAQGPLKETIGDFWQMIFQRKVKVIVMLTELKHGDQEICAQYW--GEGKQTYGDIEVDL 1042
Cdd:cd14541     2 YINANYVnMEIPGSGIVnryIAAQGPLPNTCADFWQMVWEQKSTLIVMLTTLVERGRVKCHQYWpdLGETMQFGNLQITC 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578801329 1043 KDTDKSSTYTLRVFELRHSKRKDSRTVYQYQYTNWSVEQLPAEPKELISMIQVVKQklpqknssegNKHHKSTPLLIHCR 1122
Cdd:cd14541    82 VSEEVTPSFAFREFILTNTNTGEERHITQMQYLAWPDHGVPDDSSDFLDFVKRVRQ----------NRVGMVEPTVVHCS 151

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 578801329 1123 DGSQQTGIfcalLNLLESA----ETEEVVDIFQVVKALRKARPGMVSTFEQYQFLYDVIASTY 1181
Cdd:cd14541   152 AGIGRTGV----LITMETAmcliEANEPVYPLDIVRTMRDQRAMLIQTPSQYRFVCEAILRVY 210
PHA02742 PHA02742
protein tyrosine phosphatase; Provisional
 919-1174 1.13e-31

protein tyrosine phosphatase; Provisional


Pssm-ID: 165109 [Multi-domain]  Cd Length: 303  Bit Score: 126.27  E-value: 1.13e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578801329  919 ENKSKNRNSNVIPYDYNRVPLKHELEMSKesehdsdessdddsdseepskYINASFIMSYWKPEVMIAAQGPLKETIGDF 998
Cdd:PHA02742   51 KNMKKCRYPDAPCFDRNRVILKIEDGGDD---------------------FINASYVDGHNAKGRFICTQAPLEETALDF 109

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578801329  999 WQMIFQRKVKVIVMLTELKHGDQEICAQYWG---EGKQTYGDIEVDLKDTDKSSTYTLRVFELRHSKRKDSRTVYQYQYT 1075
Cdd:PHA02742  110 WQAIFQDQVRVIVMITKIMEDGKEACYPYWMpheRGKATHGEFKIKTKKIKSFRNYAVTNLCLTDTNTGASLDIKHFAYE 189

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578801329 1076 NWSVEQLPAEPKELISMIQVVKQ-KLPQKNSSEGNKHHKSTPLLIHCRDGSQQTGIFCALLNLLESAETEEVVDIFQVVK 1154
Cdd:PHA02742  190 DWPHGGLPRDPNKFLDFVLAVREaDLKADVDIKGENIVKEPPILVHCSAGLDRAGAFCAIDICISKYNERAIIPLLSIVR 269

                         250       260
                  ....*....|....*....|
gi 578801329 1155 ALRKARPGMVSTFEQYQFLY 1174
Cdd:PHA02742  270 DLRKQRHNCLSLPQQYIFCY 289
PTPc_motif smart00404
Protein tyrosine phosphatase, catalytic domain motif;
1068-1179 3.22e-31

Protein tyrosine phosphatase, catalytic domain motif;


Pssm-ID: 214649 [Multi-domain]  Cd Length: 105  Bit Score: 118.23  E-value: 3.22e-31
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578801329   1068 TVYQYQYTNWSVEQLPAEPKELISMIQVVKQKLPQKNSSegnkhhksTPLLIHCRDGSQQTGIFCALLNLLESAETE-EV 1146
Cdd:smart00404    1 TVKHYHYTGWPDHGVPESPDSILELLRAVKKNLNQSESS--------GPVVVHCSAGVGRTGTFVAIDILLQQLEAEaGE 72

                            90       100       110
                    ....*....|....*....|....*....|...
gi 578801329   1147 VDIFQVVKALRKARPGMVSTFEQYQFLYDVIAS 1179
Cdd:smart00404   73 VDIFDTVKELRSQRPGMVQTEEQYLFLYRALLE 105
PTPc_DSPc smart00012
Protein tyrosine phosphatase, catalytic domain, undefined specificity; Protein tyrosine ...
 1068-1179 3.22e-31

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: 118.23  E-value: 3.22e-31
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578801329   1068 TVYQYQYTNWSVEQLPAEPKELISMIQVVKQKLPQKNSSegnkhhksTPLLIHCRDGSQQTGIFCALLNLLESAETE-EV 1146
Cdd:smart00012    1 TVKHYHYTGWPDHGVPESPDSILELLRAVKKNLNQSESS--------GPVVVHCSAGVGRTGTFVAIDILLQQLEAEaGE 72

                            90       100       110
                    ....*....|....*....|....*....|...
gi 578801329   1147 VDIFQVVKALRKARPGMVSTFEQYQFLYDVIAS 1179
Cdd:smart00012   73 VDIFDTVKELRSQRPGMVQTEEQYLFLYRALLE 105
R-PTPc-M-2 cd14635
PTP domain of receptor-type tyrosine-protein phosphatase M, repeat 2; Receptor-type ...
 969-1176 5.11e-31

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: 121.33  E-value: 5.11e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578801329  969 YINASFIMSYWKPEVMIAAQGPLKETIGDFWQMIFQRKVKVIVMLTELKHGdqEICAQYWGE-GKQTYGDIEVDLKDTDK 1047
Cdd:cd14635     1 YINAALMDSYKQPSAFIVTQHPLPNTVKDFWRLVLDYHCTSIVMLNDVDPA--QLCPQYWPEnGVHRHGPIQVEFVSADL 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578801329 1048 SSTYTLRVFELRHSKRKDS--RTVYQYQYTNWSV-EQLPAEPKELISMIQVVKQKLPQKNSSEGNKhhkstplLIHCRDG 1124
Cdd:cd14635    79 EEDIISRIFRIYNAARPQDgyRMVQQFQFLGWPMyRDTPVSKRSFLKLIRQVDKWQEEYNGGEGRT-------VVHCLNG 151

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 578801329 1125 SQQTGIFCALLNLLESAETEEVVDIFQVVKALRKARPGMVSTFEQYQFLYDV 1176
Cdd:cd14635   152 GGRSGTFCAISIVCEMLRHQRAVDVFHAVKTLRNNKPNMVDLLDQYKFCYEV 203
PTPc-N3 cd14600
catalytic domain of tyrosine-protein phosphatase non-receptor type 3; Tyrosine-protein ...
 917-1181 1.04e-30

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: 122.65  E-value: 1.04e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578801329  917 QEENKSKNRNSNVIPYDYNRVPLKHElemskesehdsdessdddsdseepSKYINASFI-MSYWKPEVM---IAAQGPLK 992
Cdd:cd14600    37 LPQNMDKNRYKDVLPYDATRVVLQGN------------------------EDYINASYVnMEIPSANIVnkyIATQGPLP 92

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578801329  993 ETIGDFWQMIFQRKVKVIVMLTELKHGDQEICAQYWGEGKQT--YGDIEVDLKDTDKSSTYTLRVFELRHSKRKDSRTVY 1070
Cdd:cd14600    93 HTCAQFWQVVWEQKLSLIVMLTTLTERGRTKCHQYWPDPPDVmeYGGFRVQCHSEDCTIAYVFREMLLTNTQTGEERTVT 172

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578801329 1071 QYQYTNWSVEQLPAEPKELISMIQVVKQklpqknssegnKHHKSTPLLIHCRDGSQQTGIFCALLNLLESAETEEVVDIF 1150
Cdd:cd14600   173 HLQYVAWPDHGVPDDSSDFLEFVNYVRS-----------KRVENEPVLVHCSAGIGRTGVLVTMETAMCLTERNQPVYPL 241

                         250       260       270
                  ....*....|....*....|....*....|.
gi 578801329 1151 QVVKALRKARPGMVSTFEQYQFLYDVIASTY 1181
Cdd:cd14600   242 DIVRKMRDQRAMMVQTSSQYKFVCEAILRVY 272
PTPc-N21 cd14598
catalytic domain of tyrosine-protein phosphatase non-receptor type 21; Tyrosine-protein ...
 969-1177 1.11e-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: 120.85  E-value: 1.11e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578801329  969 YINASFIM-----SYWKpevMIAAQGPLKETIGDFWQMIFQRKVKVIVMLTELKHGDQEICAQYWG-----EGKQTYGDI 1038
Cdd:cd14598     1 YINASHIKvtvggKEWD---YIATQGPLQNTCQDFWQMVWEQGVAIIAMVTAEEEGGREKSFRYWPrlgsrHNTVTYGRF 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578801329 1039 EVDLKDTDKSSTYTLRVFELRHSKRKDSRTVYQYQYTNWSVEQLPAEPKELISMIQVVKQKLPQKNSSEGNKHHKStPLL 1118
Cdd:cd14598    78 KITTRFRTDSGCYATTGLKIKHLLTGQERTVWHLQYTDWPEHGCPEDLKGFLSYLEEIQSVRRHTNSTIDPKSPNP-PVL 156

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 578801329 1119 IHCRDGSQQTGIFCALLNLLESAETEEVVDIFQVVKALRKARPGMVSTFEQYQFLYDVI 1177
Cdd:cd14598   157 VHCSAGVGRTGVVILSEIMIACLEHNEMLDIPRVLDMLRQQRMMMVQTLSQYTFVYKVL 215
PTPc-N20 cd14596
catalytic domain of tyrosine-protein phosphatase non-receptor type 20; Tyrosine-protein ...
 969-1177 3.28e-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: 119.08  E-value: 3.28e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578801329  969 YINASFIMSYWKPE--VMIAAQGPLKETIGDFWQMIFQRKVKVIVMLTELKHGDQEICAQYWGEGKQTYGDIE---VDLK 1043
Cdd:cd14596     1 YINASYITMPVGEEelFYIATQGPLPSTIDDFWQMVWENRSDVIAMMTREVERGKVKCHRYWPETLQEPMELEnyqLRLE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578801329 1044 DTDKSSTYTLRVFELRHSKRKDSRTVYQYQYTNWSVEQLPAEPKELISMIQVVKqklpqknssegnKHHKSTPLLIHCRD 1123
Cdd:cd14596    81 NYQALQYFIIRIIKLVEKETGENRLIKHLQFTTWPDHGTPQSSDQLVKFICYMR------------KVHNTGPIVVHCSA 148

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....
gi 578801329 1124 GSQQTGIFCALLNLLESAETEEVVDIFQVVKALRKARPGMVSTFEQYQFLYDVI 1177
Cdd:cd14596   149 GIGRAGVLICVDVLLSLIEKDLSFNIKDIVREMRQQRYGMIQTKDQYLFCYKVV 202
COG5599 COG5599
Protein tyrosine phosphatase [Signal transduction mechanisms];
911-1179 4.28e-30

Protein tyrosine phosphatase [Signal transduction mechanisms];


Pssm-ID: 444335 [Multi-domain]  Cd Length: 282  Bit Score: 121.35  E-value: 4.28e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578801329  911 TQHIGNQEeNKSKNRNSNVIPYDYNRVplkhelemskesehdsdessdddsdsEEPSKYINASFIMSYwKPEVMIAAQGP 990
Cdd:COG5599    34 PQYLQNIN-GSPLNRFRDIQPYKETAL--------------------------RANLGYLNANYIQVI-GNHRYIATQYP 85

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578801329  991 LKETIGDFWQMIFQRKVKVIVMLTELKHGDQEI--CAQYWGEgKQTYGDIEVDLKDTDK---SSTYTLRVFEL-RHSKRK 1064
Cdd:COG5599    86 LEEQLEDFFQMLFDNNTPVLVVLASDDEISKPKvkMPVYFRQ-DGEYGKYEVSSELTESiqlRDGIEARTYVLtIKGTGQ 164

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578801329 1065 DSRTVYQYQYTNWSVEQLPAePKELISMIQVVKQKLPQKNSSEGnkhhkstPLLIHCRDGSQQTGIFCALLNLLES--AE 1142
Cdd:COG5599   165 KKIEIPVLHVKNWPDHGAIS-AEALKNLADLIDKKEKIKDPDKL-------LPVVHCRAGVGRTGTLIACLALSKSinAL 236

                         250       260       270
                  ....*....|....*....|....*....|....*...
gi 578801329 1143 TEEVVDIFQVVKALRKAR-PGMVSTFEQYQFLYDVIAS 1179
Cdd:COG5599   237 VQITLSVEEIVIDMRTSRnGGMVQTSEQLDVLVKLAEQ 274
R-PTPc-T-2 cd14634
PTP domain of receptor-type tyrosine-protein phosphatase T, repeat 2; Receptor-type ...
 659-863 5.66e-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: 5.66e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578801329  659 YINASYIDGFKEPRKYIAAQGPRDETVDDFWRMIWEQKATVIVMVTrcEEGNRNKCAEYWPsmEEGTRAFGDVVVKINQH 738
Cdd:cd14634     1 YINAALMDSHKQPAAFIVTQHPLPNTVADFWRLVFDYNCSSVVMLN--EMDAAQLCMQYWP--EKTSCCYGPIQVEFVSA 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578801329  739 KRCPDYIIQKLNIVNKKEKATG-REVTHIQFTSWPDH-GVPEDPHLLLKLRRRVNAFSNFF---SGPIVVHCSAGVGRTG 813
Cdd:cd14634    77 DIDEDIISRIFRICNMARPQDGyRIVQHLQYIGWPAYrDTPPSKRSILKVVRRLEKWQEQYdgrEGRTVVHCLNGGGRSG 156

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|
gi 578801329  814 TYIGIDAMLEGLEAENKVDVYGYVVKLRRQRCLMVQVEAQYILIHQALVE 863
Cdd:cd14634   157 TFCAICSVCEMIQQQNIIDVFHTVKTLRNNKSNMVETLEQYKFVYEVALE 206
CD45 pfam12567
Leukocyte receptor CD45; This family of proteins is found in eukaryotes. Proteins in this ...
 189-247 1.54e-29

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: 111.69  E-value: 1.54e-29
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 578801329   189 VDYLYNKETKLFTAKLNVNENVECGNNTCTNNEVHNLTECKNASVSISHNSCTAPDKTL 247
Cdd:pfam12567    1 VEYTYNSENKSFTAKLNVNDNVECENNDCENNELHNLQECEQINVSISHNSCTSPNKIL 59
PTPc-N4 cd14601
catalytic domain of tyrosine-protein phosphatase non-receptor type 4; Tyrosine-protein ...
 969-1181 4.45e-29

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: 116.20  E-value: 4.45e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578801329  969 YINASFI-MSYWKPEVM---IAAQGPLKETIGDFWQMIFQRKVKVIVMLTELKHGDQEICAQYWGE--GKQTYGDIEVDL 1042
Cdd:cd14601     2 YINANYInMEIPSSSIInryIACQGPLPNTCSDFWQMTWEQGSSMVVMLTTQVERGRVKCHQYWPEpsGSSSYGGFQVTC 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578801329 1043 KDTDKSSTYTLRVFELRHSKRKDSRTVYQYQYTNWSVEQLPAEPKELISMIQVVKQKlpqknssegnKHHKSTPLLIHCR 1122
Cdd:cd14601    82 HSEEGNPAYVFREMTLTNLEKNESRPLTQIQYIAWPDHGVPDDSSDFLDFVCLVRNK----------RAGKDEPVVVHCS 151

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 578801329 1123 DGSQQTGIFCALLNLLESAETEEVVDIFQVVKALRKARPGMVSTFEQYQFLYDVIASTY 1181
Cdd:cd14601   152 AGIGRTGVLITMETAMCLIECNQPVYPLDIVRTMRDQRAMMIQTPSQYRFVCEAILKVY 210
R5-PTP-2 cd14550
PTP-like domain of R5 subfamily receptor-type tyrosine-protein phosphatases, repeat 2; The R5 ...
 969-1174 8.49e-29

PTP-like domain of R5 subfamily receptor-type tyrosine-protein phosphatases, repeat 2; The R5 subfamily of receptor-type phosphotyrosine phosphatases (RPTP) is composed of receptor-type tyrosine-protein phosphatase Z (PTPRZ) and G (PTPRG). They belong to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. They are type 1 integral membrane proteins consisting of an extracellular region with a carbonic anhydrase-like (CAH) and a fibronectin type III (FN3) domains, and an intracellular region with a catalytic PTP domain (repeat 1) proximal to the membrane, and a catalytically inactive PTP-fold domain (repeat 2) distal to the membrane. This model represents the inactive PTP-like domain (repeat 2).


Pssm-ID: 350398 [Multi-domain]  Cd Length: 200  Bit Score: 114.73  E-value: 8.49e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578801329  969 YINASFIMSYWKPEVMIAAQGPLKETIGDFWQMIFQRKVKVIVMLTELkHGDQEiCAQYWGEGKQT--YGDIEVDLKDTD 1046
Cdd:cd14550     1 YINASYLQGYRRSNEFIITQHPLEHTIKDFWQMIWDHNSQTIVMLTDN-ELNED-EPIYWPTKEKPleCETFKVTLSGED 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578801329 1047 KSST-----YTLRVFELRHSKRKDSRTVYQYQYTNWSVEQLPAEPK-ELISMIQvvkqklpqknssegnKHHKST--PLL 1118
Cdd:cd14550    79 HSCLsneirLIVRDFILESTQDDYVLEVRQFQCPSWPNPCSPIHTVfELINTVQ---------------EWAQQRdgPIV 143

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 578801329 1119 IHCRDGSQQTGIFCALLNLLESAETEEVVDIFQVVKALRKARPGMVSTFEQYQFLY 1174
Cdd:cd14550   144 VHDRYGGVQAATFCALTTLHQQLEHESSVDVYQVAKLYHLMRPGVFTSKEDYQFLY 199
R5-PTP-2 cd14550
PTP-like domain of R5 subfamily receptor-type tyrosine-protein phosphatases, repeat 2; The R5 ...
 659-845 2.80e-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: 113.18  E-value: 2.80e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578801329  659 YINASYIDGFKEPRKYIAAQGPRDETVDDFWRMIWEQKATVIVMVTRCEEgnRNKCAEYWPSMEEGTRAFGDVVVKINQH 738
Cdd:cd14550     1 YINASYLQGYRRSNEFIITQHPLEHTIKDFWQMIWDHNSQTIVMLTDNEL--NEDEPIYWPTKEKPLECETFKVTLSGED 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578801329  739 KRC----PDYIIQKLNIVNKKEKATgREVTHIQFTSWPDHGVPedPHLLLKLRRRVNAFSNFFSGPIVVHCSAGVGRTGT 814
Cdd:cd14550    79 HSClsneIRLIVRDFILESTQDDYV-LEVRQFQCPSWPNPCSP--IHTVFELINTVQEWAQQRDGPIVVHDRYGGVQAAT 155

                         170       180       190
                  ....*....|....*....|....*....|...
gi 578801329  815 YIGIDAMLEGLEAENKVDVYGYVV--KLRRQRC 845
Cdd:cd14550   156 FCALTTLHQQLEHESSVDVYQVAKlyHLMRPGV 188
R-PTP-Z-2 cd17669
catalytic domain of receptor-type tyrosine-protein phosphatase Z, repeat 2; Receptor-type ...
 969-1177 4.70e-27

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: 110.08  E-value: 4.70e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578801329  969 YINASFIMSYWKPEVMIAAQGPLKETIGDFWQMIFQRKVKVIVMLTELKHGDQEICAqYWGEGKQ-------TYGDIEVD 1041
Cdd:cd17669     1 YINASYIMGYYQSNEFIITQHPLLHTIKDFWRMIWDHNAQLIVMLPDGQNMAEDEFV-YWPNKDEpincetfKVTLIAEE 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578801329 1042 LKDTDKSSTYTLRVFELRHSKRKDSRTVYQYQYTNWSVEQLP-AEPKELISMIqvvKQKLPQKNSsegnkhhkstPLLIH 1120
Cdd:cd17669    80 HKCLSNEEKLIIQDFILEATQDDYVLEVRHFQCPKWPNPDSPiSKTFELISII---KEEAANRDG----------PMIVH 146

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 578801329 1121 CRDGSQQTGIFCALLNLLESAETEEVVDIFQVVKALRKARPGMVSTFEQYQFLYDVI 1177
Cdd:cd17669   147 DEHGGVTAGTFCALTTLMHQLEKENSVDVYQVAKMINLMRPGVFTDIEQYQFLYKAI 203
R-PTPc-M-2 cd14635
PTP domain of receptor-type tyrosine-protein phosphatase M, repeat 2; Receptor-type ...
 659-863 3.89e-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: 107.47  E-value: 3.89e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578801329  659 YINASYIDGFKEPRKYIAAQGPRDETVDDFWRMIWEQKATVIVMVTRCEEGNRnkCAEYWPsmEEGTRAFGDVVVKINQH 738
Cdd:cd14635     1 YINAALMDSYKQPSAFIVTQHPLPNTVKDFWRLVLDYHCTSIVMLNDVDPAQL--CPQYWP--ENGVHRHGPIQVEFVSA 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578801329  739 KRCPDYIIQKLNIVNKKEKATG-REVTHIQFTSWPDH-GVPEDPHLLLKLRRRVNAFSNFF---SGPIVVHCSAGVGRTG 813
Cdd:cd14635    77 DLEEDIISRIFRIYNAARPQDGyRMVQQFQFLGWPMYrDTPVSKRSFLKLIRQVDKWQEEYnggEGRTVVHCLNGGGRSG 156

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|
gi 578801329  814 TYIGIDAMLEGLEAENKVDVYGYVVKLRRQRCLMVQVEAQYILIHQALVE 863
Cdd:cd14635   157 TFCAISIVCEMLRHQRAVDVFHAVKTLRNNKPNMVDLLDQYKFCYEVALE 206
R-PTP-G-2 cd17670
PTP-like domain of receptor-type tyrosine-protein phosphatase G, repeat 2; Receptor-type ...
 969-1179 1.54e-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: 105.53  E-value: 1.54e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578801329  969 YINASFIMSYWKPEVMIAAQGPLKETIGDFWQMIFQRKVKVIVMLTElKHGDQEICAQYWGEGKQTYG--DIEVDLKDTD 1046
Cdd:cd17670     1 YINASYIMGYYRSNEFIITQHPLPHTTKDFWRMIWDHNAQIIVMLPD-NQGLAEDEFVYWPSREESMNceAFTVTLISKD 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578801329 1047 K-----SSTYTLRVFELRHSKRKDSRTVYQYQYTNWSVEQLPAEpkELISMIQVVKQKLPQKNSsegnkhhkstPLLIHC 1121
Cdd:cd17670    80 RlclsnEEQIIIHDFILEATQDDYVLEVRHFQCPKWPNPDAPIS--STFELINVIKEEALTRDG----------PTIVHD 147

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 578801329 1122 RDGSQQTGIFCALLNLLESAETEEVVDIFQVVKALRKARPGMVSTFEQYQFLYDVIAS 1179
Cdd:cd17670   148 EFGAVSAGTLCALTTLSQQLENENAVDVYQVAKMINLMRPGVFTDIEQYQFLYKAMLS 205
R-PTP-Z-2 cd17669
catalytic domain of receptor-type tyrosine-protein phosphatase Z, repeat 2; Receptor-type ...
 659-862 2.98e-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: 101.99  E-value: 2.98e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578801329  659 YINASYIDGFKEPRKYIAAQGPRDETVDDFWRMIWEQKATVIVMVTRCEEGNRNKCAeYWPSMEEGTRAFGDVVVKINQH 738
Cdd:cd17669     1 YINASYIMGYYQSNEFIITQHPLLHTIKDFWRMIWDHNAQLIVMLPDGQNMAEDEFV-YWPNKDEPINCETFKVTLIAEE 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578801329  739 KRC----PDYIIQKLnIVNKKEKATGREVTHIQFTSWPDhgvPEDP-HLLLKLRRRVNAFSNFFSGPIVVHCSAGVGRTG 813
Cdd:cd17669    80 HKClsneEKLIIQDF-ILEATQDDYVLEVRHFQCPKWPN---PDSPiSKTFELISIIKEEAANRDGPMIVHDEHGGVTAG 155

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*....
gi 578801329  814 TYIGIDAMLEGLEAENKVDVYGYVVKLRRQRCLMVQVEAQYILIHQALV 862
Cdd:cd17669   156 TFCALTTLMHQLEKENSVDVYQVAKMINLMRPGVFTDIEQYQFLYKAIL 204
R-PTPc-K-2 cd14636
PTP domain of receptor-type tyrosine-protein phosphatase K, repeat 2; Receptor-type ...
 659-863 5.62e-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: 5.62e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578801329  659 YINASYIDGFKEPRKYIAAQGPRDETVDDFWRMIWEQKATVIVMVTRCEEGnrNKCAEYWPsmEEGTRAFGDVVVKINQH 738
Cdd:cd14636     1 YINAALMDSYRQPAAFIVTQHPLPNTVKDFWRLVYDYGCTSIVMLNEVDLA--QGCPQYWP--EEGMLRYGPIQVECMSC 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578801329  739 KRCPDYIIQKLNIVNKKEKATGR-EVTHIQFTSWPDH-GVPEDPHLLLKLRRRVNAFS---NFFSGPIVVHCSAGVGRTG 813
Cdd:cd14636    77 SMDCDVISRIFRICNLTRPQEGYlMVQQFQYLGWASHrEVPGSKRSFLKLILQVEKWQeecDEGEGRTIIHCLNGGGRSG 156

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|
gi 578801329  814 TYIGIDAMLEGLEAENKVDVYGYVVKLRRQRCLMVQVEAQYILIHQALVE 863
Cdd:cd14636   157 MFCAISIVCEMIKRQNVVDVFHAVKTLRNSKPNMVETPEQYRFCYDVALE 206
R-PTP-G-2 cd17670
PTP-like domain of receptor-type tyrosine-protein phosphatase G, repeat 2; Receptor-type ...
 659-862 1.15e-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: 1.15e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578801329  659 YINASYIDGFKEPRKYIAAQGPRDETVDDFWRMIWEQKATVIVMVTRcEEGNRNKCAEYWPSMEEGTRAFGDVVVKINQH 738
Cdd:cd17670     1 YINASYIMGYYRSNEFIITQHPLPHTTKDFWRMIWDHNAQIIVMLPD-NQGLAEDEFVYWPSREESMNCEAFTVTLISKD 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578801329  739 KRC---PDYIIQKLNIVNKKEKATGREVTHIQFTSWPDHGVPEDPHLLLKLRRRVNAFSNffSGPIVVHCSAGVGRTGTY 815
Cdd:cd17670    80 RLClsnEEQIIIHDFILEATQDDYVLEVRHFQCPKWPNPDAPISSTFELINVIKEEALTR--DGPTIVHDEFGAVSAGTL 157

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*..
gi 578801329  816 IGIDAMLEGLEAENKVDVYGYVVKLRRQRCLMVQVEAQYILIHQALV 862
Cdd:cd17670   158 CALTTLSQQLENENAVDVYQVAKMINLMRPGVFTDIEQYQFLYKAML 204
PHA02738 PHA02738
hypothetical protein; Provisional
 917-1177 1.31e-22

hypothetical protein; Provisional


Pssm-ID: 222923 [Multi-domain]  Cd Length: 320  Bit Score: 100.38  E-value: 1.31e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578801329  917 QEENKSKNRNSNVIPYDYNRVPLKHElemskesehdsdessdddsdsEEPSKYINASFIMSYWKPEVMIAAQGPLKETIG 996
Cdd:PHA02738   46 EKKNRKLNRYLDAVCFDHSRVILPAE---------------------RNRGDYINANYVDGFEYKKKFICGQAPTRQTCY 104

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578801329  997 DFWQMIFQRKVKVIVMLTELKHGDQEICAQYWGEGKQT---YGDIEVDLKDTDKSSTYTLRVFELRHSKRKdSRTVYQYQ 1073
Cdd:PHA02738  105 DFYRMLWMEHVQIIVMLCKKKENGREKCFPYWSDVEQGsirFGKFKITTTQVETHPHYVKSTLLLTDGTSA-TQTVTHFN 183

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578801329 1074 YTNWSVEQLPAEPKELISMIQVVKQ---KLPQKNSSEGNKHHKSTPLLIHCRDGSQQTGIFCALLNLLESAETEEVVDIF 1150
Cdd:PHA02738  184 FTAWPDHDVPKNTSEFLNFVLEVRQcqkELAQESLQIGHNRLQPPPIVVHCNAGLGRTPCYCVVDISISRFDACATVSIP 263

                         250       260
                  ....*....|....*....|....*..
gi 578801329 1151 QVVKALRKARPGMVSTFEQYQFLYDVI 1177
Cdd:PHA02738  264 SIVSSIRNQRYYSLFIPFQYFFCYRAV 290
R-PTPc-U-2 cd14637
PTP domain of receptor-type tyrosine-protein phosphatase U, repeat 2; Receptor-type ...
 659-863 1.25e-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: 88.81  E-value: 1.25e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578801329  659 YINASYIDGFKEPRKYIAAQGPRDETVDDFWRMIWEQKATVIVMVTRCEEGNRN-KCAEYWPsmEEGTRAFGDVVVKINQ 737
Cdd:cd14637     1 YINAALTDSYTRSAAFIVTLHPLQNTTTDFWRLVYDYGCTSVVMLNQLNQSNSAwPCLQYWP--EPGLQQYGPMEVEFVS 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578801329  738 HKRCPDYIIQKLNIVNKKEKATGR-EVTHIQFTSW-PDHGVPEDPHLLLKLRRRVNAF-SNFFSGPIVVHCSAGVGRTGT 814
Cdd:cd14637    79 GSADEDIVTRLFRVQNITRLQEGHlMVRHFQFLRWsAYRDTPDSKKAFLHLLASVEKWqRESGEGRTVVHCLNGGGRSGT 158

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*....
gi 578801329  815 YIGIDAMLEGLEAENKVDVYGYVVKLRRQRCLMVQVEAQYILIHQALVE 863
Cdd:cd14637   159 YCASAMILEMIRCHNIVDVFYAVKTLRNYKPNMVETLEQYRFCYEIALE 207
PHA02740 PHA02740
protein tyrosine phosphatase; Provisional
 623-864 8.68e-18

protein tyrosine phosphatase; Provisional


Pssm-ID: 165107 [Multi-domain]  Cd Length: 298  Bit Score: 85.40  E-value: 8.68e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578801329  623 EARKPFNQNKNRYVD-ILPYDYNRVELSEINGDAGSNYINASYIDGFKEPRKYIAAQGPRDETVDDFWRMIWEQKATVIV 701
Cdd:PHA02740   41 EANKACAQAENKAKDeNLALHITRLLHRRIKLFNDEKVLDARFVDGYDFEQKFICIINLCEDACDKFLQALSDNKVQIIV 120

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578801329  702 MVTRCEEgnRNKCAEYWPSMEEGTRAFGDVVVKINQHKRCPDYIIQKLNIVNKKEKAtgREVTHIQFTSWPDHGVPEDPH 781
Cdd:PHA02740  121 LISRHAD--KKCFNQFWSLKEGCVITSDKFQIETLEIIIKPHFNLTLLSLTDKFGQA--QKISHFQYTAWPADGFSHDPD 196

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578801329  782 -----------LLLKLRRRvNAFSNFfsGPIVVHCSAGVGRTGTYIGIDAMLEGLEAENKVDVYGYVVKLRRQRCLMVQV 850
Cdd:PHA02740  197 afidffcniddLCADLEKH-KADGKI--APIIIDCIDGISSSAVFCVFDICATEFDKTGMLSIANALKKVRQKKYGCMNC 273

                         250
                  ....*....|....
gi 578801329  851 EAQYILIHQALVEY 864
Cdd:PHA02740  274 LDDYVFCYHLIAAY 287
PTP_YopH-like cd14559
YopH and related bacterial protein tyrosine phosphatases; Yersinia outer protein H (YopH) ...
 660-854 9.40e-13

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: 68.97  E-value: 9.40e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578801329  660 INASYIDgFKEPRKYIAAQGPRDETVDDFWRMIWEQKATVIVMVTRCEEGNRNKCAEYWpsmeEGTRAFGDVVVKINQHK 739
Cdd:cd14559    18 LNANRVQ-IGNKNVAIACQYPKNEQLEDHLKMLADNRTPCLVVLASNKDIQRKGLPPYF----RQSGTYGSVTVKSKKTG 92

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578801329  740 rcPDYIIQKLNI------VNKKEKATGREVTHIqfTSWPDHGvPEDPHLLLKLRRRVN----------------AFSNFF 797
Cdd:cd14559    93 --KDELVDGLKAdmynlkITDGNKTITIPVVHV--TNWPDHT-AISSEGLKELADLVNksaeekrnfykskgssAINDKN 167

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 578801329  798 SGPIVVHCSAGVGRTGTYIgidAMLEGLEAENKVDVYGYVVKLRRQRC-LMVQVEAQY 854
Cdd:cd14559   168 KLLPVIHCRAGVGRTGQLA---AAMELNKSPNNLSVEDIVSDMRTSRNgKMVQKDEQL 222
PTP_YopH-like cd14559
YopH and related bacterial protein tyrosine phosphatases; Yersinia outer protein H (YopH) ...
 982-1173 3.35e-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: 67.42  E-value: 3.35e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578801329  982 EVMIAAQGPLKETIGDFWQMIFQRKVKVIVMLTElkhgDQEICA----QYWGEGKqTYGDIEV--------DLKDTDKSS 1049
Cdd:cd14559    29 NVAIACQYPKNEQLEDHLKMLADNRTPCLVVLAS----NKDIQRkglpPYFRQSG-TYGSVTVkskktgkdELVDGLKAD 103

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578801329 1050 TYTLRvfeLRHSKRKDSRTVYQYqyTNW------SVEQLpaepKELISMIQVVKQK----LPQKNSSEGNKHHKSTPLlI 1119
Cdd:cd14559   104 MYNLK---ITDGNKTITIPVVHV--TNWpdhtaiSSEGL----KELADLVNKSAEEkrnfYKSKGSSAINDKNKLLPV-I 173

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 578801329 1120 HCRDGSQQTGIFCALLNLLESAETEEVVDIfqvVKALRKARPG-MVSTFEQYQFL 1173
Cdd:cd14559   174 HCRAGVGRTGQLAAAMELNKSPNNLSVEDI---VSDMRTSRNGkMVQKDEQLDTL 225
PHA02740 PHA02740
protein tyrosine phosphatase; Provisional
 968-1178 6.33e-12

protein tyrosine phosphatase; Provisional


Pssm-ID: 165107 [Multi-domain]  Cd Length: 298  Bit Score: 68.07  E-value: 6.33e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578801329  968 KYINASFIMSYWKPEVMIAAQGPLKETIGDFWQMIFQRKVKVIVMLTelKHGDQEICAQYWGEGKQTygdievdLKDTDK 1047
Cdd:PHA02740   77 KVLDARFVDGYDFEQKFICIINLCEDACDKFLQALSDNKVQIIVLIS--RHADKKCFNQFWSLKEGC-------VITSDK 147

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578801329 1048 SSTYTLRVFELRH---------SKRKDSRTVYQYQYTNWSVEQLPAEPKELISMIQVVKQKLPQKNSSEGNKhhKSTPLL 1118
Cdd:PHA02740  148 FQIETLEIIIKPHfnltllsltDKFGQAQKISHFQYTAWPADGFSHDPDAFIDFFCNIDDLCADLEKHKADG--KIAPII 225

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 578801329 1119 IHCRDGSQQTGIFCALLNLLESAETEEVVDIFQVVKALRKARPGMVSTFEQYQFLYDVIA 1178
Cdd:PHA02740  226 IDCIDGISSSAVFCVFDICATEFDKTGMLSIANALKKVRQKKYGCMNCLDDYVFCYHLIA 285
PHA03255 PHA03255
BDLF3; Provisional
 18-183 2.53e-10

BDLF3; Provisional


Pssm-ID: 165513 [Multi-domain]  Cd Length: 234  Bit Score: 62.23  E-value: 2.53e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578801329   18 DTEVFVTGQSPTP-SPTGLTTAKMPSVPLSSDPLP------THTTAFSPAstferendfseTTTSLSPDNTSTQVSPDSl 90
Cdd:PHA03255   19 ETSLIWTSSGSSTaSAGNVTGTTAVTTPSPSASGPstnqstTLTTTSAPI-----------TTTAILSTNTTTVTSTGT- 86

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578801329   91 dNASAFNTTgvSSVQTPHLPTHADSQT---PSAGTDTQTFSGSaanaklNPTPGSNAISDAYLNASETTTLSPSGSAVIS 167
Cdd:PHA03255   87 -TVTPVPTT--SNASTINVTTKVTAQNitaTEAGTGTSTGVTS------NVTTRSSSTTSATTRITNATTLAPTLSSKGT 157

                         170
                  ....*....|....*..
gi 578801329  168 TTTIATTPSKPTC-DEK 183
Cdd:PHA03255  158 SNATKTTAELPTVpDER 174
PTP_N pfam12453
Protein tyrosine phosphatase N terminal; This domain family is found in eukaryotes, and is ...
 7-32 2.55e-10

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: 56.40  E-value: 2.55e-10
                           10        20
                   ....*....|....*....|....*.
gi 578801329     7 LKLLAFGFAFLDTEVFVTGQSPTPSP 32
Cdd:pfam12453    1 LKLLAFGFAFLDTEVFVTGESLTSST 26
FN3 cd00063
Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein ...
 437-517 1.96e-09

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: 55.97  E-value: 1.96e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578801329  437 PSQVWNMTVSMTSDNSMHVKCRPPRDRNGPHERYHLEVEAGN----TLVRNESHKNCDFRVKDLQYSTDYTFKAYFHNGD 512
Cdd:cd00063     1 PSPPTNLRVTDVTSTSVTLSWTPPEDDGGPITGYVVEYREKGsgdwKEVEVTPGSETSYTLTGLKPGTEYEFRVRAVNGG 80


                  ....*
gi 578801329  513 YPGEP 517
Cdd:cd00063    81 GESPP 85
CDC14 COG2453
Protein-tyrosine phosphatase [Signal transduction mechanisms];
771-859 5.48e-07

Protein-tyrosine phosphatase [Signal transduction mechanisms];


Pssm-ID: 441989 [Multi-domain]  Cd Length: 140  Bit Score: 50.35  E-value: 5.48e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578801329  771 WPDHGVPEDPHL---LLKLRRRVNAfsnffSGPIVVHCSAGVGRTGTYIGIDAMLEGLEAENKVDvygyvvKLRRQRCLM 847
Cdd:COG2453    55 IPDFGAPDDEQLqeaVDFIDEALRE-----GKKVLVHCRGGIGRTGTVAAAYLVLLGLSAEEALA------RVRAARPGA 123

                          90
                  ....*....|..
gi 578801329  848 VQVEAQYILIHQ 859
Cdd:COG2453   124 VETPAQRAFLER 135
fn3 pfam00041
Fibronectin type III domain;
438-517 1.98e-06

Fibronectin type III domain;


Pssm-ID: 394996 [Multi-domain]  Cd Length: 85  Bit Score: 47.02  E-value: 1.98e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578801329   438 SQVWNMTVSMTSDNSMHVKCRPPRDRNGPHERYHLEVEAGN--------TLVRNESHkncdFRVKDLQYSTDYTFKAYFH 509
Cdd:pfam00041    1 SAPSNLTVTDVTSTSLTVSWTPPPDGNGPITGYEVEYRPKNsgepwneiTVPGTTTS----VTLTGLKPGTEYEVRVQAV 76


                   ....*...
gi 578801329   510 NGDYPGEP 517
Cdd:pfam00041   77 NGGGEGPP 84
Chi1 COG3469
Chitinase [Carbohydrate transport and metabolism];
10-179 2.64e-06

Chitinase [Carbohydrate transport and metabolism];


Pssm-ID: 442692 [Multi-domain]  Cd Length: 534  Bit Score: 51.68  E-value: 2.64e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578801329   10 LAFGFAFLDTEVFVTGQSPTPSPTGLTTAKMPSVPLSSDPLPTHTTAFSPASTferendfseTTTSLSPDNTSTQVSPDS 89
Cdd:COG3469    49 VVVAASGSAGSGTGTTAASSTAATSSTTSTTATATAAAAAATSTSATLVATST---------ASGANTGTSTVTTTSTGA 119

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578801329   90 LDNASAFNTTGVSSVQTPHLPTHADSQTPSAGTDTQTFSGSAANAKLNPTPGSNAISDAYLNASETTTLSPSGSAVISTT 169
Cdd:COG3469   120 GSVTSTTSSTAGSTTTSGASATSSAGSTTTTTTVSGTETATGGTTTTSTTTTTTSASTTPSATTTATATTASGATTPSAT 199

                         170
                  ....*....|
gi 578801329  170 TIATTPSKPT 179
Cdd:COG3469   200 TTATTTGPPT 209
CDKN3-like cd14505
cyclin-dependent kinase inhibitor 3 and similar proteins; This family is composed of ...
 1117-1175 2.89e-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: 48.80  E-value: 2.89e-06
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 578801329 1117 LLIHCRDGSQQTGIFCA--LLNLLESAETEevvdifQVVKALRKARPGMVSTFEQYQFLYD 1175
Cdd:cd14505   109 VLIHCKGGLGRTGLIAAclLLELGDTLDPE------QAIAAVRALRPGAIQTPKQENFLHQ 163
Herpes_BLLF1 pfam05109
Herpes virus major outer envelope glycoprotein (BLLF1); This family consists of the BLLF1 ...
 27-199 2.38e-05

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: 48.76  E-value: 2.38e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578801329    27 SPTPSPTGLTTAKMPSVPLSSDPlPTHTTAfspASTFERENDFSETTTSLS--PDNTSTQVSPDSLDNASAF-------- 96
Cdd:pfam05109  599 SPQANTTNHTLGGTSSTPVVTSP-PKNATS---AVTTGQHNITSSSTSSMSlrPSSISETLSPSTSDNSTSHmplltsah 674

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578801329    97 -----NTTGVS--SVQTPHLPThaDSQTPSAGTDTQtfSGSAANAKLNPTPGSNAISDAYLNASETTTLSPSG--SAVIS 167
Cdd:pfam05109  675 ptggeNITQVTpaSTSTHHVST--SSPAPRPGTTSQ--ASGPGNSSTSTKPGEVNVTKGTPPKNATSPQAPSGqkTAVPT 750

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*....
gi 578801329   168 TTTI-----------------ATTPSKPTCDEKYANITVDYLYNKETKL 199
Cdd:pfam05109  751 VTSTggkansttggkhttghgARTSTEPTTDYGGDSTTPRTRYNATTYL 799
fn3 pfam00041
Fibronectin type III domain;
345-414 4.61e-05

Fibronectin type III domain;


Pssm-ID: 394996 [Multi-domain]  Cd Length: 85  Bit Score: 43.17  E-value: 4.61e-05
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 578801329   345 GEPQIIFCRSEAAHQGVITWNPP---QRSFHNFTLCYIKETEKDC---LNLDKNLIKYDLQNLKPYTKYVLSLHAY 414
Cdd:pfam00041    1 SAPSNLTVTDVTSTSLTVSWTPPpdgNGPITGYEVEYRPKNSGEPwneITVPGTTTSVTLTGLKPGTEYEVRVQAV 76
FN3 smart00060
Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, ...
 437-512 8.20e-05

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


Pssm-ID: 214495 [Multi-domain]  Cd Length: 83  Bit Score: 42.22  E-value: 8.20e-05
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578801329    437 PSQVWNMTVSMTSDNSMHVKCRPPRDRNGPHERYHLEVE----AGNTLVRNESHKNCDFRVKDLQYSTDYTFK--AYFHN 510
Cdd:smart00060    1 PSPPSNLRVTDVTSTSVTLSWEPPPDDGITGYIVGYRVEyreeGSEWKEVNVTPSSTSYTLTGLKPGTEYEFRvrAVNGA 80


                    ..
gi 578801329    511 GD 512
Cdd:smart00060   81 GE 82
FN3 cd00063
Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein ...
 344-414 8.75e-05

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


Pssm-ID: 238020 [Multi-domain]  Cd Length: 93  Bit Score: 42.48  E-value: 8.75e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 578801329  344 PGEPQIIFCRSEAAHQGVITWNPPQRS---FHNFTLCYIKETEKDCLNLDKNLIK---YDLQNLKPYTKYVLSLHAY 414
Cdd:cd00063     1 PSPPTNLRVTDVTSTSVTLSWTPPEDDggpITGYVVEYREKGSGDWKEVEVTPGSetsYTLTGLKPGTEYEFRVRAV 77
PTP_DSP_cys cd14494
cys-based protein tyrosine phosphatase and dual-specificity phosphatase superfamily; This ...
 799-844 1.42e-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: 1.42e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*.
gi 578801329  799 GPIVVHCSAGVGRTGTYIGIDAMLEGleaenKVDVYGYVVKLRRQR 844
Cdd:cd14494    57 EPVLVHCKAGVGRTGTLVACYLVLLG-----GMSAEEAVRIVRLIR 97
Chi1 COG3469
Chitinase [Carbohydrate transport and metabolism];
24-180 2.33e-04

Chitinase [Carbohydrate transport and metabolism];


Pssm-ID: 442692 [Multi-domain]  Cd Length: 534  Bit Score: 45.51  E-value: 2.33e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578801329   24 TGQSPTPSPTGLTTAKMPSVPLSSDPLPTHTTAFSPASTFER---ENDFSETTTSLSPDNTSTQVSPDSLDNASAFNTTG 100
Cdd:COG3469    12 AGGASATAVTLLGAAATAASVTLTAATATTVVSTTGSVVVAAsgsAGSGTGTTAASSTAATSSTTSTTATATAAAAAATS 91

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578801329  101 VSSVQTPHLPTHADSQTPSAGTDTQTFSGSAANAKLNPTPGSNAISDAYLNASETTTLSPSGSAV-------ISTTTIAT 173
Cdd:COG3469    92 TSATLVATSTASGANTGTSTVTTTSTGAGSVTSTTSSTAGSTTTSGASATSSAGSTTTTTTVSGTetatggtTTTSTTTT 171


                  ....*..
gi 578801329  174 TPSKPTC 180
Cdd:COG3469   172 TTSASTT 178
PTP_DSP_cys cd14494
cys-based protein tyrosine phosphatase and dual-specificity phosphatase superfamily; This ...
 1116-1175 3.09e-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: 3.09e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 578801329 1116 PLLIHCRDGSQQTGIFCALLNLLESAETeevvdIFQVVKALRKARPGMVS-TFEQYQFLYD 1175
Cdd:cd14494    58 PVLVHCKAGVGRTGTLVACYLVLLGGMS-----AEEAVRIVRLIRPGGIPqTIEQLDFLIK 113
PLN03209 PLN03209
translocon at the inner envelope of chloroplast subunit 62; Provisional
 27-179 8.92e-04

translocon at the inner envelope of chloroplast subunit 62; Provisional


Pssm-ID: 178748 [Multi-domain]  Cd Length: 576  Bit Score: 43.38  E-value: 8.92e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578801329   27 SPTPSPTGLTTAKMPSV-----PLSSDPLPTHTTAFSPASTfERENDFSETTTSLSPDNTSTQVSPDSLDNASAFNTTGV 101
Cdd:PLN03209  385 SPIPTPPSSSPASSKSVdavakPAEPDVVPSPGSASNVPEV-EPAQVEAKKTRPLSPYARYEDLKPPTSPSPTAPTGVSP 463

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 578801329  102 SSVQTPHLPTHADSQTPSAGTDTQtfsgsaanakLNPTPGSNAISDAYLNASETTTLSPSGSAVISTTTIATTPSKPT 179
Cdd:PLN03209  464 SVSSTSSVPAVPDTAPATAATDAA----------APPPANMRPLSPYAVYDDLKPPTSPSPAAPVGKVAPSSTNEVVK 531
CDC14_C cd14499
C-terminal dual-specificity phosphatase domain of CDC14 family proteins; The cell division ...
 799-821 1.19e-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: 1.19e-03
                          10        20
                  ....*....|....*....|...
gi 578801329  799 GPIVVHCSAGVGRTGTYIGIDAM 821
Cdd:cd14499   110 GAIAVHCKAGLGRTGTLIACYLM 132
CDC14 COG2453
Protein-tyrosine phosphatase [Signal transduction mechanisms];
1116-1175 3.02e-03

Protein-tyrosine phosphatase [Signal transduction mechanisms];


Pssm-ID: 441989 [Multi-domain]  Cd Length: 140  Bit Score: 39.18  E-value: 3.02e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 578801329 1116 PLLIHCRDGSQQTGIFCALLNLLESAETEEVVdifqvvKALRKARPGMVSTFEQYQFLYD 1175
Cdd:COG2453    82 KVLVHCRGGIGRTGTVAAAYLVLLGLSAEEAL------ARVRAARPGAVETPAQRAFLER 135
TpbA-like cd14529
bacterial protein tyrosine and dual-specificity phosphatases related to Pseudomonas aeruginosa ...
 756-887 3.19e-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: 3.19e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578801329  756 EKATGREVTHIQFTSWpdhgVPEDPHLLLKLRRRVNAFSNffsGPIVVHCSAGVGRTGTYIGIdamlegleaenkvdvYG 835
Cdd:cd14529    54 AKIDGVKYVNLPLSAT----RPTESDVQSFLLIMDLKLAP---GPVLIHCKHGKDRTGLVSAL---------------YR 111

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 578801329  836 YVVKLRRQrclmvQVEAQYILIHQALVEYNQFGETEVNLSELHPYLHNMKKR 887
Cdd:cd14529   112 IVYGGSKE-----EANEDYRLSNRHLEGLRSGIALDSKGGVKGRYLAAYFER 158
DUSP23 cd14504
dual specificity phosphatase 23; Dual specificity phosphatase 23 (DUSP23), also known as ...
 795-853 4.08e-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: 4.08e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 578801329  795 NFFSGPIVVHCSAGVGRTGT----YIGIDAMLEGLEAenkvdvygyVVKLRRQRCLMVQVEAQ 853
Cdd:cd14504    79 NAKNEAVLVHCLAGKGRTGTmlacYLVKTGKISAVDA---------INEIRRIRPGSIETSEQ 132
FN3 smart00060
Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, ...
 344-414 4.24e-03

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


Pssm-ID: 214495 [Multi-domain]  Cd Length: 83  Bit Score: 37.59  E-value: 4.24e-03
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 578801329    344 PGEPQIIFCRSEAAHQGVITWNPPQRSFHN-FTLCYIKETEKDC-----LNLDKNLIKYDLQNLKPYTKYVLSLHAY 414
Cdd:smart00060    1 PSPPSNLRVTDVTSTSVTLSWEPPPDDGITgYIVGYRVEYREEGsewkeVNVTPSSTSYTLTGLKPGTEYEFRVRAV 77
PTP_PTPDC1 cd14506
protein tyrosine phosphatase domain of PTP domain-containing protein 1; protein tyrosine ...
 770-816 5.56e-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: 5.56e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*..
gi 578801329  770 SWPDHGVPEdPHLLLKLRRrVNAFSNFFSGPIVVHCSAGVGRTGTYI 816
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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