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Conserved domains on  [gi|578801331|ref|XP_006711536|]
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receptor-type tyrosine-protein phosphatase C isoform X3 [Homo sapiens]

Protein Classification

fibronectin type III domain-containing protein( domain architecture ID 13781555)

fibronectin type III (FN3) domain-containing protein may be involved in specific interactions with other molecules through its FN3 domain

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 ...
 641-841 1.10e-149

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


:

Pssm-ID: 350405 [Multi-domain]  Cd Length: 201  Bit Score: 448.12  E-value: 1.10e-149
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578801331  641 YINASYIDGFKEPRKYIAAQGPRDETVDDFWRMIWEQKATVIVMVTRCEEGNRNKCAEYWPSMEEGTRAFGDVVVKINQH 720
Cdd:cd14557     1 YINASYIDGFKEPRKYIAAQGPKDETVDDFWRMIWEQKSTVIVMVTRCEEGNRNKCAQYWPSMEEGSRAFGDVVVKINEE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578801331  721 KRCPDYIIQKLNIVNKKEKATGREVTHIQFTSWPDHGVPEDPHLLLKLRRRVNAFSNFFSGPIVVHCSAGVGRTGTYIGI 800
Cdd:cd14557    81 KICPDYIIRKLNINNKKEKGSGREVTHIQFTSWPDHGVPEDPHLLLKLRRRVNAFNNFFSGPIVVHCSAGVGRTGTYIGI 160

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|.
gi 578801331  801 DAMLEGLEAENKVDVYGYVVKLRRQRCLMVQVEAQYILIHQ 841
Cdd:cd14557   161 DAMLEGLEAEGRVDVYGYVVKLRRQRCLMVQVEAQYILIHQ 201
R-PTP-C-2 cd14558
PTP-like domain of receptor-type tyrosine-protein phosphatase C, repeat 2; Receptor-type ...
 951-1157 1.85e-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: 1.85e-129
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578801331  951 YINASFIMSYWKPEVMIAAQGPLKETIGDFWQMIFQRKVKVIVMLTELKHGDQEICAQYWGEGKQTYGDIEVDLKDTDKS 1030
Cdd:cd14558     1 YINASFIDGYWGPKSLIATQGPLPDTIADFWQMIFQKKVKVIVMLTELKEGDQEQCAQYWGDEKKTYGDIEVELKDTEKS 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578801331 1031 STYTLRVFELRHSKRKDSRTVYQYQYTNWSVEQLPAEPKELISMIQVVKQKLPQKNSsegnKHHKSTPLLIHCRDGSQQT 1110
Cdd:cd14558    81 PTYTVRVFEITHLKRKDSRTVYQYQYHKWKGEELPEKPKDLVDMIKSIKQKLPYKNS----KHGRSVPIVVHCSDGSSRT 156

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*..
gi 578801331 1111 GIFCALLNLLESAETEEVVDIFQVVKALRKARPGMVSTFEQYQFLYD 1157
Cdd:cd14558   157 GIFCALWNLLESAETEKVVDVFQVVKALRKQRPGMVSTLEQYQFLYD 203
CD45 pfam12567
Leukocyte receptor CD45; This family of proteins is found in eukaryotes. Proteins in this ...
 171-229 1.25e-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: 112.08  E-value: 1.25e-29
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 578801331   171 VDYLYNKETKLFTAKLNVNENVECGNNTCTNNEVHNLTECKNASVSISHNSCTAPDKTL 229
Cdd:pfam12567    1 VEYTYNSENKSFTAKLNVNDNVECENNDCENNELHNLQECEQINVSISHNSCTSPNKIL 59
PTP_N pfam12453
Protein tyrosine phosphatase N terminal; This domain family is found in eukaryotes, and is ...
 7-32 2.52e-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: 2.52e-10
                           10        20
                   ....*....|....*....|....*.
gi 578801331     7 LKLLAFGFAFLDTEVFVTGQSPTPSP 32
Cdd:pfam12453    1 LKLLAFGFAFLDTEVFVTGESLTSST 26
PHA03255 super family cl31530
BDLF3; Provisional
 27-165 1.76e-09

BDLF3; Provisional


The actual alignment was detected with superfamily member PHA03255:

Pssm-ID: 165513 [Multi-domain]  Cd Length: 234  Bit Score: 59.53  E-value: 1.76e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578801331   27 SPTPSPTGVSSVQTPHLPTHADSQTPSAG----TDTQTFSGSAANAKLNPTPGS--NAISDVPGERSTASTFPTDPVSPL 100
Cdd:PHA03255   45 TPSPSASGPSTNQSTTLTTTSAPITTTAIlstnTTTVTSTGTTVTPVPTTSNAStiNVTTKVTAQNITATEAGTGTSTGV 124

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 578801331  101 TTtlslahhssaalpartSNTTITANTSDAYLNASETTTLSPSGSAVISTTTIATTPSKPTC-DEK 165
Cdd:PHA03255  125 TS----------------NVTTRSSSTTSATTRITNATTLAPTLSSKGTSNATKTTAELPTVpDER 174
FN3 cd00063
Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein ...
 419-499 1.88e-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: 1.88e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578801331  419 PSQVWNMTVSMTSDNSMHVKCRPPRDRNGPHERYHLEVEAGN----TLVRNESHKNCDFRVKDLQYSTDYTFKAYFHNGD 494
Cdd:cd00063     1 PSPPTNLRVTDVTSTSVTLSWTPPEDDGGPITGYVVEYREKGsgdwKEVEVTPGSETSYTLTGLKPGTEYEFRVRAVNGG 80


                  ....*
gi 578801331  495 YPGEP 499
Cdd:cd00063    81 GESPP 85
fn3 pfam00041
Fibronectin type III domain;
327-396 4.37e-05

Fibronectin type III domain;


:

Pssm-ID: 394996 [Multi-domain]  Cd Length: 85  Bit Score: 43.17  E-value: 4.37e-05
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 578801331   327 GEPQIIFCRSEAAHQGVITWNPP---QRSFHNFTLCYIKETEKDC---LNLDKNLIKYDLQNLKPYTKYVLSLHAY 396
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 ...
 641-841 1.10e-149

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


Pssm-ID: 350405 [Multi-domain]  Cd Length: 201  Bit Score: 448.12  E-value: 1.10e-149
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578801331  641 YINASYIDGFKEPRKYIAAQGPRDETVDDFWRMIWEQKATVIVMVTRCEEGNRNKCAEYWPSMEEGTRAFGDVVVKINQH 720
Cdd:cd14557     1 YINASYIDGFKEPRKYIAAQGPKDETVDDFWRMIWEQKSTVIVMVTRCEEGNRNKCAQYWPSMEEGSRAFGDVVVKINEE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578801331  721 KRCPDYIIQKLNIVNKKEKATGREVTHIQFTSWPDHGVPEDPHLLLKLRRRVNAFSNFFSGPIVVHCSAGVGRTGTYIGI 800
Cdd:cd14557    81 KICPDYIIRKLNINNKKEKGSGREVTHIQFTSWPDHGVPEDPHLLLKLRRRVNAFNNFFSGPIVVHCSAGVGRTGTYIGI 160

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|.
gi 578801331  801 DAMLEGLEAENKVDVYGYVVKLRRQRCLMVQVEAQYILIHQ 841
Cdd:cd14557   161 DAMLEGLEAEGRVDVYGYVVKLRRQRCLMVQVEAQYILIHQ 201
R-PTP-C-2 cd14558
PTP-like domain of receptor-type tyrosine-protein phosphatase C, repeat 2; Receptor-type ...
 951-1157 1.85e-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: 1.85e-129
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578801331  951 YINASFIMSYWKPEVMIAAQGPLKETIGDFWQMIFQRKVKVIVMLTELKHGDQEICAQYWGEGKQTYGDIEVDLKDTDKS 1030
Cdd:cd14558     1 YINASFIDGYWGPKSLIATQGPLPDTIADFWQMIFQKKVKVIVMLTELKEGDQEQCAQYWGDEKKTYGDIEVELKDTEKS 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578801331 1031 STYTLRVFELRHSKRKDSRTVYQYQYTNWSVEQLPAEPKELISMIQVVKQKLPQKNSsegnKHHKSTPLLIHCRDGSQQT 1110
Cdd:cd14558    81 PTYTVRVFEITHLKRKDSRTVYQYQYHKWKGEELPEKPKDLVDMIKSIKQKLPYKNS----KHGRSVPIVVHCSDGSSRT 156

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*..
gi 578801331 1111 GIFCALLNLLESAETEEVVDIFQVVKALRKARPGMVSTFEQYQFLYD 1157
Cdd:cd14558   157 GIFCALWNLLESAETEKVVDVFQVVKALRKQRPGMVSTLEQYQFLYD 203
PTPc smart00194
Protein tyrosine phosphatase, catalytic domain;
586-845 2.94e-111

Protein tyrosine phosphatase, catalytic domain;


Pssm-ID: 214550 [Multi-domain]  Cd Length: 259  Bit Score: 348.88  E-value: 2.94e-111
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578801331    586 LFLAEFQSIPRVFS-KFPIKEARKPFNQNKNRYVDILPYDYNRVELSEINGDaGSNYINASYIDGFKEPRKYIAAQGPRD 664
Cdd:smart00194    1 GLEEEFEKLDRLKPdDESCTVAAFPENRDKNRYKDVLPYDHTRVKLKPPPGE-GSDYINASYIDGPNGPKAYIATQGPLP 79

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578801331    665 ETVDDFWRMIWEQKATVIVMVTRCEEGNRNKCAEYWPSMEEGTRAFGDVVVKINQHKRCPDYIIQKLNIVNKKEKATgRE 744
Cdd:smart00194   80 STVEDFWRMVWEQKVTVIVMLTELVEKGREKCAQYWPDEEGEPLTYGDITVTLKSVEKVDDYTIRTLEVTNTGCSET-RT 158

                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578801331    745 VTHIQFTSWPDHGVPEDPHLLLKLRRRVNAFSNFFSGPIVVHCSAGVGRTGTYIGIDAMLEGLEAENKVDVYGYVVKLRR 824
Cdd:smart00194  159 VTHYHYTNWPDHGVPESPESILDLIRAVRKSQSTSTGPIVVHCSAGVGRTGTFIAIDILLQQLEAGKEVDIFEIVKELRS 238

                           250       260
                    ....*....|....*....|.
gi 578801331    825 QRCLMVQVEAQYILIHQALVE 845
Cdd:smart00194  239 QRPGMVQTEEQYIFLYRAILE 259
Y_phosphatase pfam00102
Protein-tyrosine phosphatase;
611-845 3.84e-107

Protein-tyrosine phosphatase;


Pssm-ID: 459674 [Multi-domain]  Cd Length: 234  Bit Score: 336.52  E-value: 3.84e-107
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578801331   611 NQNKNRYVDILPYDYNRVELSEINGDagSNYINASYIDGFKEPRKYIAAQGPRDETVDDFWRMIWEQKATVIVMVTRCEE 690
Cdd:pfam00102    1 NLEKNRYKDVLPYDHTRVKLTGDPGP--SDYINASYIDGYKKPKKYIATQGPLPNTVEDFWRMVWEEKVTIIVMLTELEE 78

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578801331   691 GNRNKCAEYWPSMEEGTRAFGDVVVKI-NQHKRCPDYIIQKLNIVNKKEKATgREVTHIQFTSWPDHGVPEDPHLLLKLR 769
Cdd:pfam00102   79 KGREKCAQYWPEEEGESLEYGDFTVTLkKEKEDEKDYTVRTLEVSNGGSEET-RTVKHFHYTGWPDHGVPESPNSLLDLL 157

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 578801331   770 RRVNAFSN-FFSGPIVVHCSAGVGRTGTYIGIDAMLEGLEAENKVDVYGYVVKLRRQRCLMVQVEAQYILIHQALVE 845
Cdd:pfam00102  158 RKVRKSSLdGRSGPIVVHCSAGIGRTGTFIAIDIALQQLEAEGEVDIFQIVKELRSQRPGMVQTLEQYIFLYDAILE 234
PTPc smart00194
Protein tyrosine phosphatase, catalytic domain;
878-1160 2.66e-96

Protein tyrosine phosphatase, catalytic domain;


Pssm-ID: 214550 [Multi-domain]  Cd Length: 259  Bit Score: 308.43  E-value: 2.66e-96
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578801331    878 LEAEFQRLPSYRSW-RTQHIGNQEENKSKNRNSNVIPYDYNRVPLKHELEmskesehdsdessdddsdseEPSKYINASF 956
Cdd:smart00194    2 LEEEFEKLDRLKPDdESCTVAAFPENRDKNRYKDVLPYDHTRVKLKPPPG--------------------EGSDYINASY 61

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578801331    957 IMSYWKPEVMIAAQGPLKETIGDFWQMIFQRKVKVIVMLTELKHGDQEICAQYW---GEGKQTYGDIEVDLKDTDKSSTY 1033
Cdd:smart00194   62 IDGPNGPKAYIATQGPLPSTVEDFWRMVWEQKVTVIVMLTELVEKGREKCAQYWpdeEGEPLTYGDITVTLKSVEKVDDY 141

                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578801331   1034 TLRVFELRHSKRKDSRTVYQYQYTNWSVEQLPAEPKELISMIQVVKQKLPqknssegnkhHKSTPLLIHCRDGSQQTGIF 1113
Cdd:smart00194  142 TIRTLEVTNTGCSETRTVTHYHYTNWPDHGVPESPESILDLIRAVRKSQS----------TSTGPIVVHCSAGVGRTGTF 211

                           250       260       270       280
                    ....*....|....*....|....*....|....*....|....*..
gi 578801331   1114 CALLNLLESAETEEVVDIFQVVKALRKARPGMVSTFEQYQFLYDVIA 1160
Cdd:smart00194  212 IAIDILLQQLEAGKEVDIFEIVKELRSQRPGMVQTEEQYIFLYRAIL 258
Y_phosphatase pfam00102
Protein-tyrosine phosphatase;
902-1160 1.44e-85

Protein-tyrosine phosphatase;


Pssm-ID: 459674 [Multi-domain]  Cd Length: 234  Bit Score: 277.97  E-value: 1.44e-85
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578801331   902 NKSKNRNSNVIPYDYNRVPLKHElemskesehdsdessdddsdsEEPSKYINASFIMSYWKPEVMIAAQGPLKETIGDFW 981
Cdd:pfam00102    1 NLEKNRYKDVLPYDHTRVKLTGD---------------------PGPSDYINASYIDGYKKPKKYIATQGPLPNTVEDFW 59

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578801331   982 QMIFQRKVKVIVMLTELKHGDQEICAQYW---GEGKQTYGDIEVDLKDTDK-SSTYTLRVFELRHSKRKDSRTVYQYQYT 1057
Cdd:pfam00102   60 RMVWEEKVTIIVMLTELEEKGREKCAQYWpeeEGESLEYGDFTVTLKKEKEdEKDYTVRTLEVSNGGSEETRTVKHFHYT 139

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578801331  1058 NWSVEQLPAEPKELISMIQVVKQKlpqknssegNKHHKSTPLLIHCRDGSQQTGIFCALLNLLESAETEEVVDIFQVVKA 1137
Cdd:pfam00102  140 GWPDHGVPESPNSLLDLLRKVRKS---------SLDGRSGPIVVHCSAGIGRTGTFIAIDIALQQLEAEGEVDIFQIVKE 210

                          250       260
                   ....*....|....*....|...
gi 578801331  1138 LRKARPGMVSTFEQYQFLYDVIA 1160
Cdd:pfam00102  211 LRSQRPGMVQTLEQYIFLYDAIL 233
PHA02746 PHA02746
protein tyrosine phosphatase; Provisional
 608-843 1.00e-51

protein tyrosine phosphatase; Provisional


Pssm-ID: 165113 [Multi-domain]  Cd Length: 323  Bit Score: 185.23  E-value: 1.00e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578801331  608 KPFNQNKNRYVDILPYDYNRVELSE-------------------INGDAGSNYINASYIDGFKEPRKYIAAQGPRDETVD 668
Cdd:PHA02746   48 KKENLKKNRFHDIPCWDHSRVVINAheslkmfdvgdsdgkkievTSEDNAENYIHANFVDGFKEANKFICAQGPKEDTSE 127

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578801331  669 DFWRMIWEQKATVIVMVTRCEEGNRnKCAEYWPSMEEGTRAFGDVVVKINQHKRCPDYIIQKLNIVNKKEKaTGREVTHI 748
Cdd:PHA02746  128 DFFKLISEHESQVIVSLTDIDDDDE-KCFELWTKEEDSELAFGRFVAKILDIIEELSFTKTRLMITDKISD-TSREIHHF 205

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578801331  749 QFTSWPDHGVPEDPHLLLKLRRRVNA----------FSNFFSGPIVVHCSAGVGRTGTYIGIDAMLEGLEAENKVDVYGY 818
Cdd:PHA02746  206 WFPDWPDNGIPTGMAEFLELINKVNEeqaelikqadNDPQTLGPIVVHCSAGIGRAGTFCAIDNALEQLEKEKEVCLGEI 285

                         250       260
                  ....*....|....*....|....*
gi 578801331  819 VVKLRRQRCLMVQVEAQYILIHQAL 843
Cdd:PHA02746  286 VLKIRKQRHSSVFLPEQYAFCYKAL 310
COG5599 COG5599
Protein tyrosine phosphatase [Signal transduction mechanisms];
614-839 6.69e-40

Protein tyrosine phosphatase [Signal transduction mechanisms];


Pssm-ID: 444335 [Multi-domain]  Cd Length: 282  Bit Score: 149.47  E-value: 6.69e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578801331  614 KNRYVDILPYDYNRVElseINGdagsNYINASYIDGfKEPRKYIAAQGPRDETVDDFWRMIWEQKATVIVMVTRCEEG-- 691
Cdd:COG5599    45 LNRFRDIQPYKETALR---ANL----GYLNANYIQV-IGNHRYIATQYPLEEQLEDFFQMLFDNNTPVLVVLASDDEIsk 116

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578801331  692 NRNKCAEYWPsmEEGTRAFGDVVVKINQHKRCPDYIIQKLNIVNKKEKA-TGREVTHIQFTSWPDHGVP--EDPHLLLKL 768
Cdd:COG5599   117 PKVKMPVYFR--QDGEYGKYEVSSELTESIQLRDGIEARTYVLTIKGTGqKKIEIPVLHVKNWPDHGAIsaEALKNLADL 194

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 578801331  769 RRRVNAFSNFFSGPIVVHCSAGVGRTGTYIGIDAMLEGLEAEN--KVDVYGYVVKLRRQR-CLMVQVEAQYILI 839
Cdd:COG5599   195 IDKKEKIKDPDKLLPVVHCRAGVGRTGTLIACLALSKSINALVqiTLSVEEIVIDMRTSRnGGMVQTSEQLDVL 268
PHA02747 PHA02747
protein tyrosine phosphatase; Provisional
 901-1155 5.67e-35

protein tyrosine phosphatase; Provisional


Pssm-ID: 165114 [Multi-domain]  Cd Length: 312  Bit Score: 136.28  E-value: 5.67e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578801331  901 ENKSKNRNSNVIPYDYNRVPLKhelemskesehdsdessdddSDSEEPSKYINASFIMSYWKPEVMIAAQGPLKETIGDF 980
Cdd:PHA02747   50 ENQPKNRYWDIPCWDHNRVILD--------------------SGGGSTSDYIHANWIDGFEDDKKFIATQGPFAETCADF 109

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578801331  981 WQMIFQRKVKVIVMLTELKHGD-QEICAQYWG---EGKQTYGDIEVDLKDTDKSSTYTLRVFELRHSKRKDSRTVYQYQY 1056
Cdd:PHA02747  110 WKAVWQEHCSIIVMLTPTKGTNgEEKCYQYWClneDGNIDMEDFRIETLKTSVRAKYILTLIEITDKILKDSRKISHFQC 189

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578801331 1057 TNWSVEQLPAEPKELISMIQVVKQKLPQKNSSEGNKHHKSTPLLIHCRDGSQQTGIFCALLNLLESAETEEVVDIFQVVK 1136
Cdd:PHA02747  190 SEWFEDETPSDHPDFIKFIKIIDINRKKSGKLFNPKDALLCPIVVHCSDGVGKTGIFCAVDICLNQLVKRKAICLAKTAE 269

                         250
                  ....*....|....*....
gi 578801331 1137 ALRKARPGMVSTFEQYQFL 1155
Cdd:PHA02747  270 KIREQRHAGIMNFDDYLFI 288
COG5599 COG5599
Protein tyrosine phosphatase [Signal transduction mechanisms];
893-1161 4.21e-30

Protein tyrosine phosphatase [Signal transduction mechanisms];


Pssm-ID: 444335 [Multi-domain]  Cd Length: 282  Bit Score: 121.35  E-value: 4.21e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578801331  893 TQHIGNQEeNKSKNRNSNVIPYDYNRVplkhelemskesehdsdessdddsdsEEPSKYINASFIMSYwKPEVMIAAQGP 972
Cdd:COG5599    34 PQYLQNIN-GSPLNRFRDIQPYKETAL--------------------------RANLGYLNANYIQVI-GNHRYIATQYP 85

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578801331  973 LKETIGDFWQMIFQRKVKVIVMLTELKHGDQEI--CAQYWGEgKQTYGDIEVDLKDTDK---SSTYTLRVFEL-RHSKRK 1046
Cdd:COG5599    86 LEEQLEDFFQMLFDNNTPVLVVLASDDEISKPKvkMPVYFRQ-DGEYGKYEVSSELTESiqlRDGIEARTYVLtIKGTGQ 164

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578801331 1047 DSRTVYQYQYTNWSVEQLPAePKELISMIQVVKQKLPQKNSSEGnkhhkstPLLIHCRDGSQQTGIFCALLNLLES--AE 1124
Cdd:COG5599   165 KKIEIPVLHVKNWPDHGAIS-AEALKNLADLIDKKEKIKDPDKL-------LPVVHCRAGVGRTGTLIACLALSKSinAL 236

                         250       260       270
                  ....*....|....*....|....*....|....*...
gi 578801331 1125 TEEVVDIFQVVKALRKAR-PGMVSTFEQYQFLYDVIAS 1161
Cdd:COG5599   237 VQITLSVEEIVIDMRTSRnGGMVQTSEQLDVLVKLAEQ 274
CD45 pfam12567
Leukocyte receptor CD45; This family of proteins is found in eukaryotes. Proteins in this ...
 171-229 1.25e-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: 112.08  E-value: 1.25e-29
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 578801331   171 VDYLYNKETKLFTAKLNVNENVECGNNTCTNNEVHNLTECKNASVSISHNSCTAPDKTL 229
Cdd:pfam12567    1 VEYTYNSENKSFTAKLNVNDNVECENNDCENNELHNLQECEQINVSISHNSCTSPNKIL 59
PTP_N pfam12453
Protein tyrosine phosphatase N terminal; This domain family is found in eukaryotes, and is ...
 7-32 2.52e-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: 2.52e-10
                           10        20
                   ....*....|....*....|....*.
gi 578801331     7 LKLLAFGFAFLDTEVFVTGQSPTPSP 32
Cdd:pfam12453    1 LKLLAFGFAFLDTEVFVTGESLTSST 26
PHA03255 PHA03255
BDLF3; Provisional
 27-165 1.76e-09

BDLF3; Provisional


Pssm-ID: 165513 [Multi-domain]  Cd Length: 234  Bit Score: 59.53  E-value: 1.76e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578801331   27 SPTPSPTGVSSVQTPHLPTHADSQTPSAG----TDTQTFSGSAANAKLNPTPGS--NAISDVPGERSTASTFPTDPVSPL 100
Cdd:PHA03255   45 TPSPSASGPSTNQSTTLTTTSAPITTTAIlstnTTTVTSTGTTVTPVPTTSNAStiNVTTKVTAQNITATEAGTGTSTGV 124

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 578801331  101 TTtlslahhssaalpartSNTTITANTSDAYLNASETTTLSPSGSAVISTTTIATTPSKPTC-DEK 165
Cdd:PHA03255  125 TS----------------NVTTRSSSTTSATTRITNATTLAPTLSSKGTSNATKTTAELPTVpDER 174
FN3 cd00063
Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein ...
 419-499 1.88e-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: 1.88e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578801331  419 PSQVWNMTVSMTSDNSMHVKCRPPRDRNGPHERYHLEVEAGN----TLVRNESHKNCDFRVKDLQYSTDYTFKAYFHNGD 494
Cdd:cd00063     1 PSPPTNLRVTDVTSTSVTLSWTPPEDDGGPITGYVVEYREKGsgdwKEVEVTPGSETSYTLTGLKPGTEYEFRVRAVNGG 80


                  ....*
gi 578801331  495 YPGEP 499
Cdd:cd00063    81 GESPP 85
fn3 pfam00041
Fibronectin type III domain;
420-499 1.86e-06

Fibronectin type III domain;


Pssm-ID: 394996 [Multi-domain]  Cd Length: 85  Bit Score: 47.02  E-value: 1.86e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578801331   420 SQVWNMTVSMTSDNSMHVKCRPPRDRNGPHERYHLEVEAGN--------TLVRNESHkncdFRVKDLQYSTDYTFKAYFH 491
Cdd:pfam00041    1 SAPSNLTVTDVTSTSLTVSWTPPPDGNGPITGYEVEYRPKNsgepwneiTVPGTTTS----VTLTGLKPGTEYEVRVQAV 76


                   ....*...
gi 578801331   492 NGDYPGEP 499
Cdd:pfam00041   77 NGGGEGPP 84
Chi1 COG3469
Chitinase [Carbohydrate transport and metabolism];
24-161 9.65e-06

Chitinase [Carbohydrate transport and metabolism];


Pssm-ID: 442692 [Multi-domain]  Cd Length: 534  Bit Score: 49.75  E-value: 9.65e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578801331   24 TGQSPTPSPTGVSSVQTPHLPTHADSQTPSAGTDTQTFSGSAANAKLNPTPGSNAISDVPGERSTASTFPTDPVS-PLTT 102
Cdd:COG3469    59 SGTGTTAASSTAATSSTTSTTATATAAAAAATSTSATLVATSTASGANTGTSTVTTTSTGAGSVTSTTSSTAGSTtTSGA 138

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 578801331  103 TLSLAHHSSAALPARTSNTTITANTSDAY---LNASETTTLSPSGSAVISTTTIATTPSKPT 161
Cdd:COG3469   139 SATSSAGSTTTTTTVSGTETATGGTTTTStttTTTSASTTPSATTTATATTASGATTPSATT 200
fn3 pfam00041
Fibronectin type III domain;
327-396 4.37e-05

Fibronectin type III domain;


Pssm-ID: 394996 [Multi-domain]  Cd Length: 85  Bit Score: 43.17  E-value: 4.37e-05
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 578801331   327 GEPQIIFCRSEAAHQGVITWNPP---QRSFHNFTLCYIKETEKDC---LNLDKNLIKYDLQNLKPYTKYVLSLHAY 396
Cdd:pfam00041    1 SAPSNLTVTDVTSTSLTVSWTPPpdgNGPITGYEVEYRPKNSGEPwneITVPGTTTSVTLTGLKPGTEYEVRVQAV 76
FN3 smart00060
Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, ...
 419-494 8.00e-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: 8.00e-05
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578801331    419 PSQVWNMTVSMTSDNSMHVKCRPPRDRNGPHERYHLEVE----AGNTLVRNESHKNCDFRVKDLQYSTDYTFK--AYFHN 492
Cdd:smart00060    1 PSPPSNLRVTDVTSTSVTLSWEPPPDDGITGYIVGYRVEyreeGSEWKEVNVTPSSTSYTLTGLKPGTEYEFRvrAVNGA 80


                    ..
gi 578801331    493 GD 494
Cdd:smart00060   81 GE 82
FN3 cd00063
Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein ...
 326-396 8.29e-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: 8.29e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 578801331  326 PGEPQIIFCRSEAAHQGVITWNPPQRS---FHNFTLCYIKETEKDCLNLDKNLIK---YDLQNLKPYTKYVLSLHAY 396
Cdd:cd00063     1 PSPPTNLRVTDVTSTSVTLSWTPPEDDggpITGYVVEYREKGSGDWKEVEVTPGSetsYTLTGLKPGTEYEFRVRAV 77
FN3 smart00060
Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, ...
 326-396 4.14e-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: 4.14e-03
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 578801331    326 PGEPQIIFCRSEAAHQGVITWNPPQRSFHN-FTLCYIKETEKDC-----LNLDKNLIKYDLQNLKPYTKYVLSLHAY 396
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 ...
 641-841 1.10e-149

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


Pssm-ID: 350405 [Multi-domain]  Cd Length: 201  Bit Score: 448.12  E-value: 1.10e-149
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578801331  641 YINASYIDGFKEPRKYIAAQGPRDETVDDFWRMIWEQKATVIVMVTRCEEGNRNKCAEYWPSMEEGTRAFGDVVVKINQH 720
Cdd:cd14557     1 YINASYIDGFKEPRKYIAAQGPKDETVDDFWRMIWEQKSTVIVMVTRCEEGNRNKCAQYWPSMEEGSRAFGDVVVKINEE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578801331  721 KRCPDYIIQKLNIVNKKEKATGREVTHIQFTSWPDHGVPEDPHLLLKLRRRVNAFSNFFSGPIVVHCSAGVGRTGTYIGI 800
Cdd:cd14557    81 KICPDYIIRKLNINNKKEKGSGREVTHIQFTSWPDHGVPEDPHLLLKLRRRVNAFNNFFSGPIVVHCSAGVGRTGTYIGI 160

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|.
gi 578801331  801 DAMLEGLEAENKVDVYGYVVKLRRQRCLMVQVEAQYILIHQ 841
Cdd:cd14557   161 DAMLEGLEAEGRVDVYGYVVKLRRQRCLMVQVEAQYILIHQ 201
R-PTP-C-2 cd14558
PTP-like domain of receptor-type tyrosine-protein phosphatase C, repeat 2; Receptor-type ...
 951-1157 1.85e-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: 1.85e-129
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578801331  951 YINASFIMSYWKPEVMIAAQGPLKETIGDFWQMIFQRKVKVIVMLTELKHGDQEICAQYWGEGKQTYGDIEVDLKDTDKS 1030
Cdd:cd14558     1 YINASFIDGYWGPKSLIATQGPLPDTIADFWQMIFQKKVKVIVMLTELKEGDQEQCAQYWGDEKKTYGDIEVELKDTEKS 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578801331 1031 STYTLRVFELRHSKRKDSRTVYQYQYTNWSVEQLPAEPKELISMIQVVKQKLPQKNSsegnKHHKSTPLLIHCRDGSQQT 1110
Cdd:cd14558    81 PTYTVRVFEITHLKRKDSRTVYQYQYHKWKGEELPEKPKDLVDMIKSIKQKLPYKNS----KHGRSVPIVVHCSDGSSRT 156

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*..
gi 578801331 1111 GIFCALLNLLESAETEEVVDIFQVVKALRKARPGMVSTFEQYQFLYD 1157
Cdd:cd14558   157 GIFCALWNLLESAETEKVVDVFQVVKALRKQRPGMVSTLEQYQFLYD 203
PTPc smart00194
Protein tyrosine phosphatase, catalytic domain;
586-845 2.94e-111

Protein tyrosine phosphatase, catalytic domain;


Pssm-ID: 214550 [Multi-domain]  Cd Length: 259  Bit Score: 348.88  E-value: 2.94e-111
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578801331    586 LFLAEFQSIPRVFS-KFPIKEARKPFNQNKNRYVDILPYDYNRVELSEINGDaGSNYINASYIDGFKEPRKYIAAQGPRD 664
Cdd:smart00194    1 GLEEEFEKLDRLKPdDESCTVAAFPENRDKNRYKDVLPYDHTRVKLKPPPGE-GSDYINASYIDGPNGPKAYIATQGPLP 79

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578801331    665 ETVDDFWRMIWEQKATVIVMVTRCEEGNRNKCAEYWPSMEEGTRAFGDVVVKINQHKRCPDYIIQKLNIVNKKEKATgRE 744
Cdd:smart00194   80 STVEDFWRMVWEQKVTVIVMLTELVEKGREKCAQYWPDEEGEPLTYGDITVTLKSVEKVDDYTIRTLEVTNTGCSET-RT 158

                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578801331    745 VTHIQFTSWPDHGVPEDPHLLLKLRRRVNAFSNFFSGPIVVHCSAGVGRTGTYIGIDAMLEGLEAENKVDVYGYVVKLRR 824
Cdd:smart00194  159 VTHYHYTNWPDHGVPESPESILDLIRAVRKSQSTSTGPIVVHCSAGVGRTGTFIAIDILLQQLEAGKEVDIFEIVKELRS 238

                           250       260
                    ....*....|....*....|.
gi 578801331    825 QRCLMVQVEAQYILIHQALVE 845
Cdd:smart00194  239 QRPGMVQTEEQYIFLYRAILE 259
Y_phosphatase pfam00102
Protein-tyrosine phosphatase;
611-845 3.84e-107

Protein-tyrosine phosphatase;


Pssm-ID: 459674 [Multi-domain]  Cd Length: 234  Bit Score: 336.52  E-value: 3.84e-107
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578801331   611 NQNKNRYVDILPYDYNRVELSEINGDagSNYINASYIDGFKEPRKYIAAQGPRDETVDDFWRMIWEQKATVIVMVTRCEE 690
Cdd:pfam00102    1 NLEKNRYKDVLPYDHTRVKLTGDPGP--SDYINASYIDGYKKPKKYIATQGPLPNTVEDFWRMVWEEKVTIIVMLTELEE 78

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578801331   691 GNRNKCAEYWPSMEEGTRAFGDVVVKI-NQHKRCPDYIIQKLNIVNKKEKATgREVTHIQFTSWPDHGVPEDPHLLLKLR 769
Cdd:pfam00102   79 KGREKCAQYWPEEEGESLEYGDFTVTLkKEKEDEKDYTVRTLEVSNGGSEET-RTVKHFHYTGWPDHGVPESPNSLLDLL 157

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 578801331   770 RRVNAFSN-FFSGPIVVHCSAGVGRTGTYIGIDAMLEGLEAENKVDVYGYVVKLRRQRCLMVQVEAQYILIHQALVE 845
Cdd:pfam00102  158 RKVRKSSLdGRSGPIVVHCSAGIGRTGTFIAIDIALQQLEAEGEVDIFQIVKELRSQRPGMVQTLEQYIFLYDAILE 234
R-PTPc-LAR-1 cd14553
catalytic domain of LAR family receptor-type tyrosine-protein phosphatases, repeat 1; The LAR ...
 611-845 1.30e-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: 310.87  E-value: 1.30e-97
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578801331  611 NQNKNRYVDILPYDYNRVELSEINGDAGSNYINASYIDGFKEPRKYIAAQGPRDETVDDFWRMIWEQKATVIVMVTRCEE 690
Cdd:cd14553     3 NKPKNRYANVIAYDHSRVILQPIEGVPGSDYINANYCDGYRKQNAYIATQGPLPETFGDFWRMVWEQRSATIVMMTKLEE 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578801331  691 GNRNKCAEYWPSmeEGTRAFGDVVVKINQHKRCPDYIIQKLNIVNKKEKATgREVTHIQFTSWPDHGVPEDPHLLLKLRR 770
Cdd:cd14553    83 RSRVKCDQYWPT--RGTETYGLIQVTLLDTVELATYTVRTFALHKNGSSEK-REVRQFQFTAWPDHGVPEHPTPFLAFLR 159

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 578801331  771 RVNAFSNFFSGPIVVHCSAGVGRTGTYIGIDAMLEGLEAENKVDVYGYVVKLRRQRCLMVQVEAQYILIHQALVE 845
Cdd:cd14553   160 RVKACNPPDAGPIVVHCSAGVGRTGCFIVIDSMLERIKHEKTVDIYGHVTCLRAQRNYMVQTEDQYIFIHDALLE 234
PTPc smart00194
Protein tyrosine phosphatase, catalytic domain;
878-1160 2.66e-96

Protein tyrosine phosphatase, catalytic domain;


Pssm-ID: 214550 [Multi-domain]  Cd Length: 259  Bit Score: 308.43  E-value: 2.66e-96
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578801331    878 LEAEFQRLPSYRSW-RTQHIGNQEENKSKNRNSNVIPYDYNRVPLKHELEmskesehdsdessdddsdseEPSKYINASF 956
Cdd:smart00194    2 LEEEFEKLDRLKPDdESCTVAAFPENRDKNRYKDVLPYDHTRVKLKPPPG--------------------EGSDYINASY 61

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578801331    957 IMSYWKPEVMIAAQGPLKETIGDFWQMIFQRKVKVIVMLTELKHGDQEICAQYW---GEGKQTYGDIEVDLKDTDKSSTY 1033
Cdd:smart00194   62 IDGPNGPKAYIATQGPLPSTVEDFWRMVWEQKVTVIVMLTELVEKGREKCAQYWpdeEGEPLTYGDITVTLKSVEKVDDY 141

                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578801331   1034 TLRVFELRHSKRKDSRTVYQYQYTNWSVEQLPAEPKELISMIQVVKQKLPqknssegnkhHKSTPLLIHCRDGSQQTGIF 1113
Cdd:smart00194  142 TIRTLEVTNTGCSETRTVTHYHYTNWPDHGVPESPESILDLIRAVRKSQS----------TSTGPIVVHCSAGVGRTGTF 211

                           250       260       270       280
                    ....*....|....*....|....*....|....*....|....*..
gi 578801331   1114 CALLNLLESAETEEVVDIFQVVKALRKARPGMVSTFEQYQFLYDVIA 1160
Cdd:smart00194  212 IAIDILLQQLEAGKEVDIFEIVKELRSQRPGMVQTEEQYIFLYRAIL 258
PTPc cd00047
catalytic domain of protein tyrosine phosphatases; Protein tyrosine phosphatases (PTP, EC 3.1. ...
 641-841 3.86e-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: 302.67  E-value: 3.86e-95
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578801331  641 YINASYIDGFKEPRKYIAAQGPRDETVDDFWRMIWEQKATVIVMVTRCEEGNRNKCAEYWPSMEEGTRAFGDVVVKINQH 720
Cdd:cd00047     1 YINASYIDGYRGPKEYIATQGPLPNTVEDFWRMVWEQKVSVIVMLTNLVEKGREKCERYWPEEGGKPLEYGDITVTLVSE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578801331  721 KRCPDYIIQKLNIVNKKEKATgREVTHIQFTSWPDHGVPEDPHLLLKLRRRVNAFSNFFSGPIVVHCSAGVGRTGTYIGI 800
Cdd:cd00047    81 EELSDYTIRTLELSPKGCSES-REVTHLHYTGWPDHGVPSSPEDLLALVRRVRKEARKPNGPIVVHCSAGVGRTGTFIAI 159

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|.
gi 578801331  801 DAMLEGLEAENKVDVYGYVVKLRRQRCLMVQVEAQYILIHQ 841
Cdd:cd00047   160 DILLERLEAEGEVDVFEIVKALRKQRPGMVQTLEQYEFIYE 200
R3-PTPc cd14548
catalytic domain of R3 subfamily receptor-type tyrosine-protein phosphatases and similar ...
 616-841 8.39e-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: 8.39e-93
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578801331  616 RYVDILPYDYNRVELSEINGDAGSNYINASYIDGFKEPRKYIAAQGPRDETVDDFWRMIWEQKATVIVMVTRCEEGNRNK 695
Cdd:cd14548     1 RYTNILPYDHSRVKLIPINEEEGSDYINANYIPGYNSPREFIATQGPLPGTKDDFWRMVWEQNSHTIVMLTQCMEKGRVK 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578801331  696 CAEYWPSMEEGTrAFGDVVVKINQHKRCPDYIIQKLNIVNKKEKatgREVTHIQFTSWPDHGVPEDPHLLLKLRRRVNAF 775
Cdd:cd14548    81 CDHYWPFDQDPV-YYGDITVTMLSESVLPDWTIREFKLERGDEV---RSVRQFHFTAWPDHGVPEAPDSLLRFVRLVRDY 156

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 578801331  776 SNFFSGPIVVHCSAGVGRTGTYIGIDAMLEGLEAENKVDVYGYVVKLRRQRCLMVQVEAQYILIHQ 841
Cdd:cd14548   157 IKQEKGPTIVHCSAGVGRTGTFIALDRLLQQIESEDYVDIFGIVYDLRKHRPLMVQTEAQYIFLHQ 222
R-PTPc-A-1 cd14621
catalytic domain of receptor-type tyrosine-protein phosphatase A, repeat 1; Receptor-type ...
 566-854 3.04e-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: 290.39  E-value: 3.04e-89
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578801331  566 PIHADILLETYKRKIADEGRLFLAEFQSIPRVFSKFPIKEARKPFNQNKNRYVDILPYDYNRVELSEINGDAGSNYINAS 645
Cdd:cd14621     7 PLPVDKLEEEINRRMADDNKLFREEFNALPACPIQATCEAASKEENKEKNRYVNILPYDHSRVHLTPVEGVPDSDYINAS 86

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578801331  646 YIDGFKEPRKYIAAQGPRDETVDDFWRMIWEQKATVIVMVTRCEEGNRNKCAEYWPsmEEGTRAFGDVVVKINQHKRCPD 725
Cdd:cd14621    87 FINGYQEKNKFIAAQGPKEETVNDFWRMIWEQNTATIVMVTNLKERKECKCAQYWP--DQGCWTYGNIRVSVEDVTVLVD 164

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578801331  726 YIIQKL------NIVNKKEKatgREVTHIQFTSWPDHGVPEDPHLLLKLRRRVNAFSNFFSGPIVVHCSAGVGRTGTYIG 799
Cdd:cd14621   165 YTVRKFciqqvgDVTNKKPQ---RLITQFHFTSWPDFGVPFTPIGMLKFLKKVKNCNPQYAGAIVVHCSAGVGRTGTFIV 241

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 578801331  800 IDAMLEGLEAENKVDVYGYVVKLRRQRCLMVQVEAQYILIHQALVEYNQFGETEV 854
Cdd:cd14621   242 IDAMLDMMHAERKVDVYGFVSRIRAQRCQMVQTDMQYVFIYQALLEHYLYGDTEL 296
Y_phosphatase pfam00102
Protein-tyrosine phosphatase;
902-1160 1.44e-85

Protein-tyrosine phosphatase;


Pssm-ID: 459674 [Multi-domain]  Cd Length: 234  Bit Score: 277.97  E-value: 1.44e-85
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578801331   902 NKSKNRNSNVIPYDYNRVPLKHElemskesehdsdessdddsdsEEPSKYINASFIMSYWKPEVMIAAQGPLKETIGDFW 981
Cdd:pfam00102    1 NLEKNRYKDVLPYDHTRVKLTGD---------------------PGPSDYINASYIDGYKKPKKYIATQGPLPNTVEDFW 59

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578801331   982 QMIFQRKVKVIVMLTELKHGDQEICAQYW---GEGKQTYGDIEVDLKDTDK-SSTYTLRVFELRHSKRKDSRTVYQYQYT 1057
Cdd:pfam00102   60 RMVWEEKVTIIVMLTELEEKGREKCAQYWpeeEGESLEYGDFTVTLKKEKEdEKDYTVRTLEVSNGGSEETRTVKHFHYT 139

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578801331  1058 NWSVEQLPAEPKELISMIQVVKQKlpqknssegNKHHKSTPLLIHCRDGSQQTGIFCALLNLLESAETEEVVDIFQVVKA 1137
Cdd:pfam00102  140 GWPDHGVPESPNSLLDLLRKVRKS---------SLDGRSGPIVVHCSAGIGRTGTFIAIDIALQQLEAEGEVDIFQIVKE 210

                          250       260
                   ....*....|....*....|...
gi 578801331  1138 LRKARPGMVSTFEQYQFLYDVIA 1160
Cdd:pfam00102  211 LRSQRPGMVQTLEQYIFLYDAIL 233
R5-PTPc-1 cd14549
catalytic domain of R5 subfamily receptor-type tyrosine-protein phosphatases, repeat 1; The R5 ...
 641-840 2.90e-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: 270.38  E-value: 2.90e-83
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578801331  641 YINASYIDGFKEPRKYIAAQGPRDETVDDFWRMIWEQKATVIVMVTRCEEGNRNKCAEYWPSmeEGTRAFGDVVVKINQH 720
Cdd:cd14549     1 YINANYVDGYNKARAYIATQGPLPSTFDDFWRMVWEQNSAIIVMITNLVERGRRKCDQYWPK--EGTETYGNIQVTLLST 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578801331  721 KRCPDYIIQKLNIVNKKEK-----ATGREVTHIQFTSWPDHGVPEDPHLLLKLRRRVNAFSNFFSGPIVVHCSAGVGRTG 795
Cdd:cd14549    79 EVLATYTVRTFSLKNLKLKkvkgrSSERVVYQYHYTQWPDHGVPDYTLPVLSFVRKSSAANPPGAGPIVVHCSAGVGRTG 158

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*
gi 578801331  796 TYIGIDAMLEGLEAENKVDVYGYVVKLRRQRCLMVQVEAQYILIH 840
Cdd:cd14549   159 TYIVIDSMLQQIQDKGTVNVFGFLKHIRTQRNYLVQTEEQYIFIH 203
PTPc cd00047
catalytic domain of protein tyrosine phosphatases; Protein tyrosine phosphatases (PTP, EC 3.1. ...
 951-1157 7.40e-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: 266.07  E-value: 7.40e-82
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578801331  951 YINASFIMSYWKPEVMIAAQGPLKETIGDFWQMIFQRKVKVIVMLTELKHGDQEICAQYW---GEGKQTYGDIEVDLKDT 1027
Cdd:cd00047     1 YINASYIDGYRGPKEYIATQGPLPNTVEDFWRMVWEQKVSVIVMLTNLVEKGREKCERYWpeeGGKPLEYGDITVTLVSE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578801331 1028 DKSSTYTLRVFELRHSKRKDSRTVYQYQYTNWSVEQLPAEPKELISMIQVVKQKLPQKNSsegnkhhkstPLLIHCRDGS 1107
Cdd:cd00047    81 EELSDYTIRTLELSPKGCSESREVTHLHYTGWPDHGVPSSPEDLLALVRRVRKEARKPNG----------PIVVHCSAGV 150

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|
gi 578801331 1108 QQTGIFCALLNLLESAETEEVVDIFQVVKALRKARPGMVSTFEQYQFLYD 1157
Cdd:cd00047   151 GRTGTFIAIDILLERLEAEGEVDVFEIVKALRKQRPGMVQTLEQYEFIYE 200
R-PTPc-E-1 cd14620
catalytic domain of receptor-type tyrosine-protein phosphatase E, repeat 1; Receptor-type ...
 617-845 9.18e-81

catalytic domain of receptor-type tyrosine-protein phosphatase E, repeat 1; Receptor-type tyrosine-protein phosphatase E (PTPRE), also known as receptor-type tyrosine-protein phosphatase epsilon (R-PTP-epsilon), belongs to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. The PTPRE gene contains two distinct promoters that generate the two major isoforms: transmembrane (receptor type RPTPe or PTPeM) and cytoplasmic (cyt-PTPe or PTPeC). Receptor type RPTPe plays a critical role in signaling transduction pathways and phosphoprotein network topology in red blood cells, and may also play a role in osteoclast formation and function. It also negatively regulates PDGFRbeta-mediated signaling pathways that are crucial for the pathogenesis of atherosclerosis. cyt-PTPe acts as a negative regulator of insulin receptor signaling in skeletal muscle. It regulates insulin-induced phosphorylation of proteins downstream of the insulin receptor. Receptor type RPTPe contains a small extracellular region, a single transmembrane segment, and an intracellular region two tandem catalytic PTP domains. This model represents the first PTP domain (repeat 1).


Pssm-ID: 350468 [Multi-domain]  Cd Length: 229  Bit Score: 264.50  E-value: 9.18e-81
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578801331  617 YVDILPYDYNRVELSEINGDAGSNYINASYIDGFKEPRKYIAAQGPRDETVDDFWRMIWEQKATVIVMVTRCEEGNRNKC 696
Cdd:cd14620     1 YPNILPYDHSRVILSQLDGIPCSDYINASYIDGYKEKNKFIAAQGPKQETVNDFWRMVWEQKSATIVMLTNLKERKEEKC 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578801331  697 AEYWPsmEEGTRAFGDVVVKINQHKRCPDYIIQKLNIVNKKEKAT--GREVTHIQFTSWPDHGVPEDPHLLLKLRRRVNA 774
Cdd:cd14620    81 YQYWP--DQGCWTYGNIRVAVEDCVVLVDYTIRKFCIQPQLPDGCkaPRLVTQLHFTSWPDFGVPFTPIGMLKFLKKVKS 158

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 578801331  775 FSNFFSGPIVVHCSAGVGRTGTYIGIDAMLEGLEAENKVDVYGYVVKLRRQRCLMVQVEAQYILIHQALVE 845
Cdd:cd14620   159 VNPVHAGPIVVHCSAGVGRTGTFIVIDAMIDMMHAEQKVDVFEFVSRIRNQRPQMVQTDMQYSFIYQALLE 229
R-PTPc-F-1 cd14626
catalytic domain of receptor-type tyrosine-protein phosphatase F, repeat 1; Receptor-type ...
 572-845 9.85e-81

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: 9.85e-81
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578801331  572 LLETYKRKIADEGRLFLAEFQSI-PRvfSKFPIKEARKPFNQNKNRYVDILPYDYNRVELSEINGDAGSNYINASYIDGF 650
Cdd:cd14626     3 LADNIERLKANDGLKFSQEYESIdPG--QQFTWENSNLEVNKPKNRYANVIAYDHSRVILTSVDGVPGSDYINANYIDGY 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578801331  651 KEPRKYIAAQGPRDETVDDFWRMIWEQKATVIVMVTRCEEGNRNKCAEYWPSmeEGTRAFGDVVVKINQHKRCPDYIIQK 730
Cdd:cd14626    81 RKQNAYIATQGPLPETLSDFWRMVWEQRTATIVMMTRLEEKSRVKCDQYWPI--RGTETYGMIQVTLLDTVELATYSVRT 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578801331  731 LNiVNKKEKATGREVTHIQFTSWPDHGVPEDPHLLLKLRRRVNAFSNFFSGPIVVHCSAGVGRTGTYIGIDAMLEGLEAE 810
Cdd:cd14626   159 FA-LYKNGSSEKREVRQFQFMAWPDHGVPEYPTPILAFLRRVKACNPPDAGPMVVHCSAGVGRTGCFIVIDAMLERMKHE 237

                         250       260       270
                  ....*....|....*....|....*....|....*
gi 578801331  811 NKVDVYGYVVKLRRQRCLMVQVEAQYILIHQALVE 845
Cdd:cd14626   238 KTVDIYGHVTCMRSQRNYMVQTEDQYIFIHEALLE 272
PTPc-N9 cd14543
catalytic domain of tyrosine-protein phosphatase non-receptor type 9; Tyrosine-protein ...
 606-840 1.33e-80

catalytic domain of tyrosine-protein phosphatase non-receptor type 9; Tyrosine-protein phosphatase non-receptor type 9 (PTPN9), also called protein-tyrosine phosphatase MEG2, belongs to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. PTPN9 plays an important role in promoting intracellular secretary vesicle fusion in hematopoietic cells and promotes the dephosphorylation of ErbB2 and EGFR in breast cancer cells, leading to impaired activation of STAT5 and STAT3. It also directly dephosphorylates STAT3 at the Tyr705 residue, resulting in its inactivation. PTPN9 has been found to be dysregulated in various human cancers, including breast, colorectal, and gastric cancer.


Pssm-ID: 350391 [Multi-domain]  Cd Length: 271  Bit Score: 265.38  E-value: 1.33e-80
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578801331  606 ARKPFNQNKNRYVDILPYDYNRVELSEINGDAGSNYINASYIDGFKEPRKYIAAQGPRDETVDDFWRMIWEQKATVIVMV 685
Cdd:cd14543    24 SLAPANQEKNRYGDVLCLDQSRVKLPKRNGDERTDYINANFMDGYKQKNAYIATQGPLPKTYSDFWRMVWEQKVLVIVMT 103

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578801331  686 TRCEEGNRNKCAEYWPSMEEGTRAFGDVVVkINQHKRC-PDYIIQKLNIVNKKEKATgREVTHIQFTSWPDHGVPEDPHL 764
Cdd:cd14543   104 TRVVERGRVKCGQYWPLEEGSSLRYGDLTV-TNLSVENkEHYKKTTLEIHNTETDES-RQVTHFQFTSWPDFGVPSSAAA 181

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578801331  765 LL--------KLRRRVNAFSNFFSG-----PIVVHCSAGVGRTGTYIGIDAMLEGLEAENKVDVYGYVVKLRRQRCLMVQ 831
Cdd:cd14543   182 LLdflgevrqQQALAVKAMGDRWKGhppgpPIVVHCSAGIGRTGTFCTLDICLSQLEDVGTLNVMQTVRRMRTQRAFSIQ 261


                  ....*....
gi 578801331  832 VEAQYILIH 840
Cdd:cd14543   262 TPDQYYFCY 270
R-PTPc-H cd14619
catalytic domain of receptor-type tyrosine-protein phosphatase H; Receptor-type ...
 615-846 3.94e-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: 3.94e-77
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578801331  615 NRYVDILPYDYNRVELSEINGDAGSNYINASYIDGFKEPRKYIAAQGPRDETVDDFWRMIWEQKATVIVMVTRCEEGNRN 694
Cdd:cd14619     1 NRFRNVLPYDWSRVPLKPIHEEPGSDYINANYMPGYWSSQEFIATQGPLPQTVGDFWRMIWEQQSSTIVMLTNCMEAGRV 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578801331  695 KCAEYWPsMEEGTRAFGDVVVKINQHKRCPDYIIQKLNIVNKKEKATgREVTHIQFTSWPDHGVPEDPHLLLKLRRRVNA 774
Cdd:cd14619    81 KCEHYWP-LDYTPCTYGHLRVTVVSEEVMENWTVREFLLKQVEEQKT-LSVRHFHFTAWPDHGVPSSTDTLLAFRRLLRQ 158

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 578801331  775 F--SNFFSGPIVVHCSAGVGRTGTYIGIDAMLEGLEAENKVDVYGYVVKLRRQRCLMVQVEAQYILIHQALVEY 846
Cdd:cd14619   159 WldQTMSGGPTVVHCSAGVGRTGTLIALDVLLQQLQSEGLLGPFSFVQKMRENRPLMVQTESQYVFLHQCILDF 232
R-PTPc-A-E-1 cd14551
catalytic domain of receptor-type tyrosine-protein phosphatase A and E, repeat 1; ...
 641-841 8.53e-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: 8.53e-76
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578801331  641 YINASYIDGFKEPRKYIAAQGPRDETVDDFWRMIWEQKATVIVMVTRCEEGNRNKCAEYWPsmEEGTRAFGDVVVKINQH 720
Cdd:cd14551     1 YINASYIDGYQEKNKFIAAQGPKDETVNDFWRMIWEQGSATIVMVTNLKERKEKKCSQYWP--DQGCWTYGNLRVRVEDT 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578801331  721 KRCPDYIIQKLnIVNKKEKATG----REVTHIQFTSWPDHGVPEDPHLLLKLRRRVNAFSNFFSGPIVVHCSAGVGRTGT 796
Cdd:cd14551    79 VVLVDYTTRKF-CIQKVNRGIGekrvRLVTQFHFTSWPDFGVPFTPIGMLKFLKKVKSANPPRAGPIVVHCSAGVGRTGT 157

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*
gi 578801331  797 YIGIDAMLEGLEAENKVDVYGYVVKLRRQRCLMVQVEAQYILIHQ 841
Cdd:cd14551   158 FIVIDAMLDMMHAEGKVDVFGFVSRIRQQRSQMVQTDMQYVFIYQ 202
R-PTPc-B cd14617
catalytic domain of receptor-type tyrosine-protein phosphatase B; Receptor-type ...
 615-841 6.66e-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: 6.66e-75
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578801331  615 NRYVDILPYDYNRVELSEINGDAGSNYINASYIDGFKEPRKYIAAQGPRDETVDDFWRMIWEQKATVIVMVTRCEEGNRN 694
Cdd:cd14617     1 NRYNNILPYDSTRVKLSNVDDDPCSDYINASYIPGNNFRREYIATQGPLPGTKDDFWKMVWEQNVHNIVMVTQCVEKGRV 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578801331  695 KCAEYWPsMEEGTRAFGDVVVKINQHKRCPDYIIQKLNIVNKKEKATGREVTHIQFTSWPDHGVPEDPHLLLKLRRRVNA 774
Cdd:cd14617    81 KCDHYWP-ADQDSLYYGDLIVQMLSESVLPEWTIREFKICSEEQLDAPRLVRHFHYTVWPDHGVPETTQSLIQFVRTVRD 159

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 578801331  775 FSNFF--SGPIVVHCSAGVGRTGTYIGIDAMLEGLEAENKVDVYGYVVKLRRQRCLMVQVEAQYILIHQ 841
Cdd:cd14617   160 YINRTpgSGPTVVHCSAGVGRTGTFIALDRILQQLDSKDSVDIYGAVHDLRLHRVHMVQTECQYVYLHQ 228
R-PTPc-J cd14615
catalytic domain of receptor-type tyrosine-protein phosphatase J; Receptor-type ...
 615-841 1.79e-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: 1.79e-74
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578801331  615 NRYVDILPYDYNRVELSeINGDAGSNYINASYIDGFKEPRKYIAAQGPRDETVDDFWRMIWEQKATVIVMVTRCEEGNRN 694
Cdd:cd14615     1 NRYNNVLPYDISRVKLS-VQSHSTDDYINANYMPGYNSKKEFIAAQGPLPNTVKDFWRMVWEKNVYAIVMLTKCVEQGRT 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578801331  695 KCAEYWPSmeEGTRAFGDVVVKINQHKRCPDYIIQKLNIVNKKEkATGREVTHIQFTSWPDHGVPEDPHLLLKLRRRVNA 774
Cdd:cd14615    80 KCEEYWPS--KQKKDYGDITVTMTSEIVLPEWTIRDFTVKNAQT-NESRTVRHFHFTSWPDHGVPETTDLLINFRHLVRE 156

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 578801331  775 FS--NFFSGPIVVHCSAGVGRTGTYIGIDAMLEGLEAENKVDVYGYVVKLRRQRCLMVQVEAQYILIHQ 841
Cdd:cd14615   157 YMkqNPPNSPILVHCSAGVGRTGTFIAIDRLIYQIENENVVDVYGIVYDLRMHRPLMVQTEDQYVFLNQ 225
R-PTPc-S-1 cd14625
catalytic domain of receptor-type tyrosine-protein phosphatase S, repeat 1; Receptor-type ...
 566-845 6.90e-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: 6.90e-73
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578801331  566 PIHADILLETYKRKIADEGRLFLAEFQSIPRvFSKFPIKEARKPFNQNKNRYVDILPYDYNRVELSEINGDAGSNYINAS 645
Cdd:cd14625     3 PIPISELAEHTERLKANDNLKLSQEYESIDP-GQQFTWEHSNLEVNKPKNRYANVIAYDHSRVILQPIEGIMGSDYINAN 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578801331  646 YIDGFKEPRKYIAAQGPRDETVDDFWRMIWEQKATVIVMVTRCEEGNRNKCAEYWPSmeEGTRAFGDVVVKINQHKRCPD 725
Cdd:cd14625    82 YIDGYRKQNAYIATQGPLPETFGDFWRMVWEQRSATVVMMTKLEEKSRIKCDQYWPS--RGTETYGMIQVTLLDTIELAT 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578801331  726 YIIQKLNIvNKKEKATGREVTHIQFTSWPDHGVPEDPHLLLKLRRRVNAFSNFFSGPIVVHCSAGVGRTGTYIGIDAMLE 805
Cdd:cd14625   160 FCVRTFSL-HKNGSSEKREVRQFQFTAWPDHGVPEYPTPFLAFLRRVKTCNPPDAGPIVVHCSAGVGRTGCFIVIDAMLE 238

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|
gi 578801331  806 GLEAENKVDVYGYVVKLRRQRCLMVQVEAQYILIHQALVE 845
Cdd:cd14625   239 RIKHEKTVDIYGHVTLMRSQRNYMVQTEDQYSFIHDALLE 278
R-PTPc-D-1 cd14624
catalytic domain of receptor-type tyrosine-protein phosphatase D, repeat 1; Receptor-type ...
 566-845 1.10e-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: 1.10e-72
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578801331  566 PIHADILLETYKRKIADEGRLFLAEFQSIPRvFSKFPIKEARKPFNQNKNRYVDILPYDYNRVELSEINGDAGSNYINAS 645
Cdd:cd14624     3 PIPILELADHIERLKANDNLKFSQEYESIDP-GQQFTWEHSNLEVNKPKNRYANVIAYDHSRVLLSAIEGIPGSDYINAN 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578801331  646 YIDGFKEPRKYIAAQGPRDETVDDFWRMIWEQKATVIVMVTRCEEGNRNKCAEYWPSmeEGTRAFGDVVVKINQHKRCPD 725
Cdd:cd14624    82 YIDGYRKQNAYIATQGALPETFGDFWRMIWEQRSATVVMMTKLEERSRVKCDQYWPS--RGTETYGLIQVTLLDTVELAT 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578801331  726 YIIQKLNIVnKKEKATGREVTHIQFTSWPDHGVPEDPHLLLKLRRRVNAFSNFFSGPIVVHCSAGVGRTGTYIGIDAMLE 805
Cdd:cd14624   160 YCVRTFALY-KNGSSEKREVRQFQFTAWPDHGVPEHPTPFLAFLRRVKTCNPPDAGPMVVHCSAGVGRTGCFIVIDAMLE 238

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|
gi 578801331  806 GLEAENKVDVYGYVVKLRRQRCLMVQVEAQYILIHQALVE 845
Cdd:cd14624   239 RIKHEKTVDIYGHVTLMRAQRNYMVQTEDQYIFIHDALLE 278
PTPc-KIM cd14547
catalytic domain of the kinase interaction motif (KIM) family of protein-tyrosine phosphatases; ...
 615-841 2.61e-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: 2.61e-72
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578801331  615 NRYVDILPYDYNRVELSEINGDAGSNYINASYIDGFK-EPRKYIAAQGPRDETVDDFWRMIWEQKATVIVMVTRCEEGNR 693
Cdd:cd14547     1 NRYKTILPNEHSRVCLPSVDDDPLSSYINANYIRGYDgEEKAYIATQGPLPNTVADFWRMVWQEKTPIIVMITNLTEAKE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578801331  694 nKCAEYWPsMEEGTRaFGDVVVKINQHKRCPDYIIQKLNIVNKKEKatgREVTHIQFTSWPDHGVPEDPHLLLKLRRRVN 773
Cdd:cd14547    81 -KCAQYWP-EEENET-YGDFEVTVQSVKETDGYTVRKLTLKYGGEK---RYLKHYWYTSWPDHKTPEAAQPLLSLVQEVE 154

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578801331  774 --AFSNFFSGPIVVHCSAGVGRTGTYIGIDAMLEGLEAENKVDVYGYVVKLRRQRCLMVQVEAQYILIHQ 841
Cdd:cd14547   155 eaRQTEPHRGPIVVHCSAGIGRTGCFIATSIGCQQLREEGVVDVLGIVCQLRLDRGGMVQTAEQYEFVHR 224
R-PTPc-O cd14614
catalytic domain of receptor-type tyrosine-protein phosphatase O; Receptor-type ...
 606-841 4.95e-72

catalytic domain of receptor-type tyrosine-protein phosphatase O; Receptor-type tyrosine-protein phosphatase O (PTPRO or R-PTP-O), also known as glomerular epithelial protein 1 or protein tyrosine phosphatase U2 (PTP-U2), belongs to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. PTPRO is a member of the R3 subfamily of receptor-type phosphotyrosine phosphatases (RPTP), characterized by a unique modular composition consisting of multiple extracellular fibronectin type III (FN3) repeats and a single (most RPTP subtypes have two) cytoplasmic catalytic PTP domain. It is essential for sustaining the structure and function of foot processes by regulating tyrosine phosphorylation of podocyte proteins. It has been identified as a synaptic cell adhesion molecule (CAM) that serves as a potent initiator of synapse formation. It is also a tumor suppressor in several types of cancer, such as hepatocellular carcinoma, lung cancer, and breast cancer.


Pssm-ID: 350462 [Multi-domain]  Cd Length: 245  Bit Score: 240.56  E-value: 4.95e-72
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578801331  606 ARKPFNQNKNRYVDILPYDYNRVELSEINGDAGSNYINASYIDGFKEPRKYIAAQGPRDETVDDFWRMIWEQKATVIVMV 685
Cdd:cd14614     7 ADLPVNRCKNRYTNILPYDFSRVKLVSMHEEEGSDYINANYIPGYNSPQEYIATQGPLPETRNDFWKMVLQQKSQIIVML 86

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578801331  686 TRCEEGNRNKCAEYWPSMEEGTrAFGDVVVKINQHKRCPDYIIQKLNIVNKKEKatgREVTHIQFTSWPDHGVP--EDPH 763
Cdd:cd14614    87 TQCNEKRRVKCDHYWPFTEEPV-AYGDITVEMLSEEEQPDWAIREFRVSYADEV---QDVMHFNYTAWPDHGVPtaNAAE 162

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 578801331  764 LLLKLRRRVNAFSNFFSGPIVVHCSAGVGRTGTYIGIDAMLEGLEAENKVDVYGYVVKLRRQRCLMVQVEAQYILIHQ 841
Cdd:cd14614   163 SILQFVQMVRQQAVKSKGPMIIHCSAGVGRTGTFIALDRLLQHIRDHEFVDILGLVSEMRSYRMSMVQTEEQYIFIHQ 240
R-PTPc-G-1 cd17667
catalytic domain of receptor-type tyrosine-protein phosphatase G, repeat 1; Receptor-type ...
 587-845 5.62e-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: 5.62e-71
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578801331  587 FLAEFQSIPRVFSKFPI--KEARKPFNQNKNRYVDILPYDYNRVELSEINGDAG--SNYINASYIDGFKEPRKYIAAQGP 662
Cdd:cd17667     1 FSEDFEEVQRCTADMNItaEHSNHPDNKHKNRYINILAYDHSRVKLRPLPGKDSkhSDYINANYVDGYNKAKAYIATQGP 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578801331  663 RDETVDDFWRMIWEQKATVIVMVTRCEEGNRNKCAEYWPSmeEGTRAFGDVVVKINQHKRCPDYIIQKLNIVNKKEK--- 739
Cdd:cd17667    81 LKSTFEDFWRMIWEQNTGIIVMITNLVEKGRRKCDQYWPT--ENSEEYGNIIVTLKSTKIHACYTVRRFSIRNTKVKkgq 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578801331  740 ---ATGRE----VTHIQFTSWPDHGVPEDPHLLLKLRRRVNAFSNFFSGPIVVHCSAGVGRTGTYIGIDAMLEGLEAENK 812
Cdd:cd17667   159 kgnPKGRQnertVIQYHYTQWPDMGVPEYALPVLTFVRRSSAARTPEMGPVLVHCSAGVGRTGTYIVIDSMLQQIKDKST 238

                         250       260       270
                  ....*....|....*....|....*....|...
gi 578801331  813 VDVYGYVVKLRRQRCLMVQVEAQYILIHQALVE 845
Cdd:cd17667   239 VNVLGFLKHIRTQRNYLVQTEEQYIFIHDALLE 271
R-PTPc-T-1 cd14630
catalytic domain of receptor-type tyrosine-protein phosphatase T, repeat 1; Receptor-type ...
 611-845 1.85e-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: 1.85e-70
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578801331  611 NQNKNRYVDILPYDYNRVELSEINGDAGSNYINASYIDGFKEPRKYIAAQGPRDETVDDFWRMIWEQKATVIVMVTRCEE 690
Cdd:cd14630     3 NRNKNRYGNIISYDHSRVRLQLLDGDPHSDYINANYIDGYHRPRHYIATQGPMQETVKDFWRMIWQENSASVVMVTNLVE 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578801331  691 GNRNKCAEYWPsmeEGTRAFGDVVVKINQHKRCPDYIIQKLNiVNKKEKATGREVTHIQFTSWPDHGVPEDPHLLLKLRR 770
Cdd:cd14630    83 VGRVKCVRYWP---DDTEVYGDIKVTLIETEPLAEYVIRTFT-VQKKGYHEIREIRQFHFTSWPDHGVPCYATGLLGFVR 158

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 578801331  771 RVNAFSNFFSGPIVVHCSAGVGRTGTYIGIDAMLEGLEAENKVDVYGYVVKLRRQRCLMVQVEAQYILIHQALVE 845
Cdd:cd14630   159 QVKFLNPPDAGPIVVHCSAGAGRTGCFIAIDIMLDMAENEGVVDIFNCVRELRAQRVNMVQTEEQYVFVHDAILE 233
PTPc-N11_6 cd14544
catalytic domain of tyrosine-protein phosphatase non-receptor type 11 and type 6; ...
 611-846 6.15e-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: 6.15e-69
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578801331  611 NQNKNRYVDILPYDYNRVELSEINGD-AGSNYINASYI-------DGFKEPRKYIAAQGPRDETVDDFWRMIWEQKATVI 682
Cdd:cd14544     1 NKGKNRYKNILPFDHTRVILKDRDPNvPGSDYINANYIrnenegpTTDENAKTYIATQGCLENTVSDFWSMVWQENSRVI 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578801331  683 VMVTRCEEGNRNKCAEYWPSmEEGTRAFGDVVVKINQHKRCPDYIIQKLNIVNKKEKATGREVTHIQFTSWPDHGVPEDP 762
Cdd:cd14544    81 VMTTKEVERGKNKCVRYWPD-EGMQKQYGPYRVQNVSEHDTTDYTLRELQVSKLDQGDPIREIWHYQYLSWPDHGVPSDP 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578801331  763 HLLLKLRRRVNAFSNFF--SGPIVVHCSAGVGRTGTYIGIDAMLE-----GLEAEnkVDVYGYVVKLRRQRCLMVQVEAQ 835
Cdd:cd14544   160 GGVLNFLEDVNQRQESLphAGPIVVHCSAGIGRTGTFIVIDMLLDqikrkGLDCD--IDIQKTIQMVRSQRSGMVQTEAQ 237

                         250
                  ....*....|.
gi 578801331  836 YILIHQALVEY 846
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 ...
 606-842 7.90e-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: 230.87  E-value: 7.90e-69
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578801331  606 ARKPFNQNKNRYVDILPYDYNRVELSEINGDAGSNYINASYIDGFKEPRKYIAAQGPRDETVDDFWRMIWEQKATVIVMV 685
Cdd:cd14554     1 ANLPCNKFKNRLVNILPYESTRVCLQPIRGVEGSDYINASFIDGYRQRGAYIATQGPLAETTEDFWRMLWEHNSTIIVML 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578801331  686 TRCEEGNRNKCAEYWPSmEEGTRAFGDVVVKINQHKRcPDYIIQKLNIVNKKEKaTGREVTHIQFTSWPDHGVPEDPHLL 765
Cdd:cd14554    81 TKLREMGREKCHQYWPA-ERSARYQYFVVDPMAEYNM-PQYILREFKVTDARDG-QSRTVRQFQFTDWPEQGVPKSGEGF 157

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 578801331  766 LKLRRRV-NAFSNF-FSGPIVVHCSAGVGRTGTYIGIDAMLEGLEAENKVDVYGYVVKLRRQRCLMVQVEAQYILIHQA 842
Cdd:cd14554   158 IDFIGQVhKTKEQFgQEGPITVHCSAGVGRTGVFITLSIVLERMRYEGVVDVFQTVKLLRTQRPAMVQTEDQYQFCYRA 236
PTP_fungal cd18533
fungal protein tyrosine phosphatases; This subfamily contains Saccharomyces cerevisiae ...
 641-841 8.25e-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: 224.05  E-value: 8.25e-67
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578801331  641 YINASYID-GFKEPRKYIAAQGPRDETVDDFWRMIWEQKATVIVMVTRCEEGNRNKCAEYWPSmEEGTRAFGDVVVKINQ 719
Cdd:cd18533     1 YINASYITlPGTSSKRYIATQGPLPATIGDFWKMIWQNNVGVIVMLTPLVENGREKCDQYWPS-GEYEGEYGDLTVELVS 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578801331  720 HKRCPDYIIQKLNIVNKKEKATGREVTHIQFTSWPDHGVPEDPHLLLKLRRRVNA--FSNFFSGPIVVHCSAGVGRTGTY 797
Cdd:cd18533    80 EEENDDGGFIVREFELSKEDGKVKKVYHIQYKSWPDFGVPDSPEDLLTLIKLKRElnDSASLDPPIIVHCSAGVGRTGTF 159

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 578801331  798 IGIDAMLEGLEA--------ENKVD-VYGYVVKLRRQRCLMVQVEAQYILIHQ 841
Cdd:cd18533   160 IALDSLLDELKRglsdsqdlEDSEDpVYEIVNQLRKQRMSMVQTLRQYIFLYD 212
R-PTPc-M-1 cd14633
catalytic domain of receptor-type tyrosine-protein phosphatase M, repeat 1; Receptor-type ...
 570-845 4.17e-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: 224.54  E-value: 4.17e-66
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578801331  570 DILLETYKRKIAdEGRLFLAEFQSIPRVFSKfPIKEARKPFNQNKNRYVDILPYDYNRVELSEINGDAGSNYINASYIDG 649
Cdd:cd14633     1 DLLQHITQMKCA-EGYGFKEEYESFFEGQSA-PWDSAKKDENRMKNRYGNIIAYDHSRVRLQPIEGETSSDYINGNYIDG 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578801331  650 FKEPRKYIAAQGPRDETVDDFWRMIWEQKATVIVMVTRCEEGNRNKCAEYWPsmeEGTRAFGDVVVKINQHKRCPDYIIQ 729
Cdd:cd14633    79 YHRPNHYIATQGPMQETIYDFWRMVWHENTASIIMVTNLVEVGRVKCCKYWP---DDTEIYKDIKVTLIETELLAEYVIR 155

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578801331  730 KLnIVNKKEKATGREVTHIQFTSWPDHGVPEDPHLLLKLRRRVNAFSNFFSGPIVVHCSAGVGRTGTYIGIDAMLEGLEA 809
Cdd:cd14633   156 TF-AVEKRGVHEIREIRQFHFTGWPDHGVPYHATGLLGFVRQVKSKSPPNAGPLVVHCSAGAGRTGCFIVIDIMLDMAER 234

                         250       260       270
                  ....*....|....*....|....*....|....*.
gi 578801331  810 ENKVDVYGYVVKLRRQRCLMVQVEAQYILIHQALVE 845
Cdd:cd14633   235 EGVVDIYNCVRELRSRRVNMVQTEEQYVFIHDAILE 270
R-PTPc-V cd14618
catalytic domain of receptor-type tyrosine-protein phosphatase V; Receptor-type ...
 615-844 4.48e-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: 222.90  E-value: 4.48e-66
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578801331  615 NRYVDILPYDYNRVELSEINGDAGSNYINASYIDGFKEPRKYIAAQGPRDETVDDFWRMIWEQKATVIVMVTRCEEGNRN 694
Cdd:cd14618     1 NRYPHVLPYDHSRVRLSQLGGEPHSDYINANFIPGYTSPQEFIATQGPLKKTIEDFWRLVWEQQVCNIIMLTVGMENGRV 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578801331  695 KCAEYWPSmEEGTRAFGDVVVKINQHKRCPDYIIQKLNIVNKKEKATgREVTHIQFTSWPDHGVPEDPHLLLKLRRRVNA 774
Cdd:cd14618    81 LCDHYWPS-ESTPVSYGHITVHLLAQSSEDEWTRREFKLWHEDLRKE-RRVKHLHYTAWPDHGIPESTSSLMAFRELVRE 158

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 578801331  775 F--SNFFSGPIVVHCSAGVGRTGTYIGIDAMLEGLEAENKVDVYGYVVKLRRQRCLMVQVEAQYILIHQALV 844
Cdd:cd14618   159 HvqATKGKGPTLVHCSAGVGRSGTFIALDRLLRQLKEEKVVDVFNTVYILRMHRYLMIQTLSQYIFLHSCIL 230
R-PTPc-Z-1 cd17668
catalytic domain of receptor-type tyrosine-protein phosphatase Z, repeat 1; Receptor-type ...
 641-844 3.94e-64

catalytic domain of receptor-type tyrosine-protein phosphatase Z, repeat 1; Receptor-type tyrosine-protein phosphatase Z (PTPRZ), also called receptor-type tyrosine-protein phosphatase zeta (R-PTP-zeta), belongs to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. Three isoforms are generated by alternative splicing from a single PTPRZ gene: two transmembrane isoforms, PTPRZ-A and PTPRZ-B, and one secretory isoform, PTPRZ-S (also known as phosphacan); all are preferentially expressed in the central nervous system (CNS) as chondroitin sulfate (CS) proteoglycans. PTPRZ isoforms play important roles in maintaining oligodendrocyte precursor cells in an undifferentiated state. PTPRZ is a type 1 integral membrane protein consisting of an extracellular region with a carbonic anhydrase-like (CAH) and a fibronectin type III (FN3) domains, and an intracellular region with a catalytic PTP domain (repeat 1) proximal to the membrane, and a catalytically inactive PTP-fold domain (repeat 2) distal to the membrane. This model represents the catalytic PTP domain (repeat 1).


Pssm-ID: 350506 [Multi-domain]  Cd Length: 209  Bit Score: 216.38  E-value: 3.94e-64
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578801331  641 YINASYIDGFKEPRKYIAAQGPRDETVDDFWRMIWEQKATVIVMVTRCEEGNRNKCAEYWPSmeEGTRAFGDVVVKINQH 720
Cdd:cd17668     1 YINANYVDGYNKPKAYIAAQGPLKSTAEDFWRMIWEHNVEVIVMITNLVEKGRRKCDQYWPA--DGSEEYGNFLVTQKSV 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578801331  721 KRCPDYIIQKLNIVN-------KKEKATGREVTHIQFTSWPDHGVPEDPHLLLKLRRRVNAFSNFFSGPIVVHCSAGVGR 793
Cdd:cd17668    79 QVLAYYTVRNFTLRNtkikkgsQKGRPSGRVVTQYHYTQWPDMGVPEYTLPVLTFVRKASYAKRHAVGPVVVHCSAGVGR 158

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|.
gi 578801331  794 TGTYIGIDAMLEGLEAENKVDVYGYVVKLRRQRCLMVQVEAQYILIHQALV 844
Cdd:cd17668   159 TGTYIVLDSMLQQIQHEGTVNIFGFLKHIRSQRNYLVQTEEQYVFIHDALV 209
R-PTPc-Q cd14616
catalytic domain of receptor-type tyrosine-protein phosphatase Q; Receptor-type ...
 615-841 1.15e-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: 1.15e-63
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578801331  615 NRYVDILPYDYNRVELSEINGDAGSNYINASYIDGFKEPRKYIAAQGPRDETVDDFWRMIWEQKATVIVMVTRCEEGNRN 694
Cdd:cd14616     1 NRFPNIKPYNNNRVKLIADAGVPGSDYINASYISGYLCPNEFIATQGPLPGTVGDFWRMVWETRAKTIVMLTQCFEKGRI 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578801331  695 KCAEYWPSMEEGTRAFGDVVVKINQHKRCPDYIIQKLNIVNKKEKATgreVTHIQFTSWPDHGVPEDPHLLLKLRRRVNA 774
Cdd:cd14616    81 RCHQYWPEDNKPVTVFGDIVITKLMEDVQIDWTIRDLKIERHGDYMM---VRQCNFTSWPEHGVPESSAPLIHFVKLVRA 157

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 578801331  775 FSNFFSGPIVVHCSAGVGRTGTYIGIDAMLEGLEAENKVDVYGYVVKLRRQRCLMVQVEAQYILIHQ 841
Cdd:cd14616   158 SRAHDNTPMIVHCSAGVGRTGVFIALDHLTQHINDHDFVDIYGLVAELRSERMCMVQNLAQYIFLHQ 224
R-PTPc-typeIIb-1 cd14555
catalytic domain of type IIb (or R2B) subfamily receptor-type tyrosine-protein phosphatases, ...
 641-845 6.19e-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: 212.85  E-value: 6.19e-63
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578801331  641 YINASYIDGFKEPRKYIAAQGPRDETVDDFWRMIWEQKATVIVMVTRCEEGNRNKCAEYWPsmeEGTRAFGDVVVKINQH 720
Cdd:cd14555     1 YINANYIDGYHRPNHYIATQGPMQETVYDFWRMVWQENSASIVMVTNLVEVGRVKCSRYWP---DDTEVYGDIKVTLVET 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578801331  721 KRCPDYIIQKLNiVNKKEKATGREVTHIQFTSWPDHGVPEDPHLLLKLRRRVNAFSNFFSGPIVVHCSAGVGRTGTYIGI 800
Cdd:cd14555    78 EPLAEYVVRTFA-LERRGYHEIREVRQFHFTGWPDHGVPYHATGLLGFIRRVKASNPPSAGPIVVHCSAGAGRTGCYIVI 156

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*
gi 578801331  801 DAMLEGLEAENKVDVYGYVVKLRRQRCLMVQVEAQYILIHQALVE 845
Cdd:cd14555   157 DIMLDMAEREGVVDIYNCVKELRSRRVNMVQTEEQYIFIHDAILE 201
PTPc-N6 cd14606
catalytic domain of tyrosine-protein phosphatase non-receptor type 6; Tyrosine-protein ...
 604-846 9.54e-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: 9.54e-62
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578801331  604 KEARKPFNQNKNRYVDILPYDYNRVELSeiNGDA---GSNYINASYID----GFKEPRK-YIAAQGPRDETVDDFWRMIW 675
Cdd:cd14606    11 LEGQRPENKSKNRYKNILPFDHSRVILQ--GRDSnipGSDYINANYVKnqllGPDENAKtYIASQGCLEATVNDFWQMAW 88

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578801331  676 EQKATVIVMVTRCEEGNRNKCAEYWPSMeEGTRAFGDVVVKINQHKRCPDYIIQKLNIVNKKEKATGREVTHIQFTSWPD 755
Cdd:cd14606    89 QENSRVIVMTTREVEKGRNKCVPYWPEV-GMQRAYGPYSVTNCGEHDTTEYKLRTLQVSPLDNGELIREIWHYQYLSWPD 167

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578801331  756 HGVPEDPHLLLKLRRRVNAFSNFF--SGPIVVHCSAGVGRTGTYIGIDAMLEGLEAEN---KVDVYGYVVKLRRQRCLMV 830
Cdd:cd14606   168 HGVPSEPGGVLSFLDQINQRQESLphAGPIIVHCSAGIGRTGTIIVIDMLMENISTKGldcDIDIQKTIQMVRAQRSGMV 247

                         250
                  ....*....|....*.
gi 578801331  831 QVEAQYILIHQALVEY 846
Cdd:cd14606   248 QTEAQYKFIYVAIAQF 263
PTPc-N20_13 cd14538
catalytic domain of tyrosine-protein phosphatase non-receptor type 20 and type 13; ...
 641-845 6.90e-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: 6.90e-61
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578801331  641 YINASYI--DGFKEPRKYIAAQGPRDETVDDFWRMIWEQKATVIVMVTRCEEGNRNKCAEYWP-SMEEGTRAFGDVVVKI 717
Cdd:cd14538     1 YINASHIriPVGGDTYHYIACQGPLPNTTGDFWQMVWEQKSEVIAMVTQDVEGGKVKCHRYWPdSLNKPLICGGRLEVSL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578801331  718 NQHKRCPDYIIQKLNIvnkKEKATG--REVTHIQFTSWPDHGVPEDPHLLLKLRRRVNAFSNffSGPIVVHCSAGVGRTG 795
Cdd:cd14538    81 EKYQSLQDFVIRRISL---RDKETGevHHITHLNFTTWPDHGTPQSADPLLRFIRYMRRIHN--SGPIVVHCSAGIGRTG 155

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|
gi 578801331  796 TYIGIDAMLEGLEAENKVDVYGYVVKLRRQRCLMVQVEAQYILIHQALVE 845
Cdd:cd14538   156 VLITIDVALGLIERDLPFDIQDIVKDLREQRQGMIQTKDQYIFCYKACLE 205
R-PTP-S-2 cd14627
PTP-like domain of receptor-type tyrosine-protein phosphatase S, repeat 2; Receptor-type ...
 606-846 6.92e-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: 6.92e-61
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578801331  606 ARKPFNQNKNRYVDILPYDYNRVELSEINGDAGSNYINASYIDGFKEPRKYIAAQGPRDETVDDFWRMIWEQKATVIVMV 685
Cdd:cd14627    48 ANLPCNKFKNRLVNIMPYETTRVCLQPIRGVEGSDYINASFIDGYRQQKAYIATQGPLAETTEDFWRMLWENNSTIVVML 127

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578801331  686 TRCEEGNRNKCAEYWPSmeEGTRAFGDVVVKINQHKRCPDYIIQKLNIVNKKEkATGREVTHIQFTSWPDHGVPEDPHLL 765
Cdd:cd14627   128 TKLREMGREKCHQYWPA--ERSARYQYFVVDPMAEYNMPQYILREFKVTDARD-GQSRTVRQFQFTDWPEQGVPKSGEGF 204

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578801331  766 LKLRRRVNAFSNFF--SGPIVVHCSAGVGRTGTYIGIDAMLEGLEAENKVDVYGYVVKLRRQRCLMVQVEAQYILIHQAL 843
Cdd:cd14627   205 IDFIGQVHKTKEQFgqDGPISVHCSAGVGRTGVFITLSIVLERMRYEGVVDIFQTVKMLRTQRPAMVQTEDEYQFCYQAA 284


                  ...
gi 578801331  844 VEY 846
Cdd:cd14627   285 LEY 287
R-PTP-D-2 cd14628
PTP-like domain of receptor-type tyrosine-protein phosphatase D, repeat 2; Receptor-type ...
 606-846 1.22e-60

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


Pssm-ID: 350476 [Multi-domain]  Cd Length: 292  Bit Score: 209.97  E-value: 1.22e-60
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578801331  606 ARKPFNQNKNRYVDILPYDYNRVELSEINGDAGSNYINASYIDGFKEPRKYIAAQGPRDETVDDFWRMIWEQKATVIVMV 685
Cdd:cd14628    47 ANLPCNKFKNRLVNIMPYESTRVCLQPIRGVEGSDYINASFIDGYRQQKAYIATQGPLAETTEDFWRMLWEHNSTIVVML 126

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578801331  686 TRCEEGNRNKCAEYWPSmeEGTRAFGDVVVKINQHKRCPDYIIQKLNIVNKKEkATGREVTHIQFTSWPDHGVPEDPHLL 765
Cdd:cd14628   127 TKLREMGREKCHQYWPA--ERSARYQYFVVDPMAEYNMPQYILREFKVTDARD-GQSRTVRQFQFTDWPEQGVPKSGEGF 203

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578801331  766 LKLRRRVNAFSNFF--SGPIVVHCSAGVGRTGTYIGIDAMLEGLEAENKVDVYGYVVKLRRQRCLMVQVEAQYILIHQAL 843
Cdd:cd14628   204 IDFIGQVHKTKEQFgqDGPISVHCSAGVGRTGVFITLSIVLERMRYEGVVDIFQTVKMLRTQRPAMVQTEDQYQFCYRAA 283


                  ...
gi 578801331  844 VEY 846
Cdd:cd14628   284 LEY 286
R-PTP-F-2 cd14629
PTP-like domain of receptor-type tyrosine-protein phosphatase F, repeat 2; Receptor-type ...
 606-846 1.88e-60

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


Pssm-ID: 350477 [Multi-domain]  Cd Length: 291  Bit Score: 209.20  E-value: 1.88e-60
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578801331  606 ARKPFNQNKNRYVDILPYDYNRVELSEINGDAGSNYINASYIDGFKEPRKYIAAQGPRDETVDDFWRMIWEQKATVIVMV 685
Cdd:cd14629    48 ANLPCNKFKNRLVNIMPYELTRVCLQPIRGVEGSDYINASFIDGYRQQKAYIATQGPLAETTEDFWRMLWEHNSTIVVML 127

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578801331  686 TRCEEGNRNKCAEYWPSmeEGTRAFGDVVVKINQHKRCPDYIIQKLNIVNKKEkATGREVTHIQFTSWPDHGVPEDPHLL 765
Cdd:cd14629   128 TKLREMGREKCHQYWPA--ERSARYQYFVVDPMAEYNMPQYILREFKVTDARD-GQSRTIRQFQFTDWPEQGVPKTGEGF 204

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578801331  766 LKLRRRVNAFSNFF--SGPIVVHCSAGVGRTGTYIGIDAMLEGLEAENKVDVYGYVVKLRRQRCLMVQVEAQYILIHQAL 843
Cdd:cd14629   205 IDFIGQVHKTKEQFgqDGPITVHCSAGVGRTGVFITLSIVLERMRYEGVVDMFQTVKTLRTQRPAMVQTEDQYQLCYRAA 284


                  ...
gi 578801331  844 VEY 846
Cdd:cd14629   285 LEY 287
R-PTPc-K-1 cd14631
catalytic domain of receptor-type tyrosine-protein phosphatase K, repeat 1; Receptor-type ...
 627-845 2.71e-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: 2.71e-60
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578801331  627 RVELSEINGDAGSNYINASYIDGFKEPRKYIAAQGPRDETVDDFWRMIWEQKATVIVMVTRCEEGNRNKCAEYWPsmeEG 706
Cdd:cd14631     1 RVILQPVEDDPSSDYINANYIDGYQRPSHYIATQGPVHETVYDFWRMIWQEQSACIVMVTNLVEVGRVKCYKYWP---DD 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578801331  707 TRAFGDVVVKINQHKRCPDYIIQKLNIvNKKEKATGREVTHIQFTSWPDHGVPEDPHLLLKLRRRVNAFSNFFSGPIVVH 786
Cdd:cd14631    78 TEVYGDFKVTCVEMEPLAEYVVRTFTL-ERRGYNEIREVKQFHFTGWPDHGVPYHATGLLSFIRRVKLSNPPSAGPIVVH 156

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 578801331  787 CSAGVGRTGTYIGIDAMLEGLEAENKVDVYGYVVKLRRQRCLMVQVEAQYILIHQALVE 845
Cdd:cd14631   157 CSAGAGRTGCYIVIDIMLDMAEREGVVDIYNCVKALRSRRINMVQTEEQYIFIHDAILE 215
PTPc-N7 cd14612
catalytic domain of tyrosine-protein phosphatase non-receptor type 7; Tyrosine-protein ...
 609-846 1.09e-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: 1.09e-59
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578801331  609 PFNQNKNRYVDILPYDYNRVEL-SEINGDAGSNYINASYIDGFK-EPRKYIAAQGPRDETVDDFWRMIWEQKATVIVMVT 686
Cdd:cd14612    13 PGHASKDRYKTILPNPQSRVCLrRAGSQEEEGSYINANYIRGYDgKEKAYIATQGPMLNTVSDFWEMVWQEECPIIVMIT 92

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578801331  687 RCEEGNRnKCAEYWPSmEEGTraFGDVVVKINQHKRCPDYIIQKLNIVNKKEKatgREVTHIQFTSWPDHGVPEDPHLLL 766
Cdd:cd14612    93 KLKEKKE-KCVHYWPE-KEGT--YGRFEIRVQDMKECDGYTIRDLTIQLEEES---RSVKHYWFSSWPDHQTPESAGPLL 165

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578801331  767 KL-----RRRVNAFSnffSGPIVVHCSAGVGRTGTYIGIDAMLEGLEAENKVDVYGYVVKLRRQRCLMVQVEAQYILIHQ 841
Cdd:cd14612   166 RLvaeveESRQTAAS---PGPIVVHCSAGIGRTGCFIATSIGCQQLKDTGKVDILGIVCQLRLDRGGMIQTSEQYQFLHH 242


                  ....*
gi 578801331  842 ALVEY 846
Cdd:cd14612   243 TLALY 247
R-PTPc-A-E-2 cd14552
catalytic domain of receptor-type tyrosine-protein phosphatase A and E, repeat 2; ...
 951-1159 1.44e-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: 1.44e-59
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578801331  951 YINASFIMSYWKPEVMIAAQGPLKETIGDFWQMIFQRKVKVIVMLTELKHGDQEICAQYW-GEGKQTYGDIEVDLKDTDK 1029
Cdd:cd14552     1 YINASFIDGYRQKDAYIATQGPLDHTVEDFWRMIWEWKSCSIVMLTEIKERSQNKCAQYWpEDGSVSSGDITVELKDQTD 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578801331 1030 SSTYTLRVFELRHSKRKDSRTVYQYQYTNWSVEQLPAEPKELISMIQVVkqklpQKNSSEGNKHhkstPLLIHCRDGSQQ 1109
Cdd:cd14552    81 YEDYTLRDFLVTKGKGGSTRTVRQFHFHGWPEVGIPDNGKGMIDLIAAV-----QKQQQQSGNH----PITVHCSAGAGR 151

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|
gi 578801331 1110 TGIFCALLNLLESAETEEVVDIFQVVKALRKARPGMVSTFEQYQFLYDVI 1159
Cdd:cd14552   152 TGTFCALSTVLERVKAEGVLDVFQVVKSLRLQRPHMVQTLEQYEFCYKVV 201
R-PTPc-U-1 cd14632
catalytic domain of receptor-type tyrosine-protein phosphatase U, repeat 1; Receptor-type ...
 641-845 9.96e-58

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: 9.96e-58
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578801331  641 YINASYIDGFKEPRKYIAAQGPRDETVDDFWRMIWEQKATVIVMVTRCEEGNRNKCAEYWPsmeEGTRAFGDVVVKINQH 720
Cdd:cd14632     1 YINANYIDGYHRSNHFIATQGPKQEMVYDFWRMVWQEHCSSIVMITKLVEVGRVKCSKYWP---DDSDTYGDIKITLLKT 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578801331  721 KRCPDYIIQKLNIvNKKEKATGREVTHIQFTSWPDHGVPEDPHLLLKLRRRVNAFSNFFSGPIVVHCSAGVGRTGTYIGI 800
Cdd:cd14632    78 ETLAEYSVRTFAL-ERRGYSARHEVKQFHFTSWPEHGVPYHATGLLAFIRRVKASTPPDAGPVVVHCSAGAGRTGCYIVL 156

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*
gi 578801331  801 DAMLEGLEAENKVDVYGYVVKLRRQRCLMVQVEAQYILIHQALVE 845
Cdd:cd14632   157 DVMLDMAECEGVVDIYNCVKTLCSRRINMIQTEEQYIFIHDAILE 201
PTPc-N21_14 cd14540
catalytic domain of tyrosine-protein phosphatase non-receptor type 21 and type 14; ...
 641-846 1.43e-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: 1.43e-57
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578801331  641 YINASYID---GFKEpRKYIAAQGPRDETVDDFWRMIWEQKATVIVMVTRCEEGNRNKCAEYWPSM--EEGTRAFGD--V 713
Cdd:cd14540     1 YINASHITatvGGKQ-RFYIAAQGPLQNTVGDFWQMVWEQGVYLVVMVTAEEEGGREKCFRYWPTLggEHDALTFGEykV 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578801331  714 VVKINQHKRCpdYIIQKLNIVNKKEKaTGREVTHIQFTSWPDHGVPEDPHLLL-------KLRRRVNAFS--NFFSGPIV 784
Cdd:cd14540    80 STKFSVSSGC--YTTTGLRVKHTLSG-QSRTVWHLQYTDWPDHGCPEDVSGFLdfleeinSVRRHTNQDVagHNRNPPTL 156

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 578801331  785 VHCSAGVGRTGTYIGIDAMLEGLEAENKVDVYGYVVKLRRQRCLMVQVEAQYILIHQALVEY 846
Cdd:cd14540   157 VHCSAGVGRTGVVILADLMLYCLDHNEELDIPRVLALLRHQRMLLVQTLAQYKFVYNVLIQY 218
R-PTPc-A-2 cd14623
catalytic domain of receptor-type tyrosine-protein phosphatase A, repeat 2; Receptor-type ...
 616-845 1.76e-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: 1.76e-57
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578801331  616 RYVDILPYDYNRVELSEINGDAGSNYINASYIDGFKEPRKYIAAQGPRDETVDDFWRMIWEQKATVIVMVTRCEEGNRNK 695
Cdd:cd14623     1 RVLQIIPYEFNRVIIPVKRGEENTDYVNASFIDGYRQKDSYIASQGPLQHTIEDFWRMIWEWKSCSIVMLTELEERGQEK 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578801331  696 CAEYWPSmeEGTRAFGDVVVKINQHKRCPDYIIQKLNIVNKKEKATgREVTHIQFTSWPDHGVPEDP----HLLLKLRRR 771
Cdd:cd14623    81 CAQYWPS--DGSVSYGDITIELKKEEECESYTVRDLLVTNTRENKS-RQIRQFHFHGWPEVGIPSDGkgmiNIIAAVQKQ 157

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 578801331  772 VNAFSNFfsgPIVVHCSAGVGRTGTYIGIDAMLEGLEAENKVDVYGYVVKLRRQRCLMVQVEAQYILIHQALVE 845
Cdd:cd14623   158 QQQSGNH---PITVHCSAGAGRTGTFCALSTVLERVKAEGILDVFQTVKSLRLQRPHMVQTLEQYEFCYKVVQE 228
PTPc-N11 cd14605
catalytic domain of tyrosine-protein phosphatase non-receptor type 11; Tyrosine-protein ...
 611-846 2.01e-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: 2.01e-57
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578801331  611 NQNKNRYVDILPYDYNRVELSEinGDA---GSNYINASYI--------DGFKEPRKYIAAQGPRDETVDDFWRMIWEQKA 679
Cdd:cd14605     2 NKNKNRYKNILPFDHTRVVLHD--GDPnepVSDYINANIImpefetkcNNSKPKKSYIATQGCLQNTVNDFWRMVFQENS 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578801331  680 TVIVMVTRCEEGNRNKCAEYWPSmEEGTRAFGDVVVKINQHKRCPDYIIQKLNIVNKKEKATGREVTHIQFTSWPDHGVP 759
Cdd:cd14605    80 RVIVMTTKEVERGKSKCVKYWPD-EYALKEYGVMRVRNVKESAAHDYILRELKLSKVGQGNTERTVWQYHFRTWPDHGVP 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578801331  760 EDPHLLLKLRRRVNAFSNFFS--GPIVVHCSAGVGRTGTYIGIDAMLEGLEAEN---KVDVYGYVVKLRRQRCLMVQVEA 834
Cdd:cd14605   159 SDPGGVLDFLEEVHHKQESIMdaGPVVVHCSAGIGRTGTFIVIDILIDIIREKGvdcDIDVPKTIQMVRSQRSGMVQTEA 238

                         250
                  ....*....|..
gi 578801331  835 QYILIHQALVEY 846
Cdd:cd14605   239 QYRFIYMAVQHY 250
PTPc-N18 cd14603
catalytic domain of tyrosine-protein phosphatase non-receptor type 18; Tyrosine-protein ...
 611-845 4.74e-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: 4.74e-57
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578801331  611 NQNKNRYVDILPYDYNRVELSEINGDAGSNYINASYIDGFKEPRKYIAAQGPRDETVDDFWRMIWEQKATVIVMVTRCEE 690
Cdd:cd14603    30 NVKKNRYKDILPYDQTRVILSLLQEEGHSDYINANFIKGVDGSRAYIATQGPLSHTVLDFWRMIWQYGVKVILMACREIE 109

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578801331  691 GNRNKCAEYWPSMEEgTRAFGD-VVVKINQHKRCPDYIIQKLNIVNKKEKatgREVTHIQFTSWPDHGVPEDPHLLLKLR 769
Cdd:cd14603   110 MGKKKCERYWAQEQE-PLQTGPfTITLVKEKRLNEEVILRTLKVTFQKES---RSVSHFQYMAWPDHGIPDSPDCMLAMI 185

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 578801331  770 RRVNAFSNFFSGPIVVHCSAGVGRTGTYIGIDAMLEGLEAEN---KVDVYGYVVKLRRQRCLMVQVEAQYILIHQALVE 845
Cdd:cd14603   186 ELARRLQGSGPEPLCVHCSAGCGRTGVICTVDYVRQLLLTQRippDFSIFDVVLEMRKQRPAAVQTEEQYEFLYHTVAQ 264
PTPc-N13 cd14597
catalytic domain of tyrosine-protein phosphatase non-receptor type 13; Tyrosine-protein ...
 611-844 1.05e-56

catalytic domain of tyrosine-protein phosphatase non-receptor type 13; Tyrosine-protein phosphatase non-receptor type 13 (PTPN13, also known as PTPL1) belongs to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. Human PTPN13 is an important regulator of tumor aggressiveness. It regulates breast cancer cell aggressiveness through direct inactivation of Src kinase. In hepatocellular carcinoma, PTPN13 is a tumor suppressor. PTPN13 contains a FERM domain, five PDZ domains, and a C-terminal catalytic PTP domain. With its PDZ domains, PTPN13 has numerous interacting partners that can actively participate in the regulation of its phosphatase activity or can permit direct or indirect recruitment of tyrosine phosphorylated substrates. Its FERM domain is necessary for localization to the membrane.


Pssm-ID: 350445 [Multi-domain]  Cd Length: 234  Bit Score: 196.20  E-value: 1.05e-56
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578801331  611 NQNKNRYVDILPYDYNRVELSEINGdagsnYINASYIdgfKEPRK-----YIAAQGPRDETVDDFWRMIWEQKATVIVMV 685
Cdd:cd14597     3 NRKKNRYKNILPYDTTRVPLGDEGG-----YINASFI---KMPVGdeefvYIACQGPLPTTVADFWQMVWEQKSTVIAMM 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578801331  686 TRCEEGNRNKCAEYWPSMEEGTRAFGD----VVVKINQHKrcpDYIIQKLNIVNKKEKATgREVTHIQFTSWPDHGVPED 761
Cdd:cd14597    75 TQEVEGGKIKCQRYWPEILGKTTMVDNrlqlTLVRMQQLK---NFVIRVLELEDIQTREV-RHITHLNFTAWPDHDTPSQ 150

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578801331  762 PHLLLKL---RRRVNAfsnffSGPIVVHCSAGVGRTGTYIGIDAMLEGLEAENKVDVYGYVVKLRRQRCLMVQVEAQYIL 838
Cdd:cd14597   151 PEQLLTFisyMRHIHK-----SGPIITHCSAGIGRSGTLICIDVVLGLISKDLDFDISDIVRTMRLQRHGMVQTEDQYIF 225


                  ....*.
gi 578801331  839 IHQALV 844
Cdd:cd14597   226 CYQVIL 231
PTPc-N1_2 cd14545
catalytic domain of tyrosine-protein phosphatase non-receptor type 1 and type 2; ...
 614-835 5.64e-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: 5.64e-56
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578801331  614 KNRYVDILPYDYNRVELSEINGDagSNYINASYIDGFKEPRKYIAAQGPRDETVDDFWRMIWEQKATVIVMVTRCEEGNR 693
Cdd:cd14545     1 LNRYRDRDPYDHDRSRVKLKQGD--NDYINASLVEVEEAKRSYILTQGPLPNTSGHFWQMVWEQNSKAVIMLNKLMEKGQ 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578801331  694 NKCAEYWPSMEEGTRAFGDVVVKIN--QHKRCPDYIIQKLNIVNKKEKATgREVTHIQFTSWPDHGVPEDP----HLLLK 767
Cdd:cd14545    79 IKCAQYWPQGEGNAMIFEDTGLKVTllSEEDKSYYTVRTLELENLKTQET-REVLHFHYTTWPDFGVPESPaaflNFLQK 157

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578801331  768 LRRRVNAFSNFfsGPIVVHCSAGVGRTGTYIGIDAMLEGLEAEN--KVDVYGYVVKLRRQRCLMVQVEAQ 835
Cdd:cd14545   158 VRESGSLSSDV--GPPVVHCSAGIGRSGTFCLVDTCLVLIEKGNpsSVDVKKVLLEMRKYRMGLIQTPDQ 225
PTPc-N22_18_12 cd14542
catalytic domain of tyrosine-protein phosphatase non-receptor type 22, type 18 and type 12; ...
 641-841 6.09e-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: 192.64  E-value: 6.09e-56
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578801331  641 YINASYIDGFKEPRKYIAAQGPRDETVDDFWRMIWEQKATVIVMVTRCEEGNRNKCAEYWPSMEEGTRAFGDVVVK-INQ 719
Cdd:cd14542     1 YINANFIKGVSGSKAYIATQGPLPNTVLDFWRMIWEYNVQVIVMACREFEMGKKKCERYWPEEGEEQLQFGPFKISlEKE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578801331  720 HKRCPDYIIQKLNIVNKKEKatgREVTHIQFTSWPDHGVPEDPHLLLKLRRRVNAFSNFFSGPIVVHCSAGVGRTGTYIG 799
Cdd:cd14542    81 KRVGPDFLIRTLKVTFQKES---RTVYQFHYTAWPDHGVPSSVDPILDLVRLVRDYQGSEDVPICVHCSAGCGRTGTICA 157

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*.
gi 578801331  800 ID----AMLEGLEAENkVDVYGYVVKLRRQRCLMVQVEAQYILIHQ 841
Cdd:cd14542   158 IDyvwnLLKTGKIPEE-FSLFDLVREMRKQRPAMVQTKEQYELVYR 202
R-PTPc-A-E-2 cd14552
catalytic domain of receptor-type tyrosine-protein phosphatase A and E, repeat 2; ...
 641-844 6.36e-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: 6.36e-56
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578801331  641 YINASYIDGFKEPRKYIAAQGPRDETVDDFWRMIWEQKATVIVMVTRCEEGNRNKCAEYWPsmEEGTRAFGDVVVKINQH 720
Cdd:cd14552     1 YINASFIDGYRQKDAYIATQGPLDHTVEDFWRMIWEWKSCSIVMLTEIKERSQNKCAQYWP--EDGSVSSGDITVELKDQ 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578801331  721 KRCPDYIIQKLNIVNKKEKATgREVTHIQFTSWPDHGVPEDP----HLLLKLRRRVNAFSNffsGPIVVHCSAGVGRTGT 796
Cdd:cd14552    79 TDYEDYTLRDFLVTKGKGGST-RTVRQFHFHGWPEVGIPDNGkgmiDLIAAVQKQQQQSGN---HPITVHCSAGAGRTGT 154

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*...
gi 578801331  797 YIGIDAMLEGLEAENKVDVYGYVVKLRRQRCLMVQVEAQYILIHQALV 844
Cdd:cd14552   155 FCALSTVLERVKAEGVLDVFQVVKSLRLQRPHMVQTLEQYEFCYKVVQ 202
R-PTPc-A-2 cd14623
catalytic domain of receptor-type tyrosine-protein phosphatase A, repeat 2; Receptor-type ...
 907-1159 3.38e-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: 3.38e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578801331  907 RNSNVIPYDYNRV--PLKHELEmskesehdsdessdddsdseePSKYINASFIMSYWKPEVMIAAQGPLKETIGDFWQMI 984
Cdd:cd14623     1 RVLQIIPYEFNRViiPVKRGEE---------------------NTDYVNASFIDGYRQKDSYIASQGPLQHTIEDFWRMI 59

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578801331  985 FQRKVKVIVMLTELKHGDQEICAQYW-GEGKQTYGDIEVDLKDTDKSSTYTLRVFELRHSKRKDSRTVYQYQYTNWSVEQ 1063
Cdd:cd14623    60 WEWKSCSIVMLTELEERGQEKCAQYWpSDGSVSYGDITIELKKEEECESYTVRDLLVTNTRENKSRQIRQFHFHGWPEVG 139

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578801331 1064 LPAEPKELISMIQVVkqklpQKNSSEGNKHhkstPLLIHCRDGSQQTGIFCALLNLLESAETEEVVDIFQVVKALRKARP 1143
Cdd:cd14623   140 IPSDGKGMINIIAAV-----QKQQQQSGNH----PITVHCSAGAGRTGTFCALSTVLERVKAEGILDVFQTVKSLRLQRP 210

                         250
                  ....*....|....*.
gi 578801331 1144 GMVSTFEQYQFLYDVI 1159
Cdd:cd14623   211 HMVQTLEQYEFCYKVV 226
PTPc-N14 cd14599
catalytic domain of tyrosine-protein phosphatase non-receptor type 14; Tyrosine-protein ...
 574-846 5.97e-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: 5.97e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578801331  574 ETYKRKIaDEGRLFlAEFQSIPRVFSKFPIKEARKPFNQNKNRYVDILPYDYNRVELSEiNGDAGSNYINASYIDGF--K 651
Cdd:cd14599     3 KTLERKL-EEGMVF-TEYEQIPKKKADGVFTTATLPENAERNRIREVVPYEENRVELVP-TKENNTGYINASHIKVTvgG 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578801331  652 EPRKYIAAQGPRDETVDDFWRMIWEQKATVIVMVTRCEEGNRNKCAEYWPSM--EEGTRAFGDVVVKINQHKRCPDYIIQ 729
Cdd:cd14599    80 EEWHYIATQGPLPHTCHDFWQMVWEQGVNVIAMVTAEEEGGRSKSHRYWPKLgsKHSSATYGKFKVTTKFRTDSGCYATT 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578801331  730 KLNIvnkKEKATGREVT--HIQFTSWPDHGVPEDPHLLLK-------LRRRVNAF---SNFFSGPIVVHCSAGVGRTGTY 797
Cdd:cd14599   160 GLKV---KHLLSGQERTvwHLQYTDWPDHGCPEEVQGFLSyleeiqsVRRHTNSMldsTKNCNPPIVVHCSAGVGRTGVV 236

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*....
gi 578801331  798 IGIDAMLEGLEAENKVDVYGYVVKLRRQRCLMVQVEAQYILIHQALVEY 846
Cdd:cd14599   237 ILTELMIGCLEHNEKVEVPVMLRHLREQRMFMIQTIAQYKFVYQVLIQF 285
R3-PTPc cd14548
catalytic domain of R3 subfamily receptor-type tyrosine-protein phosphatases and similar ...
 907-1156 8.65e-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: 190.26  E-value: 8.65e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578801331  907 RNSNVIPYDYNRVPLKhelemskesehdsdessddDSDSEEPSKYINASFIMSYWKPEVMIAAQGPLKETIGDFWQMIFQ 986
Cdd:cd14548     1 RYTNILPYDHSRVKLI-------------------PINEEEGSDYINANYIPGYNSPREFIATQGPLPGTKDDFWRMVWE 61

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578801331  987 RKVKVIVMLTELKHGDQEICAQYWGEGKQ--TYGDIEVDLKDTDKSSTYTLRVFELRHskRKDSRTVYQYQYTNWSVEQL 1064
Cdd:cd14548    62 QNSHTIVMLTQCMEKGRVKCDHYWPFDQDpvYYGDITVTMLSESVLPDWTIREFKLER--GDEVRSVRQFHFTAWPDHGV 139

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578801331 1065 PAEPKELISMIQVVKQKLPQKNssegnkhhksTPLLIHCRDGSQQTGIFCALLNLLESAETEEVVDIFQVVKALRKARPG 1144
Cdd:cd14548   140 PEAPDSLLRFVRLVRDYIKQEK----------GPTIVHCSAGVGRTGTFIALDRLLQQIESEDYVDIFGIVYDLRKHRPL 209

                         250
                  ....*....|..
gi 578801331 1145 MVSTFEQYQFLY 1156
Cdd:cd14548   210 MVQTEAQYIFLH 221
R-PTPc-LAR-1 cd14553
catalytic domain of LAR family receptor-type tyrosine-protein phosphatases, repeat 1; The LAR ...
 900-1159 1.71e-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: 189.92  E-value: 1.71e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578801331  900 EENKSKNRNSNVIPYDYNRVPLKhelemskesehdsdessddDSDSEEPSKYINASFIMSYWKPEVMIAAQGPLKETIGD 979
Cdd:cd14553     1 EVNKPKNRYANVIAYDHSRVILQ-------------------PIEGVPGSDYINANYCDGYRKQNAYIATQGPLPETFGD 61

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578801331  980 FWQMIFQRKVKVIVMLTELKHGDQEICAQYW-GEGKQTYGDIEVDLKDTDKSSTYTLRVFELRHSKRKDSRTVYQYQYTN 1058
Cdd:cd14553    62 FWRMVWEQRSATIVMMTKLEERSRVKCDQYWpTRGTETYGLIQVTLLDTVELATYTVRTFALHKNGSSEKREVRQFQFTA 141

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578801331 1059 WSVEQLPAEPKELISMIQVVKQKLPQknssegnkhhKSTPLLIHCRDGSQQTGIFCALLNLLESAETEEVVDIFQVVKAL 1138
Cdd:cd14553   142 WPDHGVPEHPTPFLAFLRRVKACNPP----------DAGPIVVHCSAGVGRTGCFIVIDSMLERIKHEKTVDIYGHVTCL 211

                         250       260
                  ....*....|....*....|.
gi 578801331 1139 RKARPGMVSTFEQYQFLYDVI 1159
Cdd:cd14553   212 RAQRNYMVQTEDQYIFIHDAL 232
R5-PTPc-1 cd14549
catalytic domain of R5 subfamily receptor-type tyrosine-protein phosphatases, repeat 1; The R5 ...
 951-1157 2.00e-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: 188.71  E-value: 2.00e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578801331  951 YINASFIMSYWKPEVMIAAQGPLKETIGDFWQMIFQRKVKVIVMLTELKHGDQEICAQYW-GEGKQTYGDIEVDLKDTDK 1029
Cdd:cd14549     1 YINANYVDGYNKARAYIATQGPLPSTFDDFWRMVWEQNSAIIVMITNLVERGRRKCDQYWpKEGTETYGNIQVTLLSTEV 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578801331 1030 SSTYTLRVFELRHSK------RKDSRTVYQYQYTNWSVEQLPAEPKELISMIQvvkqklpqkNSSEGNKHHkSTPLLIHC 1103
Cdd:cd14549    81 LATYTVRTFSLKNLKlkkvkgRSSERVVYQYHYTQWPDHGVPDYTLPVLSFVR---------KSSAANPPG-AGPIVVHC 150

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....
gi 578801331 1104 RDGSQQTGIFCALLNLLESAETEEVVDIFQVVKALRKARPGMVSTFEQYQFLYD 1157
Cdd:cd14549   151 SAGVGRTGTYIVIDSMLQQIQDKGTVNVFGFLKHIRTQRNYLVQTEEQYIFIHD 204
R-PTPc-E-2 cd14622
catalytic domain of receptor-type tyrosine-protein phosphatase E, repeat 2; Receptor-type ...
 951-1159 2.92e-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: 2.92e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578801331  951 YINASFIMSYWKPEVMIAAQGPLKETIGDFWQMIFQRKVKVIVMLTELKHGDQEICAQYW-GEGKQTYGDIEVDLKDTDK 1029
Cdd:cd14622     2 YINASFIDGYRQKDYFIATQGPLAHTVEDFWRMVWEWKCHTIVMLTELQEREQEKCVQYWpSEGSVTHGEITIEIKNDTL 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578801331 1030 SSTYTLRVFELRHSKRKDSRTVYQYQYTNWSVEQLPAEPKELISMIQVVkqklpQKNSSEGNKHhkstPLLIHCRDGSQQ 1109
Cdd:cd14622    82 LETISIRDFLVTYNQEKQTRLVRQFHFHGWPEIGIPAEGKGMIDLIAAV-----QKQQQQTGNH----PIVVHCSAGAGR 152

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|
gi 578801331 1110 TGIFCALLNLLESAETEEVVDIFQVVKALRKARPGMVSTFEQYQFLYDVI 1159
Cdd:cd14622   153 TGTFIALSNILERVKAEGLLDVFQTVKSLRLQRPHMVQTLEQYEFCYRVV 202
PTPc-N3_4 cd14541
catalytic domain of tyrosine-protein phosphatase non-receptor type 21 and type 14; ...
 641-836 6.47e-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: 6.47e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578801331  641 YINASYID----GFKEPRKYIAAQGPRDETVDDFWRMIWEQKATVIVMVTRCEEGNRNKCAEYWPSMEEgTRAFGDVVVK 716
Cdd:cd14541     2 YINANYVNmeipGSGIVNRYIAAQGPLPNTCADFWQMVWEQKSTLIVMLTTLVERGRVKCHQYWPDLGE-TMQFGNLQIT 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578801331  717 INQHKRCPDYIIQKLNIVNKKEKATgREVTHIQFTSWPDHGVPEDPHLLLKLRRRVNAFSNFFSGPIVVHCSAGVGRTGT 796
Cdd:cd14541    81 CVSEEVTPSFAFREFILTNTNTGEE-RHITQMQYLAWPDHGVPDDSSDFLDFVKRVRQNRVGMVEPTVVHCSAGIGRTGV 159

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|
gi 578801331  797 YIGIDAMLEGLEAENKVDVYGYVVKLRRQRCLMVQVEAQY 836
Cdd:cd14541   160 LITMETAMCLIEANEPVYPLDIVRTMRDQRAMLIQTPSQY 199
PTPc-N22 cd14602
catalytic domain of tyrosine-protein phosphatase non-receptor type 22; Tyrosine-protein ...
 614-845 8.52e-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: 187.74  E-value: 8.52e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578801331  614 KNRYVDILPYDYNRVELSEINGDAGSNYINASYIDGFKEPRKYIAAQGPRDETVDDFWRMIWEQKATVIVMVTRCEEGNR 693
Cdd:cd14602     1 KNRYKDILPYDHSRVELSLITSDEDSDYINANFIKGVYGPRAYIATQGPLSTTLLDFWRMIWEYSVLIIVMACMEFEMGK 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578801331  694 NKCAEYWPSMEEGTRAFGDVVVKINQHKRCPDYIIQKLNIVNKKEKatgREVTHIQFTSWPDHGVPEDPHLLLKLRRRVN 773
Cdd:cd14602    81 KKCERYWAEPGEMQLEFGPFSVTCEAEKRKSDYIIRTLKVKFNSET---RTIYQFHYKNWPDHDVPSSIDPILELIWDVR 157

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 578801331  774 AFSNFFSGPIVVHCSAGVGRTGTYIGID----AMLEGLEAENkVDVYGYVVKLRRQRCLMVQVEAQYILIHQALVE 845
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 ...
 641-836 1.11e-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: 1.11e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578801331  641 YINASYIDGFKEPRKYIAAQGPRDETVDDFWRMIWEQKATVIVMVTRCEEGNRNKCAEYWPsmeEGTRAFGDVVVKINQH 720
Cdd:cd14558     1 YINASFIDGYWGPKSLIATQGPLPDTIADFWQMIFQKKVKVIVMLTELKEGDQEQCAQYWG---DEKKTYGDIEVELKDT 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578801331  721 KRCPDYIIQKLNIVNKKEKATgREVTHIQFTSWPDHGVPEDPHLLLKLRRRV------NAFSNFFSGPIVVHCSAGVGRT 794
Cdd:cd14558    78 EKSPTYTVRVFEITHLKRKDS-RTVYQYQYHKWKGEELPEKPKDLVDMIKSIkqklpyKNSKHGRSVPIVVHCSDGSSRT 156

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|..
gi 578801331  795 GTYIGIDAMLEGLEAENKVDVYGYVVKLRRQRCLMVQVEAQY 836
Cdd:cd14558   157 GIFCALWNLLESAETEKVVDVFQVVKALRKQRPGMVSTLEQY 198
PTPc-N12 cd14604
catalytic domain of tyrosine-protein phosphatase non-receptor type 12; Tyrosine-protein ...
 587-845 2.97e-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: 2.97e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578801331  587 FLAEFQSIPRVFSKF------PIKEARKPFNQNKNRYVDILPYDYNRVELSEINGDAGSNYINASYIDGFKEPRKYIAAQ 660
Cdd:cd14604    27 FASDFMRLRRLSTKYrtekiyPTATGEKEENVKKNRYKDILPFDHSRVKLTLKTSSQDSDYINANFIKGVYGPKAYIATQ 106

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578801331  661 GPRDETVDDFWRMIWEQKATVIVMVTRCEEGNRNKCAEYWPSMEEGTRAFGDVVVKINQHKRCPDYIIQKLNIVNKKEKa 740
Cdd:cd14604   107 GPLANTVIDFWRMIWEYNVAIIVMACREFEMGRKKCERYWPLYGEEPMTFGPFRISCEAEQARTDYFIRTLLLEFQNET- 185

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578801331  741 tgREVTHIQFTSWPDHGVPEDPHLLLKLRRRVNAFSNFFSGPIVVHCSAGVGRTGTYIGIDAMLEGLEA---ENKVDVYG 817
Cdd:cd14604   186 --RRLYQFHYVNWPDHDVPSSFDSILDMISLMRKYQEHEDVPICIHCSAGCGRTGAICAIDYTWNLLKAgkiPEEFNVFN 263

                         250       260
                  ....*....|....*....|....*...
gi 578801331  818 YVVKLRRQRCLMVQVEAQYILIHQALVE 845
Cdd:cd14604   264 LIQEMRTQRHSAVQTKEQYELVHRAIAQ 291
PTPc-N1 cd14608
catalytic domain of tyrosine-protein phosphatase non-receptor type 1; Tyrosine-protein ...
 591-854 4.27e-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: 4.27e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578801331  591 FQSIPRVFSKFPIKEARKPFNQNKNRYVDILPYDYNRVELSEINGDagsnYINASYIDGFKEPRKYIAAQGPRDETVDDF 670
Cdd:cd14608     5 YQDIRHEASDFPCRVAKLPKNKNRNRYRDVSPFDHSRIKLHQEDND----YINASLIKMEEAQRSYILTQGPLPNTCGHF 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578801331  671 WRMIWEQKATVIVMVTRCEEGNRNKCAEYWPSMEEGTRAFGDVVVKIN--QHKRCPDYIIQKLNIVNKKEKATgREVTHI 748
Cdd:cd14608    81 WEMVWEQKSRGVVMLNRVMEKGSLKCAQYWPQKEEKEMIFEDTNLKLTliSEDIKSYYTVRQLELENLTTQET-REILHF 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578801331  749 QFTSWPDHGVPEDP----HLLLKLRRrvNAFSNFFSGPIVVHCSAGVGRTGTYIGIDA---MLEGLEAENKVDVYGYVVK 821
Cdd:cd14608   160 HYTTWPDFGVPESPasflNFLFKVRE--SGSLSPEHGPVVVHCSAGIGRSGTFCLADTcllLMDKRKDPSSVDIKKVLLE 237

                         250       260       270
                  ....*....|....*....|....*....|....*
gi 578801331  822 LRRQRCLMVQVEAQYILIHQALVEYNQF--GETEV 854
Cdd:cd14608   238 MRKFRMGLIQTADQLRFSYLAVIEGAKFimGDSSV 272
PTPc-N3 cd14600
catalytic domain of tyrosine-protein phosphatase non-receptor type 3; Tyrosine-protein ...
 588-844 8.02e-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: 8.02e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578801331  588 LAEFQSIPRVFSKFPIKEARKPFNQNKNRYVDILPYDYNRVELSEingdaGSNYINASYID----GFKEPRKYIAAQGPR 663
Cdd:cd14600    17 LIQFEQLYRKKPGLAITCAKLPQNMDKNRYKDVLPYDATRVVLQG-----NEDYINASYVNmeipSANIVNKYIATQGPL 91

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578801331  664 DETVDDFWRMIWEQKATVIVMVTRCEEGNRNKCAEYWPSMEEgTRAFGDVVVKINQHKRCPDYIIQKLNIVNKKekaTGR 743
Cdd:cd14600    92 PHTCAQFWQVVWEQKLSLIVMLTTLTERGRTKCHQYWPDPPD-VMEYGGFRVQCHSEDCTIAYVFREMLLTNTQ---TGE 167

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578801331  744 E--VTHIQFTSWPDHGVPEDPHLLLKLRRRVNAfSNFFSGPIVVHCSAGVGRTGTYIGIDAMLEGLEAENKVDVYGYVVK 821
Cdd:cd14600   168 ErtVTHLQYVAWPDHGVPDDSSDFLEFVNYVRS-KRVENEPVLVHCSAGIGRTGVLVTMETAMCLTERNQPVYPLDIVRK 246

                         250       260
                  ....*....|....*....|...
gi 578801331  822 LRRQRCLMVQVEAQYILIHQALV 844
Cdd:cd14600   247 MRDQRAMMVQTSSQYKFVCEAIL 269
PTP_fungal cd18533
fungal protein tyrosine phosphatases; This subfamily contains Saccharomyces cerevisiae ...
 951-1157 8.95e-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: 183.99  E-value: 8.95e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578801331  951 YINASFI-MSYWKPEVMIAAQGPLKETIGDFWQMIFQRKVKVIVMLTELKHGDQEICAQYW--GEGKQTYGDIEVDL--K 1025
Cdd:cd18533     1 YINASYItLPGTSSKRYIATQGPLPATIGDFWKMIWQNNVGVIVMLTPLVENGREKCDQYWpsGEYEGEYGDLTVELvsE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578801331 1026 DTDKSSTYTLRVFELRHSKRKdSRTVYQYQYTNWSVEQLPAEPKELISMIQVVKQKLpqknssegNKHHKSTPLLIHCRD 1105
Cdd:cd18533    81 EENDDGGFIVREFELSKEDGK-VKKVYHIQYKSWPDFGVPDSPEDLLTLIKLKRELN--------DSASLDPPIIVHCSA 151

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 578801331 1106 GSQQTGIFCAL---LNLLE-----SAETEEVVD-IFQVVKALRKARPGMVSTFEQYQFLYD 1157
Cdd:cd18533   152 GVGRTGTFIALdslLDELKrglsdSQDLEDSEDpVYEIVNQLRKQRMSMVQTLRQYIFLYD 212
R-PTPc-R cd14611
catalytic domain of receptor-type tyrosine-protein phosphatase R; Receptor-type ...
 614-841 1.48e-52

catalytic domain of receptor-type tyrosine-protein phosphatase R; Receptor-type tyrosine-protein phosphatase-like R (PTPRR or R-PTP-R), also called protein-tyrosine phosphatase PCPTP1, belongs to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. PTPRR is a kinase interaction motif (KIM)-PTP, characterized by the presence of a 16-amino-acid KIM that binds specifically to members of the MAPK (mitogen-activated protein kinase) family. The human and mouse PTPRR gene produces multiple neuronal protein isoforms of varying sizes (in human, PTPPBS-alpha, beta, gamma and delta). All isoforms contain the KIM motif and the catalytic PTP domain. PTPRR-deficient mice show significant defects in fine motor coordination and balance skills that are reminiscent of a mild ataxia.


Pssm-ID: 350459 [Multi-domain]  Cd Length: 226  Bit Score: 183.97  E-value: 1.48e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578801331  614 KNRYVDILPYDYNRVELSEIN-GDAGSNYINASYIDGFK-EPRKYIAAQGPRDETVDDFWRMIWEQKATVIVMVTRCEEG 691
Cdd:cd14611     2 KNRYKTILPNPHSRVCLKPKNsNDSLSTYINANYIRGYGgKEKAFIATQGPMINTVNDFWQMVWQEDSPVIVMITKLKEK 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578801331  692 NRnKCAEYWPsmeEGTRAFGDVVVKINQHKRCPDYIIQKLNIvnkKEKATGREVTHIQFTSWPDHGVPEDPHLLLKLRRR 771
Cdd:cd14611    82 NE-KCVLYWP---EKRGIYGKVEVLVNSVKECDNYTIRNLTL---KQGSQSRSVKHYWYTSWPDHKTPDSAQPLLQLMLD 154

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 578801331  772 V--NAFSNFFSGPIVVHCSAGVGRTGTYIGIDAMLEGLEAENKVDVYGYVVKLRRQRCLMVQVEAQYILIHQ 841
Cdd:cd14611   155 VeeDRLASPGRGPVVVHCSAGIGRTGCFIATTIGCQQLKEEGVVDVLSIVCQLRVDRGGMVQTSEQYEFVHH 226
PTPc-N5 cd14613
catalytic domain of tyrosine-protein phosphatase non-receptor type 5; Tyrosine-protein ...
 589-846 3.43e-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: 3.43e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578801331  589 AEFQSIPRVFSKfPiKEARKPFNQNKNRYVDILPYDYNRVEL-SEINGDAGSNYINASYIDGF-KEPRKYIAAQGPRDET 666
Cdd:cd14613     5 AEFFEIPMNFVD-P-KEYDIPGLVRKNRYKTILPNPHSRVCLtSPDQDDPLSSYINANYIRGYgGEEKVYIATQGPTVNT 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578801331  667 VDDFWRMIWEQKATVIVMVTRCEEGNRnKCAEYWPsmeEGTRAFGDVVVKINQHKRCPDYiiqKLNIVNKKEKATGREVT 746
Cdd:cd14613    83 VGDFWRMVWQERSPIIVMITNIEEMNE-KCTEYWP---EEQVTYEGIEITVKQVIHADDY---RLRLITLKSGGEERGLK 155

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578801331  747 HIQFTSWPDHGVPEDPHLLLKLRRRVNAF---SNFFSGPIVVHCSAGVGRTGTYIGIDAMLEGLEAENKVDVYGYVVKLR 823
Cdd:cd14613   156 HYWYTSWPDQKTPDNAPPLLQLVQEVEEArqqAEPNCGPVIVHCSAGIGRTGCFIATSICCKQLRNEGVVDILRTTCQLR 235

                         250       260
                  ....*....|....*....|...
gi 578801331  824 RQRCLMVQVEAQYILIHQALVEY 846
Cdd:cd14613   236 LDRGGMIQTCEQYQFVHHVLSLY 258
PHA02746 PHA02746
protein tyrosine phosphatase; Provisional
 608-843 1.00e-51

protein tyrosine phosphatase; Provisional


Pssm-ID: 165113 [Multi-domain]  Cd Length: 323  Bit Score: 185.23  E-value: 1.00e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578801331  608 KPFNQNKNRYVDILPYDYNRVELSE-------------------INGDAGSNYINASYIDGFKEPRKYIAAQGPRDETVD 668
Cdd:PHA02746   48 KKENLKKNRFHDIPCWDHSRVVINAheslkmfdvgdsdgkkievTSEDNAENYIHANFVDGFKEANKFICAQGPKEDTSE 127

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578801331  669 DFWRMIWEQKATVIVMVTRCEEGNRnKCAEYWPSMEEGTRAFGDVVVKINQHKRCPDYIIQKLNIVNKKEKaTGREVTHI 748
Cdd:PHA02746  128 DFFKLISEHESQVIVSLTDIDDDDE-KCFELWTKEEDSELAFGRFVAKILDIIEELSFTKTRLMITDKISD-TSREIHHF 205

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578801331  749 QFTSWPDHGVPEDPHLLLKLRRRVNA----------FSNFFSGPIVVHCSAGVGRTGTYIGIDAMLEGLEAENKVDVYGY 818
Cdd:PHA02746  206 WFPDWPDNGIPTGMAEFLELINKVNEeqaelikqadNDPQTLGPIVVHCSAGIGRAGTFCAIDNALEQLEKEKEVCLGEI 285

                         250       260
                  ....*....|....*....|....*
gi 578801331  819 VVKLRRQRCLMVQVEAQYILIHQAL 843
Cdd:PHA02746  286 VLKIRKQRHSSVFLPEQYAFCYKAL 310
PTPc-N9 cd14543
catalytic domain of tyrosine-protein phosphatase non-receptor type 9; Tyrosine-protein ...
 902-1156 1.76e-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: 1.76e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578801331  902 NKSKNRNSNVIPYDYNRVPLKHELEmskesehdsdessdddsdsEEPSKYINASFIMSYWKPEVMIAAQGPLKETIGDFW 981
Cdd:cd14543    29 NQEKNRYGDVLCLDQSRVKLPKRNG-------------------DERTDYINANFMDGYKQKNAYIATQGPLPKTYSDFW 89

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578801331  982 QMIFQRKVKVIVMLTELKHGDQEICAQYW---GEGKQTYGDIEVDLKDTDKSSTYTLRVFELRHSKRKDSRTVYQYQYTN 1058
Cdd:cd14543    90 RMVWEQKVLVIVMTTRVVERGRVKCGQYWpleEGSSLRYGDLTVTNLSVENKEHYKKTTLEIHNTETDESRQVTHFQFTS 169

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578801331 1059 WSVEQLPAEPKELISMIQVVKQKLPQKNSSEGN---KHHKSTPLLIHCRDGSQQTGIFCALLNLLESAETEEVVDIFQVV 1135
Cdd:cd14543   170 WPDFGVPSSAAALLDFLGEVRQQQALAVKAMGDrwkGHPPGPPIVVHCSAGIGRTGTFCTLDICLSQLEDVGTLNVMQTV 249

                         250       260
                  ....*....|....*....|.
gi 578801331 1136 KALRKARPGMVSTFEQYQFLY 1156
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 ...
 641-855 2.19e-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: 179.95  E-value: 2.19e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578801331  641 YINASYIDGfKEPRK--YIAAQGPRDETVDDFWRMIWEQKATVIVMVTRCEEGNRNKCAEYWPsmEEGTRAFGDVVVK-I 717
Cdd:cd14546     1 YINASTIYD-HDPRNpaYIATQGPLPHTIADFWQMIWEQGCVVIVMLTRLQENGVKQCARYWP--EEGSEVYHIYEVHlV 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578801331  718 NQHKRCPDYIIQKLNIVNKKEKATgREVTHIQFTSWPDHGVPEDPHLLLKLRRRVNAFSNFFSGPIVVHCSAGVGRTGTY 797
Cdd:cd14546    78 SEHIWCDDYLVRSFYLKNLQTSET-RTVTQFHFLSWPDEGIPASAKPLLEFRRKVNKSYRGRSCPIVVHCSDGAGRTGTY 156

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 578801331  798 IGIDAMLEGLEAENK-VDVYGYVVKLRRQRCLMVQVEAQYILIHQALVEynqfgetEVN 855
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 ...
 902-1156 3.63e-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: 3.63e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578801331  902 NKSKNRNSNVIPYDYNRVPLKhelemskesehdsdessddDSDSEEPSKYINASFIMSYWKPEVMIAAQGPLKETIGDFW 981
Cdd:cd14554     6 NKFKNRLVNILPYESTRVCLQ-------------------PIRGVEGSDYINASFIDGYRQRGAYIATQGPLAETTEDFW 66

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578801331  982 QMIFQRKVKVIVMLTELKHGDQEICAQYW-GEGKQTYGDIEVDLKDTDKSSTYTLRVFELRHSKRKDSRTVYQYQYTNWS 1060
Cdd:cd14554    67 RMLWEHNSTIIVMLTKLREMGREKCHQYWpAERSARYQYFVVDPMAEYNMPQYILREFKVTDARDGQSRTVRQFQFTDWP 146

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578801331 1061 VEQLPAEPKELISMI-QVVKQKlpQKNSSEGnkhhkstPLLIHCRDGSQQTGIFCALLNLLESAETEEVVDIFQVVKALR 1139
Cdd:cd14554   147 EQGVPKSGEGFIDFIgQVHKTK--EQFGQEG-------PITVHCSAGVGRTGVFITLSIVLERMRYEGVVDVFQTVKLLR 217

                         250
                  ....*....|....*..
gi 578801331 1140 KARPGMVSTFEQYQFLY 1156
Cdd:cd14554   218 TQRPAMVQTEDQYQFCY 234
R-PTP-N2 cd14610
PTP-like domain of receptor-type tyrosine-protein phosphatase N2; Receptor-type ...
 606-845 8.64e-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: 8.64e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578801331  606 ARKPFNQNKNRYVDILPYDYNRVELSEINGDAGSNYINASYIDGfKEPRK--YIAAQGPRDETVDDFWRMIWEQKATVIV 683
Cdd:cd14610    39 AQREENVQKNRSLAVLPYDHSRIILKAENSHSHSDYINASPIMD-HDPRNpaYIATQGPLPATVADFWQMVWESGCVVIV 117

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578801331  684 MVTRCEEGNRNKCAEYWPsmEEGTRAFGDVVVK-INQHKRCPDYIIQKLNIVNKKEKATgREVTHIQFTSWPDHGVPEDP 762
Cdd:cd14610   118 MLTPLAENGVKQCYHYWP--DEGSNLYHIYEVNlVSEHIWCEDFLVRSFYLKNLQTNET-RTVTQFHFLSWNDQGVPAST 194

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578801331  763 HLLLKLRRRVNAFSNFFSGPIVVHCSAGVGRTGTYIGIDAMLEGL-EAENKVDVYGYVVKLRRQRCLMVQVEAQYILIHQ 841
Cdd:cd14610   195 RSLLDFRRKVNKCYRGRSCPIIVHCSDGAGRSGTYILIDMVLNKMaKGAKEIDIAATLEHLRDQRPGMVQTKEQFEFALT 274


                  ....
gi 578801331  842 ALVE 845
Cdd:cd14610   275 AVAE 278
R-PTPc-typeIIb-2 cd14556
PTP domain of type IIb (or R2B) subfamily receptor-type tyrosine-protein phosphatases, repeat ...
 951-1157 3.38e-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: 3.38e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578801331  951 YINASFIMSYWKPEVMIAAQGPLKETIGDFWQMIFQRKVKVIVMLTELKHGDQEiCAQYWGE-GKQTYGDIEVDLKDTDK 1029
Cdd:cd14556     1 YINAALLDSYKQPAAFIVTQHPLPNTVTDFWRLVYDYGCTSIVMLNQLDPKDQS-CPQYWPDeGSGTYGPIQVEFVSTTI 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578801331 1030 SSTYTLRVFELRHSKR--KDSRTVYQYQYTNWSVEQL-PAEPKELISMIQVVKQKlpQKNSSEGnkhhkstPLLIHCRDG 1106
Cdd:cd14556    80 DEDVISRIFRLQNTTRpqEGYRMVQQFQFLGWPRDRDtPPSKRALLKLLSEVEKW--QEQSGEG-------PIVVHCLNG 150

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|.
gi 578801331 1107 SQQTGIFCALLNLLESAETEEVVDIFQVVKALRKARPGMVSTFEQYQFLYD 1157
Cdd:cd14556   151 VGRSGVFCAISSVCERIKVENVVDVFQAVKTLRNHRPNMVETEEQYKFCYD 201
R-PTP-S-2 cd14627
PTP-like domain of receptor-type tyrosine-protein phosphatase S, repeat 2; Receptor-type ...
 852-1156 2.23e-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: 2.23e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578801331  852 TEVNLSELHPYLHNMKKRDPPSEPSPLEAEFQRLPSYRSWRTQHI-GNQEENKSKNRNSNVIPYDYNRVPLKhelemske 930
Cdd:cd14627     2 TEVPARNLYSYIQKLAQVEVGEHVTGMELEFKRLANSKAHTSRFIsANLPCNKFKNRLVNIMPYETTRVCLQ-------- 73

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578801331  931 sehdsdessddDSDSEEPSKYINASFIMSYWKPEVMIAAQGPLKETIGDFWQMIFQRKVKVIVMLTELKHGDQEICAQYW 1010
Cdd:cd14627    74 -----------PIRGVEGSDYINASFIDGYRQQKAYIATQGPLAETTEDFWRMLWENNSTIVVMLTKLREMGREKCHQYW 142

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578801331 1011 -GEGKQTYGDIEVDLKDTDKSSTYTLRVFELRHSKRKDSRTVYQYQYTNWSVEQLPAEPKELISMI-QVVKQKlpqknss 1088
Cdd:cd14627   143 pAERSARYQYFVVDPMAEYNMPQYILREFKVTDARDGQSRTVRQFQFTDWPEQGVPKSGEGFIDFIgQVHKTK------- 215

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 578801331 1089 egNKHHKSTPLLIHCRDGSQQTGIFCALLNLLESAETEEVVDIFQVVKALRKARPGMVSTFEQYQFLY 1156
Cdd:cd14627   216 --EQFGQDGPISVHCSAGVGRTGVFITLSIVLERMRYEGVVDIFQTVKMLRTQRPAMVQTEDEYQFCY 281
R-PTPc-H cd14619
catalytic domain of receptor-type tyrosine-protein phosphatase H; Receptor-type ...
 906-1159 2.30e-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: 2.30e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578801331  906 NRNSNVIPYDYNRVPLKhelemskesehdsdessddDSDSEEPSKYINASFIMSYWKPEVMIAAQGPLKETIGDFWQMIF 985
Cdd:cd14619     1 NRFRNVLPYDWSRVPLK-------------------PIHEEPGSDYINANYMPGYWSSQEFIATQGPLPQTVGDFWRMIW 61

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578801331  986 QRKVKVIVMLTELKHGDQEICAQYWGEGKQ--TYGDIEVDLKDTDKSSTYTLRVFELRHSKRKDSRTVYQYQYTNWSVEQ 1063
Cdd:cd14619    62 EQQSSTIVMLTNCMEAGRVKCEHYWPLDYTpcTYGHLRVTVVSEEVMENWTVREFLLKQVEEQKTLSVRHFHFTAWPDHG 141

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578801331 1064 LPAEPKELISMIQVVKQKLPQKNSsegnkhhkSTPLLIHCRDGSQQTGIFCALLNLLESAETEEVVDIFQVVKALRKARP 1143
Cdd:cd14619   142 VPSSTDTLLAFRRLLRQWLDQTMS--------GGPTVVHCSAGVGRTGTLIALDVLLQQLQSEGLLGPFSFVQKMRENRP 213

                         250
                  ....*....|....*.
gi 578801331 1144 GMVSTFEQYQFLYDVI 1159
Cdd:cd14619   214 LMVQTESQYVFLHQCI 229
R-PTP-N cd14609
PTP-like domain of receptor-type tyrosine-protein phosphatase N; Receptor-type ...
 588-845 3.52e-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: 3.52e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578801331  588 LAEFQSIPRVFSKfpikeARKPFNQNKNRYVDILPYDYNRVELSEINGDAGSNYINASYIDGfKEPR--KYIAAQGPRDE 665
Cdd:cd14609    24 LCAYQAEPNTCST-----AQGEANVKKNRNPDFVPYDHARIKLKAESNPSRSDYINASPIIE-HDPRmpAYIATQGPLSH 97

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578801331  666 TVDDFWRMIWEQKATVIVMVTRCEEGNRNKCAEYWPsmEEGTRAFGDVVVK-INQHKRCPDYIIQKLNIVNKKEKATgRE 744
Cdd:cd14609    98 TIADFWQMVWENGCTVIVMLTPLVEDGVKQCDRYWP--DEGSSLYHIYEVNlVSEHIWCEDFLVRSFYLKNVQTQET-RT 174

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578801331  745 VTHIQFTSWPDHGVPEDPHLLLKLRRRVNAFSNFFSGPIVVHCSAGVGRTGTYIGIDAMLEGL-EAENKVDVYGYVVKLR 823
Cdd:cd14609   175 LTQFHFLSWPAEGIPSSTRPLLDFRRKVNKCYRGRSCPIIVHCSDGAGRTGTYILIDMVLNRMaKGVKEIDIAATLEHVR 254

                         250       260
                  ....*....|....*....|..
gi 578801331  824 RQRCLMVQVEAQYILIHQALVE 845
Cdd:cd14609   255 DQRPGMVRTKDQFEFALTAVAE 276
R-PTP-D-2 cd14628
PTP-like domain of receptor-type tyrosine-protein phosphatase D, repeat 2; Receptor-type ...
 852-1156 7.28e-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: 176.08  E-value: 7.28e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578801331  852 TEVNLSELHPYLHNMKKRDPPSEPSPLEAEFQRLPSYRSWRTQHI-GNQEENKSKNRNSNVIPYDYNRVPLKhelemske 930
Cdd:cd14628     1 TEVPARNLYAYIQKLTQIETGENVTGMELEFKRLASSKAHTSRFIsANLPCNKFKNRLVNIMPYESTRVCLQ-------- 72

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578801331  931 sehdsdessddDSDSEEPSKYINASFIMSYWKPEVMIAAQGPLKETIGDFWQMIFQRKVKVIVMLTELKHGDQEICAQYW 1010
Cdd:cd14628    73 -----------PIRGVEGSDYINASFIDGYRQQKAYIATQGPLAETTEDFWRMLWEHNSTIVVMLTKLREMGREKCHQYW 141

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578801331 1011 -GEGKQTYGDIEVDLKDTDKSSTYTLRVFELRHSKRKDSRTVYQYQYTNWSVEQLPAEPKELISMI-QVVKQKlpqknss 1088
Cdd:cd14628   142 pAERSARYQYFVVDPMAEYNMPQYILREFKVTDARDGQSRTVRQFQFTDWPEQGVPKSGEGFIDFIgQVHKTK------- 214

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 578801331 1089 egNKHHKSTPLLIHCRDGSQQTGIFCALLNLLESAETEEVVDIFQVVKALRKARPGMVSTFEQYQFLY 1156
Cdd:cd14628   215 --EQFGQDGPISVHCSAGVGRTGVFITLSIVLERMRYEGVVDIFQTVKMLRTQRPAMVQTEDQYQFCY 280
R-PTPc-E-2 cd14622
catalytic domain of receptor-type tyrosine-protein phosphatase E, repeat 2; Receptor-type ...
 640-846 8.21e-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: 8.21e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578801331  640 NYINASYIDGFKEPRKYIAAQGPRDETVDDFWRMIWEQKATVIVMVTRCEEGNRNKCAEYWPSmeEGTRAFGDVVVKINQ 719
Cdd:cd14622     1 DYINASFIDGYRQKDYFIATQGPLAHTVEDFWRMVWEWKCHTIVMLTELQEREQEKCVQYWPS--EGSVTHGEITIEIKN 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578801331  720 HKRCPDYIIQKLNIVNKKEKATgREVTHIQFTSWPDHGVPEDPH----LLLKLRRRVNAFSNffsGPIVVHCSAGVGRTG 795
Cdd:cd14622    79 DTLLETISIRDFLVTYNQEKQT-RLVRQFHFHGWPEIGIPAEGKgmidLIAAVQKQQQQTGN---HPIVVHCSAGAGRTG 154

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|.
gi 578801331  796 TYIGIDAMLEGLEAENKVDVYGYVVKLRRQRCLMVQVEAQYILIHQALVEY 846
Cdd:cd14622   155 TFIALSNILERVKAEGLLDVFQTVKSLRLQRPHMVQTLEQYEFCYRVVQDF 205
PTPc-N20 cd14596
catalytic domain of tyrosine-protein phosphatase non-receptor type 20; Tyrosine-protein ...
 641-845 1.11e-48

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


Pssm-ID: 350444 [Multi-domain]  Cd Length: 207  Bit Score: 172.24  E-value: 1.11e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578801331  641 YINASYID---GFKEpRKYIAAQGPRDETVDDFWRMIWEQKATVIVMVTRCEEGNRNKCAEYWPSMEEGTRAFGDVVVKI 717
Cdd:cd14596     1 YINASYITmpvGEEE-LFYIATQGPLPSTIDDFWQMVWENRSDVIAMMTREVERGKVKCHRYWPETLQEPMELENYQLRL 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578801331  718 NQHKRCPDYIIQKLNIVNkKEKATGREVTHIQFTSWPDHGVPEDPHLLLKLRRRVNAFSNffSGPIVVHCSAGVGRTGTY 797
Cdd:cd14596    80 ENYQALQYFIIRIIKLVE-KETGENRLIKHLQFTTWPDHGTPQSSDQLVKFICYMRKVHN--TGPIVVHCSAGIGRAGVL 156

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*...
gi 578801331  798 IGIDAMLEGLEAENKVDVYGYVVKLRRQRCLMVQVEAQYILIHQALVE 845
Cdd:cd14596   157 ICVDVLLSLIEKDLSFNIKDIVREMRQQRYGMIQTKDQYLFCYKVVLE 204
PTPc-N2 cd14607
catalytic domain of tyrosine-protein phosphatase non-receptor type 2; Tyrosine-protein ...
 599-835 4.17e-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: 4.17e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578801331  599 SKFPIKEARKPFNQNKNRYVDILPYDYNRVELSEINGDagsnYINASYIDGFKEPRKYIAAQGPRDETVDDFWRMIWEQK 678
Cdd:cd14607    12 HDYPHRVAKYPENRNRNRYRDVSPYDHSRVKLQNTEND----YINASLVVIEEAQRSYILTQGPLPNTCCHFWLMVWQQK 87

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578801331  679 ATVIVMVTRCEEGNRNKCAEYWPSMEEGTRAFGDV--VVKINQHKRCPDYIIQKLNIVNKKEKATgREVTHIQFTSWPDH 756
Cdd:cd14607    88 TKAVVMLNRIVEKDSVKCAQYWPTDEEEVLSFKETgfSVKLLSEDVKSYYTVHLLQLENINSGET-RTISHFHYTTWPDF 166

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578801331  757 GVPEDP----HLLLKLRRrvNAFSNFFSGPIVVHCSAGVGRTGTYIGIDAMLEGLEAEN--KVDVYGYVVKLRRQRCLMV 830
Cdd:cd14607   167 GVPESPasflNFLFKVRE--SGSLSPEHGPAVVHCSAGIGRSGTFSLVDTCLVLMEKKDpdSVDIKQVLLDMRKYRMGLI 244


                  ....*
gi 578801331  831 QVEAQ 835
Cdd:cd14607   245 QTPDQ 249
R-PTPc-V cd14618
catalytic domain of receptor-type tyrosine-protein phosphatase V; Receptor-type ...
 906-1159 4.98e-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: 4.98e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578801331  906 NRNSNVIPYDYNRVPLKhelEMSKESEhdsdessdddsdseepSKYINASFIMSYWKPEVMIAAQGPLKETIGDFWQMIF 985
Cdd:cd14618     1 NRYPHVLPYDHSRVRLS---QLGGEPH----------------SDYINANFIPGYTSPQEFIATQGPLKKTIEDFWRLVW 61

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578801331  986 QRKVKVIVMLTELKHGDQEICAQYW--GEGKQTYGDIEVDLKDTDKSSTYTLRVFELRHSKRKDSRTVYQYQYTNWSVEQ 1063
Cdd:cd14618    62 EQQVCNIIMLTVGMENGRVLCDHYWpsESTPVSYGHITVHLLAQSSEDEWTRREFKLWHEDLRKERRVKHLHYTAWPDHG 141

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578801331 1064 LPAEPKELISMIQVVKQKLpqkNSSEGnkhhkSTPLLIHCRDGSQQTGIFCALLNLLESAETEEVVDIFQVVKALRKARP 1143
Cdd:cd14618   142 IPESTSSLMAFRELVREHV---QATKG-----KGPTLVHCSAGVGRSGTFIALDRLLRQLKEEKVVDVFNTVYILRMHRY 213

                         250
                  ....*....|....*.
gi 578801331 1144 GMVSTFEQYQFLYDVI 1159
Cdd:cd14618   214 LMIQTLSQYIFLHSCI 229
PHA02747 PHA02747
protein tyrosine phosphatase; Provisional
 603-840 2.05e-47

protein tyrosine phosphatase; Provisional


Pssm-ID: 165114 [Multi-domain]  Cd Length: 312  Bit Score: 172.49  E-value: 2.05e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578801331  603 IKEARKPFNQNKNRYVDILPYDYNRVELsEINGDAGSNYINASYIDGFKEPRKYIAAQGPRDETVDDFWRMIWEQKATVI 682
Cdd:PHA02747   43 IANFEKPENQPKNRYWDIPCWDHNRVIL-DSGGGSTSDYIHANWIDGFEDDKKFIATQGPFAETCADFWKAVWQEHCSII 121

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578801331  683 VMVTRCEEGN-RNKCAEYWPSMEEGTRAFGDVVVKINQHKRCPDYIIQKLNIVNKKEKaTGREVTHIQFTSWPDHGVPED 761
Cdd:PHA02747  122 VMLTPTKGTNgEEKCYQYWCLNEDGNIDMEDFRIETLKTSVRAKYILTLIEITDKILK-DSRKISHFQCSEWFEDETPSD 200

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578801331  762 PHLLLKL-----RRRVNAFSNFFS-----GPIVVHCSAGVGRTGTYIGIDAMLEGLEAENKVDVYGYVVKLRRQRCLMVQ 831
Cdd:PHA02747  201 HPDFIKFikiidINRKKSGKLFNPkdallCPIVVHCSDGVGKTGIFCAVDICLNQLVKRKAICLAKTAEKIREQRHAGIM 280


                  ....*....
gi 578801331  832 VEAQYILIH 840
Cdd:PHA02747  281 NFDDYLFIQ 289
PTPc_plant_PTP1 cd17658
protein tyrosine phosphatase 1 from Arabidopsis thaliana and similar plant PTPs; Arabidopsis ...
 641-840 2.30e-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: 168.41  E-value: 2.30e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578801331  641 YINASYI--DGFKEPRKYIAAQGPRDETVDDFWRMIWEQKATVIVMVTRCEEGNR-NKCAEYWPSMEEGTRAFGDVVVKI 717
Cdd:cd17658     1 YINASLVetPASESLPKFIATQGPLPHTFEDFWEMVIQQRCPVIIMLTRLVDNYStAKCADYFPAEENESREFGRISVTN 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578801331  718 NQHKrCPDYIIQKLNI-VNKKE-KATGREVTHIQFTSWPDHGVPEDPHLLLKLRRRVNAFSNFFsGPIVVHCSAGVGRTG 795
Cdd:cd17658    81 KKLK-HSQHSITLRVLeVQYIEsEEPPLSVLHIQYPEWPDHGVPKDTRSVRELLKRLYGIPPSA-GPIVVHCSAGIGRTG 158

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|
gi 578801331  796 TYIGID----AMLEG-LEAenkVDVYGYVVKLRRQRCLMVQVEAQYILIH 840
Cdd:cd17658   159 AYCTIHntirRILEGdMSA---VDLSKTVRKFRSQRIGMVQTQDQYIFCY 205
R-PTPc-F-1 cd14626
catalytic domain of receptor-type tyrosine-protein phosphatase F, repeat 1; Receptor-type ...
 898-1159 1.28e-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: 1.28e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578801331  898 NQEENKSKNRNSNVIPYDYNRVPLkhelemskesehdsdessdDDSDSEEPSKYINASFIMSYWKPEVMIAAQGPLKETI 977
Cdd:cd14626    37 NLEVNKPKNRYANVIAYDHSRVIL-------------------TSVDGVPGSDYINANYIDGYRKQNAYIATQGPLPETL 97

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578801331  978 GDFWQMIFQRKVKVIVMLTELKHGDQEICAQYW-GEGKQTYGDIEVDLKDTDKSSTYTLRVFELRHSKRKDSRTVYQYQY 1056
Cdd:cd14626    98 SDFWRMVWEQRTATIVMMTRLEEKSRVKCDQYWpIRGTETYGMIQVTLLDTVELATYSVRTFALYKNGSSEKREVRQFQF 177

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578801331 1057 TNWSVEQLPAEPKELISMIQVVKQKLPQknssegnkhhKSTPLLIHCRDGSQQTGIFCALLNLLESAETEEVVDIFQVVK 1136
Cdd:cd14626   178 MAWPDHGVPEYPTPILAFLRRVKACNPP----------DAGPMVVHCSAGVGRTGCFIVIDAMLERMKHEKTVDIYGHVT 247

                         250       260
                  ....*....|....*....|...
gi 578801331 1137 ALRKARPGMVSTFEQYQFLYDVI 1159
Cdd:cd14626   248 CMRSQRNYMVQTEDQYIFIHEAL 270
R-PTPc-T-1 cd14630
catalytic domain of receptor-type tyrosine-protein phosphatase T, repeat 1; Receptor-type ...
 900-1159 1.98e-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: 1.98e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578801331  900 EENKSKNRNSNVIPYDYNRVPLKhELEMSKEsehdsdessdddsdseepSKYINASFIMSYWKPEVMIAAQGPLKETIGD 979
Cdd:cd14630     1 DENRNKNRYGNIISYDHSRVRLQ-LLDGDPH------------------SDYINANYIDGYHRPRHYIATQGPMQETVKD 61

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578801331  980 FWQMIFQRKVKVIVMLTELKHGDQEICAQYWGEGKQTYGDIEVDLKDTDKSSTYTLRVFELRHSKRKDSRTVYQYQYTNW 1059
Cdd:cd14630    62 FWRMIWQENSASVVMVTNLVEVGRVKCVRYWPDDTEVYGDIKVTLIETEPLAEYVIRTFTVQKKGYHEIREIRQFHFTSW 141

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578801331 1060 SVEQLPAEPKELISMIQVVKQKLPQknssegnkhhKSTPLLIHCRDGSQQTGIFCALLNLLESAETEEVVDIFQVVKALR 1139
Cdd:cd14630   142 PDHGVPCYATGLLGFVRQVKFLNPP----------DAGPIVVHCSAGAGRTGCFIAIDIMLDMAENEGVVDIFNCVRELR 211

                         250       260
                  ....*....|....*....|
gi 578801331 1140 KARPGMVSTFEQYQFLYDVI 1159
Cdd:cd14630   212 AQRVNMVQTEEQYVFVHDAI 231
R-PTP-F-2 cd14629
PTP-like domain of receptor-type tyrosine-protein phosphatase F, repeat 2; Receptor-type ...
 852-1156 2.58e-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: 2.58e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578801331  852 TEVNLSELHPYLHNMKKRDPPSEPSPLEAEFQRLPSYRSWRTQHI-GNQEENKSKNRNSNVIPYDYNRVPLKhelemske 930
Cdd:cd14629     2 TEVPARNLYAHIQKLTQVPPGESVTAMELEFKLLANSKAHTSRFIsANLPCNKFKNRLVNIMPYELTRVCLQ-------- 73

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578801331  931 sehdsdessddDSDSEEPSKYINASFIMSYWKPEVMIAAQGPLKETIGDFWQMIFQRKVKVIVMLTELKHGDQEICAQYW 1010
Cdd:cd14629    74 -----------PIRGVEGSDYINASFIDGYRQQKAYIATQGPLAETTEDFWRMLWEHNSTIVVMLTKLREMGREKCHQYW 142

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578801331 1011 -GEGKQTYGDIEVDLKDTDKSSTYTLRVFELRHSKRKDSRTVYQYQYTNWSVEQLPAEPKELISMI-QVVKQKlpqknss 1088
Cdd:cd14629   143 pAERSARYQYFVVDPMAEYNMPQYILREFKVTDARDGQSRTIRQFQFTDWPEQGVPKTGEGFIDFIgQVHKTK------- 215

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 578801331 1089 egNKHHKSTPLLIHCRDGSQQTGIFCALLNLLESAETEEVVDIFQVVKALRKARPGMVSTFEQYQFLY 1156
Cdd:cd14629   216 --EQFGQDGPITVHCSAGVGRTGVFITLSIVLERMRYEGVVDMFQTVKTLRTQRPAMVQTEDQYQLCY 281
PTPc-KIM cd14547
catalytic domain of the kinase interaction motif (KIM) family of protein-tyrosine phosphatases; ...
 949-1156 4.70e-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: 4.70e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578801331  949 SKYINASFIMSY-WKPEVMIAAQGPLKETIGDFWQMIFQRKVKVIVMLTELKHGDQEiCAQYWGEGK-QTYGDIEVDLKD 1026
Cdd:cd14547    25 SSYINANYIRGYdGEEKAYIATQGPLPNTVADFWRMVWQEKTPIIVMITNLTEAKEK-CAQYWPEEEnETYGDFEVTVQS 103

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578801331 1027 TDKSSTYTLRVFELRHskRKDSRTVYQYQYTNWSVEQLPAEPKELISMIQVVKQkLPQKNSSEGnkhhkstPLLIHCRDG 1106
Cdd:cd14547   104 VKETDGYTVRKLTLKY--GGEKRYLKHYWYTSWPDHKTPEAAQPLLSLVQEVEE-ARQTEPHRG-------PIVVHCSAG 173

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|
gi 578801331 1107 SQQTGIFCALLNLLESAETEEVVDIFQVVKALRKARPGMVSTFEQYQFLY 1156
Cdd:cd14547   174 IGRTGCFIATSIGCQQLREEGVVDVLGIVCQLRLDRGGMVQTAEQYEFVH 223
R-PTPc-J cd14615
catalytic domain of receptor-type tyrosine-protein phosphatase J; Receptor-type ...
 906-1155 1.08e-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: 1.08e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578801331  906 NRNSNVIPYDYNRVPLKHElemskesehdsdessdddsdSEEPSKYINASFIMSYWKPEVMIAAQGPLKETIGDFWQMIF 985
Cdd:cd14615     1 NRYNNVLPYDISRVKLSVQ--------------------SHSTDDYINANYMPGYNSKKEFIAAQGPLPNTVKDFWRMVW 60

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578801331  986 QRKVKVIVMLTELKHGDQEICAQYW-GEGKQTYGDIEVDLKDTDKSSTYTLRVFELRHSKRKDSRTVYQYQYTNWSVEQL 1064
Cdd:cd14615    61 EKNVYAIVMLTKCVEQGRTKCEEYWpSKQKKDYGDITVTMTSEIVLPEWTIRDFTVKNAQTNESRTVRHFHFTSWPDHGV 140

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578801331 1065 PAEPKELISMIQVVKQKLPQknssegnkHHKSTPLLIHCRDGSQQTGIFCALLNLLESAETEEVVDIFQVVKALRKARPG 1144
Cdd:cd14615   141 PETTDLLINFRHLVREYMKQ--------NPPNSPILVHCSAGVGRTGTFIAIDRLIYQIENENVVDVYGIVYDLRMHRPL 212

                         250
                  ....*....|.
gi 578801331 1145 MVSTFEQYQFL 1155
Cdd:cd14615   213 MVQTEDQYVFL 223
R-PTPc-S-1 cd14625
catalytic domain of receptor-type tyrosine-protein phosphatase S, repeat 1; Receptor-type ...
 854-1159 1.08e-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: 1.08e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578801331  854 VNLSELHPYLHNMKKRDPPSepspLEAEFQRLPSYRSWRTQHiGNQEENKSKNRNSNVIPYDYNRVPLKhelemskeseh 933
Cdd:cd14625     4 IPISELAEHTERLKANDNLK----LSQEYESIDPGQQFTWEH-SNLEVNKPKNRYANVIAYDHSRVILQ----------- 67

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578801331  934 dsdessddDSDSEEPSKYINASFIMSYWKPEVMIAAQGPLKETIGDFWQMIFQRKVKVIVMLTELKHGDQEICAQYW-GE 1012
Cdd:cd14625    68 --------PIEGIMGSDYINANYIDGYRKQNAYIATQGPLPETFGDFWRMVWEQRSATVVMMTKLEEKSRIKCDQYWpSR 139

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578801331 1013 GKQTYGDIEVDLKDTDKSSTYTLRVFELRHSKRKDSRTVYQYQYTNWSVEQLPAEPKELISMIQVVKQKLPQknssegnk 1092
Cdd:cd14625   140 GTETYGMIQVTLLDTIELATFCVRTFSLHKNGSSEKREVRQFQFTAWPDHGVPEYPTPFLAFLRRVKTCNPP-------- 211

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 578801331 1093 hhKSTPLLIHCRDGSQQTGIFCALLNLLESAETEEVVDIFQVVKALRKARPGMVSTFEQYQFLYDVI 1159
Cdd:cd14625   212 --DAGPIVVHCSAGVGRTGCFIVIDAMLERIKHEKTVDIYGHVTLMRSQRNYMVQTEDQYSFIHDAL 276
R-PTPc-typeIIb-1 cd14555
catalytic domain of type IIb (or R2B) subfamily receptor-type tyrosine-protein phosphatases, ...
 951-1159 1.75e-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: 160.08  E-value: 1.75e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578801331  951 YINASFIMSYWKPEVMIAAQGPLKETIGDFWQMIFQRKVKVIVMLTELKHGDQEICAQYWGEGKQTYGDIEVDLKDTDKS 1030
Cdd:cd14555     1 YINANYIDGYHRPNHYIATQGPMQETVYDFWRMVWQENSASIVMVTNLVEVGRVKCSRYWPDDTEVYGDIKVTLVETEPL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578801331 1031 STYTLRVFELRHSKRKDSRTVYQYQYTNWSVEQLPAEPKELISMIQVVKQKLPQknssegnkhhKSTPLLIHCRDGSQQT 1110
Cdd:cd14555    81 AEYVVRTFALERRGYHEIREVRQFHFTGWPDHGVPYHATGLLGFIRRVKASNPP----------SAGPIVVHCSAGAGRT 150

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*....
gi 578801331 1111 GIFCALLNLLESAETEEVVDIFQVVKALRKARPGMVSTFEQYQFLYDVI 1159
Cdd:cd14555   151 GCYIVIDIMLDMAEREGVVDIYNCVKELRSRRVNMVQTEEQYIFIHDAI 199
PTP-N23 cd14539
PTP-like domain of tyrosine-protein phosphatase non-receptor type 23; Tyrosine-protein ...
 641-841 1.15e-43

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


Pssm-ID: 350387 [Multi-domain]  Cd Length: 205  Bit Score: 157.55  E-value: 1.15e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578801331  641 YINASYIDGFKE--PRkYIAAQGPRDETVDDFWRMIWEQKATVIVMVTRCEEGNRNKCAEYWPSMEEGTRAFGDVVVKIN 718
Cdd:cd14539     1 YINASLIEDLTPycPR-FIATQAPLPGTAADFWLMVYEQQVSVIVMLVSEQENEKQKVHRYWPTERGQALVYGAITVSLQ 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578801331  719 QHKRCPDYIIQKLNIVNKKEKATgREVTHIQFTSWPDHGVPEDPHLLLKLRRRVNAFSNFFSG---PIVVHCSAGVGRTG 795
Cdd:cd14539    80 SVRTTPTHVERIISIQHKDTRLS-RSVVHLQFTTWPELGLPDSPNPLLRFIEEVHSHYLQQRSlqtPIVVHCSSGVGRTG 158

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*...
gi 578801331  796 TY-IGIDAMLEgLEAENKV-DVYGYVVKLRRQRCLMVQVEAQYILIHQ 841
Cdd:cd14539   159 AFcLLYAAVQE-IEAGNGIpDLPQLVRKMRQQRKYMLQEKEHLKFCYE 205
PTPc-N4 cd14601
catalytic domain of tyrosine-protein phosphatase non-receptor type 4; Tyrosine-protein ...
 640-845 1.41e-43

catalytic domain of tyrosine-protein phosphatase non-receptor type 4; Tyrosine-protein phosphatase non-receptor type 4 (PTPN4), also called protein-tyrosine phosphatase MEG1, belongs to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. PTPN4 functions in TCR cell signaling, apoptosis, cerebellar synaptic plasticity, and innate immune responses. It specifically inhibits the TRIF-dependent TLR4 pathway by suppressing tyrosine phosphorylation of TRAM. It is a large modular protein containing an N-terminal FERM domain, a PDZ domain and a C-terminal catalytic PTP domain; the PDZ domain regulates the catalytic activity of PTPN4.


Pssm-ID: 350449 [Multi-domain]  Cd Length: 212  Bit Score: 157.80  E-value: 1.41e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578801331  640 NYINASYID----GFKEPRKYIAAQGPRDETVDDFWRMIWEQKATVIVMVTRCEEGNRNKCAEYWPSMeEGTRAFGDVVV 715
Cdd:cd14601     1 DYINANYINmeipSSSIINRYIACQGPLPNTCSDFWQMTWEQGSSMVVMLTTQVERGRVKCHQYWPEP-SGSSSYGGFQV 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578801331  716 KINQHKRCPDYIIQKLNIVNkKEKATGREVTHIQFTSWPDHGVPEDPHLLLKLRRRVNAFSNFFSGPIVVHCSAGVGRTG 795
Cdd:cd14601    80 TCHSEEGNPAYVFREMTLTN-LEKNESRPLTQIQYIAWPDHGVPDDSSDFLDFVCLVRNKRAGKDEPVVVHCSAGIGRTG 158

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|
gi 578801331  796 TYIGIDAMLEGLEAENKVDVYGYVVKLRRQRCLMVQVEAQYILIHQALVE 845
Cdd:cd14601   159 VLITMETAMCLIECNQPVYPLDIVRTMRDQRAMMIQTPSQYRFVCEAILK 208
PTPc-N12 cd14604
catalytic domain of tyrosine-protein phosphatase non-receptor type 12; Tyrosine-protein ...
 863-1166 2.29e-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: 2.29e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578801331  863 LHNMKKRDPPSEPSpLEAEFQRLPSYRS-WRTQHI-----GNQEENKSKNRNSNVIPYDYNRVPLKheLEMSKESehdsd 936
Cdd:cd14604    13 VQAMKSTDHNGEDN-FASDFMRLRRLSTkYRTEKIyptatGEKEENVKKNRYKDILPFDHSRVKLT--LKTSSQD----- 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578801331  937 essdddsdseepSKYINASFIMSYWKPEVMIAAQGPLKETIGDFWQMIFQRKVKVIVMLT-ELKHGDQEiCAQYW---GE 1012
Cdd:cd14604    85 ------------SDYINANFIKGVYGPKAYIATQGPLANTVIDFWRMIWEYNVAIIVMACrEFEMGRKK-CERYWplyGE 151

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578801331 1013 GKQTYGDIEVDLKDTDKSSTYTLRVFELRHskRKDSRTVYQYQYTNWSVEQLPAEPKELISMIQVVKQklpqknssegNK 1092
Cdd:cd14604   152 EPMTFGPFRISCEAEQARTDYFIRTLLLEF--QNETRRLYQFHYVNWPDHDVPSSFDSILDMISLMRK----------YQ 219

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 578801331 1093 HHKSTPLLIHCRDGSQQTGIFCAL---LNLLESAETEEVVDIFQVVKALRKARPGMVSTFEQYQFLYDVIASTYPAQ 1166
Cdd:cd14604   220 EHEDVPICIHCSAGCGRTGAICAIdytWNLLKAGKIPEEFNVFNLIQEMRTQRHSAVQTKEQYELVHRAIAQLFEKQ 296
PTPc-N21 cd14598
catalytic domain of tyrosine-protein phosphatase non-receptor type 21; Tyrosine-protein ...
 641-846 2.56e-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: 2.56e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578801331  641 YINASYID---GFKEpRKYIAAQGPRDETVDDFWRMIWEQKATVIVMVTRCEEGNRNKCAEYWPSM--EEGTRAFGDVVV 715
Cdd:cd14598     1 YINASHIKvtvGGKE-WDYIATQGPLQNTCQDFWQMVWEQGVAIIAMVTAEEEGGREKSFRYWPRLgsRHNTVTYGRFKI 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578801331  716 KINQHKRCPDYIIQKLNIvnkKEKATGREVT--HIQFTSWPDHGVPEDPHLLL-------KLRRRVNAFSNFFSG--PIV 784
Cdd:cd14598    80 TTRFRTDSGCYATTGLKI---KHLLTGQERTvwHLQYTDWPEHGCPEDLKGFLsyleeiqSVRRHTNSTIDPKSPnpPVL 156

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 578801331  785 VHCSAGVGRTGTYIGIDAMLEGLEAENKVDVYGYVVKLRRQRCLMVQVEAQYILIHQALVEY 846
Cdd:cd14598   157 VHCSAGVGRTGVVILSEIMIACLEHNEMLDIPRVLDMLRQQRMMMVQTLSQYTFVYKVLIQF 218
PHA02738 PHA02738
hypothetical protein; Provisional
 611-854 3.38e-43

hypothetical protein; Provisional


Pssm-ID: 222923 [Multi-domain]  Cd Length: 320  Bit Score: 160.48  E-value: 3.38e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578801331  611 NQNKNRYVDILPYDYNRVEL-SEINGdagSNYINASYIDGFKEPRKYIAAQGPRDETVDDFWRMIWEQKATVIVMVTRCE 689
Cdd:PHA02738   49 NRKLNRYLDAVCFDHSRVILpAERNR---GDYINANYVDGFEYKKKFICGQAPTRQTCYDFYRMLWMEHVQIIVMLCKKK 125

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578801331  690 EGNRNKCAEYWPSMEEGTRAFGDVVVKINQHKRCPDYIIQKLNIVNKKEkATgREVTHIQFTSWPDHGVPEDPHLLLKLR 769
Cdd:PHA02738  126 ENGREKCFPYWSDVEQGSIRFGKFKITTTQVETHPHYVKSTLLLTDGTS-AT-QTVTHFNFTAWPDHDVPKNTSEFLNFV 203

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578801331  770 RRV---------NAFSN----FFSGPIVVHCSAGVGRTGTYIGIDAMLEGLEAENKVDVYGYVVKLRRQRCLMVQVEAQY 836
Cdd:PHA02738  204 LEVrqcqkelaqESLQIghnrLQPPPIVVHCNAGLGRTPCYCVVDISISRFDACATVSIPSIVSSIRNQRYYSLFIPFQY 283

                         250
                  ....*....|....*...
gi 578801331  837 ILIHQALVEYNQFGETEV 854
Cdd:PHA02738  284 FFCYRAVKRYVNLTVNKV 301
R-PTPc-G-1 cd17667
catalytic domain of receptor-type tyrosine-protein phosphatase G, repeat 1; Receptor-type ...
 881-1159 4.59e-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: 4.59e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578801331  881 EFQRLPSYRSWRTQHiGNQEENKSKNRNSNVIPYDYNRVPLKhelemskesehdsdessDDDSDSEEPSKYINASFIMSY 960
Cdd:cd17667     7 EVQRCTADMNITAEH-SNHPDNKHKNRYINILAYDHSRVKLR-----------------PLPGKDSKHSDYINANYVDGY 68

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578801331  961 WKPEVMIAAQGPLKETIGDFWQMIFQRKVKVIVMLTELKHGDQEICAQYW-GEGKQTYGDIEVDLKDTDKSSTYTLRVFE 1039
Cdd:cd17667    69 NKAKAYIATQGPLKSTFEDFWRMIWEQNTGIIVMITNLVEKGRRKCDQYWpTENSEEYGNIIVTLKSTKIHACYTVRRFS 148

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578801331 1040 LRHSK-----------RKDSRTVYQYQYTNWSVEQLPAEPKELISMIQvvkqklpqknSSEGNKHHKSTPLLIHCRDGSQ 1108
Cdd:cd17667   149 IRNTKvkkgqkgnpkgRQNERTVIQYHYTQWPDMGVPEYALPVLTFVR----------RSSAARTPEMGPVLVHCSAGVG 218

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|.
gi 578801331 1109 QTGIFCALLNLLESAETEEVVDIFQVVKALRKARPGMVSTFEQYQFLYDVI 1159
Cdd:cd17667   219 RTGTYIVIDSMLQQIKDKSTVNVLGFLKHIRTQRNYLVQTEEQYIFIHDAL 269
PHA02742 PHA02742
protein tyrosine phosphatase; Provisional
 601-846 5.46e-43

protein tyrosine phosphatase; Provisional


Pssm-ID: 165109 [Multi-domain]  Cd Length: 303  Bit Score: 159.40  E-value: 5.46e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578801331  601 FPIKEARKPFNQNKNRYVDILPYDYNRVELSEINGdaGSNYINASYIDGFKEPRKYIAAQGPRDETVDDFWRMIWEQKAT 680
Cdd:PHA02742   42 FSCNESLELKNMKKCRYPDAPCFDRNRVILKIEDG--GDDFINASYVDGHNAKGRFICTQAPLEETALDFWQAIFQDQVR 119

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578801331  681 VIVMVTRCEEGNRNKCAEYWPSMEEGTRAFGDVVVKINQHKRCPDYIIQKLNIVNKKeKATGREVTHIQFTSWPDHGVPE 760
Cdd:PHA02742  120 VIVMITKIMEDGKEACYPYWMPHERGKATHGEFKIKTKKIKSFRNYAVTNLCLTDTN-TGASLDIKHFAYEDWPHGGLPR 198

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578801331  761 DP-----------HLLLKLRRRVNAFSNFFSGPIVVHCSAGVGRTGTYIGIDAMLEGLEAENKVDVYGYVVKLRRQRCLM 829
Cdd:PHA02742  199 DPnkfldfvlavrEADLKADVDIKGENIVKEPPILVHCSAGLDRAGAFCAIDICISKYNERAIIPLLSIVRDLRKQRHNC 278

                         250
                  ....*....|....*..
gi 578801331  830 VQVEAQYILIHQALVEY 846
Cdd:PHA02742  279 LSLPQQYIFCYFIVLIF 295
R-PTPc-M-1 cd14633
catalytic domain of receptor-type tyrosine-protein phosphatase M, repeat 1; Receptor-type ...
 899-1159 1.23e-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: 1.23e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578801331  899 QEENKSKNRNSNVIPYDYNRVPLKhELEMSKEsehdsdessdddsdseepSKYINASFIMSYWKPEVMIAAQGPLKETIG 978
Cdd:cd14633    37 KDENRMKNRYGNIIAYDHSRVRLQ-PIEGETS------------------SDYINGNYIDGYHRPNHYIATQGPMQETIY 97

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578801331  979 DFWQMIFQRKVKVIVMLTELKHGDQEICAQYWGEGKQTYGDIEVDLKDTDKSSTYTLRVFELRHSKRKDSRTVYQYQYTN 1058
Cdd:cd14633    98 DFWRMVWHENTASIIMVTNLVEVGRVKCCKYWPDDTEIYKDIKVTLIETELLAEYVIRTFAVEKRGVHEIREIRQFHFTG 177

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578801331 1059 WSVEQLPAEPKELISMIQVVKQKLPQknssegnkhhKSTPLLIHCRDGSQQTGIFCALLNLLESAETEEVVDIFQVVKAL 1138
Cdd:cd14633   178 WPDHGVPYHATGLLGFVRQVKSKSPP----------NAGPLVVHCSAGAGRTGCFIVIDIMLDMAEREGVVDIYNCVREL 247

                         250       260
                  ....*....|....*....|.
gi 578801331 1139 RKARPGMVSTFEQYQFLYDVI 1159
Cdd:cd14633   248 RSRRVNMVQTEEQYVFIHDAI 268
R-PTPc-A-1 cd14621
catalytic domain of receptor-type tyrosine-protein phosphatase A, repeat 1; Receptor-type ...
 881-1163 3.78e-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: 156.72  E-value: 3.78e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578801331  881 EFQRLPSYRSWRTQHIGNQEENKSKNRNSNVIPYDYNRVPLkhelemskesehdsdessdDDSDSEEPSKYINASFIMSY 960
Cdd:cd14621    31 EFNALPACPIQATCEAASKEENKEKNRYVNILPYDHSRVHL-------------------TPVEGVPDSDYINASFINGY 91

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578801331  961 WKPEVMIAAQGPLKETIGDFWQMIFQRKVKVIVMLTELKHGDQEICAQYW-GEGKQTYGDIEVDLKDTDKSSTYTLRVFE 1039
Cdd:cd14621    92 QEKNKFIAAQGPKEETVNDFWRMIWEQNTATIVMVTNLKERKECKCAQYWpDQGCWTYGNIRVSVEDVTVLVDYTVRKFC 171

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578801331 1040 LRH----SKRKDSRTVYQYQYTNWSVEQLPAEPKELISMIQVVKQKLPQknssegnkhhKSTPLLIHCRDGSQQTGIFCA 1115
Cdd:cd14621   172 IQQvgdvTNKKPQRLITQFHFTSWPDFGVPFTPIGMLKFLKKVKNCNPQ----------YAGAIVVHCSAGVGRTGTFIV 241

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*...
gi 578801331 1116 LLNLLESAETEEVVDIFQVVKALRKARPGMVSTFEQYQFLYDVIASTY 1163
Cdd:cd14621   242 IDAMLDMMHAERKVDVYGFVSRIRAQRCQMVQTDMQYVFIYQALLEHY 289
R-PTP-N2 cd14610
PTP-like domain of receptor-type tyrosine-protein phosphatase N2; Receptor-type ...
 856-1160 4.02e-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: 4.02e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578801331  856 LSELHPYLHNmKKRdppsepspLEAEFQRLPSYRSW-RTQHIGNQEENKSKNRNSNVIPYDYNRVPLKHELEMSKesehd 934
Cdd:cd14610     6 LSYMEDHLKN-KNR--------LEKEWEALCAYQAEpNATNVAQREENVQKNRSLAVLPYDHSRIILKAENSHSH----- 71

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578801331  935 sdessdddsdseepSKYINASFIMSYwKPE--VMIAAQGPLKETIGDFWQMIFQRKVKVIVMLTELKHGDQEICAQYW-G 1011
Cdd:cd14610    72 --------------SDYINASPIMDH-DPRnpAYIATQGPLPATVADFWQMVWESGCVVIVMLTPLAENGVKQCYHYWpD 136

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578801331 1012 EGKQTYGDIEVDL-KDTDKSSTYTLRVFELRHSKRKDSRTVYQYQYTNWSVEQLPAEPKELISMIQVVkqklpqknsseg 1090
Cdd:cd14610   137 EGSNLYHIYEVNLvSEHIWCEDFLVRSFYLKNLQTNETRTVTQFHFLSWNDQGVPASTRSLLDFRRKV------------ 204

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 578801331 1091 NKHH--KSTPLLIHCRDGSQQTGIFCAL-LNLLESAETEEVVDIFQVVKALRKARPGMVSTFEQYQFLYDVIA 1160
Cdd:cd14610   205 NKCYrgRSCPIIVHCSDGAGRSGTYILIdMVLNKMAKGAKEIDIAATLEHLRDQRPGMVQTKEQFEFALTAVA 277
R-PTPc-D-1 cd14624
catalytic domain of receptor-type tyrosine-protein phosphatase D, repeat 1; Receptor-type ...
 881-1159 4.99e-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: 4.99e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578801331  881 EFQRLPSYRSWRTQHiGNQEENKSKNRNSNVIPYDYNRVPLKhelemskesehdsdessddDSDSEEPSKYINASFIMSY 960
Cdd:cd14624    27 EYESIDPGQQFTWEH-SNLEVNKPKNRYANVIAYDHSRVLLS-------------------AIEGIPGSDYINANYIDGY 86

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578801331  961 WKPEVMIAAQGPLKETIGDFWQMIFQRKVKVIVMLTELKHGDQEICAQYW-GEGKQTYGDIEVDLKDTDKSSTYTLRVFE 1039
Cdd:cd14624    87 RKQNAYIATQGALPETFGDFWRMIWEQRSATVVMMTKLEERSRVKCDQYWpSRGTETYGLIQVTLLDTVELATYCVRTFA 166

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578801331 1040 LRHSKRKDSRTVYQYQYTNWSVEQLPAEPKELISMIQVVKQKLPQknssegnkhhKSTPLLIHCRDGSQQTGIFCALLNL 1119
Cdd:cd14624   167 LYKNGSSEKREVRQFQFTAWPDHGVPEHPTPFLAFLRRVKTCNPP----------DAGPMVVHCSAGVGRTGCFIVIDAM 236

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|
gi 578801331 1120 LESAETEEVVDIFQVVKALRKARPGMVSTFEQYQFLYDVI 1159
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 ...
 951-1160 1.35e-41

PTP-like domain of receptor-type tyrosine-protein phosphatase-like N and N2; Receptor-type tyrosine-protein phosphatase-like N (PTPRN) and N2 (PTPRN2) belong to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). They consist of a large ectodomain that contains a RESP18HD (regulated endocrine-specific protein 18 homology domain), followed by a transmembrane segment, and a single, catalytically-impaired, PTP domain. They are mainly expressed in neuropeptidergic neurons and peptide-secreting endocrine cells, including insulin-producing pancreatic beta-cells, and are involved in involved in the generation, cargo storage, traffic, exocytosis and recycling of insulin secretory granules, as well as in beta-cell proliferation. They also are major autoantigens in type 1 diabetes and are involved in the regulation of insulin secretion.


Pssm-ID: 350394 [Multi-domain]  Cd Length: 208  Bit Score: 151.83  E-value: 1.35e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578801331  951 YINASFIMSYwKPE--VMIAAQGPLKETIGDFWQMIFQRKVKVIVMLTELKHGDQEICAQYW-GEGKQTYGDIEVDL-KD 1026
Cdd:cd14546     1 YINASTIYDH-DPRnpAYIATQGPLPHTIADFWQMIWEQGCVVIVMLTRLQENGVKQCARYWpEEGSEVYHIYEVHLvSE 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578801331 1027 TDKSSTYTLRVFELRHSKRKDSRTVYQYQYTNWSVEQLPAEPKELISMIQVVKQKLpqknssegnkHHKSTPLLIHCRDG 1106
Cdd:cd14546    80 HIWCDDYLVRSFYLKNLQTSETRTVTQFHFLSWPDEGIPASAKPLLEFRRKVNKSY----------RGRSCPIVVHCSDG 149

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 578801331 1107 SQQTGIFCAL---LNLLESAETEevVDIFQVVKALRKARPGMVSTFEQYQFLYDVIA 1160
Cdd:cd14546   150 AGRTGTYILIdmvLNRMAKGAKE--IDIAATLEHLRDQRPGMVKTKDQFEFVLTAVA 204
R-PTPc-U-1 cd14632
catalytic domain of receptor-type tyrosine-protein phosphatase U, repeat 1; Receptor-type ...
 951-1159 1.66e-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: 1.66e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578801331  951 YINASFIMSYWKPEVMIAAQGPLKETIGDFWQMIFQRKVKVIVMLTELKHGDQEICAQYWGEGKQTYGDIEVDLKDTDKS 1030
Cdd:cd14632     1 YINANYIDGYHRSNHFIATQGPKQEMVYDFWRMVWQEHCSSIVMITKLVEVGRVKCSKYWPDDSDTYGDIKITLLKTETL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578801331 1031 STYTLRVFELRHSKRKDSRTVYQYQYTNWSVEQLPAEPKELISMIQVVKQKLPQknssegnkhhKSTPLLIHCRDGSQQT 1110
Cdd:cd14632    81 AEYSVRTFALERRGYSARHEVKQFHFTSWPEHGVPYHATGLLAFIRRVKASTPP----------DAGPVVVHCSAGAGRT 150

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*....
gi 578801331 1111 GIFCALLNLLESAETEEVVDIFQVVKALRKARPGMVSTFEQYQFLYDVI 1159
Cdd:cd14632   151 GCYIVLDVMLDMAECEGVVDIYNCVKTLCSRRINMIQTEEQYIFIHDAI 199
R-PTPc-O cd14614
catalytic domain of receptor-type tyrosine-protein phosphatase O; Receptor-type ...
 902-1156 1.74e-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: 1.74e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578801331  902 NKSKNRNSNVIPYDYNRVPL--KHELEmskesehdsdessdddsdseePSKYINASFIMSYWKPEVMIAAQGPLKETIGD 979
Cdd:cd14614    12 NRCKNRYTNILPYDFSRVKLvsMHEEE---------------------GSDYINANYIPGYNSPQEYIATQGPLPETRND 70

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578801331  980 FWQMIFQRKVKVIVMLTELKHGDQEICAQYW--GEGKQTYGDIEVDLKDTDKSSTYTLRVFELRHSkrKDSRTVYQYQYT 1057
Cdd:cd14614    71 FWKMVLQQKSQIIVMLTQCNEKRRVKCDHYWpfTEEPVAYGDITVEMLSEEEQPDWAIREFRVSYA--DEVQDVMHFNYT 148

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578801331 1058 NWSVEQLPA--EPKELISMIQVVKQklpQKNSSEGnkhhkstPLLIHCRDGSQQTGIFCALLNLLESAETEEVVDIFQVV 1135
Cdd:cd14614   149 AWPDHGVPTanAAESILQFVQMVRQ---QAVKSKG-------PMIIHCSAGVGRTGTFIALDRLLQHIRDHEFVDILGLV 218

                         250       260
                  ....*....|....*....|.
gi 578801331 1136 KALRKARPGMVSTFEQYQFLY 1156
Cdd:cd14614   219 SEMRSYRMSMVQTEEQYIFIH 239
PTPc-N18 cd14603
catalytic domain of tyrosine-protein phosphatase non-receptor type 18; Tyrosine-protein ...
 893-1163 2.04e-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: 2.04e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578801331  893 TQHIGNQEENKSKNRNSNVIPYDYNRV---PLKHELEmskesehdsdessdddsdseepSKYINASFIMSYWKPEVMIAA 969
Cdd:cd14603    21 STVAGGRKENVKKNRYKDILPYDQTRVilsLLQEEGH----------------------SDYINANFIKGVDGSRAYIAT 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578801331  970 QGPLKETIGDFWQMIFQRKVKVIVM-LTELKHGDQEiCAQYWGEGKQT--YGDIEV-DLKDTDKSSTYTLRVfeLRHSKR 1045
Cdd:cd14603    79 QGPLSHTVLDFWRMIWQYGVKVILMaCREIEMGKKK-CERYWAQEQEPlqTGPFTItLVKEKRLNEEVILRT--LKVTFQ 155

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578801331 1046 KDSRTVYQYQYTNWSVEQLPAEPKELISMIQVVKQKlpQKNSSEgnkhhkstPLLIHCRDGSQQTGIFCAL---LNLLES 1122
Cdd:cd14603   156 KESRSVSHFQYMAWPDHGIPDSPDCMLAMIELARRL--QGSGPE--------PLCVHCSAGCGRTGVICTVdyvRQLLLT 225

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|.
gi 578801331 1123 AETEEVVDIFQVVKALRKARPGMVSTFEQYQFLYDVIASTY 1163
Cdd:cd14603   226 QRIPPDFSIFDVVLEMRKQRPAAVQTEEQYEFLYHTVAQMF 266
R-PTPc-A-E-1 cd14551
catalytic domain of receptor-type tyrosine-protein phosphatase A and E, repeat 1; ...
 951-1156 2.63e-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: 2.63e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578801331  951 YINASFIMSYWKPEVMIAAQGPLKETIGDFWQMIFQRKVKVIVMLTELKHGDQEICAQYW-GEGKQTYGDIEVDLKDTDK 1029
Cdd:cd14551     1 YINASYIDGYQEKNKFIAAQGPKDETVNDFWRMIWEQGSATIVMVTNLKERKEKKCSQYWpDQGCWTYGNLRVRVEDTVV 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578801331 1030 SSTYTLRVFELRH----SKRKDSRTVYQYQYTNWSVEQLPAEPKELISMIQVVKQKLPQKNSsegnkhhkstPLLIHCRD 1105
Cdd:cd14551    81 LVDYTTRKFCIQKvnrgIGEKRVRLVTQFHFTSWPDFGVPFTPIGMLKFLKKVKSANPPRAG----------PIVVHCSA 150

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|.
gi 578801331 1106 GSQQTGIFCALLNLLESAETEEVVDIFQVVKALRKARPGMVSTFEQYQFLY 1156
Cdd:cd14551   151 GVGRTGTFIVIDAMLDMMHAEGKVDVFGFVSRIRQQRSQMVQTDMQYVFIY 201
R-PTPc-Z-1 cd17668
catalytic domain of receptor-type tyrosine-protein phosphatase Z, repeat 1; Receptor-type ...
 951-1159 2.81e-41

catalytic domain of receptor-type tyrosine-protein phosphatase Z, repeat 1; Receptor-type tyrosine-protein phosphatase Z (PTPRZ), also called receptor-type tyrosine-protein phosphatase zeta (R-PTP-zeta), belongs to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. Three isoforms are generated by alternative splicing from a single PTPRZ gene: two transmembrane isoforms, PTPRZ-A and PTPRZ-B, and one secretory isoform, PTPRZ-S (also known as phosphacan); all are preferentially expressed in the central nervous system (CNS) as chondroitin sulfate (CS) proteoglycans. PTPRZ isoforms play important roles in maintaining oligodendrocyte precursor cells in an undifferentiated state. PTPRZ is a type 1 integral membrane protein consisting of an extracellular region with a carbonic anhydrase-like (CAH) and a fibronectin type III (FN3) domains, and an intracellular region with a catalytic PTP domain (repeat 1) proximal to the membrane, and a catalytically inactive PTP-fold domain (repeat 2) distal to the membrane. This model represents the catalytic PTP domain (repeat 1).


Pssm-ID: 350506 [Multi-domain]  Cd Length: 209  Bit Score: 150.90  E-value: 2.81e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578801331  951 YINASFIMSYWKPEVMIAAQGPLKETIGDFWQMIFQRKVKVIVMLTELKHGDQEICAQYW-GEGKQTYGDIEVDLKDTDK 1029
Cdd:cd17668     1 YINANYVDGYNKPKAYIAAQGPLKSTAEDFWRMIWEHNVEVIVMITNLVEKGRRKCDQYWpADGSEEYGNFLVTQKSVQV 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578801331 1030 SSTYTLRVFELRHSK--------RKDSRTVYQYQYTNWSVEQLPAEPKELISMIQvvkqklpqknSSEGNKHHKSTPLLI 1101
Cdd:cd17668    81 LAYYTVRNFTLRNTKikkgsqkgRPSGRVVTQYHYTQWPDMGVPEYTLPVLTFVR----------KASYAKRHAVGPVVV 150

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 578801331 1102 HCRDGSQQTGIFCALLNLLESAETEEVVDIFQVVKALRKARPGMVSTFEQYQFLYDVI 1159
Cdd:cd17668   151 HCSAGVGRTGTYIVLDSMLQQIQHEGTVNIFGFLKHIRSQRNYLVQTEEQYVFIHDAL 208
R-PTPc-K-1 cd14631
catalytic domain of receptor-type tyrosine-protein phosphatase K, repeat 1; Receptor-type ...
 949-1159 3.46e-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: 150.94  E-value: 3.46e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578801331  949 SKYINASFIMSYWKPEVMIAAQGPLKETIGDFWQMIFQRKVKVIVMLTELKHGDQEICAQYWGEGKQTYGDIEVDLKDTD 1028
Cdd:cd14631    13 SDYINANYIDGYQRPSHYIATQGPVHETVYDFWRMIWQEQSACIVMVTNLVEVGRVKCYKYWPDDTEVYGDFKVTCVEME 92

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578801331 1029 KSSTYTLRVFELRHSKRKDSRTVYQYQYTNWSVEQLPAEPKELISMIQVVKQKLPQknssegnkhhKSTPLLIHCRDGSQ 1108
Cdd:cd14631    93 PLAEYVVRTFTLERRGYNEIREVKQFHFTGWPDHGVPYHATGLLSFIRRVKLSNPP----------SAGPIVVHCSAGAG 162

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|.
gi 578801331 1109 QTGIFCALLNLLESAETEEVVDIFQVVKALRKARPGMVSTFEQYQFLYDVI 1159
Cdd:cd14631   163 RTGCYIVIDIMLDMAEREGVVDIYNCVKALRSRRINMVQTEEQYIFIHDAI 213
R-PTPc-E-1 cd14620
catalytic domain of receptor-type tyrosine-protein phosphatase E, repeat 1; Receptor-type ...
 910-1159 6.79e-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: 150.86  E-value: 6.79e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578801331  910 NVIPYDYNRVPLKHelemskesehdsdessdddSDSEEPSKYINASFIMSYWKPEVMIAAQGPLKETIGDFWQMIFQRKV 989
Cdd:cd14620     3 NILPYDHSRVILSQ-------------------LDGIPCSDYINASYIDGYKEKNKFIAAQGPKQETVNDFWRMVWEQKS 63

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578801331  990 KVIVMLTELKHGDQEICAQYWGE-GKQTYGDIEVDLKDTDKSSTYTLRVFELR---HSKRKDSRTVYQYQYTNWSVEQLP 1065
Cdd:cd14620    64 ATIVMLTNLKERKEEKCYQYWPDqGCWTYGNIRVAVEDCVVLVDYTIRKFCIQpqlPDGCKAPRLVTQLHFTSWPDFGVP 143

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578801331 1066 AEPkelISMIQVVKqKLPQKNSSEGNkhhkstPLLIHCRDGSQQTGIFCALLNLLESAETEEVVDIFQVVKALRKARPGM 1145
Cdd:cd14620   144 FTP---IGMLKFLK-KVKSVNPVHAG------PIVVHCSAGVGRTGTFIVIDAMIDMMHAEQKVDVFEFVSRIRNQRPQM 213

                         250
                  ....*....|....
gi 578801331 1146 VSTFEQYQFLYDVI 1159
Cdd:cd14620   214 VQTDMQYSFIYQAL 227
R-PTPc-C-1 cd14557
catalytic domain of receptor-type tyrosine-protein phosphatase C, repeat 1; Receptor-type ...
 951-1156 1.24e-40

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


Pssm-ID: 350405 [Multi-domain]  Cd Length: 201  Bit Score: 148.82  E-value: 1.24e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578801331  951 YINASFIMSYWKPEVMIAAQGPLKETIGDFWQMIFQRKVKVIVMLTELKHGDQEICAQYW---GEGKQTYGDIEVDLKDT 1027
Cdd:cd14557     1 YINASYIDGFKEPRKYIAAQGPKDETVDDFWRMIWEQKSTVIVMVTRCEEGNRNKCAQYWpsmEEGSRAFGDVVVKINEE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578801331 1028 DKSSTYTLRVFELRHSKRKDS-RTVYQYQYTNWSVEQLPAEPKELIsmiqvvkqKLPQKNSSEGNKHhkSTPLLIHCRDG 1106
Cdd:cd14557    81 KICPDYIIRKLNINNKKEKGSgREVTHIQFTSWPDHGVPEDPHLLL--------KLRRRVNAFNNFF--SGPIVVHCSAG 150

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|
gi 578801331 1107 SQQTGIFCALLNLLESAETEEVVDIFQVVKALRKARPGMVSTFEQYQFLY 1156
Cdd:cd14557   151 VGRTGTYIGIDAMLEGLEAEGRVDVYGYVVKLRRQRCLMVQVEAQYILIH 200
R-PTPc-Q cd14616
catalytic domain of receptor-type tyrosine-protein phosphatase Q; Receptor-type ...
 906-1156 1.82e-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: 1.82e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578801331  906 NRNSNVIPYDYNRVPLKHElemskesehdsdessdddsDSEEPSKYINASFIMSYWKPEVMIAAQGPLKETIGDFWQMIF 985
Cdd:cd14616     1 NRFPNIKPYNNNRVKLIAD-------------------AGVPGSDYINASYISGYLCPNEFIATQGPLPGTVGDFWRMVW 61

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578801331  986 QRKVKVIVMLTELKHGDQEICAQYWGEGKQ---TYGDIEVDLKDTDKSSTYTLRvfELRHSKRKDSRTVYQYQYTNWSVE 1062
Cdd:cd14616    62 ETRAKTIVMLTQCFEKGRIRCHQYWPEDNKpvtVFGDIVITKLMEDVQIDWTIR--DLKIERHGDYMMVRQCNFTSWPEH 139

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578801331 1063 QLPAEPKELISMIQVVKqklpqknsseGNKHHKSTPLLIHCRDGSQQTGIFCALLNLLESAETEEVVDIFQVVKALRKAR 1142
Cdd:cd14616   140 GVPESSAPLIHFVKLVR----------ASRAHDNTPMIVHCSAGVGRTGVFIALDHLTQHINDHDFVDIYGLVAELRSER 209

                         250
                  ....*....|....
gi 578801331 1143 PGMVSTFEQYQFLY 1156
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; ...
 951-1156 3.36e-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: 147.57  E-value: 3.36e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578801331  951 YINASFIMSYWKPEVMIAAQGPLKETIGDFWQMIFQRKVKVIVMLTELKHGDQEICAQYW---GEGKQTYGDIEVDL-KD 1026
Cdd:cd14542     1 YINANFIKGVSGSKAYIATQGPLPNTVLDFWRMIWEYNVQVIVMACREFEMGKKKCERYWpeeGEEQLQFGPFKISLeKE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578801331 1027 TDKSSTYTLRVFELRHSkrKDSRTVYQYQYTNWSVEQLPAEPKELISMIQVVKQKlpqknssegnKHHKSTPLLIHCRDG 1106
Cdd:cd14542    81 KRVGPDFLIRTLKVTFQ--KESRTVYQFHYTAWPDHGVPSSVDPILDLVRLVRDY----------QGSEDVPICVHCSAG 148

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 578801331 1107 SQQTGIFCAL---LNLLESAETEEVVDIFQVVKALRKARPGMVSTFEQYQFLY 1156
Cdd:cd14542   149 CGRTGTICAIdyvWNLLKTGKIPEEFSLFDLVREMRKQRPAMVQTKEQYELVY 201
R-PTPc-typeIIb-2 cd14556
PTP domain of type IIb (or R2B) subfamily receptor-type tyrosine-protein phosphatases, repeat ...
 641-841 5.66e-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: 5.66e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578801331  641 YINASYIDGFKEPRKYIAAQGPRDETVDDFWRMIWEQKATVIVMVTRCEEGNRNkCAEYWPsmEEGTRAFGDVVVKINQH 720
Cdd:cd14556     1 YINAALLDSYKQPAAFIVTQHPLPNTVTDFWRLVYDYGCTSIVMLNQLDPKDQS-CPQYWP--DEGSGTYGPIQVEFVST 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578801331  721 KRCPDYIIQKLNIVNKKEKATG-REVTHIQFTSWPDHG-VPEDPHLLLKLRRRVNA-FSNFFSGPIVVHCSAGVGRTGTY 797
Cdd:cd14556    78 TIDEDVISRIFRLQNTTRPQEGyRMVQQFQFLGWPRDRdTPPSKRALLKLLSEVEKwQEQSGEGPIVVHCLNGVGRSGVF 157

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....
gi 578801331  798 IGIDAMLEGLEAENKVDVYGYVVKLRRQRCLMVQVEAQYILIHQ 841
Cdd:cd14556   158 CAISSVCERIKVENVVDVFQAVKTLRNHRPNMVETEEQYKFCYD 201
COG5599 COG5599
Protein tyrosine phosphatase [Signal transduction mechanisms];
614-839 6.69e-40

Protein tyrosine phosphatase [Signal transduction mechanisms];


Pssm-ID: 444335 [Multi-domain]  Cd Length: 282  Bit Score: 149.47  E-value: 6.69e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578801331  614 KNRYVDILPYDYNRVElseINGdagsNYINASYIDGfKEPRKYIAAQGPRDETVDDFWRMIWEQKATVIVMVTRCEEG-- 691
Cdd:COG5599    45 LNRFRDIQPYKETALR---ANL----GYLNANYIQV-IGNHRYIATQYPLEEQLEDFFQMLFDNNTPVLVVLASDDEIsk 116

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578801331  692 NRNKCAEYWPsmEEGTRAFGDVVVKINQHKRCPDYIIQKLNIVNKKEKA-TGREVTHIQFTSWPDHGVP--EDPHLLLKL 768
Cdd:COG5599   117 PKVKMPVYFR--QDGEYGKYEVSSELTESIQLRDGIEARTYVLTIKGTGqKKIEIPVLHVKNWPDHGAIsaEALKNLADL 194

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 578801331  769 RRRVNAFSNFFSGPIVVHCSAGVGRTGTYIGIDAMLEGLEAEN--KVDVYGYVVKLRRQR-CLMVQVEAQYILI 839
Cdd:COG5599   195 IDKKEKIKDPDKLLPVVHCRAGVGRTGTLIACLALSKSINALVqiTLSVEEIVIDMRTSRnGGMVQTSEQLDVL 268
PTPc-N7 cd14612
catalytic domain of tyrosine-protein phosphatase non-receptor type 7; Tyrosine-protein ...
 904-1160 2.41e-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: 2.41e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578801331  904 SKNRNSNVIPYDYNRVPLKHElemskesehdsdessdddSDSEEPSKYINASFIMSY-WKPEVMIAAQGPLKETIGDFWQ 982
Cdd:cd14612    17 SKDRYKTILPNPQSRVCLRRA------------------GSQEEEGSYINANYIRGYdGKEKAYIATQGPMLNTVSDFWE 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578801331  983 MIFQRKVKVIVMLTELKHGdQEICAQYWGEGKQTYGDIEVDLKDTDKSSTYTLRVFELRHSkrKDSRTVYQYQYTNWSVE 1062
Cdd:cd14612    79 MVWQEECPIIVMITKLKEK-KEKCVHYWPEKEGTYGRFEIRVQDMKECDGYTIRDLTIQLE--EESRSVKHYWFSSWPDH 155

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578801331 1063 QLPAEPKELISMIQVVKQKlPQKNSSEGnkhhkstPLLIHCRDGSQQTGIFCALLNLLESAETEEVVDIFQVVKALRKAR 1142
Cdd:cd14612   156 QTPESAGPLLRLVAEVEES-RQTAASPG-------PIVVHCSAGIGRTGCFIATSIGCQQLKDTGKVDILGIVCQLRLDR 227

                         250
                  ....*....|....*...
gi 578801331 1143 PGMVSTFEQYQFLYDVIA 1160
Cdd:cd14612   228 GGMIQTSEQYQFLHHTLA 245
PTPc-N22 cd14602
catalytic domain of tyrosine-protein phosphatase non-receptor type 22; Tyrosine-protein ...
 905-1159 2.59e-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: 146.14  E-value: 2.59e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578801331  905 KNRNSNVIPYDYNRVPLKhelemskesehdsdessddDSDSEEPSKYINASFIMSYWKPEVMIAAQGPLKETIGDFWQMI 984
Cdd:cd14602     1 KNRYKDILPYDHSRVELS-------------------LITSDEDSDYINANFIKGVYGPRAYIATQGPLSTTLLDFWRMI 61

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578801331  985 FQRKVKVIVM-LTELKHGDQEiCAQYW---GEGKQTYGDIEVDLKDTDKSSTYTLRVfeLRHSKRKDSRTVYQYQYTNWS 1060
Cdd:cd14602    62 WEYSVLIIVMaCMEFEMGKKK-CERYWaepGEMQLEFGPFSVTCEAEKRKSDYIIRT--LKVKFNSETRTIYQFHYKNWP 138

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578801331 1061 VEQLPAEPKELISMIQVVKQKlpqknssegnKHHKSTPLLIHCRDGSQQTGIFCAL---LNLLESAETEEVVDIFQVVKA 1137
Cdd:cd14602   139 DHDVPSSIDPILELIWDVRCY----------QEDDSVPICIHCSAGCGRTGVICAIdytWMLLKDGIIPENFSVFSLIQE 208

                         250       260
                  ....*....|....*....|..
gi 578801331 1138 LRKARPGMVSTFEQYQFLYDVI 1159
Cdd:cd14602   209 MRTQRPSLVQTKEQYELVYNAV 230
R-PTP-N cd14609
PTP-like domain of receptor-type tyrosine-protein phosphatase N; Receptor-type ...
 878-1160 5.32e-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: 5.32e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578801331  878 LEAEFQRLPSYRSW-RTQHIGNQEENKSKNRNSNVIPYDYNRVPLKHELEMSKesehdsdessdddsdseepSKYINASF 956
Cdd:cd14609    17 LAKEWQALCAYQAEpNTCSTAQGEANVKKNRNPDFVPYDHARIKLKAESNPSR-------------------SDYINASP 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578801331  957 IMSYwKPEV--MIAAQGPLKETIGDFWQMIFQRKVKVIVMLTELKHGDQEICAQYW-GEGKQTYGDIEVDL-KDTDKSST 1032
Cdd:cd14609    78 IIEH-DPRMpaYIATQGPLSHTIADFWQMVWENGCTVIVMLTPLVEDGVKQCDRYWpDEGSSLYHIYEVNLvSEHIWCED 156

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578801331 1033 YTLRVFELRHSKRKDSRTVYQYQYTNWSVEQLPAEPKELISMIQVVkqklpqknssegNKHH--KSTPLLIHCRDGSQQT 1110
Cdd:cd14609   157 FLVRSFYLKNVQTQETRTLTQFHFLSWPAEGIPSSTRPLLDFRRKV------------NKCYrgRSCPIIVHCSDGAGRT 224

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|...
gi 578801331 1111 GIFCAL---LNLLESAETEevVDIFQVVKALRKARPGMVSTFEQYQFLYDVIA 1160
Cdd:cd14609   225 GTYILIdmvLNRMAKGVKE--IDIAATLEHVRDQRPGMVRTKDQFEFALTAVA 275
PTPc-N13 cd14597
catalytic domain of tyrosine-protein phosphatase non-receptor type 13; Tyrosine-protein ...
 900-1159 8.36e-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: 8.36e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578801331  900 EENKSKNRNSNVIPYDYNRVPLKHElemskesehdsdessdddsdseepSKYINASFI-MSYWKPE-VMIAAQGPLKETI 977
Cdd:cd14597     1 KENRKKNRYKNILPYDTTRVPLGDE------------------------GGYINASFIkMPVGDEEfVYIACQGPLPTTV 56

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578801331  978 GDFWQMIFQRKVKVIVMLTELKHGDQEICAQYWGE--GKQTYGD--IEVDLKDTDKSSTYTLRVFELRHSKRKDSRTVYQ 1053
Cdd:cd14597    57 ADFWQMVWEQKSTVIAMMTQEVEGGKIKCQRYWPEilGKTTMVDnrLQLTLVRMQQLKNFVIRVLELEDIQTREVRHITH 136

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578801331 1054 YQYTNWSVEQLPAEPKELISMIQVVKQKlpqknssegnkhHKSTPLLIHCRDGSQQTGIFCALLNLLESAETEEVVDIFQ 1133
Cdd:cd14597   137 LNFTAWPDHDTPSQPEQLLTFISYMRHI------------HKSGPIITHCSAGIGRSGTLICIDVVLGLISKDLDFDISD 204

                         250       260
                  ....*....|....*....|....*.
gi 578801331 1134 VVKALRKARPGMVSTFEQYQFLYDVI 1159
Cdd:cd14597   205 IVRTMRLQRHGMVQTEDQYIFCYQVI 230
PTPc-N5 cd14613
catalytic domain of tyrosine-protein phosphatase non-receptor type 5; Tyrosine-protein ...
 905-1160 1.82e-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: 1.82e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578801331  905 KNRNSNVIPYDYNRVPLKHELEMSKEsehdsdessdddsdseepSKYINASFIMSYWKPE-VMIAAQGPLKETIGDFWQM 983
Cdd:cd14613    28 KNRYKTILPNPHSRVCLTSPDQDDPL------------------SSYINANYIRGYGGEEkVYIATQGPTVNTVGDFWRM 89

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578801331  984 IFQRKVKVIVMLTELKHGDqEICAQYWGEGKQTYGDIEVDLKDTDKSSTYTLRVFELRhsKRKDSRTVYQYQYTNWSVEQ 1063
Cdd:cd14613    90 VWQERSPIIVMITNIEEMN-EKCTEYWPEEQVTYEGIEITVKQVIHADDYRLRLITLK--SGGEERGLKHYWYTSWPDQK 166

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578801331 1064 LPAEPKELISMIQVVKQKLPQKNSSEGnkhhkstPLLIHCRDGSQQTGIFCALLNLLESAETEEVVDIFQVVKALRKARP 1143
Cdd:cd14613   167 TPDNAPPLLQLVQEVEEARQQAEPNCG-------PVIVHCSAGIGRTGCFIATSICCKQLRNEGVVDILRTTCQLRLDRG 239

                         250
                  ....*....|....*..
gi 578801331 1144 GMVSTFEQYQFLYDVIA 1160
Cdd:cd14613   240 GMIQTCEQYQFVHHVLS 256
PTPc_motif smart00404
Protein tyrosine phosphatase, catalytic domain motif;
744-845 8.03e-38

Protein tyrosine phosphatase, catalytic domain motif;


Pssm-ID: 214649 [Multi-domain]  Cd Length: 105  Bit Score: 137.10  E-value: 8.03e-38
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578801331    744 EVTHIQFTSWPDHGVPEDPHLLLKLRRRVNAFSNF--FSGPIVVHCSAGVGRTGTYIGIDAMLEGLEAE-NKVDVYGYVV 820
Cdd:smart00404    1 TVKHYHYTGWPDHGVPESPDSILELLRAVKKNLNQseSSGPVVVHCSAGVGRTGTFVAIDILLQQLEAEaGEVDIFDTVK 80

                            90       100
                    ....*....|....*....|....*
gi 578801331    821 KLRRQRCLMVQVEAQYILIHQALVE 845
Cdd:smart00404   81 ELRSQRPGMVQTEEQYLFLYRALLE 105
PTPc_DSPc smart00012
Protein tyrosine phosphatase, catalytic domain, undefined specificity; Protein tyrosine ...
 744-845 8.03e-38

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


Pssm-ID: 214469 [Multi-domain]  Cd Length: 105  Bit Score: 137.10  E-value: 8.03e-38
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578801331    744 EVTHIQFTSWPDHGVPEDPHLLLKLRRRVNAFSNF--FSGPIVVHCSAGVGRTGTYIGIDAMLEGLEAE-NKVDVYGYVV 820
Cdd:smart00012    1 TVKHYHYTGWPDHGVPESPDSILELLRAVKKNLNQseSSGPVVVHCSAGVGRTGTFVAIDILLQQLEAEaGEVDIFDTVK 80

                            90       100
                    ....*....|....*....|....*
gi 578801331    821 KLRRQRCLMVQVEAQYILIHQALVE 845
Cdd:smart00012   81 ELRSQRPGMVQTEEQYLFLYRALLE 105
PTPc-N11_6 cd14544
catalytic domain of tyrosine-protein phosphatase non-receptor type 11 and type 6; ...
 902-1160 8.79e-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: 8.79e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578801331  902 NKSKNRNSNVIPYDYNRVPLKhelemskesehdsdessdDDSDSEEPSKYINASFIMS-------YWKPEVMIAAQGPLK 974
Cdd:cd14544     1 NKGKNRYKNILPFDHTRVILK------------------DRDPNVPGSDYINANYIRNenegpttDENAKTYIATQGCLE 62

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578801331  975 ETIGDFWQMIFQRKVKVIVMLTELKHGDQEICAQYW---GEGKQtYGDIEV-DLKDTDKSStYTLRVFELRHSKRKDS-R 1049
Cdd:cd14544    63 NTVSDFWSMVWQENSRVIVMTTKEVERGKNKCVRYWpdeGMQKQ-YGPYRVqNVSEHDTTD-YTLRELQVSKLDQGDPiR 140

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578801331 1050 TVYQYQYTNWSVEQLPAEPKELISMIQVVKQKLPQKNSsegnkhhkSTPLLIHCRDGSQQTGIFCALLNLLESAETEEV- 1128
Cdd:cd14544   141 EIWHYQYLSWPDHGVPSDPGGVLNFLEDVNQRQESLPH--------AGPIVVHCSAGIGRTGTFIVIDMLLDQIKRKGLd 212

                         250       260       270
                  ....*....|....*....|....*....|....
gi 578801331 1129 --VDIFQVVKALRKARPGMVSTFEQYQFLYDVIA 1160
Cdd:cd14544   213 cdIDIQKTIQMVRSQRSGMVQTEAQYKFIYVAVA 246
PTPc-N21_14 cd14540
catalytic domain of tyrosine-protein phosphatase non-receptor type 21 and type 14; ...
 951-1159 1.08e-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: 1.08e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578801331  951 YINASFImsywKPEV------MIAAQGPLKETIGDFWQMIFQRKVKVIVMLTELKHGDQEICAQYW-----GEGKQTYGD 1019
Cdd:cd14540     1 YINASHI----TATVggkqrfYIAAQGPLQNTVGDFWQMVWEQGVYLVVMVTAEEEGGREKCFRYWptlggEHDALTFGE 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578801331 1020 IEVDLKDTDKSSTYTLRVFELRHSKRKDSRTVYQYQYTNWSVEQLPAEPKELISMIQVVkQKLPQKNSSEGNKHHKSTPL 1099
Cdd:cd14540    77 YKVSTKFSVSSGCYTTTGLRVKHTLSGQSRTVWHLQYTDWPDHGCPEDVSGFLDFLEEI-NSVRRHTNQDVAGHNRNPPT 155

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 578801331 1100 LIHCRDGSQQTG--IFCALlnLLESAETEEVVDIFQVVKALRKARPGMVSTFEQYQFLYDVI 1159
Cdd:cd14540   156 LVHCSAGVGRTGvvILADL--MLYCLDHNEELDIPRVLALLRHQRMLLVQTLAQYKFVYNVL 215
R-PTPc-R cd14611
catalytic domain of receptor-type tyrosine-protein phosphatase R; Receptor-type ...
 904-1156 5.57e-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: 5.57e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578801331  904 SKNRNSNVIPYDYNRVPLKhelemskesehdsdessdDDSDSEEPSKYINASFIMSYW-KPEVMIAAQGPLKETIGDFWQ 982
Cdd:cd14611     1 TKNRYKTILPNPHSRVCLK------------------PKNSNDSLSTYINANYIRGYGgKEKAFIATQGPMINTVNDFWQ 62

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578801331  983 MIFQRKVKVIVMLTELKHGDqEICAQYWGEGKQTYGDIEVDLKDTDKSSTYTLRVFELRHSKRkdSRTVYQYQYTNWSVE 1062
Cdd:cd14611    63 MVWQEDSPVIVMITKLKEKN-EKCVLYWPEKRGIYGKVEVLVNSVKECDNYTIRNLTLKQGSQ--SRSVKHYWYTSWPDH 139

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578801331 1063 QLPAEPKELISMIQVVKQKlPQKNSSEGnkhhkstPLLIHCRDGSQQTGIFCALLNLLESAETEEVVDIFQVVKALRKAR 1142
Cdd:cd14611   140 KTPDSAQPLLQLMLDVEED-RLASPGRG-------PVVVHCSAGIGRTGCFIATTIGCQQLKEEGVVDVLSIVCQLRVDR 211

                         250
                  ....*....|....
gi 578801331 1143 PGMVSTFEQYQFLY 1156
Cdd:cd14611   212 GGMVQTSEQYEFVH 225
PTPc-N20_13 cd14538
catalytic domain of tyrosine-protein phosphatase non-receptor type 20 and type 13; ...
 951-1159 1.30e-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: 1.30e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578801331  951 YINASFI--------MSYwkpevmIAAQGPLKETIGDFWQMIFQRKVKVIVMLTELKHGDQEICAQYWGEGKQT----YG 1018
Cdd:cd14538     1 YINASHIripvggdtYHY------IACQGPLPNTTGDFWQMVWEQKSEVIAMVTQDVEGGKVKCHRYWPDSLNKplicGG 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578801331 1019 DIEVDLKDTDKSSTYTLRVFELRHSKRKDSRTVYQYQYTNWSVEQLPAEPKELISMIQVVKqklpqknssegnKHHKSTP 1098
Cdd:cd14538    75 RLEVSLEKYQSLQDFVIRRISLRDKETGEVHHITHLNFTTWPDHGTPQSADPLLRFIRYMR------------RIHNSGP 142

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 578801331 1099 LLIHCRDGSQQTGIFCALLNLLESAETEEVVDIFQVVKALRKARPGMVSTFEQYQFLYDVI 1159
Cdd:cd14538   143 IVVHCSAGIGRTGVLITIDVALGLIERDLPFDIQDIVKDLREQRQGMIQTKDQYIFCYKAC 203
PTPc-N6 cd14606
catalytic domain of tyrosine-protein phosphatase non-receptor type 6; Tyrosine-protein ...
 894-1160 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 578801331  894 QHIGNQEENKSKNRNSNVIPYDYNRVPLKhelemskesehdsdessdDDSDSEEPSKYINASFIMSYW-----KPEVMIA 968
Cdd:cd14606    10 RLEGQRPENKSKNRYKNILPFDHSRVILQ------------------GRDSNIPGSDYINANYVKNQLlgpdeNAKTYIA 71

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578801331  969 AQGPLKETIGDFWQMIFQRKVKVIVMLT-ELKHGDQEiCAQYWGE--GKQTYGDIEVDLKDTDKSSTYTLRVFELRHSKR 1045
Cdd:cd14606    72 SQGCLEATVNDFWQMAWQENSRVIVMTTrEVEKGRNK-CVPYWPEvgMQRAYGPYSVTNCGEHDTTEYKLRTLQVSPLDN 150

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578801331 1046 KDS-RTVYQYQYTNWSVEQLPAEPKELISMIQVVKQK---LPqknssegnkhhKSTPLLIHCRDGSQQTGIFCALLNLLE 1121
Cdd:cd14606   151 GELiREIWHYQYLSWPDHGVPSEPGGVLSFLDQINQRqesLP-----------HAGPIIVHCSAGIGRTGTIIVIDMLME 219

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|..
gi 578801331 1122 SAETEEV---VDIFQVVKALRKARPGMVSTFEQYQFLYDVIA 1160
Cdd:cd14606   220 NISTKGLdcdIDIQKTIQMVRAQRSGMVQTEAQYKFIYVAIA 261
PTP-N23 cd14539
PTP-like domain of tyrosine-protein phosphatase non-receptor type 23; Tyrosine-protein ...
 951-1157 1.82e-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: 1.82e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578801331  951 YINASFI--MSYWKPEVmIAAQGPLKETIGDFWQMIFQRKVKVIVMLTelkhGDQEICAQ----YWGEGK---QTYGDIE 1021
Cdd:cd14539     1 YINASLIedLTPYCPRF-IATQAPLPGTAADFWLMVYEQQVSVIVMLV----SEQENEKQkvhrYWPTERgqaLVYGAIT 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578801331 1022 VDLKDTDKSSTYTLRVFELRHSKRKDSRTVYQYQYTNWSVEQLPAEPKELISMIQVVKQKLPQKNSSEgnkhhksTPLLI 1101
Cdd:cd14539    76 VSLQSVRTTPTHVERIISIQHKDTRLSRSVVHLQFTTWPELGLPDSPNPLLRFIEEVHSHYLQQRSLQ-------TPIVV 148

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 578801331 1102 HCRDGSQQTGIFCALLN-LLESAETEEVVDIFQVVKALRKARPGMVSTFEQYQFLYD 1157
Cdd:cd14539   149 HCSSGVGRTGAFCLLYAaVQEIEAGNGIPDLPQLVRKMRQQRKYMLQEKEHLKFCYE 205
PTPc-N11 cd14605
catalytic domain of tyrosine-protein phosphatase non-receptor type 11; Tyrosine-protein ...
 901-1156 2.13e-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: 2.13e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578801331  901 ENKSKNRNSNVIPYDYNRVPLkHELEMSKESehdsdessdddsdseepSKYINASFIMSYW-------KPE-VMIAAQGP 972
Cdd:cd14605     1 ENKNKNRYKNILPFDHTRVVL-HDGDPNEPV-----------------SDYINANIIMPEFetkcnnsKPKkSYIATQGC 62

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578801331  973 LKETIGDFWQMIFQRKVKVIVMLT-ELKHGDQEiCAQYWGE--GKQTYGDIEV-DLKDTdKSSTYTLRvfELRHSK---R 1045
Cdd:cd14605    63 LQNTVNDFWRMVFQENSRVIVMTTkEVERGKSK-CVKYWPDeyALKEYGVMRVrNVKES-AAHDYILR--ELKLSKvgqG 138

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578801331 1046 KDSRTVYQYQYTNWSVEQLPAEPKELISMIQVVKQKlpQKNSSEGNkhhkstPLLIHCRDGSQQTGIFCA---LLNLLES 1122
Cdd:cd14605   139 NTERTVWQYHFRTWPDHGVPSDPGGVLDFLEEVHHK--QESIMDAG------PVVVHCSAGIGRTGTFIVidiLIDIIRE 210

                         250       260       270
                  ....*....|....*....|....*....|....
gi 578801331 1123 AETEEVVDIFQVVKALRKARPGMVSTFEQYQFLY 1156
Cdd:cd14605   211 KGVDCDIDVPKTIQMVRSQRSGMVQTEAQYRFIY 244
PTPc-N1_2 cd14545
catalytic domain of tyrosine-protein phosphatase non-receptor type 1 and type 2; ...
 905-1156 3.10e-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: 3.10e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578801331  905 KNRNSNVIPYDYNRVPLKHELEmskesehdsdessdddsdseePSKYINASFIMSYWKPEVMIAAQGPLKETIGDFWQMI 984
Cdd:cd14545     1 LNRYRDRDPYDHDRSRVKLKQG---------------------DNDYINASLVEVEEAKRSYILTQGPLPNTSGHFWQMV 59

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578801331  985 FQRKVKVIVMLTELKHGDQEICAQYWGEGKQTYGDIE-----VDLKDTDKSSTYTLRVFELRHSKRKDSRTVYQYQYTNW 1059
Cdd:cd14545    60 WEQNSKAVIMLNKLMEKGQIKCAQYWPQGEGNAMIFEdtglkVTLLSEEDKSYYTVRTLELENLKTQETREVLHFHYTTW 139

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578801331 1060 SVEQLPAEPKELISMIQVVKqklpQKNSSEGNKhhksTPLLIHCRDGSQQTGIFC---ALLNLLESAETEEvVDIFQVVK 1136
Cdd:cd14545   140 PDFGVPESPAAFLNFLQKVR----ESGSLSSDV----GPPVVHCSAGIGRSGTFClvdTCLVLIEKGNPSS-VDVKKVLL 210

                         250       260
                  ....*....|....*....|
gi 578801331 1137 ALRKARPGMVSTFEQYQFLY 1156
Cdd:cd14545   211 EMRKYRMGLIQTPDQLRFSY 230
R-PTPc-T-2 cd14634
PTP domain of receptor-type tyrosine-protein phosphatase T, repeat 2; Receptor-type ...
 951-1158 1.40e-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: 1.40e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578801331  951 YINASFIMSYWKPEVMIAAQGPLKETIGDFWQMIFQRKVKVIVMLTELKHGdqEICAQYWGEGKQ-TYGDIEVDLKDTDK 1029
Cdd:cd14634     1 YINAALMDSHKQPAAFIVTQHPLPNTVADFWRLVFDYNCSSVVMLNEMDAA--QLCMQYWPEKTScCYGPIQVEFVSADI 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578801331 1030 SSTYTLRVFELRHSKRKDS--RTVYQYQYTNW-SVEQLPAEPKELISMIQVVKQKLPQKNSSEGNKhhkstplLIHCRDG 1106
Cdd:cd14634    79 DEDIISRIFRICNMARPQDgyRIVQHLQYIGWpAYRDTPPSKRSILKVVRRLEKWQEQYDGREGRT-------VVHCLNG 151

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 578801331 1107 SQQTGIFCALLNLLESAETEEVVDIFQVVKALRKARPGMVSTFEQYQFLYDV 1158
Cdd:cd14634   152 GGRSGTFCAICSVCEMIQQQNIIDVFHTVKTLRNNKSNMVETLEQYKFVYEV 203
PHA02747 PHA02747
protein tyrosine phosphatase; Provisional
 901-1155 5.67e-35

protein tyrosine phosphatase; Provisional


Pssm-ID: 165114 [Multi-domain]  Cd Length: 312  Bit Score: 136.28  E-value: 5.67e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578801331  901 ENKSKNRNSNVIPYDYNRVPLKhelemskesehdsdessdddSDSEEPSKYINASFIMSYWKPEVMIAAQGPLKETIGDF 980
Cdd:PHA02747   50 ENQPKNRYWDIPCWDHNRVILD--------------------SGGGSTSDYIHANWIDGFEDDKKFIATQGPFAETCADF 109

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578801331  981 WQMIFQRKVKVIVMLTELKHGD-QEICAQYWG---EGKQTYGDIEVDLKDTDKSSTYTLRVFELRHSKRKDSRTVYQYQY 1056
Cdd:PHA02747  110 WKAVWQEHCSIIVMLTPTKGTNgEEKCYQYWClneDGNIDMEDFRIETLKTSVRAKYILTLIEITDKILKDSRKISHFQC 189

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578801331 1057 TNWSVEQLPAEPKELISMIQVVKQKLPQKNSSEGNKHHKSTPLLIHCRDGSQQTGIFCALLNLLESAETEEVVDIFQVVK 1136
Cdd:PHA02747  190 SEWFEDETPSDHPDFIKFIKIIDINRKKSGKLFNPKDALLCPIVVHCSDGVGKTGIFCAVDICLNQLVKRKAICLAKTAE 269

                         250
                  ....*....|....*....
gi 578801331 1137 ALRKARPGMVSTFEQYQFL 1155
Cdd:PHA02747  270 KIREQRHAGIMNFDDYLFI 288
PHA02746 PHA02746
protein tyrosine phosphatase; Provisional
 899-1159 8.30e-35

protein tyrosine phosphatase; Provisional


Pssm-ID: 165113 [Multi-domain]  Cd Length: 323  Bit Score: 136.31  E-value: 8.30e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578801331  899 QEENKSKNRNSNVIPYDYNRVPLKHELEMSKESEHDSDESSDDDSDSEEPSKYINASFIMSYWKPEVMIAAQGPLKETIG 978
Cdd:PHA02746   48 KKENLKKNRFHDIPCWDHSRVVINAHESLKMFDVGDSDGKKIEVTSEDNAENYIHANFVDGFKEANKFICAQGPKEDTSE 127

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578801331  979 DFWQMIFQRKVKVIVMLTELKHgDQEICAQYWGEGKQ---TYGDIEVDLKDTDKSSTYTLRVFELRHSKRKDSRTVYQYQ 1055
Cdd:PHA02746  128 DFFKLISEHESQVIVSLTDIDD-DDEKCFELWTKEEDselAFGRFVAKILDIIEELSFTKTRLMITDKISDTSREIHHFW 206

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578801331 1056 YTNWSVEQLPAEPKELISMIQVVKQKLPQKNSSEGNKHHKSTPLLIHCRDGSQQTGIFCALLNLLESAETEEVVDIFQVV 1135
Cdd:PHA02746  207 FPDWPDNGIPTGMAEFLELINKVNEEQAELIKQADNDPQTLGPIVVHCSAGIGRAGTFCAIDNALEQLEKEKEVCLGEIV 286

                         250       260
                  ....*....|....*....|....
gi 578801331 1136 KALRKARPGMVSTFEQYQFLYDVI 1159
Cdd:PHA02746  287 LKIRKQRHSSVFLPEQYAFCYKAL 310
R-PTPc-K-2 cd14636
PTP domain of receptor-type tyrosine-protein phosphatase K, repeat 2; Receptor-type ...
 951-1158 3.14e-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: 130.53  E-value: 3.14e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578801331  951 YINASFIMSYWKPEVMIAAQGPLKETIGDFWQMIFQRKVKVIVMLTELKHgdQEICAQYW-GEGKQTYGDIEVDLKDTDK 1029
Cdd:cd14636     1 YINAALMDSYRQPAAFIVTQHPLPNTVKDFWRLVYDYGCTSIVMLNEVDL--AQGCPQYWpEEGMLRYGPIQVECMSCSM 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578801331 1030 SSTYTLRVFELRHSKRKDS--RTVYQYQYTNW-SVEQLPAEPKELISMIQVVKQKLPQKNSSEGNKhhkstplLIHCRDG 1106
Cdd:cd14636    79 DCDVISRIFRICNLTRPQEgyLMVQQFQYLGWaSHREVPGSKRSFLKLILQVEKWQEECDEGEGRT-------IIHCLNG 151

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 578801331 1107 SQQTGIFCALLNLLESAETEEVVDIFQVVKALRKARPGMVSTFEQYQFLYDV 1158
Cdd:cd14636   152 GGRSGMFCAISIVCEMIKRQNVVDVFHAVKTLRNSKPNMVETPEQYRFCYDV 203
R-PTPc-U-2 cd14637
PTP domain of receptor-type tyrosine-protein phosphatase U, repeat 2; Receptor-type ...
 951-1158 2.95e-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: 2.95e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578801331  951 YINASFIMSYWKPEVMIAAQGPLKETIGDFWQMIFQRKVKVIVMLTELKHGDQEI-CAQYWGE-GKQTYGDIEVDLKDTD 1028
Cdd:cd14637     1 YINAALTDSYTRSAAFIVTLHPLQNTTTDFWRLVYDYGCTSVVMLNQLNQSNSAWpCLQYWPEpGLQQYGPMEVEFVSGS 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578801331 1029 KSSTYTLRVFELRHSKR--KDSRTVYQYQYTNWSV-EQLPAEPKELISMIQVVKQKlpQKNSSEGNKhhkstplLIHCRD 1105
Cdd:cd14637    81 ADEDIVTRLFRVQNITRlqEGHLMVRHFQFLRWSAyRDTPDSKKAFLHLLASVEKW--QRESGEGRT-------VVHCLN 151

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 578801331 1106 GSQQTGIFCALLNLLESAETEEVVDIFQVVKALRKARPGMVSTFEQYQFLYDV 1158
Cdd:cd14637   152 GGGRSGTYCASAMILEMIRCHNIVDVFYAVKTLRNYKPNMVETLEQYRFCYEI 204
PTPc_plant_PTP1 cd17658
protein tyrosine phosphatase 1 from Arabidopsis thaliana and similar plant PTPs; Arabidopsis ...
 951-1156 1.24e-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: 1.24e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578801331  951 YINASFIMSYWKPEV--MIAAQGPLKETIGDFWQMIFQRKVKVIVMLTELKHGDQEI-CAQYW---GEGKQTYGDIEVDL 1024
Cdd:cd17658     1 YINASLVETPASESLpkFIATQGPLPHTFEDFWEMVIQQRCPVIIMLTRLVDNYSTAkCADYFpaeENESREFGRISVTN 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578801331 1025 KDTDKSST-YTLRVFELRHSKRKDS-RTVYQYQYTNWSVEQLPAEPKELISMIQVVKQKLPqknsSEGnkhhkstPLLIH 1102
Cdd:cd17658    81 KKLKHSQHsITLRVLEVQYIESEEPpLSVLHIQYPEWPDHGVPKDTRSVRELLKRLYGIPP----SAG-------PIVVH 149

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 578801331 1103 CRDGSQQTGIFCALLNLLES--AETEEVVDIFQVVKALRKARPGMVSTFEQYQFLY 1156
Cdd:cd17658   150 CSAGIGRTGAYCTIHNTIRRilEGDMSAVDLSKTVRKFRSQRIGMVQTQDQYIFCY 205
PTPc-N14 cd14599
catalytic domain of tyrosine-protein phosphatase non-receptor type 14; Tyrosine-protein ...
 881-1159 1.28e-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: 128.58  E-value: 1.28e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578801331  881 EFQRLPSYRSWRTQHIGNQEENKSKNRNSNVIPYDYNRVPLKHELEmskesehdsdessdddsdseEPSKYINASFIMSY 960
Cdd:cd14599    17 EYEQIPKKKADGVFTTATLPENAERNRIREVVPYEENRVELVPTKE--------------------NNTGYINASHIKVT 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578801331  961 WKPEV--MIAAQGPLKETIGDFWQMIFQRKVKVIVMLTELKHGDQEICAQYWGE-----GKQTYGDIEVDLKDTDKSSTY 1033
Cdd:cd14599    77 VGGEEwhYIATQGPLPHTCHDFWQMVWEQGVNVIAMVTAEEEGGRSKSHRYWPKlgskhSSATYGKFKVTTKFRTDSGCY 156

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578801331 1034 TLRVFELRHSKRKDSRTVYQYQYTNWSVEQLPAEPKELISMIQVVKQKLPQKNSSEGNKHHKSTPLLIHCRDGSQQTGIF 1113
Cdd:cd14599   157 ATTGLKVKHLLSGQERTVWHLQYTDWPDHGCPEEVQGFLSYLEEIQSVRRHTNSMLDSTKNCNPPIVVHCSAGVGRTGVV 236

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*.
gi 578801331 1114 CALLNLLESAETEEVVDIFQVVKALRKARPGMVSTFEQYQFLYDVI 1159
Cdd:cd14599   237 ILTELMIGCLEHNEKVEVPVMLRHLREQRMFMIQTIAQYKFVYQVL 282
PTPc-N2 cd14607
catalytic domain of tyrosine-protein phosphatase non-receptor type 2; Tyrosine-protein ...
 901-1156 2.13e-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: 2.13e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578801331  901 ENKSKNRNSNVIPYDYNRVPLKHelemskesehdsdessdddsdseEPSKYINASFIMSYWKPEVMIAAQGPLKETIGDF 980
Cdd:cd14607    23 ENRNRNRYRDVSPYDHSRVKLQN-----------------------TENDYINASLVVIEEAQRSYILTQGPLPNTCCHF 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578801331  981 WQMIFQRKVKVIVMLTELKHGDQEICAQYW---GEGKQTYGD--IEVDLKDTDKSSTYTLRVFELRHSKRKDSRTVYQYQ 1055
Cdd:cd14607    80 WLMVWQQKTKAVVMLNRIVEKDSVKCAQYWptdEEEVLSFKEtgFSVKLLSEDVKSYYTVHLLQLENINSGETRTISHFH 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578801331 1056 YTNWSVEQLPAEPKELISMIQVVKQklpqknssEGNKHHKSTPLLIHCRDGSQQTGIFCAL---LNLLESAETEEvVDIF 1132
Cdd:cd14607   160 YTTWPDFGVPESPASFLNFLFKVRE--------SGSLSPEHGPAVVHCSAGIGRSGTFSLVdtcLVLMEKKDPDS-VDIK 230

                         250       260
                  ....*....|....*....|....
gi 578801331 1133 QVVKALRKARPGMVSTFEQYQFLY 1156
Cdd:cd14607   231 QVLLDMRKYRMGLIQTPDQLRFSY 254
PTPc-N1 cd14608
catalytic domain of tyrosine-protein phosphatase non-receptor type 1; Tyrosine-protein ...
 896-1156 6.34e-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: 6.34e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578801331  896 IGNQEENKSKNRNSNVIPYDYNRVPLKHElemskesehdsdessdddsdseePSKYINASFIMSYWKPEVMIAAQGPLKE 975
Cdd:cd14608    19 VAKLPKNKNRNRYRDVSPFDHSRIKLHQE-----------------------DNDYINASLIKMEEAQRSYILTQGPLPN 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578801331  976 TIGDFWQMIFQRKVKVIVMLTELKHGDQEICAQYW--GEGKQTY---GDIEVDLKDTDKSSTYTLRVFELRHSKRKDSRT 1050
Cdd:cd14608    76 TCGHFWEMVWEQKSRGVVMLNRVMEKGSLKCAQYWpqKEEKEMIfedTNLKLTLISEDIKSYYTVRQLELENLTTQETRE 155

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578801331 1051 VYQYQYTNWSVEQLPAEPKELISMIQVVKQklpqknssEGNKHHKSTPLLIHCRDGSQQTGIFC---ALLNLLESAETEE 1127
Cdd:cd14608   156 ILHFHYTTWPDFGVPESPASFLNFLFKVRE--------SGSLSPEHGPVVVHCSAGIGRSGTFCladTCLLLMDKRKDPS 227

                         250       260
                  ....*....|....*....|....*....
gi 578801331 1128 VVDIFQVVKALRKARPGMVSTFEQYQFLY 1156
Cdd:cd14608   228 SVDIKKVLLEMRKFRMGLIQTADQLRFSY 256
R-PTPc-B cd14617
catalytic domain of receptor-type tyrosine-protein phosphatase B; Receptor-type ...
 906-1156 8.50e-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: 124.26  E-value: 8.50e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578801331  906 NRNSNVIPYDYNRVPLKHelemskesehdsdessdddSDSEEPSKYINASFIMSYWKPEVMIAAQGPLKETIGDFWQMIF 985
Cdd:cd14617     1 NRYNNILPYDSTRVKLSN-------------------VDDDPCSDYINASYIPGNNFRREYIATQGPLPGTKDDFWKMVW 61

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578801331  986 QRKVKVIVMLTELKHGDQEICAQYWGEGKQT--YGDIEVDLKDTDKSSTYTLRVFELRHSKRKDS-RTVYQYQYTNWSVE 1062
Cdd:cd14617    62 EQNVHNIVMVTQCVEKGRVKCDHYWPADQDSlyYGDLIVQMLSESVLPEWTIREFKICSEEQLDApRLVRHFHYTVWPDH 141

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578801331 1063 QLPAEPKELISMIQVVKQKLpqknssegNKHHKSTPLLIHCRDGSQQTGIFCALLNLLESAETEEVVDIFQVVKALRKAR 1142
Cdd:cd14617   142 GVPETTQSLIQFVRTVRDYI--------NRTPGSGPTVVHCSAGVGRTGTFIALDRILQQLDSKDSVDIYGAVHDLRLHR 213

                         250
                  ....*....|....
gi 578801331 1143 PGMVSTFEQYQFLY 1156
Cdd:cd14617   214 VHMVQTECQYVYLH 227
PTPc-N3_4 cd14541
catalytic domain of tyrosine-protein phosphatase non-receptor type 21 and type 14; ...
 951-1163 9.10e-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: 123.59  E-value: 9.10e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578801331  951 YINASFI-MSYWKPEVM---IAAQGPLKETIGDFWQMIFQRKVKVIVMLTELKHGDQEICAQYW--GEGKQTYGDIEVDL 1024
Cdd:cd14541     2 YINANYVnMEIPGSGIVnryIAAQGPLPNTCADFWQMVWEQKSTLIVMLTTLVERGRVKCHQYWpdLGETMQFGNLQITC 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578801331 1025 KDTDKSSTYTLRVFELRHSKRKDSRTVYQYQYTNWSVEQLPAEPKELISMIQVVKQklpqknssegNKHHKSTPLLIHCR 1104
Cdd:cd14541    82 VSEEVTPSFAFREFILTNTNTGEERHITQMQYLAWPDHGVPDDSSDFLDFVKRVRQ----------NRVGMVEPTVVHCS 151

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 578801331 1105 DGSQQTGIfcalLNLLESA----ETEEVVDIFQVVKALRKARPGMVSTFEQYQFLYDVIASTY 1163
Cdd:cd14541   152 AGIGRTGV----LITMETAmcliEANEPVYPLDIVRTMRDQRAMLIQTPSQYRFVCEAILRVY 210
PHA02742 PHA02742
protein tyrosine phosphatase; Provisional
 901-1156 1.14e-31

protein tyrosine phosphatase; Provisional


Pssm-ID: 165109 [Multi-domain]  Cd Length: 303  Bit Score: 126.27  E-value: 1.14e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578801331  901 ENKSKNRNSNVIPYDYNRVPLKHELEMSKesehdsdessdddsdseepskYINASFIMSYWKPEVMIAAQGPLKETIGDF 980
Cdd:PHA02742   51 KNMKKCRYPDAPCFDRNRVILKIEDGGDD---------------------FINASYVDGHNAKGRFICTQAPLEETALDF 109

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578801331  981 WQMIFQRKVKVIVMLTELKHGDQEICAQYWG---EGKQTYGDIEVDLKDTDKSSTYTLRVFELRHSKRKDSRTVYQYQYT 1057
Cdd:PHA02742  110 WQAIFQDQVRVIVMITKIMEDGKEACYPYWMpheRGKATHGEFKIKTKKIKSFRNYAVTNLCLTDTNTGASLDIKHFAYE 189

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578801331 1058 NWSVEQLPAEPKELISMIQVVKQ-KLPQKNSSEGNKHHKSTPLLIHCRDGSQQTGIFCALLNLLESAETEEVVDIFQVVK 1136
Cdd:PHA02742  190 DWPHGGLPRDPNKFLDFVLAVREaDLKADVDIKGENIVKEPPILVHCSAGLDRAGAFCAIDICISKYNERAIIPLLSIVR 269

                         250       260
                  ....*....|....*....|
gi 578801331 1137 ALRKARPGMVSTFEQYQFLY 1156
Cdd:PHA02742  270 DLRKQRHNCLSLPQQYIFCY 289
PTPc_motif smart00404
Protein tyrosine phosphatase, catalytic domain motif;
1050-1161 3.27e-31

Protein tyrosine phosphatase, catalytic domain motif;


Pssm-ID: 214649 [Multi-domain]  Cd Length: 105  Bit Score: 118.23  E-value: 3.27e-31
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578801331   1050 TVYQYQYTNWSVEQLPAEPKELISMIQVVKQKLPQKNSSegnkhhksTPLLIHCRDGSQQTGIFCALLNLLESAETE-EV 1128
Cdd:smart00404    1 TVKHYHYTGWPDHGVPESPDSILELLRAVKKNLNQSESS--------GPVVVHCSAGVGRTGTFVAIDILLQQLEAEaGE 72

                            90       100       110
                    ....*....|....*....|....*....|...
gi 578801331   1129 VDIFQVVKALRKARPGMVSTFEQYQFLYDVIAS 1161
Cdd:smart00404   73 VDIFDTVKELRSQRPGMVQTEEQYLFLYRALLE 105
PTPc_DSPc smart00012
Protein tyrosine phosphatase, catalytic domain, undefined specificity; Protein tyrosine ...
 1050-1161 3.27e-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: 3.27e-31
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578801331   1050 TVYQYQYTNWSVEQLPAEPKELISMIQVVKQKLPQKNSSegnkhhksTPLLIHCRDGSQQTGIFCALLNLLESAETE-EV 1128
Cdd:smart00012    1 TVKHYHYTGWPDHGVPESPDSILELLRAVKKNLNQSESS--------GPVVVHCSAGVGRTGTFVAIDILLQQLEAEaGE 72

                            90       100       110
                    ....*....|....*....|....*....|...
gi 578801331   1129 VDIFQVVKALRKARPGMVSTFEQYQFLYDVIAS 1161
Cdd:smart00012   73 VDIFDTVKELRSQRPGMVQTEEQYLFLYRALLE 105
R-PTPc-M-2 cd14635
PTP domain of receptor-type tyrosine-protein phosphatase M, repeat 2; Receptor-type ...
 951-1158 4.74e-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: 121.72  E-value: 4.74e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578801331  951 YINASFIMSYWKPEVMIAAQGPLKETIGDFWQMIFQRKVKVIVMLTELKHGdqEICAQYWGE-GKQTYGDIEVDLKDTDK 1029
Cdd:cd14635     1 YINAALMDSYKQPSAFIVTQHPLPNTVKDFWRLVLDYHCTSIVMLNDVDPA--QLCPQYWPEnGVHRHGPIQVEFVSADL 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578801331 1030 SSTYTLRVFELRHSKRKDS--RTVYQYQYTNWSV-EQLPAEPKELISMIQVVKQKLPQKNSSEGNKhhkstplLIHCRDG 1106
Cdd:cd14635    79 EEDIISRIFRIYNAARPQDgyRMVQQFQFLGWPMyRDTPVSKRSFLKLIRQVDKWQEEYNGGEGRT-------VVHCLNG 151

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 578801331 1107 SQQTGIFCALLNLLESAETEEVVDIFQVVKALRKARPGMVSTFEQYQFLYDV 1158
Cdd:cd14635   152 GGRSGTFCAISIVCEMLRHQRAVDVFHAVKTLRNNKPNMVDLLDQYKFCYEV 203
PTPc-N3 cd14600
catalytic domain of tyrosine-protein phosphatase non-receptor type 3; Tyrosine-protein ...
 899-1163 1.05e-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: 1.05e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578801331  899 QEENKSKNRNSNVIPYDYNRVPLKHElemskesehdsdessdddsdseepSKYINASFI-MSYWKPEVM---IAAQGPLK 974
Cdd:cd14600    37 LPQNMDKNRYKDVLPYDATRVVLQGN------------------------EDYINASYVnMEIPSANIVnkyIATQGPLP 92

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578801331  975 ETIGDFWQMIFQRKVKVIVMLTELKHGDQEICAQYWGEGKQT--YGDIEVDLKDTDKSSTYTLRVFELRHSKRKDSRTVY 1052
Cdd:cd14600    93 HTCAQFWQVVWEQKLSLIVMLTTLTERGRTKCHQYWPDPPDVmeYGGFRVQCHSEDCTIAYVFREMLLTNTQTGEERTVT 172

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578801331 1053 QYQYTNWSVEQLPAEPKELISMIQVVKQklpqknssegnKHHKSTPLLIHCRDGSQQTGIFCALLNLLESAETEEVVDIF 1132
Cdd:cd14600   173 HLQYVAWPDHGVPDDSSDFLEFVNYVRS-----------KRVENEPVLVHCSAGIGRTGVLVTMETAMCLTERNQPVYPL 241

                         250       260       270
                  ....*....|....*....|....*....|.
gi 578801331 1133 QVVKALRKARPGMVSTFEQYQFLYDVIASTY 1163
Cdd:cd14600   242 DIVRKMRDQRAMMVQTSSQYKFVCEAILRVY 272
PTPc-N21 cd14598
catalytic domain of tyrosine-protein phosphatase non-receptor type 21; Tyrosine-protein ...
 951-1159 1.09e-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: 1.09e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578801331  951 YINASFIM-----SYWKpevMIAAQGPLKETIGDFWQMIFQRKVKVIVMLTELKHGDQEICAQYWG-----EGKQTYGDI 1020
Cdd:cd14598     1 YINASHIKvtvggKEWD---YIATQGPLQNTCQDFWQMVWEQGVAIIAMVTAEEEGGREKSFRYWPrlgsrHNTVTYGRF 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578801331 1021 EVDLKDTDKSSTYTLRVFELRHSKRKDSRTVYQYQYTNWSVEQLPAEPKELISMIQVVKQKLPQKNSSEGNKHHKStPLL 1100
Cdd:cd14598    78 KITTRFRTDSGCYATTGLKIKHLLTGQERTVWHLQYTDWPEHGCPEDLKGFLSYLEEIQSVRRHTNSTIDPKSPNP-PVL 156

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 578801331 1101 IHCRDGSQQTGIFCALLNLLESAETEEVVDIFQVVKALRKARPGMVSTFEQYQFLYDVI 1159
Cdd:cd14598   157 VHCSAGVGRTGVVILSEIMIACLEHNEMLDIPRVLDMLRQQRMMMVQTLSQYTFVYKVL 215
PTPc-N20 cd14596
catalytic domain of tyrosine-protein phosphatase non-receptor type 20; Tyrosine-protein ...
 951-1159 3.77e-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: 3.77e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578801331  951 YINASFIMSYWKPE--VMIAAQGPLKETIGDFWQMIFQRKVKVIVMLTELKHGDQEICAQYWGEGKQTYGDIE---VDLK 1025
Cdd:cd14596     1 YINASYITMPVGEEelFYIATQGPLPSTIDDFWQMVWENRSDVIAMMTREVERGKVKCHRYWPETLQEPMELEnyqLRLE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578801331 1026 DTDKSSTYTLRVFELRHSKRKDSRTVYQYQYTNWSVEQLPAEPKELISMIQVVKqklpqknssegnKHHKSTPLLIHCRD 1105
Cdd:cd14596    81 NYQALQYFIIRIIKLVEKETGENRLIKHLQFTTWPDHGTPQSSDQLVKFICYMR------------KVHNTGPIVVHCSA 148

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....
gi 578801331 1106 GSQQTGIFCALLNLLESAETEEVVDIFQVVKALRKARPGMVSTFEQYQFLYDVI 1159
Cdd:cd14596   149 GIGRAGVLICVDVLLSLIEKDLSFNIKDIVREMRQQRYGMIQTKDQYLFCYKVV 202
COG5599 COG5599
Protein tyrosine phosphatase [Signal transduction mechanisms];
893-1161 4.21e-30

Protein tyrosine phosphatase [Signal transduction mechanisms];


Pssm-ID: 444335 [Multi-domain]  Cd Length: 282  Bit Score: 121.35  E-value: 4.21e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578801331  893 TQHIGNQEeNKSKNRNSNVIPYDYNRVplkhelemskesehdsdessdddsdsEEPSKYINASFIMSYwKPEVMIAAQGP 972
Cdd:COG5599    34 PQYLQNIN-GSPLNRFRDIQPYKETAL--------------------------RANLGYLNANYIQVI-GNHRYIATQYP 85

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578801331  973 LKETIGDFWQMIFQRKVKVIVMLTELKHGDQEI--CAQYWGEgKQTYGDIEVDLKDTDK---SSTYTLRVFEL-RHSKRK 1046
Cdd:COG5599    86 LEEQLEDFFQMLFDNNTPVLVVLASDDEISKPKvkMPVYFRQ-DGEYGKYEVSSELTESiqlRDGIEARTYVLtIKGTGQ 164

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578801331 1047 DSRTVYQYQYTNWSVEQLPAePKELISMIQVVKQKLPQKNSSEGnkhhkstPLLIHCRDGSQQTGIFCALLNLLES--AE 1124
Cdd:COG5599   165 KKIEIPVLHVKNWPDHGAIS-AEALKNLADLIDKKEKIKDPDKL-------LPVVHCRAGVGRTGTLIACLALSKSinAL 236

                         250       260       270
                  ....*....|....*....|....*....|....*...
gi 578801331 1125 TEEVVDIFQVVKALRKAR-PGMVSTFEQYQFLYDVIAS 1161
Cdd:COG5599   237 VQITLSVEEIVIDMRTSRnGGMVQTSEQLDVLVKLAEQ 274
R-PTPc-T-2 cd14634
PTP domain of receptor-type tyrosine-protein phosphatase T, repeat 2; Receptor-type ...
 641-845 5.56e-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: 5.56e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578801331  641 YINASYIDGFKEPRKYIAAQGPRDETVDDFWRMIWEQKATVIVMVTrcEEGNRNKCAEYWPsmEEGTRAFGDVVVKINQH 720
Cdd:cd14634     1 YINAALMDSHKQPAAFIVTQHPLPNTVADFWRLVFDYNCSSVVMLN--EMDAAQLCMQYWP--EKTSCCYGPIQVEFVSA 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578801331  721 KRCPDYIIQKLNIVNKKEKATG-REVTHIQFTSWPDH-GVPEDPHLLLKLRRRVNAFSNFF---SGPIVVHCSAGVGRTG 795
Cdd:cd14634    77 DIDEDIISRIFRICNMARPQDGyRIVQHLQYIGWPAYrDTPPSKRSILKVVRRLEKWQEQYdgrEGRTVVHCLNGGGRSG 156

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|
gi 578801331  796 TYIGIDAMLEGLEAENKVDVYGYVVKLRRQRCLMVQVEAQYILIHQALVE 845
Cdd:cd14634   157 TFCAICSVCEMIQQQNIIDVFHTVKTLRNNKSNMVETLEQYKFVYEVALE 206
CD45 pfam12567
Leukocyte receptor CD45; This family of proteins is found in eukaryotes. Proteins in this ...
 171-229 1.25e-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: 112.08  E-value: 1.25e-29
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 578801331   171 VDYLYNKETKLFTAKLNVNENVECGNNTCTNNEVHNLTECKNASVSISHNSCTAPDKTL 229
Cdd:pfam12567    1 VEYTYNSENKSFTAKLNVNDNVECENNDCENNELHNLQECEQINVSISHNSCTSPNKIL 59
PTPc-N4 cd14601
catalytic domain of tyrosine-protein phosphatase non-receptor type 4; Tyrosine-protein ...
 951-1163 4.06e-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: 4.06e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578801331  951 YINASFI-MSYWKPEVM---IAAQGPLKETIGDFWQMIFQRKVKVIVMLTELKHGDQEICAQYWGE--GKQTYGDIEVDL 1024
Cdd:cd14601     2 YINANYInMEIPSSSIInryIACQGPLPNTCSDFWQMTWEQGSSMVVMLTTQVERGRVKCHQYWPEpsGSSSYGGFQVTC 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578801331 1025 KDTDKSSTYTLRVFELRHSKRKDSRTVYQYQYTNWSVEQLPAEPKELISMIQVVKQKlpqknssegnKHHKSTPLLIHCR 1104
Cdd:cd14601    82 HSEEGNPAYVFREMTLTNLEKNESRPLTQIQYIAWPDHGVPDDSSDFLDFVCLVRNK----------RAGKDEPVVVHCS 151

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 578801331 1105 DGSQQTGIFCALLNLLESAETEEVVDIFQVVKALRKARPGMVSTFEQYQFLYDVIASTY 1163
Cdd:cd14601   152 AGIGRTGVLITMETAMCLIECNQPVYPLDIVRTMRDQRAMMIQTPSQYRFVCEAILKVY 210
R5-PTP-2 cd14550
PTP-like domain of R5 subfamily receptor-type tyrosine-protein phosphatases, repeat 2; The R5 ...
 951-1156 6.76e-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: 115.11  E-value: 6.76e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578801331  951 YINASFIMSYWKPEVMIAAQGPLKETIGDFWQMIFQRKVKVIVMLTELkHGDQEiCAQYWGEGKQT--YGDIEVDLKDTD 1028
Cdd:cd14550     1 YINASYLQGYRRSNEFIITQHPLEHTIKDFWQMIWDHNSQTIVMLTDN-ELNED-EPIYWPTKEKPleCETFKVTLSGED 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578801331 1029 KSST-----YTLRVFELRHSKRKDSRTVYQYQYTNWSVEQLPAEPK-ELISMIQvvkqklpqknssegnKHHKST--PLL 1100
Cdd:cd14550    79 HSCLsneirLIVRDFILESTQDDYVLEVRQFQCPSWPNPCSPIHTVfELINTVQ---------------EWAQQRdgPIV 143

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 578801331 1101 IHCRDGSQQTGIFCALLNLLESAETEEVVDIFQVVKALRKARPGMVSTFEQYQFLY 1156
Cdd:cd14550   144 VHDRYGGVQAATFCALTTLHQQLEHESSVDVYQVAKLYHLMRPGVFTSKEDYQFLY 199
R5-PTP-2 cd14550
PTP-like domain of R5 subfamily receptor-type tyrosine-protein phosphatases, repeat 2; The R5 ...
 641-827 2.32e-28

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


Pssm-ID: 350398 [Multi-domain]  Cd Length: 200  Bit Score: 113.57  E-value: 2.32e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578801331  641 YINASYIDGFKEPRKYIAAQGPRDETVDDFWRMIWEQKATVIVMVTRCEEgnRNKCAEYWPSMEEGTRAFGDVVVKINQH 720
Cdd:cd14550     1 YINASYLQGYRRSNEFIITQHPLEHTIKDFWQMIWDHNSQTIVMLTDNEL--NEDEPIYWPTKEKPLECETFKVTLSGED 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578801331  721 KRC----PDYIIQKLNIVNKKEKATgREVTHIQFTSWPDHGVPedPHLLLKLRRRVNAFSNFFSGPIVVHCSAGVGRTGT 796
Cdd:cd14550    79 HSClsneIRLIVRDFILESTQDDYV-LEVRQFQCPSWPNPCSP--IHTVFELINTVQEWAQQRDGPIVVHDRYGGVQAAT 155

                         170       180       190
                  ....*....|....*....|....*....|...
gi 578801331  797 YIGIDAMLEGLEAENKVDVYGYVV--KLRRQRC 827
Cdd:cd14550   156 FCALTTLHQQLEHESSVDVYQVAKlyHLMRPGV 188
R-PTP-Z-2 cd17669
catalytic domain of receptor-type tyrosine-protein phosphatase Z, repeat 2; Receptor-type ...
 951-1159 4.24e-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: 4.24e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578801331  951 YINASFIMSYWKPEVMIAAQGPLKETIGDFWQMIFQRKVKVIVMLTELKHGDQEICAqYWGEGKQ-------TYGDIEVD 1023
Cdd:cd17669     1 YINASYIMGYYQSNEFIITQHPLLHTIKDFWRMIWDHNAQLIVMLPDGQNMAEDEFV-YWPNKDEpincetfKVTLIAEE 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578801331 1024 LKDTDKSSTYTLRVFELRHSKRKDSRTVYQYQYTNWSVEQLP-AEPKELISMIqvvKQKLPQKNSsegnkhhkstPLLIH 1102
Cdd:cd17669    80 HKCLSNEEKLIIQDFILEATQDDYVLEVRHFQCPKWPNPDSPiSKTFELISII---KEEAANRDG----------PMIVH 146

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 578801331 1103 CRDGSQQTGIFCALLNLLESAETEEVVDIFQVVKALRKARPGMVSTFEQYQFLYDVI 1159
Cdd:cd17669   147 DEHGGVTAGTFCALTTLMHQLEKENSVDVYQVAKMINLMRPGVFTDIEQYQFLYKAI 203
R-PTPc-M-2 cd14635
PTP domain of receptor-type tyrosine-protein phosphatase M, repeat 2; Receptor-type ...
 641-845 3.68e-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: 3.68e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578801331  641 YINASYIDGFKEPRKYIAAQGPRDETVDDFWRMIWEQKATVIVMVTRCEEGNRnkCAEYWPsmEEGTRAFGDVVVKINQH 720
Cdd:cd14635     1 YINAALMDSYKQPSAFIVTQHPLPNTVKDFWRLVLDYHCTSIVMLNDVDPAQL--CPQYWP--ENGVHRHGPIQVEFVSA 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578801331  721 KRCPDYIIQKLNIVNKKEKATG-REVTHIQFTSWPDH-GVPEDPHLLLKLRRRVNAFSNFF---SGPIVVHCSAGVGRTG 795
Cdd:cd14635    77 DLEEDIISRIFRIYNAARPQDGyRMVQQFQFLGWPMYrDTPVSKRSFLKLIRQVDKWQEEYnggEGRTVVHCLNGGGRSG 156

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|
gi 578801331  796 TYIGIDAMLEGLEAENKVDVYGYVVKLRRQRCLMVQVEAQYILIHQALVE 845
Cdd:cd14635   157 TFCAISIVCEMLRHQRAVDVFHAVKTLRNNKPNMVDLLDQYKFCYEVALE 206
R-PTP-G-2 cd17670
PTP-like domain of receptor-type tyrosine-protein phosphatase G, repeat 2; Receptor-type ...
 951-1161 1.47e-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: 1.47e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578801331  951 YINASFIMSYWKPEVMIAAQGPLKETIGDFWQMIFQRKVKVIVMLTElKHGDQEICAQYWGEGKQTYG--DIEVDLKDTD 1028
Cdd:cd17670     1 YINASYIMGYYRSNEFIITQHPLPHTTKDFWRMIWDHNAQIIVMLPD-NQGLAEDEFVYWPSREESMNceAFTVTLISKD 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578801331 1029 K-----SSTYTLRVFELRHSKRKDSRTVYQYQYTNWSVEQLPAEpkELISMIQVVKQKLPQKNSsegnkhhkstPLLIHC 1103
Cdd:cd17670    80 RlclsnEEQIIIHDFILEATQDDYVLEVRHFQCPKWPNPDAPIS--STFELINVIKEEALTRDG----------PTIVHD 147

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 578801331 1104 RDGSQQTGIFCALLNLLESAETEEVVDIFQVVKALRKARPGMVSTFEQYQFLYDVIAS 1161
Cdd:cd17670   148 EFGAVSAGTLCALTTLSQQLENENAVDVYQVAKMINLMRPGVFTDIEQYQFLYKAMLS 205
R-PTP-Z-2 cd17669
catalytic domain of receptor-type tyrosine-protein phosphatase Z, repeat 2; Receptor-type ...
 641-844 2.87e-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: 2.87e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578801331  641 YINASYIDGFKEPRKYIAAQGPRDETVDDFWRMIWEQKATVIVMVTRCEEGNRNKCAeYWPSMEEGTRAFGDVVVKINQH 720
Cdd:cd17669     1 YINASYIMGYYQSNEFIITQHPLLHTIKDFWRMIWDHNAQLIVMLPDGQNMAEDEFV-YWPNKDEPINCETFKVTLIAEE 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578801331  721 KRC----PDYIIQKLnIVNKKEKATGREVTHIQFTSWPDhgvPEDP-HLLLKLRRRVNAFSNFFSGPIVVHCSAGVGRTG 795
Cdd:cd17669    80 HKClsneEKLIIQDF-ILEATQDDYVLEVRHFQCPKWPN---PDSPiSKTFELISIIKEEAANRDGPMIVHDEHGGVTAG 155

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*....
gi 578801331  796 TYIGIDAMLEGLEAENKVDVYGYVVKLRRQRCLMVQVEAQYILIHQALV 844
Cdd:cd17669   156 TFCALTTLMHQLEKENSVDVYQVAKMINLMRPGVFTDIEQYQFLYKAIL 204
R-PTPc-K-2 cd14636
PTP domain of receptor-type tyrosine-protein phosphatase K, repeat 2; Receptor-type ...
 641-845 5.74e-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: 5.74e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578801331  641 YINASYIDGFKEPRKYIAAQGPRDETVDDFWRMIWEQKATVIVMVTRCEEGnrNKCAEYWPsmEEGTRAFGDVVVKINQH 720
Cdd:cd14636     1 YINAALMDSYRQPAAFIVTQHPLPNTVKDFWRLVYDYGCTSIVMLNEVDLA--QGCPQYWP--EEGMLRYGPIQVECMSC 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578801331  721 KRCPDYIIQKLNIVNKKEKATGR-EVTHIQFTSWPDH-GVPEDPHLLLKLRRRVNAFS---NFFSGPIVVHCSAGVGRTG 795
Cdd:cd14636    77 SMDCDVISRIFRICNLTRPQEGYlMVQQFQYLGWASHrEVPGSKRSFLKLILQVEKWQeecDEGEGRTIIHCLNGGGRSG 156

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|
gi 578801331  796 TYIGIDAMLEGLEAENKVDVYGYVVKLRRQRCLMVQVEAQYILIHQALVE 845
Cdd:cd14636   157 MFCAISIVCEMIKRQNVVDVFHAVKTLRNSKPNMVETPEQYRFCYDVALE 206
R-PTP-G-2 cd17670
PTP-like domain of receptor-type tyrosine-protein phosphatase G, repeat 2; Receptor-type ...
 641-844 1.14e-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: 1.14e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578801331  641 YINASYIDGFKEPRKYIAAQGPRDETVDDFWRMIWEQKATVIVMVTRcEEGNRNKCAEYWPSMEEGTRAFGDVVVKINQH 720
Cdd:cd17670     1 YINASYIMGYYRSNEFIITQHPLPHTTKDFWRMIWDHNAQIIVMLPD-NQGLAEDEFVYWPSREESMNCEAFTVTLISKD 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578801331  721 KRC---PDYIIQKLNIVNKKEKATGREVTHIQFTSWPDHGVPEDPHLLLKLRRRVNAFSNffSGPIVVHCSAGVGRTGTY 797
Cdd:cd17670    80 RLClsnEEQIIIHDFILEATQDDYVLEVRHFQCPKWPNPDAPISSTFELINVIKEEALTR--DGPTIVHDEFGAVSAGTL 157

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*..
gi 578801331  798 IGIDAMLEGLEAENKVDVYGYVVKLRRQRCLMVQVEAQYILIHQALV 844
Cdd:cd17670   158 CALTTLSQQLENENAVDVYQVAKMINLMRPGVFTDIEQYQFLYKAML 204
PHA02738 PHA02738
hypothetical protein; Provisional
 899-1159 1.30e-22

hypothetical protein; Provisional


Pssm-ID: 222923 [Multi-domain]  Cd Length: 320  Bit Score: 100.38  E-value: 1.30e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578801331  899 QEENKSKNRNSNVIPYDYNRVPLKHElemskesehdsdessdddsdsEEPSKYINASFIMSYWKPEVMIAAQGPLKETIG 978
Cdd:PHA02738   46 EKKNRKLNRYLDAVCFDHSRVILPAE---------------------RNRGDYINANYVDGFEYKKKFICGQAPTRQTCY 104

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578801331  979 DFWQMIFQRKVKVIVMLTELKHGDQEICAQYWGEGKQT---YGDIEVDLKDTDKSSTYTLRVFELRHSKRKdSRTVYQYQ 1055
Cdd:PHA02738  105 DFYRMLWMEHVQIIVMLCKKKENGREKCFPYWSDVEQGsirFGKFKITTTQVETHPHYVKSTLLLTDGTSA-TQTVTHFN 183

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578801331 1056 YTNWSVEQLPAEPKELISMIQVVKQ---KLPQKNSSEGNKHHKSTPLLIHCRDGSQQTGIFCALLNLLESAETEEVVDIF 1132
Cdd:PHA02738  184 FTAWPDHDVPKNTSEFLNFVLEVRQcqkELAQESLQIGHNRLQPPPIVVHCNAGLGRTPCYCVVDISISRFDACATVSIP 263

                         250       260
                  ....*....|....*....|....*..
gi 578801331 1133 QVVKALRKARPGMVSTFEQYQFLYDVI 1159
Cdd:PHA02738  264 SIVSSIRNQRYYSLFIPFQYFFCYRAV 290
R-PTPc-U-2 cd14637
PTP domain of receptor-type tyrosine-protein phosphatase U, repeat 2; Receptor-type ...
 641-845 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 578801331  641 YINASYIDGFKEPRKYIAAQGPRDETVDDFWRMIWEQKATVIVMVTRCEEGNRN-KCAEYWPsmEEGTRAFGDVVVKINQ 719
Cdd:cd14637     1 YINAALTDSYTRSAAFIVTLHPLQNTTTDFWRLVYDYGCTSVVMLNQLNQSNSAwPCLQYWP--EPGLQQYGPMEVEFVS 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578801331  720 HKRCPDYIIQKLNIVNKKEKATGR-EVTHIQFTSW-PDHGVPEDPHLLLKLRRRVNAF-SNFFSGPIVVHCSAGVGRTGT 796
Cdd:cd14637    79 GSADEDIVTRLFRVQNITRLQEGHlMVRHFQFLRWsAYRDTPDSKKAFLHLLASVEKWqRESGEGRTVVHCLNGGGRSGT 158

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*....
gi 578801331  797 YIGIDAMLEGLEAENKVDVYGYVVKLRRQRCLMVQVEAQYILIHQALVE 845
Cdd:cd14637   159 YCASAMILEMIRCHNIVDVFYAVKTLRNYKPNMVETLEQYRFCYEIALE 207
PHA02740 PHA02740
protein tyrosine phosphatase; Provisional
 605-846 6.95e-18

protein tyrosine phosphatase; Provisional


Pssm-ID: 165107 [Multi-domain]  Cd Length: 298  Bit Score: 85.79  E-value: 6.95e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578801331  605 EARKPFNQNKNRYVD-ILPYDYNRVELSEINGDAGSNYINASYIDGFKEPRKYIAAQGPRDETVDDFWRMIWEQKATVIV 683
Cdd:PHA02740   41 EANKACAQAENKAKDeNLALHITRLLHRRIKLFNDEKVLDARFVDGYDFEQKFICIINLCEDACDKFLQALSDNKVQIIV 120

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578801331  684 MVTRCEEgnRNKCAEYWPSMEEGTRAFGDVVVKINQHKRCPDYIIQKLNIVNKKEKAtgREVTHIQFTSWPDHGVPEDPH 763
Cdd:PHA02740  121 LISRHAD--KKCFNQFWSLKEGCVITSDKFQIETLEIIIKPHFNLTLLSLTDKFGQA--QKISHFQYTAWPADGFSHDPD 196

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578801331  764 -----------LLLKLRRRvNAFSNFfsGPIVVHCSAGVGRTGTYIGIDAMLEGLEAENKVDVYGYVVKLRRQRCLMVQV 832
Cdd:PHA02740  197 afidffcniddLCADLEKH-KADGKI--APIIIDCIDGISSSAVFCVFDICATEFDKTGMLSIANALKKVRQKKYGCMNC 273

                         250
                  ....*....|....
gi 578801331  833 EAQYILIHQALVEY 846
Cdd:PHA02740  274 LDDYVFCYHLIAAY 287
PTP_YopH-like cd14559
YopH and related bacterial protein tyrosine phosphatases; Yersinia outer protein H (YopH) ...
 642-836 9.42e-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: 9.42e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578801331  642 INASYIDgFKEPRKYIAAQGPRDETVDDFWRMIWEQKATVIVMVTRCEEGNRNKCAEYWpsmeEGTRAFGDVVVKINQHK 721
Cdd:cd14559    18 LNANRVQ-IGNKNVAIACQYPKNEQLEDHLKMLADNRTPCLVVLASNKDIQRKGLPPYF----RQSGTYGSVTVKSKKTG 92

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578801331  722 rcPDYIIQKLNI------VNKKEKATGREVTHIqfTSWPDHGvPEDPHLLLKLRRRVN----------------AFSNFF 779
Cdd:cd14559    93 --KDELVDGLKAdmynlkITDGNKTITIPVVHV--TNWPDHT-AISSEGLKELADLVNksaeekrnfykskgssAINDKN 167

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 578801331  780 SGPIVVHCSAGVGRTGTYIgidAMLEGLEAENKVDVYGYVVKLRRQRC-LMVQVEAQY 836
Cdd:cd14559   168 KLLPVIHCRAGVGRTGQLA---AAMELNKSPNNLSVEDIVSDMRTSRNgKMVQKDEQL 222
PTP_YopH-like cd14559
YopH and related bacterial protein tyrosine phosphatases; Yersinia outer protein H (YopH) ...
 964-1155 3.49e-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: 3.49e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578801331  964 EVMIAAQGPLKETIGDFWQMIFQRKVKVIVMLTElkhgDQEICA----QYWGEGKqTYGDIEV--------DLKDTDKSS 1031
Cdd:cd14559    29 NVAIACQYPKNEQLEDHLKMLADNRTPCLVVLAS----NKDIQRkglpPYFRQSG-TYGSVTVkskktgkdELVDGLKAD 103

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578801331 1032 TYTLRvfeLRHSKRKDSRTVYQYqyTNW------SVEQLpaepKELISMIQVVKQK----LPQKNSSEGNKHHKSTPLlI 1101
Cdd:cd14559   104 MYNLK---ITDGNKTITIPVVHV--TNWpdhtaiSSEGL----KELADLVNKSAEEkrnfYKSKGSSAINDKNKLLPV-I 173

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 578801331 1102 HCRDGSQQTGIFCALLNLLESAETEEVVDIfqvVKALRKARPG-MVSTFEQYQFL 1155
Cdd:cd14559   174 HCRAGVGRTGQLAAAMELNKSPNNLSVEDI---VSDMRTSRNGkMVQKDEQLDTL 225
PHA02740 PHA02740
protein tyrosine phosphatase; Provisional
 950-1160 5.42e-12

protein tyrosine phosphatase; Provisional


Pssm-ID: 165107 [Multi-domain]  Cd Length: 298  Bit Score: 68.07  E-value: 5.42e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578801331  950 KYINASFIMSYWKPEVMIAAQGPLKETIGDFWQMIFQRKVKVIVMLTelKHGDQEICAQYWGEGKQTygdievdLKDTDK 1029
Cdd:PHA02740   77 KVLDARFVDGYDFEQKFICIINLCEDACDKFLQALSDNKVQIIVLIS--RHADKKCFNQFWSLKEGC-------VITSDK 147

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578801331 1030 SSTYTLRVFELRH---------SKRKDSRTVYQYQYTNWSVEQLPAEPKELISMIQVVKQKLPQKNSSEGNKhhKSTPLL 1100
Cdd:PHA02740  148 FQIETLEIIIKPHfnltllsltDKFGQAQKISHFQYTAWPADGFSHDPDAFIDFFCNIDDLCADLEKHKADG--KIAPII 225

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 578801331 1101 IHCRDGSQQTGIFCALLNLLESAETEEVVDIFQVVKALRKARPGMVSTFEQYQFLYDVIA 1160
Cdd:PHA02740  226 IDCIDGISSSAVFCVFDICATEFDKTGMLSIANALKKVRQKKYGCMNCLDDYVFCYHLIA 285
PTP_N pfam12453
Protein tyrosine phosphatase N terminal; This domain family is found in eukaryotes, and is ...
 7-32 2.52e-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: 2.52e-10
                           10        20
                   ....*....|....*....|....*.
gi 578801331     7 LKLLAFGFAFLDTEVFVTGQSPTPSP 32
Cdd:pfam12453    1 LKLLAFGFAFLDTEVFVTGESLTSST 26
PHA03255 PHA03255
BDLF3; Provisional
 27-165 1.76e-09

BDLF3; Provisional


Pssm-ID: 165513 [Multi-domain]  Cd Length: 234  Bit Score: 59.53  E-value: 1.76e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578801331   27 SPTPSPTGVSSVQTPHLPTHADSQTPSAG----TDTQTFSGSAANAKLNPTPGS--NAISDVPGERSTASTFPTDPVSPL 100
Cdd:PHA03255   45 TPSPSASGPSTNQSTTLTTTSAPITTTAIlstnTTTVTSTGTTVTPVPTTSNAStiNVTTKVTAQNITATEAGTGTSTGV 124

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 578801331  101 TTtlslahhssaalpartSNTTITANTSDAYLNASETTTLSPSGSAVISTTTIATTPSKPTC-DEK 165
Cdd:PHA03255  125 TS----------------NVTTRSSSTTSATTRITNATTLAPTLSSKGTSNATKTTAELPTVpDER 174
FN3 cd00063
Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein ...
 419-499 1.88e-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: 1.88e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578801331  419 PSQVWNMTVSMTSDNSMHVKCRPPRDRNGPHERYHLEVEAGN----TLVRNESHKNCDFRVKDLQYSTDYTFKAYFHNGD 494
Cdd:cd00063     1 PSPPTNLRVTDVTSTSVTLSWTPPEDDGGPITGYVVEYREKGsgdwKEVEVTPGSETSYTLTGLKPGTEYEFRVRAVNGG 80


                  ....*
gi 578801331  495 YPGEP 499
Cdd:cd00063    81 GESPP 85
CDC14 COG2453
Protein-tyrosine phosphatase [Signal transduction mechanisms];
753-841 5.39e-07

Protein-tyrosine phosphatase [Signal transduction mechanisms];


Pssm-ID: 441989 [Multi-domain]  Cd Length: 140  Bit Score: 50.35  E-value: 5.39e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578801331  753 WPDHGVPEDPHL---LLKLRRRVNAfsnffSGPIVVHCSAGVGRTGTYIGIDAMLEGLEAENKVDvygyvvKLRRQRCLM 829
Cdd:COG2453    55 IPDFGAPDDEQLqeaVDFIDEALRE-----GKKVLVHCRGGIGRTGTVAAAYLVLLGLSAEEALA------RVRAARPGA 123

                          90
                  ....*....|..
gi 578801331  830 VQVEAQYILIHQ 841
Cdd:COG2453   124 VETPAQRAFLER 135
fn3 pfam00041
Fibronectin type III domain;
420-499 1.86e-06

Fibronectin type III domain;


Pssm-ID: 394996 [Multi-domain]  Cd Length: 85  Bit Score: 47.02  E-value: 1.86e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578801331   420 SQVWNMTVSMTSDNSMHVKCRPPRDRNGPHERYHLEVEAGN--------TLVRNESHkncdFRVKDLQYSTDYTFKAYFH 491
Cdd:pfam00041    1 SAPSNLTVTDVTSTSLTVSWTPPPDGNGPITGYEVEYRPKNsgepwneiTVPGTTTS----VTLTGLKPGTEYEVRVQAV 76


                   ....*...
gi 578801331   492 NGDYPGEP 499
Cdd:pfam00041   77 NGGGEGPP 84
CDKN3-like cd14505
cyclin-dependent kinase inhibitor 3 and similar proteins; This family is composed of ...
 1099-1157 2.84e-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: 2.84e-06
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 578801331 1099 LLIHCRDGSQQTGIFCA--LLNLLESAETEevvdifQVVKALRKARPGMVSTFEQYQFLYD 1157
Cdd:cd14505   109 VLIHCKGGLGRTGLIAAclLLELGDTLDPE------QAIAAVRALRPGAIQTPKQENFLHQ 163
Chi1 COG3469
Chitinase [Carbohydrate transport and metabolism];
24-161 9.65e-06

Chitinase [Carbohydrate transport and metabolism];


Pssm-ID: 442692 [Multi-domain]  Cd Length: 534  Bit Score: 49.75  E-value: 9.65e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578801331   24 TGQSPTPSPTGVSSVQTPHLPTHADSQTPSAGTDTQTFSGSAANAKLNPTPGSNAISDVPGERSTASTFPTDPVS-PLTT 102
Cdd:COG3469    59 SGTGTTAASSTAATSSTTSTTATATAAAAAATSTSATLVATSTASGANTGTSTVTTTSTGAGSVTSTTSSTAGSTtTSGA 138

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 578801331  103 TLSLAHHSSAALPARTSNTTITANTSDAY---LNASETTTLSPSGSAVISTTTIATTPSKPT 161
Cdd:COG3469   139 SATSSAGSTTTTTTVSGTETATGGTTTTStttTTTSASTTPSATTTATATTASGATTPSATT 200
Chi1 COG3469
Chitinase [Carbohydrate transport and metabolism];
23-161 3.15e-05

Chitinase [Carbohydrate transport and metabolism];


Pssm-ID: 442692 [Multi-domain]  Cd Length: 534  Bit Score: 48.21  E-value: 3.15e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578801331   23 VTGQSPTPSPTGVSSVQTPHLPTHADSQTPSAGTDTQTFSGSAANAKLNPTPGSNAISDVPGERSTASTFPTDPvsplTT 102
Cdd:COG3469    80 ATATAAAAAATSTSATLVATSTASGANTGTSTVTTTSTGAGSVTSTTSSTAGSTTTSGASATSSAGSTTTTTTV----SG 155

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 578801331  103 TLSLAHHSSAalparTSNTTITANTSDAYLNASETTTLSPSGSAVISTTTIATTPSKPT 161
Cdd:COG3469   156 TETATGGTTT-----TSTTTTTTSASTTPSATTTATATTASGATTPSATTTATTTGPPT 209
fn3 pfam00041
Fibronectin type III domain;
327-396 4.37e-05

Fibronectin type III domain;


Pssm-ID: 394996 [Multi-domain]  Cd Length: 85  Bit Score: 43.17  E-value: 4.37e-05
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 578801331   327 GEPQIIFCRSEAAHQGVITWNPP---QRSFHNFTLCYIKETEKDC---LNLDKNLIKYDLQNLKPYTKYVLSLHAY 396
Cdd:pfam00041    1 SAPSNLTVTDVTSTSLTVSWTPPpdgNGPITGYEVEYRPKNSGEPwneITVPGTTTSVTLTGLKPGTEYEVRVQAV 76
FN3 smart00060
Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, ...
 419-494 8.00e-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: 8.00e-05
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578801331    419 PSQVWNMTVSMTSDNSMHVKCRPPRDRNGPHERYHLEVE----AGNTLVRNESHKNCDFRVKDLQYSTDYTFK--AYFHN 492
Cdd:smart00060    1 PSPPSNLRVTDVTSTSVTLSWEPPPDDGITGYIVGYRVEyreeGSEWKEVNVTPSSTSYTLTGLKPGTEYEFRvrAVNGA 80


                    ..
gi 578801331    493 GD 494
Cdd:smart00060   81 GE 82
FN3 cd00063
Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein ...
 326-396 8.29e-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: 8.29e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 578801331  326 PGEPQIIFCRSEAAHQGVITWNPPQRS---FHNFTLCYIKETEKDCLNLDKNLIK---YDLQNLKPYTKYVLSLHAY 396
Cdd:cd00063     1 PSPPTNLRVTDVTSTSVTLSWTPPEDDggpITGYVVEYREKGSGDWKEVEVTPGSetsYTLTGLKPGTEYEFRVRAV 77
Chi1 COG3469
Chitinase [Carbohydrate transport and metabolism];
21-161 1.29e-04

Chitinase [Carbohydrate transport and metabolism];


Pssm-ID: 442692 [Multi-domain]  Cd Length: 534  Bit Score: 46.28  E-value: 1.29e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578801331   21 VFVTGQSPTPSPTGVSSVQTPHLPTHADSQ----TPSAGTDTQTFSGSAANAKLNPTPGSNAISDVPGERSTASTFPTDP 96
Cdd:COG3469    37 ATATTVVSTTGSVVVAASGSAGSGTGTTAAsstaATSSTTSTTATATAAAAAATSTSATLVATSTASGANTGTSTVTTTS 116

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 578801331   97 VSPLTTTLSLAHHSSAALPARTSNTTITANTSDAYLNASETTTLSPSGSAVISTTTIA--TTPSKPT 161
Cdd:COG3469   117 TGAGSVTSTTSSTAGSTTTSGASATSSAGSTTTTTTVSGTETATGGTTTTSTTTTTTSasTTPSATT 183
PTP_DSP_cys cd14494
cys-based protein tyrosine phosphatase and dual-specificity phosphatase superfamily; This ...
 781-826 1.40e-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: 1.40e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*.
gi 578801331  781 GPIVVHCSAGVGRTGTYIGIDAMLEGleaenKVDVYGYVVKLRRQR 826
Cdd:cd14494    57 EPVLVHCKAGVGRTGTLVACYLVLLG-----GMSAEEAVRIVRLIR 97
Chi1 COG3469
Chitinase [Carbohydrate transport and metabolism];
24-161 1.45e-04

Chitinase [Carbohydrate transport and metabolism];


Pssm-ID: 442692 [Multi-domain]  Cd Length: 534  Bit Score: 45.90  E-value: 1.45e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578801331   24 TGQSPTPSPTGVSSVQTPHLPTHADSQTPSAGTDTQTfSGSAANAKLNPTPGSNAISDVPGERSTASTFPTDPVSPLTTT 103
Cdd:COG3469    54 SGSAGSGTGTTAASSTAATSSTTSTTATATAAAAAAT-STSATLVATSTASGANTGTSTVTTTSTGAGSVTSTTSSTAGS 132

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 578801331  104 LSLAHHSSAALPARTSNTTITANTSDAYLNASETTTLSPSGSAviSTTTIATTPSKPT 161
Cdd:COG3469   133 TTTSGASATSSAGSTTTTTTVSGTETATGGTTTTSTTTTTTSA--STTPSATTTATAT 188
PTP_DSP_cys cd14494
cys-based protein tyrosine phosphatase and dual-specificity phosphatase superfamily; This ...
 1098-1157 3.04e-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: 3.04e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 578801331 1098 PLLIHCRDGSQQTGIFCALLNLLESAETeevvdIFQVVKALRKARPGMVS-TFEQYQFLYD 1157
Cdd:cd14494    58 PVLVHCKAGVGRTGTLVACYLVLLGGMS-----AEEAVRIVRLIRPGGIPqTIEQLDFLIK 113
CDC14_C cd14499
C-terminal dual-specificity phosphatase domain of CDC14 family proteins; The cell division ...
 781-803 1.17e-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: 1.17e-03
                          10        20
                  ....*....|....*....|...
gi 578801331  781 GPIVVHCSAGVGRTGTYIGIDAM 803
Cdd:cd14499   110 GAIAVHCKAGLGRTGTLIACYLM 132
CDC14 COG2453
Protein-tyrosine phosphatase [Signal transduction mechanisms];
1098-1157 2.97e-03

Protein-tyrosine phosphatase [Signal transduction mechanisms];


Pssm-ID: 441989 [Multi-domain]  Cd Length: 140  Bit Score: 39.18  E-value: 2.97e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 578801331 1098 PLLIHCRDGSQQTGIFCALLNLLESAETEEVVdifqvvKALRKARPGMVSTFEQYQFLYD 1157
Cdd:COG2453    82 KVLVHCRGGIGRTGTVAAAYLVLLGLSAEEAL------ARVRAARPGAVETPAQRAFLER 135
TpbA-like cd14529
bacterial protein tyrosine and dual-specificity phosphatases related to Pseudomonas aeruginosa ...
 738-869 3.14e-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: 3.14e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578801331  738 EKATGREVTHIQFTSWpdhgVPEDPHLLLKLRRRVNAFSNffsGPIVVHCSAGVGRTGTYIGIdamlegleaenkvdvYG 817
Cdd:cd14529    54 AKIDGVKYVNLPLSAT----RPTESDVQSFLLIMDLKLAP---GPVLIHCKHGKDRTGLVSAL---------------YR 111

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 578801331  818 YVVKLRRQrclmvQVEAQYILIHQALVEYNQFGETEVNLSELHPYLHNMKKR 869
Cdd:cd14529   112 IVYGGSKE-----EANEDYRLSNRHLEGLRSGIALDSKGGVKGRYLAAYFER 158
DUSP23 cd14504
dual specificity phosphatase 23; Dual specificity phosphatase 23 (DUSP23), also known as ...
 777-835 4.02e-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: 4.02e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 578801331  777 NFFSGPIVVHCSAGVGRTGT----YIGIDAMLEGLEAenkvdvygyVVKLRRQRCLMVQVEAQ 835
Cdd:cd14504    79 NAKNEAVLVHCLAGKGRTGTmlacYLVKTGKISAVDA---------INEIRRIRPGSIETSEQ 132
FN3 smart00060
Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, ...
 326-396 4.14e-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: 4.14e-03
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 578801331    326 PGEPQIIFCRSEAAHQGVITWNPPQRSFHN-FTLCYIKETEKDC-----LNLDKNLIKYDLQNLKPYTKYVLSLHAY 396
Cdd:smart00060    1 PSPPSNLRVTDVTSTSVTLSWEPPPDDGITgYIVGYRVEYREEGsewkeVNVTPSSTSYTLTGLKPGTEYEFRVRAV 77
PTP_PTPDC1 cd14506
protein tyrosine phosphatase domain of PTP domain-containing protein 1; protein tyrosine ...
 752-798 5.47e-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: 5.47e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*..
gi 578801331  752 SWPDHGVPEdPHLLLKLRRrVNAFSNFFSGPIVVHCSAGVGRTGTYI 798
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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