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Conserved domains on  [gi|158138488|ref|NP_612516|]
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receptor-type tyrosine-protein phosphatase C isoform 4 precursor [Rattus norvegicus]

Protein Classification

fibronectin type III domain-containing protein( domain architecture ID 13272695)

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 ...
 676-876 2.98e-146

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: 440.03  E-value: 2.98e-146
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158138488  676 YINASYIDGFKEPRKYIAAQGPRDETVDDFWKMIWEQKATVIVMVTRCEEGNRNKCAEYWPCMEEGTRTFRDVVVTINDH 755
Cdd:cd14557     1 YINASYIDGFKEPRKYIAAQGPKDETVDDFWRMIWEQKSTVIVMVTRCEEGNRNKCAQYWPSMEEGSRAFGDVVVKINEE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158138488  756 KRCPDYIIQKLSIAHKKEKATGREVTHIQFTSWPDHGVPEDPHLLLKLRRRVNAFSNFFSGPIVVHCSAGVGRTGTYIGI 835
Cdd:cd14557    81 KICPDYIIRKLNINNKKEKGSGREVTHIQFTSWPDHGVPEDPHLLLKLRRRVNAFNNFFSGPIVVHCSAGVGRTGTYIGI 160

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|.
gi 158138488  836 DAMLESLEAEGKVDVYGYVVNLRRQRCLMVQVEAQYILIHQ 876
Cdd:cd14557   161 DAMLEGLEAEGRVDVYGYVVKLRRQRCLMVQVEAQYILIHQ 201
R-PTP-C-2 cd14558
PTP-like domain of receptor-type tyrosine-protein phosphatase C, repeat 2; Receptor-type ...
 986-1191 1.94e-118

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: 366.33  E-value: 1.94e-118
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158138488  986 YINASFVMSYWKPEMMIAAQGPLKETIGDFWQMIFQRKVKVIVMLTELMSGDQEVCAQYWGEGKQTYGDMEVMLKDTNKS 1065
Cdd:cd14558     1 YINASFIDGYWGPKSLIATQGPLPDTIADFWQMIFQKKVKVIVMLTELKEGDQEQCAQYWGDEKKTYGDIEVELKDTEKS 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158138488 1066 SAYILRAFELRHSKRKEPRTVYQYQCTTWKGEELPAEPKDLVTLIQNIKQKLPKSGSegmKYHKHASILVHCRDGSQQTG 1145
Cdd:cd14558    81 PTYTVRVFEITHLKRKDSRTVYQYQYHKWKGEELPEKPKDLVDMIKSIKQKLPYKNS---KHGRSVPIVVHCSDGSSRTG 157

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*.
gi 158138488 1146 LFCALFNLLESAETEDVVDVFQVVKSLRKARPGMVGSFEQYQFLYD 1191
Cdd:cd14558   158 IFCALWNLLESAETEKVVDVFQVVKALRKQRPGMVSTLEQYQFLYD 203
CD45 pfam12567
Leukocyte receptor CD45; This family of proteins is found in eukaryotes. Proteins in this ...
 203-259 5.63e-20

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: 84.73  E-value: 5.63e-20
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 158138488   203 VRYIYDDSSKNFNANLEGDKKPKCEYTDCEK-ELKNLPECSQKNVTLSNGSCT-PDKII 259
Cdd:pfam12567    1 VEYTYNSENKSFTAKLNVNDNVECENNDCENnELHNLQECEQINVSISHNSCTsPNKIL 59
FN3 cd00063
Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein ...
 366-431 2.07e-08

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: 52.88  E-value: 2.07e-08
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 158138488  366 HVQCKNSTNSTTLVSWAEPA---SKHHGYILCYKKTPSE---KCENLANDVNSFEVKNLRPYTEYTVSLFAY 431
Cdd:cd00063     6 NLRVTDVTSTSVTLSWTPPEddgGPITGYVVEYREKGSGdwkEVEVTPGSETSYTLTGLKPGTEYEFRVRAV 77
FN3 cd00063
Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein ...
 454-534 1.68e-07

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: 50.19  E-value: 1.68e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158138488  454 PGKVNGMKTSRASDNSINVTCNSPYEINGPEARYILEVKSGGS----LVKTFNQSTCKFVVDNLYYSTDYEFLVYFYNGE 529
Cdd:cd00063     1 PSPPTNLRVTDVTSTSVTLSWTPPEDDGGPITGYVVEYREKGSgdwkEVEVTPGSETSYTLTGLKPGTEYEFRVRAVNGG 80


                  ....*
gi 158138488  530 YLGDP 534
Cdd:cd00063    81 GESPP 85
PHA03255 super family cl31530
BDLF3; Provisional
 82-191 1.02e-06

BDLF3; Provisional


The actual alignment was detected with superfamily member PHA03255:

Pssm-ID: 165513 [Multi-domain]  Cd Length: 234  Bit Score: 51.44  E-value: 1.02e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158138488   82 TPQPDSQTPSARGADTQTLSSQ---------ADLTTLTAapSGETDPPgvpeestVPETFPGGTPILARNSTAPSPTHTS 152
Cdd:PHA03255   45 TPSPSASGPSTNQSTTLTTTSApitttailsTNTTTVTS--TGTTVTP-------VPTTSNASTINVTTKVTAQNITATE 115

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 158138488  153 NVSTTDISSGANLTTPAPSTLG---FASNTTTSTeiATPQTK 191
Cdd:PHA03255  116 AGTGTSTGVTSNVTTRSSSTTSattRITNATTLA--PTLSSK 155
Wzy_O6_O28 super family cl41481
oligosaccharide repeat unit polymerase; Members of this family are oligosaccharide repeat unit ...
 521-580 2.71e-04

oligosaccharide repeat unit polymerase; Members of this family are oligosaccharide repeat unit polymerases in a subfamily that includes the Wzy proteins for polymerization of the O-antigens O6, O28, O39, O59, and several others.


The actual alignment was detected with superfamily member NF033860:

Pssm-ID: 468211  Cd Length: 384  Bit Score: 44.91  E-value: 2.71e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 158138488  521 FLVYFYNGEYLGDpeikPQSTSYNSKALIIFLVFLIIVTSIALLVVLYKIYDLRKKRSSN 580
Cdd:NF033860   18 FIYFIITGELGGD----FSGVEINLSNILLLIILLLILLFFLFLYLLYKLFKKIKVKNKS 73
 
Name Accession Description Interval E-value
R-PTPc-C-1 cd14557
catalytic domain of receptor-type tyrosine-protein phosphatase C, repeat 1; Receptor-type ...
 676-876 2.98e-146

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: 440.03  E-value: 2.98e-146
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158138488  676 YINASYIDGFKEPRKYIAAQGPRDETVDDFWKMIWEQKATVIVMVTRCEEGNRNKCAEYWPCMEEGTRTFRDVVVTINDH 755
Cdd:cd14557     1 YINASYIDGFKEPRKYIAAQGPKDETVDDFWRMIWEQKSTVIVMVTRCEEGNRNKCAQYWPSMEEGSRAFGDVVVKINEE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158138488  756 KRCPDYIIQKLSIAHKKEKATGREVTHIQFTSWPDHGVPEDPHLLLKLRRRVNAFSNFFSGPIVVHCSAGVGRTGTYIGI 835
Cdd:cd14557    81 KICPDYIIRKLNINNKKEKGSGREVTHIQFTSWPDHGVPEDPHLLLKLRRRVNAFNNFFSGPIVVHCSAGVGRTGTYIGI 160

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|.
gi 158138488  836 DAMLESLEAEGKVDVYGYVVNLRRQRCLMVQVEAQYILIHQ 876
Cdd:cd14557   161 DAMLEGLEAEGRVDVYGYVVKLRRQRCLMVQVEAQYILIHQ 201
R-PTP-C-2 cd14558
PTP-like domain of receptor-type tyrosine-protein phosphatase C, repeat 2; Receptor-type ...
 986-1191 1.94e-118

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: 366.33  E-value: 1.94e-118
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158138488  986 YINASFVMSYWKPEMMIAAQGPLKETIGDFWQMIFQRKVKVIVMLTELMSGDQEVCAQYWGEGKQTYGDMEVMLKDTNKS 1065
Cdd:cd14558     1 YINASFIDGYWGPKSLIATQGPLPDTIADFWQMIFQKKVKVIVMLTELKEGDQEQCAQYWGDEKKTYGDIEVELKDTEKS 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158138488 1066 SAYILRAFELRHSKRKEPRTVYQYQCTTWKGEELPAEPKDLVTLIQNIKQKLPKSGSegmKYHKHASILVHCRDGSQQTG 1145
Cdd:cd14558    81 PTYTVRVFEITHLKRKDSRTVYQYQYHKWKGEELPEKPKDLVDMIKSIKQKLPYKNS---KHGRSVPIVVHCSDGSSRTG 157

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*.
gi 158138488 1146 LFCALFNLLESAETEDVVDVFQVVKSLRKARPGMVGSFEQYQFLYD 1191
Cdd:cd14558   158 IFCALWNLLESAETEKVVDVFQVVKALRKQRPGMVSTLEQYQFLYD 203
PTPc smart00194
Protein tyrosine phosphatase, catalytic domain;
621-880 6.18e-111

Protein tyrosine phosphatase, catalytic domain;


Pssm-ID: 214550 [Multi-domain]  Cd Length: 259  Bit Score: 348.49  E-value: 6.18e-111
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158138488    621 LFLAEFQSIPRVFS-KFPIKDARKSQNQNKNRYVDILPYDYNRVELSEINGDaGSTYINASYIDGFKEPRKYIAAQGPRD 699
Cdd:smart00194    1 GLEEEFEKLDRLKPdDESCTVAAFPENRDKNRYKDVLPYDHTRVKLKPPPGE-GSDYINASYIDGPNGPKAYIATQGPLP 79

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158138488    700 ETVDDFWKMIWEQKATVIVMVTRCEEGNRNKCAEYWPCMEEGTRTFRDVVVTINDHKRCPDYIIQKLSIAHKKEKATgRE 779
Cdd:smart00194   80 STVEDFWRMVWEQKVTVIVMLTELVEKGREKCAQYWPDEEGEPLTYGDITVTLKSVEKVDDYTIRTLEVTNTGCSET-RT 158

                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158138488    780 VTHIQFTSWPDHGVPEDPHLLLKLRRRVNAFSNFFSGPIVVHCSAGVGRTGTYIGIDAMLESLEAEGKVDVYGYVVNLRR 859
Cdd:smart00194  159 VTHYHYTNWPDHGVPESPESILDLIRAVRKSQSTSTGPIVVHCSAGVGRTGTFIAIDILLQQLEAGKEVDIFEIVKELRS 238

                           250       260
                    ....*....|....*....|.
gi 158138488    860 QRCLMVQVEAQYILIHQALVE 880
Cdd:smart00194  239 QRPGMVQTEEQYIFLYRAILE 259
Y_phosphatase pfam00102
Protein-tyrosine phosphatase;
646-880 1.02e-106

Protein-tyrosine phosphatase;


Pssm-ID: 459674 [Multi-domain]  Cd Length: 234  Bit Score: 336.14  E-value: 1.02e-106
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158138488   646 NQNKNRYVDILPYDYNRVELSEINGDagSTYINASYIDGFKEPRKYIAAQGPRDETVDDFWKMIWEQKATVIVMVTRCEE 725
Cdd:pfam00102    1 NLEKNRYKDVLPYDHTRVKLTGDPGP--SDYINASYIDGYKKPKKYIATQGPLPNTVEDFWRMVWEEKVTIIVMLTELEE 78

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158138488   726 GNRNKCAEYWPCMEEGTRTFRDVVVTI-NDHKRCPDYIIQKLSIAHKKEKATgREVTHIQFTSWPDHGVPEDPHLLLKLR 804
Cdd:pfam00102   79 KGREKCAQYWPEEEGESLEYGDFTVTLkKEKEDEKDYTVRTLEVSNGGSEET-RTVKHFHYTGWPDHGVPESPNSLLDLL 157

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 158138488   805 RRVNAFSN-FFSGPIVVHCSAGVGRTGTYIGIDAMLESLEAEGKVDVYGYVVNLRRQRCLMVQVEAQYILIHQALVE 880
Cdd:pfam00102  158 RKVRKSSLdGRSGPIVVHCSAGIGRTGTFIAIDIALQQLEAEGEVDIFQIVKELRSQRPGMVQTLEQYIFLYDAILE 234
PTPc smart00194
Protein tyrosine phosphatase, catalytic domain;
913-1194 1.58e-89

Protein tyrosine phosphatase, catalytic domain;


Pssm-ID: 214550 [Multi-domain]  Cd Length: 259  Bit Score: 289.94  E-value: 1.58e-89
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158138488    913 LEAEYQRLPSYRSWR-TQHIGNQEENKKKNRSSNVVPYDFNRVPLKHELEmskeseaesdessdedsdseETSKYINASF 991
Cdd:smart00194    2 LEEEFEKLDRLKPDDeSCTVAAFPENRDKNRYKDVLPYDHTRVKLKPPPG--------------------EGSDYINASY 61

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158138488    992 VMSYWKPEMMIAAQGPLKETIGDFWQMIFQRKVKVIVMLTELMSGDQEVCAQYW---GEGKQTYGDMEVMLKDTNKSSAY 1068
Cdd:smart00194   62 IDGPNGPKAYIATQGPLPSTVEDFWRMVWEQKVTVIVMLTELVEKGREKCAQYWpdeEGEPLTYGDITVTLKSVEKVDDY 141

                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158138488   1069 ILRAFELRHSKRKEPRTVYQYQCTTWKGEELPAEPKDLVTLIQNIKQKLPksgsegmkyHKHASILVHCRDGSQQTGLFC 1148
Cdd:smart00194  142 TIRTLEVTNTGCSETRTVTHYHYTNWPDHGVPESPESILDLIRAVRKSQS---------TSTGPIVVHCSAGVGRTGTFI 212

                           250       260       270       280
                    ....*....|....*....|....*....|....*....|....*.
gi 158138488   1149 ALFNLLESAETEDVVDVFQVVKSLRKARPGMVGSFEQYQFLYDIMA 1194
Cdd:smart00194  213 AIDILLQQLEAGKEVDIFEIVKELRSQRPGMVQTEEQYIFLYRAIL 258
Y_phosphatase pfam00102
Protein-tyrosine phosphatase;
937-1194 4.79e-85

Protein-tyrosine phosphatase;


Pssm-ID: 459674 [Multi-domain]  Cd Length: 234  Bit Score: 276.43  E-value: 4.79e-85
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158138488   937 NKKKNRSSNVVPYDFNRVPLKHElemskeseaesdessdedsdsEETSKYINASFVMSYWKPEMMIAAQGPLKETIGDFW 1016
Cdd:pfam00102    1 NLEKNRYKDVLPYDHTRVKLTGD---------------------PGPSDYINASYIDGYKKPKKYIATQGPLPNTVEDFW 59

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158138488  1017 QMIFQRKVKVIVMLTELMSGDQEVCAQYW---GEGKQTYGDMEVMLKDTNK-SSAYILRAFELRHSKRKEPRTVYQYQCT 1092
Cdd:pfam00102   60 RMVWEEKVTIIVMLTELEEKGREKCAQYWpeeEGESLEYGDFTVTLKKEKEdEKDYTVRTLEVSNGGSEETRTVKHFHYT 139

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158138488  1093 TWKGEELPAEPKDLVTLIQNIKQKLPKsgsegmkyHKHASILVHCRDGSQQTGLFCALFNLLESAETEDVVDVFQVVKSL 1172
Cdd:pfam00102  140 GWPDHGVPESPNSLLDLLRKVRKSSLD--------GRSGPIVVHCSAGIGRTGTFIAIDIALQQLEAEGEVDIFQIVKEL 211

                          250       260
                   ....*....|....*....|..
gi 158138488  1173 RKARPGMVGSFEQYQFLYDIMA 1194
Cdd:pfam00102  212 RSQRPGMVQTLEQYIFLYDAIL 233
PHA02746 PHA02746
protein tyrosine phosphatase; Provisional
 604-878 1.94e-49

protein tyrosine phosphatase; Provisional


Pssm-ID: 165113 [Multi-domain]  Cd Length: 323  Bit Score: 178.68  E-value: 1.94e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158138488  604 SDLLLETYKRKIADEGRLFLAEFQSIPrvfSKFPIKDARKSQNQNKNRYVDILPYDYNRVELSE---------------- 667
Cdd:PHA02746   12 FDFFDKTNHAKFCEFVLLEHAEVMDIP---IRGTTNHFLKKENLKKNRFHDIPCWDHSRVVINAheslkmfdvgdsdgkk 88

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158138488  668 ---INGDAGSTYINASYIDGFKEPRKYIAAQGPRDETVDDFWKMIWEQKATVIVMVTRCEEGNRnKCAEYWPCMEEGTRT 744
Cdd:PHA02746   89 ievTSEDNAENYIHANFVDGFKEANKFICAQGPKEDTSEDFFKLISEHESQVIVSLTDIDDDDE-KCFELWTKEEDSELA 167

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158138488  745 FRDVVVTINDHKRCPDYIIQKLSIAHKKEKaTGREVTHIQFTSWPDHGVPEDPHLLLKLRRRVNA----------FSNFF 814
Cdd:PHA02746  168 FGRFVAKILDIIEELSFTKTRLMITDKISD-TSREIHHFWFPDWPDNGIPTGMAEFLELINKVNEeqaelikqadNDPQT 246

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 158138488  815 SGPIVVHCSAGVGRTGTYIGIDAMLESLEAEGKVDVYGYVVNLRRQRCLMVQVEAQYILIHQAL 878
Cdd:PHA02746  247 LGPIVVHCSAGIGRAGTFCAIDNALEQLEKEKEVCLGEIVLKIRKQRHSSVFLPEQYAFCYKAL 310
COG5599 COG5599
Protein tyrosine phosphatase [Signal transduction mechanisms];
639-874 2.89e-41

Protein tyrosine phosphatase [Signal transduction mechanisms];


Pssm-ID: 444335 [Multi-domain]  Cd Length: 282  Bit Score: 153.71  E-value: 2.89e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158138488  639 KDARKSQNQN---KNRYVDILPYDYNRVElseINGdagsTYINASYIDGfKEPRKYIAAQGPRDETVDDFWKMIWEQKAT 715
Cdd:COG5599    32 NDPQYLQNINgspLNRFRDIQPYKETALR---ANL----GYLNANYIQV-IGNHRYIATQYPLEEQLEDFFQMLFDNNTP 103

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158138488  716 VIVMVTRCEEG--NRNKCAEYWPcmEEGTRTFRDVVVTINDHKRCPDYI---IQKLSIAHKKEKatGREVTHIQFTSWPD 790
Cdd:COG5599   104 VLVVLASDDEIskPKVKMPVYFR--QDGEYGKYEVSSELTESIQLRDGIearTYVLTIKGTGQK--KIEIPVLHVKNWPD 179

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158138488  791 HGVP--EDPHLLLKLRRRVNAFSNFFSGPIVVHCSAGVGRTGTYIGIDAMLESLEAEG--KVDVYGYVVNLRRQR-CLMV 865
Cdd:COG5599   180 HGAIsaEALKNLADLIDKKEKIKDPDKLLPVVHCRAGVGRTGTLIACLALSKSINALVqiTLSVEEIVIDMRTSRnGGMV 259


                  ....*....
gi 158138488  866 QVEAQYILI 874
Cdd:COG5599   260 QTSEQLDVL 268
PHA02747 PHA02747
protein tyrosine phosphatase; Provisional
 936-1189 5.03e-33

protein tyrosine phosphatase; Provisional


Pssm-ID: 165114 [Multi-domain]  Cd Length: 312  Bit Score: 130.51  E-value: 5.03e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158138488  936 ENKKKNRSSNVVPYDFNRVPLKhelemskeseaesdessdedSDSEETSKYINASFVMSYWKPEMMIAAQGPLKETIGDF 1015
Cdd:PHA02747   50 ENQPKNRYWDIPCWDHNRVILD--------------------SGGGSTSDYIHANWIDGFEDDKKFIATQGPFAETCADF 109

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158138488 1016 WQMIFQRKVKVIVML--TELMSGdQEVCAQYWGEGKQTYGDMEVMLKDTNKSSA---YILRAFELRHSKRKEPRTVYQYQ 1090
Cdd:PHA02747  110 WKAVWQEHCSIIVMLtpTKGTNG-EEKCYQYWCLNEDGNIDMEDFRIETLKTSVrakYILTLIEITDKILKDSRKISHFQ 188

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158138488 1091 CTTWKGEELPAEPKDLVTLIQNIKQKLPKSGSE-GMKYHKHASILVHCRDGSQQTGLFCALFNLLESAETEDVVDVFQVV 1169
Cdd:PHA02747  189 CSEWFEDETPSDHPDFIKFIKIIDINRKKSGKLfNPKDALLCPIVVHCSDGVGKTGIFCAVDICLNQLVKRKAICLAKTA 268

                         250       260
                  ....*....|....*....|
gi 158138488 1170 KSLRKARPGMVGSFEQYQFL 1189
Cdd:PHA02747  269 EKIREQRHAGIMNFDDYLFI 288
COG5599 COG5599
Protein tyrosine phosphatase [Signal transduction mechanisms];
928-1196 1.17e-23

Protein tyrosine phosphatase [Signal transduction mechanisms];


Pssm-ID: 444335 [Multi-domain]  Cd Length: 282  Bit Score: 102.48  E-value: 1.17e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158138488  928 TQHIGNQEeNKKKNRSSNVVPYDFNRVplkhelemskeseaesdessdedsdsEETSKYINASFVMSYwKPEMMIAAQGP 1007
Cdd:COG5599    34 PQYLQNIN-GSPLNRFRDIQPYKETAL--------------------------RANLGYLNANYIQVI-GNHRYIATQYP 85

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158138488 1008 LKETIGDFWQMIFQRKVKVIVMLT--ELMSGDQEVCAQYWGEgKQTYGDMEVMLKDTNK---SSAYILRAFEL-RHSKRK 1081
Cdd:COG5599    86 LEEQLEDFFQMLFDNNTPVLVVLAsdDEISKPKVKMPVYFRQ-DGEYGKYEVSSELTESiqlRDGIEARTYVLtIKGTGQ 164

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158138488 1082 EPRTVYQYQCTTWK-GEELPAEP-KDLVTLIqnIKQKLPKSGSEGmkyhkhaSILVHCRDGSQQTGLFCALFNLLES--A 1157
Cdd:COG5599   165 KKIEIPVLHVKNWPdHGAISAEAlKNLADLI--DKKEKIKDPDKL-------LPVVHCRAGVGRTGTLIACLALSKSinA 235

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|
gi 158138488 1158 ETEDVVDVFQVVKSLRKAR-PGMVGSFEQYQFLYDIMASI 1196
Cdd:COG5599   236 LVQITLSVEEIVIDMRTSRnGGMVQTSEQLDVLVKLAEQQ 275
CD45 pfam12567
Leukocyte receptor CD45; This family of proteins is found in eukaryotes. Proteins in this ...
 203-259 5.63e-20

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: 84.73  E-value: 5.63e-20
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 158138488   203 VRYIYDDSSKNFNANLEGDKKPKCEYTDCEK-ELKNLPECSQKNVTLSNGSCT-PDKII 259
Cdd:pfam12567    1 VEYTYNSENKSFTAKLNVNDNVECENNDCENnELHNLQECEQINVSISHNSCTsPNKIL 59
FN3 cd00063
Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein ...
 366-431 2.07e-08

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: 52.88  E-value: 2.07e-08
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 158138488  366 HVQCKNSTNSTTLVSWAEPA---SKHHGYILCYKKTPSE---KCENLANDVNSFEVKNLRPYTEYTVSLFAY 431
Cdd:cd00063     6 NLRVTDVTSTSVTLSWTPPEddgGPITGYVVEYREKGSGdwkEVEVTPGSETSYTLTGLKPGTEYEFRVRAV 77
FN3 cd00063
Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein ...
 454-534 1.68e-07

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: 50.19  E-value: 1.68e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158138488  454 PGKVNGMKTSRASDNSINVTCNSPYEINGPEARYILEVKSGGS----LVKTFNQSTCKFVVDNLYYSTDYEFLVYFYNGE 529
Cdd:cd00063     1 PSPPTNLRVTDVTSTSVTLSWTPPEDDGGPITGYVVEYREKGSgdwkEVEVTPGSETSYTLTGLKPGTEYEFRVRAVNGG 80


                  ....*
gi 158138488  530 YLGDP 534
Cdd:cd00063    81 GESPP 85
FN3 smart00060
Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, ...
 365-431 6.74e-07

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: 48.38  E-value: 6.74e-07
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 158138488    365 PHVQCKNSTNSTTLVSWAEPASKHH-GYILCYK-----KTPSEKCENLANDVNSFEVKNLRPYTEYTVSLFAY 431
Cdd:smart00060    5 SNLRVTDVTSTSVTLSWEPPPDDGItGYIVGYRveyreEGSEWKEVNVTPSSTSYTLTGLKPGTEYEFRVRAV 77
PHA03255 PHA03255
BDLF3; Provisional
 82-191 1.02e-06

BDLF3; Provisional


Pssm-ID: 165513 [Multi-domain]  Cd Length: 234  Bit Score: 51.44  E-value: 1.02e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158138488   82 TPQPDSQTPSARGADTQTLSSQ---------ADLTTLTAapSGETDPPgvpeestVPETFPGGTPILARNSTAPSPTHTS 152
Cdd:PHA03255   45 TPSPSASGPSTNQSTTLTTTSApitttailsTNTTTVTS--TGTTVTP-------VPTTSNASTINVTTKVTAQNITATE 115

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 158138488  153 NVSTTDISSGANLTTPAPSTLG---FASNTTTSTeiATPQTK 191
Cdd:PHA03255  116 AGTGTSTGVTSNVTTRSSSTTSattRITNATTLA--PTLSSK 155
fn3 pfam00041
Fibronectin type III domain;
367-431 1.35e-06

Fibronectin type III domain;


Pssm-ID: 394996 [Multi-domain]  Cd Length: 85  Bit Score: 47.41  E-value: 1.35e-06
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 158138488   367 VQCKNSTNSTTLVSWAEPASKH---HGYILCYKKTPSEKCE---NLANDVNSFEVKNLRPYTEYTVSLFAY 431
Cdd:pfam00041    6 LTVTDVTSTSLTVSWTPPPDGNgpiTGYEVEYRPKNSGEPWneiTVPGTTTSVTLTGLKPGTEYEVRVQAV 76
Wzy_O6_O28 NF033860
oligosaccharide repeat unit polymerase; Members of this family are oligosaccharide repeat unit ...
 521-580 2.71e-04

oligosaccharide repeat unit polymerase; Members of this family are oligosaccharide repeat unit polymerases in a subfamily that includes the Wzy proteins for polymerization of the O-antigens O6, O28, O39, O59, and several others.


Pssm-ID: 468211  Cd Length: 384  Bit Score: 44.91  E-value: 2.71e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 158138488  521 FLVYFYNGEYLGDpeikPQSTSYNSKALIIFLVFLIIVTSIALLVVLYKIYDLRKKRSSN 580
Cdd:NF033860   18 FIYFIITGELGGD----FSGVEINLSNILLLIILLLILLFFLFLYLLYKLFKKIKVKNKS 73
fn3 pfam00041
Fibronectin type III domain;
455-534 1.39e-03

Fibronectin type III domain;


Pssm-ID: 394996 [Multi-domain]  Cd Length: 85  Bit Score: 38.94  E-value: 1.39e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158138488   455 GKVNGMKTSRASDNSINVTCNSPYEINGPEARYILEVKS--GGSLVKTFN--QSTCKFVVDNLYYSTDYEFLVYFYNGEY 530
Cdd:pfam00041    1 SAPSNLTVTDVTSTSLTVSWTPPPDGNGPITGYEVEYRPknSGEPWNEITvpGTTTSVTLTGLKPGTEYEVRVQAVNGGG 80


                   ....
gi 158138488   531 LGDP 534
Cdd:pfam00041   81 EGPP 84
Chi1 COG3469
Chitinase [Carbohydrate transport and metabolism];
21-193 3.98e-03

Chitinase [Carbohydrate transport and metabolism];


Pssm-ID: 442692 [Multi-domain]  Cd Length: 534  Bit Score: 41.28  E-value: 3.98e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158138488   21 VTGQGTTDDGLDTTEIVLLPQTDPLPARTTEFTPPSISERGNGSSETTYLPGFSSTLMPHLTPQPDSQTPSARGADTQTL 100
Cdd:COG3469    17 ATAVTLLGAAATAASVTLTAATATTVVSTTGSVVVAASGSAGSGTGTTAASSTAATSSTTSTTATATAAAAAATSTSATL 96

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158138488  101 SSQADLTTLTAAPSGETDPPGVPEESTVPETFPGGTPILARNS---------TAPSPTHTSNVSTTDISSGANLTTPAPS 171
Cdd:COG3469    97 VATSTASGANTGTSTVTTTSTGAGSVTSTTSSTAGSTTTSGASatssagsttTTTTVSGTETATGGTTTTSTTTTTTSAS 176

                         170       180
                  ....*....|....*....|..
gi 158138488  172 TLGFASNTTTSTEIATPQTKPS 193
Cdd:COG3469   177 TTPSATTTATATTASGATTPSA 198
FN3 smart00060
Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, ...
 454-524 4.21e-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: 4.21e-03
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 158138488    454 PGKVNGMKTSRASDNSINVTCNSPYE--INGPEARYILEVKSGGSLVKTFN--QSTCKFVVDNLYYSTDYEFLVY 524
Cdd:smart00060    1 PSPPSNLRVTDVTSTSVTLSWEPPPDdgITGYIVGYRVEYREEGSEWKEVNvtPSSTSYTLTGLKPGTEYEFRVR 75
 
Name Accession Description Interval E-value
R-PTPc-C-1 cd14557
catalytic domain of receptor-type tyrosine-protein phosphatase C, repeat 1; Receptor-type ...
 676-876 2.98e-146

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: 440.03  E-value: 2.98e-146
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158138488  676 YINASYIDGFKEPRKYIAAQGPRDETVDDFWKMIWEQKATVIVMVTRCEEGNRNKCAEYWPCMEEGTRTFRDVVVTINDH 755
Cdd:cd14557     1 YINASYIDGFKEPRKYIAAQGPKDETVDDFWRMIWEQKSTVIVMVTRCEEGNRNKCAQYWPSMEEGSRAFGDVVVKINEE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158138488  756 KRCPDYIIQKLSIAHKKEKATGREVTHIQFTSWPDHGVPEDPHLLLKLRRRVNAFSNFFSGPIVVHCSAGVGRTGTYIGI 835
Cdd:cd14557    81 KICPDYIIRKLNINNKKEKGSGREVTHIQFTSWPDHGVPEDPHLLLKLRRRVNAFNNFFSGPIVVHCSAGVGRTGTYIGI 160

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|.
gi 158138488  836 DAMLESLEAEGKVDVYGYVVNLRRQRCLMVQVEAQYILIHQ 876
Cdd:cd14557   161 DAMLEGLEAEGRVDVYGYVVKLRRQRCLMVQVEAQYILIHQ 201
R-PTP-C-2 cd14558
PTP-like domain of receptor-type tyrosine-protein phosphatase C, repeat 2; Receptor-type ...
 986-1191 1.94e-118

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: 366.33  E-value: 1.94e-118
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158138488  986 YINASFVMSYWKPEMMIAAQGPLKETIGDFWQMIFQRKVKVIVMLTELMSGDQEVCAQYWGEGKQTYGDMEVMLKDTNKS 1065
Cdd:cd14558     1 YINASFIDGYWGPKSLIATQGPLPDTIADFWQMIFQKKVKVIVMLTELKEGDQEQCAQYWGDEKKTYGDIEVELKDTEKS 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158138488 1066 SAYILRAFELRHSKRKEPRTVYQYQCTTWKGEELPAEPKDLVTLIQNIKQKLPKSGSegmKYHKHASILVHCRDGSQQTG 1145
Cdd:cd14558    81 PTYTVRVFEITHLKRKDSRTVYQYQYHKWKGEELPEKPKDLVDMIKSIKQKLPYKNS---KHGRSVPIVVHCSDGSSRTG 157

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*.
gi 158138488 1146 LFCALFNLLESAETEDVVDVFQVVKSLRKARPGMVGSFEQYQFLYD 1191
Cdd:cd14558   158 IFCALWNLLESAETEKVVDVFQVVKALRKQRPGMVSTLEQYQFLYD 203
PTPc smart00194
Protein tyrosine phosphatase, catalytic domain;
621-880 6.18e-111

Protein tyrosine phosphatase, catalytic domain;


Pssm-ID: 214550 [Multi-domain]  Cd Length: 259  Bit Score: 348.49  E-value: 6.18e-111
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158138488    621 LFLAEFQSIPRVFS-KFPIKDARKSQNQNKNRYVDILPYDYNRVELSEINGDaGSTYINASYIDGFKEPRKYIAAQGPRD 699
Cdd:smart00194    1 GLEEEFEKLDRLKPdDESCTVAAFPENRDKNRYKDVLPYDHTRVKLKPPPGE-GSDYINASYIDGPNGPKAYIATQGPLP 79

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158138488    700 ETVDDFWKMIWEQKATVIVMVTRCEEGNRNKCAEYWPCMEEGTRTFRDVVVTINDHKRCPDYIIQKLSIAHKKEKATgRE 779
Cdd:smart00194   80 STVEDFWRMVWEQKVTVIVMLTELVEKGREKCAQYWPDEEGEPLTYGDITVTLKSVEKVDDYTIRTLEVTNTGCSET-RT 158

                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158138488    780 VTHIQFTSWPDHGVPEDPHLLLKLRRRVNAFSNFFSGPIVVHCSAGVGRTGTYIGIDAMLESLEAEGKVDVYGYVVNLRR 859
Cdd:smart00194  159 VTHYHYTNWPDHGVPESPESILDLIRAVRKSQSTSTGPIVVHCSAGVGRTGTFIAIDILLQQLEAGKEVDIFEIVKELRS 238

                           250       260
                    ....*....|....*....|.
gi 158138488    860 QRCLMVQVEAQYILIHQALVE 880
Cdd:smart00194  239 QRPGMVQTEEQYIFLYRAILE 259
Y_phosphatase pfam00102
Protein-tyrosine phosphatase;
646-880 1.02e-106

Protein-tyrosine phosphatase;


Pssm-ID: 459674 [Multi-domain]  Cd Length: 234  Bit Score: 336.14  E-value: 1.02e-106
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158138488   646 NQNKNRYVDILPYDYNRVELSEINGDagSTYINASYIDGFKEPRKYIAAQGPRDETVDDFWKMIWEQKATVIVMVTRCEE 725
Cdd:pfam00102    1 NLEKNRYKDVLPYDHTRVKLTGDPGP--SDYINASYIDGYKKPKKYIATQGPLPNTVEDFWRMVWEEKVTIIVMLTELEE 78

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158138488   726 GNRNKCAEYWPCMEEGTRTFRDVVVTI-NDHKRCPDYIIQKLSIAHKKEKATgREVTHIQFTSWPDHGVPEDPHLLLKLR 804
Cdd:pfam00102   79 KGREKCAQYWPEEEGESLEYGDFTVTLkKEKEDEKDYTVRTLEVSNGGSEET-RTVKHFHYTGWPDHGVPESPNSLLDLL 157

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 158138488   805 RRVNAFSN-FFSGPIVVHCSAGVGRTGTYIGIDAMLESLEAEGKVDVYGYVVNLRRQRCLMVQVEAQYILIHQALVE 880
Cdd:pfam00102  158 RKVRKSSLdGRSGPIVVHCSAGIGRTGTFIAIDIALQQLEAEGEVDIFQIVKELRSQRPGMVQTLEQYIFLYDAILE 234
R-PTPc-LAR-1 cd14553
catalytic domain of LAR family receptor-type tyrosine-protein phosphatases, repeat 1; The LAR ...
 646-880 1.28e-97

catalytic domain of LAR family receptor-type tyrosine-protein phosphatases, repeat 1; The LAR (leukocyte common antigen-related) family of receptor-type tyrosine-protein phosphatases (RPTPs) include three vertebrate members: LAR (or PTPRF), R-PTP-delta (or PTPRD), and R-PTP-sigma (or PTPRS). They belong to the larger family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. LAR-RPTPs are synaptic adhesion molecules; they bind to distinct synaptic membrane proteins and are physiologically responsible for mediating presynaptic development by shaping various synaptic adhesion pathways. They play roles in various aspects of neuronal development, including axon guidance, neurite extension, and synapse formation and function. LAR-RPTPs contain an extracellular region with three immunoglobulin-like (Ig) domains and four to eight fibronectin type III (FN3) repeats (determined by alternative splicing), a single transmembrane domain, followed by an intracellular region with a membrane-proximal catalytic PTP domain (repeat 1, also called D1) and a membrane-distal non-catalytic PTP-like domain (repeat 2, also called D2). This model represents the catalytic PTP domain (repeat 1).


Pssm-ID: 350401 [Multi-domain]  Cd Length: 238  Bit Score: 311.64  E-value: 1.28e-97
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158138488  646 NQNKNRYVDILPYDYNRVELSEINGDAGSTYINASYIDGFKEPRKYIAAQGPRDETVDDFWKMIWEQKATVIVMVTRCEE 725
Cdd:cd14553     3 NKPKNRYANVIAYDHSRVILQPIEGVPGSDYINANYCDGYRKQNAYIATQGPLPETFGDFWRMVWEQRSATIVMMTKLEE 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158138488  726 GNRNKCAEYWPcmEEGTRTFRDVVVTINDHKRCPDYIIQKLSIaHKKEKATGREVTHIQFTSWPDHGVPEDPHLLLKLRR 805
Cdd:cd14553    83 RSRVKCDQYWP--TRGTETYGLIQVTLLDTVELATYTVRTFAL-HKNGSSEKREVRQFQFTAWPDHGVPEHPTPFLAFLR 159

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 158138488  806 RVNAFSNFFSGPIVVHCSAGVGRTGTYIGIDAMLESLEAEGKVDVYGYVVNLRRQRCLMVQVEAQYILIHQALVE 880
Cdd:cd14553   160 RVKACNPPDAGPIVVHCSAGVGRTGCFIVIDSMLERIKHEKTVDIYGHVTCLRAQRNYMVQTEDQYIFIHDALLE 234
PTPc cd00047
catalytic domain of protein tyrosine phosphatases; Protein tyrosine phosphatases (PTP, EC 3.1. ...
 676-876 8.68e-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: 302.28  E-value: 8.68e-95
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158138488  676 YINASYIDGFKEPRKYIAAQGPRDETVDDFWKMIWEQKATVIVMVTRCEEGNRNKCAEYWPCMEEGTRTFRDVVVTINDH 755
Cdd:cd00047     1 YINASYIDGYRGPKEYIATQGPLPNTVEDFWRMVWEQKVSVIVMLTNLVEKGREKCERYWPEEGGKPLEYGDITVTLVSE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158138488  756 KRCPDYIIQKLSIAHKKEKATgREVTHIQFTSWPDHGVPEDPHLLLKLRRRVNAFSNFFSGPIVVHCSAGVGRTGTYIGI 835
Cdd:cd00047    81 EELSDYTIRTLELSPKGCSES-REVTHLHYTGWPDHGVPSSPEDLLALVRRVRKEARKPNGPIVVHCSAGVGRTGTFIAI 159

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|.
gi 158138488  836 DAMLESLEAEGKVDVYGYVVNLRRQRCLMVQVEAQYILIHQ 876
Cdd:cd00047   160 DILLERLEAEGEVDVFEIVKALRKQRPGMVQTLEQYEFIYE 200
R3-PTPc cd14548
catalytic domain of R3 subfamily receptor-type tyrosine-protein phosphatases and similar ...
 651-876 4.22e-92

catalytic domain of R3 subfamily receptor-type tyrosine-protein phosphatases and similar proteins; R3 subfamily receptor-type phosphotyrosine phosphatases (RPTP) are characterized by a unique modular composition consisting of multiple extracellular fibronectin type III (FN3) repeats and a single (most RPTP subtypes have two) cytoplasmic catalytic PTP domain. Vertebrate members include receptor-type tyrosine-protein phosphatase-like O (PTPRO), J (PTPRJ), Q (PTPRQ), B (PTPRB), V (PTPRV) and H (PTPRH). They belong to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. Most members are PTPs, except for PTPRQ, which dephosphorylates phosphatidylinositide substrates. PTPRV is characterized only in rodents; its function has been lost in humans. Both vertebrate and invertebrate R3 subfamily RPTPs are involved in the control of a variety of cellular processes, including cell growth, differentiation, mitotic cycle and oncogenic transformation.


Pssm-ID: 350396 [Multi-domain]  Cd Length: 222  Bit Score: 295.80  E-value: 4.22e-92
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158138488  651 RYVDILPYDYNRVELSEINGDAGSTYINASYIDGFKEPRKYIAAQGPRDETVDDFWKMIWEQKATVIVMVTRCEEGNRNK 730
Cdd:cd14548     1 RYTNILPYDHSRVKLIPINEEEGSDYINANYIPGYNSPREFIATQGPLPGTKDDFWRMVWEQNSHTIVMLTQCMEKGRVK 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158138488  731 CAEYWPCMEEGTrTFRDVVVTINDHKRCPDYIIQKLSIAHKKEKatgREVTHIQFTSWPDHGVPEDPHLLLKLRRRVNAF 810
Cdd:cd14548    81 CDHYWPFDQDPV-YYGDITVTMLSESVLPDWTIREFKLERGDEV---RSVRQFHFTAWPDHGVPEAPDSLLRFVRLVRDY 156

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 158138488  811 SNFFSGPIVVHCSAGVGRTGTYIGIDAMLESLEAEGKVDVYGYVVNLRRQRCLMVQVEAQYILIHQ 876
Cdd:cd14548   157 IKQEKGPTIVHCSAGVGRTGTFIALDRLLQQIESEDYVDIFGIVYDLRKHRPLMVQTEAQYIFLHQ 222
PTPc smart00194
Protein tyrosine phosphatase, catalytic domain;
913-1194 1.58e-89

Protein tyrosine phosphatase, catalytic domain;


Pssm-ID: 214550 [Multi-domain]  Cd Length: 259  Bit Score: 289.94  E-value: 1.58e-89
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158138488    913 LEAEYQRLPSYRSWR-TQHIGNQEENKKKNRSSNVVPYDFNRVPLKHELEmskeseaesdessdedsdseETSKYINASF 991
Cdd:smart00194    2 LEEEFEKLDRLKPDDeSCTVAAFPENRDKNRYKDVLPYDHTRVKLKPPPG--------------------EGSDYINASY 61

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158138488    992 VMSYWKPEMMIAAQGPLKETIGDFWQMIFQRKVKVIVMLTELMSGDQEVCAQYW---GEGKQTYGDMEVMLKDTNKSSAY 1068
Cdd:smart00194   62 IDGPNGPKAYIATQGPLPSTVEDFWRMVWEQKVTVIVMLTELVEKGREKCAQYWpdeEGEPLTYGDITVTLKSVEKVDDY 141

                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158138488   1069 ILRAFELRHSKRKEPRTVYQYQCTTWKGEELPAEPKDLVTLIQNIKQKLPksgsegmkyHKHASILVHCRDGSQQTGLFC 1148
Cdd:smart00194  142 TIRTLEVTNTGCSETRTVTHYHYTNWPDHGVPESPESILDLIRAVRKSQS---------TSTGPIVVHCSAGVGRTGTFI 212

                           250       260       270       280
                    ....*....|....*....|....*....|....*....|....*.
gi 158138488   1149 ALFNLLESAETEDVVDVFQVVKSLRKARPGMVGSFEQYQFLYDIMA 1194
Cdd:smart00194  213 AIDILLQQLEAGKEVDIFEIVKELRSQRPGMVQTEEQYIFLYRAIL 258
R-PTPc-A-1 cd14621
catalytic domain of receptor-type tyrosine-protein phosphatase A, repeat 1; Receptor-type ...
 601-889 2.26e-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: 291.16  E-value: 2.26e-89
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158138488  601 PIHSDLLLETYKRKIADEGRLFLAEFQSIPRVFSKFPIKDARKSQNQNKNRYVDILPYDYNRVELSEINGDAGSTYINAS 680
Cdd:cd14621     7 PLPVDKLEEEINRRMADDNKLFREEFNALPACPIQATCEAASKEENKEKNRYVNILPYDHSRVHLTPVEGVPDSDYINAS 86

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158138488  681 YIDGFKEPRKYIAAQGPRDETVDDFWKMIWEQKATVIVMVTRCEEGNRNKCAEYWPcmEEGTRTFRDVVVTINDHKRCPD 760
Cdd:cd14621    87 FINGYQEKNKFIAAQGPKEETVNDFWRMIWEQNTATIVMVTNLKERKECKCAQYWP--DQGCWTYGNIRVSVEDVTVLVD 164

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158138488  761 YIIQKLSIAHKKE---KATGREVTHIQFTSWPDHGVPEDPHLLLKLRRRVNAFSNFFSGPIVVHCSAGVGRTGTYIGIDA 837
Cdd:cd14621   165 YTVRKFCIQQVGDvtnKKPQRLITQFHFTSWPDFGVPFTPIGMLKFLKKVKNCNPQYAGAIVVHCSAGVGRTGTFIVIDA 244

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|..
gi 158138488  838 MLESLEAEGKVDVYGYVVNLRRQRCLMVQVEAQYILIHQALVEYNQFGETEV 889
Cdd:cd14621   245 MLDMMHAERKVDVYGFVSRIRAQRCQMVQTDMQYVFIYQALLEHYLYGDTEL 296
Y_phosphatase pfam00102
Protein-tyrosine phosphatase;
937-1194 4.79e-85

Protein-tyrosine phosphatase;


Pssm-ID: 459674 [Multi-domain]  Cd Length: 234  Bit Score: 276.43  E-value: 4.79e-85
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158138488   937 NKKKNRSSNVVPYDFNRVPLKHElemskeseaesdessdedsdsEETSKYINASFVMSYWKPEMMIAAQGPLKETIGDFW 1016
Cdd:pfam00102    1 NLEKNRYKDVLPYDHTRVKLTGD---------------------PGPSDYINASYIDGYKKPKKYIATQGPLPNTVEDFW 59

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158138488  1017 QMIFQRKVKVIVMLTELMSGDQEVCAQYW---GEGKQTYGDMEVMLKDTNK-SSAYILRAFELRHSKRKEPRTVYQYQCT 1092
Cdd:pfam00102   60 RMVWEEKVTIIVMLTELEEKGREKCAQYWpeeEGESLEYGDFTVTLKKEKEdEKDYTVRTLEVSNGGSEETRTVKHFHYT 139

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158138488  1093 TWKGEELPAEPKDLVTLIQNIKQKLPKsgsegmkyHKHASILVHCRDGSQQTGLFCALFNLLESAETEDVVDVFQVVKSL 1172
Cdd:pfam00102  140 GWPDHGVPESPNSLLDLLRKVRKSSLD--------GRSGPIVVHCSAGIGRTGTFIAIDIALQQLEAEGEVDIFQIVKEL 211

                          250       260
                   ....*....|....*....|..
gi 158138488  1173 RKARPGMVGSFEQYQFLYDIMA 1194
Cdd:pfam00102  212 RSQRPGMVQTLEQYIFLYDAIL 233
R5-PTPc-1 cd14549
catalytic domain of R5 subfamily receptor-type tyrosine-protein phosphatases, repeat 1; The R5 ...
 676-875 1.70e-84

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: 273.84  E-value: 1.70e-84
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158138488  676 YINASYIDGFKEPRKYIAAQGPRDETVDDFWKMIWEQKATVIVMVTRCEEGNRNKCAEYWPcmEEGTRTFRDVVVTINDH 755
Cdd:cd14549     1 YINANYVDGYNKARAYIATQGPLPSTFDDFWRMVWEQNSAIIVMITNLVERGRRKCDQYWP--KEGTETYGNIQVTLLST 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158138488  756 KRCPDYIIQKLSIAHKKEK-----ATGREVTHIQFTSWPDHGVPEDPHLLLKLRRRVNAFSNFFSGPIVVHCSAGVGRTG 830
Cdd:cd14549    79 EVLATYTVRTFSLKNLKLKkvkgrSSERVVYQYHYTQWPDHGVPDYTLPVLSFVRKSSAANPPGAGPIVVHCSAGVGRTG 158

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*
gi 158138488  831 TYIGIDAMLESLEAEGKVDVYGYVVNLRRQRCLMVQVEAQYILIH 875
Cdd:cd14549   159 TYIVIDSMLQQIQDKGTVNVFGFLKHIRTQRNYLVQTEEQYIFIH 203
R-PTPc-F-1 cd14626
catalytic domain of receptor-type tyrosine-protein phosphatase F, repeat 1; Receptor-type ...
 607-880 4.69e-83

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: 272.68  E-value: 4.69e-83
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158138488  607 LLETYKRKIADEGRLFLAEFQSI-PRvfSKFPIKDARKSQNQNKNRYVDILPYDYNRVELSEINGDAGSTYINASYIDGF 685
Cdd:cd14626     3 LADNIERLKANDGLKFSQEYESIdPG--QQFTWENSNLEVNKPKNRYANVIAYDHSRVILTSVDGVPGSDYINANYIDGY 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158138488  686 KEPRKYIAAQGPRDETVDDFWKMIWEQKATVIVMVTRCEEGNRNKCAEYWPCmeEGTRTFRDVVVTINDHKRCPDYIIQK 765
Cdd:cd14626    81 RKQNAYIATQGPLPETLSDFWRMVWEQRTATIVMMTRLEEKSRVKCDQYWPI--RGTETYGMIQVTLLDTVELATYSVRT 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158138488  766 LSIaHKKEKATGREVTHIQFTSWPDHGVPEDPHLLLKLRRRVNAFSNFFSGPIVVHCSAGVGRTGTYIGIDAMLESLEAE 845
Cdd:cd14626   159 FAL-YKNGSSEKREVRQFQFMAWPDHGVPEYPTPILAFLRRVKACNPPDAGPMVVHCSAGVGRTGCFIVIDAMLERMKHE 237

                         250       260       270
                  ....*....|....*....|....*....|....*
gi 158138488  846 GKVDVYGYVVNLRRQRCLMVQVEAQYILIHQALVE 880
Cdd:cd14626   238 KTVDIYGHVTCMRSQRNYMVQTEDQYIFIHEALLE 272
R-PTPc-E-1 cd14620
catalytic domain of receptor-type tyrosine-protein phosphatase E, repeat 1; Receptor-type ...
 652-880 1.96e-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: 266.42  E-value: 1.96e-81
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158138488  652 YVDILPYDYNRVELSEINGDAGSTYINASYIDGFKEPRKYIAAQGPRDETVDDFWKMIWEQKATVIVMVTRCEEGNRNKC 731
Cdd:cd14620     1 YPNILPYDHSRVILSQLDGIPCSDYINASYIDGYKEKNKFIAAQGPKQETVNDFWRMVWEQKSATIVMLTNLKERKEEKC 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158138488  732 AEYWPcmEEGTRTFRDVVVTINDHKRCPDYIIQKLSIA---HKKEKATgREVTHIQFTSWPDHGVPEDPHLLLKLRRRVN 808
Cdd:cd14620    81 YQYWP--DQGCWTYGNIRVAVEDCVVLVDYTIRKFCIQpqlPDGCKAP-RLVTQLHFTSWPDFGVPFTPIGMLKFLKKVK 157

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 158138488  809 AFSNFFSGPIVVHCSAGVGRTGTYIGIDAMLESLEAEGKVDVYGYVVNLRRQRCLMVQVEAQYILIHQALVE 880
Cdd:cd14620   158 SVNPVHAGPIVVHCSAGVGRTGTFIVIDAMIDMMHAEQKVDVFEFVSRIRNQRPQMVQTDMQYSFIYQALLE 229
PTPc-N9 cd14543
catalytic domain of tyrosine-protein phosphatase non-receptor type 9; Tyrosine-protein ...
 641-875 1.72e-78

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


Pssm-ID: 350391 [Multi-domain]  Cd Length: 271  Bit Score: 259.60  E-value: 1.72e-78
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158138488  641 ARKSQNQNKNRYVDILPYDYNRVELSEINGDAGSTYINASYIDGFKEPRKYIAAQGPRDETVDDFWKMIWEQKATVIVMV 720
Cdd:cd14543    24 SLAPANQEKNRYGDVLCLDQSRVKLPKRNGDERTDYINANFMDGYKQKNAYIATQGPLPKTYSDFWRMVWEQKVLVIVMT 103

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158138488  721 TRCEEGNRNKCAEYWPCMEEGTRTFRDVVVT---INDHKrcpDYIIQKLSIaHKKEKATGREVTHIQFTSWPDHGVPEDP 797
Cdd:cd14543   104 TRVVERGRVKCGQYWPLEEGSSLRYGDLTVTnlsVENKE---HYKKTTLEI-HNTETDESRQVTHFQFTSWPDFGVPSSA 179

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158138488  798 HLLL--------KLRRRVNAFSNFFSG-----PIVVHCSAGVGRTGTYIGIDAMLESLEAEGKVDVYGYVVNLRRQRCLM 864
Cdd:cd14543   180 AALLdflgevrqQQALAVKAMGDRWKGhppgpPIVVHCSAGIGRTGTFCTLDICLSQLEDVGTLNVMQTVRRMRTQRAFS 259

                         250
                  ....*....|.
gi 158138488  865 VQVEAQYILIH 875
Cdd:cd14543   260 IQTPDQYYFCY 270
R-PTPc-H cd14619
catalytic domain of receptor-type tyrosine-protein phosphatase H; Receptor-type ...
 650-881 9.54e-77

catalytic domain of receptor-type tyrosine-protein phosphatase H; Receptor-type tyrosine-protein phosphatase H (PTPRH or R-PTP-H), also known as stomach cancer-associated protein tyrosine phosphatase 1 (SAP-1), belongs to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. PTPRH is a member of the R3 subfamily of receptor-type phosphotyrosine phosphatases (RPTP), characterized by a unique modular composition consisting of multiple extracellular fibronectin type III (FN3) repeats and a single (most RPTP subtypes have two) cytoplasmic catalytic PTP domain. It is localized specifically at microvilli of the brush border in gastrointestinal epithelial cells. It plays a role in intestinal immunity by regulating CEACAM20 through tyrosine dephosphorylation. It is also a negative regulator of integrin-mediated signaling and may contribute to contact inhibition of cell growth and motility.


Pssm-ID: 350467 [Multi-domain]  Cd Length: 233  Bit Score: 253.27  E-value: 9.54e-77
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158138488  650 NRYVDILPYDYNRVELSEINGDAGSTYINASYIDGFKEPRKYIAAQGPRDETVDDFWKMIWEQKATVIVMVTRCEEGNRN 729
Cdd:cd14619     1 NRFRNVLPYDWSRVPLKPIHEEPGSDYINANYMPGYWSSQEFIATQGPLPQTVGDFWRMIWEQQSSTIVMLTNCMEAGRV 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158138488  730 KCAEYWPcMEEGTRTFRDVVVTINDHKRCPDYIIQKLSIAHKKEKATgREVTHIQFTSWPDHGVPEDPHLLLKLRRRVNA 809
Cdd:cd14619    81 KCEHYWP-LDYTPCTYGHLRVTVVSEEVMENWTVREFLLKQVEEQKT-LSVRHFHFTAWPDHGVPSSTDTLLAFRRLLRQ 158

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 158138488  810 F--SNFFSGPIVVHCSAGVGRTGTYIGIDAMLESLEAEGKVDVYGYVVNLRRQRCLMVQVEAQYILIHQALVEY 881
Cdd:cd14619   159 WldQTMSGGPTVVHCSAGVGRTGTLIALDVLLQQLQSEGLLGPFSFVQKMRENRPLMVQTESQYVFLHQCILDF 232
R-PTPc-A-E-1 cd14551
catalytic domain of receptor-type tyrosine-protein phosphatase A and E, repeat 1; ...
 676-876 1.19e-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: 251.76  E-value: 1.19e-76
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158138488  676 YINASYIDGFKEPRKYIAAQGPRDETVDDFWKMIWEQKATVIVMVTRCEEGNRNKCAEYWPcmEEGTRTFRDVVVTINDH 755
Cdd:cd14551     1 YINASYIDGYQEKNKFIAAQGPKDETVNDFWRMIWEQGSATIVMVTNLKERKEKKCSQYWP--DQGCWTYGNLRVRVEDT 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158138488  756 KRCPDYIIQKLSIaHKKEKATG----REVTHIQFTSWPDHGVPEDPHLLLKLRRRVNAFSNFFSGPIVVHCSAGVGRTGT 831
Cdd:cd14551    79 VVLVDYTTRKFCI-QKVNRGIGekrvRLVTQFHFTSWPDFGVPFTPIGMLKFLKKVKSANPPRAGPIVVHCSAGVGRTGT 157

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*
gi 158138488  832 YIGIDAMLESLEAEGKVDVYGYVVNLRRQRCLMVQVEAQYILIHQ 876
Cdd:cd14551   158 FIVIDAMLDMMHAEGKVDVFGFVSRIRQQRSQMVQTDMQYVFIYQ 202
PTPc cd00047
catalytic domain of protein tyrosine phosphatases; Protein tyrosine phosphatases (PTP, EC 3.1. ...
 986-1191 1.65e-76

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: 251.44  E-value: 1.65e-76
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158138488  986 YINASFVMSYWKPEMMIAAQGPLKETIGDFWQMIFQRKVKVIVMLTELMSGDQEVCAQYW---GEGKQTYGDMEVMLKDT 1062
Cdd:cd00047     1 YINASYIDGYRGPKEYIATQGPLPNTVEDFWRMVWEQKVSVIVMLTNLVEKGREKCERYWpeeGGKPLEYGDITVTLVSE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158138488 1063 NKSSAYILRAFELRHSKRKEPRTVYQYQCTTWKGEELPAEPKDLVTLIQNIKQKLPKSgsegmkyhkHASILVHCRDGSQ 1142
Cdd:cd00047    81 EELSDYTIRTLELSPKGCSESREVTHLHYTGWPDHGVPSSPEDLLALVRRVRKEARKP---------NGPIVVHCSAGVG 151

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*....
gi 158138488 1143 QTGLFCALFNLLESAETEDVVDVFQVVKSLRKARPGMVGSFEQYQFLYD 1191
Cdd:cd00047   152 RTGTFIAIDILLERLEAEGEVDVFEIVKALRKQRPGMVQTLEQYEFIYE 200
R-PTPc-S-1 cd14625
catalytic domain of receptor-type tyrosine-protein phosphatase S, repeat 1; Receptor-type ...
 601-880 2.32e-74

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: 248.47  E-value: 2.32e-74
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158138488  601 PIHSDLLLETYKRKIADEGRLFLAEFQSIPRvFSKFPIKDARKSQNQNKNRYVDILPYDYNRVELSEINGDAGSTYINAS 680
Cdd:cd14625     3 PIPISELAEHTERLKANDNLKLSQEYESIDP-GQQFTWEHSNLEVNKPKNRYANVIAYDHSRVILQPIEGIMGSDYINAN 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158138488  681 YIDGFKEPRKYIAAQGPRDETVDDFWKMIWEQKATVIVMVTRCEEGNRNKCAEYWPcmEEGTRTFRDVVVTINDHKRCPD 760
Cdd:cd14625    82 YIDGYRKQNAYIATQGPLPETFGDFWRMVWEQRSATVVMMTKLEEKSRIKCDQYWP--SRGTETYGMIQVTLLDTIELAT 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158138488  761 YIIQKLSIaHKKEKATGREVTHIQFTSWPDHGVPEDPHLLLKLRRRVNAFSNFFSGPIVVHCSAGVGRTGTYIGIDAMLE 840
Cdd:cd14625   160 FCVRTFSL-HKNGSSEKREVRQFQFTAWPDHGVPEYPTPFLAFLRRVKTCNPPDAGPIVVHCSAGVGRTGCFIVIDAMLE 238

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|
gi 158138488  841 SLEAEGKVDVYGYVVNLRRQRCLMVQVEAQYILIHQALVE 880
Cdd:cd14625   239 RIKHEKTVDIYGHVTLMRSQRNYMVQTEDQYSFIHDALLE 278
PTPc-KIM cd14547
catalytic domain of the kinase interaction motif (KIM) family of protein-tyrosine phosphatases; ...
 650-876 2.52e-74

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: 246.15  E-value: 2.52e-74
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158138488  650 NRYVDILPYDYNRVELSEINGDAGSTYINASYIDGFK-EPRKYIAAQGPRDETVDDFWKMIWEQKATVIVMVTRCEEGNR 728
Cdd:cd14547     1 NRYKTILPNEHSRVCLPSVDDDPLSSYINANYIRGYDgEEKAYIATQGPLPNTVADFWRMVWQEKTPIIVMITNLTEAKE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158138488  729 nKCAEYWPcMEEGTRtFRDVVVTINDHKRCPDYIIQKLSIAHKKEKatgREVTHIQFTSWPDHGVPEDPHLLLKLRRRVN 808
Cdd:cd14547    81 -KCAQYWP-EEENET-YGDFEVTVQSVKETDGYTVRKLTLKYGGEK---RYLKHYWYTSWPDHKTPEAAQPLLSLVQEVE 154

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158138488  809 --AFSNFFSGPIVVHCSAGVGRTGTYIGIDAMLESLEAEGKVDVYGYVVNLRRQRCLMVQVEAQYILIHQ 876
Cdd:cd14547   155 eaRQTEPHRGPIVVHCSAGIGRTGCFIATSIGCQQLREEGVVDVLGIVCQLRLDRGGMVQTAEQYEFVHR 224
R-PTPc-J cd14615
catalytic domain of receptor-type tyrosine-protein phosphatase J; Receptor-type ...
 650-876 6.65e-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: 245.11  E-value: 6.65e-74
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158138488  650 NRYVDILPYDYNRVELSeINGDAGSTYINASYIDGFKEPRKYIAAQGPRDETVDDFWKMIWEQKATVIVMVTRCEEGNRN 729
Cdd:cd14615     1 NRYNNVLPYDISRVKLS-VQSHSTDDYINANYMPGYNSKKEFIAAQGPLPNTVKDFWRMVWEKNVYAIVMLTKCVEQGRT 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158138488  730 KCAEYWPcmEEGTRTFRDVVVTINDHKRCPDYIIQKLSIAHKKEkATGREVTHIQFTSWPDHGVPEDPHLLLKLRRRVNA 809
Cdd:cd14615    80 KCEEYWP--SKQKKDYGDITVTMTSEIVLPEWTIRDFTVKNAQT-NESRTVRHFHFTSWPDHGVPETTDLLINFRHLVRE 156

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 158138488  810 FS--NFFSGPIVVHCSAGVGRTGTYIGIDAMLESLEAEGKVDVYGYVVNLRRQRCLMVQVEAQYILIHQ 876
Cdd:cd14615   157 YMkqNPPNSPILVHCSAGVGRTGTFIAIDRLIYQIENENVVDVYGIVYDLRMHRPLMVQTEDQYVFLNQ 225
R-PTPc-D-1 cd14624
catalytic domain of receptor-type tyrosine-protein phosphatase D, repeat 1; Receptor-type ...
 601-880 2.47e-73

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: 245.80  E-value: 2.47e-73
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158138488  601 PIHSDLLLETYKRKIADEGRLFLAEFQSIPRvFSKFPIKDARKSQNQNKNRYVDILPYDYNRVELSEINGDAGSTYINAS 680
Cdd:cd14624     3 PIPILELADHIERLKANDNLKFSQEYESIDP-GQQFTWEHSNLEVNKPKNRYANVIAYDHSRVLLSAIEGIPGSDYINAN 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158138488  681 YIDGFKEPRKYIAAQGPRDETVDDFWKMIWEQKATVIVMVTRCEEGNRNKCAEYWPcmEEGTRTFRDVVVTINDHKRCPD 760
Cdd:cd14624    82 YIDGYRKQNAYIATQGALPETFGDFWRMIWEQRSATVVMMTKLEERSRVKCDQYWP--SRGTETYGLIQVTLLDTVELAT 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158138488  761 YIIQKLSIaHKKEKATGREVTHIQFTSWPDHGVPEDPHLLLKLRRRVNAFSNFFSGPIVVHCSAGVGRTGTYIGIDAMLE 840
Cdd:cd14624   160 YCVRTFAL-YKNGSSEKREVRQFQFTAWPDHGVPEHPTPFLAFLRRVKTCNPPDAGPMVVHCSAGVGRTGCFIVIDAMLE 238

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|
gi 158138488  841 SLEAEGKVDVYGYVVNLRRQRCLMVQVEAQYILIHQALVE 880
Cdd:cd14624   239 RIKHEKTVDIYGHVTLMRAQRNYMVQTEDQYIFIHDALLE 278
R-PTPc-B cd14617
catalytic domain of receptor-type tyrosine-protein phosphatase B; Receptor-type ...
 650-876 3.60e-73

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: 242.90  E-value: 3.60e-73
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158138488  650 NRYVDILPYDYNRVELSEINGDAGSTYINASYIDGFKEPRKYIAAQGPRDETVDDFWKMIWEQKATVIVMVTRCEEGNRN 729
Cdd:cd14617     1 NRYNNILPYDSTRVKLSNVDDDPCSDYINASYIPGNNFRREYIATQGPLPGTKDDFWKMVWEQNVHNIVMVTQCVEKGRV 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158138488  730 KCAEYWPcMEEGTRTFRDVVVTINDHKRCPDYIIQKLSIAHKKEKATGREVTHIQFTSWPDHGVPEDPHLLLKLRRRVNA 809
Cdd:cd14617    81 KCDHYWP-ADQDSLYYGDLIVQMLSESVLPEWTIREFKICSEEQLDAPRLVRHFHYTVWPDHGVPETTQSLIQFVRTVRD 159

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 158138488  810 FSNFF--SGPIVVHCSAGVGRTGTYIGIDAMLESLEAEGKVDVYGYVVNLRRQRCLMVQVEAQYILIHQ 876
Cdd:cd14617   160 YINRTpgSGPTVVHCSAGVGRTGTFIALDRILQQLDSKDSVDIYGAVHDLRLHRVHMVQTECQYVYLHQ 228
R-PTPc-T-1 cd14630
catalytic domain of receptor-type tyrosine-protein phosphatase T, repeat 1; Receptor-type ...
 645-880 8.71e-71

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


Pssm-ID: 350478 [Multi-domain]  Cd Length: 237  Bit Score: 236.85  E-value: 8.71e-71
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158138488  645 QNQNKNRYVDILPYDYNRVELSEINGDAGSTYINASYIDGFKEPRKYIAAQGPRDETVDDFWKMIWEQKATVIVMVTRCE 724
Cdd:cd14630     2 ENRNKNRYGNIISYDHSRVRLQLLDGDPHSDYINANYIDGYHRPRHYIATQGPMQETVKDFWRMIWQENSASVVMVTNLV 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158138488  725 EGNRNKCAEYWPcmeEGTRTFRDVVVTINDHKRCPDYIIQKLSIaHKKEKATGREVTHIQFTSWPDHGVPEDPHLLLKLR 804
Cdd:cd14630    82 EVGRVKCVRYWP---DDTEVYGDIKVTLIETEPLAEYVIRTFTV-QKKGYHEIREIRQFHFTSWPDHGVPCYATGLLGFV 157

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 158138488  805 RRVNAFSNFFSGPIVVHCSAGVGRTGTYIGIDAMLESLEAEGKVDVYGYVVNLRRQRCLMVQVEAQYILIHQALVE 880
Cdd:cd14630   158 RQVKFLNPPDAGPIVVHCSAGAGRTGCFIAIDIMLDMAENEGVVDIFNCVRELRAQRVNMVQTEEQYVFVHDAILE 233
R-PTPc-O cd14614
catalytic domain of receptor-type tyrosine-protein phosphatase O; Receptor-type ...
 629-876 2.19e-70

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: 235.94  E-value: 2.19e-70
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158138488  629 IPRVFSKFPIkdarksqNQNKNRYVDILPYDYNRVELSEINGDAGSTYINASYIDGFKEPRKYIAAQGPRDETVDDFWKM 708
Cdd:cd14614     2 IPHFAADLPV-------NRCKNRYTNILPYDFSRVKLVSMHEEEGSDYINANYIPGYNSPQEYIATQGPLPETRNDFWKM 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158138488  709 IWEQKATVIVMVTRCEEGNRNKCAEYWPCMEEGTrTFRDVVVTINDHKRCPDYIIQKLSIAHKKEKatgREVTHIQFTSW 788
Cdd:cd14614    75 VLQQKSQIIVMLTQCNEKRRVKCDHYWPFTEEPV-AYGDITVEMLSEEEQPDWAIREFRVSYADEV---QDVMHFNYTAW 150

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158138488  789 PDHGVP--EDPHLLLKLRRRVNAFSNFFSGPIVVHCSAGVGRTGTYIGIDAMLESLEAEGKVDVYGYVVNLRRQRCLMVQ 866
Cdd:cd14614   151 PDHGVPtaNAAESILQFVQMVRQQAVKSKGPMIIHCSAGVGRTGTFIALDRLLQHIRDHEFVDILGLVSEMRSYRMSMVQ 230

                         250
                  ....*....|
gi 158138488  867 VEAQYILIHQ 876
Cdd:cd14614   231 TEEQYIFIHQ 240
R-PTPc-M-1 cd14633
catalytic domain of receptor-type tyrosine-protein phosphatase M, repeat 1; Receptor-type ...
 605-880 7.94e-70

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: 235.32  E-value: 7.94e-70
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158138488  605 DLLLETYKRKIAdEGRLFLAEFQSIPRVFSKfPIKDARKSQNQNKNRYVDILPYDYNRVELSEINGDAGSTYINASYIDG 684
Cdd:cd14633     1 DLLQHITQMKCA-EGYGFKEEYESFFEGQSA-PWDSAKKDENRMKNRYGNIIAYDHSRVRLQPIEGETSSDYINGNYIDG 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158138488  685 FKEPRKYIAAQGPRDETVDDFWKMIWEQKATVIVMVTRCEEGNRNKCAEYWPcmeEGTRTFRDVVVTINDHKRCPDYIIQ 764
Cdd:cd14633    79 YHRPNHYIATQGPMQETIYDFWRMVWHENTASIIMVTNLVEVGRVKCCKYWP---DDTEIYKDIKVTLIETELLAEYVIR 155

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158138488  765 KLSIaHKKEKATGREVTHIQFTSWPDHGVPEDPHLLLKLRRRVNAFSNFFSGPIVVHCSAGVGRTGTYIGIDAMLESLEA 844
Cdd:cd14633   156 TFAV-EKRGVHEIREIRQFHFTGWPDHGVPYHATGLLGFVRQVKSKSPPNAGPLVVHCSAGAGRTGCFIVIDIMLDMAER 234

                         250       260       270
                  ....*....|....*....|....*....|....*.
gi 158138488  845 EGKVDVYGYVVNLRRQRCLMVQVEAQYILIHQALVE 880
Cdd:cd14633   235 EGVVDIYNCVRELRSRRVNMVQTEEQYVFIHDAILE 270
R-PTPc-G-1 cd17667
catalytic domain of receptor-type tyrosine-protein phosphatase G, repeat 1; Receptor-type ...
 622-880 1.52e-69

catalytic domain of receptor-type tyrosine-protein phosphatase G, repeat 1; Receptor-type tyrosine-protein phosphatase G (PTPRG), also called protein-tyrosine phosphatase gamma (R-PTP-gamma), belongs to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. PTPRG is an important tumor suppressor gene in multiple human cancers such as lung, ovarian, and breast cancers. It is widely expressed in many tissues, including the central nervous system, where it plays a role during neuroinflammation processes. It can dephosphorylate platelet-derived growth factor receptor beta (PDGFRB) and may play a role in PDGFRB-related infantile myofibromatosis. PTPRG has four splicing isoforms: three transmembrane isoforms, PTPRG-A, B, and C, and one secretory isoform, PTPRG-S, which are expressed in many tissues including the brain. PTPRG is a type 1 integral membrane protein consisting of an extracellular region with a carbonic anhydrase-like (CAH) and a fibronectin type III (FN3) domains, and an intracellular region with a catalytic PTP domain (repeat 1) proximal to the membrane, and a catalytically inactive PTP-fold domain (repeat 2) distal to the membrane. This model represents the catalytic PTP domain (repeat 1).


Pssm-ID: 350505 [Multi-domain]  Cd Length: 274  Bit Score: 234.54  E-value: 1.52e-69
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158138488  622 FLAEFQSIPRVFSKFPI--KDARKSQNQNKNRYVDILPYDYNRVELSEINGDAG--STYINASYIDGFKEPRKYIAAQGP 697
Cdd:cd17667     1 FSEDFEEVQRCTADMNItaEHSNHPDNKHKNRYINILAYDHSRVKLRPLPGKDSkhSDYINANYVDGYNKAKAYIATQGP 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158138488  698 RDETVDDFWKMIWEQKATVIVMVTRCEEGNRNKCAEYWPcmEEGTRTFRDVVVTINDHKRCPDYIIQKLSIAHKKEK--- 774
Cdd:cd17667    81 LKSTFEDFWRMIWEQNTGIIVMITNLVEKGRRKCDQYWP--TENSEEYGNIIVTLKSTKIHACYTVRRFSIRNTKVKkgq 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158138488  775 ---ATGRE----VTHIQFTSWPDHGVPEDPHLLLKLRRRVNAFSNFFSGPIVVHCSAGVGRTGTYIGIDAMLESLEAEGK 847
Cdd:cd17667   159 kgnPKGRQnertVIQYHYTQWPDMGVPEYALPVLTFVRRSSAARTPEMGPVLVHCSAGVGRTGTYIVIDSMLQQIKDKST 238

                         250       260       270
                  ....*....|....*....|....*....|...
gi 158138488  848 VDVYGYVVNLRRQRCLMVQVEAQYILIHQALVE 880
Cdd:cd17667   239 VNVLGFLKHIRTQRNYLVQTEEQYIFIHDALLE 271
PTPc-N11_6 cd14544
catalytic domain of tyrosine-protein phosphatase non-receptor type 11 and type 6; ...
 646-881 1.42e-67

catalytic domain of tyrosine-protein phosphatase non-receptor type 11 and type 6; Tyrosine-protein phosphatase non-receptor type 11 (PTPN11) and type 6 (PTPN6) belong to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. PTPN11 and PTPN6, are also called SH2 domain-containing tyrosine phosphatase 2 (SHP2) and 1 (SHP1), respectively. They contain two tandem SH2 domains: a catalytic PTP domain, and a C-terminal tail with regulatory properties. Although structurally similar, they have different localization and different roles in signal transduction. PTPN11/SHP2 is expressed ubiquitously and plays a positive role in cell signaling, leading to cell activation, while PTPN6/SHP1 expression is restricted mainly to hematopoietic and epithelial cells and functions as a negative regulator of signaling events.


Pssm-ID: 350392 [Multi-domain]  Cd Length: 251  Bit Score: 228.12  E-value: 1.42e-67
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158138488  646 NQNKNRYVDILPYDYNRVELSEINGD-AGSTYINASYI-------DGFKEPRKYIAAQGPRDETVDDFWKMIWEQKATVI 717
Cdd:cd14544     1 NKGKNRYKNILPFDHTRVILKDRDPNvPGSDYINANYIrnenegpTTDENAKTYIATQGCLENTVSDFWSMVWQENSRVI 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158138488  718 VMVTRCEEGNRNKCAEYWPcmEEG-TRTFRDVVVTINDHKRCPDYIIQKLSIAHKKEKATGREVTHIQFTSWPDHGVPED 796
Cdd:cd14544    81 VMTTKEVERGKNKCVRYWP--DEGmQKQYGPYRVQNVSEHDTTDYTLRELQVSKLDQGDPIREIWHYQYLSWPDHGVPSD 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158138488  797 PHLLLKLRRRVNAFSNFF--SGPIVVHCSAGVGRTGTYIGIDAMLESLEAEG---KVDVYGYVVNLRRQRCLMVQVEAQY 871
Cdd:cd14544   159 PGGVLNFLEDVNQRQESLphAGPIVVHCSAGIGRTGTFIVIDMLLDQIKRKGldcDIDIQKTIQMVRSQRSGMVQTEAQY 238

                         250
                  ....*....|
gi 158138488  872 ILIHQALVEY 881
Cdd:cd14544   239 KFIYVAVAQY 248
R-PTP-LAR-2 cd14554
PTP-like domain of the LAR family receptor-type tyrosine-protein phosphatases, repeat 2; The ...
 646-877 3.30e-67

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: 226.64  E-value: 3.30e-67
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158138488  646 NQNKNRYVDILPYDYNRVELSEINGDAGSTYINASYIDGFKEPRKYIAAQGPRDETVDDFWKMIWEQKATVIVMVTRCEE 725
Cdd:cd14554     6 NKFKNRLVNILPYESTRVCLQPIRGVEGSDYINASFIDGYRQRGAYIATQGPLAETTEDFWRMLWEHNSTIIVMLTKLRE 85

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158138488  726 GNRNKCAEYWPcMEEGTRTFRDVVVTINDHKRcPDYIIQKLSIAHKKEKaTGREVTHIQFTSWPDHGVPEDPHLLLKLRR 805
Cdd:cd14554    86 MGREKCHQYWP-AERSARYQYFVVDPMAEYNM-PQYILREFKVTDARDG-QSRTVRQFQFTDWPEQGVPKSGEGFIDFIG 162

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 158138488  806 RV-NAFSNF-FSGPIVVHCSAGVGRTGTYIGIDAMLESLEAEGKVDVYGYVVNLRRQRCLMVQVEAQYILIHQA 877
Cdd:cd14554   163 QVhKTKEQFgQEGPITVHCSAGVGRTGVFITLSIVLERMRYEGVVDVFQTVKLLRTQRPAMVQTEDQYQFCYRA 236
PTP_fungal cd18533
fungal protein tyrosine phosphatases; This subfamily contains Saccharomyces cerevisiae ...
 676-876 6.38e-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: 224.82  E-value: 6.38e-67
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158138488  676 YINASYID-GFKEPRKYIAAQGPRDETVDDFWKMIWEQKATVIVMVTRCEEGNRNKCAEYWPCMEEGTRTFrDVVVTIND 754
Cdd:cd18533     1 YINASYITlPGTSSKRYIATQGPLPATIGDFWKMIWQNNVGVIVMLTPLVENGREKCDQYWPSGEYEGEYG-DLTVELVS 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158138488  755 HKRCPD--YIIQKLSIAHKKEKAtgREVTHIQFTSWPDHGVPEDPHLLLKLRRRVNA--FSNFFSGPIVVHCSAGVGRTG 830
Cdd:cd18533    80 EEENDDggFIVREFELSKEDGKV--KKVYHIQYKSWPDFGVPDSPEDLLTLIKLKRElnDSASLDPPIIVHCSAGVGRTG 157

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 158138488  831 TYIGIDAMLESLEA--------EGKVD-VYGYVVNLRRQRCLMVQVEAQYILIHQ 876
Cdd:cd18533   158 TFIALDSLLDELKRglsdsqdlEDSEDpVYEIVNQLRKQRMSMVQTLRQYIFLYD 212
R-PTPc-V cd14618
catalytic domain of receptor-type tyrosine-protein phosphatase V; Receptor-type ...
 650-879 1.55e-65

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: 221.36  E-value: 1.55e-65
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158138488  650 NRYVDILPYDYNRVELSEINGDAGSTYINASYIDGFKEPRKYIAAQGPRDETVDDFWKMIWEQKATVIVMVTRCEEGNRN 729
Cdd:cd14618     1 NRYPHVLPYDHSRVRLSQLGGEPHSDYINANFIPGYTSPQEFIATQGPLKKTIEDFWRLVWEQQVCNIIMLTVGMENGRV 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158138488  730 KCAEYWPcMEEGTRTFRDVVVTINDHKRCPDYIIQKLSIAHKKEKATgREVTHIQFTSWPDHGVPEDPHLLLKLRRRVNA 809
Cdd:cd14618    81 LCDHYWP-SESTPVSYGHITVHLLAQSSEDEWTRREFKLWHEDLRKE-RRVKHLHYTAWPDHGIPESTSSLMAFRELVRE 158

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 158138488  810 F--SNFFSGPIVVHCSAGVGRTGTYIGIDAMLESLEAEGKVDVYGYVVNLRRQRCLMVQVEAQYILIHQALV 879
Cdd:cd14618   159 HvqATKGKGPTLVHCSAGVGRSGTFIALDRLLRQLKEEKVVDVFNTVYILRMHRYLMIQTLSQYIFLHSCIL 230
R-PTPc-typeIIb-1 cd14555
catalytic domain of type IIb (or R2B) subfamily receptor-type tyrosine-protein phosphatases, ...
 676-880 3.05e-64

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: 216.71  E-value: 3.05e-64
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158138488  676 YINASYIDGFKEPRKYIAAQGPRDETVDDFWKMIWEQKATVIVMVTRCEEGNRNKCAEYWPcmeEGTRTFRDVVVTINDH 755
Cdd:cd14555     1 YINANYIDGYHRPNHYIATQGPMQETVYDFWRMVWQENSASIVMVTNLVEVGRVKCSRYWP---DDTEVYGDIKVTLVET 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158138488  756 KRCPDYIIQKLSIAHKKEKATgREVTHIQFTSWPDHGVPEDPHLLLKLRRRVNAFSNFFSGPIVVHCSAGVGRTGTYIGI 835
Cdd:cd14555    78 EPLAEYVVRTFALERRGYHEI-REVRQFHFTGWPDHGVPYHATGLLGFIRRVKASNPPSAGPIVVHCSAGAGRTGCYIVI 156

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*
gi 158138488  836 DAMLESLEAEGKVDVYGYVVNLRRQRCLMVQVEAQYILIHQALVE 880
Cdd:cd14555   157 DIMLDMAEREGVVDIYNCVKELRSRRVNMVQTEEQYIFIHDAILE 201
R-PTPc-Z-1 cd17668
catalytic domain of receptor-type tyrosine-protein phosphatase Z, repeat 1; Receptor-type ...
 676-879 1.18e-63

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: 215.23  E-value: 1.18e-63
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158138488  676 YINASYIDGFKEPRKYIAAQGPRDETVDDFWKMIWEQKATVIVMVTRCEEGNRNKCAEYWPCmeEGTRTFRDVVVTINDH 755
Cdd:cd17668     1 YINANYVDGYNKPKAYIAAQGPLKSTAEDFWRMIWEHNVEVIVMITNLVEKGRRKCDQYWPA--DGSEEYGNFLVTQKSV 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158138488  756 KRCPDYIIQ-------KLSIAHKKEKATGREVTHIQFTSWPDHGVPEDPHLLLKLRRRVNAFSNFFSGPIVVHCSAGVGR 828
Cdd:cd17668    79 QVLAYYTVRnftlrntKIKKGSQKGRPSGRVVTQYHYTQWPDMGVPEYTLPVLTFVRKASYAKRHAVGPVVVHCSAGVGR 158

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|.
gi 158138488  829 TGTYIGIDAMLESLEAEGKVDVYGYVVNLRRQRCLMVQVEAQYILIHQALV 879
Cdd:cd17668   159 TGTYIVLDSMLQQIQHEGTVNIFGFLKHIRSQRNYLVQTEEQYVFIHDALV 209
R-PTPc-Q cd14616
catalytic domain of receptor-type tyrosine-protein phosphatase Q; Receptor-type ...
 650-876 2.34e-62

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: 212.07  E-value: 2.34e-62
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158138488  650 NRYVDILPYDYNRVELSEINGDAGSTYINASYIDGFKEPRKYIAAQGPRDETVDDFWKMIWEQKATVIVMVTRCEEGNRN 729
Cdd:cd14616     1 NRFPNIKPYNNNRVKLIADAGVPGSDYINASYISGYLCPNEFIATQGPLPGTVGDFWRMVWETRAKTIVMLTQCFEKGRI 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158138488  730 KCAEYWPCMEEGTRTFRDVVVTINDHKRCPDYIIQKLSIAHKKEKATgreVTHIQFTSWPDHGVPEDPHLLLKLRRRVNA 809
Cdd:cd14616    81 RCHQYWPEDNKPVTVFGDIVITKLMEDVQIDWTIRDLKIERHGDYMM---VRQCNFTSWPEHGVPESSAPLIHFVKLVRA 157

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 158138488  810 FSNFFSGPIVVHCSAGVGRTGTYIGIDAMLESLEAEGKVDVYGYVVNLRRQRCLMVQVEAQYILIHQ 876
Cdd:cd14616   158 SRAHDNTPMIVHCSAGVGRTGVFIALDHLTQHINDHDFVDIYGLVAELRSERMCMVQNLAQYIFLHQ 224
R-PTPc-K-1 cd14631
catalytic domain of receptor-type tyrosine-protein phosphatase K, repeat 1; Receptor-type ...
 662-880 1.00e-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: 207.18  E-value: 1.00e-60
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158138488  662 RVELSEINGDAGSTYINASYIDGFKEPRKYIAAQGPRDETVDDFWKMIWEQKATVIVMVTRCEEGNRNKCAEYWPcmeEG 741
Cdd:cd14631     1 RVILQPVEDDPSSDYINANYIDGYQRPSHYIATQGPVHETVYDFWRMIWQEQSACIVMVTNLVEVGRVKCYKYWP---DD 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158138488  742 TRTFRDVVVTINDHKRCPDYIIQKLSIAHKKEKATgREVTHIQFTSWPDHGVPEDPHLLLKLRRRVNAFSNFFSGPIVVH 821
Cdd:cd14631    78 TEVYGDFKVTCVEMEPLAEYVVRTFTLERRGYNEI-REVKQFHFTGWPDHGVPYHATGLLSFIRRVKLSNPPSAGPIVVH 156

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 158138488  822 CSAGVGRTGTYIGIDAMLESLEAEGKVDVYGYVVNLRRQRCLMVQVEAQYILIHQALVE 880
Cdd:cd14631   157 CSAGAGRTGCYIVIDIMLDMAEREGVVDIYNCVKALRSRRINMVQTEEQYIFIHDAILE 215
PTPc-N7 cd14612
catalytic domain of tyrosine-protein phosphatase non-receptor type 7; Tyrosine-protein ...
 649-881 1.92e-60

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: 207.38  E-value: 1.92e-60
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158138488  649 KNRYVDILPYDYNRVEL-SEINGDAGSTYINASYIDGFK-EPRKYIAAQGPRDETVDDFWKMIWEQKATVIVMVTRCEEG 726
Cdd:cd14612    18 KDRYKTILPNPQSRVCLrRAGSQEEEGSYINANYIRGYDgKEKAYIATQGPMLNTVSDFWEMVWQEECPIIVMITKLKEK 97

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158138488  727 NRnKCAEYWPCMEEgtrTFRDVVVTINDHKRCPDYIIQKLSIAHKKEKatgREVTHIQFTSWPDHGVPEDPHLLLKL--- 803
Cdd:cd14612    98 KE-KCVHYWPEKEG---TYGRFEIRVQDMKECDGYTIRDLTIQLEEES---RSVKHYWFSSWPDHQTPESAGPLLRLvae 170

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158138488  804 --RRRVNAFSnffSGPIVVHCSAGVGRTGTYIGIDAMLESLEAEGKVDVYGYVVNLRRQRCLMVQVEAQYILIHQALVEY 881
Cdd:cd14612   171 veESRQTAAS---PGPIVVHCSAGIGRTGCFIATSIGCQQLKDTGKVDILGIVCQLRLDRGGMIQTSEQYQFLHHTLALY 247
PTPc-N6 cd14606
catalytic domain of tyrosine-protein phosphatase non-receptor type 6; Tyrosine-protein ...
 639-881 4.05e-60

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: 207.43  E-value: 4.05e-60
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158138488  639 KDARKSQNQNKNRYVDILPYDYNRVELSeiNGDA---GSTYINASYID----GFKEPRK-YIAAQGPRDETVDDFWKMIW 710
Cdd:cd14606    11 LEGQRPENKSKNRYKNILPFDHSRVILQ--GRDSnipGSDYINANYVKnqllGPDENAKtYIASQGCLEATVNDFWQMAW 88

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158138488  711 EQKATVIVMVTRCEEGNRNKCAEYWPCMeEGTRTFRDVVVTINDHKRCPDYIIQ--KLSIAHKKEKAtgREVTHIQFTSW 788
Cdd:cd14606    89 QENSRVIVMTTREVEKGRNKCVPYWPEV-GMQRAYGPYSVTNCGEHDTTEYKLRtlQVSPLDNGELI--REIWHYQYLSW 165

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158138488  789 PDHGVPEDPHLLLKLRRRVNAFSNFF--SGPIVVHCSAGVGRTGTYIGIDAMLESLEAEG---KVDVYGYVVNLRRQRCL 863
Cdd:cd14606   166 PDHGVPSEPGGVLSFLDQINQRQESLphAGPIIVHCSAGIGRTGTIIVIDMLMENISTKGldcDIDIQKTIQMVRAQRSG 245

                         250
                  ....*....|....*...
gi 158138488  864 MVQVEAQYILIHQALVEY 881
Cdd:cd14606   246 MVQTEAQYKFIYVAIAQF 263
R-PTP-S-2 cd14627
PTP-like domain of receptor-type tyrosine-protein phosphatase S, repeat 2; Receptor-type ...
 646-881 8.80e-60

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: 207.28  E-value: 8.80e-60
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158138488  646 NQNKNRYVDILPYDYNRVELSEINGDAGSTYINASYIDGFKEPRKYIAAQGPRDETVDDFWKMIWEQKATVIVMVTRCEE 725
Cdd:cd14627    53 NKFKNRLVNIMPYETTRVCLQPIRGVEGSDYINASFIDGYRQQKAYIATQGPLAETTEDFWRMLWENNSTIVVMLTKLRE 132

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158138488  726 GNRNKCAEYWPCmeEGTRTFRDVVVTINDHKRCPDYIIQKLSIAHKKEkATGREVTHIQFTSWPDHGVPEDPHLLLKLRR 805
Cdd:cd14627   133 MGREKCHQYWPA--ERSARYQYFVVDPMAEYNMPQYILREFKVTDARD-GQSRTVRQFQFTDWPEQGVPKSGEGFIDFIG 209

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 158138488  806 RVNAFSNFF--SGPIVVHCSAGVGRTGTYIGIDAMLESLEAEGKVDVYGYVVNLRRQRCLMVQVEAQYILIHQALVEY 881
Cdd:cd14627   210 QVHKTKEQFgqDGPISVHCSAGVGRTGVFITLSIVLERMRYEGVVDIFQTVKMLRTQRPAMVQTEDEYQFCYQAALEY 287
R-PTP-D-2 cd14628
PTP-like domain of receptor-type tyrosine-protein phosphatase D, repeat 2; Receptor-type ...
 646-881 1.34e-59

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


Pssm-ID: 350476 [Multi-domain]  Cd Length: 292  Bit Score: 206.89  E-value: 1.34e-59
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158138488  646 NQNKNRYVDILPYDYNRVELSEINGDAGSTYINASYIDGFKEPRKYIAAQGPRDETVDDFWKMIWEQKATVIVMVTRCEE 725
Cdd:cd14628    52 NKFKNRLVNIMPYESTRVCLQPIRGVEGSDYINASFIDGYRQQKAYIATQGPLAETTEDFWRMLWEHNSTIVVMLTKLRE 131

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158138488  726 GNRNKCAEYWPCmeEGTRTFRDVVVTINDHKRCPDYIIQKLSIAHKKEkATGREVTHIQFTSWPDHGVPEDPHLLLKLRR 805
Cdd:cd14628   132 MGREKCHQYWPA--ERSARYQYFVVDPMAEYNMPQYILREFKVTDARD-GQSRTVRQFQFTDWPEQGVPKSGEGFIDFIG 208

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 158138488  806 RVNAFSNFF--SGPIVVHCSAGVGRTGTYIGIDAMLESLEAEGKVDVYGYVVNLRRQRCLMVQVEAQYILIHQALVEY 881
Cdd:cd14628   209 QVHKTKEQFgqDGPISVHCSAGVGRTGVFITLSIVLERMRYEGVVDIFQTVKMLRTQRPAMVQTEDQYQFCYRAALEY 286
R-PTP-F-2 cd14629
PTP-like domain of receptor-type tyrosine-protein phosphatase F, repeat 2; Receptor-type ...
 646-881 1.55e-59

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: 206.50  E-value: 1.55e-59
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158138488  646 NQNKNRYVDILPYDYNRVELSEINGDAGSTYINASYIDGFKEPRKYIAAQGPRDETVDDFWKMIWEQKATVIVMVTRCEE 725
Cdd:cd14629    53 NKFKNRLVNIMPYELTRVCLQPIRGVEGSDYINASFIDGYRQQKAYIATQGPLAETTEDFWRMLWEHNSTIVVMLTKLRE 132

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158138488  726 GNRNKCAEYWPCmeEGTRTFRDVVVTINDHKRCPDYIIQKLSIAHKKEkATGREVTHIQFTSWPDHGVPEDPHLLLKLRR 805
Cdd:cd14629   133 MGREKCHQYWPA--ERSARYQYFVVDPMAEYNMPQYILREFKVTDARD-GQSRTIRQFQFTDWPEQGVPKTGEGFIDFIG 209

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 158138488  806 RVNAFSNFF--SGPIVVHCSAGVGRTGTYIGIDAMLESLEAEGKVDVYGYVVNLRRQRCLMVQVEAQYILIHQALVEY 881
Cdd:cd14629   210 QVHKTKEQFgqDGPITVHCSAGVGRTGVFITLSIVLERMRYEGVVDMFQTVKTLRTQRPAMVQTEDQYQLCYRAALEY 287
PTPc-N20_13 cd14538
catalytic domain of tyrosine-protein phosphatase non-receptor type 20 and type 13; ...
 676-880 3.20e-59

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


Pssm-ID: 350386 [Multi-domain]  Cd Length: 207  Bit Score: 202.60  E-value: 3.20e-59
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158138488  676 YINASYI--DGFKEPRKYIAAQGPRDETVDDFWKMIWEQKATVIVMVTRCEEGNRNKCAEYWP------CMEEGTRTFRD 747
Cdd:cd14538     1 YINASHIriPVGGDTYHYIACQGPLPNTTGDFWQMVWEQKSEVIAMVTQDVEGGKVKCHRYWPdslnkpLICGGRLEVSL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158138488  748 VVVTINDhkrcpDYIIQKLSIAHKkEKATGREVTHIQFTSWPDHGVPEDPHLLLKLRRRVNAFSNffSGPIVVHCSAGVG 827
Cdd:cd14538    81 EKYQSLQ-----DFVIRRISLRDK-ETGEVHHITHLNFTTWPDHGTPQSADPLLRFIRYMRRIHN--SGPIVVHCSAGIG 152

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 158138488  828 RTGTYIGIDAMLESLEAEGKVDVYGYVVNLRRQRCLMVQVEAQYILIHQALVE 880
Cdd:cd14538   153 RTGVLITIDVALGLIERDLPFDIQDIVKDLREQRQGMIQTKDQYIFCYKACLE 205
R-PTPc-U-1 cd14632
catalytic domain of receptor-type tyrosine-protein phosphatase U, repeat 1; Receptor-type ...
 676-880 7.20e-59

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: 201.43  E-value: 7.20e-59
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158138488  676 YINASYIDGFKEPRKYIAAQGPRDETVDDFWKMIWEQKATVIVMVTRCEEGNRNKCAEYWPcmeEGTRTFRDVVVTINDH 755
Cdd:cd14632     1 YINANYIDGYHRSNHFIATQGPKQEMVYDFWRMVWQEHCSSIVMITKLVEVGRVKCSKYWP---DDSDTYGDIKITLLKT 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158138488  756 KRCPDYIIQKLSIAHKKEKATgREVTHIQFTSWPDHGVPEDPHLLLKLRRRVNAFSNFFSGPIVVHCSAGVGRTGTYIGI 835
Cdd:cd14632    78 ETLAEYSVRTFALERRGYSAR-HEVKQFHFTSWPEHGVPYHATGLLAFIRRVKASTPPDAGPVVVHCSAGAGRTGCYIVL 156

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*
gi 158138488  836 DAMLESLEAEGKVDVYGYVVNLRRQRCLMVQVEAQYILIHQALVE 880
Cdd:cd14632   157 DVMLDMAECEGVVDIYNCVKTLCSRRINMIQTEEQYIFIHDAILE 201
R-PTP-C-2 cd14558
PTP-like domain of receptor-type tyrosine-protein phosphatase C, repeat 2; Receptor-type ...
 676-871 8.62e-58

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: 198.00  E-value: 8.62e-58
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158138488  676 YINASYIDGFKEPRKYIAAQGPRDETVDDFWKMIWEQKATVIVMVTRCEEGNRNKCAEYWPcmeEGTRTFRDVVVTINDH 755
Cdd:cd14558     1 YINASFIDGYWGPKSLIATQGPLPDTIADFWQMIFQKKVKVIVMLTELKEGDQEQCAQYWG---DEKKTYGDIEVELKDT 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158138488  756 KRCPDYIIQKLSIAHKKEKATgREVTHIQFTSWPDHGVPEDPHLLLKLRRRV------NAFSNFFSGPIVVHCSAGVGRT 829
Cdd:cd14558    78 EKSPTYTVRVFEITHLKRKDS-RTVYQYQYHKWKGEELPEKPKDLVDMIKSIkqklpyKNSKHGRSVPIVVHCSDGSSRT 156

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|..
gi 158138488  830 GTYIGIDAMLESLEAEGKVDVYGYVVNLRRQRCLMVQVEAQY 871
Cdd:cd14558   157 GIFCALWNLLESAETEKVVDVFQVVKALRKQRPGMVSTLEQY 198
PTPc-N13 cd14597
catalytic domain of tyrosine-protein phosphatase non-receptor type 13; Tyrosine-protein ...
 645-879 9.82e-58

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: 199.29  E-value: 9.82e-58
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158138488  645 QNQNKNRYVDILPYDYNRVELSEINGdagstYINASYID---GfKEPRKYIAAQGPRDETVDDFWKMIWEQKATVIVMVT 721
Cdd:cd14597     2 ENRKKNRYKNILPYDTTRVPLGDEGG-----YINASFIKmpvG-DEEFVYIACQGPLPTTVADFWQMVWEQKSTVIAMMT 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158138488  722 RCEEGNRNKCAEYWP-CMEEGTRTFRDVVVTINDHKRCPDYIIQKLSIaHKKEKATGREVTHIQFTSWPDHGVPEDPHLL 800
Cdd:cd14597    76 QEVEGGKIKCQRYWPeILGKTTMVDNRLQLTLVRMQQLKNFVIRVLEL-EDIQTREVRHITHLNFTAWPDHDTPSQPEQL 154

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158138488  801 LKL---RRRVNAfsnffSGPIVVHCSAGVGRTGTYIGIDAMLESLEAEGKVDVYGYVVNLRRQRCLMVQVEAQYILIHQA 877
Cdd:cd14597   155 LTFisyMRHIHK-----SGPIITHCSAGIGRSGTLICIDVVLGLISKDLDFDISDIVRTMRLQRHGMVQTEDQYIFCYQV 229


                  ..
gi 158138488  878 LV 879
Cdd:cd14597   230 IL 231
PTPc-N11 cd14605
catalytic domain of tyrosine-protein phosphatase non-receptor type 11; Tyrosine-protein ...
 645-881 8.76e-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: 197.16  E-value: 8.76e-57
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158138488  645 QNQNKNRYVDILPYDYNRVELSEinGDA---GSTYINASYI--------DGFKEPRKYIAAQGPRDETVDDFWKMIWEQK 713
Cdd:cd14605     1 ENKNKNRYKNILPFDHTRVVLHD--GDPnepVSDYINANIImpefetkcNNSKPKKSYIATQGCLQNTVNDFWRMVFQEN 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158138488  714 ATVIVMVTRCEEGNRNKCAEYWP----CMEEGTRTFRDVvvtindhKRCP--DYIIQKLSIAHKKEKATGREVTHIQFTS 787
Cdd:cd14605    79 SRVIVMTTKEVERGKSKCVKYWPdeyaLKEYGVMRVRNV-------KESAahDYILRELKLSKVGQGNTERTVWQYHFRT 151

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158138488  788 WPDHGVPEDPHLLLKLRRRVNAFSNFFS--GPIVVHCSAGVGRTGTYIGIDAMLESLEAEG---KVDVYGYVVNLRRQRC 862
Cdd:cd14605   152 WPDHGVPSDPGGVLDFLEEVHHKQESIMdaGPVVVHCSAGIGRTGTFIVIDILIDIIREKGvdcDIDVPKTIQMVRSQRS 231

                         250
                  ....*....|....*....
gi 158138488  863 LMVQVEAQYILIHQALVEY 881
Cdd:cd14605   232 GMVQTEAQYRFIYMAVQHY 250
PTPc-N21_14 cd14540
catalytic domain of tyrosine-protein phosphatase non-receptor type 21 and type 14; ...
 676-881 1.14e-56

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: 195.75  E-value: 1.14e-56
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158138488  676 YINASYID---GFKEpRKYIAAQGPRDETVDDFWKMIWEQKATVIVMVTRCEEGNRNKCAEYWPCM--EEGTRTFRDVVV 750
Cdd:cd14540     1 YINASHITatvGGKQ-RFYIAAQGPLQNTVGDFWQMVWEQGVYLVVMVTAEEEGGREKCFRYWPTLggEHDALTFGEYKV 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158138488  751 TINDHKRCPDYIIQKLSIAHKKEKaTGREVTHIQFTSWPDHGVPEDPHLLL-------KLRRRVNAFS--NFFSGPIVVH 821
Cdd:cd14540    80 STKFSVSSGCYTTTGLRVKHTLSG-QSRTVWHLQYTDWPDHGCPEDVSGFLdfleeinSVRRHTNQDVagHNRNPPTLVH 158

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 158138488  822 CSAGVGRTGTYIGIDAMLESLEAEGKVDVYGYVVNLRRQRCLMVQVEAQYILIHQALVEY 881
Cdd:cd14540   159 CSAGVGRTGVVILADLMLYCLDHNEELDIPRVLALLRHQRMLLVQTLAQYKFVYNVLIQY 218
PTPc-N18 cd14603
catalytic domain of tyrosine-protein phosphatase non-receptor type 18; Tyrosine-protein ...
 645-880 1.90e-56

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: 196.97  E-value: 1.90e-56
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158138488  645 QNQNKNRYVDILPYDYNRVELSEINGDAGSTYINASYIDGFKEPRKYIAAQGPRDETVDDFWKMIWEQKATVIVMVTRCE 724
Cdd:cd14603    29 ENVKKNRYKDILPYDQTRVILSLLQEEGHSDYINANFIKGVDGSRAYIATQGPLSHTVLDFWRMIWQYGVKVILMACREI 108

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158138488  725 EGNRNKCAEYWPCMEEGTRTFRDVVVTINDHKRCPDYIIQKLSIAHKKEKatgREVTHIQFTSWPDHGVPEDPHLLLKLR 804
Cdd:cd14603   109 EMGKKKCERYWAQEQEPLQTGPFTITLVKEKRLNEEVILRTLKVTFQKES---RSVSHFQYMAWPDHGIPDSPDCMLAMI 185

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 158138488  805 RRVNAFSNFFSGPIVVHCSAGVGRTGTYIGID---AMLESLEAEGKVDVYGYVVNLRRQRCLMVQVEAQYILIHQALVE 880
Cdd:cd14603   186 ELARRLQGSGPEPLCVHCSAGCGRTGVICTVDyvrQLLLTQRIPPDFSIFDVVLEMRKQRPAAVQTEEQYEFLYHTVAQ 264
PTPc-N1_2 cd14545
catalytic domain of tyrosine-protein phosphatase non-receptor type 1 and type 2; ...
 649-870 9.45e-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: 193.38  E-value: 9.45e-56
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158138488  649 KNRYVDILPYDYNRVELSEINGDagSTYINASYIDGFKEPRKYIAAQGPRDETVDDFWKMIWEQKATVIVMVTRCEEGNR 728
Cdd:cd14545     1 LNRYRDRDPYDHDRSRVKLKQGD--NDYINASLVEVEEAKRSYILTQGPLPNTSGHFWQMVWEQNSKAVIMLNKLMEKGQ 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158138488  729 NKCAEYWPCMEEGTRTFRDVV--VTINDHKRCPDYIIQKLSIAHKKEKATgREVTHIQFTSWPDHGVPEDP----HLLLK 802
Cdd:cd14545    79 IKCAQYWPQGEGNAMIFEDTGlkVTLLSEEDKSYYTVRTLELENLKTQET-REVLHFHYTTWPDFGVPESPaaflNFLQK 157

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158138488  803 LRRRVNAFSNFfsGPIVVHCSAGVGRTGTYIGIDAMLESLEAEG--KVDVYGYVVNLRRQRCLMVQVEAQ 870
Cdd:cd14545   158 VRESGSLSSDV--GPPVVHCSAGIGRSGTFCLVDTCLVLIEKGNpsSVDVKKVLLEMRKYRMGLIQTPDQ 225
PTPc-N14 cd14599
catalytic domain of tyrosine-protein phosphatase non-receptor type 14; Tyrosine-protein ...
 609-881 1.55e-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: 194.83  E-value: 1.55e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158138488  609 ETYKRKIaDEGRLFlAEFQSIPRVFSKFPIKDARKSQNQNKNRYVDILPYDYNRVELSEiNGDAGSTYINASYIDGF--K 686
Cdd:cd14599     3 KTLERKL-EEGMVF-TEYEQIPKKKADGVFTTATLPENAERNRIREVVPYEENRVELVP-TKENNTGYINASHIKVTvgG 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158138488  687 EPRKYIAAQGPRDETVDDFWKMIWEQKATVIVMVTRCEEGNRNKCAEYWPCM--EEGTRTFRDVVVTINDHKRCPDYIIQ 764
Cdd:cd14599    80 EEWHYIATQGPLPHTCHDFWQMVWEQGVNVIAMVTAEEEGGRSKSHRYWPKLgsKHSSATYGKFKVTTKFRTDSGCYATT 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158138488  765 KLSIAHKkekATGREVT--HIQFTSWPDHGVPEDPHLLLK-------LRRRVNAF---SNFFSGPIVVHCSAGVGRTGTY 832
Cdd:cd14599   160 GLKVKHL---LSGQERTvwHLQYTDWPDHGCPEEVQGFLSyleeiqsVRRHTNSMldsTKNCNPPIVVHCSAGVGRTGVV 236

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*....
gi 158138488  833 IGIDAMLESLEAEGKVDVYGYVVNLRRQRCLMVQVEAQYILIHQALVEY 881
Cdd:cd14599   237 ILTELMIGCLEHNEKVEVPVMLRHLREQRMFMIQTIAQYKFVYQVLIQF 285
R-PTPc-A-E-2 cd14552
catalytic domain of receptor-type tyrosine-protein phosphatase A and E, repeat 2; ...
 676-879 1.83e-55

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: 191.33  E-value: 1.83e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158138488  676 YINASYIDGFKEPRKYIAAQGPRDETVDDFWKMIWEQKATVIVMVTRCEEGNRNKCAEYWPcmEEGTRTFRDVVVTINDH 755
Cdd:cd14552     1 YINASFIDGYRQKDAYIATQGPLDHTVEDFWRMIWEWKSCSIVMLTEIKERSQNKCAQYWP--EDGSVSSGDITVELKDQ 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158138488  756 KRCPDYIIQKLSIAHKKEKATgREVTHIQFTSWPDHGVPEDP----HLLLKLRRRVNAFSNffsGPIVVHCSAGVGRTGT 831
Cdd:cd14552    79 TDYEDYTLRDFLVTKGKGGST-RTVRQFHFHGWPEVGIPDNGkgmiDLIAAVQKQQQQSGN---HPITVHCSAGAGRTGT 154

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*...
gi 158138488  832 YIGIDAMLESLEAEGKVDVYGYVVNLRRQRCLMVQVEAQYILIHQALV 879
Cdd:cd14552   155 FCALSTVLERVKAEGVLDVFQVVKSLRLQRPHMVQTLEQYEFCYKVVQ 202
PTPc-N22_18_12 cd14542
catalytic domain of tyrosine-protein phosphatase non-receptor type 22, type 18 and type 12; ...
 676-876 1.99e-55

catalytic domain of tyrosine-protein phosphatase non-receptor type 22, type 18 and type 12; Tyrosine-protein phosphatase non-receptor type 22 (PTPN22), type 18 (PTPN18) and type 12 (PTPN12) belong to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. PTPN22 is expressed in hematopoietic cells and it functions as a key regulator of immune homeostasis by inhibiting T-cell receptor signaling through the direct dephosphorylation of Src family kinases (Lck and Fyn), ITAMs of the TCRz/CD3 complex, and other signaling molecules. TPN18 regulates HER2-mediated cellular functions through defining both its phosphorylation and ubiquitination states. PTPN12 is characterized as a tumor suppressor and a pivotal regulator of EGFR/HER2 signaling.


Pssm-ID: 350390 [Multi-domain]  Cd Length: 202  Bit Score: 191.48  E-value: 1.99e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158138488  676 YINASYIDGFKEPRKYIAAQGPRDETVDDFWKMIWEQKATVIVMVTRCEEGNRNKCAEYWPCMEEGTRTFRDVVVTINDH 755
Cdd:cd14542     1 YINANFIKGVSGSKAYIATQGPLPNTVLDFWRMIWEYNVQVIVMACREFEMGKKKCERYWPEEGEEQLQFGPFKISLEKE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158138488  756 KR-CPDYIIQKLSIAHKKEKatgREVTHIQFTSWPDHGVPEDPHLLLKLRRRVNAFSNFFSGPIVVHCSAGVGRTGTYIG 834
Cdd:cd14542    81 KRvGPDFLIRTLKVTFQKES---RTVYQFHYTAWPDHGVPSSVDPILDLVRLVRDYQGSEDVPICVHCSAGCGRTGTICA 157

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*
gi 158138488  835 IDAMLESLEAEGKVD---VYGYVVNLRRQRCLMVQVEAQYILIHQ 876
Cdd:cd14542   158 IDYVWNLLKTGKIPEefsLFDLVREMRKQRPAMVQTKEQYELVYR 202
R-PTPc-A-2 cd14623
catalytic domain of receptor-type tyrosine-protein phosphatase A, repeat 2; Receptor-type ...
 651-880 3.74e-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: 3.74e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158138488  651 RYVDILPYDYNRVELSEINGDAGSTYINASYIDGFKEPRKYIAAQGPRDETVDDFWKMIWEQKATVIVMVTRCEEGNRNK 730
Cdd:cd14623     1 RVLQIIPYEFNRVIIPVKRGEENTDYVNASFIDGYRQKDSYIASQGPLQHTIEDFWRMIWEWKSCSIVMLTELEERGQEK 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158138488  731 CAEYWPcmEEGTRTFRDVVVTINDHKRCPDYIIQKLSIAHKKEKATgREVTHIQFTSWPDHGVPEDP----HLLLKLRRR 806
Cdd:cd14623    81 CAQYWP--SDGSVSYGDITIELKKEEECESYTVRDLLVTNTRENKS-RQIRQFHFHGWPEVGIPSDGkgmiNIIAAVQKQ 157

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 158138488  807 VNAFSNFfsgPIVVHCSAGVGRTGTYIGIDAMLESLEAEGKVDVYGYVVNLRRQRCLMVQVEAQYILIHQALVE 880
Cdd:cd14623   158 QQQSGNH---PITVHCSAGAGRTGTFCALSTVLERVKAEGILDVFQTVKSLRLQRPHMVQTLEQYEFCYKVVQE 228
PTPc-N12 cd14604
catalytic domain of tyrosine-protein phosphatase non-receptor type 12; Tyrosine-protein ...
 622-880 6.74e-55

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: 193.61  E-value: 6.74e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158138488  622 FLAEFQSIPRVFSKF------PIKDARKSQNQNKNRYVDILPYDYNRVELSEINGDAGSTYINASYIDGFKEPRKYIAAQ 695
Cdd:cd14604    27 FASDFMRLRRLSTKYrtekiyPTATGEKEENVKKNRYKDILPFDHSRVKLTLKTSSQDSDYINANFIKGVYGPKAYIATQ 106

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158138488  696 GPRDETVDDFWKMIWEQKATVIVMVTRCEEGNRNKCAEYWPCMEEGTRTFRDVVVTINDHKRCPDYIIQKLSIAHKKEKa 775
Cdd:cd14604   107 GPLANTVIDFWRMIWEYNVAIIVMACREFEMGRKKCERYWPLYGEEPMTFGPFRISCEAEQARTDYFIRTLLLEFQNET- 185

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158138488  776 tgREVTHIQFTSWPDHGVPEDPHLLLKLRRRVNAFSNFFSGPIVVHCSAGVGRTGTYIGIDAMLESLEAeGKV----DVY 851
Cdd:cd14604   186 --RRLYQFHYVNWPDHDVPSSFDSILDMISLMRKYQEHEDVPICIHCSAGCGRTGAICAIDYTWNLLKA-GKIpeefNVF 262

                         250       260
                  ....*....|....*....|....*....
gi 158138488  852 GYVVNLRRQRCLMVQVEAQYILIHQALVE 880
Cdd:cd14604   263 NLIQEMRTQRHSAVQTKEQYELVHRAIAQ 291
R-PTPc-A-E-2 cd14552
catalytic domain of receptor-type tyrosine-protein phosphatase A and E, repeat 2; ...
 986-1193 2.11e-54

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: 188.63  E-value: 2.11e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158138488  986 YINASFVMSYWKPEMMIAAQGPLKETIGDFWQMIFQRKVKVIVMLTELMSGDQEVCAQYW-GEGKQTYGDMEVMLKDTNK 1064
Cdd:cd14552     1 YINASFIDGYRQKDAYIATQGPLDHTVEDFWRMIWEWKSCSIVMLTEIKERSQNKCAQYWpEDGSVSSGDITVELKDQTD 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158138488 1065 SSAYILRAFELRHSKRKEPRTVYQYQCTTWKGEELPAEPKDLVTLIQNIKQKLPKSGSEgmkyhkhaSILVHCRDGSQQT 1144
Cdd:cd14552    81 YEDYTLRDFLVTKGKGGSTRTVRQFHFHGWPEVGIPDNGKGMIDLIAAVQKQQQQSGNH--------PITVHCSAGAGRT 152

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*....
gi 158138488 1145 GLFCALFNLLESAETEDVVDVFQVVKSLRKARPGMVGSFEQYQFLYDIM 1193
Cdd:cd14552   153 GTFCALSTVLERVKAEGVLDVFQVVKSLRLQRPHMVQTLEQYEFCYKVV 201
PTPc-N3_4 cd14541
catalytic domain of tyrosine-protein phosphatase non-receptor type 21 and type 14; ...
 676-871 2.24e-53

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: 186.00  E-value: 2.24e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158138488  676 YINASYID----GFKEPRKYIAAQGPRDETVDDFWKMIWEQKATVIVMVTRCEEGNRNKCAEYWPCMEEgTRTFRDVVVT 751
Cdd:cd14541     2 YINANYVNmeipGSGIVNRYIAAQGPLPNTCADFWQMVWEQKSTLIVMLTTLVERGRVKCHQYWPDLGE-TMQFGNLQIT 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158138488  752 INDHKRCPDYIIQKLSIAHKKEKATgREVTHIQFTSWPDHGVPEDPHLLLKLRRRVNAFSNFFSGPIVVHCSAGVGRTGT 831
Cdd:cd14541    81 CVSEEVTPSFAFREFILTNTNTGEE-RHITQMQYLAWPDHGVPDDSSDFLDFVKRVRQNRVGMVEPTVVHCSAGIGRTGV 159

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|
gi 158138488  832 YIGIDAMLESLEAEGKVDVYGYVVNLRRQRCLMVQVEAQY 871
Cdd:cd14541   160 LITMETAMCLIEANEPVYPLDIVRTMRDQRAMLIQTPSQY 199
R-PTPc-R cd14611
catalytic domain of receptor-type tyrosine-protein phosphatase R; Receptor-type ...
 649-876 4.36e-53

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: 185.51  E-value: 4.36e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158138488  649 KNRYVDILPYDYNRVELSEIN-GDAGSTYINASYIDGFK-EPRKYIAAQGPRDETVDDFWKMIWEQKATVIVMVTRCEEG 726
Cdd:cd14611     2 KNRYKTILPNPHSRVCLKPKNsNDSLSTYINANYIRGYGgKEKAFIATQGPMINTVNDFWQMVWQEDSPVIVMITKLKEK 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158138488  727 NRnKCAEYWPcmeEGTRTFRDVVVTINDHKRCPDYIIQKLSIahkKEKATGREVTHIQFTSWPDHGVPEDPHLLLKLRRR 806
Cdd:cd14611    82 NE-KCVLYWP---EKRGIYGKVEVLVNSVKECDNYTIRNLTL---KQGSQSRSVKHYWYTSWPDHKTPDSAQPLLQLMLD 154

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 158138488  807 V--NAFSNFFSGPIVVHCSAGVGRTGTYIGIDAMLESLEAEGKVDVYGYVVNLRRQRCLMVQVEAQYILIHQ 876
Cdd:cd14611   155 VeeDRLASPGRGPVVVHCSAGIGRTGCFIATTIGCQQLKEEGVVDVLSIVCQLRVDRGGMVQTSEQYEFVHH 226
PTPc-N22 cd14602
catalytic domain of tyrosine-protein phosphatase non-receptor type 22; Tyrosine-protein ...
 649-880 2.04e-52

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: 183.89  E-value: 2.04e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158138488  649 KNRYVDILPYDYNRVELSEINGDAGSTYINASYIDGFKEPRKYIAAQGPRDETVDDFWKMIWEQKATVIVMVTRCEEGNR 728
Cdd:cd14602     1 KNRYKDILPYDHSRVELSLITSDEDSDYINANFIKGVYGPRAYIATQGPLSTTLLDFWRMIWEYSVLIIVMACMEFEMGK 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158138488  729 NKCAEYWPCMEEGTRTFRDVVVTINDHKRCPDYIIQKLSIAHKKEKatgREVTHIQFTSWPDHGVPEDPHLLLKLRRRVN 808
Cdd:cd14602    81 KKCERYWAEPGEMQLEFGPFSVTCEAEKRKSDYIIRTLKVKFNSET---RTIYQFHYKNWPDHDVPSSIDPILELIWDVR 157

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 158138488  809 AFSNFFSGPIVVHCSAGVGRTGTYIGIDAMLESLEaEGKV----DVYGYVVNLRRQRCLMVQVEAQYILIHQALVE 880
Cdd:cd14602   158 CYQEDDSVPICIHCSAGCGRTGVICAIDYTWMLLK-DGIIpenfSVFSLIQEMRTQRPSLVQTKEQYELVYNAVIE 232
PTPc-N5 cd14613
catalytic domain of tyrosine-protein phosphatase non-receptor type 5; Tyrosine-protein ...
 649-881 3.18e-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: 3.18e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158138488  649 KNRYVDILPYDYNRVEL-SEINGDAGSTYINASYIDGF-KEPRKYIAAQGPRDETVDDFWKMIWEQKATVIVMVTRCEEG 726
Cdd:cd14613    28 KNRYKTILPNPHSRVCLtSPDQDDPLSSYINANYIRGYgGEEKVYIATQGPTVNTVGDFWRMVWQERSPIIVMITNIEEM 107

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158138488  727 NRnKCAEYWPcmeEGTRTFRDVVVTINDHKRCPDYIIQKLSIAHKKEKatgREVTHIQFTSWPDHGVPEDPHLLLKLRRR 806
Cdd:cd14613   108 NE-KCTEYWP---EEQVTYEGIEITVKQVIHADDYRLRLITLKSGGEE---RGLKHYWYTSWPDQKTPDNAPPLLQLVQE 180

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 158138488  807 VNAF---SNFFSGPIVVHCSAGVGRTGTYIGIDAMLESLEAEGKVDVYGYVVNLRRQRCLMVQVEAQYILIHQALVEY 881
Cdd:cd14613   181 VEEArqqAEPNCGPVIVHCSAGIGRTGCFIATSICCKQLRNEGVVDILRTTCQLRLDRGGMIQTCEQYQFVHHVLSLY 258
R-PTP-N2 cd14610
PTP-like domain of receptor-type tyrosine-protein phosphatase N2; Receptor-type ...
 641-880 6.04e-52

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: 184.49  E-value: 6.04e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158138488  641 ARKSQNQNKNRYVDILPYDYNRVELSEINGDAGSTYINASYIDGfKEPRK--YIAAQGPRDETVDDFWKMIWEQKATVIV 718
Cdd:cd14610    39 AQREENVQKNRSLAVLPYDHSRIILKAENSHSHSDYINASPIMD-HDPRNpaYIATQGPLPATVADFWQMVWESGCVVIV 117

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158138488  719 MVTRCEEGNRNKCAEYWPcmEEGTRTFRDVVVT-INDHKRCPDYIIQKLSIAHKKEKATgREVTHIQFTSWPDHGVPEDP 797
Cdd:cd14610   118 MLTPLAENGVKQCYHYWP--DEGSNLYHIYEVNlVSEHIWCEDFLVRSFYLKNLQTNET-RTVTQFHFLSWNDQGVPAST 194

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158138488  798 HLLLKLRRRVNAFSNFFSGPIVVHCSAGVGRTGTYIGIDAMLESLEAEGK-VDVYGYVVNLRRQRCLMVQVEAQYILIHQ 876
Cdd:cd14610   195 RSLLDFRRKVNKCYRGRSCPIIVHCSDGAGRSGTYILIDMVLNKMAKGAKeIDIAATLEHLRDQRPGMVQTKEQFEFALT 274


                  ....
gi 158138488  877 ALVE 880
Cdd:cd14610   275 AVAE 278
PTPc-N1 cd14608
catalytic domain of tyrosine-protein phosphatase non-receptor type 1; Tyrosine-protein ...
 626-889 7.62e-52

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: 184.07  E-value: 7.62e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158138488  626 FQSIPRVFSKFPIKDARKSQNQNKNRYVDILPYDYNRVELSEINGDagstYINASYIDGFKEPRKYIAAQGPRDETVDDF 705
Cdd:cd14608     5 YQDIRHEASDFPCRVAKLPKNKNRNRYRDVSPFDHSRIKLHQEDND----YINASLIKMEEAQRSYILTQGPLPNTCGHF 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158138488  706 WKMIWEQKATVIVMVTRCEEGNRNKCAEYWPCMEEGTRTFRD--VVVTINDHKRCPDYIIQKLSIAHKKEKATgREVTHI 783
Cdd:cd14608    81 WEMVWEQKSRGVVMLNRVMEKGSLKCAQYWPQKEEKEMIFEDtnLKLTLISEDIKSYYTVRQLELENLTTQET-REILHF 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158138488  784 QFTSWPDHGVPEDP----HLLLKLRRrvNAFSNFFSGPIVVHCSAGVGRTGTYIGIDA---MLESLEAEGKVDVYGYVVN 856
Cdd:cd14608   160 HYTTWPDFGVPESPasflNFLFKVRE--SGSLSPEHGPVVVHCSAGIGRSGTFCLADTcllLMDKRKDPSSVDIKKVLLE 237

                         250       260       270
                  ....*....|....*....|....*....|....*
gi 158138488  857 LRRQRCLMVQVEAQYILIHQALVEYNQF--GETEV 889
Cdd:cd14608   238 MRKFRMGLIQTADQLRFSYLAVIEGAKFimGDSSV 272
R-PTP-N-N2 cd14546
PTP-like domain of receptor-type tyrosine-protein phosphatase-like N and N2; Receptor-type ...
 676-890 1.33e-51

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


Pssm-ID: 350394 [Multi-domain]  Cd Length: 208  Bit Score: 180.72  E-value: 1.33e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158138488  676 YINASYIDGfKEPRK--YIAAQGPRDETVDDFWKMIWEQKATVIVMVTRCEEGNRNKCAEYWPcmEEGTRTFRDVVVT-I 752
Cdd:cd14546     1 YINASTIYD-HDPRNpaYIATQGPLPHTIADFWQMIWEQGCVVIVMLTRLQENGVKQCARYWP--EEGSEVYHIYEVHlV 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158138488  753 NDHKRCPDYIIQKLSIAHKKEKATgREVTHIQFTSWPDHGVPEDPHLLLKLRRRVNAFSNFFSGPIVVHCSAGVGRTGTY 832
Cdd:cd14546    78 SEHIWCDDYLVRSFYLKNLQTSET-RTVTQFHFLSWPDEGIPASAKPLLEFRRKVNKSYRGRSCPIVVHCSDGAGRTGTY 156

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 158138488  833 IGIDAMLESLEAEGK-VDVYGYVVNLRRQRCLMVQVEAQYILIHQALVEynqfgetEVN 890
Cdd:cd14546   157 ILIDMVLNRMAKGAKeIDIAATLEHLRDQRPGMVKTKDQFEFVLTAVAE-------EVN 208
R-PTPc-A-2 cd14623
catalytic domain of receptor-type tyrosine-protein phosphatase A, repeat 2; Receptor-type ...
 942-1193 2.86e-51

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: 180.63  E-value: 2.86e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158138488  942 RSSNVVPYDFNRV--PLKHELEmskeseaesdessdedsdseeTSKYINASFVMSYWKPEMMIAAQGPLKETIGDFWQMI 1019
Cdd:cd14623     1 RVLQIIPYEFNRViiPVKRGEE---------------------NTDYVNASFIDGYRQKDSYIASQGPLQHTIEDFWRMI 59

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158138488 1020 FQRKVKVIVMLTELMSGDQEVCAQYW-GEGKQTYGDMEVMLKDTNKSSAYILRAFELRHSKRKEPRTVYQYQCTTWKGEE 1098
Cdd:cd14623    60 WEWKSCSIVMLTELEERGQEKCAQYWpSDGSVSYGDITIELKKEEECESYTVRDLLVTNTRENKSRQIRQFHFHGWPEVG 139

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158138488 1099 LPAEPKDLVTLIQNIKQKLPKSGSEgmkyhkhaSILVHCRDGSQQTGLFCALFNLLESAETEDVVDVFQVVKSLRKARPG 1178
Cdd:cd14623   140 IPSDGKGMINIIAAVQKQQQQSGNH--------PITVHCSAGAGRTGTFCALSTVLERVKAEGILDVFQTVKSLRLQRPH 211

                         250
                  ....*....|....*
gi 158138488 1179 MVGSFEQYQFLYDIM 1193
Cdd:cd14623   212 MVQTLEQYEFCYKVV 226
R3-PTPc cd14548
catalytic domain of R3 subfamily receptor-type tyrosine-protein phosphatases and similar ...
 942-1190 3.41e-51

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: 179.86  E-value: 3.41e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158138488  942 RSSNVVPYDFNRVPLKhelemskeseaesdessdeDSDSEETSKYINASFVMSYWKPEMMIAAQGPLKETIGDFWQMIFQ 1021
Cdd:cd14548     1 RYTNILPYDHSRVKLI-------------------PINEEEGSDYINANYIPGYNSPREFIATQGPLPGTKDDFWRMVWE 61

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158138488 1022 RKVKVIVMLTELMSGDQEVCAQYWGEGKQ--TYGDMEVMLKDTNKSSAYILRAFELRHskRKEPRTVYQYQCTTWKGEEL 1099
Cdd:cd14548    62 QNSHTIVMLTQCMEKGRVKCDHYWPFDQDpvYYGDITVTMLSESVLPDWTIREFKLER--GDEVRSVRQFHFTAWPDHGV 139

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158138488 1100 PAEPKDLVTLIQNIKQKLPKSGSegmkyhkhaSILVHCRDGSQQTGLFCALFNLLESAETEDVVDVFQVVKSLRKARPGM 1179
Cdd:cd14548   140 PEAPDSLLRFVRLVRDYIKQEKG---------PTIVHCSAGVGRTGTFIALDRLLQQIESEDYVDIFGIVYDLRKHRPLM 210

                         250
                  ....*....|.
gi 158138488 1180 VGSFEQYQFLY 1190
Cdd:cd14548   211 VQTEAQYIFLH 221
PTPc-N3 cd14600
catalytic domain of tyrosine-protein phosphatase non-receptor type 3; Tyrosine-protein ...
 623-879 6.74e-51

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: 181.20  E-value: 6.74e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158138488  623 LAEFQSIPRVFSKFPIKDARKSQNQNKNRYVDILPYDYNRVELSEingdaGSTYINASYID----GFKEPRKYIAAQGPR 698
Cdd:cd14600    17 LIQFEQLYRKKPGLAITCAKLPQNMDKNRYKDVLPYDATRVVLQG-----NEDYINASYVNmeipSANIVNKYIATQGPL 91

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158138488  699 DETVDDFWKMIWEQKATVIVMVTRCEEGNRNKCAEYWP----CMEEGtrTFRdvvVTINDHKRCPDYIIQKLSIAhKKEK 774
Cdd:cd14600    92 PHTCAQFWQVVWEQKLSLIVMLTTLTERGRTKCHQYWPdppdVMEYG--GFR---VQCHSEDCTIAYVFREMLLT-NTQT 165

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158138488  775 ATGREVTHIQFTSWPDHGVPEDPHLLLKLRRRVNAfSNFFSGPIVVHCSAGVGRTGTYIGIDAMLESLEAEGKVDVYGYV 854
Cdd:cd14600   166 GEERTVTHLQYVAWPDHGVPDDSSDFLEFVNYVRS-KRVENEPVLVHCSAGIGRTGVLVTMETAMCLTERNQPVYPLDIV 244

                         250       260
                  ....*....|....*....|....*
gi 158138488  855 VNLRRQRCLMVQVEAQYILIHQALV 879
Cdd:cd14600   245 RKMRDQRAMMVQTSSQYKFVCEAIL 269
PTP_fungal cd18533
fungal protein tyrosine phosphatases; This subfamily contains Saccharomyces cerevisiae ...
 986-1191 1.02e-50

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: 178.21  E-value: 1.02e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158138488  986 YINASFV-MSYWKPEMMIAAQGPLKETIGDFWQMIFQRKVKVIVMLTELMSGDQEVCAQYW--GEGKQTYGD--MEVMLK 1060
Cdd:cd18533     1 YINASYItLPGTSSKRYIATQGPLPATIGDFWKMIWQNNVGVIVMLTPLVENGREKCDQYWpsGEYEGEYGDltVELVSE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158138488 1061 DTNKSSAYILRAFELRHSKrKEPRTVYQYQCTTWKGEELPAEPKDLVTLIQnIKQKLPKSGSEGmkyhkhASILVHCRDG 1140
Cdd:cd18533    81 EENDDGGFIVREFELSKED-GKVKKVYHIQYKSWPDFGVPDSPEDLLTLIK-LKRELNDSASLD------PPIIVHCSAG 152

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 158138488 1141 SQQTGLFCALFNLL--------ESAETEDVVD-VFQVVKSLRKARPGMVGSFEQYQFLYD 1191
Cdd:cd18533   153 VGRTGTFIALDSLLdelkrglsDSQDLEDSEDpVYEIVNQLRKQRMSMVQTLRQYIFLYD 212
R-PTPc-E-2 cd14622
catalytic domain of receptor-type tyrosine-protein phosphatase E, repeat 2; Receptor-type ...
 986-1193 6.47e-50

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: 175.58  E-value: 6.47e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158138488  986 YINASFVMSYWKPEMMIAAQGPLKETIGDFWQMIFQRKVKVIVMLTELMSGDQEVCAQYW-GEGKQTYGDMEVMLKDTNK 1064
Cdd:cd14622     2 YINASFIDGYRQKDYFIATQGPLAHTVEDFWRMVWEWKCHTIVMLTELQEREQEKCVQYWpSEGSVTHGEITIEIKNDTL 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158138488 1065 SSAYILRAFELRHSKRKEPRTVYQYQCTTWKGEELPAEPKDLVTLIQNIKQKLPKSGSEgmkyhkhaSILVHCRDGSQQT 1144
Cdd:cd14622    82 LETISIRDFLVTYNQEKQTRLVRQFHFHGWPEIGIPAEGKGMIDLIAAVQKQQQQTGNH--------PIVVHCSAGAGRT 153

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*....
gi 158138488 1145 GLFCALFNLLESAETEDVVDVFQVVKSLRKARPGMVGSFEQYQFLYDIM 1193
Cdd:cd14622   154 GTFIALSNILERVKAEGLLDVFQTVKSLRLQRPHMVQTLEQYEFCYRVV 202
R-PTP-N cd14609
PTP-like domain of receptor-type tyrosine-protein phosphatase N; Receptor-type ...
 623-880 1.27e-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: 177.92  E-value: 1.27e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158138488  623 LAEFQSIPRVFSKfpikdARKSQNQNKNRYVDILPYDYNRVELSEINGDAGSTYINASYIDGfKEPR--KYIAAQGPRDE 700
Cdd:cd14609    24 LCAYQAEPNTCST-----AQGEANVKKNRNPDFVPYDHARIKLKAESNPSRSDYINASPIIE-HDPRmpAYIATQGPLSH 97

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158138488  701 TVDDFWKMIWEQKATVIVMVTRCEEGNRNKCAEYWPcmEEGTRTFRDVVVT-INDHKRCPDYIIQKLSIAHKKEKATgRE 779
Cdd:cd14609    98 TIADFWQMVWENGCTVIVMLTPLVEDGVKQCDRYWP--DEGSSLYHIYEVNlVSEHIWCEDFLVRSFYLKNVQTQET-RT 174

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158138488  780 VTHIQFTSWPDHGVPEDPHLLLKLRRRVNAFSNFFSGPIVVHCSAGVGRTGTYIGIDAMLESLeAEG--KVDVYGYVVNL 857
Cdd:cd14609   175 LTQFHFLSWPAEGIPSSTRPLLDFRRKVNKCYRGRSCPIIVHCSDGAGRTGTYILIDMVLNRM-AKGvkEIDIAATLEHV 253

                         250       260
                  ....*....|....*....|...
gi 158138488  858 RRQRCLMVQVEAQYILIHQALVE 880
Cdd:cd14609   254 RDQRPGMVRTKDQFEFALTAVAE 276
PHA02746 PHA02746
protein tyrosine phosphatase; Provisional
 604-878 1.94e-49

protein tyrosine phosphatase; Provisional


Pssm-ID: 165113 [Multi-domain]  Cd Length: 323  Bit Score: 178.68  E-value: 1.94e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158138488  604 SDLLLETYKRKIADEGRLFLAEFQSIPrvfSKFPIKDARKSQNQNKNRYVDILPYDYNRVELSE---------------- 667
Cdd:PHA02746   12 FDFFDKTNHAKFCEFVLLEHAEVMDIP---IRGTTNHFLKKENLKKNRFHDIPCWDHSRVVINAheslkmfdvgdsdgkk 88

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158138488  668 ---INGDAGSTYINASYIDGFKEPRKYIAAQGPRDETVDDFWKMIWEQKATVIVMVTRCEEGNRnKCAEYWPCMEEGTRT 744
Cdd:PHA02746   89 ievTSEDNAENYIHANFVDGFKEANKFICAQGPKEDTSEDFFKLISEHESQVIVSLTDIDDDDE-KCFELWTKEEDSELA 167

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158138488  745 FRDVVVTINDHKRCPDYIIQKLSIAHKKEKaTGREVTHIQFTSWPDHGVPEDPHLLLKLRRRVNA----------FSNFF 814
Cdd:PHA02746  168 FGRFVAKILDIIEELSFTKTRLMITDKISD-TSREIHHFWFPDWPDNGIPTGMAEFLELINKVNEeqaelikqadNDPQT 246

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 158138488  815 SGPIVVHCSAGVGRTGTYIGIDAMLESLEAEGKVDVYGYVVNLRRQRCLMVQVEAQYILIHQAL 878
Cdd:PHA02746  247 LGPIVVHCSAGIGRAGTFCAIDNALEQLEKEKEVCLGEIVLKIRKQRHSSVFLPEQYAFCYKAL 310
R-PTP-LAR-2 cd14554
PTP-like domain of the LAR family receptor-type tyrosine-protein phosphatases, repeat 2; The ...
 937-1190 3.58e-49

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: 175.02  E-value: 3.58e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158138488  937 NKKKNRSSNVVPYDFNRVPLKhelemskeseaesdessdeDSDSEETSKYINASFVMSYWKPEMMIAAQGPLKETIGDFW 1016
Cdd:cd14554     6 NKFKNRLVNILPYESTRVCLQ-------------------PIRGVEGSDYINASFIDGYRQRGAYIATQGPLAETTEDFW 66

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158138488 1017 QMIFQRKVKVIVMLTELMSGDQEVCAQYW-GEGKQTYGDMEVMLKDTNKSSAYILRAFELRHSKRKEPRTVYQYQCTTWK 1095
Cdd:cd14554    67 RMLWEHNSTIIVMLTKLREMGREKCHQYWpAERSARYQYFVVDPMAEYNMPQYILREFKVTDARDGQSRTVRQFQFTDWP 146

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158138488 1096 GEELPAEPKDLVTLIQNIKQKLPKSGSEGmkyhkhaSILVHCRDGSQQTGLFCALFNLLESAETEDVVDVFQVVKSLRKA 1175
Cdd:cd14554   147 EQGVPKSGEGFIDFIGQVHKTKEQFGQEG-------PITVHCSAGVGRTGVFITLSIVLERMRYEGVVDVFQTVKLLRTQ 219

                         250
                  ....*....|....*
gi 158138488 1176 RPGMVGSFEQYQFLY 1190
Cdd:cd14554   220 RPAMVQTEDQYQFCY 234
R5-PTPc-1 cd14549
catalytic domain of R5 subfamily receptor-type tyrosine-protein phosphatases, repeat 1; The R5 ...
 986-1191 1.49e-48

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: 171.77  E-value: 1.49e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158138488  986 YINASFVMSYWKPEMMIAAQGPLKETIGDFWQMIFQRKVKVIVMLTELMSGDQEVCAQYW-GEGKQTYGDMEVMLKDTNK 1064
Cdd:cd14549     1 YINANYVDGYNKARAYIATQGPLPSTFDDFWRMVWEQNSAIIVMITNLVERGRRKCDQYWpKEGTETYGNIQVTLLSTEV 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158138488 1065 SSAYILRAFELRHSK------RKEPRTVYQYQCTTWKGEELPAEPKDLVTLIQNikqklpksgSEGMKYHKHASILVHCR 1138
Cdd:cd14549    81 LATYTVRTFSLKNLKlkkvkgRSSERVVYQYHYTQWPDHGVPDYTLPVLSFVRK---------SSAANPPGAGPIVVHCS 151

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 158138488 1139 DGSQQTGLFCALFNLLESAETEDVVDVFQVVKSLRKARPGMVGSFEQYQFLYD 1191
Cdd:cd14549   152 AGVGRTGTYIVIDSMLQQIQDKGTVNVFGFLKHIRTQRNYLVQTEEQYIFIHD 204
R-PTPc-E-2 cd14622
catalytic domain of receptor-type tyrosine-protein phosphatase E, repeat 2; Receptor-type ...
 676-881 1.78e-48

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: 171.73  E-value: 1.78e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158138488  676 YINASYIDGFKEPRKYIAAQGPRDETVDDFWKMIWEQKATVIVMVTRCEEGNRNKCAEYWPcmEEGTRTFRDVVVTINDH 755
Cdd:cd14622     2 YINASFIDGYRQKDYFIATQGPLAHTVEDFWRMVWEWKCHTIVMLTELQEREQEKCVQYWP--SEGSVTHGEITIEIKND 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158138488  756 KRCPDYIIQKLSIAHKKEKATgREVTHIQFTSWPDHGVPEDPH----LLLKLRRRVNAFSNffsGPIVVHCSAGVGRTGT 831
Cdd:cd14622    80 TLLETISIRDFLVTYNQEKQT-RLVRQFHFHGWPEIGIPAEGKgmidLIAAVQKQQQQTGN---HPIVVHCSAGAGRTGT 155

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|
gi 158138488  832 YIGIDAMLESLEAEGKVDVYGYVVNLRRQRCLMVQVEAQYILIHQALVEY 881
Cdd:cd14622   156 FIALSNILERVKAEGLLDVFQTVKSLRLQRPHMVQTLEQYEFCYRVVQDF 205
R-PTPc-LAR-1 cd14553
catalytic domain of LAR family receptor-type tyrosine-protein phosphatases, repeat 1; The LAR ...
 935-1191 1.80e-48

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: 172.97  E-value: 1.80e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158138488  935 EENKKKNRSSNVVPYDFNRVPLKhelemskeseaesdessdeDSDSEETSKYINASFVMSYWKPEMMIAAQGPLKETIGD 1014
Cdd:cd14553     1 EVNKPKNRYANVIAYDHSRVILQ-------------------PIEGVPGSDYINANYCDGYRKQNAYIATQGPLPETFGD 61

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158138488 1015 FWQMIFQRKVKVIVMLTELMSGDQEVCAQYW-GEGKQTYGDMEVMLKDTNKSSAYILRAFELRHSKRKEPRTVYQYQCTT 1093
Cdd:cd14553    62 FWRMVWEQRSATIVMMTKLEERSRVKCDQYWpTRGTETYGLIQVTLLDTVELATYTVRTFALHKNGSSEKREVRQFQFTA 141

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158138488 1094 WKGEELPAEPKDLVTLIQNIKQ-KLPKSGsegmkyhkhaSILVHCRDGSQQTGLFCALFNLLESAETEDVVDVFQVVKSL 1172
Cdd:cd14553   142 WPDHGVPEHPTPFLAFLRRVKAcNPPDAG----------PIVVHCSAGVGRTGCFIVIDSMLERIKHEKTVDIYGHVTCL 211

                         250
                  ....*....|....*....
gi 158138488 1173 RKARPGMVGSFEQYQFLYD 1191
Cdd:cd14553   212 RAQRNYMVQTEDQYIFIHD 230
PTPc-N2 cd14607
catalytic domain of tyrosine-protein phosphatase non-receptor type 2; Tyrosine-protein ...
 634-870 1.16e-47

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: 171.30  E-value: 1.16e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158138488  634 SKFPIKDARKSQNQNKNRYVDILPYDYNRVELSEINGDagstYINASYIDGFKEPRKYIAAQGPRDETVDDFWKMIWEQK 713
Cdd:cd14607    12 HDYPHRVAKYPENRNRNRYRDVSPYDHSRVKLQNTEND----YINASLVVIEEAQRSYILTQGPLPNTCCHFWLMVWQQK 87

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158138488  714 ATVIVMVTRCEEGNRNKCAEYWPCMEEGTRTFRDV--VVTINDHKRCPDYIIQKLSIAHKKEKATgREVTHIQFTSWPDH 791
Cdd:cd14607    88 TKAVVMLNRIVEKDSVKCAQYWPTDEEEVLSFKETgfSVKLLSEDVKSYYTVHLLQLENINSGET-RTISHFHYTTWPDF 166

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158138488  792 GVPEDP----HLLLKLRRrvNAFSNFFSGPIVVHCSAGVGRTGTYIGIDAMLESLEAEG--KVDVYGYVVNLRRQRCLMV 865
Cdd:cd14607   167 GVPESPasflNFLFKVRE--SGSLSPEHGPAVVHCSAGIGRSGTFSLVDTCLVLMEKKDpdSVDIKQVLLDMRKYRMGLI 244


                  ....*
gi 158138488  866 QVEAQ 870
Cdd:cd14607   245 QTPDQ 249
PTPc_plant_PTP1 cd17658
protein tyrosine phosphatase 1 from Arabidopsis thaliana and similar plant PTPs; Arabidopsis ...
 676-875 1.53e-47

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


Pssm-ID: 350496 [Multi-domain]  Cd Length: 206  Bit Score: 168.80  E-value: 1.53e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158138488  676 YINASYI--DGFKEPRKYIAAQGPRDETVDDFWKMIWEQKATVIVMVTRCEEGNR-NKCAEYWPCMEEGTRTFRDVVVTI 752
Cdd:cd17658     1 YINASLVetPASESLPKFIATQGPLPHTFEDFWEMVIQQRCPVIIMLTRLVDNYStAKCADYFPAEENESREFGRISVTN 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158138488  753 NDHKrCPDYIIQK--LSIAHKKEKATGREVTHIQFTSWPDHGVPEDPHLLLKLRRRVNAFSNFFsGPIVVHCSAGVGRTG 830
Cdd:cd17658    81 KKLK-HSQHSITLrvLEVQYIESEEPPLSVLHIQYPEWPDHGVPKDTRSVRELLKRLYGIPPSA-GPIVVHCSAGIGRTG 158

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|
gi 158138488  831 TYIGIDAMLE-----SLEAegkVDVYGYVVNLRRQRCLMVQVEAQYILIH 875
Cdd:cd17658   159 AYCTIHNTIRrilegDMSA---VDLSKTVRKFRSQRIGMVQTQDQYIFCY 205
PTPc-N20 cd14596
catalytic domain of tyrosine-protein phosphatase non-receptor type 20; Tyrosine-protein ...
 676-880 1.59e-47

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: 168.77  E-value: 1.59e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158138488  676 YINASYID---GFKEpRKYIAAQGPRDETVDDFWKMIWEQKATVIVMVTRCEEGNRNKCAEYWPCMEEGTRTFRDVVVTI 752
Cdd:cd14596     1 YINASYITmpvGEEE-LFYIATQGPLPSTIDDFWQMVWENRSDVIAMMTREVERGKVKCHRYWPETLQEPMELENYQLRL 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158138488  753 NDHKRCPDYIIQKLSIAhKKEKATGREVTHIQFTSWPDHGVPEDPHLLLKLRRRVNAFSNffSGPIVVHCSAGVGRTGTY 832
Cdd:cd14596    80 ENYQALQYFIIRIIKLV-EKETGENRLIKHLQFTTWPDHGTPQSSDQLVKFICYMRKVHN--TGPIVVHCSAGIGRAGVL 156

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*...
gi 158138488  833 IGIDAMLESLEAEGKVDVYGYVVNLRRQRCLMVQVEAQYILIHQALVE 880
Cdd:cd14596   157 ICVDVLLSLIEKDLSFNIKDIVREMRQQRYGMIQTKDQYLFCYKVVLE 204
R-PTPc-H cd14619
catalytic domain of receptor-type tyrosine-protein phosphatase H; Receptor-type ...
 941-1193 1.67e-46

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: 166.99  E-value: 1.67e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158138488  941 NRSSNVVPYDFNRVPLKhelemskeseaesdessdeDSDSEETSKYINASFVMSYWKPEMMIAAQGPLKETIGDFWQMIF 1020
Cdd:cd14619     1 NRFRNVLPYDWSRVPLK-------------------PIHEEPGSDYINANYMPGYWSSQEFIATQGPLPQTVGDFWRMIW 61

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158138488 1021 QRKVKVIVMLTELMSGDQEVCAQYWGEGKQ--TYGDMEVMLKDTNKSSAYILRAFELRHSKRKEPRTVYQYQCTTWKGEE 1098
Cdd:cd14619    62 EQQSSTIVMLTNCMEAGRVKCEHYWPLDYTpcTYGHLRVTVVSEEVMENWTVREFLLKQVEEQKTLSVRHFHFTAWPDHG 141

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158138488 1099 LPAEPKDLVTLIQNIKQKLPKSGSEGmkyhkhaSILVHCRDGSQQTGLFCALFNLLESAETEDVVDVFQVVKSLRKARPG 1178
Cdd:cd14619   142 VPSSTDTLLAFRRLLRQWLDQTMSGG-------PTVVHCSAGVGRTGTLIALDVLLQQLQSEGLLGPFSFVQKMRENRPL 214

                         250
                  ....*....|....*
gi 158138488 1179 MVGSFEQYQFLYDIM 1193
Cdd:cd14619   215 MVQTESQYVFLHQCI 229
PHA02747 PHA02747
protein tyrosine phosphatase; Provisional
 638-875 4.76e-46

protein tyrosine phosphatase; Provisional


Pssm-ID: 165114 [Multi-domain]  Cd Length: 312  Bit Score: 168.64  E-value: 4.76e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158138488  638 IKDARKSQNQNKNRYVDILPYDYNRVELsEINGDAGSTYINASYIDGFKEPRKYIAAQGPRDETVDDFWKMIWEQKATVI 717
Cdd:PHA02747   43 IANFEKPENQPKNRYWDIPCWDHNRVIL-DSGGGSTSDYIHANWIDGFEDDKKFIATQGPFAETCADFWKAVWQEHCSII 121

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158138488  718 VMVTRCEEGN-RNKCAEYWPCMEEGTRTFRDVVV-TINDHKRcPDYIIQKLSIAHKKEKaTGREVTHIQFTSWPDHGVPE 795
Cdd:PHA02747  122 VMLTPTKGTNgEEKCYQYWCLNEDGNIDMEDFRIeTLKTSVR-AKYILTLIEITDKILK-DSRKISHFQCSEWFEDETPS 199

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158138488  796 DPHLLLKL-----RRRVNAFSNFFS-----GPIVVHCSAGVGRTGTYIGIDAMLESLEAEGKVDVYGYVVNLRRQRCLMV 865
Cdd:PHA02747  200 DHPDFIKFikiidINRKKSGKLFNPkdallCPIVVHCSDGVGKTGIFCAVDICLNQLVKRKAICLAKTAEKIREQRHAGI 279

                         250
                  ....*....|
gi 158138488  866 QVEAQYILIH 875
Cdd:PHA02747  280 MNFDDYLFIQ 289
PTPc-N9 cd14543
catalytic domain of tyrosine-protein phosphatase non-receptor type 9; Tyrosine-protein ...
 937-1190 1.22e-45

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: 166.00  E-value: 1.22e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158138488  937 NKKKNRSSNVVPYDFNRVPLKHELEmskeseaesdessdedsdsEETSKYINASFVMSYWKPEMMIAAQGPLKETIGDFW 1016
Cdd:cd14543    29 NQEKNRYGDVLCLDQSRVKLPKRNG-------------------DERTDYINANFMDGYKQKNAYIATQGPLPKTYSDFW 89

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158138488 1017 QMIFQRKVKVIVMLTELMSGDQEVCAQYW---GEGKQTYGDMEVMLKDTNKSSAYILRAFELRHSKRKEPRTVYQYQCTT 1093
Cdd:cd14543    90 RMVWEQKVLVIVMTTRVVERGRVKCGQYWpleEGSSLRYGDLTVTNLSVENKEHYKKTTLEIHNTETDESRQVTHFQFTS 169

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158138488 1094 WKGEELPAEPKDLVTLIQNIKQKLPKSGSE-GMKYHKHAS---ILVHCRDGSQQTGLFCALFNLLESAETEDVVDVFQVV 1169
Cdd:cd14543   170 WPDFGVPSSAAALLDFLGEVRQQQALAVKAmGDRWKGHPPgppIVVHCSAGIGRTGTFCTLDICLSQLEDVGTLNVMQTV 249

                         250       260
                  ....*....|....*....|.
gi 158138488 1170 KSLRKARPGMVGSFEQYQFLY 1190
Cdd:cd14543   250 RRMRTQRAFSIQTPDQYYFCY 270
R-PTP-S-2 cd14627
PTP-like domain of receptor-type tyrosine-protein phosphatase S, repeat 2; Receptor-type ...
 887-1190 1.27e-45

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: 166.45  E-value: 1.27e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158138488  887 TEVNLSELHSCLQNLKKRDPPSDPSPLEAEYQRLPSYRSWRTQHI-GNQEENKKKNRSSNVVPYDFNRVPLKhelemske 965
Cdd:cd14627     2 TEVPARNLYSYIQKLAQVEVGEHVTGMELEFKRLANSKAHTSRFIsANLPCNKFKNRLVNIMPYETTRVCLQ-------- 73

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158138488  966 seaesdessdeDSDSEETSKYINASFVMSYWKPEMMIAAQGPLKETIGDFWQMIFQRKVKVIVMLTELMSGDQEVCAQYW 1045
Cdd:cd14627    74 -----------PIRGVEGSDYINASFIDGYRQQKAYIATQGPLAETTEDFWRMLWENNSTIVVMLTKLREMGREKCHQYW 142

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158138488 1046 -GEGKQTYGDMEVMLKDTNKSSAYILRAFELRHSKRKEPRTVYQYQCTTWKGEELPAEPKDLVTLIQNIKQKLPKSGSEG 1124
Cdd:cd14627   143 pAERSARYQYFVVDPMAEYNMPQYILREFKVTDARDGQSRTVRQFQFTDWPEQGVPKSGEGFIDFIGQVHKTKEQFGQDG 222

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 158138488 1125 mkyhkhaSILVHCRDGSQQTGLFCALFNLLESAETEDVVDVFQVVKSLRKARPGMVGSFEQYQFLY 1190
Cdd:cd14627   223 -------PISVHCSAGVGRTGVFITLSIVLERMRYEGVVDIFQTVKMLRTQRPAMVQTEDEYQFCY 281
R-PTP-D-2 cd14628
PTP-like domain of receptor-type tyrosine-protein phosphatase D, repeat 2; Receptor-type ...
 887-1190 1.54e-45

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: 166.45  E-value: 1.54e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158138488  887 TEVNLSELHSCLQNLKKRDPPSDPSPLEAEYQRLPSYRSWRTQHI-GNQEENKKKNRSSNVVPYDFNRVPLKhelemske 965
Cdd:cd14628     1 TEVPARNLYAYIQKLTQIETGENVTGMELEFKRLASSKAHTSRFIsANLPCNKFKNRLVNIMPYESTRVCLQ-------- 72

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158138488  966 seaesdessdeDSDSEETSKYINASFVMSYWKPEMMIAAQGPLKETIGDFWQMIFQRKVKVIVMLTELMSGDQEVCAQYW 1045
Cdd:cd14628    73 -----------PIRGVEGSDYINASFIDGYRQQKAYIATQGPLAETTEDFWRMLWEHNSTIVVMLTKLREMGREKCHQYW 141

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158138488 1046 -GEGKQTYGDMEVMLKDTNKSSAYILRAFELRHSKRKEPRTVYQYQCTTWKGEELPAEPKDLVTLIQNIKQKLPKSGSEG 1124
Cdd:cd14628   142 pAERSARYQYFVVDPMAEYNMPQYILREFKVTDARDGQSRTVRQFQFTDWPEQGVPKSGEGFIDFIGQVHKTKEQFGQDG 221

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 158138488 1125 mkyhkhaSILVHCRDGSQQTGLFCALFNLLESAETEDVVDVFQVVKSLRKARPGMVGSFEQYQFLY 1190
Cdd:cd14628   222 -------PISVHCSAGVGRTGVFITLSIVLERMRYEGVVDIFQTVKMLRTQRPAMVQTEDQYQFCY 280
R-PTPc-typeIIb-2 cd14556
PTP domain of type IIb (or R2B) subfamily receptor-type tyrosine-protein phosphatases, repeat ...
 986-1191 7.65e-45

PTP domain of type IIb (or R2B) subfamily receptor-type tyrosine-protein phosphatases, repeat 2; The type IIb (or R2B) subfamily of receptor protein tyrosine phosphatases (RPTPs) include the prototypical member PTPmu (or PTPRM), PCP-2 (or PTPRU), PTPrho (or PTPRT), and PTPkappa (or PTPRK). They belong to the larger family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. Type IIb RPTPs mediate cell-cell adhesion though homophilic interactions; their ligand is an identical molecule on an adjacent cell. No heterophilic interactions between the subfamily members have been observed. They also commonly function as tumor suppressors. They contain an extracellular region with an Meprin-A5 (neuropilin)-mu (MAM) domain, an immunoglobulin (Ig) domain, and four fibronectin type III (FN3) repeats, a transmembrane domain, and an intracellular segment with a juxtamembrane domain similar to the cytoplasmic domain of classical cadherins and two tandem PTP domains. This model represents the second (repeat 2) PTP domain.


Pssm-ID: 350404 [Multi-domain]  Cd Length: 201  Bit Score: 161.04  E-value: 7.65e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158138488  986 YINASFVMSYWKPEMMIAAQGPLKETIGDFWQMIFQRKVKVIVMLTELMSGDQEvCAQYWGE-GKQTYGDMEVMLKDTNK 1064
Cdd:cd14556     1 YINAALLDSYKQPAAFIVTQHPLPNTVTDFWRLVYDYGCTSIVMLNQLDPKDQS-CPQYWPDeGSGTYGPIQVEFVSTTI 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158138488 1065 SSAYILRAFELRHSKRKEP--RTVYQYQCTTW-KGEELPAEPKDLVTLIQNIKQKLPKSGSEgmkyhkhaSILVHCRDGS 1141
Cdd:cd14556    80 DEDVISRIFRLQNTTRPQEgyRMVQQFQFLGWpRDRDTPPSKRALLKLLSEVEKWQEQSGEG--------PIVVHCLNGV 151

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|
gi 158138488 1142 QQTGLFCALFNLLESAETEDVVDVFQVVKSLRKARPGMVGSFEQYQFLYD 1191
Cdd:cd14556   152 GRSGVFCAISSVCERIKVENVVDVFQAVKTLRNHRPNMVETEEQYKFCYD 201
R-PTPc-T-1 cd14630
catalytic domain of receptor-type tyrosine-protein phosphatase T, repeat 1; Receptor-type ...
 935-1191 2.86e-44

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: 160.58  E-value: 2.86e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158138488  935 EENKKKNRSSNVVPYDFNRVPLKhelemskeseaesdessdeDSDSEETSKYINASFVMSYWKPEMMIAAQGPLKETIGD 1014
Cdd:cd14630     1 DENRNKNRYGNIISYDHSRVRLQ-------------------LLDGDPHSDYINANYIDGYHRPRHYIATQGPMQETVKD 61

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158138488 1015 FWQMIFQRKVKVIVMLTELMSGDQEVCAQYWGEGKQTYGDMEVMLKDTNKSSAYILRAFELRHSKRKEPRTVYQYQCTTW 1094
Cdd:cd14630    62 FWRMIWQENSASVVMVTNLVEVGRVKCVRYWPDDTEVYGDIKVTLIETEPLAEYVIRTFTVQKKGYHEIREIRQFHFTSW 141

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158138488 1095 KGEELPAEPKDLVTLIQNIKQKLPKSGsegmkyhkhASILVHCRDGSQQTGLFCALFNLLESAETEDVVDVFQVVKSLRK 1174
Cdd:cd14630   142 PDHGVPCYATGLLGFVRQVKFLNPPDA---------GPIVVHCSAGAGRTGCFIAIDIMLDMAENEGVVDIFNCVRELRA 212

                         250
                  ....*....|....*..
gi 158138488 1175 ARPGMVGSFEQYQFLYD 1191
Cdd:cd14630   213 QRVNMVQTEEQYVFVHD 229
R-PTPc-J cd14615
catalytic domain of receptor-type tyrosine-protein phosphatase J; Receptor-type ...
 941-1189 2.90e-44

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: 160.37  E-value: 2.90e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158138488  941 NRSSNVVPYDFNRVPLKHElemskeseaesdessdedsdSEETSKYINASFVMSYWKPEMMIAAQGPLKETIGDFWQMIF 1020
Cdd:cd14615     1 NRYNNVLPYDISRVKLSVQ--------------------SHSTDDYINANYMPGYNSKKEFIAAQGPLPNTVKDFWRMVW 60

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158138488 1021 QRKVKVIVMLTELMSGDQEVCAQYW-GEGKQTYGDMEVMLKDTNKSSAYILRAFELRHSKRKEPRTVYQYQCTTWKGEEL 1099
Cdd:cd14615    61 EKNVYAIVMLTKCVEQGRTKCEEYWpSKQKKDYGDITVTMTSEIVLPEWTIRDFTVKNAQTNESRTVRHFHFTSWPDHGV 140

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158138488 1100 PaEPKDLVTLIQNIKQklpksgsEGMKYH-KHASILVHCRDGSQQTGLFCALFNLLESAETEDVVDVFQVVKSLRKARPG 1178
Cdd:cd14615   141 P-ETTDLLINFRHLVR-------EYMKQNpPNSPILVHCSAGVGRTGTFIAIDRLIYQIENENVVDVYGIVYDLRMHRPL 212

                         250
                  ....*....|.
gi 158138488 1179 MVGSFEQYQFL 1189
Cdd:cd14615   213 MVQTEDQYVFL 223
R-PTP-F-2 cd14629
PTP-like domain of receptor-type tyrosine-protein phosphatase F, repeat 2; Receptor-type ...
 887-1190 3.32e-44

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: 162.59  E-value: 3.32e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158138488  887 TEVNLSELHSCLQNLKKRDPPSDPSPLEAEYQRLPSYRSWRTQHI-GNQEENKKKNRSSNVVPYDFNRVPLKhelemske 965
Cdd:cd14629     2 TEVPARNLYAHIQKLTQVPPGESVTAMELEFKLLANSKAHTSRFIsANLPCNKFKNRLVNIMPYELTRVCLQ-------- 73

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158138488  966 seaesdessdeDSDSEETSKYINASFVMSYWKPEMMIAAQGPLKETIGDFWQMIFQRKVKVIVMLTELMSGDQEVCAQYW 1045
Cdd:cd14629    74 -----------PIRGVEGSDYINASFIDGYRQQKAYIATQGPLAETTEDFWRMLWEHNSTIVVMLTKLREMGREKCHQYW 142

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158138488 1046 -GEGKQTYGDMEVMLKDTNKSSAYILRAFELRHSKRKEPRTVYQYQCTTWKGEELPAEPKDLVTLIQNIKQKLPKSGSEG 1124
Cdd:cd14629   143 pAERSARYQYFVVDPMAEYNMPQYILREFKVTDARDGQSRTIRQFQFTDWPEQGVPKTGEGFIDFIGQVHKTKEQFGQDG 222

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 158138488 1125 mkyhkhaSILVHCRDGSQQTGLFCALFNLLESAETEDVVDVFQVVKSLRKARPGMVGSFEQYQFLY 1190
Cdd:cd14629   223 -------PITVHCSAGVGRTGVFITLSIVLERMRYEGVVDMFQTVKTLRTQRPAMVQTEDQYQLCY 281
R-PTPc-V cd14618
catalytic domain of receptor-type tyrosine-protein phosphatase V; Receptor-type ...
 941-1190 8.79e-44

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: 158.95  E-value: 8.79e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158138488  941 NRSSNVVPYDFNRVPLKHelemskeseaesdessdedSDSEETSKYINASFVMSYWKPEMMIAAQGPLKETIGDFWQMIF 1020
Cdd:cd14618     1 NRYPHVLPYDHSRVRLSQ-------------------LGGEPHSDYINANFIPGYTSPQEFIATQGPLKKTIEDFWRLVW 61

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158138488 1021 QRKVKVIVMLTELMSGDQEVCAQYWGEGKQ--TYGDMEVMLKDTNKSSAYILRAFELRHSKRKEPRTVYQYQCTTWKGEE 1098
Cdd:cd14618    62 EQQVCNIIMLTVGMENGRVLCDHYWPSESTpvSYGHITVHLLAQSSEDEWTRREFKLWHEDLRKERRVKHLHYTAWPDHG 141

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158138488 1099 LPAEPKDLVTLIQNIKQKLPKSGSEGmkyhkhaSILVHCRDGSQQTGLFCALFNLLESAETEDVVDVFQVVKSLRKARPG 1178
Cdd:cd14618   142 IPESTSSLMAFRELVREHVQATKGKG-------PTLVHCSAGVGRSGTFIALDRLLRQLKEEKVVDVFNTVYILRMHRYL 214

                         250
                  ....*....|..
gi 158138488 1179 MVGSFEQYQFLY 1190
Cdd:cd14618   215 MIQTLSQYIFLH 226
PTPc-N21 cd14598
catalytic domain of tyrosine-protein phosphatase non-receptor type 21; Tyrosine-protein ...
 676-881 1.20e-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: 158.21  E-value: 1.20e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158138488  676 YINASYID---GFKEpRKYIAAQGPRDETVDDFWKMIWEQKATVIVMVTRCEEGNRNKCAEYWPCM--EEGTRTFRDVVV 750
Cdd:cd14598     1 YINASHIKvtvGGKE-WDYIATQGPLQNTCQDFWQMVWEQGVAIIAMVTAEEEGGREKSFRYWPRLgsRHNTVTYGRFKI 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158138488  751 TINDHKRCPDYIIQKLSIAHkkeKATGREVT--HIQFTSWPDHGVPEDPHLLL-------KLRRRVNAFSNFFSG--PIV 819
Cdd:cd14598    80 TTRFRTDSGCYATTGLKIKH---LLTGQERTvwHLQYTDWPEHGCPEDLKGFLsyleeiqSVRRHTNSTIDPKSPnpPVL 156

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 158138488  820 VHCSAGVGRTGTYIGIDAMLESLEAEGKVDVYGYVVNLRRQRCLMVQVEAQYILIHQALVEY 881
Cdd:cd14598   157 VHCSAGVGRTGVVILSEIMIACLEHNEMLDIPRVLDMLRQQRMMMVQTLSQYTFVYKVLIQF 218
PTP-N23 cd14539
PTP-like domain of tyrosine-protein phosphatase non-receptor type 23; Tyrosine-protein ...
 676-876 4.26e-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: 156.00  E-value: 4.26e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158138488  676 YINASYIDGFKE--PRkYIAAQGPRDETVDDFWKMIWEQKATVIVMVTRCEEGNRNKCAEYWPCMEEGTRTFRDVVVTIN 753
Cdd:cd14539     1 YINASLIEDLTPycPR-FIATQAPLPGTAADFWLMVYEQQVSVIVMLVSEQENEKQKVHRYWPTERGQALVYGAITVSLQ 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158138488  754 DHKRCPDYIIQKLSIAHKKEKATgREVTHIQFTSWPDHGVPEDPHLLLKLRRRVNAFSNFFSG---PIVVHCSAGVGRTG 830
Cdd:cd14539    80 SVRTTPTHVERIISIQHKDTRLS-RSVVHLQFTTWPELGLPDSPNPLLRFIEEVHSHYLQQRSlqtPIVVHCSSGVGRTG 158

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*..
gi 158138488  831 TY-IGIDAMLESLEAEGKVDVYGYVVNLRRQRCLMVQVEAQYILIHQ 876
Cdd:cd14539   159 AFcLLYAAVQEIEAGNGIPDLPQLVRKMRQQRKYMLQEKEHLKFCYE 205
PTPc-N4 cd14601
catalytic domain of tyrosine-protein phosphatase non-receptor type 4; Tyrosine-protein ...
 676-880 4.42e-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: 156.26  E-value: 4.42e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158138488  676 YINASYID----GFKEPRKYIAAQGPRDETVDDFWKMIWEQKATVIVMVTRCEEGNRNKCAEYWPcMEEGTRTFRDVVVT 751
Cdd:cd14601     2 YINANYINmeipSSSIINRYIACQGPLPNTCSDFWQMTWEQGSSMVVMLTTQVERGRVKCHQYWP-EPSGSSSYGGFQVT 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158138488  752 INDHKRCPDYIIQKLSIAHkKEKATGREVTHIQFTSWPDHGVPEDPHLLLKLRRRVNAFSNFFSGPIVVHCSAGVGRTGT 831
Cdd:cd14601    81 CHSEEGNPAYVFREMTLTN-LEKNESRPLTQIQYIAWPDHGVPDDSSDFLDFVCLVRNKRAGKDEPVVVHCSAGIGRTGV 159

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*....
gi 158138488  832 YIGIDAMLESLEAEGKVDVYGYVVNLRRQRCLMVQVEAQYILIHQALVE 880
Cdd:cd14601   160 LITMETAMCLIECNQPVYPLDIVRTMRDQRAMMIQTPSQYRFVCEAILK 208
R-PTPc-typeIIb-1 cd14555
catalytic domain of type IIb (or R2B) subfamily receptor-type tyrosine-protein phosphatases, ...
 986-1191 4.87e-43

catalytic domain of type IIb (or R2B) subfamily receptor-type tyrosine-protein phosphatases, repeat 1; The type II (or R2B) subfamily of receptor protein tyrosine phosphatases (RPTPs) include the prototypical member PTPmu (or PTPRM), PCP-2 (or PTPRU), PTPrho (or PTPRT), and PTPkappa (or PTPRK). They belong to the larger family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. Type IIb RPTPs mediate cell-cell adhesion though homophilic interactions; their ligand is an identical molecule on an adjacent cell. No heterophilic interactions between the subfamily members have been observed. They also commonly function as tumor suppressors. They contain an extracellular region with an Meprin-A5 (neuropilin)-mu (MAM) domain, an immunoglobulin (Ig) domain, and four fibronectin type III (FN3) repeats, a transmembrane domain, and an intracellular segment with a juxtamembrane domain similar to the cytoplasmic domain of classical cadherins and two tandem PTP domains. This model represents the first (repeat 1) PTP domain.


Pssm-ID: 350403 [Multi-domain]  Cd Length: 204  Bit Score: 155.85  E-value: 4.87e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158138488  986 YINASFVMSYWKPEMMIAAQGPLKETIGDFWQMIFQRKVKVIVMLTELMSGDQEVCAQYWGEGKQTYGDMEVMLKDTNKS 1065
Cdd:cd14555     1 YINANYIDGYHRPNHYIATQGPMQETVYDFWRMVWQENSASIVMVTNLVEVGRVKCSRYWPDDTEVYGDIKVTLVETEPL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158138488 1066 SAYILRAFELRHSKRKEPRTVYQYQCTTWKGEELPAEPKDLVTLIQNIKQKLPKSGsegmkyhkhASILVHCRDGSQQTG 1145
Cdd:cd14555    81 AEYVVRTFALERRGYHEIREVRQFHFTGWPDHGVPYHATGLLGFIRRVKASNPPSA---------GPIVVHCSAGAGRTG 151

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*.
gi 158138488 1146 LFCALFNLLESAETEDVVDVFQVVKSLRKARPGMVGSFEQYQFLYD 1191
Cdd:cd14555   152 CYIVIDIMLDMAEREGVVDIYNCVKELRSRRVNMVQTEEQYIFIHD 197
PHA02738 PHA02738
hypothetical protein; Provisional
 645-889 3.56e-42

hypothetical protein; Provisional


Pssm-ID: 222923 [Multi-domain]  Cd Length: 320  Bit Score: 157.39  E-value: 3.56e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158138488  645 QNQNKNRYVDILPYDYNRVEL-SEIN-GDagstYINASYIDGFKEPRKYIAAQGPRDETVDDFWKMIWEQKATVIVMVTR 722
Cdd:PHA02738   48 KNRKLNRYLDAVCFDHSRVILpAERNrGD----YINANYVDGFEYKKKFICGQAPTRQTCYDFYRMLWMEHVQIIVMLCK 123

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158138488  723 CEEGNRNKCAEYWPCMEEGTRTFRDVVVTINDHKRCPDYIIQKLSIAHKKEkATgREVTHIQFTSWPDHGVPEDPHLLLK 802
Cdd:PHA02738  124 KKENGREKCFPYWSDVEQGSIRFGKFKITTTQVETHPHYVKSTLLLTDGTS-AT-QTVTHFNFTAWPDHDVPKNTSEFLN 201

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158138488  803 LRRRV---------NAFSN----FFSGPIVVHCSAGVGRTGTYIGIDAMLESLEAEGKVDVYGYVVNLRRQRCLMVQVEA 869
Cdd:PHA02738  202 FVLEVrqcqkelaqESLQIghnrLQPPPIVVHCNAGLGRTPCYCVVDISISRFDACATVSIPSIVSSIRNQRYYSLFIPF 281

                         250       260
                  ....*....|....*....|
gi 158138488  870 QYILIHQALVEYNQFGETEV 889
Cdd:PHA02738  282 QYFFCYRAVKRYVNLTVNKV 301
PHA02742 PHA02742
protein tyrosine phosphatase; Provisional
 643-881 3.72e-42

protein tyrosine phosphatase; Provisional


Pssm-ID: 165109 [Multi-domain]  Cd Length: 303  Bit Score: 157.09  E-value: 3.72e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158138488  643 KSQNQNKNRYVDILPYDYNRVELSEINGdaGSTYINASYIDGFKEPRKYIAAQGPRDETVDDFWKMIWEQKATVIVMVTR 722
Cdd:PHA02742   49 ELKNMKKCRYPDAPCFDRNRVILKIEDG--GDDFINASYVDGHNAKGRFICTQAPLEETALDFWQAIFQDQVRVIVMITK 126

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158138488  723 CEEGNRNKCAEYWPCMEEGTRTFRDVVVTINDHKRCPDYIIQKLSIAHKKeKATGREVTHIQFTSWPDHGVPEDP----- 797
Cdd:PHA02742  127 IMEDGKEACYPYWMPHERGKATHGEFKIKTKKIKSFRNYAVTNLCLTDTN-TGASLDIKHFAYEDWPHGGLPRDPnkfld 205

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158138488  798 ------HLLLKLRRRVNAFSNFFSGPIVVHCSAGVGRTGTYIGIDAMLESLEAEGKVDVYGYVVNLRRQRCLMVQVEAQY 871
Cdd:PHA02742  206 fvlavrEADLKADVDIKGENIVKEPPILVHCSAGLDRAGAFCAIDICISKYNERAIIPLLSIVRDLRKQRHNCLSLPQQY 285

                         250
                  ....*....|
gi 158138488  872 ILIHQALVEY 881
Cdd:PHA02742  286 IFCYFIVLIF 295
R-PTPc-S-1 cd14625
catalytic domain of receptor-type tyrosine-protein phosphatase S, repeat 1; Receptor-type ...
 889-1193 7.70e-42

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: 155.25  E-value: 7.70e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158138488  889 VNLSELHSCLQNLKKrdppSDPSPLEAEYQRLPSYRSWRTQHiGNQEENKKKNRSSNVVPYDFNRVPLKhelemskesea 968
Cdd:cd14625     4 IPISELAEHTERLKA----NDNLKLSQEYESIDPGQQFTWEH-SNLEVNKPKNRYANVIAYDHSRVILQ----------- 67

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158138488  969 esdessdeDSDSEETSKYINASFVMSYWKPEMMIAAQGPLKETIGDFWQMIFQRKVKVIVMLTELMSGDQEVCAQYW-GE 1047
Cdd:cd14625    68 --------PIEGIMGSDYINANYIDGYRKQNAYIATQGPLPETFGDFWRMVWEQRSATVVMMTKLEEKSRIKCDQYWpSR 139

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158138488 1048 GKQTYGDMEVMLKDTNKSSAYILRAFELRHSKRKEPRTVYQYQCTTWKGEELPAEPKDLVTLIQNIKQKLPKSGsegmky 1127
Cdd:cd14625   140 GTETYGMIQVTLLDTIELATFCVRTFSLHKNGSSEKREVRQFQFTAWPDHGVPEYPTPFLAFLRRVKTCNPPDA------ 213

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 158138488 1128 hkhASILVHCRDGSQQTGLFCALFNLLESAETEDVVDVFQVVKSLRKARPGMVGSFEQYQFLYDIM 1193
Cdd:cd14625   214 ---GPIVVHCSAGVGRTGCFIVIDAMLERIKHEKTVDIYGHVTLMRSQRNYMVQTEDQYSFIHDAL 276
COG5599 COG5599
Protein tyrosine phosphatase [Signal transduction mechanisms];
639-874 2.89e-41

Protein tyrosine phosphatase [Signal transduction mechanisms];


Pssm-ID: 444335 [Multi-domain]  Cd Length: 282  Bit Score: 153.71  E-value: 2.89e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158138488  639 KDARKSQNQN---KNRYVDILPYDYNRVElseINGdagsTYINASYIDGfKEPRKYIAAQGPRDETVDDFWKMIWEQKAT 715
Cdd:COG5599    32 NDPQYLQNINgspLNRFRDIQPYKETALR---ANL----GYLNANYIQV-IGNHRYIATQYPLEEQLEDFFQMLFDNNTP 103

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158138488  716 VIVMVTRCEEG--NRNKCAEYWPcmEEGTRTFRDVVVTINDHKRCPDYI---IQKLSIAHKKEKatGREVTHIQFTSWPD 790
Cdd:COG5599   104 VLVVLASDDEIskPKVKMPVYFR--QDGEYGKYEVSSELTESIQLRDGIearTYVLTIKGTGQK--KIEIPVLHVKNWPD 179

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158138488  791 HGVP--EDPHLLLKLRRRVNAFSNFFSGPIVVHCSAGVGRTGTYIGIDAMLESLEAEG--KVDVYGYVVNLRRQR-CLMV 865
Cdd:COG5599   180 HGAIsaEALKNLADLIDKKEKIKDPDKLLPVVHCRAGVGRTGTLIACLALSKSINALVqiTLSVEEIVIDMRTSRnGGMV 259


                  ....*....
gi 158138488  866 QVEAQYILI 874
Cdd:COG5599   260 QTSEQLDVL 268
R-PTP-N-N2 cd14546
PTP-like domain of receptor-type tyrosine-protein phosphatase-like N and N2; Receptor-type ...
 986-1194 3.28e-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: 150.67  E-value: 3.28e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158138488  986 YINASFVMSYwKPE--MMIAAQGPLKETIGDFWQMIFQRKVKVIVMLTELMSGDQEVCAQYW-GEGKQTYGDMEVML-KD 1061
Cdd:cd14546     1 YINASTIYDH-DPRnpAYIATQGPLPHTIADFWQMIWEQGCVVIVMLTRLQENGVKQCARYWpEEGSEVYHIYEVHLvSE 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158138488 1062 TNKSSAYILRAFELRHSKRKEPRTVYQYQCTTWKGEELPAEPKDLVtliqNIKQKLPKSgsegmkYHKHAS-ILVHCRDG 1140
Cdd:cd14546    80 HIWCDDYLVRSFYLKNLQTSETRTVTQFHFLSWPDEGIPASAKPLL----EFRRKVNKS------YRGRSCpIVVHCSDG 149

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 158138488 1141 SQQTGLFCALFNLLES-AETEDVVDVFQVVKSLRKARPGMVGSFEQYQFLYDIMA 1194
Cdd:cd14546   150 AGRTGTYILIDMVLNRmAKGAKEIDIAATLEHLRDQRPGMVKTKDQFEFVLTAVA 204
R-PTPc-M-1 cd14633
catalytic domain of receptor-type tyrosine-protein phosphatase M, repeat 1; Receptor-type ...
 934-1191 3.32e-41

catalytic domain of receptor-type tyrosine-protein phosphatase M, repeat 1; Receptor-type tyrosine-protein phosphatase M (PTPRM), also known as protein-tyrosine phosphatase mu (R-PTP-mu or PTPmu), belongs to the type IIb subfamily of receptor protein tyrosine phosphatases (RPTPs), which belong to the larger family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. PTPRM/PTPmu is a homophilic cell adhesion molecule expressed in CNS neurons and glia. It is required for E-, N-, and R-cadherin-dependent neurite outgrowth. Loss of PTPmu contributes to tumor cell migration and dispersal of human glioblastomas. PTPRM contains an extracellular region with an Meprin-A5 (neuropilin)-mu (MAM) domain, an immunoglobulin (Ig) domain, and four fibronectin type III (FN3) repeats, a transmembrane domain, and an intracellular segment with a juxtamembrane domain similar to the cytoplasmic domain of classical cadherins and two tandem PTP domains. This model represents the first (repeat 1) PTP domain.


Pssm-ID: 350481 [Multi-domain]  Cd Length: 273  Bit Score: 153.27  E-value: 3.32e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158138488  934 QEENKKKNRSSNVVPYDFNRVPLKhelemskeseaesdessdeDSDSEETSKYINASFVMSYWKPEMMIAAQGPLKETIG 1013
Cdd:cd14633    37 KDENRMKNRYGNIIAYDHSRVRLQ-------------------PIEGETSSDYINGNYIDGYHRPNHYIATQGPMQETIY 97

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158138488 1014 DFWQMIFQRKVKVIVMLTELMSGDQEVCAQYWGEGKQTYGDMEVMLKDTNKSSAYILRAFELRHSKRKEPRTVYQYQCTT 1093
Cdd:cd14633    98 DFWRMVWHENTASIIMVTNLVEVGRVKCCKYWPDDTEIYKDIKVTLIETELLAEYVIRTFAVEKRGVHEIREIRQFHFTG 177

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158138488 1094 WKGEELPAEPKDLVTLIQNIKQKLPKSGsegmkyhkhASILVHCRDGSQQTGLFCALFNLLESAETEDVVDVFQVVKSLR 1173
Cdd:cd14633   178 WPDHGVPYHATGLLGFVRQVKSKSPPNA---------GPLVVHCSAGAGRTGCFIVIDIMLDMAEREGVVDIYNCVRELR 248

                         250
                  ....*....|....*...
gi 158138488 1174 KARPGMVGSFEQYQFLYD 1191
Cdd:cd14633   249 SRRVNMVQTEEQYVFIHD 266
R-PTPc-G-1 cd17667
catalytic domain of receptor-type tyrosine-protein phosphatase G, repeat 1; Receptor-type ...
 916-1193 4.48e-41

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: 152.88  E-value: 4.48e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158138488  916 EYQRLPSYRSWRTQHiGNQEENKKKNRSSNVVPYDFNRVPLKhelemskeseaesdessDEDSDSEETSKYINASFVMSY 995
Cdd:cd17667     7 EVQRCTADMNITAEH-SNHPDNKHKNRYINILAYDHSRVKLR-----------------PLPGKDSKHSDYINANYVDGY 68

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158138488  996 WKPEMMIAAQGPLKETIGDFWQMIFQRKVKVIVMLTELMSGDQEVCAQYW-GEGKQTYGDMEVMLKDTNKSSAYILRAFE 1074
Cdd:cd17667    69 NKAKAYIATQGPLKSTFEDFWRMIWEQNTGIIVMITNLVEKGRRKCDQYWpTENSEEYGNIIVTLKSTKIHACYTVRRFS 148

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158138488 1075 LRHSK-----------RKEPRTVYQYQCTTWKGEELPAEPKDLVTLI-QNIKQKLPKSGsegmkyhkhaSILVHCRDGSQ 1142
Cdd:cd17667   149 IRNTKvkkgqkgnpkgRQNERTVIQYHYTQWPDMGVPEYALPVLTFVrRSSAARTPEMG----------PVLVHCSAGVG 218

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|.
gi 158138488 1143 QTGLFCALFNLLESAETEDVVDVFQVVKSLRKARPGMVGSFEQYQFLYDIM 1193
Cdd:cd17667   219 RTGTYIVIDSMLQQIKDKSTVNVLGFLKHIRTQRNYLVQTEEQYIFIHDAL 269
PTPc-KIM cd14547
catalytic domain of the kinase interaction motif (KIM) family of protein-tyrosine phosphatases; ...
 984-1190 4.99e-41

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: 151.01  E-value: 4.99e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158138488  984 SKYINASFVMSY-WKPEMMIAAQGPLKETIGDFWQMIFQRKVKVIVMLTELMSGDQEvCAQYWGEGK-QTYGDMEVMLKD 1061
Cdd:cd14547    25 SSYINANYIRGYdGEEKAYIATQGPLPNTVADFWRMVWQEKTPIIVMITNLTEAKEK-CAQYWPEEEnETYGDFEVTVQS 103

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158138488 1062 TNKSSAYILRAFELRHskRKEPRTVYQYQCTTWKGEELPAEPKDLVTLIQNIKQkLPKSGSEgmkyhkHASILVHCRDGS 1141
Cdd:cd14547   104 VKETDGYTVRKLTLKY--GGEKRYLKHYWYTSWPDHKTPEAAQPLLSLVQEVEE-ARQTEPH------RGPIVVHCSAGI 174

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*....
gi 158138488 1142 QQTGLFCALFNLLESAETEDVVDVFQVVKSLRKARPGMVGSFEQYQFLY 1190
Cdd:cd14547   175 GRTGCFIATSIGCQQLREEGVVDVLGIVCQLRLDRGGMVQTAEQYEFVH 223
R-PTPc-F-1 cd14626
catalytic domain of receptor-type tyrosine-protein phosphatase F, repeat 1; Receptor-type ...
 892-1193 5.73e-41

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: 152.50  E-value: 5.73e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158138488  892 SELHSCLQNLKKrdppSDPSPLEAEYQRLPSYRSWrTQHIGNQEENKKKNRSSNVVPYDFNRVPLkhelemskeseaesd 971
Cdd:cd14626     1 SDLADNIERLKA----NDGLKFSQEYESIDPGQQF-TWENSNLEVNKPKNRYANVIAYDHSRVIL--------------- 60

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158138488  972 essdEDSDSEETSKYINASFVMSYWKPEMMIAAQGPLKETIGDFWQMIFQRKVKVIVMLTELMSGDQEVCAQYW-GEGKQ 1050
Cdd:cd14626    61 ----TSVDGVPGSDYINANYIDGYRKQNAYIATQGPLPETLSDFWRMVWEQRTATIVMMTRLEEKSRVKCDQYWpIRGTE 136

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158138488 1051 TYGDMEVMLKDTNKSSAYILRAFELRHSKRKEPRTVYQYQCTTWKGEELPAEPKDLVTLIQNIKQKLPKSGsegmkyhkh 1130
Cdd:cd14626   137 TYGMIQVTLLDTVELATYSVRTFALYKNGSSEKREVRQFQFMAWPDHGVPEYPTPILAFLRRVKACNPPDA--------- 207

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 158138488 1131 ASILVHCRDGSQQTGLFCALFNLLESAETEDVVDVFQVVKSLRKARPGMVGSFEQYQFLYDIM 1193
Cdd:cd14626   208 GPMVVHCSAGVGRTGCFIVIDAMLERMKHEKTVDIYGHVTCMRSQRNYMVQTEDQYIFIHEAL 270
R-PTPc-K-1 cd14631
catalytic domain of receptor-type tyrosine-protein phosphatase K, repeat 1; Receptor-type ...
 983-1191 2.89e-40

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: 148.63  E-value: 2.89e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158138488  983 TSKYINASFVMSYWKPEMMIAAQGPLKETIGDFWQMIFQRKVKVIVMLTELMSGDQEVCAQYWGEGKQTYGDMEVMLKDT 1062
Cdd:cd14631    12 SSDYINANYIDGYQRPSHYIATQGPVHETVYDFWRMIWQEQSACIVMVTNLVEVGRVKCYKYWPDDTEVYGDFKVTCVEM 91

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158138488 1063 NKSSAYILRAFELRHSKRKEPRTVYQYQCTTWKGEELPAEPKDLVTLIQNIKQKLPKSGsegmkyhkhASILVHCRDGSQ 1142
Cdd:cd14631    92 EPLAEYVVRTFTLERRGYNEIREVKQFHFTGWPDHGVPYHATGLLSFIRRVKLSNPPSA---------GPIVVHCSAGAG 162

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*....
gi 158138488 1143 QTGLFCALFNLLESAETEDVVDVFQVVKSLRKARPGMVGSFEQYQFLYD 1191
Cdd:cd14631   163 RTGCYIVIDIMLDMAEREGVVDIYNCVKALRSRRINMVQTEEQYIFIHD 211
R-PTP-N2 cd14610
PTP-like domain of receptor-type tyrosine-protein phosphatase N2; Receptor-type ...
 891-1188 3.03e-39

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: 147.90  E-value: 3.03e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158138488  891 LSELHSCLQNlKKRdppsdpspLEAEYQRLPSYRSW-RTQHIGNQEENKKKNRSSNVVPYDFNRVPLKHElemskeseae 969
Cdd:cd14610     6 LSYMEDHLKN-KNR--------LEKEWEALCAYQAEpNATNVAQREENVQKNRSLAVLPYDHSRIILKAE---------- 66

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158138488  970 sdessdedsDSEETSKYINASFVMSYwKPE--MMIAAQGPLKETIGDFWQMIFQRKVKVIVMLTELMSGDQEVCAQYW-G 1046
Cdd:cd14610    67 ---------NSHSHSDYINASPIMDH-DPRnpAYIATQGPLPATVADFWQMVWESGCVVIVMLTPLAENGVKQCYHYWpD 136

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158138488 1047 EGKQTYGDMEVMLKDTNK-SSAYILRAFELRHSKRKEPRTVYQYQCTTWKGEELPAEPKDLVtliqNIKQKLPKSgsegm 1125
Cdd:cd14610   137 EGSNLYHIYEVNLVSEHIwCEDFLVRSFYLKNLQTNETRTVTQFHFLSWNDQGVPASTRSLL----DFRRKVNKC----- 207

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 158138488 1126 kYH-KHASILVHCRDGSQQTGLFCALFNLLES-AETEDVVDVFQVVKSLRKARPGMVGSFEQYQF 1188
Cdd:cd14610   208 -YRgRSCPIIVHCSDGAGRSGTYILIDMVLNKmAKGAKEIDIAATLEHLRDQRPGMVQTKEQFEF 271
R-PTPc-Z-1 cd17668
catalytic domain of receptor-type tyrosine-protein phosphatase Z, repeat 1; Receptor-type ...
 986-1193 4.12e-39

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: 144.74  E-value: 4.12e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158138488  986 YINASFVMSYWKPEMMIAAQGPLKETIGDFWQMIFQRKVKVIVMLTELMSGDQEVCAQYW-GEGKQTYGDMEVMLKDTNK 1064
Cdd:cd17668     1 YINANYVDGYNKPKAYIAAQGPLKSTAEDFWRMIWEHNVEVIVMITNLVEKGRRKCDQYWpADGSEEYGNFLVTQKSVQV 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158138488 1065 SSAYILRAFELRHSK--------RKEPRTVYQYQCTTWKGEELPAEPKDLVTLIQNikqklpksgSEGMKYHKHASILVH 1136
Cdd:cd17668    81 LAYYTVRNFTLRNTKikkgsqkgRPSGRVVTQYHYTQWPDMGVPEYTLPVLTFVRK---------ASYAKRHAVGPVVVH 151

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 158138488 1137 CRDGSQQTGLFCALFNLLESAETEDVVDVFQVVKSLRKARPGMVGSFEQYQFLYDIM 1193
Cdd:cd17668   152 CSAGVGRTGTYIVLDSMLQQIQHEGTVNIFGFLKHIRSQRNYLVQTEEQYVFIHDAL 208
R-PTPc-U-1 cd14632
catalytic domain of receptor-type tyrosine-protein phosphatase U, repeat 1; Receptor-type ...
 986-1191 5.98e-39

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: 144.42  E-value: 5.98e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158138488  986 YINASFVMSYWKPEMMIAAQGPLKETIGDFWQMIFQRKVKVIVMLTELMSGDQEVCAQYWGEGKQTYGDMEVMLKDTNKS 1065
Cdd:cd14632     1 YINANYIDGYHRSNHFIATQGPKQEMVYDFWRMVWQEHCSSIVMITKLVEVGRVKCSKYWPDDSDTYGDIKITLLKTETL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158138488 1066 SAYILRAFELRHSKRKEPRTVYQYQCTTWKGEELPAEPKDLVTLIQNIKQKLPKSGsegmkyhkhASILVHCRDGSQQTG 1145
Cdd:cd14632    81 AEYSVRTFALERRGYSARHEVKQFHFTSWPEHGVPYHATGLLAFIRRVKASTPPDA---------GPVVVHCSAGAGRTG 151

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*.
gi 158138488 1146 LFCALFNLLESAETEDVVDVFQVVKSLRKARPGMVGSFEQYQFLYD 1191
Cdd:cd14632   152 CYIVLDVMLDMAECEGVVDIYNCVKTLCSRRINMIQTEEQYIFIHD 197
R-PTPc-D-1 cd14624
catalytic domain of receptor-type tyrosine-protein phosphatase D, repeat 1; Receptor-type ...
 903-1193 9.89e-39

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: 146.41  E-value: 9.89e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158138488  903 KRDPPSDPSPLEAEYQRLPSYRSWRTQHiGNQEENKKKNRSSNVVPYDFNRVPLKhelemskeseaesdessdeDSDSEE 982
Cdd:cd14624    14 ERLKANDNLKFSQEYESIDPGQQFTWEH-SNLEVNKPKNRYANVIAYDHSRVLLS-------------------AIEGIP 73

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158138488  983 TSKYINASFVMSYWKPEMMIAAQGPLKETIGDFWQMIFQRKVKVIVMLTELMSGDQEVCAQYW-GEGKQTYGDMEVMLKD 1061
Cdd:cd14624    74 GSDYINANYIDGYRKQNAYIATQGALPETFGDFWRMIWEQRSATVVMMTKLEERSRVKCDQYWpSRGTETYGLIQVTLLD 153

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158138488 1062 TNKSSAYILRAFELRHSKRKEPRTVYQYQCTTWKGEELPAEPKDLVTLIQNIKQKLPKSGsegmkyhkhASILVHCRDGS 1141
Cdd:cd14624   154 TVELATYCVRTFALYKNGSSEKREVRQFQFTAWPDHGVPEHPTPFLAFLRRVKTCNPPDA---------GPMVVHCSAGV 224

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|..
gi 158138488 1142 QQTGLFCALFNLLESAETEDVVDVFQVVKSLRKARPGMVGSFEQYQFLYDIM 1193
Cdd:cd14624   225 GRTGCFIVIDAMLERIKHEKTVDIYGHVTLMRAQRNYMVQTEDQYIFIHDAL 276
R-PTPc-A-E-1 cd14551
catalytic domain of receptor-type tyrosine-protein phosphatase A and E, repeat 1; ...
 986-1190 1.45e-38

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: 143.13  E-value: 1.45e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158138488  986 YINASFVMSYWKPEMMIAAQGPLKETIGDFWQMIFQRKVKVIVMLTELMSGDQEVCAQYW-GEGKQTYGDMEVMLKDTNK 1064
Cdd:cd14551     1 YINASYIDGYQEKNKFIAAQGPKDETVNDFWRMIWEQGSATIVMVTNLKERKEKKCSQYWpDQGCWTYGNLRVRVEDTVV 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158138488 1065 SSAYILRAFELRH----SKRKEPRTVYQYQCTTWKGEELPAEPKDLVTLIQNIKQKLPKsgsegmkyhKHASILVHCRDG 1140
Cdd:cd14551    81 LVDYTTRKFCIQKvnrgIGEKRVRLVTQFHFTSWPDFGVPFTPIGMLKFLKKVKSANPP---------RAGPIVVHCSAG 151

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|
gi 158138488 1141 SQQTGLFCALFNLLESAETEDVVDVFQVVKSLRKARPGMVGSFEQYQFLY 1190
Cdd:cd14551   152 VGRTGTFIVIDAMLDMMHAEGKVDVFGFVSRIRQQRSQMVQTDMQYVFIY 201
R-PTPc-C-1 cd14557
catalytic domain of receptor-type tyrosine-protein phosphatase C, repeat 1; Receptor-type ...
 986-1190 2.42e-38

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: 142.27  E-value: 2.42e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158138488  986 YINASFVMSYWKPEMMIAAQGPLKETIGDFWQMIFQRKVKVIVMLTELMSGDQEVCAQYW---GEGKQTYGDMEVMLKDT 1062
Cdd:cd14557     1 YINASYIDGFKEPRKYIAAQGPKDETVDDFWRMIWEQKSTVIVMVTRCEEGNRNKCAQYWpsmEEGSRAFGDVVVKINEE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158138488 1063 NKSSAYILRAFELRHSKRK-EPRTVYQYQCTTWKGEELPAEPKDLVTLIQNIkQKLPKSGSegmkyhkhASILVHCRDGS 1141
Cdd:cd14557    81 KICPDYIIRKLNINNKKEKgSGREVTHIQFTSWPDHGVPEDPHLLLKLRRRV-NAFNNFFS--------GPIVVHCSAGV 151

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*....
gi 158138488 1142 QQTGLFCALFNLLESAETEDVVDVFQVVKSLRKARPGMVGSFEQYQFLY 1190
Cdd:cd14557   152 GRTGTYIGIDAMLEGLEAEGRVDVYGYVVKLRRQRCLMVQVEAQYILIH 200
PTPc-N11_6 cd14544
catalytic domain of tyrosine-protein phosphatase non-receptor type 11 and type 6; ...
 937-1190 3.71e-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: 143.76  E-value: 3.71e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158138488  937 NKKKNRSSNVVPYDFNRVPLKhelemskeseaesdessdEDSDSEETSKYINASFVMSYW--KPEMM-----IAAQGPLK 1009
Cdd:cd14544     1 NKGKNRYKNILPFDHTRVILK------------------DRDPNVPGSDYINANYIRNENegPTTDEnaktyIATQGCLE 62

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158138488 1010 ETIGDFWQMIFQRKVKVIVMLTELMSGDQEVCAQYW---GEGKQtYGDMEVMLKDTNKSSAYILRAFEL-RHSKRKEPRT 1085
Cdd:cd14544    63 NTVSDFWSMVWQENSRVIVMTTKEVERGKNKCVRYWpdeGMQKQ-YGPYRVQNVSEHDTTDYTLRELQVsKLDQGDPIRE 141

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158138488 1086 VYQYQCTTWKGEELPAEPKDLVTLIQNIKQK---LPKSGsegmkyhkhaSILVHCRDGSQQTGLFCALFNLLESAETEDV 1162
Cdd:cd14544   142 IWHYQYLSWPDHGVPSDPGGVLNFLEDVNQRqesLPHAG----------PIVVHCSAGIGRTGTFIVIDMLLDQIKRKGL 211

                         250       260       270
                  ....*....|....*....|....*....|.
gi 158138488 1163 ---VDVFQVVKSLRKARPGMVGSFEQYQFLY 1190
Cdd:cd14544   212 dcdIDIQKTIQMVRSQRSGMVQTEAQYKFIY 242
R-PTPc-A-1 cd14621
catalytic domain of receptor-type tyrosine-protein phosphatase A, repeat 1; Receptor-type ...
 898-1197 5.54e-38

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: 144.78  E-value: 5.54e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158138488  898 LQNLKKRDPPSDPSPLEAEYQRLPSYRSWRTQHIGNQEENKKKNRSSNVVPYDFNRVPLkhelemskeseaesdessdED 977
Cdd:cd14621    13 LEEEINRRMADDNKLFREEFNALPACPIQATCEAASKEENKEKNRYVNILPYDHSRVHL-------------------TP 73

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158138488  978 SDSEETSKYINASFVMSYWKPEMMIAAQGPLKETIGDFWQMIFQRKVKVIVMLTELMSGDQEVCAQYW-GEGKQTYGDME 1056
Cdd:cd14621    74 VEGVPDSDYINASFINGYQEKNKFIAAQGPKEETVNDFWRMIWEQNTATIVMVTNLKERKECKCAQYWpDQGCWTYGNIR 153

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158138488 1057 VMLKDTNKSSAYILRAFELRH----SKRKEPRTVYQYQCTTWKGEELPAEPKDLVTLIQNIKQKLPKSGsegmkyhkhAS 1132
Cdd:cd14621   154 VSVEDVTVLVDYTVRKFCIQQvgdvTNKKPQRLITQFHFTSWPDFGVPFTPIGMLKFLKKVKNCNPQYA---------GA 224

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 158138488 1133 ILVHCRDGSQQTGLFCALFNLLESAETEDVVDVFQVVKSLRKARPGMVGSFEQYQFLYDIMASIY 1197
Cdd:cd14621   225 IVVHCSAGVGRTGTFIVIDAMLDMMHAERKVDVYGFVSRIRAQRCQMVQTDMQYVFIYQALLEHY 289
PTPc-N13 cd14597
catalytic domain of tyrosine-protein phosphatase non-receptor type 13; Tyrosine-protein ...
 935-1193 7.45e-38

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


Pssm-ID: 350445 [Multi-domain]  Cd Length: 234  Bit Score: 142.28  E-value: 7.45e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158138488  935 EENKKKNRSSNVVPYDFNRVPLKHElemskeseaesdessdedsdseetSKYINASFV-MSYWKPEMM-IAAQGPLKETI 1012
Cdd:cd14597     1 KENRKKNRYKNILPYDTTRVPLGDE------------------------GGYINASFIkMPVGDEEFVyIACQGPLPTTV 56

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158138488 1013 GDFWQMIFQRKVKVIVMLTELMSGDQEVCAQYWGE--GKQTYGD--MEVMLKDTNKSSAYILRAFELRHSKRKEPRTVYQ 1088
Cdd:cd14597    57 ADFWQMVWEQKSTVIAMMTQEVEGGKIKCQRYWPEilGKTTMVDnrLQLTLVRMQQLKNFVIRVLELEDIQTREVRHITH 136

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158138488 1089 YQCTTWKGEELPAEPKDLVTLIQNIKQklpksgsegmkYHKHASILVHCRDGSQQTGLFCALFNLLESAETEDVVDVFQV 1168
Cdd:cd14597   137 LNFTAWPDHDTPSQPEQLLTFISYMRH-----------IHKSGPIITHCSAGIGRSGTLICIDVVLGLISKDLDFDISDI 205

                         250       260
                  ....*....|....*....|....*
gi 158138488 1169 VKSLRKARPGMVGSFEQYQFLYDIM 1193
Cdd:cd14597   206 VRTMRLQRHGMVQTEDQYIFCYQVI 230
PTPc_DSPc smart00012
Protein tyrosine phosphatase, catalytic domain, undefined specificity; Protein tyrosine ...
 779-880 1.20e-37

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


Pssm-ID: 214469 [Multi-domain]  Cd Length: 105  Bit Score: 136.72  E-value: 1.20e-37
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158138488    779 EVTHIQFTSWPDHGVPEDPHLLLKLRRRVNAFSNF--FSGPIVVHCSAGVGRTGTYIGIDAMLESLEAE-GKVDVYGYVV 855
Cdd:smart00012    1 TVKHYHYTGWPDHGVPESPDSILELLRAVKKNLNQseSSGPVVVHCSAGVGRTGTFVAIDILLQQLEAEaGEVDIFDTVK 80

                            90       100
                    ....*....|....*....|....*
gi 158138488    856 NLRRQRCLMVQVEAQYILIHQALVE 880
Cdd:smart00012   81 ELRSQRPGMVQTEEQYLFLYRALLE 105
PTPc_motif smart00404
Protein tyrosine phosphatase, catalytic domain motif;
779-880 1.20e-37

Protein tyrosine phosphatase, catalytic domain motif;


Pssm-ID: 214649 [Multi-domain]  Cd Length: 105  Bit Score: 136.72  E-value: 1.20e-37
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158138488    779 EVTHIQFTSWPDHGVPEDPHLLLKLRRRVNAFSNF--FSGPIVVHCSAGVGRTGTYIGIDAMLESLEAE-GKVDVYGYVV 855
Cdd:smart00404    1 TVKHYHYTGWPDHGVPESPDSILELLRAVKKNLNQseSSGPVVVHCSAGVGRTGTFVAIDILLQQLEAEaGEVDIFDTVK 80

                            90       100
                    ....*....|....*....|....*
gi 158138488    856 NLRRQRCLMVQVEAQYILIHQALVE 880
Cdd:smart00404   81 ELRSQRPGMVQTEEQYLFLYRALLE 105
R-PTPc-E-1 cd14620
catalytic domain of receptor-type tyrosine-protein phosphatase E, repeat 1; Receptor-type ...
 945-1190 2.07e-37

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: 140.85  E-value: 2.07e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158138488  945 NVVPYDFNRVPLKHelemskeseaesdessdedSDSEETSKYINASFVMSYWKPEMMIAAQGPLKETIGDFWQMIFQRKV 1024
Cdd:cd14620     3 NILPYDHSRVILSQ-------------------LDGIPCSDYINASYIDGYKEKNKFIAAQGPKQETVNDFWRMVWEQKS 63

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158138488 1025 KVIVMLTELMSGDQEVCAQYWGE-GKQTYGDMEVMLKDTNKSSAYILRAFELR---HSKRKEPRTVYQYQCTTWKGEELP 1100
Cdd:cd14620    64 ATIVMLTNLKERKEEKCYQYWPDqGCWTYGNIRVAVEDCVVLVDYTIRKFCIQpqlPDGCKAPRLVTQLHFTSWPDFGVP 143

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158138488 1101 AEPKDLVTLIQNIKQKLPksgsegmkyhKHAS-ILVHCRDGSQQTGLFCALFNLLESAETEDVVDVFQVVKSLRKARPGM 1179
Cdd:cd14620   144 FTPIGMLKFLKKVKSVNP----------VHAGpIVVHCSAGVGRTGTFIVIDAMIDMMHAEQKVDVFEFVSRIRNQRPQM 213

                         250
                  ....*....|.
gi 158138488 1180 VGSFEQYQFLY 1190
Cdd:cd14620   214 VQTDMQYSFIY 224
R-PTPc-O cd14614
catalytic domain of receptor-type tyrosine-protein phosphatase O; Receptor-type ...
 937-1190 8.53e-37

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: 139.64  E-value: 8.53e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158138488  937 NKKKNRSSNVVPYDFNRVPL--KHELEmskeseaesdessdedsdseeTSKYINASFVMSYWKPEMMIAAQGPLKETIGD 1014
Cdd:cd14614    12 NRCKNRYTNILPYDFSRVKLvsMHEEE---------------------GSDYINANYIPGYNSPQEYIATQGPLPETRND 70

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158138488 1015 FWQMIFQRKVKVIVMLTELMSGDQEVCAQYW--GEGKQTYGDMEVMLKDTNKSSAYILRAFELRHSkrKEPRTVYQYQCT 1092
Cdd:cd14614    71 FWKMVLQQKSQIIVMLTQCNEKRRVKCDHYWpfTEEPVAYGDITVEMLSEEEQPDWAIREFRVSYA--DEVQDVMHFNYT 148

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158138488 1093 TWKGEELPA--EPKDLVTLIQNIKQKLPKSgsegmkyhkHASILVHCRDGSQQTGLFCALFNLLESAETEDVVDVFQVVK 1170
Cdd:cd14614   149 AWPDHGVPTanAAESILQFVQMVRQQAVKS---------KGPMIIHCSAGVGRTGTFIALDRLLQHIRDHEFVDILGLVS 219

                         250       260
                  ....*....|....*....|
gi 158138488 1171 SLRKARPGMVGSFEQYQFLY 1190
Cdd:cd14614   220 EMRSYRMSMVQTEEQYIFIH 239
PTPc-N12 cd14604
catalytic domain of tyrosine-protein phosphatase non-receptor type 12; Tyrosine-protein ...
 898-1200 9.22e-37

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: 141.22  E-value: 9.22e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158138488  898 LQNLKKRDPPSDPSpLEAEYQRLPSYRS-WRTQHI-----GNQEENKKKNRSSNVVPYDFNRVPLKHELEmskeseaesd 971
Cdd:cd14604    13 VQAMKSTDHNGEDN-FASDFMRLRRLSTkYRTEKIyptatGEKEENVKKNRYKDILPFDHSRVKLTLKTS---------- 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158138488  972 essdedsdsEETSKYINASFVMSYWKPEMMIAAQGPLKETIGDFWQMIFQRKVKVIVMLTELMSGDQEVCAQYW---GEG 1048
Cdd:cd14604    82 ---------SQDSDYINANFIKGVYGPKAYIATQGPLANTVIDFWRMIWEYNVAIIVMACREFEMGRKKCERYWplyGEE 152

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158138488 1049 KQTYGDMEVMLKDTNKSSAYILRAFELRHskRKEPRTVYQYQCTTWKGEELPAEPKDLVTLIQNIKQklpksgsegMKYH 1128
Cdd:cd14604   153 PMTFGPFRISCEAEQARTDYFIRTLLLEF--QNETRRLYQFHYVNWPDHDVPSSFDSILDMISLMRK---------YQEH 221

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 158138488 1129 KHASILVHCRDGSQQTGLFCAL---FNLLESAETEDVVDVFQVVKSLRKARPGMVGSFEQYQFLYDIMASIYPTQ 1200
Cdd:cd14604   222 EDVPICIHCSAGCGRTGAICAIdytWNLLKAGKIPEEFNVFNLIQEMRTQRHSAVQTKEQYELVHRAIAQLFEKQ 296
R-PTP-N cd14609
PTP-like domain of receptor-type tyrosine-protein phosphatase N; Receptor-type ...
 900-1188 1.77e-36

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: 139.79  E-value: 1.77e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158138488  900 NLKKRDPpsdpspLEAEYQRLPSYRSW-RTQHIGNQEENKKKNRSSNVVPYDFNRVPLKHELEmskeseaesdessdeds 978
Cdd:cd14609    10 HLRNRDR------LAKEWQALCAYQAEpNTCSTAQGEANVKKNRNPDFVPYDHARIKLKAESN----------------- 66

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158138488  979 dsEETSKYINASFVMSYwKPEM--MIAAQGPLKETIGDFWQMIFQRKVKVIVMLTELMSGDQEVCAQYW-GEGKQTYGDM 1055
Cdd:cd14609    67 --PSRSDYINASPIIEH-DPRMpaYIATQGPLSHTIADFWQMVWENGCTVIVMLTPLVEDGVKQCDRYWpDEGSSLYHIY 143

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158138488 1056 EVMLKDTNK-SSAYILRAFELRHSKRKEPRTVYQYQCTTWKGEELPAEPKDLVtliqNIKQKLPKSgsegmkYH-KHASI 1133
Cdd:cd14609   144 EVNLVSEHIwCEDFLVRSFYLKNVQTQETRTLTQFHFLSWPAEGIPSSTRPLL----DFRRKVNKC------YRgRSCPI 213

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 158138488 1134 LVHCRDGSQQTGLFCALFNLLES-AETEDVVDVFQVVKSLRKARPGMVGSFEQYQF 1188
Cdd:cd14609   214 IVHCSDGAGRTGTYILIDMVLNRmAKGVKEIDIAATLEHVRDQRPGMVRTKDQFEF 269
PTPc-N7 cd14612
catalytic domain of tyrosine-protein phosphatase non-receptor type 7; Tyrosine-protein ...
 983-1194 5.58e-36

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: 137.27  E-value: 5.58e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158138488  983 TSKYINASFVMSY-WKPEMMIAAQGPLKETIGDFWQMIFQRKVKVIVMLTELMSGdQEVCAQYWGEGKQTYGDMEVMLKD 1061
Cdd:cd14612    43 EGSYINANYIRGYdGKEKAYIATQGPMLNTVSDFWEMVWQEECPIIVMITKLKEK-KEKCVHYWPEKEGTYGRFEIRVQD 121

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158138488 1062 TNKSSAYILRAFELRHSkrKEPRTVYQYQCTTWKGEELPAEPKDLVTLIQNIKQKLPKSGSEGmkyhkhaSILVHCRDGS 1141
Cdd:cd14612   122 MKECDGYTIRDLTIQLE--EESRSVKHYWFSSWPDHQTPESAGPLLRLVAEVEESRQTAASPG-------PIVVHCSAGI 192

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 158138488 1142 QQTGLFCALFNLLESAETEDVVDVFQVVKSLRKARPGMVGSFEQYQFLYDIMA 1194
Cdd:cd14612   193 GRTGCFIATSIGCQQLKDTGKVDILGIVCQLRLDRGGMIQTSEQYQFLHHTLA 245
R-PTPc-typeIIb-2 cd14556
PTP domain of type IIb (or R2B) subfamily receptor-type tyrosine-protein phosphatases, repeat ...
 676-876 5.60e-36

PTP domain of type IIb (or R2B) subfamily receptor-type tyrosine-protein phosphatases, repeat 2; The type IIb (or R2B) subfamily of receptor protein tyrosine phosphatases (RPTPs) include the prototypical member PTPmu (or PTPRM), PCP-2 (or PTPRU), PTPrho (or PTPRT), and PTPkappa (or PTPRK). They belong to the larger family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. Type IIb RPTPs mediate cell-cell adhesion though homophilic interactions; their ligand is an identical molecule on an adjacent cell. No heterophilic interactions between the subfamily members have been observed. They also commonly function as tumor suppressors. They contain an extracellular region with an Meprin-A5 (neuropilin)-mu (MAM) domain, an immunoglobulin (Ig) domain, and four fibronectin type III (FN3) repeats, a transmembrane domain, and an intracellular segment with a juxtamembrane domain similar to the cytoplasmic domain of classical cadherins and two tandem PTP domains. This model represents the second (repeat 2) PTP domain.


Pssm-ID: 350404 [Multi-domain]  Cd Length: 201  Bit Score: 135.61  E-value: 5.60e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158138488  676 YINASYIDGFKEPRKYIAAQGPRDETVDDFWKMIWEQKATVIVMVTRCEEGNRNkCAEYWPcmEEGTRTFRDVVVTINDH 755
Cdd:cd14556     1 YINAALLDSYKQPAAFIVTQHPLPNTVTDFWRLVYDYGCTSIVMLNQLDPKDQS-CPQYWP--DEGSGTYGPIQVEFVST 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158138488  756 KRCPDYIIQKLSIAHKKEKATG-REVTHIQFTSWPDHG-VPEDPHLLLKLRRRVNA-FSNFFSGPIVVHCSAGVGRTGTY 832
Cdd:cd14556    78 TIDEDVISRIFRLQNTTRPQEGyRMVQQFQFLGWPRDRdTPPSKRALLKLLSEVEKwQEQSGEGPIVVHCLNGVGRSGVF 157

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....
gi 158138488  833 IGIDAMLESLEAEGKVDVYGYVVNLRRQRCLMVQVEAQYILIHQ 876
Cdd:cd14556   158 CAISSVCERIKVENVVDVFQAVKTLRNHRPNMVETEEQYKFCYD 201
PTPc-N11 cd14605
catalytic domain of tyrosine-protein phosphatase non-receptor type 11; Tyrosine-protein ...
 936-1190 1.38e-35

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: 136.30  E-value: 1.38e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158138488  936 ENKKKNRSSNVVPYDFNRVPLkHELEMSKEseaesdessdedsdseeTSKYINASFVMSYW-------KPEM-MIAAQGP 1007
Cdd:cd14605     1 ENKNKNRYKNILPFDHTRVVL-HDGDPNEP-----------------VSDYINANIIMPEFetkcnnsKPKKsYIATQGC 62

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158138488 1008 LKETIGDFWQMIFQRKVKVIVMLTELMSGDQEVCAQYWGE--GKQTYGDMEVMLKDTNKSSAYILRafELRHSKRKE--- 1082
Cdd:cd14605    63 LQNTVNDFWRMVFQENSRVIVMTTKEVERGKSKCVKYWPDeyALKEYGVMRVRNVKESAAHDYILR--ELKLSKVGQgnt 140

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158138488 1083 PRTVYQYQCTTWKGEELPAEPKDLVTLIQNIKQKlpksgSEGMKyhKHASILVHCRDGSQQTGLFCALFNLLESAETEDV 1162
Cdd:cd14605   141 ERTVWQYHFRTWPDHGVPSDPGGVLDFLEEVHHK-----QESIM--DAGPVVVHCSAGIGRTGTFIVIDILIDIIREKGV 213

                         250       260       270
                  ....*....|....*....|....*....|.
gi 158138488 1163 ---VDVFQVVKSLRKARPGMVGSFEQYQFLY 1190
Cdd:cd14605   214 dcdIDVPKTIQMVRSQRSGMVQTEAQYRFIY 244
PTPc-N22_18_12 cd14542
catalytic domain of tyrosine-protein phosphatase non-receptor type 22, type 18 and type 12; ...
 986-1190 2.26e-35

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: 133.70  E-value: 2.26e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158138488  986 YINASFVMSYWKPEMMIAAQGPLKETIGDFWQMIFQRKVKVIVML-TELMSGDQEvCAQYW---GEGKQTYGDMEVML-K 1060
Cdd:cd14542     1 YINANFIKGVSGSKAYIATQGPLPNTVLDFWRMIWEYNVQVIVMAcREFEMGKKK-CERYWpeeGEEQLQFGPFKISLeK 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158138488 1061 DTNKSSAYILRAFELRHSkrKEPRTVYQYQCTTWKGEELPAEPKDLVTLIQNIKqKLPKSGSEgmkyhkhaSILVHCRDG 1140
Cdd:cd14542    80 EKRVGPDFLIRTLKVTFQ--KESRTVYQFHYTAWPDHGVPSSVDPILDLVRLVR-DYQGSEDV--------PICVHCSAG 148

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 158138488 1141 SQQTGLFCAL---FNLLESAETEDVVDVFQVVKSLRKARPGMVGSFEQYQFLY 1190
Cdd:cd14542   149 CGRTGTICAIdyvWNLLKTGKIPEEFSLFDLVREMRKQRPAMVQTKEQYELVY 201
PTPc-N18 cd14603
catalytic domain of tyrosine-protein phosphatase non-receptor type 18; Tyrosine-protein ...
 928-1197 9.85e-35

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: 134.18  E-value: 9.85e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158138488  928 TQHIGNQEENKKKNRSSNVVPYDFNRV---PLKHELEmskeseaesdessdedsdseetSKYINASFVMSYWKPEMMIAA 1004
Cdd:cd14603    21 STVAGGRKENVKKNRYKDILPYDQTRVilsLLQEEGH----------------------SDYINANFIKGVDGSRAYIAT 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158138488 1005 QGPLKETIGDFWQMIFQRKVKVIVMLTELMSGDQEVCAQYWGEGKQT--YGDMEV-MLKDTNKSSAYILRAfeLRHSKRK 1081
Cdd:cd14603    79 QGPLSHTVLDFWRMIWQYGVKVILMACREIEMGKKKCERYWAQEQEPlqTGPFTItLVKEKRLNEEVILRT--LKVTFQK 156

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158138488 1082 EPRTVYQYQCTTWKGEELPAEPKDLVTLIQNIKQklpKSGSEgmkyhkHASILVHCRDGSQQTGLFCAL---FNLLESAE 1158
Cdd:cd14603   157 ESRSVSHFQYMAWPDHGIPDSPDCMLAMIELARR---LQGSG------PEPLCVHCSAGCGRTGVICTVdyvRQLLLTQR 227

                         250       260       270
                  ....*....|....*....|....*....|....*....
gi 158138488 1159 TEDVVDVFQVVKSLRKARPGMVGSFEQYQFLYDIMASIY 1197
Cdd:cd14603   228 IPPDFSIFDVVLEMRKQRPAAVQTEEQYEFLYHTVAQMF 266
PTPc-N20_13 cd14538
catalytic domain of tyrosine-protein phosphatase non-receptor type 20 and type 13; ...
 986-1192 1.13e-34

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: 132.11  E-value: 1.13e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158138488  986 YINASFV--------MSYwkpemmIAAQGPLKETIGDFWQMIFQRKVKVIVMLTELMSGDQEVCAQYWGEGKQT----YG 1053
Cdd:cd14538     1 YINASHIripvggdtYHY------IACQGPLPNTTGDFWQMVWEQKSEVIAMVTQDVEGGKVKCHRYWPDSLNKplicGG 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158138488 1054 DMEVMLKDTNKSSAYILRAFELRHSKRKEPRTVYQYQCTTWKGEELPAEPKDLVTLIQNIKqklpksgsegmKYHKHASI 1133
Cdd:cd14538    75 RLEVSLEKYQSLQDFVIRRISLRDKETGEVHHITHLNFTTWPDHGTPQSADPLLRFIRYMR-----------RIHNSGPI 143

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 158138488 1134 LVHCRDGSQQTGLFCALFNLLESAETEDVVDVFQVVKSLRKARPGMVGSFEQYQFLYDI 1192
Cdd:cd14538   144 VVHCSAGIGRTGVLITIDVALGLIERDLPFDIQDIVKDLREQRQGMIQTKDQYIFCYKA 202
PTPc-N5 cd14613
catalytic domain of tyrosine-protein phosphatase non-receptor type 5; Tyrosine-protein ...
 939-1197 2.58e-34

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: 132.68  E-value: 2.58e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158138488  939 KKNRSSNVVPYDFNRVPLKHELEmskeseaesdessdedsdSEETSKYINASFVMSYWKPE-MMIAAQGPLKETIGDFWQ 1017
Cdd:cd14613    27 RKNRYKTILPNPHSRVCLTSPDQ------------------DDPLSSYINANYIRGYGGEEkVYIATQGPTVNTVGDFWR 88

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158138488 1018 MIFQRKVKVIVMLTELMSGDqEVCAQYWGEGKQTYGDMEVMLKDTNKSSAYILRAFELRhsKRKEPRTVYQYQCTTWKGE 1097
Cdd:cd14613    89 MVWQERSPIIVMITNIEEMN-EKCTEYWPEEQVTYEGIEITVKQVIHADDYRLRLITLK--SGGEERGLKHYWYTSWPDQ 165

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158138488 1098 ELPAEPKDLVTLIQNIKQKLPKSGSegmkyhKHASILVHCRDGSQQTGLFCALFNLLESAETEDVVDVFQVVKSLRKARP 1177
Cdd:cd14613   166 KTPDNAPPLLQLVQEVEEARQQAEP------NCGPVIVHCSAGIGRTGCFIATSICCKQLRNEGVVDILRTTCQLRLDRG 239

                         250       260
                  ....*....|....*....|
gi 158138488 1178 GMVGSFEQYQFLYDIMaSIY 1197
Cdd:cd14613   240 GMIQTCEQYQFVHHVL-SLY 258
PTPc-N6 cd14606
catalytic domain of tyrosine-protein phosphatase non-receptor type 6; Tyrosine-protein ...
 929-1190 2.59e-34

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


Pssm-ID: 350454 [Multi-domain]  Cd Length: 266  Bit Score: 133.08  E-value: 2.59e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158138488  929 QHIGNQEENKKKNRSSNVVPYDFNRVPLKhelemskeseaesdessdEDSDSEETSKYINASFVMSYW-----KPEMMIA 1003
Cdd:cd14606    10 RLEGQRPENKSKNRYKNILPFDHSRVILQ------------------GRDSNIPGSDYINANYVKNQLlgpdeNAKTYIA 71

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158138488 1004 AQGPLKETIGDFWQMIFQRKVKVIVMLTELMSGDQEVCAQYWGE--GKQTYGDMEVMLKDTNKSSAYILRAFELRHSKRK 1081
Cdd:cd14606    72 SQGCLEATVNDFWQMAWQENSRVIVMTTREVEKGRNKCVPYWPEvgMQRAYGPYSVTNCGEHDTTEYKLRTLQVSPLDNG 151

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158138488 1082 E-PRTVYQYQCTTWKGEELPAEPKDLVTLIQNIKQK---LPKSGsegmkyhkhaSILVHCRDGSQQTGLFCALFNLLESA 1157
Cdd:cd14606   152 ElIREIWHYQYLSWPDHGVPSEPGGVLSFLDQINQRqesLPHAG----------PIIVHCSAGIGRTGTIIVIDMLMENI 221

                         250       260       270
                  ....*....|....*....|....*....|....*.
gi 158138488 1158 ETEDV---VDVFQVVKSLRKARPGMVGSFEQYQFLY 1190
Cdd:cd14606   222 STKGLdcdIDIQKTIQMVRAQRSGMVQTEAQYKFIY 257
R-PTPc-Q cd14616
catalytic domain of receptor-type tyrosine-protein phosphatase Q; Receptor-type ...
 941-1190 2.85e-34

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: 131.57  E-value: 2.85e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158138488  941 NRSSNVVPYDFNRVPLKHElemskeseaesdessdedsDSEETSKYINASFVMSYWKPEMMIAAQGPLKETIGDFWQMIF 1020
Cdd:cd14616     1 NRFPNIKPYNNNRVKLIAD-------------------AGVPGSDYINASYISGYLCPNEFIATQGPLPGTVGDFWRMVW 61

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158138488 1021 QRKVKVIVMLTELMSGDQEVCAQYWGEGKQ---TYGDMEVMLKDTNKSSAYILRafELRHSKRKEPRTVYQYQCTTWKGE 1097
Cdd:cd14616    62 ETRAKTIVMLTQCFEKGRIRCHQYWPEDNKpvtVFGDIVITKLMEDVQIDWTIR--DLKIERHGDYMMVRQCNFTSWPEH 139

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158138488 1098 ELPAEPKDLVTLIQNIKQKlpksgsegmKYHKHASILVHCRDGSQQTGLFCALFNLLESAETEDVVDVFQVVKSLRKARP 1177
Cdd:cd14616   140 GVPESSAPLIHFVKLVRAS---------RAHDNTPMIVHCSAGVGRTGVFIALDHLTQHINDHDFVDIYGLVAELRSERM 210

                         250
                  ....*....|...
gi 158138488 1178 GMVGSFEQYQFLY 1190
Cdd:cd14616   211 CMVQNLAQYIFLH 223
PTPc-N21_14 cd14540
catalytic domain of tyrosine-protein phosphatase non-receptor type 21 and type 14; ...
 986-1193 5.92e-34

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: 130.27  E-value: 5.92e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158138488  986 YINASFV-MSYWKPEMM-IAAQGPLKETIGDFWQMIFQRKVKVIVMLTELMSGDQEVCAQYW-----GEGKQTYGDMEVM 1058
Cdd:cd14540     1 YINASHItATVGGKQRFyIAAQGPLQNTVGDFWQMVWEQGVYLVVMVTAEEEGGREKCFRYWptlggEHDALTFGEYKVS 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158138488 1059 LKDTNKSSAYILRAFELRHSKRKEPRTVYQYQCTTWKGEELPAEPKDLVTLIQNIKQKLPKSGSEGMKYHKHASILVHCR 1138
Cdd:cd14540    81 TKFSVSSGCYTTTGLRVKHTLSGQSRTVWHLQYTDWPDHGCPEDVSGFLDFLEEINSVRRHTNQDVAGHNRNPPTLVHCS 160

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 158138488 1139 DGSQQTG--LFCALfnLLESAETEDVVDVFQVVKSLRKARPGMVGSFEQYQFLYDIM 1193
Cdd:cd14540   161 AGVGRTGvvILADL--MLYCLDHNEELDIPRVLALLRHQRMLLVQTLAQYKFVYNVL 215
R-PTPc-R cd14611
catalytic domain of receptor-type tyrosine-protein phosphatase R; Receptor-type ...
 940-1190 1.03e-33

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: 130.04  E-value: 1.03e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158138488  940 KNRSSNVVPYDFNRVPLKhelemskeseaesdessdEDSDSEETSKYINASFVMSYW-KPEMMIAAQGPLKETIGDFWQM 1018
Cdd:cd14611     2 KNRYKTILPNPHSRVCLK------------------PKNSNDSLSTYINANYIRGYGgKEKAFIATQGPMINTVNDFWQM 63

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158138488 1019 IFQRKVKVIVMLTELMSGDqEVCAQYWGEGKQTYGDMEVMLKDTNKSSAYILRAFELRHSKRKepRTVYQYQCTTWKGEE 1098
Cdd:cd14611    64 VWQEDSPVIVMITKLKEKN-EKCVLYWPEKRGIYGKVEVLVNSVKECDNYTIRNLTLKQGSQS--RSVKHYWYTSWPDHK 140

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158138488 1099 LPAEPKDLVTLIQNIKQKLPKSGSEGmkyhkhaSILVHCRDGSQQTGLFCALFNLLESAETEDVVDVFQVVKSLRKARPG 1178
Cdd:cd14611   141 TPDSAQPLLQLMLDVEEDRLASPGRG-------PVVVHCSAGIGRTGCFIATTIGCQQLKEEGVVDVLSIVCQLRVDRGG 213

                         250
                  ....*....|..
gi 158138488 1179 MVGSFEQYQFLY 1190
Cdd:cd14611   214 MVQTSEQYEFVH 225
PTPc-N1_2 cd14545
catalytic domain of tyrosine-protein phosphatase non-receptor type 1 and type 2; ...
 940-1190 1.05e-33

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: 130.20  E-value: 1.05e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158138488  940 KNRSSNVVPYDFNRVPLKHELEmskeseaesdessdedsdseeTSKYINASFVMSYWKPEMMIAAQGPLKETIGDFWQMI 1019
Cdd:cd14545     1 LNRYRDRDPYDHDRSRVKLKQG---------------------DNDYINASLVEVEEAKRSYILTQGPLPNTSGHFWQMV 59

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158138488 1020 FQRKVKVIVMLTELMSGDQEVCAQYWGEGKQTYGDME-----VMLKDTNKSSAYILRAFELRHSKRKEPRTVYQYQCTTW 1094
Cdd:cd14545    60 WEQNSKAVIMLNKLMEKGQIKCAQYWPQGEGNAMIFEdtglkVTLLSEEDKSYYTVRTLELENLKTQETREVLHFHYTTW 139

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158138488 1095 KGEELPAEPKDLVTLIQNIKQklpkSGSEGmkyHKHASILVHCRDGSQQTGLFCALFNLLESAETEDV--VDVFQVVKSL 1172
Cdd:cd14545   140 PDFGVPESPAAFLNFLQKVRE----SGSLS---SDVGPPVVHCSAGIGRSGTFCLVDTCLVLIEKGNPssVDVKKVLLEM 212

                         250
                  ....*....|....*...
gi 158138488 1173 RKARPGMVGSFEQYQFLY 1190
Cdd:cd14545   213 RKYRMGLIQTPDQLRFSY 230
PTP-N23 cd14539
PTP-like domain of tyrosine-protein phosphatase non-receptor type 23; Tyrosine-protein ...
 986-1191 3.89e-33

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: 127.50  E-value: 3.89e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158138488  986 YINASFV--MSYWKPEMmIAAQGPLKETIGDFWQMIFQRKVKVIVMLTELMSGDQEVCAQYWGEGK---QTYGDMEVMLK 1060
Cdd:cd14539     1 YINASLIedLTPYCPRF-IATQAPLPGTAADFWLMVYEQQVSVIVMLVSEQENEKQKVHRYWPTERgqaLVYGAITVSLQ 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158138488 1061 DTNKSSAYILRAFELRHSKRKEPRTVYQYQCTTWKGEELPAEPKDLVTLIQNIKQKLPKSGSEgmkyhkHASILVHCRDG 1140
Cdd:cd14539    80 SVRTTPTHVERIISIQHKDTRLSRSVVHLQFTTWPELGLPDSPNPLLRFIEEVHSHYLQQRSL------QTPIVVHCSSG 153

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 158138488 1141 SQQTGLFCALFN-LLESAETEDVVDVFQVVKSLRKARPGMVGSFEQYQFLYD 1191
Cdd:cd14539   154 VGRTGAFCLLYAaVQEIEAGNGIPDLPQLVRKMRQQRKYMLQEKEHLKFCYE 205
PTPc-N22 cd14602
catalytic domain of tyrosine-protein phosphatase non-receptor type 22; Tyrosine-protein ...
 940-1191 4.27e-33

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: 128.42  E-value: 4.27e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158138488  940 KNRSSNVVPYDFNRVPLKhelemskeseaesdessdeDSDSEETSKYINASFVMSYWKPEMMIAAQGPLKETIGDFWQMI 1019
Cdd:cd14602     1 KNRYKDILPYDHSRVELS-------------------LITSDEDSDYINANFIKGVYGPRAYIATQGPLSTTLLDFWRMI 61

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158138488 1020 FQRKVKVIVMLTELMSGDQEVCAQYW---GEGKQTYGDMEVMLKDTNKSSAYILRAfeLRHSKRKEPRTVYQYQCTTWKG 1096
Cdd:cd14602    62 WEYSVLIIVMACMEFEMGKKKCERYWaepGEMQLEFGPFSVTCEAEKRKSDYIIRT--LKVKFNSETRTIYQFHYKNWPD 139

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158138488 1097 EELPAEPKDLVTLIQNIKQklpksgsegmkYHKHAS--ILVHCRDGSQQTGLFCAL---FNLLESAETEDVVDVFQVVKS 1171
Cdd:cd14602   140 HDVPSSIDPILELIWDVRC-----------YQEDDSvpICIHCSAGCGRTGVICAIdytWMLLKDGIIPENFSVFSLIQE 208

                         250       260
                  ....*....|....*....|
gi 158138488 1172 LRKARPGMVGSFEQYQFLYD 1191
Cdd:cd14602   209 MRTQRPSLVQTKEQYELVYN 228
PHA02747 PHA02747
protein tyrosine phosphatase; Provisional
 936-1189 5.03e-33

protein tyrosine phosphatase; Provisional


Pssm-ID: 165114 [Multi-domain]  Cd Length: 312  Bit Score: 130.51  E-value: 5.03e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158138488  936 ENKKKNRSSNVVPYDFNRVPLKhelemskeseaesdessdedSDSEETSKYINASFVMSYWKPEMMIAAQGPLKETIGDF 1015
Cdd:PHA02747   50 ENQPKNRYWDIPCWDHNRVILD--------------------SGGGSTSDYIHANWIDGFEDDKKFIATQGPFAETCADF 109

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158138488 1016 WQMIFQRKVKVIVML--TELMSGdQEVCAQYWGEGKQTYGDMEVMLKDTNKSSA---YILRAFELRHSKRKEPRTVYQYQ 1090
Cdd:PHA02747  110 WKAVWQEHCSIIVMLtpTKGTNG-EEKCYQYWCLNEDGNIDMEDFRIETLKTSVrakYILTLIEITDKILKDSRKISHFQ 188

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158138488 1091 CTTWKGEELPAEPKDLVTLIQNIKQKLPKSGSE-GMKYHKHASILVHCRDGSQQTGLFCALFNLLESAETEDVVDVFQVV 1169
Cdd:PHA02747  189 CSEWFEDETPSDHPDFIKFIKIIDINRKKSGKLfNPKDALLCPIVVHCSDGVGKTGIFCAVDICLNQLVKRKAICLAKTA 268

                         250       260
                  ....*....|....*....|
gi 158138488 1170 KSLRKARPGMVGSFEQYQFL 1189
Cdd:PHA02747  269 EKIREQRHAGIMNFDDYLFI 288
R-PTPc-K-2 cd14636
PTP domain of receptor-type tyrosine-protein phosphatase K, repeat 2; Receptor-type ...
 986-1192 2.67e-32

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: 125.14  E-value: 2.67e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158138488  986 YINASFVMSYWKPEMMIAAQGPLKETIGDFWQMIFQRKVKVIVMLTE--LMSGdqevCAQYW-GEGKQTYGDMEVMLKDT 1062
Cdd:cd14636     1 YINAALMDSYRQPAAFIVTQHPLPNTVKDFWRLVYDYGCTSIVMLNEvdLAQG----CPQYWpEEGMLRYGPIQVECMSC 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158138488 1063 NKSSAYILRAFELRHSKRKEP--RTVYQYQCTTWKGE-ELPAEPKDLVTLIQNIkQKLPKSGSEGmkyhkHASILVHCRD 1139
Cdd:cd14636    77 SMDCDVISRIFRICNLTRPQEgyLMVQQFQYLGWASHrEVPGSKRSFLKLILQV-EKWQEECDEG-----EGRTIIHCLN 150

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 158138488 1140 GSQQTGLFCALFNLLESAETEDVVDVFQVVKSLRKARPGMVGSFEQYQFLYDI 1192
Cdd:cd14636   151 GGGRSGMFCAISIVCEMIKRQNVVDVFHAVKTLRNSKPNMVETPEQYRFCYDV 203
R-PTPc-T-2 cd14634
PTP domain of receptor-type tyrosine-protein phosphatase T, repeat 2; Receptor-type ...
 986-1192 8.11e-32

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: 123.98  E-value: 8.11e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158138488  986 YINASFVMSYWKPEMMIAAQGPLKETIGDFWQMIFQRKVKVIVMLTELMSGdqEVCAQYWGEGKQ-TYGDMEVMLKDTNK 1064
Cdd:cd14634     1 YINAALMDSHKQPAAFIVTQHPLPNTVADFWRLVFDYNCSSVVMLNEMDAA--QLCMQYWPEKTScCYGPIQVEFVSADI 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158138488 1065 SSAYILRAFELRHSKRKEP--RTVYQYQCTTWKG-EELPAEPKDLVTLIQNI-KQKLPKSGSEGmkyhkhaSILVHCRDG 1140
Cdd:cd14634    79 DEDIISRIFRICNMARPQDgyRIVQHLQYIGWPAyRDTPPSKRSILKVVRRLeKWQEQYDGREG-------RTVVHCLNG 151

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 158138488 1141 SQQTGLFCALFNLLESAETEDVVDVFQVVKSLRKARPGMVGSFEQYQFLYDI 1192
Cdd:cd14634   152 GGRSGTFCAICSVCEMIQQQNIIDVFHTVKTLRNNKSNMVETLEQYKFVYEV 203
R-PTPc-U-2 cd14637
PTP domain of receptor-type tyrosine-protein phosphatase U, repeat 2; Receptor-type ...
 986-1192 1.39e-31

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: 123.09  E-value: 1.39e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158138488  986 YINASFVMSYWKPEMMIAAQGPLKETIGDFWQMIFQRKVKVIVMLTEL-MSGDQEVCAQYWGE-GKQTYGDMEVMLKDTN 1063
Cdd:cd14637     1 YINAALTDSYTRSAAFIVTLHPLQNTTTDFWRLVYDYGCTSVVMLNQLnQSNSAWPCLQYWPEpGLQQYGPMEVEFVSGS 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158138488 1064 KSSAYILRAFELRHSKR--KEPRTVYQYQCTTWKG-EELPAEPKDLVTLIQNIKQKLPKSGsEGmkyhkhaSILVHCRDG 1140
Cdd:cd14637    81 ADEDIVTRLFRVQNITRlqEGHLMVRHFQFLRWSAyRDTPDSKKAFLHLLASVEKWQRESG-EG-------RTVVHCLNG 152

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 158138488 1141 SQQTGLFCALFNLLESAETEDVVDVFQVVKSLRKARPGMVGSFEQYQFLYDI 1192
Cdd:cd14637   153 GGRSGTYCASAMILEMIRCHNIVDVFYAVKTLRNYKPNMVETLEQYRFCYEI 204
PTPc-N2 cd14607
catalytic domain of tyrosine-protein phosphatase non-receptor type 2; Tyrosine-protein ...
 936-1190 3.21e-31

catalytic domain of tyrosine-protein phosphatase non-receptor type 2; Tyrosine-protein phosphatase non-receptor type 2 (PTPN2), also called T-cell protein-tyrosine phosphatase (TCPTP), belongs to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. PTPN2, a tumor suppressor, dephosphorylates and inactivates EGFRs, Src family kinases, Janus-activated kinases (JAKs)-1 and -3, and signal transducer and activators of transcription (STATs)-1, -3 and -5, in a cell type and context-dependent manner. It is deleted in 6% of all T-cell acute lymphoblastic leukemias and is associated with constitutive JAK1/STAT5 signaling and tumorigenesis.


Pssm-ID: 350455 [Multi-domain]  Cd Length: 257  Bit Score: 123.92  E-value: 3.21e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158138488  936 ENKKKNRSSNVVPYDFNRVPLKHelemskeseaesdessdedsdseETSKYINASFVMSYWKPEMMIAAQGPLKETIGDF 1015
Cdd:cd14607    23 ENRNRNRYRDVSPYDHSRVKLQN-----------------------TENDYINASLVVIEEAQRSYILTQGPLPNTCCHF 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158138488 1016 WQMIFQRKVKVIVMLTELMSGDQEVCAQYW---GEGKQTYGD--MEVMLKDTNKSSAYILRAFELRHSKRKEPRTVYQYQ 1090
Cdd:cd14607    80 WLMVWQQKTKAVVMLNRIVEKDSVKCAQYWptdEEEVLSFKEtgFSVKLLSEDVKSYYTVHLLQLENINSGETRTISHFH 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158138488 1091 CTTWKGEELPAEPKDLVtliqNIKQKLPKSGSEGMkyhKHASILVHCRDGSQQTGLFCALFNLLESAETED--VVDVFQV 1168
Cdd:cd14607   160 YTTWPDFGVPESPASFL----NFLFKVRESGSLSP---EHGPAVVHCSAGIGRSGTFSLVDTCLVLMEKKDpdSVDIKQV 232

                         250       260
                  ....*....|....*....|..
gi 158138488 1169 VKSLRKARPGMVGSFEQYQFLY 1190
Cdd:cd14607   233 LLDMRKYRMGLIQTPDQLRFSY 254
PTPc_plant_PTP1 cd17658
protein tyrosine phosphatase 1 from Arabidopsis thaliana and similar plant PTPs; Arabidopsis ...
 986-1190 3.31e-31

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: 122.19  E-value: 3.31e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158138488  986 YINASFVM--SYWKPEMMIAAQGPLKETIGDFWQMIFQRKVKVIVMLTELMSGDQEV-CAQYW---GEGKQTYGDMEVML 1059
Cdd:cd17658     1 YINASLVEtpASESLPKFIATQGPLPHTFEDFWEMVIQQRCPVIIMLTRLVDNYSTAkCADYFpaeENESREFGRISVTN 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158138488 1060 KDTNKSSAYI-LRAFELRHSKRKE-PRTVYQYQCTTWKGEELPAEPKDLVTLIQNIKQKLPKSGsegmkyhkhaSILVHC 1137
Cdd:cd17658    81 KKLKHSQHSItLRVLEVQYIESEEpPLSVLHIQYPEWPDHGVPKDTRSVRELLKRLYGIPPSAG----------PIVVHC 150

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 158138488 1138 RDGSQQTGLFCALFNLLESAETEDV--VDVFQVVKSLRKARPGMVGSFEQYQFLY 1190
Cdd:cd17658   151 SAGIGRTGAYCTIHNTIRRILEGDMsaVDLSKTVRKFRSQRIGMVQTQDQYIFCY 205
PTPc-N3_4 cd14541
catalytic domain of tyrosine-protein phosphatase non-receptor type 21 and type 14; ...
 986-1197 1.21e-30

catalytic domain of tyrosine-protein phosphatase non-receptor type 21 and type 14; Tyrosine-protein phosphatase non-receptor type 3 (PTPN3) and type 4 (PTPN4) belong to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. PTPN3 and PTPN4 are large modular proteins containing an N-terminal FERM domain, a PDZ domain and a C-terminal catalytic PTP domain. PTPN3 interacts with mitogen-activated protein kinase p38gamma and serves as its specific phosphatase. PTPN4 functions in TCR cell signaling, apoptosis, cerebellar synaptic plasticity, and innate immune responses.


Pssm-ID: 350389 [Multi-domain]  Cd Length: 212  Bit Score: 120.51  E-value: 1.21e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158138488  986 YINASFV-MSYWKPEMM---IAAQGPLKETIGDFWQMIFQRKVKVIVMLTELMSGDQEVCAQYW--GEGKQTYGDMEVML 1059
Cdd:cd14541     2 YINANYVnMEIPGSGIVnryIAAQGPLPNTCADFWQMVWEQKSTLIVMLTTLVERGRVKCHQYWpdLGETMQFGNLQITC 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158138488 1060 KDTNKSSAYILRAFELRHSKRKEPRTVYQYQCTTWKGEELPAEPKDLVTLIQNIKQKlpksgSEGMKYhkhaSILVHCRD 1139
Cdd:cd14541    82 VSEEVTPSFAFREFILTNTNTGEERHITQMQYLAWPDHGVPDDSSDFLDFVKRVRQN-----RVGMVE----PTVVHCSA 152

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 158138488 1140 GSQQTGLFCAL---FNLLESAETedvVDVFQVVKSLRKARPGMVGSFEQYQFLYDIMASIY 1197
Cdd:cd14541   153 GIGRTGVLITMetaMCLIEANEP---VYPLDIVRTMRDQRAMLIQTPSQYRFVCEAILRVY 210
R5-PTP-2 cd14550
PTP-like domain of R5 subfamily receptor-type tyrosine-protein phosphatases, repeat 2; The R5 ...
 986-1190 1.84e-30

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: 119.73  E-value: 1.84e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158138488  986 YINASFVMSYWKPEMMIAAQGPLKETIGDFWQMIFQRKVKVIVMLTEL-MSGDqevCAQYW-GEGKqtygDME-----VM 1058
Cdd:cd14550     1 YINASYLQGYRRSNEFIITQHPLEHTIKDFWQMIWDHNSQTIVMLTDNeLNED---EPIYWpTKEK----PLEcetfkVT 73

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158138488 1059 LKDTNKSSA-----YILRAFELRHSKRKEPRTVYQYQCTTWKGEELPaePKDLVTLIQNIkQKLPKSgsegmkyhKHASI 1133
Cdd:cd14550    74 LSGEDHSCLsneirLIVRDFILESTQDDYVLEVRQFQCPSWPNPCSP--IHTVFELINTV-QEWAQQ--------RDGPI 142

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 158138488 1134 LVHCRDGSQQTGLFCALFNLLESAETEDVVDVFQVVKSLRKARPGMVGSFEQYQFLY 1190
Cdd:cd14550   143 VVHDRYGGVQAATFCALTTLHQQLEHESSVDVYQVAKLYHLMRPGVFTSKEDYQFLY 199
PTPc-N1 cd14608
catalytic domain of tyrosine-protein phosphatase non-receptor type 1; Tyrosine-protein ...
 931-1190 4.31e-30

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: 121.29  E-value: 4.31e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158138488  931 IGNQEENKKKNRSSNVVPYDFNRVPLKHElemskeseaesdessdedsdseeTSKYINASFVMSYWKPEMMIAAQGPLKE 1010
Cdd:cd14608    19 VAKLPKNKNRNRYRDVSPFDHSRIKLHQE-----------------------DNDYINASLIKMEEAQRSYILTQGPLPN 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158138488 1011 TIGDFWQMIFQRKVKVIVMLTELMSGDQEVCAQYWGEGKqtygDMEVMLKDTN---------KSSAYILRAFELRHSKRK 1081
Cdd:cd14608    76 TCGHFWEMVWEQKSRGVVMLNRVMEKGSLKCAQYWPQKE----EKEMIFEDTNlkltlisedIKSYYTVRQLELENLTTQ 151

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158138488 1082 EPRTVYQYQCTTWKGEELPAEPKDLVTLIQNIKQklpkSGSEGmkyHKHASILVHCRDGSQQTGLFC---ALFNLLESAE 1158
Cdd:cd14608   152 ETREILHFHYTTWPDFGVPESPASFLNFLFKVRE----SGSLS---PEHGPVVVHCSAGIGRSGTFCladTCLLLMDKRK 224

                         250       260       270
                  ....*....|....*....|....*....|..
gi 158138488 1159 TEDVVDVFQVVKSLRKARPGMVGSFEQYQFLY 1190
Cdd:cd14608   225 DPSSVDIKKVLLEMRKFRMGLIQTADQLRFSY 256
PHA02746 PHA02746
protein tyrosine phosphatase; Provisional
 934-1190 8.66e-30

protein tyrosine phosphatase; Provisional


Pssm-ID: 165113 [Multi-domain]  Cd Length: 323  Bit Score: 121.67  E-value: 8.66e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158138488  934 QEENKKKNRSSNVVPYDFNRVPLKHELEMSKESEAESDESSDEDSDSEETSKYINASFVMSYWKPEMMIAAQGPLKETIG 1013
Cdd:PHA02746   48 KKENLKKNRFHDIPCWDHSRVVINAHESLKMFDVGDSDGKKIEVTSEDNAENYIHANFVDGFKEANKFICAQGPKEDTSE 127

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158138488 1014 DFWQMIFQRKVKVIVMLTELmSGDQEVCAQYWGEGKQ---TYGDMEVMLKDTNKSSAYILRAFELRHSKRKEPRTVYQYQ 1090
Cdd:PHA02746  128 DFFKLISEHESQVIVSLTDI-DDDDEKCFELWTKEEDselAFGRFVAKILDIIEELSFTKTRLMITDKISDTSREIHHFW 206

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158138488 1091 CTTWKGEELPAEPKDLVTLIQ--NIKQKLPKSGSEGmKYHKHASILVHCRDGSQQTGLFCALFNLLESAETEDVVDVFQV 1168
Cdd:PHA02746  207 FPDWPDNGIPTGMAEFLELINkvNEEQAELIKQADN-DPQTLGPIVVHCSAGIGRAGTFCAIDNALEQLEKEKEVCLGEI 285

                         250       260
                  ....*....|....*....|..
gi 158138488 1169 VKSLRKARPGMVGSFEQYQFLY 1190
Cdd:PHA02746  286 VLKIRKQRHSSVFLPEQYAFCY 307
R-PTPc-B cd14617
catalytic domain of receptor-type tyrosine-protein phosphatase B; Receptor-type ...
 941-1190 2.58e-29

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: 117.33  E-value: 2.58e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158138488  941 NRSSNVVPYDFNRVPLKHelemskeseaesdessdedSDSEETSKYINASFVMSYWKPEMMIAAQGPLKETIGDFWQMIF 1020
Cdd:cd14617     1 NRYNNILPYDSTRVKLSN-------------------VDDDPCSDYINASYIPGNNFRREYIATQGPLPGTKDDFWKMVW 61

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158138488 1021 QRKVKVIVMLTELMSGDQEVCAQYWGEGKQT--YGDMEVMLKDTNKSSAYILRAFEL-RHSKRKEPRTVYQYQCTTWKGE 1097
Cdd:cd14617    62 EQNVHNIVMVTQCVEKGRVKCDHYWPADQDSlyYGDLIVQMLSESVLPEWTIREFKIcSEEQLDAPRLVRHFHYTVWPDH 141

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158138488 1098 ELPAEPKDLVTLIQNIKQKLPKSGSEGMKyhkhasiLVHCRDGSQQTGLFCALFNLLESAETEDVVDVFQVVKSLRKARP 1177
Cdd:cd14617   142 GVPETTQSLIQFVRTVRDYINRTPGSGPT-------VVHCSAGVGRTGTFIALDRILQQLDSKDSVDIYGAVHDLRLHRV 214

                         250
                  ....*....|...
gi 158138488 1178 GMVGSFEQYQFLY 1190
Cdd:cd14617   215 HMVQTECQYVYLH 227
R5-PTP-2 cd14550
PTP-like domain of R5 subfamily receptor-type tyrosine-protein phosphatases, repeat 2; The R5 ...
 676-862 5.26e-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: 115.50  E-value: 5.26e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158138488  676 YINASYIDGFKEPRKYIAAQGPRDETVDDFWKMIWEQKATVIVMVTRCEEgnRNKCAEYWPCMEE--GTRTFRdVVVTIN 753
Cdd:cd14550     1 YINASYLQGYRRSNEFIITQHPLEHTIKDFWQMIWDHNSQTIVMLTDNEL--NEDEPIYWPTKEKplECETFK-VTLSGE 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158138488  754 DHK---RCPDYIIQKLSIAHKKEKATgREVTHIQFTSWPDHGVPedPHLLLKLRRRVNAFSNFFSGPIVVHCSAGVGRTG 830
Cdd:cd14550    78 DHSclsNEIRLIVRDFILESTQDDYV-LEVRQFQCPSWPNPCSP--IHTVFELINTVQEWAQQRDGPIVVHDRYGGVQAA 154

                         170       180       190
                  ....*....|....*....|....*....|....
gi 158138488  831 TYIGIDAMLESLEAEGKVDVYGYVV--NLRRQRC 862
Cdd:cd14550   155 TFCALTTLHQQLEHESSVDVYQVAKlyHLMRPGV 188
PTPc-N3 cd14600
catalytic domain of tyrosine-protein phosphatase non-receptor type 3; Tyrosine-protein ...
 934-1197 8.81e-29

catalytic domain of tyrosine-protein phosphatase non-receptor type 3; Tyrosine-protein phosphatase non-receptor type 3 (PTPN3), also called protein-tyrosine phosphatase H1 (PTP-H1), belongs to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. PTPN3 interacts with mitogen-activated protein kinase p38gamma and serves as its specific phosphatase. PTPN3 and p38gamma cooperate to promote Ras-induced oncogenesis. PTPN3 is a large modular protein containing an N-terminal FERM domain, a PDZ domain and a C-terminal catalytic PTP domain. Its PDZ domain binds with the PDZ-binding motif of p38gamma and enables efficient tyrosine dephosphorylation.


Pssm-ID: 350448 [Multi-domain]  Cd Length: 274  Bit Score: 117.26  E-value: 8.81e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158138488  934 QEENKKKNRSSNVVPYDFNRVPLKHElemskeseaesdessdedsdseetSKYINASFV-MSYWKPEMM---IAAQGPLK 1009
Cdd:cd14600    37 LPQNMDKNRYKDVLPYDATRVVLQGN------------------------EDYINASYVnMEIPSANIVnkyIATQGPLP 92

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158138488 1010 ETIGDFWQMIFQRKVKVIVMLTELMSGDQEVCAQYWGEGKQT--YGDMEVMLKDTNKSSAYILRAFELRHSKRKEPRTVY 1087
Cdd:cd14600    93 HTCAQFWQVVWEQKLSLIVMLTTLTERGRTKCHQYWPDPPDVmeYGGFRVQCHSEDCTIAYVFREMLLTNTQTGEERTVT 172

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158138488 1088 QYQCTTWKGEELPAEPKDLVTLIQNIKQKLPKSgsegmkyhkhASILVHCRDGSQQTGLFCALFNLLESAETEDVVDVFQ 1167
Cdd:cd14600   173 HLQYVAWPDHGVPDDSSDFLEFVNYVRSKRVEN----------EPVLVHCSAGIGRTGVLVTMETAMCLTERNQPVYPLD 242

                         250       260       270
                  ....*....|....*....|....*....|
gi 158138488 1168 VVKSLRKARPGMVGSFEQYQFLYDIMASIY 1197
Cdd:cd14600   243 IVRKMRDQRAMMVQTSSQYKFVCEAILRVY 272
PHA02742 PHA02742
protein tyrosine phosphatase; Provisional
 936-1190 1.45e-28

protein tyrosine phosphatase; Provisional


Pssm-ID: 165109 [Multi-domain]  Cd Length: 303  Bit Score: 117.41  E-value: 1.45e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158138488  936 ENKKKNRSSNVVPYDFNRVPLKHElemskeseaesdessdedsdsEETSKYINASFVMSYWKPEMMIAAQGPLKETIGDF 1015
Cdd:PHA02742   51 KNMKKCRYPDAPCFDRNRVILKIE---------------------DGGDDFINASYVDGHNAKGRFICTQAPLEETALDF 109

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158138488 1016 WQMIFQRKVKVIVMLTELMSGDQEVCAQYWG---EGKQTYGDMEVMLKDTNKSSAYILRAFELRHSKRKEPRTVYQYQCT 1092
Cdd:PHA02742  110 WQAIFQDQVRVIVMITKIMEDGKEACYPYWMpheRGKATHGEFKIKTKKIKSFRNYAVTNLCLTDTNTGASLDIKHFAYE 189

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158138488 1093 TWKGEELPAEPKDLVTLIQNIKQKLPKSG--SEGMKYHKHASILVHCRDGSQQTGLFCALFNLLESAETEDVVDVFQVVK 1170
Cdd:PHA02742  190 DWPHGGLPRDPNKFLDFVLAVREADLKADvdIKGENIVKEPPILVHCSAGLDRAGAFCAIDICISKYNERAIIPLLSIVR 269

                         250       260
                  ....*....|....*....|
gi 158138488 1171 SLRKARPGMVGSFEQYQFLY 1190
Cdd:PHA02742  270 DLRKQRHNCLSLPQQYIFCY 289
PTPc-N20 cd14596
catalytic domain of tyrosine-protein phosphatase non-receptor type 20; Tyrosine-protein ...
 986-1193 1.61e-28

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: 114.46  E-value: 1.61e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158138488  986 YINASFVMSYWKPE--MMIAAQGPLKETIGDFWQMIFQRKVKVIVMLTELMSGDQEVCAQYWGEGKQT---YGDMEVMLK 1060
Cdd:cd14596     1 YINASYITMPVGEEelFYIATQGPLPSTIDDFWQMVWENRSDVIAMMTREVERGKVKCHRYWPETLQEpmeLENYQLRLE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158138488 1061 DTNKSSAYILRAFELRHSKRKEPRTVYQYQCTTWKGEELPAEPKDLVTLIQNIKqklpksgsegmKYHKHASILVHCRDG 1140
Cdd:cd14596    81 NYQALQYFIIRIIKLVEKETGENRLIKHLQFTTWPDHGTPQSSDQLVKFICYMR-----------KVHNTGPIVVHCSAG 149

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 158138488 1141 SQQTGLFCALFNLLESAETEDVVDVFQVVKSLRKARPGMVGSFEQYQFLYDIM 1193
Cdd:cd14596   150 IGRAGVLICVDVLLSLIEKDLSFNIKDIVREMRQQRYGMIQTKDQYLFCYKVV 202
R-PTP-Z-2 cd17669
catalytic domain of receptor-type tyrosine-protein phosphatase Z, repeat 2; Receptor-type ...
 986-1193 1.79e-28

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


Pssm-ID: 350507 [Multi-domain]  Cd Length: 204  Bit Score: 113.94  E-value: 1.79e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158138488  986 YINASFVMSYWKPEMMIAAQGPLKETIGDFWQMIFQRKVKVIVMLTELMSGDQEVCAqYWGEGKQTYG----DMEVMLKD 1061
Cdd:cd17669     1 YINASYIMGYYQSNEFIITQHPLLHTIKDFWRMIWDHNAQLIVMLPDGQNMAEDEFV-YWPNKDEPINcetfKVTLIAEE 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158138488 1062 ---TNKSSAYILRAFELRHSKRKEPRTVYQYQCTTWKGEELPAEPKdlVTLIQNIKQKLPksgsegmkyHKHASILVHCR 1138
Cdd:cd17669    80 hkcLSNEEKLIIQDFILEATQDDYVLEVRHFQCPKWPNPDSPISKT--FELISIIKEEAA---------NRDGPMIVHDE 148

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 158138488 1139 DGSQQTGLFCALFNLLESAETEDVVDVFQVVKSLRKARPGMVGSFEQYQFLYDIM 1193
Cdd:cd17669   149 HGGVTAGTFCALTTLMHQLEKENSVDVYQVAKMINLMRPGVFTDIEQYQFLYKAI 203
PTPc-N14 cd14599
catalytic domain of tyrosine-protein phosphatase non-receptor type 14; Tyrosine-protein ...
 916-1193 2.23e-28

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: 116.25  E-value: 2.23e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158138488  916 EYQRLPSYRSWRTQHIGNQEENKKKNRSSNVVPYDFNRVPLKHELEmskeseaesdessdedsdseETSKYINASF--VM 993
Cdd:cd14599    17 EYEQIPKKKADGVFTTATLPENAERNRIREVVPYEENRVELVPTKE--------------------NNTGYINASHikVT 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158138488  994 SYWKPEMMIAAQGPLKETIGDFWQMIFQRKVKVIVMLTELMSGDQEVCAQYWGE-----GKQTYGDMEVMLKDTNKSSAY 1068
Cdd:cd14599    77 VGGEEWHYIATQGPLPHTCHDFWQMVWEQGVNVIAMVTAEEEGGRSKSHRYWPKlgskhSSATYGKFKVTTKFRTDSGCY 156

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158138488 1069 ILRAFELRHSKRKEPRTVYQYQCTTWKGEELPAEPKDLVTLIQNIK--QKLPKSGSEGMKyHKHASILVHCRDGSQQTGL 1146
Cdd:cd14599   157 ATTGLKVKHLLSGQERTVWHLQYTDWPDHGCPEEVQGFLSYLEEIQsvRRHTNSMLDSTK-NCNPPIVVHCSAGVGRTGV 235

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*..
gi 158138488 1147 FCALFNLLESAETEDVVDVFQVVKSLRKARPGMVGSFEQYQFLYDIM 1193
Cdd:cd14599   236 VILTELMIGCLEHNEKVEVPVMLRHLREQRMFMIQTIAQYKFVYQVL 282
R-PTPc-M-2 cd14635
PTP domain of receptor-type tyrosine-protein phosphatase M, repeat 2; Receptor-type ...
 986-1192 6.36e-28

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: 112.47  E-value: 6.36e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158138488  986 YINASFVMSYWKPEMMIAAQGPLKETIGDFWQMIFQRKVKVIVMLTELmsGDQEVCAQYWGE-GKQTYGDMEVMLKDTNK 1064
Cdd:cd14635     1 YINAALMDSYKQPSAFIVTQHPLPNTVKDFWRLVLDYHCTSIVMLNDV--DPAQLCPQYWPEnGVHRHGPIQVEFVSADL 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158138488 1065 SSAYILRAFELRHSKRKEP--RTVYQYQCTTWKG-EELPAEPKDLVTLIQNI-KQKLPKSGSEGmkyhkhaSILVHCRDG 1140
Cdd:cd14635    79 EEDIISRIFRIYNAARPQDgyRMVQQFQFLGWPMyRDTPVSKRSFLKLIRQVdKWQEEYNGGEG-------RTVVHCLNG 151

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 158138488 1141 SQQTGLFCALFNLLESAETEDVVDVFQVVKSLRKARPGMVGSFEQYQFLYDI 1192
Cdd:cd14635   152 GGRSGTFCAISIVCEMLRHQRAVDVFHAVKTLRNNKPNMVDLLDQYKFCYEV 203
PTPc_DSPc smart00012
Protein tyrosine phosphatase, catalytic domain, undefined specificity; Protein tyrosine ...
 1085-1195 1.18e-27

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: 108.22  E-value: 1.18e-27
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158138488   1085 TVYQYQCTTWKGEELPAEPKDLVTLIQNIKQKLPKSGSegmkyhkHASILVHCRDGSQQTGLFCALFNLLESAETE-DVV 1163
Cdd:smart00012    1 TVKHYHYTGWPDHGVPESPDSILELLRAVKKNLNQSES-------SGPVVVHCSAGVGRTGTFVAIDILLQQLEAEaGEV 73

                            90       100       110
                    ....*....|....*....|....*....|..
gi 158138488   1164 DVFQVVKSLRKARPGMVGSFEQYQFLYDIMAS 1195
Cdd:smart00012   74 DIFDTVKELRSQRPGMVQTEEQYLFLYRALLE 105
PTPc_motif smart00404
Protein tyrosine phosphatase, catalytic domain motif;
1085-1195 1.18e-27

Protein tyrosine phosphatase, catalytic domain motif;


Pssm-ID: 214649 [Multi-domain]  Cd Length: 105  Bit Score: 108.22  E-value: 1.18e-27
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158138488   1085 TVYQYQCTTWKGEELPAEPKDLVTLIQNIKQKLPKSGSegmkyhkHASILVHCRDGSQQTGLFCALFNLLESAETE-DVV 1163
Cdd:smart00404    1 TVKHYHYTGWPDHGVPESPDSILELLRAVKKNLNQSES-------SGPVVVHCSAGVGRTGTFVAIDILLQQLEAEaGEV 73

                            90       100       110
                    ....*....|....*....|....*....|..
gi 158138488   1164 DVFQVVKSLRKARPGMVGSFEQYQFLYDIMAS 1195
Cdd:smart00404   74 DIFDTVKELRSQRPGMVQTEEQYLFLYRALLE 105
R-PTP-G-2 cd17670
PTP-like domain of receptor-type tyrosine-protein phosphatase G, repeat 2; Receptor-type ...
 986-1195 1.03e-26

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: 109.00  E-value: 1.03e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158138488  986 YINASFVMSYWKPEMMIAAQGPLKETIGDFWQMIFQRKVKVIVML--TELMSGDQEVcaqYWGEGKQTYG--DMEVMLKD 1061
Cdd:cd17670     1 YINASYIMGYYRSNEFIITQHPLPHTTKDFWRMIWDHNAQIIVMLpdNQGLAEDEFV---YWPSREESMNceAFTVTLIS 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158138488 1062 TNK-----SSAYILRAFELRHSKRKEPRTVYQYQCTTWKGEELPAEpkDLVTLIQNIKQklpksgsEGMKyhKHASILVH 1136
Cdd:cd17670    78 KDRlclsnEEQIIIHDFILEATQDDYVLEVRHFQCPKWPNPDAPIS--STFELINVIKE-------EALT--RDGPTIVH 146

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 158138488 1137 CRDGSQQTGLFCALFNLLESAETEDVVDVFQVVKSLRKARPGMVGSFEQYQFLYDIMAS 1195
Cdd:cd17670   147 DEFGAVSAGTLCALTTLSQQLENENAVDVYQVAKMINLMRPGVFTDIEQYQFLYKAMLS 205
PTPc-N4 cd14601
catalytic domain of tyrosine-protein phosphatase non-receptor type 4; Tyrosine-protein ...
 986-1197 1.84e-26

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: 108.49  E-value: 1.84e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158138488  986 YINASFV-MSYWKPEMM---IAAQGPLKETIGDFWQMIFQRKVKVIVMLTELMSGDQEVCAQYWGE--GKQTYGDMEVML 1059
Cdd:cd14601     2 YINANYInMEIPSSSIInryIACQGPLPNTCSDFWQMTWEQGSSMVVMLTTQVERGRVKCHQYWPEpsGSSSYGGFQVTC 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158138488 1060 KDTNKSSAYILRAFELRHSKRKEPRTVYQYQCTTWKGEELPAEPKDLVTLIQNIKQKlpksgsegmKYHKHASILVHCRD 1139
Cdd:cd14601    82 HSEEGNPAYVFREMTLTNLEKNESRPLTQIQYIAWPDHGVPDDSSDFLDFVCLVRNK---------RAGKDEPVVVHCSA 152

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 158138488 1140 GSQQTGLFCALFNLLESAETEDVVDVFQVVKSLRKARPGMVGSFEQYQFLYDIMASIY 1197
Cdd:cd14601   153 GIGRTGVLITMETAMCLIECNQPVYPLDIVRTMRDQRAMMIQTPSQYRFVCEAILKVY 210
R-PTPc-T-2 cd14634
PTP domain of receptor-type tyrosine-protein phosphatase T, repeat 2; Receptor-type ...
 676-880 2.03e-26

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: 108.18  E-value: 2.03e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158138488  676 YINASYIDGFKEPRKYIAAQGPRDETVDDFWKMIWEQKATVIVMVTrcEEGNRNKCAEYWPcmEEGTRTFRDVVVTINDH 755
Cdd:cd14634     1 YINAALMDSHKQPAAFIVTQHPLPNTVADFWRLVFDYNCSSVVMLN--EMDAAQLCMQYWP--EKTSCCYGPIQVEFVSA 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158138488  756 KRCPDYIIQKLSIAHKKEKATG-REVTHIQFTSWPDH-GVPEDPHLLLKLRRRVNAFSNFF---SGPIVVHCSAGVGRTG 830
Cdd:cd14634    77 DIDEDIISRIFRICNMARPQDGyRIVQHLQYIGWPAYrDTPPSKRSILKVVRRLEKWQEQYdgrEGRTVVHCLNGGGRSG 156

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|
gi 158138488  831 TYIGIDAMLESLEAEGKVDVYGYVVNLRRQRCLMVQVEAQYILIHQALVE 880
Cdd:cd14634   157 TFCAICSVCEMIQQQNIIDVFHTVKTLRNNKSNMVETLEQYKFVYEVALE 206
PTPc-N21 cd14598
catalytic domain of tyrosine-protein phosphatase non-receptor type 21; Tyrosine-protein ...
 986-1193 4.24e-25

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: 105.06  E-value: 4.24e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158138488  986 YINASFVM-----SYWKpemMIAAQGPLKETIGDFWQMIFQRKVKVIVMLTELMSGDQEVCAQYWG-----EGKQTYGDM 1055
Cdd:cd14598     1 YINASHIKvtvggKEWD---YIATQGPLQNTCQDFWQMVWEQGVAIIAMVTAEEEGGREKSFRYWPrlgsrHNTVTYGRF 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158138488 1056 EVMLKDTNKSSAYILRAFELRHSKRKEPRTVYQYQCTTWKGEELPAEPKDLVTLIQNIKQKLPKSGSEGMKYHKHASILV 1135
Cdd:cd14598    78 KITTRFRTDSGCYATTGLKIKHLLTGQERTVWHLQYTDWPEHGCPEDLKGFLSYLEEIQSVRRHTNSTIDPKSPNPPVLV 157

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 158138488 1136 HCRDGSQQTGLFCALFNLLESAETEDVVDVFQVVKSLRKARPGMVGSFEQYQFLYDIM 1193
Cdd:cd14598   158 HCSAGVGRTGVVILSEIMIACLEHNEMLDIPRVLDMLRQQRMMMVQTLSQYTFVYKVL 215
COG5599 COG5599
Protein tyrosine phosphatase [Signal transduction mechanisms];
928-1196 1.17e-23

Protein tyrosine phosphatase [Signal transduction mechanisms];


Pssm-ID: 444335 [Multi-domain]  Cd Length: 282  Bit Score: 102.48  E-value: 1.17e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158138488  928 TQHIGNQEeNKKKNRSSNVVPYDFNRVplkhelemskeseaesdessdedsdsEETSKYINASFVMSYwKPEMMIAAQGP 1007
Cdd:COG5599    34 PQYLQNIN-GSPLNRFRDIQPYKETAL--------------------------RANLGYLNANYIQVI-GNHRYIATQYP 85

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158138488 1008 LKETIGDFWQMIFQRKVKVIVMLT--ELMSGDQEVCAQYWGEgKQTYGDMEVMLKDTNK---SSAYILRAFEL-RHSKRK 1081
Cdd:COG5599    86 LEEQLEDFFQMLFDNNTPVLVVLAsdDEISKPKVKMPVYFRQ-DGEYGKYEVSSELTESiqlRDGIEARTYVLtIKGTGQ 164

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158138488 1082 EPRTVYQYQCTTWK-GEELPAEP-KDLVTLIqnIKQKLPKSGSEGmkyhkhaSILVHCRDGSQQTGLFCALFNLLES--A 1157
Cdd:COG5599   165 KKIEIPVLHVKNWPdHGAISAEAlKNLADLI--DKKEKIKDPDKL-------LPVVHCRAGVGRTGTLIACLALSKSinA 235

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|
gi 158138488 1158 ETEDVVDVFQVVKSLRKAR-PGMVGSFEQYQFLYDIMASI 1196
Cdd:COG5599   236 LVQITLSVEEIVIDMRTSRnGGMVQTSEQLDVLVKLAEQQ 275
R-PTPc-M-2 cd14635
PTP domain of receptor-type tyrosine-protein phosphatase M, repeat 2; Receptor-type ...
 676-880 1.26e-23

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: 100.15  E-value: 1.26e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158138488  676 YINASYIDGFKEPRKYIAAQGPRDETVDDFWKMIWEQKATVIVMVTRCEEGNRnkCAEYWPcmEEGTRTFRDVVVTINDH 755
Cdd:cd14635     1 YINAALMDSYKQPSAFIVTQHPLPNTVKDFWRLVLDYHCTSIVMLNDVDPAQL--CPQYWP--ENGVHRHGPIQVEFVSA 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158138488  756 KRCPDYIIQKLSIAHKKEKATG-REVTHIQFTSWPDH-GVPEDPHLLLKLRRRVNAFSNFF---SGPIVVHCSAGVGRTG 830
Cdd:cd14635    77 DLEEDIISRIFRIYNAARPQDGyRMVQQFQFLGWPMYrDTPVSKRSFLKLIRQVDKWQEEYnggEGRTVVHCLNGGGRSG 156

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|
gi 158138488  831 TYIGIDAMLESLEAEGKVDVYGYVVNLRRQRCLMVQVEAQYILIHQALVE 880
Cdd:cd14635   157 TFCAISIVCEMLRHQRAVDVFHAVKTLRNNKPNMVDLLDQYKFCYEVALE 206
R-PTP-Z-2 cd17669
catalytic domain of receptor-type tyrosine-protein phosphatase Z, repeat 2; Receptor-type ...
 676-879 1.42e-22

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: 96.99  E-value: 1.42e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158138488  676 YINASYIDGFKEPRKYIAAQGPRDETVDDFWKMIWEQKATVIVMVTRCEEGNRNKCAeYWPCMEE--GTRTFRdVVVTIN 753
Cdd:cd17669     1 YINASYIMGYYQSNEFIITQHPLLHTIKDFWRMIWDHNAQLIVMLPDGQNMAEDEFV-YWPNKDEpiNCETFK-VTLIAE 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158138488  754 DHKrC----PDYIIQKLsIAHKKEKATGREVTHIQFTSWPDhgvPEDP-HLLLKLRRRVNAFSNFFSGPIVVHCSAGVGR 828
Cdd:cd17669    79 EHK-ClsneEKLIIQDF-ILEATQDDYVLEVRHFQCPKWPN---PDSPiSKTFELISIIKEEAANRDGPMIVHDEHGGVT 153

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 158138488  829 TGTYIGIDAMLESLEAEGKVDVYGYV--VNLRRQRcLMVQVEaQYILIHQALV 879
Cdd:cd17669   154 AGTFCALTTLMHQLEKENSVDVYQVAkmINLMRPG-VFTDIE-QYQFLYKAIL 204
R-PTP-G-2 cd17670
PTP-like domain of receptor-type tyrosine-protein phosphatase G, repeat 2; Receptor-type ...
 676-879 3.14e-21

PTP-like domain of receptor-type tyrosine-protein phosphatase G, repeat 2; Receptor-type tyrosine-protein phosphatase G (PTPRG), also called protein-tyrosine phosphatase gamma (R-PTP-gamma), belongs to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. PTPRG is an important tumor suppressor gene in multiple human cancers such as lung, ovarian, and breast cancers. It is widely expressed in many tissues, including the central nervous system, where it plays a role during neuroinflammation processes. It can dephosphorylate platelet-derived growth factor receptor beta (PDGFRB) and may play a role in PDGFRB-related infantile myofibromatosis. PTPRG is a type 1 integral membrane protein consisting of an extracellular region with a carbonic anhydrase-like (CAH) and a fibronectin type III (FN3) domains, and an intracellular region with a catalytic PTP domain (repeat 1) proximal to the membrane, and a catalytically inactive PTP-fold domain (repeat 2) distal to the membrane. This model represents the inactive PTP-like domain (repeat 2).


Pssm-ID: 350508 [Multi-domain]  Cd Length: 205  Bit Score: 93.20  E-value: 3.14e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158138488  676 YINASYIDGFKEPRKYIAAQGPRDETVDDFWKMIWEQKATVIVMVTRcEEGNRNKCAEYWPCMEEGTRTFRDVVVTINDH 755
Cdd:cd17670     1 YINASYIMGYYRSNEFIITQHPLPHTTKDFWRMIWDHNAQIIVMLPD-NQGLAEDEFVYWPSREESMNCEAFTVTLISKD 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158138488  756 KRC---PDYIIQKLSIAHKKEKATGREVTHIQFTSWPDHGVPEDPHLLLKLRRRVNAFSNffSGPIVVHCSAGVGRTGTY 832
Cdd:cd17670    80 RLClsnEEQIIIHDFILEATQDDYVLEVRHFQCPKWPNPDAPISSTFELINVIKEEALTR--DGPTIVHDEFGAVSAGTL 157

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*....
gi 158138488  833 IGIDAMLESLEAEGKVDVY--GYVVNLRRQRcLMVQVEaQYILIHQALV 879
Cdd:cd17670   158 CALTTLSQQLENENAVDVYqvAKMINLMRPG-VFTDIE-QYQFLYKAML 204
R-PTPc-K-2 cd14636
PTP domain of receptor-type tyrosine-protein phosphatase K, repeat 2; Receptor-type ...
 676-880 1.43e-20

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: 91.24  E-value: 1.43e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158138488  676 YINASYIDGFKEPRKYIAAQGPRDETVDDFWKMIWEQKATVIVMVTRCEEGnrNKCAEYWPcmEEGTRTFRDVVVTINDH 755
Cdd:cd14636     1 YINAALMDSYRQPAAFIVTQHPLPNTVKDFWRLVYDYGCTSIVMLNEVDLA--QGCPQYWP--EEGMLRYGPIQVECMSC 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158138488  756 KRCPDYIIQKLSIAHKKEKATGR-EVTHIQFTSWPDH-GVPEDPHLLLKLRRRVNAFS---NFFSGPIVVHCSAGVGRTG 830
Cdd:cd14636    77 SMDCDVISRIFRICNLTRPQEGYlMVQQFQYLGWASHrEVPGSKRSFLKLILQVEKWQeecDEGEGRTIIHCLNGGGRSG 156

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|
gi 158138488  831 TYIGIDAMLESLEAEGKVDVYGYVVNLRRQRCLMVQVEAQYILIHQALVE 880
Cdd:cd14636   157 MFCAISIVCEMIKRQNVVDVFHAVKTLRNSKPNMVETPEQYRFCYDVALE 206
CD45 pfam12567
Leukocyte receptor CD45; This family of proteins is found in eukaryotes. Proteins in this ...
 203-259 5.63e-20

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: 84.73  E-value: 5.63e-20
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 158138488   203 VRYIYDDSSKNFNANLEGDKKPKCEYTDCEK-ELKNLPECSQKNVTLSNGSCT-PDKII 259
Cdd:pfam12567    1 VEYTYNSENKSFTAKLNVNDNVECENNDCENnELHNLQECEQINVSISHNSCTsPNKIL 59
PHA02738 PHA02738
hypothetical protein; Provisional
 913-1193 6.76e-20

hypothetical protein; Provisional


Pssm-ID: 222923 [Multi-domain]  Cd Length: 320  Bit Score: 92.30  E-value: 6.76e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158138488  913 LEAEYQRLPSYRSWRTqhIGNQEENKKKNRSSNVVPYDFNRVPLKHElemskeseaesdessdedsdsEETSKYINASFV 992
Cdd:PHA02738   27 ITREHQKVISEKVDGT--FNAEKKNRKLNRYLDAVCFDHSRVILPAE---------------------RNRGDYINANYV 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158138488  993 MSYWKPEMMIAAQGPLKETIGDFWQMIFQRKVKVIVMLTELMSGDQEVCAQYWGEGKQT---YGDMEVMLKDTNKSSAYI 1069
Cdd:PHA02738   84 DGFEYKKKFICGQAPTRQTCYDFYRMLWMEHVQIIVMLCKKKENGREKCFPYWSDVEQGsirFGKFKITTTQVETHPHYV 163

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158138488 1070 LRAFELRHSKrKEPRTVYQYQCTTWKGEELPAEPKDLVTLIQNIKQKLPKSGSEGMKY-HKHAS---ILVHCRDGSQQTG 1145
Cdd:PHA02738  164 KSTLLLTDGT-SATQTVTHFNFTAWPDHDVPKNTSEFLNFVLEVRQCQKELAQESLQIgHNRLQpppIVVHCNAGLGRTP 242

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*...
gi 158138488 1146 LFCALFNLLESAETEDVVDVFQVVKSLRKARPGMVGSFEQYQFLYDIM 1193
Cdd:PHA02738  243 CYCVVDISISRFDACATVSIPSIVSSIRNQRYYSLFIPFQYFFCYRAV 290
PHA02740 PHA02740
protein tyrosine phosphatase; Provisional
 640-881 3.37e-18

protein tyrosine phosphatase; Provisional


Pssm-ID: 165107 [Multi-domain]  Cd Length: 298  Bit Score: 86.94  E-value: 3.37e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158138488  640 DARKSQNQNKNRYVD-ILPYDYNRVELSEINGDAGSTYINASYIDGFKEPRKYIAAQGPRDETVDDFWKMIWEQKATVIV 718
Cdd:PHA02740   41 EANKACAQAENKAKDeNLALHITRLLHRRIKLFNDEKVLDARFVDGYDFEQKFICIINLCEDACDKFLQALSDNKVQIIV 120

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158138488  719 MVTRCEEgnRNKCAEYWPCMEEGTRTFRDVVVTINDHKRCPDYIIQKLSIAHKKEKAtgREVTHIQFTSWPDHGVPEDPH 798
Cdd:PHA02740  121 LISRHAD--KKCFNQFWSLKEGCVITSDKFQIETLEIIIKPHFNLTLLSLTDKFGQA--QKISHFQYTAWPADGFSHDPD 196

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158138488  799 -----------LLLKLRRRvNAFSNFfsGPIVVHCSAGVGRTGTYIGIDAMLESLEAEGKVDVYGYVVNLRRQRCLMVQV 867
Cdd:PHA02740  197 afidffcniddLCADLEKH-KADGKI--APIIIDCIDGISSSAVFCVFDICATEFDKTGMLSIANALKKVRQKKYGCMNC 273

                         250
                  ....*....|....
gi 158138488  868 EAQYILIHQALVEY 881
Cdd:PHA02740  274 LDDYVFCYHLIAAY 287
R-PTPc-U-2 cd14637
PTP domain of receptor-type tyrosine-protein phosphatase U, repeat 2; Receptor-type ...
 676-880 2.90e-16

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: 78.80  E-value: 2.90e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158138488  676 YINASYIDGFKEPRKYIAAQGPRDETVDDFWKMIWEQKATVIVMVTRCEEGNRN-KCAEYWPcmEEGTRTFRDVVVTIND 754
Cdd:cd14637     1 YINAALTDSYTRSAAFIVTLHPLQNTTTDFWRLVYDYGCTSVVMLNQLNQSNSAwPCLQYWP--EPGLQQYGPMEVEFVS 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158138488  755 HKRCPDYIIQKLSIAHKKEKATGR-EVTHIQFTSW-PDHGVPEDPHLLLKLRRRVNAF-SNFFSGPIVVHCSAGVGRTGT 831
Cdd:cd14637    79 GSADEDIVTRLFRVQNITRLQEGHlMVRHFQFLRWsAYRDTPDSKKAFLHLLASVEKWqRESGEGRTVVHCLNGGGRSGT 158

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*....
gi 158138488  832 YIGIDAMLESLEAEGKVDVYGYVVNLRRQRCLMVQVEAQYILIHQALVE 880
Cdd:cd14637   159 YCASAMILEMIRCHNIVDVFYAVKTLRNYKPNMVETLEQYRFCYEIALE 207
PTP_YopH-like cd14559
YopH and related bacterial protein tyrosine phosphatases; Yersinia outer protein H (YopH) ...
 677-871 2.87e-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: 70.51  E-value: 2.87e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158138488  677 INASYIDgFKEPRKYIAAQGPRDETVDDFWKMIWEQKATVIVMVTRCEEGNRNKCAEYWpcmeegTRTFRDVVVTINDHK 756
Cdd:cd14559    18 LNANRVQ-IGNKNVAIACQYPKNEQLEDHLKMLADNRTPCLVVLASNKDIQRKGLPPYF------RQSGTYGSVTVKSKK 90

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158138488  757 RCPDYIIQKLSIAHKKEKATGREVTH----IQFTSWPDHGvPEDPHLLLKLRRRVN----------------AFSNFFSG 816
Cdd:cd14559    91 TGKDELVDGLKADMYNLKITDGNKTItipvVHVTNWPDHT-AISSEGLKELADLVNksaeekrnfykskgssAINDKNKL 169

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 158138488  817 PIVVHCSAGVGRTGTYIGIDAMLESleaEGKVDVYGYVVNLRRQRC-LMVQVEAQY 871
Cdd:cd14559   170 LPVIHCRAGVGRTGQLAAAMELNKS---PNNLSVEDIVSDMRTSRNgKMVQKDEQL 222
PHA02740 PHA02740
protein tyrosine phosphatase; Provisional
 985-1194 1.56e-10

protein tyrosine phosphatase; Provisional


Pssm-ID: 165107 [Multi-domain]  Cd Length: 298  Bit Score: 63.83  E-value: 1.56e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158138488  985 KYINASFVMSYWKPEMMIAAQGPLKETIGDFWQMIFQRKVKVIVMLTELmsGDQEVCAQYWGEGKQ---TYGDMEVMLKD 1061
Cdd:PHA02740   77 KVLDARFVDGYDFEQKFICIINLCEDACDKFLQALSDNKVQIIVLISRH--ADKKCFNQFWSLKEGcviTSDKFQIETLE 154

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158138488 1062 TNKSSAYILRAFELRHSKRKEpRTVYQYQCTTWKGEELPAEPKDLVTLIQNIKQ---KLPKSGSEGmkyhKHASILVHCR 1138
Cdd:PHA02740  155 IIIKPHFNLTLLSLTDKFGQA-QKISHFQYTAWPADGFSHDPDAFIDFFCNIDDlcaDLEKHKADG----KIAPIIIDCI 229

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 158138488 1139 DGSQQTGLFCALFNLLESAETEDVVDVFQVVKSLRKARPGMVGSFEQYQFLYDIMA 1194
Cdd:PHA02740  230 DGISSSAVFCVFDICATEFDKTGMLSIANALKKVRQKKYGCMNCLDDYVFCYHLIA 285
FN3 cd00063
Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein ...
 366-431 2.07e-08

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: 52.88  E-value: 2.07e-08
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 158138488  366 HVQCKNSTNSTTLVSWAEPA---SKHHGYILCYKKTPSE---KCENLANDVNSFEVKNLRPYTEYTVSLFAY 431
Cdd:cd00063     6 NLRVTDVTSTSVTLSWTPPEddgGPITGYVVEYREKGSGdwkEVEVTPGSETSYTLTGLKPGTEYEFRVRAV 77
FN3 cd00063
Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein ...
 454-534 1.68e-07

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: 50.19  E-value: 1.68e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158138488  454 PGKVNGMKTSRASDNSINVTCNSPYEINGPEARYILEVKSGGS----LVKTFNQSTCKFVVDNLYYSTDYEFLVYFYNGE 529
Cdd:cd00063     1 PSPPTNLRVTDVTSTSVTLSWTPPEDDGGPITGYVVEYREKGSgdwkEVEVTPGSETSYTLTGLKPGTEYEFRVRAVNGG 80


                  ....*
gi 158138488  530 YLGDP 534
Cdd:cd00063    81 GESPP 85
FN3 smart00060
Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, ...
 365-431 6.74e-07

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: 48.38  E-value: 6.74e-07
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 158138488    365 PHVQCKNSTNSTTLVSWAEPASKHH-GYILCYK-----KTPSEKCENLANDVNSFEVKNLRPYTEYTVSLFAY 431
Cdd:smart00060    5 SNLRVTDVTSTSVTLSWEPPPDDGItGYIVGYRveyreEGSEWKEVNVTPSSTSYTLTGLKPGTEYEFRVRAV 77
PHA03255 PHA03255
BDLF3; Provisional
 82-191 1.02e-06

BDLF3; Provisional


Pssm-ID: 165513 [Multi-domain]  Cd Length: 234  Bit Score: 51.44  E-value: 1.02e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158138488   82 TPQPDSQTPSARGADTQTLSSQ---------ADLTTLTAapSGETDPPgvpeestVPETFPGGTPILARNSTAPSPTHTS 152
Cdd:PHA03255   45 TPSPSASGPSTNQSTTLTTTSApitttailsTNTTTVTS--TGTTVTP-------VPTTSNASTINVTTKVTAQNITATE 115

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 158138488  153 NVSTTDISSGANLTTPAPSTLG---FASNTTTSTeiATPQTK 191
Cdd:PHA03255  116 AGTGTSTGVTSNVTTRSSSTTSattRITNATTLA--PTLSSK 155
fn3 pfam00041
Fibronectin type III domain;
367-431 1.35e-06

Fibronectin type III domain;


Pssm-ID: 394996 [Multi-domain]  Cd Length: 85  Bit Score: 47.41  E-value: 1.35e-06
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 158138488   367 VQCKNSTNSTTLVSWAEPASKH---HGYILCYKKTPSEKCE---NLANDVNSFEVKNLRPYTEYTVSLFAY 431
Cdd:pfam00041    6 LTVTDVTSTSLTVSWTPPPDGNgpiTGYEVEYRPKNSGEPWneiTVPGTTTSVTLTGLKPGTEYEVRVQAV 76
CDC14 COG2453
Protein-tyrosine phosphatase [Signal transduction mechanisms];
788-876 1.39e-05

Protein-tyrosine phosphatase [Signal transduction mechanisms];


Pssm-ID: 441989 [Multi-domain]  Cd Length: 140  Bit Score: 46.12  E-value: 1.39e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158138488  788 WPDHGVPEDPHL---LLKLRRRVNAfsnffSGPIVVHCSAGVGRTGTYIGIDAMLESLEAEgkvDVYGYVvnlRRQRCLM 864
Cdd:COG2453    55 IPDFGAPDDEQLqeaVDFIDEALRE-----GKKVLVHCRGGIGRTGTVAAAYLVLLGLSAE---EALARV---RAARPGA 123

                          90
                  ....*....|..
gi 158138488  865 VQVEAQYILIHQ 876
Cdd:COG2453   124 VETPAQRAFLER 135
CDKN3-like cd14505
cyclin-dependent kinase inhibitor 3 and similar proteins; This family is composed of ...
 1133-1191 4.91e-05

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


Pssm-ID: 350355 [Multi-domain]  Cd Length: 163  Bit Score: 44.95  E-value: 4.91e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 158138488 1133 ILVHCRDGSQQTGLFCALFnLLEsaeTEDVVDVFQVVKSLRKARPGMVGSFEQYQFLYD 1191
Cdd:cd14505   109 VLIHCKGGLGRTGLIAACL-LLE---LGDTLDPEQAIAAVRALRPGAIQTPKQENFLHQ 163
Wzy_O6_O28 NF033860
oligosaccharide repeat unit polymerase; Members of this family are oligosaccharide repeat unit ...
 521-580 2.71e-04

oligosaccharide repeat unit polymerase; Members of this family are oligosaccharide repeat unit polymerases in a subfamily that includes the Wzy proteins for polymerization of the O-antigens O6, O28, O39, O59, and several others.


Pssm-ID: 468211  Cd Length: 384  Bit Score: 44.91  E-value: 2.71e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 158138488  521 FLVYFYNGEYLGDpeikPQSTSYNSKALIIFLVFLIIVTSIALLVVLYKIYDLRKKRSSN 580
Cdd:NF033860   18 FIYFIITGELGGD----FSGVEINLSNILLLIILLLILLFFLFLYLLYKLFKKIKVKNKS 73
PTP_YopH-like cd14559
YopH and related bacterial protein tyrosine phosphatases; Yersinia outer protein H (YopH) ...
 1002-1189 6.18e-04

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: 42.77  E-value: 6.18e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158138488 1002 IAAQGPLKETIGDFWQMIFQRKVKVIVMLTelmSGDQEVCAQ---YWGEGKqTYGDMEVMLKDTNKSSA--------YIL 1070
Cdd:cd14559    32 IACQYPKNEQLEDHLKMLADNRTPCLVVLA---SNKDIQRKGlppYFRQSG-TYGSVTVKSKKTGKDELvdglkadmYNL 107

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158138488 1071 RafeLRHSKRKEPRTVYQyqCTTWKG------EELpAEPKDLVTL-IQNIKQKLPKSGSEGMKYHKHASILVHCRDGSQQ 1143
Cdd:cd14559   108 K---ITDGNKTITIPVVH--VTNWPDhtaissEGL-KELADLVNKsAEEKRNFYKSKGSSAINDKNKLLPVIHCRAGVGR 181

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*..
gi 158138488 1144 TGLFCALFNLLESaetEDVVDVFQVVKSLRKARPG-MVGSFEQYQFL 1189
Cdd:cd14559   182 TGQLAAAMELNKS---PNNLSVEDIVSDMRTSRNGkMVQKDEQLDTL 225
PTP_DSP_cys cd14494
cys-based protein tyrosine phosphatase and dual-specificity phosphatase superfamily; This ...
 816-842 7.92e-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: 40.41  E-value: 7.92e-04
                          10        20
                  ....*....|....*....|....*..
gi 158138488  816 GPIVVHCSAGVGRTGTYIGIDAMLESL 842
Cdd:cd14494    57 EPVLVHCKAGVGRTGTLVACYLVLLGG 83
PTP_DSP_cys cd14494
cys-based protein tyrosine phosphatase and dual-specificity phosphatase superfamily; This ...
 1133-1191 1.12e-03

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: 40.03  E-value: 1.12e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 158138488 1133 ILVHCRDGSQQTGLFCALFNLLESAETedvvdVFQVVKSLRKARPGMVG-SFEQYQFLYD 1191
Cdd:cd14494    59 VLVHCKAGVGRTGTLVACYLVLLGGMS-----AEEAVRIVRLIRPGGIPqTIEQLDFLIK 113
CDC14_C cd14499
C-terminal dual-specificity phosphatase domain of CDC14 family proteins; The cell division ...
 816-838 1.20e-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: 1.20e-03
                          10        20
                  ....*....|....*....|...
gi 158138488  816 GPIVVHCSAGVGRTGTYIGIDAM 838
Cdd:cd14499   110 GAIAVHCKAGLGRTGTLIACYLM 132
PRK10856 PRK10856
cytoskeleton protein RodZ;
77-163 1.27e-03

cytoskeleton protein RodZ;


Pssm-ID: 236776 [Multi-domain]  Cd Length: 331  Bit Score: 42.71  E-value: 1.27e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158138488   77 LMPHLTPQPDSQTPSARGADTQTLSSQADLTTLTAAPSGETDPPGV--PEESTV-PETFPGGTPILARNSTAPSPTHTSN 153
Cdd:PRK10856  164 LDTSTTTDPATTPAPAAPVDTTPTNSQTPAVATAPAPAVDPQQNAVvaPSQANVdTAATPAPAAPATPDGAAPLPTDQAG 243

                          90
                  ....*....|
gi 158138488  154 VSTTDISSGA 163
Cdd:PRK10856  244 VSTPAADPNA 253
fn3 pfam00041
Fibronectin type III domain;
455-534 1.39e-03

Fibronectin type III domain;


Pssm-ID: 394996 [Multi-domain]  Cd Length: 85  Bit Score: 38.94  E-value: 1.39e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158138488   455 GKVNGMKTSRASDNSINVTCNSPYEINGPEARYILEVKS--GGSLVKTFN--QSTCKFVVDNLYYSTDYEFLVYFYNGEY 530
Cdd:pfam00041    1 SAPSNLTVTDVTSTSLTVSWTPPPDGNGPITGYEVEYRPknSGEPWNEITvpGTTTSVTLTGLKPGTEYEVRVQAVNGGG 80


                   ....
gi 158138488   531 LGDP 534
Cdd:pfam00041   81 EGPP 84
Chi1 COG3469
Chitinase [Carbohydrate transport and metabolism];
21-193 3.98e-03

Chitinase [Carbohydrate transport and metabolism];


Pssm-ID: 442692 [Multi-domain]  Cd Length: 534  Bit Score: 41.28  E-value: 3.98e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158138488   21 VTGQGTTDDGLDTTEIVLLPQTDPLPARTTEFTPPSISERGNGSSETTYLPGFSSTLMPHLTPQPDSQTPSARGADTQTL 100
Cdd:COG3469    17 ATAVTLLGAAATAASVTLTAATATTVVSTTGSVVVAASGSAGSGTGTTAASSTAATSSTTSTTATATAAAAAATSTSATL 96

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158138488  101 SSQADLTTLTAAPSGETDPPGVPEESTVPETFPGGTPILARNS---------TAPSPTHTSNVSTTDISSGANLTTPAPS 171
Cdd:COG3469    97 VATSTASGANTGTSTVTTTSTGAGSVTSTTSSTAGSTTTSGASatssagsttTTTTVSGTETATGGTTTTSTTTTTTSAS 176

                         170       180
                  ....*....|....*....|..
gi 158138488  172 TLGFASNTTTSTEIATPQTKPS 193
Cdd:COG3469   177 TTPSATTTATATTASGATTPSA 198
FN3 smart00060
Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, ...
 454-524 4.21e-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: 4.21e-03
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 158138488    454 PGKVNGMKTSRASDNSINVTCNSPYE--INGPEARYILEVKSGGSLVKTFN--QSTCKFVVDNLYYSTDYEFLVY 524
Cdd:smart00060    1 PSPPSNLRVTDVTSTSVTLSWEPPPDdgITGYIVGYRVEYREEGSEWKEVNvtPSSTSYTLTGLKPGTEYEFRVR 75
CDC14 COG2453
Protein-tyrosine phosphatase [Signal transduction mechanisms];
1127-1192 5.17e-03

Protein-tyrosine phosphatase [Signal transduction mechanisms];


Pssm-ID: 441989 [Multi-domain]  Cd Length: 140  Bit Score: 38.80  E-value: 5.17e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 158138488 1127 YHKHASILVHCRDGSQQTGLFCALFNLLESAETEDVVDVfqvvksLRKARPGMVGSFEQYQFLYDI 1192
Cdd:COG2453    77 LREGKKVLVHCRGGIGRTGTVAAAYLVLLGLSAEEALAR------VRAARPGAVETPAQRAFLERF 136
PTP_PTPDC1 cd14506
protein tyrosine phosphatase domain of PTP domain-containing protein 1; protein tyrosine ...
 787-833 5.63e-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: 5.63e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*..
gi 158138488  787 SWPDHGVPEdPHLLLKLRRrVNAFSNFFSGPIVVHCSAGVGRTGTYI 833
Cdd:cd14506    83 GWKDYGVPS-LTTILDIVK-VMAFALQEGGKVAVHCHAGLGRTGVLI 127
DUSP23 cd14504
dual specificity phosphatase 23; Dual specificity phosphatase 23 (DUSP23), also known as ...
 812-840 9.01e-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: 38.03  E-value: 9.01e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|
gi 158138488  812 NFFSGPIVVHCSAGVGRTGT----YI-------GIDAMLE 840
Cdd:cd14504    79 NAKNEAVLVHCLAGKGRTGTmlacYLvktgkisAVDAINE 118
 
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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