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Conserved domains on  [gi|2032733617|ref|XP_041317758|]
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receptor-type tyrosine-protein phosphatase gamma [Pyrgilauda ruficollis]

Protein Classification

fibronectin type III domain-containing protein( domain architecture ID 12931086)

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-G-1 cd17667
catalytic domain of receptor-type tyrosine-protein phosphatase G, repeat 1; Receptor-type ...
 709-982 0e+00

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: 640.55  E-value: 0e+00
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032733617  709 FSEDFEEVQRCTADMNITAEHSNHPDNKHKNRYINILAYDHSRVKLRPLPGKDSKHSDYINANYVDGYNKAKAYIATQGP 788
Cdd:cd17667      1 FSEDFEEVQRCTADMNITAEHSNHPDNKHKNRYINILAYDHSRVKLRPLPGKDSKHSDYINANYVDGYNKAKAYIATQGP 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032733617  789 LKSTFEDFWRMIWEQNTGIIVMITNLVEKGRRKCDQYWPTENSEEYGNIIVTLKSTNVHACYTVRRFTVRNTKMKKGQKG 868
Cdd:cd17667     81 LKSTFEDFWRMIWEQNTGIIVMITNLVEKGRRKCDQYWPTENSEEYGNIIVTLKSTKIHACYTVRRFSIRNTKVKKGQKG 160

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032733617  869 NPKGRQNERTVIQYHYTQWPDMGVPEYALPVLTFVRRSSAARTPDMGPVVVHCSAGVGRTGTYIVIDSMLQQIKDKSTVN 948
Cdd:cd17667    161 NPKGRQNERTVIQYHYTQWPDMGVPEYALPVLTFVRRSSAARTPEMGPVLVHCSAGVGRTGTYIVIDSMLQQIKDKSTVN 240

                          250       260       270
                   ....*....|....*....|....*....|....
gi 2032733617  949 VLGFLKHIRTQRNYLVQTEEQYIFIHDALLEAIL 982
Cdd:cd17667    241 VLGFLKHIRTQRNYLVQTEEQYIFIHDALLEAIL 274
R-PTP-G-2 cd17670
PTP-like domain of receptor-type tyrosine-protein phosphatase G, repeat 2; Receptor-type ...
 1066-1270 8.92e-159

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: 473.78  E-value: 8.92e-159
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032733617 1066 YINASYIMGYYRSNEFIITQHPLPHTTKDFWRMIWDHNAQIIVMLPDNQSLAEDEFVYWPSREESMNCEAFTVTLISKDR 1145
Cdd:cd17670      1 YINASYIMGYYRSNEFIITQHPLPHTTKDFWRMIWDHNAQIIVMLPDNQGLAEDEFVYWPSREESMNCEAFTVTLISKDR 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032733617 1146 LCLSNEEQIIIHDFILEATQDDYVLEVRHFQCPKWPNPDAPISSTFELINVIKEEALTRDGPTIVHDEYGAVSAGTLCAL 1225
Cdd:cd17670     81 LCLSNEEQIIIHDFILEATQDDYVLEVRHFQCPKWPNPDAPISSTFELINVIKEEALTRDGPTIVHDEFGAVSAGTLCAL 160

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*
gi 2032733617 1226 TTLSQQLENENAVDVFQVAKMINLMRPGVFTDIEQYQFLYKAMLS 1270
Cdd:cd17670    161 TTLSQQLENENAVDVYQVAKMINLMRPGVFTDIEQYQFLYKAMLS 205
alpha_CARP_receptor_like cd03122
Carbonic anhydrase alpha related protein, receptor_like subfamily. Carbonic anhydrase related ...
 1-203 8.89e-103

Carbonic anhydrase alpha related protein, receptor_like subfamily. Carbonic anhydrase related proteins (CARPs) are sequence similar to carbonic anhydrases. Carbonic anhydrases are zinc-containing enzymes that catalyze the reversible hydration of carbon dioxide in a two-step mechanism. CARPs have lost conserved histidines involved in zinc binding and consequently their catalytic activity. This sub-family of carbonic anhydrase-related domains found in tyrosine phosphatase receptors may play a role in cell adhesion.


:

Pssm-ID: 239396 [Multi-domain]  Cd Length: 253  Bit Score: 326.62  E-value: 8.89e-103
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032733617    1 MKNTGKTVAILLKD---DYFVSGAGLPGRFKAEKVEFHWGQSNgSAGSEHSINGKRFPVEMQIFFYNPDDFDSFgTAVLE 77
Cdd:cd03122     51 LENTGKTVILRLEGnssDPFVSGGPLLGRYKFSEITFHWGTCN-SDGSEHSIDGHKFPLEMQILHRNTDFFDSF-EAIKS 128

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032733617   78 NRVVGAMAVFFQVSQRDNSALDPIIHGLKGVVHHEKETFLDPFVLRELLPTSLGSYYRYTGSLTTPPCSEIVEWIVFRKP 157
Cdd:cd03122    129 PGGVLALAYLFELSHEDNPFLDPIIEGLRNVSRPGKEVELPPFPLSDLLPPFTDKYYSYEGSLTTPPCSETVEWIVFREP 208

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*.
gi 2032733617  158 VPISYHQLEAFYSIFTTEQQDhVKSVEYLRNNFRPQQSLNNRKVSK 203
Cdd:cd03122    209 VPISSRQLEAFRELLTRRQDG-VMSGDYLPNNGRPQQPLGSRTVFS 253
FN3 cd00063
Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein ...
 233-322 1.35e-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: 53.27  E-value: 1.35e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032733617  233 PPVNMKVQPVNRTALLVTWNQPETIyHPPIMNYMISYSWTKNEDEKEktFTKDSDKDLKAIISHVSPDILYLFRVQAVcR 312
Cdd:cd00063      3 PPTNLRVTDVTSTSVTLSWTPPEDD-GGPITGYVVEYREKGSGDWKE--VEVTPGSETSYTLTGLKPGTEYEFRVRAV-N 78

                           90
                   ....*....|
gi 2032733617  313 NEMRSDFSQT 322
Cdd:cd00063     79 GGGESPPSES 88
 
Name Accession Description Interval E-value
R-PTPc-G-1 cd17667
catalytic domain of receptor-type tyrosine-protein phosphatase G, repeat 1; Receptor-type ...
 709-982 0e+00

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: 640.55  E-value: 0e+00
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032733617  709 FSEDFEEVQRCTADMNITAEHSNHPDNKHKNRYINILAYDHSRVKLRPLPGKDSKHSDYINANYVDGYNKAKAYIATQGP 788
Cdd:cd17667      1 FSEDFEEVQRCTADMNITAEHSNHPDNKHKNRYINILAYDHSRVKLRPLPGKDSKHSDYINANYVDGYNKAKAYIATQGP 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032733617  789 LKSTFEDFWRMIWEQNTGIIVMITNLVEKGRRKCDQYWPTENSEEYGNIIVTLKSTNVHACYTVRRFTVRNTKMKKGQKG 868
Cdd:cd17667     81 LKSTFEDFWRMIWEQNTGIIVMITNLVEKGRRKCDQYWPTENSEEYGNIIVTLKSTKIHACYTVRRFSIRNTKVKKGQKG 160

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032733617  869 NPKGRQNERTVIQYHYTQWPDMGVPEYALPVLTFVRRSSAARTPDMGPVVVHCSAGVGRTGTYIVIDSMLQQIKDKSTVN 948
Cdd:cd17667    161 NPKGRQNERTVIQYHYTQWPDMGVPEYALPVLTFVRRSSAARTPEMGPVLVHCSAGVGRTGTYIVIDSMLQQIKDKSTVN 240

                          250       260       270
                   ....*....|....*....|....*....|....
gi 2032733617  949 VLGFLKHIRTQRNYLVQTEEQYIFIHDALLEAIL 982
Cdd:cd17667    241 VLGFLKHIRTQRNYLVQTEEQYIFIHDALLEAIL 274
R-PTP-G-2 cd17670
PTP-like domain of receptor-type tyrosine-protein phosphatase G, repeat 2; Receptor-type ...
 1066-1270 8.92e-159

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: 473.78  E-value: 8.92e-159
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032733617 1066 YINASYIMGYYRSNEFIITQHPLPHTTKDFWRMIWDHNAQIIVMLPDNQSLAEDEFVYWPSREESMNCEAFTVTLISKDR 1145
Cdd:cd17670      1 YINASYIMGYYRSNEFIITQHPLPHTTKDFWRMIWDHNAQIIVMLPDNQGLAEDEFVYWPSREESMNCEAFTVTLISKDR 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032733617 1146 LCLSNEEQIIIHDFILEATQDDYVLEVRHFQCPKWPNPDAPISSTFELINVIKEEALTRDGPTIVHDEYGAVSAGTLCAL 1225
Cdd:cd17670     81 LCLSNEEQIIIHDFILEATQDDYVLEVRHFQCPKWPNPDAPISSTFELINVIKEEALTRDGPTIVHDEFGAVSAGTLCAL 160

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*
gi 2032733617 1226 TTLSQQLENENAVDVFQVAKMINLMRPGVFTDIEQYQFLYKAMLS 1270
Cdd:cd17670    161 TTLSQQLENENAVDVYQVAKMINLMRPGVFTDIEQYQFLYKAMLS 205
PTPc smart00194
Protein tyrosine phosphatase, catalytic domain;
708-979 4.87e-120

Protein tyrosine phosphatase, catalytic domain;


Pssm-ID: 214550 [Multi-domain]  Cd Length: 259  Bit Score: 373.53  E-value: 4.87e-120
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032733617   708 GFSEDFEEVQRCTADMnITAEHSNHPDNKHKNRYINILAYDHSRVKLRPLPGKDSkhsDYINANYVDGYNKAKAYIATQG 787
Cdd:smart00194    1 GLEEEFEKLDRLKPDD-ESCTVAAFPENRDKNRYKDVLPYDHTRVKLKPPPGEGS---DYINASYIDGPNGPKAYIATQG 76

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032733617   788 PLKSTFEDFWRMIWEQNTGIIVMITNLVEKGRRKCDQYWPTENSE--EYGNIIVTLKSTNVHACYTVRRFTVRNTkmkkg 865
Cdd:smart00194   77 PLPSTVEDFWRMVWEQKVTVIVMLTELVEKGREKCAQYWPDEEGEplTYGDITVTLKSVEKVDDYTIRTLEVTNT----- 151

                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032733617   866 qkgnpkGRQNERTVIQYHYTQWPDMGVPEYALPVLTFVRRSSAARTPDMGPVVVHCSAGVGRTGTYIVIDSMLQQIKDKS 945
Cdd:smart00194  152 ------GCSETRTVTHYHYTNWPDHGVPESPESILDLIRAVRKSQSTSTGPIVVHCSAGVGRTGTFIAIDILLQQLEAGK 225

                           250       260       270
                    ....*....|....*....|....*....|....
gi 2032733617   946 TVNVLGFLKHIRTQRNYLVQTEEQYIFIHDALLE 979
Cdd:smart00194  226 EVDIFEIVKELRSQRPGMVQTEEQYIFLYRAILE 259
Y_phosphatase pfam00102
Protein-tyrosine phosphatase;
735-979 2.17e-113

Protein-tyrosine phosphatase;


Pssm-ID: 459674 [Multi-domain]  Cd Length: 234  Bit Score: 354.63  E-value: 2.17e-113
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032733617  735 NKHKNRYINILAYDHSRVKLRPLPGkdskHSDYINANYVDGYNKAKAYIATQGPLKSTFEDFWRMIWEQNTGIIVMITNL 814
Cdd:pfam00102    1 NLEKNRYKDVLPYDHTRVKLTGDPG----PSDYINASYIDGYKKPKKYIATQGPLPNTVEDFWRMVWEEKVTIIVMLTEL 76

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032733617  815 VEKGRRKCDQYWPTEN--SEEYGNIIVTLKSTNVH-ACYTVRRFTVRNtkmkkgqkgnpKGRQNERTVIQYHYTQWPDMG 891
Cdd:pfam00102   77 EEKGREKCAQYWPEEEgeSLEYGDFTVTLKKEKEDeKDYTVRTLEVSN-----------GGSEETRTVKHFHYTGWPDHG 145

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032733617  892 VPEYALPVLTFVRR-SSAARTPDMGPVVVHCSAGVGRTGTYIVIDSMLQQIKDKSTVNVLGFLKHIRTQRNYLVQTEEQY 970
Cdd:pfam00102  146 VPESPNSLLDLLRKvRKSSLDGRSGPIVVHCSAGIGRTGTFIAIDIALQQLEAEGEVDIFQIVKELRSQRPGMVQTLEQY 225


                   ....*....
gi 2032733617  971 IFIHDALLE 979
Cdd:pfam00102  226 IFLYDAILE 234
alpha_CARP_receptor_like cd03122
Carbonic anhydrase alpha related protein, receptor_like subfamily. Carbonic anhydrase related ...
 1-203 8.89e-103

Carbonic anhydrase alpha related protein, receptor_like subfamily. Carbonic anhydrase related proteins (CARPs) are sequence similar to carbonic anhydrases. Carbonic anhydrases are zinc-containing enzymes that catalyze the reversible hydration of carbon dioxide in a two-step mechanism. CARPs have lost conserved histidines involved in zinc binding and consequently their catalytic activity. This sub-family of carbonic anhydrase-related domains found in tyrosine phosphatase receptors may play a role in cell adhesion.


Pssm-ID: 239396 [Multi-domain]  Cd Length: 253  Bit Score: 326.62  E-value: 8.89e-103
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032733617    1 MKNTGKTVAILLKD---DYFVSGAGLPGRFKAEKVEFHWGQSNgSAGSEHSINGKRFPVEMQIFFYNPDDFDSFgTAVLE 77
Cdd:cd03122     51 LENTGKTVILRLEGnssDPFVSGGPLLGRYKFSEITFHWGTCN-SDGSEHSIDGHKFPLEMQILHRNTDFFDSF-EAIKS 128

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032733617   78 NRVVGAMAVFFQVSQRDNSALDPIIHGLKGVVHHEKETFLDPFVLRELLPTSLGSYYRYTGSLTTPPCSEIVEWIVFRKP 157
Cdd:cd03122    129 PGGVLALAYLFELSHEDNPFLDPIIEGLRNVSRPGKEVELPPFPLSDLLPPFTDKYYSYEGSLTTPPCSETVEWIVFREP 208

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*.
gi 2032733617  158 VPISYHQLEAFYSIFTTEQQDhVKSVEYLRNNFRPQQSLNNRKVSK 203
Cdd:cd03122    209 VPISSRQLEAFRELLTRRQDG-VMSGDYLPNNGRPQQPLGSRTVFS 253
PTPc smart00194
Protein tyrosine phosphatase, catalytic domain;
1011-1269 2.11e-80

Protein tyrosine phosphatase, catalytic domain;


Pssm-ID: 214550 [Multi-domain]  Cd Length: 259  Bit Score: 264.91  E-value: 2.11e-80
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032733617  1011 LEKQFKLVTQCNAKYVECFSAQKDCNKEKNRNSSVVPSERARVGLAPLPGmKGTDYINASYIMGYYRSNEFIITQHPLPH 1090
Cdd:smart00194    2 LEEEFEKLDRLKPDDESCTVAAFPENRDKNRYKDVLPYDHTRVKLKPPPG-EGSDYINASYIDGPNGPKAYIATQGPLPS 80

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032733617  1091 TTKDFWRMIWDHNAQIIVMLPDNQSL-AEDEFVYWPSRE-ESMNCEAFTVTLISKDRLclsneEQIIIHDFILEATQDDY 1168
Cdd:smart00194   81 TVEDFWRMVWEQKVTVIVMLTELVEKgREKCAQYWPDEEgEPLTYGDITVTLKSVEKV-----DDYTIRTLEVTNTGCSE 155

                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032733617  1169 VLEVRHFQCPKWPNPDAP--ISSTFELINVIKEEALTRDGPTIVHDEYGAVSAGTLCALTTLSQQLENENAVDVFQVAKM 1246
Cdd:smart00194  156 TRTVTHYHYTNWPDHGVPesPESILDLIRAVRKSQSTSTGPIVVHCSAGVGRTGTFIAIDILLQQLEAGKEVDIFEIVKE 235

                           250       260
                    ....*....|....*....|...
gi 2032733617  1247 INLMRPGVFTDIEQYQFLYKAML 1269
Cdd:smart00194  236 LRSQRPGMVQTEEQYIFLYRAIL 258
Y_phosphatase pfam00102
Protein-tyrosine phosphatase;
1036-1269 1.73e-79

Protein-tyrosine phosphatase;


Pssm-ID: 459674 [Multi-domain]  Cd Length: 234  Bit Score: 261.41  E-value: 1.73e-79
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032733617 1036 NKEKNRNSSVVPSERARVGLAPLPGmkGTDYINASYIMGYYRSNEFIITQHPLPHTTKDFWRMIWDHNAQIIVMLPDNQS 1115
Cdd:pfam00102    1 NLEKNRYKDVLPYDHTRVKLTGDPG--PSDYINASYIDGYKKPKKYIATQGPLPNTVEDFWRMVWEEKVTIIVMLTELEE 78

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032733617 1116 LA-EDEFVYWP-SREESMNCEAFTVTLISKDrlclSNEEQIIIHDFILEATQDDYVLEVRHFQCPKWPNPDAP--ISSTF 1191
Cdd:pfam00102   79 KGrEKCAQYWPeEEGESLEYGDFTVTLKKEK----EDEKDYTVRTLEVSNGGSEETRTVKHFHYTGWPDHGVPesPNSLL 154

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2032733617 1192 ELINVIKEEALT-RDGPTIVHDEYGAVSAGTLCALTTLSQQLENENAVDVFQVAKMINLMRPGVFTDIEQYQFLYKAML 1269
Cdd:pfam00102  155 DLLRKVRKSSLDgRSGPIVVHCSAGIGRTGTFIAIDIALQQLEAEGEVDIFQIVKELRSQRPGMVQTLEQYIFLYDAIL 233
Carb_anhydrase smart01057
Eukaryotic-type carbonic anhydrase; Carbonic anhydrases are zinc metalloenzymes which catalyse ...
 1-200 3.45e-79

Eukaryotic-type carbonic anhydrase; Carbonic anhydrases are zinc metalloenzymes which catalyse the reversible hydration of carbon dioxide to bicarbonate.. CAs have essential roles in facilitating the transport of carbon dioxide and protons in the intracellular space, across biological membranes and in the layers of the extracellular space; they are also involved in many other processes, from respiration and photosynthesis in eukaryotes to cyanate degradation in prokaryotes. There are five known evolutionarily distinct CA families (alpha, beta, gamma, delta and epsilon) that have no significant sequence identity and have structurally distinct overall folds. Some CAs are membrane-bound, while others act in the cytosol; there are several related proteins that lack enzymatic activity. The active site of alpha-CAs is well described, consisting of a zinc ion coordinated through 3 histidine residues and a water molecule/hydroxide ion that acts as a potent nucleophile. The enzyme employs a two-step mechanism: in the first step, there is a nucleophilic attack of a zinc-bound hydroxide ion on carbon dioxide; in the second step, the active site is regenerated by the ionisation of the zinc-bound water molecule and the removal of a proton from the active site. Beta- and gamma-CAs also employ a zinc hydroxide mechanism, although at least some beta-class enzymes do not have water directly coordinated to the metal ion.


Pssm-ID: 215000 [Multi-domain]  Cd Length: 247  Bit Score: 261.09  E-value: 3.45e-79
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032733617     1 MKNTGKTVAILLKDD-YFVSGAGLPGRFKAEKVEFHWGqSNGSAGSEHSINGKRFPVEMQIFFYNPDDfdSFGTAVLENR 79
Cdd:smart01057   56 ILNNGHTVQVNFDDDgSTLSGGPLPGRYRLKQFHFHWG-GSDSEGSEHTIDGKRFPLELHLVHYNSKG--SFSEAVSKPG 132

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032733617    80 VVGAMAVFFQVSQRDNSALDPIIHGLKGVVHHEKETFLDPFVLRELLPTSLGSYYRYTGSLTTPPCSEIVEWIVFRKPVP 159
Cdd:smart01057  133 GLAVVAVFFKVGAEENPALQAILDHLPLIKYKGQETELTPFDLSSLLPASTRHYYTYNGSLTTPPCSEGVTWIVFKEPIT 212

                           170       180       190       200
                    ....*....|....*....|....*....|....*....|.
gi 2032733617   160 ISYHQLEAFYSIFTTEQQdhvksvEYLRNNFRPQQSLNNRK 200
Cdd:smart01057  213 ISTEQLEKFRTLLPMEGN------EPLVNNARPLQPLNGRV 247
Carb_anhydrase pfam00194
Eukaryotic-type carbonic anhydrase;
1-204 1.93e-76

Eukaryotic-type carbonic anhydrase;


Pssm-ID: 459707 [Multi-domain]  Cd Length: 252  Bit Score: 253.34  E-value: 1.93e-76
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032733617    1 MKNTGKTVAILLKDDY--FVSGAGLPGRFKAEKVEFHWGqSNGSAGSEHSINGKRFPVEMQIFFYNpDDFDSFGTAVLEN 78
Cdd:pfam00194   51 LTNNGHTVQVSLDDGDpsTISGGPLATRYRLVQFHFHWG-STDSRGSEHTIDGKRYPAELHIVHYN-SKYKSFDEAAKHP 128

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032733617   79 RVVGAMAVFFQVSQRDNSALDPIIHGLKGVVHHEKETFLDPFVLRELLPTSLGSYYRYTGSLTTPPCSEIVEWIVFRKPV 158
Cdd:pfam00194  129 DGLAVLGVFFEVGDENNPYLQPIVSALDNIKYKGKSVLLPPFDLSDLLPEDLTSYYTYNGSLTTPPCSESVTWIVFKEPI 208

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*.
gi 2032733617  159 PISYHQLEAFYSIFTTEQQDHvksVEYLRNNFRPQQSLNNRKVSKS 204
Cdd:pfam00194  209 SISEEQLEAFRTLLFSDGGEE---PRPLVNNFRPTQPLNGRVVFAS 251
PHA02738 PHA02738
hypothetical protein; Provisional
 712-977 1.20e-47

hypothetical protein; Provisional


Pssm-ID: 222923 [Multi-domain]  Cd Length: 320  Bit Score: 173.57  E-value: 1.20e-47
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032733617  712 DFEEVqrctadmnITAEH------------SNHPDNKHKNRYINILAYDHSRVKLRplpgKDSKHSDYINANYVDGYNKA 779
Cdd:PHA02738    22 DCEEV--------ITREHqkvisekvdgtfNAEKKNRKLNRYLDAVCFDHSRVILP----AERNRGDYINANYVDGFEYK 89

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032733617  780 KAYIATQGPLKSTFEDFWRMIWEQNTGIIVMITNLVEKGRRKCDQYWPT--ENSEEYGNIIVTLKSTNVHACYTVRRFTV 857
Cdd:PHA02738    90 KKFICGQAPTRQTCYDFYRMLWMEHVQIIVMLCKKKENGREKCFPYWSDveQGSIRFGKFKITTTQVETHPHYVKSTLLL 169

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032733617  858 RNtkmkkgqkgnpkGRQNERTVIQYHYTQWPDMGVPEYALPVLTFV------RRSSAARTPDMG-------PVVVHCSAG 924
Cdd:PHA02738   170 TD------------GTSATQTVTHFNFTAWPDHDVPKNTSEFLNFVlevrqcQKELAQESLQIGhnrlqppPIVVHCNAG 237

                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|...
gi 2032733617  925 VGRTGTYIVIDSMLQQIKDKSTVNVLGFLKHIRTQRNYLVQTEEQYIFIHDAL 977
Cdd:PHA02738   238 LGRTPCYCVVDISISRFDACATVSIPSIVSSIRNQRYYSLFIPFQYFFCYRAV 290
COG5599 COG5599
Protein tyrosine phosphatase [Signal transduction mechanisms];
729-973 6.43e-43

Protein tyrosine phosphatase [Signal transduction mechanisms];


Pssm-ID: 444335 [Multi-domain]  Cd Length: 282  Bit Score: 158.33  E-value: 6.43e-43
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032733617  729 HSNHPDNKHKNRYINILAYDHSRVklrplpGKDSKhsdYINANYVDGYNKaKAYIATQGPLKSTFEDFWRMIWEQNTGII 808
Cdd:COG5599     36 YLQNINGSPLNRFRDIQPYKETAL------RANLG---YLNANYIQVIGN-HRYIATQYPLEEQLEDFFQMLFDNNTPVL 105

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032733617  809 VMITNLVE--KGRRKCDQYWPTenSEEYGNIIVTLKSTNVHACYTvrRFTVRNTKMKKGQKGnpkgrQNERTVIQYHYTQ 886
Cdd:COG5599    106 VVLASDDEisKPKVKMPVYFRQ--DGEYGKYEVSSELTESIQLRD--GIEARTYVLTIKGTG-----QKKIEIPVLHVKN 176

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032733617  887 WPDMGVP--EYALPVLTFVRRSSAARTPDMGPVVVHCSAGVGRTGTYIVIDSMLQQIKDKS--TVNVLGFLKHIRTQRNY 962
Cdd:COG5599    177 WPDHGAIsaEALKNLADLIDKKEKIKDPDKLLPVVHCRAGVGRTGTLIACLALSKSINALVqiTLSVEEIVIDMRTSRNG 256

                          250
                   ....*....|..
gi 2032733617  963 -LVQTEEQYIFI 973
Cdd:COG5599    257 gMVQTSEQLDVL 268
Cah COG3338
Carbonic anhydrase [Inorganic ion transport and metabolism];
1-204 5.79e-34

Carbonic anhydrase [Inorganic ion transport and metabolism];


Pssm-ID: 442567 [Multi-domain]  Cd Length: 247  Bit Score: 131.16  E-value: 5.79e-34
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032733617    1 MKNTGKTVAILLKDDYFVSGAGLpgRFKAEKVEFHwgqsngsAGSEHSINGKRFPVEMQIFFYNPDDfdsfGTAVLenrv 80
Cdd:COG3338     82 IVNNGHTIQVNVDPGSTLTVDGK--RYELKQFHFH-------TPSEHTINGKSYPMEAHLVHKDADG----ELAVV---- 144

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032733617   81 vgamAVFFQVSQRdNSALDPIIHGL---KGvvhhEKETFLDPFVLRELLPTSLgSYYRYTGSLTTPPCSEIVEWIVFRKP 157
Cdd:COG3338    145 ----GVLFEEGAE-NPALAKLWANLpleAG----EEVALDATIDLNDLLPEDR-SYYRYSGSLTTPPCSEGVLWIVLKQP 214

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*..
gi 2032733617  158 VPISYHQLEAFYSIFtteqqdhvksveylRNNFRPQQSLNNRKVSKS 204
Cdd:COG3338    215 ITVSAEQIEAFARLY--------------PNNARPVQPLNGRLILES 247
PHA02747 PHA02747
protein tyrosine phosphatase; Provisional
 987-1277 5.38e-25

protein tyrosine phosphatase; Provisional


Pssm-ID: 165114 [Multi-domain]  Cd Length: 312  Bit Score: 107.39  E-value: 5.38e-25
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032733617  987 EVSANQLHSYVNSILIPGIggkTRLEkQFKLVTQCNAKYVECFsaQKDCNKEKNRNSSVVPSERARVGLAPLPGmKGTDY 1066
Cdd:PHA02747     8 ECRAIDFLKRRNQLNCFGI---IRDE-HHQIILKPFDGLIANF--EKPENQPKNRYWDIPCWDHNRVILDSGGG-STSDY 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032733617 1067 INASYIMGYYRSNEFIITQHPLPHTTKDFWRMIWDHNAQIIVMLPDNQSLAEDE--FVYW-PSREESMNCEAFTVTLISK 1143
Cdd:PHA02747    81 IHANWIDGFEDDKKFIATQGPFAETCADFWKAVWQEHCSIIVMLTPTKGTNGEEkcYQYWcLNEDGNIDMEDFRIETLKT 160

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032733617 1144 DRLCLSNEEQIIIHDFILEATQddyvlEVRHFQCPKWPNPDAPISST-----FELINVIKEEALTRDG-------PTIVH 1211
Cdd:PHA02747   161 SVRAKYILTLIEITDKILKDSR-----KISHFQCSEWFEDETPSDHPdfikfIKIIDINRKKSGKLFNpkdallcPIVVH 235

                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2032733617 1212 DEYGAVSAGTLCALTTLSQQLENENAVDVFQVAKMINLMRPGVFTDIEQYQFL---YKAMLSLVSTKEN 1277
Cdd:PHA02747   236 CSDGVGKTGIFCAVDICLNQLVKRKAICLAKTAEKIREQRHAGIMNFDDYLFIqpgYEVLHYFLSKIKA 304
PLN02179 PLN02179
carbonic anhydrase
 15-156 9.06e-10

carbonic anhydrase


Pssm-ID: 177835  Cd Length: 235  Bit Score: 60.38  E-value: 9.06e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032733617   15 DYFVSGAGLPGRFKAEKVEFHWGQSNGSAGSEHSINGKRFPVEMQIFFynpddfdsfGTAVLENRVVGamaVFFQVSQRD 94
Cdd:PLN02179   101 DVMVSWKGDAGKITIHQTDYKLVQCHWHSPSEHTINGTSYDLELHMVH---------TSASGKTAVVG---VLYKLGEPD 168

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2032733617   95 nSALDPIIHGLKGVVHHEKET-FLDPFVLRellpTSLGSYYRYTGSLTTPPCSEIVEWIVFRK 156
Cdd:PLN02179   169 -EFLTKLLNGIKGVGKKEINLgIVDPRDIR----FETNNFYRYIGSLTIPPCTEGVIWTVVKR 226
FN3 cd00063
Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein ...
 233-322 1.35e-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: 53.27  E-value: 1.35e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032733617  233 PPVNMKVQPVNRTALLVTWNQPETIyHPPIMNYMISYSWTKNEDEKEktFTKDSDKDLKAIISHVSPDILYLFRVQAVcR 312
Cdd:cd00063      3 PPTNLRVTDVTSTSVTLSWTPPEDD-GGPITGYVVEYREKGSGDWKE--VEVTPGSETSYTLTGLKPGTEYEFRVRAV-N 78

                           90
                   ....*....|
gi 2032733617  313 NEMRSDFSQT 322
Cdd:cd00063     79 GGGESPPSES 88
FN3 smart00060
Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, ...
 233-310 1.41e-08

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: 53.00  E-value: 1.41e-08
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2032733617   233 PPVNMKVQPVNRTALLVTWNQPEtiyHPPIMNYMISYSWTKNEDEKEKTFTKDSDKDLKAIISHVSPDILYLFRVQAV 310
Cdd:smart00060    3 PPSNLRVTDVTSTSVTLSWEPPP---DDGITGYIVGYRVEYREEGSEWKEVNVTPSSTSYTLTGLKPGTEYEFRVRAV 77
fn3 pfam00041
Fibronectin type III domain;
233-310 1.26e-07

Fibronectin type III domain;


Pssm-ID: 394996 [Multi-domain]  Cd Length: 85  Bit Score: 50.49  E-value: 1.26e-07
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2032733617  233 PPVNMKVQPVNRTALLVTWNQPETiYHPPIMNYMISYsWTKNEDEKEKTFTKDSDKDlKAIISHVSPDILYLFRVQAV 310
Cdd:pfam00041    2 APSNLTVTDVTSTSLTVSWTPPPD-GNGPITGYEVEY-RPKNSGEPWNEITVPGTTT-SVTLTGLKPGTEYEVRVQAV 76
 
Name Accession Description Interval E-value
R-PTPc-G-1 cd17667
catalytic domain of receptor-type tyrosine-protein phosphatase G, repeat 1; Receptor-type ...
 709-982 0e+00

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: 640.55  E-value: 0e+00
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032733617  709 FSEDFEEVQRCTADMNITAEHSNHPDNKHKNRYINILAYDHSRVKLRPLPGKDSKHSDYINANYVDGYNKAKAYIATQGP 788
Cdd:cd17667      1 FSEDFEEVQRCTADMNITAEHSNHPDNKHKNRYINILAYDHSRVKLRPLPGKDSKHSDYINANYVDGYNKAKAYIATQGP 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032733617  789 LKSTFEDFWRMIWEQNTGIIVMITNLVEKGRRKCDQYWPTENSEEYGNIIVTLKSTNVHACYTVRRFTVRNTKMKKGQKG 868
Cdd:cd17667     81 LKSTFEDFWRMIWEQNTGIIVMITNLVEKGRRKCDQYWPTENSEEYGNIIVTLKSTKIHACYTVRRFSIRNTKVKKGQKG 160

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032733617  869 NPKGRQNERTVIQYHYTQWPDMGVPEYALPVLTFVRRSSAARTPDMGPVVVHCSAGVGRTGTYIVIDSMLQQIKDKSTVN 948
Cdd:cd17667    161 NPKGRQNERTVIQYHYTQWPDMGVPEYALPVLTFVRRSSAARTPEMGPVLVHCSAGVGRTGTYIVIDSMLQQIKDKSTVN 240

                          250       260       270
                   ....*....|....*....|....*....|....
gi 2032733617  949 VLGFLKHIRTQRNYLVQTEEQYIFIHDALLEAIL 982
Cdd:cd17667    241 VLGFLKHIRTQRNYLVQTEEQYIFIHDALLEAIL 274
R-PTP-G-2 cd17670
PTP-like domain of receptor-type tyrosine-protein phosphatase G, repeat 2; Receptor-type ...
 1066-1270 8.92e-159

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: 473.78  E-value: 8.92e-159
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032733617 1066 YINASYIMGYYRSNEFIITQHPLPHTTKDFWRMIWDHNAQIIVMLPDNQSLAEDEFVYWPSREESMNCEAFTVTLISKDR 1145
Cdd:cd17670      1 YINASYIMGYYRSNEFIITQHPLPHTTKDFWRMIWDHNAQIIVMLPDNQGLAEDEFVYWPSREESMNCEAFTVTLISKDR 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032733617 1146 LCLSNEEQIIIHDFILEATQDDYVLEVRHFQCPKWPNPDAPISSTFELINVIKEEALTRDGPTIVHDEYGAVSAGTLCAL 1225
Cdd:cd17670     81 LCLSNEEQIIIHDFILEATQDDYVLEVRHFQCPKWPNPDAPISSTFELINVIKEEALTRDGPTIVHDEFGAVSAGTLCAL 160

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*
gi 2032733617 1226 TTLSQQLENENAVDVFQVAKMINLMRPGVFTDIEQYQFLYKAMLS 1270
Cdd:cd17670    161 TTLSQQLENENAVDVYQVAKMINLMRPGVFTDIEQYQFLYKAMLS 205
R5-PTPc-1 cd14549
catalytic domain of R5 subfamily receptor-type tyrosine-protein phosphatases, repeat 1; The R5 ...
 767-975 7.19e-151

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


Pssm-ID: 350397 [Multi-domain]  Cd Length: 204  Bit Score: 452.96  E-value: 7.19e-151
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032733617  767 YINANYVDGYNKAKAYIATQGPLKSTFEDFWRMIWEQNTGIIVMITNLVEKGRRKCDQYWPTENSEEYGNIIVTLKSTNV 846
Cdd:cd14549      1 YINANYVDGYNKARAYIATQGPLPSTFDDFWRMVWEQNSAIIVMITNLVERGRRKCDQYWPKEGTETYGNIQVTLLSTEV 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032733617  847 HACYTVRRFTVRNTKMKKgqkgnPKGRQNERTVIQYHYTQWPDMGVPEYALPVLTFVRRSSAARTPDMGPVVVHCSAGVG 926
Cdd:cd14549     81 LATYTVRTFSLKNLKLKK-----VKGRSSERVVYQYHYTQWPDHGVPDYTLPVLSFVRKSSAANPPGAGPIVVHCSAGVG 155

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*....
gi 2032733617  927 RTGTYIVIDSMLQQIKDKSTVNVLGFLKHIRTQRNYLVQTEEQYIFIHD 975
Cdd:cd14549    156 RTGTYIVIDSMLQQIQDKGTVNVFGFLKHIRTQRNYLVQTEEQYIFIHD 204
R-PTP-Z-2 cd17669
catalytic domain of receptor-type tyrosine-protein phosphatase Z, repeat 2; Receptor-type ...
 1066-1269 1.73e-139

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: 422.87  E-value: 1.73e-139
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032733617 1066 YINASYIMGYYRSNEFIITQHPLPHTTKDFWRMIWDHNAQIIVMLPDNQSLAEDEFVYWPSREESMNCEAFTVTLISKDR 1145
Cdd:cd17669      1 YINASYIMGYYQSNEFIITQHPLLHTIKDFWRMIWDHNAQLIVMLPDGQNMAEDEFVYWPNKDEPINCETFKVTLIAEEH 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032733617 1146 LCLSNEEQIIIHDFILEATQDDYVLEVRHFQCPKWPNPDAPISSTFELINVIKEEALTRDGPTIVHDEYGAVSAGTLCAL 1225
Cdd:cd17669     81 KCLSNEEKLIIQDFILEATQDDYVLEVRHFQCPKWPNPDSPISKTFELISIIKEEAANRDGPMIVHDEHGGVTAGTFCAL 160

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....
gi 2032733617 1226 TTLSQQLENENAVDVFQVAKMINLMRPGVFTDIEQYQFLYKAML 1269
Cdd:cd17669    161 TTLMHQLEKENSVDVYQVAKMINLMRPGVFTDIEQYQFLYKAIL 204
R-PTPc-Z-1 cd17668
catalytic domain of receptor-type tyrosine-protein phosphatase Z, repeat 1; Receptor-type ...
 767-978 3.35e-137

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: 417.07  E-value: 3.35e-137
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032733617  767 YINANYVDGYNKAKAYIATQGPLKSTFEDFWRMIWEQNTGIIVMITNLVEKGRRKCDQYWPTENSEEYGNIIVTLKSTNV 846
Cdd:cd17668      1 YINANYVDGYNKPKAYIAAQGPLKSTAEDFWRMIWEHNVEVIVMITNLVEKGRRKCDQYWPADGSEEYGNFLVTQKSVQV 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032733617  847 HACYTVRRFTVRNTKMKKGQKgnpKGRQNERTVIQYHYTQWPDMGVPEYALPVLTFVRRSSAARTPDMGPVVVHCSAGVG 926
Cdd:cd17668     81 LAYYTVRNFTLRNTKIKKGSQ---KGRPSGRVVTQYHYTQWPDMGVPEYTLPVLTFVRKASYAKRHAVGPVVVHCSAGVG 157

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|..
gi 2032733617  927 RTGTYIVIDSMLQQIKDKSTVNVLGFLKHIRTQRNYLVQTEEQYIFIHDALL 978
Cdd:cd17668    158 RTGTYIVLDSMLQQIQHEGTVNIFGFLKHIRSQRNYLVQTEEQYVFIHDALV 209
R5-PTP-2 cd14550
PTP-like domain of R5 subfamily receptor-type tyrosine-protein phosphatases, repeat 2; The R5 ...
 1066-1266 2.66e-127

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: 390.53  E-value: 2.66e-127
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032733617 1066 YINASYIMGYYRSNEFIITQHPLPHTTKDFWRMIWDHNAQIIVMLPDNQsLAEDEFVYWPSREESMNCEAFTVTLISKDR 1145
Cdd:cd14550      1 YINASYLQGYRRSNEFIITQHPLEHTIKDFWQMIWDHNSQTIVMLTDNE-LNEDEPIYWPTKEKPLECETFKVTLSGEDH 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032733617 1146 LCLSNEEQIIIHDFILEATQDDYVLEVRHFQCPKWPNPDAPISSTFELINVIKEEALTRDGPTIVHDEYGAVSAGTLCAL 1225
Cdd:cd14550     80 SCLSNEIRLIVRDFILESTQDDYVLEVRQFQCPSWPNPCSPIHTVFELINTVQEWAQQRDGPIVVHDRYGGVQAATFCAL 159

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|.
gi 2032733617 1226 TTLSQQLENENAVDVFQVAKMINLMRPGVFTDIEQYQFLYK 1266
Cdd:cd14550    160 TTLHQQLEHESSVDVYQVAKLYHLMRPGVFTSKEDYQFLYK 200
PTPc smart00194
Protein tyrosine phosphatase, catalytic domain;
708-979 4.87e-120

Protein tyrosine phosphatase, catalytic domain;


Pssm-ID: 214550 [Multi-domain]  Cd Length: 259  Bit Score: 373.53  E-value: 4.87e-120
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032733617   708 GFSEDFEEVQRCTADMnITAEHSNHPDNKHKNRYINILAYDHSRVKLRPLPGKDSkhsDYINANYVDGYNKAKAYIATQG 787
Cdd:smart00194    1 GLEEEFEKLDRLKPDD-ESCTVAAFPENRDKNRYKDVLPYDHTRVKLKPPPGEGS---DYINASYIDGPNGPKAYIATQG 76

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032733617   788 PLKSTFEDFWRMIWEQNTGIIVMITNLVEKGRRKCDQYWPTENSE--EYGNIIVTLKSTNVHACYTVRRFTVRNTkmkkg 865
Cdd:smart00194   77 PLPSTVEDFWRMVWEQKVTVIVMLTELVEKGREKCAQYWPDEEGEplTYGDITVTLKSVEKVDDYTIRTLEVTNT----- 151

                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032733617   866 qkgnpkGRQNERTVIQYHYTQWPDMGVPEYALPVLTFVRRSSAARTPDMGPVVVHCSAGVGRTGTYIVIDSMLQQIKDKS 945
Cdd:smart00194  152 ------GCSETRTVTHYHYTNWPDHGVPESPESILDLIRAVRKSQSTSTGPIVVHCSAGVGRTGTFIAIDILLQQLEAGK 225

                           250       260       270
                    ....*....|....*....|....*....|....
gi 2032733617   946 TVNVLGFLKHIRTQRNYLVQTEEQYIFIHDALLE 979
Cdd:smart00194  226 EVDIFEIVKELRSQRPGMVQTEEQYIFLYRAILE 259
R-PTPc-LAR-1 cd14553
catalytic domain of LAR family receptor-type tyrosine-protein phosphatases, repeat 1; The LAR ...
 735-981 8.55e-119

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: 369.03  E-value: 8.55e-119
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032733617  735 NKHKNRYINILAYDHSRVKLRPLPGKDSkhSDYINANYVDGYNKAKAYIATQGPLKSTFEDFWRMIWEQNTGIIVMITNL 814
Cdd:cd14553      3 NKPKNRYANVIAYDHSRVILQPIEGVPG--SDYINANYCDGYRKQNAYIATQGPLPETFGDFWRMVWEQRSATIVMMTKL 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032733617  815 VEKGRRKCDQYWPTENSEEYGNIIVTLKSTNVHACYTVRRFTVRNTkmkkgqkgnpkGRQNERTVIQYHYTQWPDMGVPE 894
Cdd:cd14553     81 EERSRVKCDQYWPTRGTETYGLIQVTLLDTVELATYTVRTFALHKN-----------GSSEKREVRQFQFTAWPDHGVPE 149

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032733617  895 YALPVLTFVRRSSAARTPDMGPVVVHCSAGVGRTGTYIVIDSMLQQIKDKSTVNVLGFLKHIRTQRNYLVQTEEQYIFIH 974
Cdd:cd14553    150 HPTPFLAFLRRVKACNPPDAGPIVVHCSAGVGRTGCFIVIDSMLERIKHEKTVDIYGHVTCLRAQRNYMVQTEDQYIFIH 229


                   ....*..
gi 2032733617  975 DALLEAI 981
Cdd:cd14553    230 DALLEAV 236
Y_phosphatase pfam00102
Protein-tyrosine phosphatase;
735-979 2.17e-113

Protein-tyrosine phosphatase;


Pssm-ID: 459674 [Multi-domain]  Cd Length: 234  Bit Score: 354.63  E-value: 2.17e-113
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032733617  735 NKHKNRYINILAYDHSRVKLRPLPGkdskHSDYINANYVDGYNKAKAYIATQGPLKSTFEDFWRMIWEQNTGIIVMITNL 814
Cdd:pfam00102    1 NLEKNRYKDVLPYDHTRVKLTGDPG----PSDYINASYIDGYKKPKKYIATQGPLPNTVEDFWRMVWEEKVTIIVMLTEL 76

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032733617  815 VEKGRRKCDQYWPTEN--SEEYGNIIVTLKSTNVH-ACYTVRRFTVRNtkmkkgqkgnpKGRQNERTVIQYHYTQWPDMG 891
Cdd:pfam00102   77 EEKGREKCAQYWPEEEgeSLEYGDFTVTLKKEKEDeKDYTVRTLEVSN-----------GGSEETRTVKHFHYTGWPDHG 145

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032733617  892 VPEYALPVLTFVRR-SSAARTPDMGPVVVHCSAGVGRTGTYIVIDSMLQQIKDKSTVNVLGFLKHIRTQRNYLVQTEEQY 970
Cdd:pfam00102  146 VPESPNSLLDLLRKvRKSSLDGRSGPIVVHCSAGIGRTGTFIAIDIALQQLEAEGEVDIFQIVKELRSQRPGMVQTLEQY 225


                   ....*....
gi 2032733617  971 IFIHDALLE 979
Cdd:pfam00102  226 IFLYDAILE 234
alpha_CARP_receptor_like cd03122
Carbonic anhydrase alpha related protein, receptor_like subfamily. Carbonic anhydrase related ...
 1-203 8.89e-103

Carbonic anhydrase alpha related protein, receptor_like subfamily. Carbonic anhydrase related proteins (CARPs) are sequence similar to carbonic anhydrases. Carbonic anhydrases are zinc-containing enzymes that catalyze the reversible hydration of carbon dioxide in a two-step mechanism. CARPs have lost conserved histidines involved in zinc binding and consequently their catalytic activity. This sub-family of carbonic anhydrase-related domains found in tyrosine phosphatase receptors may play a role in cell adhesion.


Pssm-ID: 239396 [Multi-domain]  Cd Length: 253  Bit Score: 326.62  E-value: 8.89e-103
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032733617    1 MKNTGKTVAILLKD---DYFVSGAGLPGRFKAEKVEFHWGQSNgSAGSEHSINGKRFPVEMQIFFYNPDDFDSFgTAVLE 77
Cdd:cd03122     51 LENTGKTVILRLEGnssDPFVSGGPLLGRYKFSEITFHWGTCN-SDGSEHSIDGHKFPLEMQILHRNTDFFDSF-EAIKS 128

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032733617   78 NRVVGAMAVFFQVSQRDNSALDPIIHGLKGVVHHEKETFLDPFVLRELLPTSLGSYYRYTGSLTTPPCSEIVEWIVFRKP 157
Cdd:cd03122    129 PGGVLALAYLFELSHEDNPFLDPIIEGLRNVSRPGKEVELPPFPLSDLLPPFTDKYYSYEGSLTTPPCSETVEWIVFREP 208

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*.
gi 2032733617  158 VPISYHQLEAFYSIFTTEQQDhVKSVEYLRNNFRPQQSLNNRKVSK 203
Cdd:cd03122    209 VPISSRQLEAFRELLTRRQDG-VMSGDYLPNNGRPQQPLGSRTVFS 253
R-PTPc-F-1 cd14626
catalytic domain of receptor-type tyrosine-protein phosphatase F, repeat 1; Receptor-type ...
 697-981 4.18e-102

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: 325.84  E-value: 4.18e-102
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032733617  697 HISELYSNNQHGFSEDFEEVQrctADMNITAEHSNHPDNKHKNRYINILAYDHSRVKLRPLPGKDSkhSDYINANYVDGY 776
Cdd:cd14626      6 NIERLKANDGLKFSQEYESID---PGQQFTWENSNLEVNKPKNRYANVIAYDHSRVILTSVDGVPG--SDYINANYIDGY 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032733617  777 NKAKAYIATQGPLKSTFEDFWRMIWEQNTGIIVMITNLVEKGRRKCDQYWPTENSEEYGNIIVTLKSTNVHACYTVRRFT 856
Cdd:cd14626     81 RKQNAYIATQGPLPETLSDFWRMVWEQRTATIVMMTRLEEKSRVKCDQYWPIRGTETYGMIQVTLLDTVELATYSVRTFA 160

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032733617  857 VRNTkmkkgqkgnpkGRQNERTVIQYHYTQWPDMGVPEYALPVLTFVRRSSAARTPDMGPVVVHCSAGVGRTGTYIVIDS 936
Cdd:cd14626    161 LYKN-----------GSSEKREVRQFQFMAWPDHGVPEYPTPILAFLRRVKACNPPDAGPMVVHCSAGVGRTGCFIVIDA 229

                          250       260       270       280
                   ....*....|....*....|....*....|....*....|....*
gi 2032733617  937 MLQQIKDKSTVNVLGFLKHIRTQRNYLVQTEEQYIFIHDALLEAI 981
Cdd:cd14626    230 MLERMKHEKTVDIYGHVTCMRSQRNYMVQTEDQYIFIHEALLEAA 274
R-PTPc-S-1 cd14625
catalytic domain of receptor-type tyrosine-protein phosphatase S, repeat 1; Receptor-type ...
 689-981 8.17e-98

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: 314.34  E-value: 8.17e-98
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032733617  689 IPVKQFVKHISELYSNNQHGFSEDFEEVQrctADMNITAEHSNHPDNKHKNRYINILAYDHSRVKLRPLPGKDSkhSDYI 768
Cdd:cd14625      4 IPISELAEHTERLKANDNLKLSQEYESID---PGQQFTWEHSNLEVNKPKNRYANVIAYDHSRVILQPIEGIMG--SDYI 78

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032733617  769 NANYVDGYNKAKAYIATQGPLKSTFEDFWRMIWEQNTGIIVMITNLVEKGRRKCDQYWPTENSEEYGNIIVTLKSTNVHA 848
Cdd:cd14625     79 NANYIDGYRKQNAYIATQGPLPETFGDFWRMVWEQRSATVVMMTKLEEKSRIKCDQYWPSRGTETYGMIQVTLLDTIELA 158

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032733617  849 CYTVRRFTVRNTkmkkgqkgnpkGRQNERTVIQYHYTQWPDMGVPEYALPVLTFVRRSSAARTPDMGPVVVHCSAGVGRT 928
Cdd:cd14625    159 TFCVRTFSLHKN-----------GSSEKREVRQFQFTAWPDHGVPEYPTPFLAFLRRVKTCNPPDAGPIVVHCSAGVGRT 227

                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|...
gi 2032733617  929 GTYIVIDSMLQQIKDKSTVNVLGFLKHIRTQRNYLVQTEEQYIFIHDALLEAI 981
Cdd:cd14625    228 GCFIVIDAMLERIKHEKTVDIYGHVTLMRSQRNYMVQTEDQYSFIHDALLEAV 280
PTPc cd00047
catalytic domain of protein tyrosine phosphatases; Protein tyrosine phosphatases (PTP, EC 3.1. ...
 767-975 7.49e-97

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: 308.06  E-value: 7.49e-97
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032733617  767 YINANYVDGYNKAKAYIATQGPLKSTFEDFWRMIWEQNTGIIVMITNLVEKGRRKCDQYWPTENSE--EYGNIIVTLKST 844
Cdd:cd00047      1 YINASYIDGYRGPKEYIATQGPLPNTVEDFWRMVWEQKVSVIVMLTNLVEKGREKCERYWPEEGGKplEYGDITVTLVSE 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032733617  845 NVHACYTVRRFTVRNtkmkkgqkgnpKGRQNERTVIQYHYTQWPDMGVPEYALPVLTFVRRSSAARTPDMGPVVVHCSAG 924
Cdd:cd00047     81 EELSDYTIRTLELSP-----------KGCSESREVTHLHYTGWPDHGVPSSPEDLLALVRRVRKEARKPNGPIVVHCSAG 149

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|.
gi 2032733617  925 VGRTGTYIVIDSMLQQIKDKSTVNVLGFLKHIRTQRNYLVQTEEQYIFIHD 975
Cdd:cd00047    150 VGRTGTFIAIDILLERLEAEGEVDVFEIVKALRKQRPGMVQTLEQYEFIYE 200
R-PTPc-D-1 cd14624
catalytic domain of receptor-type tyrosine-protein phosphatase D, repeat 1; Receptor-type ...
 689-981 1.13e-95

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: 308.58  E-value: 1.13e-95
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032733617  689 IPVKQFVKHISELYSNNQHGFSEDFEEVQrctADMNITAEHSNHPDNKHKNRYINILAYDHSRVKLRPLPGKDSkhSDYI 768
Cdd:cd14624      4 IPILELADHIERLKANDNLKFSQEYESID---PGQQFTWEHSNLEVNKPKNRYANVIAYDHSRVLLSAIEGIPG--SDYI 78

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032733617  769 NANYVDGYNKAKAYIATQGPLKSTFEDFWRMIWEQNTGIIVMITNLVEKGRRKCDQYWPTENSEEYGNIIVTLKSTNVHA 848
Cdd:cd14624     79 NANYIDGYRKQNAYIATQGALPETFGDFWRMIWEQRSATVVMMTKLEERSRVKCDQYWPSRGTETYGLIQVTLLDTVELA 158

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032733617  849 CYTVRRFTVRNTkmkkgqkgnpkGRQNERTVIQYHYTQWPDMGVPEYALPVLTFVRRSSAARTPDMGPVVVHCSAGVGRT 928
Cdd:cd14624    159 TYCVRTFALYKN-----------GSSEKREVRQFQFTAWPDHGVPEHPTPFLAFLRRVKTCNPPDAGPMVVHCSAGVGRT 227

                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|...
gi 2032733617  929 GTYIVIDSMLQQIKDKSTVNVLGFLKHIRTQRNYLVQTEEQYIFIHDALLEAI 981
Cdd:cd14624    228 GCFIVIDAMLERIKHEKTVDIYGHVTLMRAQRNYMVQTEDQYIFIHDALLEAV 280
R3-PTPc cd14548
catalytic domain of R3 subfamily receptor-type tyrosine-protein phosphatases and similar ...
 740-974 2.33e-94

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: 302.35  E-value: 2.33e-94
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032733617  740 RYINILAYDHSRVKLRPLPgkDSKHSDYINANYVDGYNKAKAYIATQGPLKSTFEDFWRMIWEQNTGIIVMITNLVEKGR 819
Cdd:cd14548      1 RYTNILPYDHSRVKLIPIN--EEEGSDYINANYIPGYNSPREFIATQGPLPGTKDDFWRMVWEQNSHTIVMLTQCMEKGR 78

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032733617  820 RKCDQYWPTENSE-EYGNIIVTLKSTNVHACYTVRRFTVrntkmkkgqkgnpKGRQNERTVIQYHYTQWPDMGVPEYALP 898
Cdd:cd14548     79 VKCDHYWPFDQDPvYYGDITVTMLSESVLPDWTIREFKL-------------ERGDEVRSVRQFHFTAWPDHGVPEAPDS 145

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2032733617  899 VLTFVRRSSAARTPDMGPVVVHCSAGVGRTGTYIVIDSMLQQIKDKSTVNVLGFLKHIRTQRNYLVQTEEQYIFIH 974
Cdd:cd14548    146 LLRFVRLVRDYIKQEKGPTIVHCSAGVGRTGTFIALDRLLQQIESEDYVDIFGIVYDLRKHRPLMVQTEAQYIFLH 221
PTPc-N9 cd14543
catalytic domain of tyrosine-protein phosphatase non-receptor type 9; Tyrosine-protein ...
 706-974 1.96e-91

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: 296.20  E-value: 1.96e-91
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032733617  706 QHGFSEDFEEVQRCTADMniTAEHSNHPDNKHKNRYINILAYDHSRVKLRPLPGKDSkhSDYINANYVDGYNKAKAYIAT 785
Cdd:cd14543      2 KRGIYEEYEDIRREPPAG--TFLCSLAPANQEKNRYGDVLCLDQSRVKLPKRNGDER--TDYINANFMDGYKQKNAYIAT 77

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032733617  786 QGPLKSTFEDFWRMIWEQNTGIIVMITNLVEKGRRKCDQYWPTE--NSEEYGNIIVTLKSTNVHACYTVRRFTVRNTKMK 863
Cdd:cd14543     78 QGPLPKTYSDFWRMVWEQKVLVIVMTTRVVERGRVKCGQYWPLEegSSLRYGDLTVTNLSVENKEHYKKTTLEIHNTETD 157

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032733617  864 KGqkgnpkgrqneRTVIQYHYTQWPDMGVPEYALPVLTF---VRRSSAARTPDMG----------PVVVHCSAGVGRTGT 930
Cdd:cd14543    158 ES-----------RQVTHFQFTSWPDFGVPSSAAALLDFlgeVRQQQALAVKAMGdrwkghppgpPIVVHCSAGIGRTGT 226

                          250       260       270       280
                   ....*....|....*....|....*....|....*....|....
gi 2032733617  931 YIVIDSMLQQIKDKSTVNVLGFLKHIRTQRNYLVQTEEQYIFIH 974
Cdd:cd14543    227 FCTLDICLSQLEDVGTLNVMQTVRRMRTQRAFSIQTPDQYYFCY 270
R-PTPc-T-1 cd14630
catalytic domain of receptor-type tyrosine-protein phosphatase T, repeat 1; Receptor-type ...
 734-982 1.15e-86

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: 281.53  E-value: 1.15e-86
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032733617  734 DNKHKNRYINILAYDHSRVKLRPLPGkdSKHSDYINANYVDGYNKAKAYIATQGPLKSTFEDFWRMIWEQNTGIIVMITN 813
Cdd:cd14630      2 ENRNKNRYGNIISYDHSRVRLQLLDG--DPHSDYINANYIDGYHRPRHYIATQGPMQETVKDFWRMIWQENSASVVMVTN 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032733617  814 LVEKGRRKCDQYWPtENSEEYGNIIVTLKSTNVHACYTVRRFTVRNtkmkkgqkgnpKGRQNERTVIQYHYTQWPDMGVP 893
Cdd:cd14630     80 LVEVGRVKCVRYWP-DDTEVYGDIKVTLIETEPLAEYVIRTFTVQK-----------KGYHEIREIRQFHFTSWPDHGVP 147

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032733617  894 EYALPVLTFVRRSSAARTPDMGPVVVHCSAGVGRTGTYIVIDSMLQQIKDKSTVNVLGFLKHIRTQRNYLVQTEEQYIFI 973
Cdd:cd14630    148 CYATGLLGFVRQVKFLNPPDAGPIVVHCSAGAGRTGCFIAIDIMLDMAENEGVVDIFNCVRELRAQRVNMVQTEEQYVFV 227


                   ....*....
gi 2032733617  974 HDALLEAIL 982
Cdd:cd14630    228 HDAILEACL 236
R-PTPc-A-1 cd14621
catalytic domain of receptor-type tyrosine-protein phosphatase A, repeat 1; Receptor-type ...
 689-988 1.65e-83

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: 274.98  E-value: 1.65e-83
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032733617  689 IPVKQFVKHISELYSNNQHGFSEDFEEVQRCTadMNITAEHSNHPDNKHKNRYINILAYDHSRVKLRPLPGkdSKHSDYI 768
Cdd:cd14621      8 LPVDKLEEEINRRMADDNKLFREEFNALPACP--IQATCEAASKEENKEKNRYVNILPYDHSRVHLTPVEG--VPDSDYI 83

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032733617  769 NANYVDGYNKAKAYIATQGPLKSTFEDFWRMIWEQNTGIIVMITNLVEKGRRKCDQYWPTENSEEYGNIIVTLKSTNVHA 848
Cdd:cd14621     84 NASFINGYQEKNKFIAAQGPKEETVNDFWRMIWEQNTATIVMVTNLKERKECKCAQYWPDQGCWTYGNIRVSVEDVTVLV 163

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032733617  849 CYTVRRFTVRntkmkkgQKGNPKGRQNERTVIQYHYTQWPDMGVPEYALPVLTFVRRSSAARTPDMGPVVVHCSAGVGRT 928
Cdd:cd14621    164 DYTVRKFCIQ-------QVGDVTNKKPQRLITQFHFTSWPDFGVPFTPIGMLKFLKKVKNCNPQYAGAIVVHCSAGVGRT 236

                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032733617  929 GTYIVIDSMLQQIKDKSTVNVLGFLKHIRTQRNYLVQTEEQYIFIHDALLEAILGKETEV 988
Cdd:cd14621    237 GTFIVIDAMLDMMHAERKVDVYGFVSRIRAQRCQMVQTDMQYVFIYQALLEHYLYGDTEL 296
R-PTPc-M-1 cd14633
catalytic domain of receptor-type tyrosine-protein phosphatase M, repeat 1; Receptor-type ...
 694-982 3.09e-81

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: 267.68  E-value: 3.09e-81
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032733617  694 FVKHISELYSNNQHGFSEDFE---EVQRCTADmnitaeHSNHPDNKHKNRYINILAYDHSRVKLRPLPGKdsKHSDYINA 770
Cdd:cd14633      2 LLQHITQMKCAEGYGFKEEYEsffEGQSAPWD------SAKKDENRMKNRYGNIIAYDHSRVRLQPIEGE--TSSDYING 73

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032733617  771 NYVDGYNKAKAYIATQGPLKSTFEDFWRMIWEQNTGIIVMITNLVEKGRRKCDQYWPtENSEEYGNIIVTLKSTNVHACY 850
Cdd:cd14633     74 NYIDGYHRPNHYIATQGPMQETIYDFWRMVWHENTASIIMVTNLVEVGRVKCCKYWP-DDTEIYKDIKVTLIETELLAEY 152

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032733617  851 TVRRFTVRNtkmkkgqkgnpKGRQNERTVIQYHYTQWPDMGVPEYALPVLTFVRRSSAARTPDMGPVVVHCSAGVGRTGT 930
Cdd:cd14633    153 VIRTFAVEK-----------RGVHEIREIRQFHFTGWPDHGVPYHATGLLGFVRQVKSKSPPNAGPLVVHCSAGAGRTGC 221

                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|..
gi 2032733617  931 YIVIDSMLQQIKDKSTVNVLGFLKHIRTQRNYLVQTEEQYIFIHDALLEAIL 982
Cdd:cd14633    222 FIVIDIMLDMAEREGVVDIYNCVRELRSRRVNMVQTEEQYVFIHDAILEACL 273
PTPc smart00194
Protein tyrosine phosphatase, catalytic domain;
1011-1269 2.11e-80

Protein tyrosine phosphatase, catalytic domain;


Pssm-ID: 214550 [Multi-domain]  Cd Length: 259  Bit Score: 264.91  E-value: 2.11e-80
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032733617  1011 LEKQFKLVTQCNAKYVECFSAQKDCNKEKNRNSSVVPSERARVGLAPLPGmKGTDYINASYIMGYYRSNEFIITQHPLPH 1090
Cdd:smart00194    2 LEEEFEKLDRLKPDDESCTVAAFPENRDKNRYKDVLPYDHTRVKLKPPPG-EGSDYINASYIDGPNGPKAYIATQGPLPS 80

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032733617  1091 TTKDFWRMIWDHNAQIIVMLPDNQSL-AEDEFVYWPSRE-ESMNCEAFTVTLISKDRLclsneEQIIIHDFILEATQDDY 1168
Cdd:smart00194   81 TVEDFWRMVWEQKVTVIVMLTELVEKgREKCAQYWPDEEgEPLTYGDITVTLKSVEKV-----DDYTIRTLEVTNTGCSE 155

                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032733617  1169 VLEVRHFQCPKWPNPDAP--ISSTFELINVIKEEALTRDGPTIVHDEYGAVSAGTLCALTTLSQQLENENAVDVFQVAKM 1246
Cdd:smart00194  156 TRTVTHYHYTNWPDHGVPesPESILDLIRAVRKSQSTSTGPIVVHCSAGVGRTGTFIAIDILLQQLEAGKEVDIFEIVKE 235

                           250       260
                    ....*....|....*....|...
gi 2032733617  1247 INLMRPGVFTDIEQYQFLYKAML 1269
Cdd:smart00194  236 LRSQRPGMVQTEEQYIFLYRAIL 258
R-PTPc-B cd14617
catalytic domain of receptor-type tyrosine-protein phosphatase B; Receptor-type ...
 739-974 1.60e-79

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: 261.01  E-value: 1.60e-79
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032733617  739 NRYINILAYDHSRVKLRPLpgKDSKHSDYINANYVDGYNKAKAYIATQGPLKSTFEDFWRMIWEQNTGIIVMITNLVEKG 818
Cdd:cd14617      1 NRYNNILPYDSTRVKLSNV--DDDPCSDYINASYIPGNNFRREYIATQGPLPGTKDDFWKMVWEQNVHNIVMVTQCVEKG 78

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032733617  819 RRKCDQYWPTE-NSEEYGNIIVTLKSTNVHACYTVRRFTVRNtkmkKGQKGNPkgrqneRTVIQYHYTQWPDMGVPEYAL 897
Cdd:cd14617     79 RVKCDHYWPADqDSLYYGDLIVQMLSESVLPEWTIREFKICS----EEQLDAP------RLVRHFHYTVWPDHGVPETTQ 148

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2032733617  898 PVLTFVR--RSSAARTPDMGPVVVHCSAGVGRTGTYIVIDSMLQQIKDKSTVNVLGFLKHIRTQRNYLVQTEEQYIFIH 974
Cdd:cd14617    149 SLIQFVRtvRDYINRTPGSGPTVVHCSAGVGRTGTFIALDRILQQLDSKDSVDIYGAVHDLRLHRVHMVQTECQYVYLH 227
Y_phosphatase pfam00102
Protein-tyrosine phosphatase;
1036-1269 1.73e-79

Protein-tyrosine phosphatase;


Pssm-ID: 459674 [Multi-domain]  Cd Length: 234  Bit Score: 261.41  E-value: 1.73e-79
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032733617 1036 NKEKNRNSSVVPSERARVGLAPLPGmkGTDYINASYIMGYYRSNEFIITQHPLPHTTKDFWRMIWDHNAQIIVMLPDNQS 1115
Cdd:pfam00102    1 NLEKNRYKDVLPYDHTRVKLTGDPG--PSDYINASYIDGYKKPKKYIATQGPLPNTVEDFWRMVWEEKVTIIVMLTELEE 78

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032733617 1116 LA-EDEFVYWP-SREESMNCEAFTVTLISKDrlclSNEEQIIIHDFILEATQDDYVLEVRHFQCPKWPNPDAP--ISSTF 1191
Cdd:pfam00102   79 KGrEKCAQYWPeEEGESLEYGDFTVTLKKEK----EDEKDYTVRTLEVSNGGSEETRTVKHFHYTGWPDHGVPesPNSLL 154

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2032733617 1192 ELINVIKEEALT-RDGPTIVHDEYGAVSAGTLCALTTLSQQLENENAVDVFQVAKMINLMRPGVFTDIEQYQFLYKAML 1269
Cdd:pfam00102  155 DLLRKVRKSSLDgRSGPIVVHCSAGIGRTGTFIAIDIALQQLEAEGEVDIFQIVKELRSQRPGMVQTLEQYIFLYDAIL 233
R-PTPc-J cd14615
catalytic domain of receptor-type tyrosine-protein phosphatase J; Receptor-type ...
 739-979 2.45e-79

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: 260.52  E-value: 2.45e-79
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032733617  739 NRYINILAYDHSRVKLRPLpgkDSKHSDYINANYVDGYNKAKAYIATQGPLKSTFEDFWRMIWEQNTGIIVMITNLVEKG 818
Cdd:cd14615      1 NRYNNVLPYDISRVKLSVQ---SHSTDDYINANYMPGYNSKKEFIAAQGPLPNTVKDFWRMVWEKNVYAIVMLTKCVEQG 77

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032733617  819 RRKCDQYWPTENSEEYGNIIVTLKSTNVHACYTVRRFTVRNtkMKKGQKgnpkgrqneRTVIQYHYTQWPDMGVPEYALP 898
Cdd:cd14615     78 RTKCEEYWPSKQKKDYGDITVTMTSEIVLPEWTIRDFTVKN--AQTNES---------RTVRHFHFTSWPDHGVPETTDL 146

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032733617  899 VLTF--VRRSSAARTPDMGPVVVHCSAGVGRTGTYIVIDSMLQQIKDKSTVNVLGFLKHIRTQRNYLVQTEEQYIFIHDA 976
Cdd:cd14615    147 LINFrhLVREYMKQNPPNSPILVHCSAGVGRTGTFIAIDRLIYQIENENVVDVYGIVYDLRMHRPLMVQTEDQYVFLNQC 226


                   ...
gi 2032733617  977 LLE 979
Cdd:cd14615    227 ALD 229
Carb_anhydrase smart01057
Eukaryotic-type carbonic anhydrase; Carbonic anhydrases are zinc metalloenzymes which catalyse ...
 1-200 3.45e-79

Eukaryotic-type carbonic anhydrase; Carbonic anhydrases are zinc metalloenzymes which catalyse the reversible hydration of carbon dioxide to bicarbonate.. CAs have essential roles in facilitating the transport of carbon dioxide and protons in the intracellular space, across biological membranes and in the layers of the extracellular space; they are also involved in many other processes, from respiration and photosynthesis in eukaryotes to cyanate degradation in prokaryotes. There are five known evolutionarily distinct CA families (alpha, beta, gamma, delta and epsilon) that have no significant sequence identity and have structurally distinct overall folds. Some CAs are membrane-bound, while others act in the cytosol; there are several related proteins that lack enzymatic activity. The active site of alpha-CAs is well described, consisting of a zinc ion coordinated through 3 histidine residues and a water molecule/hydroxide ion that acts as a potent nucleophile. The enzyme employs a two-step mechanism: in the first step, there is a nucleophilic attack of a zinc-bound hydroxide ion on carbon dioxide; in the second step, the active site is regenerated by the ionisation of the zinc-bound water molecule and the removal of a proton from the active site. Beta- and gamma-CAs also employ a zinc hydroxide mechanism, although at least some beta-class enzymes do not have water directly coordinated to the metal ion.


Pssm-ID: 215000 [Multi-domain]  Cd Length: 247  Bit Score: 261.09  E-value: 3.45e-79
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032733617     1 MKNTGKTVAILLKDD-YFVSGAGLPGRFKAEKVEFHWGqSNGSAGSEHSINGKRFPVEMQIFFYNPDDfdSFGTAVLENR 79
Cdd:smart01057   56 ILNNGHTVQVNFDDDgSTLSGGPLPGRYRLKQFHFHWG-GSDSEGSEHTIDGKRFPLELHLVHYNSKG--SFSEAVSKPG 132

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032733617    80 VVGAMAVFFQVSQRDNSALDPIIHGLKGVVHHEKETFLDPFVLRELLPTSLGSYYRYTGSLTTPPCSEIVEWIVFRKPVP 159
Cdd:smart01057  133 GLAVVAVFFKVGAEENPALQAILDHLPLIKYKGQETELTPFDLSSLLPASTRHYYTYNGSLTTPPCSEGVTWIVFKEPIT 212

                           170       180       190       200
                    ....*....|....*....|....*....|....*....|.
gi 2032733617   160 ISYHQLEAFYSIFTTEQQdhvksvEYLRNNFRPQQSLNNRK 200
Cdd:smart01057  213 ISTEQLEKFRTLLPMEGN------EPLVNNARPLQPLNGRV 247
R-PTPc-typeIIb-1 cd14555
catalytic domain of type IIb (or R2B) subfamily receptor-type tyrosine-protein phosphatases, ...
 767-982 8.34e-78

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: 255.23  E-value: 8.34e-78
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032733617  767 YINANYVDGYNKAKAYIATQGPLKSTFEDFWRMIWEQNTGIIVMITNLVEKGRRKCDQYWPtENSEEYGNIIVTLKSTNV 846
Cdd:cd14555      1 YINANYIDGYHRPNHYIATQGPMQETVYDFWRMVWQENSASIVMVTNLVEVGRVKCSRYWP-DDTEVYGDIKVTLVETEP 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032733617  847 HACYTVRRFTVRNtkmkkgqkgnpKGRQNERTVIQYHYTQWPDMGVPEYALPVLTFVRRSSAARTPDMGPVVVHCSAGVG 926
Cdd:cd14555     80 LAEYVVRTFALER-----------RGYHEIREVRQFHFTGWPDHGVPYHATGLLGFIRRVKASNPPSAGPIVVHCSAGAG 148

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 2032733617  927 RTGTYIVIDSMLQQIKDKSTVNVLGFLKHIRTQRNYLVQTEEQYIFIHDALLEAIL 982
Cdd:cd14555    149 RTGCYIVIDIMLDMAEREGVVDIYNCVKELRSRRVNMVQTEEQYIFIHDAILEACL 204
Carb_anhydrase pfam00194
Eukaryotic-type carbonic anhydrase;
1-204 1.93e-76

Eukaryotic-type carbonic anhydrase;


Pssm-ID: 459707 [Multi-domain]  Cd Length: 252  Bit Score: 253.34  E-value: 1.93e-76
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032733617    1 MKNTGKTVAILLKDDY--FVSGAGLPGRFKAEKVEFHWGqSNGSAGSEHSINGKRFPVEMQIFFYNpDDFDSFGTAVLEN 78
Cdd:pfam00194   51 LTNNGHTVQVSLDDGDpsTISGGPLATRYRLVQFHFHWG-STDSRGSEHTIDGKRYPAELHIVHYN-SKYKSFDEAAKHP 128

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032733617   79 RVVGAMAVFFQVSQRDNSALDPIIHGLKGVVHHEKETFLDPFVLRELLPTSLGSYYRYTGSLTTPPCSEIVEWIVFRKPV 158
Cdd:pfam00194  129 DGLAVLGVFFEVGDENNPYLQPIVSALDNIKYKGKSVLLPPFDLSDLLPEDLTSYYTYNGSLTTPPCSESVTWIVFKEPI 208

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*.
gi 2032733617  159 PISYHQLEAFYSIFTTEQQDHvksVEYLRNNFRPQQSLNNRKVSKS 204
Cdd:pfam00194  209 SISEEQLEAFRTLLFSDGGEE---PRPLVNNFRPTQPLNGRVVFAS 251
PTPc-KIM cd14547
catalytic domain of the kinase interaction motif (KIM) family of protein-tyrosine phosphatases; ...
 739-974 2.47e-76

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: 251.93  E-value: 2.47e-76
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032733617  739 NRYINILAYDHSRVKLRPLPgkDSKHSDYINANYVDGYN-KAKAYIATQGPLKSTFEDFWRMIWEQNTGIIVMITNLVEK 817
Cdd:cd14547      1 NRYKTILPNEHSRVCLPSVD--DDPLSSYINANYIRGYDgEEKAYIATQGPLPNTVADFWRMVWQEKTPIIVMITNLTEA 78

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032733617  818 gRRKCDQYWPTENSEEYGNIIVTLKSTNVHACYTVRRFTVRNtkmkkgqkgnpkgRQNERTVIQYHYTQWPDMGVPEYAL 897
Cdd:cd14547     79 -KEKCAQYWPEEENETYGDFEVTVQSVKETDGYTVRKLTLKY-------------GGEKRYLKHYWYTSWPDHKTPEAAQ 144

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2032733617  898 PVLTFVRR--SSAARTPDMGPVVVHCSAGVGRTGTYIVIDSMLQQIKDKSTVNVLGFLKHIRTQRNYLVQTEEQYIFIH 974
Cdd:cd14547    145 PLLSLVQEveEARQTEPHRGPIVVHCSAGIGRTGCFIATSIGCQQLREEGVVDVLGIVCQLRLDRGGMVQTAEQYEFVH 223
R-PTPc-H cd14619
catalytic domain of receptor-type tyrosine-protein phosphatase H; Receptor-type ...
 739-981 7.22e-76

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: 250.96  E-value: 7.22e-76
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032733617  739 NRYINILAYDHSRVKLRPLpgKDSKHSDYINANYVDGYNKAKAYIATQGPLKSTFEDFWRMIWEQNTGIIVMITNLVEKG 818
Cdd:cd14619      1 NRFRNVLPYDWSRVPLKPI--HEEPGSDYINANYMPGYWSSQEFIATQGPLPQTVGDFWRMIWEQQSSTIVMLTNCMEAG 78

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032733617  819 RRKCDQYWPTENSE-EYGNIIVTLKSTNVHACYTVRRFTVRNTKmkkgqkgnpkgRQNERTVIQYHYTQWPDMGVPEYAL 897
Cdd:cd14619     79 RVKCEHYWPLDYTPcTYGHLRVTVVSEEVMENWTVREFLLKQVE-----------EQKTLSVRHFHFTAWPDHGVPSSTD 147

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032733617  898 PVLTFVR--RSSAARTPDMGPVVVHCSAGVGRTGTYIVIDSMLQQIKDKSTVNVLGFLKHIRTQRNYLVQTEEQYIFIHD 975
Cdd:cd14619    148 TLLAFRRllRQWLDQTMSGGPTVVHCSAGVGRTGTLIALDVLLQQLQSEGLLGPFSFVQKMRENRPLMVQTESQYVFLHQ 227


                   ....*.
gi 2032733617  976 ALLEAI 981
Cdd:cd14619    228 CILDFL 233
R-PTPc-E-1 cd14620
catalytic domain of receptor-type tyrosine-protein phosphatase E, repeat 1; Receptor-type ...
 741-979 3.74e-75

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: 248.70  E-value: 3.74e-75
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032733617  741 YINILAYDHSRVKLRPLPGKDSkhSDYINANYVDGYNKAKAYIATQGPLKSTFEDFWRMIWEQNTGIIVMITNLVEKGRR 820
Cdd:cd14620      1 YPNILPYDHSRVILSQLDGIPC--SDYINASYIDGYKEKNKFIAAQGPKQETVNDFWRMVWEQKSATIVMLTNLKERKEE 78

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032733617  821 KCDQYWPTENSEEYGNIIVTLKSTNVHACYTVRRFTVrntkmkkgQKGNPKGRQNERTVIQYHYTQWPDMGVPEYALPVL 900
Cdd:cd14620     79 KCYQYWPDQGCWTYGNIRVAVEDCVVLVDYTIRKFCI--------QPQLPDGCKAPRLVTQLHFTSWPDFGVPFTPIGML 150

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2032733617  901 TFVRRSSAARTPDMGPVVVHCSAGVGRTGTYIVIDSMLQQIKDKSTVNVLGFLKHIRTQRNYLVQTEEQYIFIHDALLE 979
Cdd:cd14620    151 KFLKKVKSVNPVHAGPIVVHCSAGVGRTGTFIVIDAMIDMMHAEQKVDVFEFVSRIRNQRPQMVQTDMQYSFIYQALLE 229
alpha_CA cd00326
Carbonic anhydrase alpha (vertebrate-like) group. Carbonic anhydrases (CAs) are ...
 1-201 2.72e-74

Carbonic anhydrase alpha (vertebrate-like) group. Carbonic anhydrases (CAs) are zinc-containing enzymes that catalyze the reversible hydration of carbon dioxide in a two-step mechanism: a nucleophilic attack of a zinc-bound hydroxide ion on carbon dioxide, followed by the regeneration of the active site by ionization of the zinc-bound water molecule and removal of a proton from the active site. They are ubiquitous enzymes involved in fundamental processes like photosynthesis, respiration, pH homeostasis and ion transport. There are three evolutionary distinct groups - alpha, beta and gamma carbonic anhydrases - which show no significant sequence identity or structural similarity. Most alpha CAs are monomeric enzymes. The zinc ion is complexed by three histidine residues and a fourth conserved histidine plays a potential role in proton transfer.


Pssm-ID: 238200  Cd Length: 227  Bit Score: 246.43  E-value: 2.72e-74
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032733617    1 MKNTGKTVAILLKDD-YFVSGAGLPGRFKAEKVEFHWGqSNGSAGSEHSINGKRFPVEMQIFFYNPDDFDSfgTAVLENR 79
Cdd:cd00326     35 LVNNGHTVQVNFDDDgGTLSGGGLPGRYKLVQFHFHWG-SENSPGSEHTIDGKRYPLELHLVHYNSDYYSS--EAAKKPG 111

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032733617   80 VVGAMAVFFQVSQRDNSALDPIIHGLKGVVHHEKETFLDPFVLRELLPTSLGSYYRYTGSLTTPPCSEIVEWIVFRKPVP 159
Cdd:cd00326    112 GLAVLGVFFEVGEKENPFLKKILDALPKIKYKGKETTLPPFDLSDLLPSSLRDYYTYEGSLTTPPCSEGVTWIVFKEPIT 191

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|..
gi 2032733617  160 ISYHQLEAFYSIFTTEqqdhvksVEYLRNNFRPQQSLNNRKV 201
Cdd:cd00326    192 ISKEQLEAFRSLLDRE-------GKPLVNNYRPVQPLNGRVV 226
R-PTP-LAR-2 cd14554
PTP-like domain of the LAR family receptor-type tyrosine-protein phosphatases, repeat 2; The ...
 730-978 2.81e-74

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: 246.67  E-value: 2.81e-74
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032733617  730 SNHPDNKHKNRYINILAYDHSRVKLRPLPGKDSkhSDYINANYVDGYNKAKAYIATQGPLKSTFEDFWRMIWEQNTGIIV 809
Cdd:cd14554      1 ANLPCNKFKNRLVNILPYESTRVCLQPIRGVEG--SDYINASFIDGYRQRGAYIATQGPLAETTEDFWRMLWEHNSTIIV 78

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032733617  810 MITNLVEKGRRKCDQYWPTENSEEYGNIIVTLKSTNVHACYTVRRFTVrnTKMKKGQkgnpkgrqnERTVIQYHYTQWPD 889
Cdd:cd14554     79 MLTKLREMGREKCHQYWPAERSARYQYFVVDPMAEYNMPQYILREFKV--TDARDGQ---------SRTVRQFQFTDWPE 147

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032733617  890 MGVPEYALPVLTFVRR--SSAARTPDMGPVVVHCSAGVGRTGTYIVIDSMLQQIKDKSTVNVLGFLKHIRTQRNYLVQTE 967
Cdd:cd14554    148 QGVPKSGEGFIDFIGQvhKTKEQFGQEGPITVHCSAGVGRTGVFITLSIVLERMRYEGVVDVFQTVKLLRTQRPAMVQTE 227

                          250
                   ....*....|.
gi 2032733617  968 EQYIFIHDALL 978
Cdd:cd14554    228 DQYQFCYRAAL 238
PTPc-N11_6 cd14544
catalytic domain of tyrosine-protein phosphatase non-receptor type 11 and type 6; ...
 735-977 4.15e-74

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: 246.61  E-value: 4.15e-74
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032733617  735 NKHKNRYINILAYDHSRVKLRPLPgKDSKHSDYINANYVDGYN-------KAKAYIATQGPLKSTFEDFWRMIWEQNTGI 807
Cdd:cd14544      1 NKGKNRYKNILPFDHTRVILKDRD-PNVPGSDYINANYIRNENegpttdeNAKTYIATQGCLENTVSDFWSMVWQENSRV 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032733617  808 IVMITNLVEKGRRKCDQYWPTE-NSEEYGNIIVTLKSTNVHACYTVRRFtvrntKMKKGQKGNPkgrqnERTVIQYHYTQ 886
Cdd:cd14544     80 IVMTTKEVERGKNKCVRYWPDEgMQKQYGPYRVQNVSEHDTTDYTLREL-----QVSKLDQGDP-----IREIWHYQYLS 149

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032733617  887 WPDMGVPEYALPVLTFV----RRSSAarTPDMGPVVVHCSAGVGRTGTYIVIDSMLQQIKDKS---TVNVLGFLKHIRTQ 959
Cdd:cd14544    150 WPDHGVPSDPGGVLNFLedvnQRQES--LPHAGPIVVHCSAGIGRTGTFIVIDMLLDQIKRKGldcDIDIQKTIQMVRSQ 227

                          250
                   ....*....|....*...
gi 2032733617  960 RNYLVQTEEQYIFIHDAL 977
Cdd:cd14544    228 RSGMVQTEAQYKFIYVAV 245
R-PTPc-V cd14618
catalytic domain of receptor-type tyrosine-protein phosphatase V; Receptor-type ...
 739-978 5.31e-73

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: 242.93  E-value: 5.31e-73
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032733617  739 NRYINILAYDHSRVKLRPLPGKdsKHSDYINANYVDGYNKAKAYIATQGPLKSTFEDFWRMIWEQNTGIIVMITNLVEKG 818
Cdd:cd14618      1 NRYPHVLPYDHSRVRLSQLGGE--PHSDYINANFIPGYTSPQEFIATQGPLKKTIEDFWRLVWEQQVCNIIMLTVGMENG 78

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032733617  819 RRKCDQYWPTENSE-EYGNIIVTLKSTNVHACYTVRRFTVRNtkmkkgqkgnpKGRQNERTVIQYHYTQWPDMGVPEYAL 897
Cdd:cd14618     79 RVLCDHYWPSESTPvSYGHITVHLLAQSSEDEWTRREFKLWH-----------EDLRKERRVKHLHYTAWPDHGIPESTS 147

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032733617  898 PVLTFVR--RSSAARTPDMGPVVVHCSAGVGRTGTYIVIDSMLQQIKDKSTVNVLGFLKHIRTQRNYLVQTEEQYIFIHD 975
Cdd:cd14618    148 SLMAFRElvREHVQATKGKGPTLVHCSAGVGRSGTFIALDRLLRQLKEEKVVDVFNTVYILRMHRYLMIQTLSQYIFLHS 227


                   ...
gi 2032733617  976 ALL 978
Cdd:cd14618    228 CIL 230
R-PTPc-O cd14614
catalytic domain of receptor-type tyrosine-protein phosphatase O; Receptor-type ...
 724-974 6.74e-73

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: 243.26  E-value: 6.74e-73
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032733617  724 NITAEHSNHPDNKHKNRYINILAYDHSRVKLRPLpgKDSKHSDYINANYVDGYNKAKAYIATQGPLKSTFEDFWRMIWEQ 803
Cdd:cd14614      1 DIPHFAADLPVNRCKNRYTNILPYDFSRVKLVSM--HEEEGSDYINANYIPGYNSPQEYIATQGPLPETRNDFWKMVLQQ 78

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032733617  804 NTGIIVMITNLVEKGRRKCDQYWP-TENSEEYGNIIVTLKSTNVHACYTVRRFTVRNTkmkkgqkgnpkgrQNERTVIQY 882
Cdd:cd14614     79 KSQIIVMLTQCNEKRRVKCDHYWPfTEEPVAYGDITVEMLSEEEQPDWAIREFRVSYA-------------DEVQDVMHF 145

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032733617  883 HYTQWPDMGVP--EYALPVLTFVR--RSSAARTPdmGPVVVHCSAGVGRTGTYIVIDSMLQQIKDKSTVNVLGFLKHIRT 958
Cdd:cd14614    146 NYTAWPDHGVPtaNAAESILQFVQmvRQQAVKSK--GPMIIHCSAGVGRTGTFIALDRLLQHIRDHEFVDILGLVSEMRS 223

                          250
                   ....*....|....*.
gi 2032733617  959 QRNYLVQTEEQYIFIH 974
Cdd:cd14614    224 YRMSMVQTEEQYIFIH 239
R-PTPc-U-1 cd14632
catalytic domain of receptor-type tyrosine-protein phosphatase U, repeat 1; Receptor-type ...
 767-982 1.43e-72

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: 240.72  E-value: 1.43e-72
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032733617  767 YINANYVDGYNKAKAYIATQGPLKSTFEDFWRMIWEQNTGIIVMITNLVEKGRRKCDQYWPtENSEEYGNIIVTLKSTNV 846
Cdd:cd14632      1 YINANYIDGYHRSNHFIATQGPKQEMVYDFWRMVWQEHCSSIVMITKLVEVGRVKCSKYWP-DDSDTYGDIKITLLKTET 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032733617  847 HACYTVRRFTVRNtkmkkgqkgnpKGRQNERTVIQYHYTQWPDMGVPEYALPVLTFVRRSSAARTPDMGPVVVHCSAGVG 926
Cdd:cd14632     80 LAEYSVRTFALER-----------RGYSARHEVKQFHFTSWPEHGVPYHATGLLAFIRRVKASTPPDAGPVVVHCSAGAG 148

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 2032733617  927 RTGTYIVIDSMLQQIKDKSTVNVLGFLKHIRTQRNYLVQTEEQYIFIHDALLEAIL 982
Cdd:cd14632    149 RTGCYIVLDVMLDMAECEGVVDIYNCVKTLCSRRINMIQTEEQYIFIHDAILEACL 204
R-PTPc-K-1 cd14631
catalytic domain of receptor-type tyrosine-protein phosphatase K, repeat 1; Receptor-type ...
 751-982 1.78e-72

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: 240.69  E-value: 1.78e-72
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032733617  751 RVKLRPLpgKDSKHSDYINANYVDGYNKAKAYIATQGPLKSTFEDFWRMIWEQNTGIIVMITNLVEKGRRKCDQYWPtEN 830
Cdd:cd14631      1 RVILQPV--EDDPSSDYINANYIDGYQRPSHYIATQGPVHETVYDFWRMIWQEQSACIVMVTNLVEVGRVKCYKYWP-DD 77

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032733617  831 SEEYGNIIVTLKSTNVHACYTVRRFTVRNtkmkkgqkgnpKGRQNERTVIQYHYTQWPDMGVPEYALPVLTFVRRSSAAR 910
Cdd:cd14631     78 TEVYGDFKVTCVEMEPLAEYVVRTFTLER-----------RGYNEIREVKQFHFTGWPDHGVPYHATGLLSFIRRVKLSN 146

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2032733617  911 TPDMGPVVVHCSAGVGRTGTYIVIDSMLQQIKDKSTVNVLGFLKHIRTQRNYLVQTEEQYIFIHDALLEAIL 982
Cdd:cd14631    147 PPSAGPIVVHCSAGAGRTGCYIVIDIMLDMAEREGVVDIYNCVKALRSRRINMVQTEEQYIFIHDAILEACL 218
PTP_fungal cd18533
fungal protein tyrosine phosphatases; This subfamily contains Saccharomyces cerevisiae ...
 767-975 2.75e-72

fungal protein tyrosine phosphatases; This subfamily contains Saccharomyces cerevisiae protein-tyrosine phosphatases 1 (PTP1) and 2 (PTP2), Schizosaccharomyces pombe PTP1, PTP2, and PTP3, and similar fungal proteins. PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides; they regulate phosphotyrosine levels in signal transduction pathways. PTP2, together with PTP3, is the major phosphatase that dephosphorylates and inactivates the MAP kinase HOG1 and also modulates its subcellular localization.


Pssm-ID: 350509 [Multi-domain]  Cd Length: 212  Bit Score: 239.84  E-value: 2.75e-72
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032733617  767 YINANYVD-GYNKAKAYIATQGPLKSTFEDFWRMIWEQNTGIIVMITNLVEKGRRKCDQYWPTENSE-EYGNIIVTL--K 842
Cdd:cd18533      1 YINASYITlPGTSSKRYIATQGPLPATIGDFWKMIWQNNVGVIVMLTPLVENGREKCDQYWPSGEYEgEYGDLTVELvsE 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032733617  843 STNVHACYTVRRFTVRNTKMKKgqkgnpkgrqneRTVIQYHYTQWPDMGVPEYALPVLTFVRRSSA--ARTPDMGPVVVH 920
Cdd:cd18533     81 EENDDGGFIVREFELSKEDGKV------------KKVYHIQYKSWPDFGVPDSPEDLLTLIKLKRElnDSASLDPPIIVH 148

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2032733617  921 CSAGVGRTGTYIVIDSMLQQIKDKSTVN---------VLGFLKHIRTQRNYLVQTEEQYIFIHD 975
Cdd:cd18533    149 CSAGVGRTGTFIALDSLLDELKRGLSDSqdledsedpVYEIVNQLRKQRMSMVQTLRQYIFLYD 212
R-PTPc-A-E-1 cd14551
catalytic domain of receptor-type tyrosine-protein phosphatase A and E, repeat 1; ...
 767-974 4.33e-71

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: 236.35  E-value: 4.33e-71
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032733617  767 YINANYVDGYNKAKAYIATQGPLKSTFEDFWRMIWEQNTGIIVMITNLVEKGRRKCDQYWPTENSEEYGNIIVTLKSTNV 846
Cdd:cd14551      1 YINASYIDGYQEKNKFIAAQGPKDETVNDFWRMIWEQGSATIVMVTNLKERKEKKCSQYWPDQGCWTYGNLRVRVEDTVV 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032733617  847 HACYTVRRFTVRntkmkkgQKGNPKGRQNERTVIQYHYTQWPDMGVPEYALPVLTFVRRSSAARTPDMGPVVVHCSAGVG 926
Cdd:cd14551     81 LVDYTTRKFCIQ-------KVNRGIGEKRVRLVTQFHFTSWPDFGVPFTPIGMLKFLKKVKSANPPRAGPIVVHCSAGVG 153

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*...
gi 2032733617  927 RTGTYIVIDSMLQQIKDKSTVNVLGFLKHIRTQRNYLVQTEEQYIFIH 974
Cdd:cd14551    154 RTGTFIVIDAMLDMMHAEGKVDVFGFVSRIRQQRSQMVQTDMQYVFIY 201
R-PTP-D-2 cd14628
PTP-like domain of receptor-type tyrosine-protein phosphatase D, repeat 2; Receptor-type ...
 689-979 6.19e-66

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: 225.00  E-value: 6.19e-66
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032733617  689 IPVKQFVKHISELYS----NNQHGFSEDFEEVQRCTADMN--ITAehsNHPDNKHKNRYINILAYDHSRVKLRPLPGKDS 762
Cdd:cd14628      3 VPARNLYAYIQKLTQietgENVTGMELEFKRLASSKAHTSrfISA---NLPCNKFKNRLVNIMPYESTRVCLQPIRGVEG 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032733617  763 khSDYINANYVDGYNKAKAYIATQGPLKSTFEDFWRMIWEQNTGIIVMITNLVEKGRRKCDQYWPTENSEEYGNIIVTLK 842
Cdd:cd14628     80 --SDYINASFIDGYRQQKAYIATQGPLAETTEDFWRMLWEHNSTIVVMLTKLREMGREKCHQYWPAERSARYQYFVVDPM 157

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032733617  843 STNVHACYTVRRFTVrnTKMKKGQkgnpkgrqnERTVIQYHYTQWPDMGVPEYALPVLTFVRRSSAARTP--DMGPVVVH 920
Cdd:cd14628    158 AEYNMPQYILREFKV--TDARDGQ---------SRTVRQFQFTDWPEQGVPKSGEGFIDFIGQVHKTKEQfgQDGPISVH 226

                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 2032733617  921 CSAGVGRTGTYIVIDSMLQQIKDKSTVNVLGFLKHIRTQRNYLVQTEEQYIFIHDALLE 979
Cdd:cd14628    227 CSAGVGRTGVFITLSIVLERMRYEGVVDIFQTVKMLRTQRPAMVQTEDQYQFCYRAALE 285
R-PTP-S-2 cd14627
PTP-like domain of receptor-type tyrosine-protein phosphatase S, repeat 2; Receptor-type ...
 730-979 1.87e-65

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: 223.84  E-value: 1.87e-65
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032733617  730 SNHPDNKHKNRYINILAYDHSRVKLRPLPGKDSkhSDYINANYVDGYNKAKAYIATQGPLKSTFEDFWRMIWEQNTGIIV 809
Cdd:cd14627     48 ANLPCNKFKNRLVNIMPYETTRVCLQPIRGVEG--SDYINASFIDGYRQQKAYIATQGPLAETTEDFWRMLWENNSTIVV 125

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032733617  810 MITNLVEKGRRKCDQYWPTENSEEYGNIIVTLKSTNVHACYTVRRFTVrnTKMKKGQkgnpkgrqnERTVIQYHYTQWPD 889
Cdd:cd14627    126 MLTKLREMGREKCHQYWPAERSARYQYFVVDPMAEYNMPQYILREFKV--TDARDGQ---------SRTVRQFQFTDWPE 194

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032733617  890 MGVPEYALPVLTFVRRSSAARTP--DMGPVVVHCSAGVGRTGTYIVIDSMLQQIKDKSTVNVLGFLKHIRTQRNYLVQTE 967
Cdd:cd14627    195 QGVPKSGEGFIDFIGQVHKTKEQfgQDGPISVHCSAGVGRTGVFITLSIVLERMRYEGVVDIFQTVKMLRTQRPAMVQTE 274

                          250
                   ....*....|..
gi 2032733617  968 EQYIFIHDALLE 979
Cdd:cd14627    275 DEYQFCYQAALE 286
PTPc-N1_2 cd14545
catalytic domain of tyrosine-protein phosphatase non-receptor type 1 and type 2; ...
 736-972 1.37e-64

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: 218.80  E-value: 1.37e-64
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032733617  736 KHKNRYINILAYDHSRVKLRplpgkdSKHSDYINANYVDGYNKAKAYIATQGPLKSTFEDFWRMIWEQNTGIIVMITNLV 815
Cdd:cd14545      1 LNRYRDRDPYDHDRSRVKLK------QGDNDYINASLVEVEEAKRSYILTQGPLPNTSGHFWQMVWEQNSKAVIMLNKLM 74

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032733617  816 EKGRRKCDQYWPTENSE----EYGNIIVTLKSTNVHACYTVRRFTVRNTKMkkgqkgnpkgrQNERTVIQYHYTQWPDMG 891
Cdd:cd14545     75 EKGQIKCAQYWPQGEGNamifEDTGLKVTLLSEEDKSYYTVRTLELENLKT-----------QETREVLHFHYTTWPDFG 143

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032733617  892 VPEYALPVLTFVR--RSSAARTPDMGPVVVHCSAGVGRTGTYIVIDSMLQQIKDK--STVNVLGFLKHIRTQRNYLVQTE 967
Cdd:cd14545    144 VPESPAAFLNFLQkvRESGSLSSDVGPPVVHCSAGIGRSGTFCLVDTCLVLIEKGnpSSVDVKKVLLEMRKYRMGLIQTP 223


                   ....*
gi 2032733617  968 EQYIF 972
Cdd:cd14545    224 DQLRF 228
R-PTPc-C-1 cd14557
catalytic domain of receptor-type tyrosine-protein phosphatase C, repeat 1; Receptor-type ...
 767-974 3.17e-64

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: 216.62  E-value: 3.17e-64
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032733617  767 YINANYVDGYNKAKAYIATQGPLKSTFEDFWRMIWEQNTGIIVMITNLVEKGRRKCDQYWPT--ENSEEYGNIIVTLKST 844
Cdd:cd14557      1 YINASYIDGFKEPRKYIAAQGPKDETVDDFWRMIWEQKSTVIVMVTRCEEGNRNKCAQYWPSmeEGSRAFGDVVVKINEE 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032733617  845 NVHACYTVRRFTVRNTKMKKGqkgnpkgrqnERTVIQYHYTQWPDMGVPEYALPVLTFVRRSSAARTPDMGPVVVHCSAG 924
Cdd:cd14557     81 KICPDYIIRKLNINNKKEKGS----------GREVTHIQFTSWPDHGVPEDPHLLLKLRRRVNAFNNFFSGPIVVHCSAG 150

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|
gi 2032733617  925 VGRTGTYIVIDSMLQQIKDKSTVNVLGFLKHIRTQRNYLVQTEEQYIFIH 974
Cdd:cd14557    151 VGRTGTYIGIDAMLEGLEAEGRVDVYGYVVKLRRQRCLMVQVEAQYILIH 200
R-PTP-F-2 cd14629
PTP-like domain of receptor-type tyrosine-protein phosphatase F, repeat 2; Receptor-type ...
 730-979 7.14e-64

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: 219.21  E-value: 7.14e-64
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032733617  730 SNHPDNKHKNRYINILAYDHSRVKLRPLPGKDSkhSDYINANYVDGYNKAKAYIATQGPLKSTFEDFWRMIWEQNTGIIV 809
Cdd:cd14629     48 ANLPCNKFKNRLVNIMPYELTRVCLQPIRGVEG--SDYINASFIDGYRQQKAYIATQGPLAETTEDFWRMLWEHNSTIVV 125

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032733617  810 MITNLVEKGRRKCDQYWPTENSEEYGNIIVTLKSTNVHACYTVRRFTVrnTKMKKGQkgnpkgrqnERTVIQYHYTQWPD 889
Cdd:cd14629    126 MLTKLREMGREKCHQYWPAERSARYQYFVVDPMAEYNMPQYILREFKV--TDARDGQ---------SRTIRQFQFTDWPE 194

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032733617  890 MGVPEYALPVLTFVRRSSAARTP--DMGPVVVHCSAGVGRTGTYIVIDSMLQQIKDKSTVNVLGFLKHIRTQRNYLVQTE 967
Cdd:cd14629    195 QGVPKTGEGFIDFIGQVHKTKEQfgQDGPITVHCSAGVGRTGVFITLSIVLERMRYEGVVDMFQTVKTLRTQRPAMVQTE 274

                          250
                   ....*....|..
gi 2032733617  968 EQYIFIHDALLE 979
Cdd:cd14629    275 DQYQLCYRAALE 286
PTPc-N11 cd14605
catalytic domain of tyrosine-protein phosphatase non-receptor type 11; Tyrosine-protein ...
 734-981 1.01e-63

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: 217.19  E-value: 1.01e-63
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032733617  734 DNKHKNRYINILAYDHSRVKLRPlPGKDSKHSDYINANYVDGYNKA--------KAYIATQGPLKSTFEDFWRMIWEQNT 805
Cdd:cd14605      1 ENKNKNRYKNILPFDHTRVVLHD-GDPNEPVSDYINANIIMPEFETkcnnskpkKSYIATQGCLQNTVNDFWRMVFQENS 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032733617  806 GIIVMITNLVEKGRRKCDQYWPTENS-EEYGNIIV-TLKSTNVHacytvrRFTVRNTKMKKGQKGNpkgrqNERTVIQYH 883
Cdd:cd14605     80 RVIVMTTKEVERGKSKCVKYWPDEYAlKEYGVMRVrNVKESAAH------DYILRELKLSKVGQGN-----TERTVWQYH 148

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032733617  884 YTQWPDMGVPEYALPVLTFVRRSSAAR--TPDMGPVVVHCSAGVGRTGTYIVIDSMLQQIKDKST---VNVLGFLKHIRT 958
Cdd:cd14605    149 FRTWPDHGVPSDPGGVLDFLEEVHHKQesIMDAGPVVVHCSAGIGRTGTFIVIDILIDIIREKGVdcdIDVPKTIQMVRS 228

                          250       260
                   ....*....|....*....|...
gi 2032733617  959 QRNYLVQTEEQYIFIHDALLEAI 981
Cdd:cd14605    229 QRSGMVQTEAQYRFIYMAVQHYI 251
PTPc-N6 cd14606
catalytic domain of tyrosine-protein phosphatase non-receptor type 6; Tyrosine-protein ...
 733-981 2.44e-62

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


Pssm-ID: 350454 [Multi-domain]  Cd Length: 266  Bit Score: 213.59  E-value: 2.44e-62
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032733617  733 PDNKHKNRYINILAYDHSRVKLRplpGKDSK--HSDYINANYVDGY-----NKAKAYIATQGPLKSTFEDFWRMIWEQNT 805
Cdd:cd14606     16 PENKSKNRYKNILPFDHSRVILQ---GRDSNipGSDYINANYVKNQllgpdENAKTYIASQGCLEATVNDFWQMAWQENS 92

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032733617  806 GIIVMITNLVEKGRRKCDQYWPTENSE-EYGNIIVTLKSTNVHACYTVRrfTVRNTKMKKGQKgnpkgrqnERTVIQYHY 884
Cdd:cd14606     93 RVIVMTTREVEKGRNKCVPYWPEVGMQrAYGPYSVTNCGEHDTTEYKLR--TLQVSPLDNGEL--------IREIWHYQY 162

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032733617  885 TQWPDMGVPEYALPVLTFVRRSSAART--PDMGPVVVHCSAGVGRTGTYIVIDSMLQQIKDK---STVNVLGFLKHIRTQ 959
Cdd:cd14606    163 LSWPDHGVPSEPGGVLSFLDQINQRQEslPHAGPIIVHCSAGIGRTGTIIVIDMLMENISTKgldCDIDIQKTIQMVRAQ 242

                          250       260
                   ....*....|....*....|..
gi 2032733617  960 RNYLVQTEEQYIFIHDALLEAI 981
Cdd:cd14606    243 RSGMVQTEAQYKFIYVAIAQFI 264
R-PTPc-Q cd14616
catalytic domain of receptor-type tyrosine-protein phosphatase Q; Receptor-type ...
 739-974 1.09e-61

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: 210.15  E-value: 1.09e-61
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032733617  739 NRYINILAYDHSRVKLRPLPGkdSKHSDYINANYVDGYNKAKAYIATQGPLKSTFEDFWRMIWEQNTGIIVMITNLVEKG 818
Cdd:cd14616      1 NRFPNIKPYNNNRVKLIADAG--VPGSDYINASYISGYLCPNEFIATQGPLPGTVGDFWRMVWETRAKTIVMLTQCFEKG 78

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032733617  819 RRKCDQYWPTENS--EEYGNIIVTLKSTNVHACYTVRRFTVRntkmKKGqkgnpkgrqNERTVIQYHYTQWPDMGVPEYA 896
Cdd:cd14616     79 RIRCHQYWPEDNKpvTVFGDIVITKLMEDVQIDWTIRDLKIE----RHG---------DYMMVRQCNFTSWPEHGVPESS 145

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2032733617  897 LPVLTFVRRSSAARTPDMGPVVVHCSAGVGRTGTYIVIDSMLQQIKDKSTVNVLGFLKHIRTQRNYLVQTEEQYIFIH 974
Cdd:cd14616    146 APLIHFVKLVRASRAHDNTPMIVHCSAGVGRTGVFIALDHLTQHINDHDFVDIYGLVAELRSERMCMVQNLAQYIFLH 223
PTPc-N3_4 cd14541
catalytic domain of tyrosine-protein phosphatase non-receptor type 21 and type 14; ...
 766-980 2.42e-61

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: 208.72  E-value: 2.42e-61
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032733617  766 DYINANYVD----GYNKAKAYIATQGPLKSTFEDFWRMIWEQNTGIIVMITNLVEKGRRKCDQYWPTEN-SEEYGNIIVT 840
Cdd:cd14541      1 DYINANYVNmeipGSGIVNRYIAAQGPLPNTCADFWQMVWEQKSTLIVMLTTLVERGRVKCHQYWPDLGeTMQFGNLQIT 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032733617  841 LKSTNVHACYTVRRFTVRNTKMKKgqkgnpkgrqnERTVIQYHYTQWPDMGVPEYALPVLTFVRRSSAARTPDMGPVVVH 920
Cdd:cd14541     81 CVSEEVTPSFAFREFILTNTNTGE-----------ERHITQMQYLAWPDHGVPDDSSDFLDFVKRVRQNRVGMVEPTVVH 149

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032733617  921 CSAGVGRTGTYIVIDSMLQQIKDKSTVNVLGFLKHIRTQRNYLVQTEEQYIFIHDALLEA 980
Cdd:cd14541    150 CSAGIGRTGVLITMETAMCLIEANEPVYPLDIVRTMRDQRAMLIQTPSQYRFVCEAILRV 209
PTPc-N7 cd14612
catalytic domain of tyrosine-protein phosphatase non-receptor type 7; Tyrosine-protein ...
 725-977 3.78e-61

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: 209.69  E-value: 3.78e-61
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032733617  725 ITAEHSNHPDNKHKNRYINILAYDHSRVKLRPlPGKDSKHSDYINANYVDGYN-KAKAYIATQGPLKSTFEDFWRMIWEQ 803
Cdd:cd14612      5 VSPEELDIPGHASKDRYKTILPNPQSRVCLRR-AGSQEEEGSYINANYIRGYDgKEKAYIATQGPMLNTVSDFWEMVWQE 83

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032733617  804 NTGIIVMITNLVEKgRRKCDQYWPtENSEEYGNIIVTLKSTNVHACYTVRRFTVrntkmkkgqkgnpKGRQNERTVIQYH 883
Cdd:cd14612     84 ECPIIVMITKLKEK-KEKCVHYWP-EKEGTYGRFEIRVQDMKECDGYTIRDLTI-------------QLEEESRSVKHYW 148

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032733617  884 YTQWPDMGVPEYALPVLTFVRRSSAAR--TPDMGPVVVHCSAGVGRTGTYIVIDSMLQQIKDKSTVNVLGFLKHIRTQRN 961
Cdd:cd14612    149 FSSWPDHQTPESAGPLLRLVAEVEESRqtAASPGPIVVHCSAGIGRTGCFIATSIGCQQLKDTGKVDILGIVCQLRLDRG 228

                          250
                   ....*....|....*.
gi 2032733617  962 YLVQTEEQYIFIHDAL 977
Cdd:cd14612    229 GMIQTSEQYQFLHHTL 244
PTPc-N1 cd14608
catalytic domain of tyrosine-protein phosphatase non-receptor type 1; Tyrosine-protein ...
 730-979 5.02e-60

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: 207.57  E-value: 5.02e-60
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032733617  730 SNHPDNKHKNRYINILAYDHSRVKLRplpgkdSKHSDYINANYVDGYNKAKAYIATQGPLKSTFEDFWRMIWEQNTGIIV 809
Cdd:cd14608     20 AKLPKNKNRNRYRDVSPFDHSRIKLH------QEDNDYINASLIKMEEAQRSYILTQGPLPNTCGHFWEMVWEQKSRGVV 93

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032733617  810 MITNLVEKGRRKCDQYWPTENSEEY----GNIIVTLKSTNVHACYTVRRFTVRNTKMkkgqkgnpkgrQNERTVIQYHYT 885
Cdd:cd14608     94 MLNRVMEKGSLKCAQYWPQKEEKEMifedTNLKLTLISEDIKSYYTVRQLELENLTT-----------QETREILHFHYT 162

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032733617  886 QWPDMGVPEYALPVLTFV--RRSSAARTPDMGPVVVHCSAGVGRTGTYIVIDS---MLQQIKDKSTVNVLGFLKHIRTQR 960
Cdd:cd14608    163 TWPDFGVPESPASFLNFLfkVRESGSLSPEHGPVVVHCSAGIGRSGTFCLADTcllLMDKRKDPSSVDIKKVLLEMRKFR 242

                          250
                   ....*....|....*....
gi 2032733617  961 NYLVQTEEQYIFIHDALLE 979
Cdd:cd14608    243 MGLIQTADQLRFSYLAVIE 261
PTPc cd00047
catalytic domain of protein tyrosine phosphatases; Protein tyrosine phosphatases (PTP, EC 3.1. ...
 1066-1266 5.21e-60

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: 204.44  E-value: 5.21e-60
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032733617 1066 YINASYIMGYYRSNEFIITQHPLPHTTKDFWRMIWDHNAQIIVMLPDNQSLAEDEFV-YWPSR-EESMNCEAFTVTLISK 1143
Cdd:cd00047      1 YINASYIDGYRGPKEYIATQGPLPNTVEDFWRMVWEQKVSVIVMLTNLVEKGREKCErYWPEEgGKPLEYGDITVTLVSE 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032733617 1144 DRLclsneEQIIIHDFILEATQDDYVLEVRHFQCPKWPNPDAP--ISSTFELINVIKEEALTRDGPTIVHDEYGAVSAGT 1221
Cdd:cd00047     81 EEL-----SDYTIRTLELSPKGCSESREVTHLHYTGWPDHGVPssPEDLLALVRRVRKEARKPNGPIVVHCSAGVGRTGT 155

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*
gi 2032733617 1222 LCALTTLSQQLENENAVDVFQVAKMINLMRPGVFTDIEQYQFLYK 1266
Cdd:cd00047    156 FIAIDILLERLEAEGEVDVFEIVKALRKQRPGMVQTLEQYEFIYE 200
PTPc-N5 cd14613
catalytic domain of tyrosine-protein phosphatase non-receptor type 5; Tyrosine-protein ...
 738-977 6.03e-60

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: 206.64  E-value: 6.03e-60
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032733617  738 KNRYINILAYDHSRVKLRPlPGKDSKHSDYINANYVDGYN-KAKAYIATQGPLKSTFEDFWRMIWEQNTGIIVMITNLVE 816
Cdd:cd14613     28 KNRYKTILPNPHSRVCLTS-PDQDDPLSSYINANYIRGYGgEEKVYIATQGPTVNTVGDFWRMVWQERSPIIVMITNIEE 106

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032733617  817 KGRrKCDQYWPtENSEEYGNIIVTLKSTNVHACYTVRRFTVrntkmKKGQKgnpkgrqnERTVIQYHYTQWPDMGVPEYA 896
Cdd:cd14613    107 MNE-KCTEYWP-EEQVTYEGIEITVKQVIHADDYRLRLITL-----KSGGE--------ERGLKHYWYTSWPDQKTPDNA 171

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032733617  897 LPVLTFVRRSSAART---PDMGPVVVHCSAGVGRTGTYIVIDSMLQQIKDKSTVNVLGFLKHIRTQRNYLVQTEEQYIFI 973
Cdd:cd14613    172 PPLLQLVQEVEEARQqaePNCGPVIVHCSAGIGRTGCFIATSICCKQLRNEGVVDILRTTCQLRLDRGGMIQTCEQYQFV 251


                   ....
gi 2032733617  974 HDAL 977
Cdd:cd14613    252 HHVL 255
PTPc-N12 cd14604
catalytic domain of tyrosine-protein phosphatase non-receptor type 12; Tyrosine-protein ...
 691-985 7.61e-60

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: 207.86  E-value: 7.61e-60
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032733617  691 VKQFVKHISELYSNNQHG---FSEDFEEVQRCTADM-------NITAEHSnhpDNKHKNRYINILAYDHSRVKLR-PLPG 759
Cdd:cd14604      6 LKKFIERVQAMKSTDHNGednFASDFMRLRRLSTKYrtekiypTATGEKE---ENVKKNRYKDILPFDHSRVKLTlKTSS 82

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032733617  760 KDSkhsDYINANYVDGYNKAKAYIATQGPLKSTFEDFWRMIWEQNTGIIVMITNLVEKGRRKCDQYWPT--ENSEEYGNI 837
Cdd:cd14604     83 QDS---DYINANFIKGVYGPKAYIATQGPLANTVIDFWRMIWEYNVAIIVMACREFEMGRKKCERYWPLygEEPMTFGPF 159

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032733617  838 IVTLKSTNVHACYTVRRFTVRntkmkkgqkgnpkgRQNE-RTVIQYHYTQWPDMGVPEYALPVLTFVRRSSAARTPDMGP 916
Cdd:cd14604    160 RISCEAEQARTDYFIRTLLLE--------------FQNEtRRLYQFHYVNWPDHDVPSSFDSILDMISLMRKYQEHEDVP 225

                          250       260       270       280       290       300       310
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2032733617  917 VVVHCSAGVGRTGTYIVID---SMLQQIKDKSTVNVLGFLKHIRTQRNYLVQTEEQYIFIHDALLEaILGKE 985
Cdd:cd14604    226 ICIHCSAGCGRTGAICAIDytwNLLKAGKIPEEFNVFNLIQEMRTQRHSAVQTKEQYELVHRAIAQ-LFEKQ 296
PTPc-N18 cd14603
catalytic domain of tyrosine-protein phosphatase non-receptor type 18; Tyrosine-protein ...
 710-979 8.56e-60

catalytic domain of tyrosine-protein phosphatase non-receptor type 18; Tyrosine-protein phosphatase non-receptor type 18 (PTPN18), also called brain-derived phosphatase, belongs to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. PTPN18 regulates HER2-mediated cellular functions through defining both its phosphorylation and ubiquitination states. The N-terminal catalytic PTP domain of PTPN18 blocks lysosomal routing and delays the degradation of HER2 by dephosphorylation, and its C-terminal PEST domain promotes K48-linked HER2 ubiquitination and its destruction via the proteasome pathway.


Pssm-ID: 350451 [Multi-domain]  Cd Length: 266  Bit Score: 206.60  E-value: 8.56e-60
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032733617  710 SEDFEEVQRCTA----DMNITAEHSNHPDNKHKNRYINILAYDHSRVKLRPLpgKDSKHSDYINANYVDGYNKAKAYIAT 785
Cdd:cd14603      1 AGEFSEIRACSAafkaDYVCSTVAGGRKENVKKNRYKDILPYDQTRVILSLL--QEEGHSDYINANFIKGVDGSRAYIAT 78

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032733617  786 QGPLKSTFEDFWRMIWEQNTGIIVMITNLVEKGRRKCDQYWP-TENSEEYGNIIVT-LKSTNVHACYTVRRFTVrntkmk 863
Cdd:cd14603     79 QGPLSHTVLDFWRMIWQYGVKVILMACREIEMGKKKCERYWAqEQEPLQTGPFTITlVKEKRLNEEVILRTLKV------ 152

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032733617  864 kgqkgnpKGRQNERTVIQYHYTQWPDMGVPEYALPVLTFVRRSSAARTPDMGPVVVHCSAGVGRTGTYIVIDS-----ML 938
Cdd:cd14603    153 -------TFQKESRSVSHFQYMAWPDHGIPDSPDCMLAMIELARRLQGSGPEPLCVHCSAGCGRTGVICTVDYvrqllLT 225

                          250       260       270       280
                   ....*....|....*....|....*....|....*....|.
gi 2032733617  939 QQIKDKstVNVLGFLKHIRTQRNYLVQTEEQYIFIHDALLE 979
Cdd:cd14603    226 QRIPPD--FSIFDVVLEMRKQRPAAVQTEEQYEFLYHTVAQ 264
PTPc-N20_13 cd14538
catalytic domain of tyrosine-protein phosphatase non-receptor type 20 and type 13; ...
 767-981 2.60e-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: 2.60e-59
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032733617  767 YINANYV--DGYNKAKAYIATQGPLKSTFEDFWRMIWEQNTGIIVMITNLVEKGRRKCDQYWPtENSEE----YGNIIVT 840
Cdd:cd14538      1 YINASHIriPVGGDTYHYIACQGPLPNTTGDFWQMVWEQKSEVIAMVTQDVEGGKVKCHRYWP-DSLNKplicGGRLEVS 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032733617  841 LKSTNVHACYTVRRFTVRNTKMKKgqkgnpkgrqnERTVIQYHYTQWPDMGVPEYALPVLTFVR--RSSAartpDMGPVV 918
Cdd:cd14538     80 LEKYQSLQDFVIRRISLRDKETGE-----------VHHITHLNFTTWPDHGTPQSADPLLRFIRymRRIH----NSGPIV 144

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2032733617  919 VHCSAGVGRTGTYIVIDSMLQQIKDKSTVNVLGFLKHIRTQRNYLVQTEEQYIFIHDALLEAI 981
Cdd:cd14538    145 VHCSAGIGRTGVLITIDVALGLIERDLPFDIQDIVKDLREQRQGMIQTKDQYIFCYKACLEVL 207
R-PTPc-A-E-2 cd14552
catalytic domain of receptor-type tyrosine-protein phosphatase A and E, repeat 2; ...
 767-977 3.16e-59

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


Pssm-ID: 350400 [Multi-domain]  Cd Length: 202  Bit Score: 202.50  E-value: 3.16e-59
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032733617  767 YINANYVDGYNKAKAYIATQGPLKSTFEDFWRMIWEQNTGIIVMITNLVEKGRRKCDQYWPTENSEEYGNIIVTLKSTNV 846
Cdd:cd14552      1 YINASFIDGYRQKDAYIATQGPLDHTVEDFWRMIWEWKSCSIVMLTEIKERSQNKCAQYWPEDGSVSSGDITVELKDQTD 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032733617  847 HACYTVRRFTVRNTKMKKgqkgnpkgrqnERTVIQYHYTQWPDMGVPEYALPVLTFVRR-SSAARTPDMGPVVVHCSAGV 925
Cdd:cd14552     81 YEDYTLRDFLVTKGKGGS-----------TRTVRQFHFHGWPEVGIPDNGKGMIDLIAAvQKQQQQSGNHPITVHCSAGA 149

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|..
gi 2032733617  926 GRTGTYIVIDSMLQQIKDKSTVNVLGFLKHIRTQRNYLVQTEEQYIFIHDAL 977
Cdd:cd14552    150 GRTGTFCALSTVLERVKAEGVLDVFQVVKSLRLQRPHMVQTLEQYEFCYKVV 201
PTPc-N3 cd14600
catalytic domain of tyrosine-protein phosphatase non-receptor type 3; Tyrosine-protein ...
 713-978 1.87e-58

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: 202.77  E-value: 1.87e-58
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032733617  713 FEEVQRCTADMNITAehSNHPDNKHKNRYINILAYDHSRVKLRplpGKDskhsDYINANYVD----GYNKAKAYIATQGP 788
Cdd:cd14600     20 FEQLYRKKPGLAITC--AKLPQNMDKNRYKDVLPYDATRVVLQ---GNE----DYINASYVNmeipSANIVNKYIATQGP 90

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032733617  789 LKSTFEDFWRMIWEQNTGIIVMITNLVEKGRRKCDQYWP-TENSEEYGNIIVTLKSTNVHACYTVRRFTVRNTkmKKGQk 867
Cdd:cd14600     91 LPHTCAQFWQVVWEQKLSLIVMLTTLTERGRTKCHQYWPdPPDVMEYGGFRVQCHSEDCTIAYVFREMLLTNT--QTGE- 167

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032733617  868 gnpkgrqnERTVIQYHYTQWPDMGVPEYALPVLTFVRRSSAARTpDMGPVVVHCSAGVGRTGTYIVIDSMLQQIKDKSTV 947
Cdd:cd14600    168 --------ERTVTHLQYVAWPDHGVPDDSSDFLEFVNYVRSKRV-ENEPVLVHCSAGIGRTGVLVTMETAMCLTERNQPV 238

                          250       260       270
                   ....*....|....*....|....*....|.
gi 2032733617  948 NVLGFLKHIRTQRNYLVQTEEQYIFIHDALL 978
Cdd:cd14600    239 YPLDIVRKMRDQRAMMVQTSSQYKFVCEAIL 269
R-PTPc-R cd14611
catalytic domain of receptor-type tyrosine-protein phosphatase R; Receptor-type ...
 738-974 3.36e-58

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: 200.53  E-value: 3.36e-58
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032733617  738 KNRYINILAYDHSRVKLRPLPGKDSKhSDYINANYVDGY-NKAKAYIATQGPLKSTFEDFWRMIWEQNTGIIVMITNLVE 816
Cdd:cd14611      2 KNRYKTILPNPHSRVCLKPKNSNDSL-STYINANYIRGYgGKEKAFIATQGPMINTVNDFWQMVWQEDSPVIVMITKLKE 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032733617  817 KGRrKCDQYWPtENSEEYGNIIVTLKSTNVHACYTVRRFTVRNtkmkkgqkgnpkGRQNeRTVIQYHYTQWPDMGVPEYA 896
Cdd:cd14611     81 KNE-KCVLYWP-EKRGIYGKVEVLVNSVKECDNYTIRNLTLKQ------------GSQS-RSVKHYWYTSWPDHKTPDSA 145

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032733617  897 LPVLTFV------RRSSAARtpdmGPVVVHCSAGVGRTGTYIVIDSMLQQIKDKSTVNVLGFLKHIRTQRNYLVQTEEQY 970
Cdd:cd14611    146 QPLLQLMldveedRLASPGR----GPVVVHCSAGIGRTGCFIATTIGCQQLKEEGVVDVLSIVCQLRVDRGGMVQTSEQY 221


                   ....
gi 2032733617  971 IFIH 974
Cdd:cd14611    222 EFVH 225
alpha_CA_IV_XV_like cd03117
Carbonic anhydrase alpha, CA_IV, CA_XV, like isozymes. Carbonic anhydrases (CAs) are ...
 1-203 1.21e-57

Carbonic anhydrase alpha, CA_IV, CA_XV, like isozymes. Carbonic anhydrases (CAs) are zinc-containing enzymes that catalyze the reversible hydration of carbon dioxide in a two-step mechanism: a nucleophilic attack of a zinc-bound hydroxide ion on carbon dioxide, followed by the regeneration of the active site by ionization of the zinc-bound water molecule and removal of a proton from the active site. They are ubiquitous enzymes involved in fundamental processes like photosynthesis, respiration, pH homeostasis and ion transport. There are three evolutionary distinct groups - alpha, beta and gamma carbonic anhydrases - which show no significant sequence identity or structural similarity. Most alpha CAs are monomeric enzymes. The zinc ion is complexed by three histidine residues. This subgroup, restricted to animals, contains isozyme IV and similar proteins such as mouse CA XV. Isozymes IV is attached to membranes via a glycosylphosphatidylinositol (GPI) tail. In mammals, Isozyme IV plays crucial roles in kidney and lung function, amongst others. This subgroup also contains the dual domain CA from the giant clam, Tridacna gigas. T. gigas CA plays a role in the movement of inorganic carbon from the surrounding seawater to the symbiotic algae found in the clam's tissues. CA XV is expressed in several species but not in humans or chimps. Similar to isozyme CA IV, CA XV attaches to membranes via a GPI tail.


Pssm-ID: 239391  Cd Length: 234  Bit Score: 199.03  E-value: 1.21e-57
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032733617    1 MKNTGKTVAILLKDDYFVSGAGLPGRFKAEKVEFHWGqSNGSAGSEHSINGKRFPVEMQIFFYNpDDFDSFGTAVLENRV 80
Cdd:cd03117     37 ITNNGHTVQVTLPDGAKISGGGLPGTYKALQFHFHWG-SNGSPGSEHTIDGERYPMELHIVHIK-ESYNSLLEALKDSDG 114

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032733617   81 VGAMAVFFQVSQRDNSALDPIIHGLKGVVHHEKETFLDPFVLRELLPT-SLGSYYRYTGSLTTPPCSEIVEWIVFRKPVP 159
Cdd:cd03117    115 LAVLGFFIEEGEEENTNFDPLISALSNIPQKGGSTNLTPFSLRSLLPSvLLTKYYRYNGSLTTPGCNEAVIWTVFEEPIP 194

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*.
gi 2032733617  160 ISYHQLEAFYSI--FTTEQQDHVKsveylrNNFRPQQSLNNRKVSK 203
Cdd:cd03117    195 ISRAQLDAFSTVlfFDTDNGQPMV------NNFRPVQPLNGRVVYA 234
PTPc-N22_18_12 cd14542
catalytic domain of tyrosine-protein phosphatase non-receptor type 22, type 18 and type 12; ...
 767-974 1.34e-57

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: 197.65  E-value: 1.34e-57
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032733617  767 YINANYVDGYNKAKAYIATQGPLKSTFEDFWRMIWEQNTGIIVMITNLVEKGRRKCDQYWPTENSEE--YGNIIVTL-KS 843
Cdd:cd14542      1 YINANFIKGVSGSKAYIATQGPLPNTVLDFWRMIWEYNVQVIVMACREFEMGKKKCERYWPEEGEEQlqFGPFKISLeKE 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032733617  844 TNVHACYTVRRFTVRNTKmkkgqkgnpkgrqNERTVIQYHYTQWPDMGVPEYALPVLTFVRRSSAARTPDMGPVVVHCSA 923
Cdd:cd14542     81 KRVGPDFLIRTLKVTFQK-------------ESRTVYQFHYTAWPDHGVPSSVDPILDLVRLVRDYQGSEDVPICVHCSA 147

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....
gi 2032733617  924 GVGRTGTYIVID---SMLQQIKDKSTVNVLGFLKHIRTQRNYLVQTEEQYIFIH 974
Cdd:cd14542    148 GCGRTGTICAIDyvwNLLKTGKIPEEFSLFDLVREMRKQRPAMVQTKEQYELVY 201
PTPc-N2 cd14607
catalytic domain of tyrosine-protein phosphatase non-receptor type 2; Tyrosine-protein ...
 730-977 2.27e-57

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: 199.04  E-value: 2.27e-57
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032733617  730 SNHPDNKHKNRYINILAYDHSRVKLRplpgkdSKHSDYINANYVDGYNKAKAYIATQGPLKSTFEDFWRMIWEQNTGIIV 809
Cdd:cd14607     19 AKYPENRNRNRYRDVSPYDHSRVKLQ------NTENDYINASLVVIEEAQRSYILTQGPLPNTCCHFWLMVWQQKTKAVV 92

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032733617  810 MITNLVEKGRRKCDQYWPTENSEEYG----NIIVTLKSTNVHACYTVRRFTVRNtkMKKGQKgnpkgrqneRTVIQYHYT 885
Cdd:cd14607     93 MLNRIVEKDSVKCAQYWPTDEEEVLSfketGFSVKLLSEDVKSYYTVHLLQLEN--INSGET---------RTISHFHYT 161

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032733617  886 QWPDMGVPEYALPVLTFV--RRSSAARTPDMGPVVVHCSAGVGRTGTYIVIDS--MLQQIKDKSTVNVLGFLKHIRTQRN 961
Cdd:cd14607    162 TWPDFGVPESPASFLNFLfkVRESGSLSPEHGPAVVHCSAGIGRSGTFSLVDTclVLMEKKDPDSVDIKQVLLDMRKYRM 241

                          250
                   ....*....|....*.
gi 2032733617  962 YLVQTEEQYIFIHDAL 977
Cdd:cd14607    242 GLIQTPDQLRFSYMAV 257
PTPc-N22 cd14602
catalytic domain of tyrosine-protein phosphatase non-receptor type 22; Tyrosine-protein ...
 738-979 3.93e-57

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: 197.76  E-value: 3.93e-57
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032733617  738 KNRYINILAYDHSRVKLRPLPGKDSkhSDYINANYVDGYNKAKAYIATQGPLKSTFEDFWRMIWEQNTGIIVMITNLVEK 817
Cdd:cd14602      1 KNRYKDILPYDHSRVELSLITSDED--SDYINANFIKGVYGPRAYIATQGPLSTTLLDFWRMIWEYSVLIIVMACMEFEM 78

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032733617  818 GRRKCDQYW--PTENSEEYGNIIVTLKSTNVHACYTVRRFTVRNTKMKkgqkgnpkgrqneRTVIQYHYTQWPDMGVPEY 895
Cdd:cd14602     79 GKKKCERYWaePGEMQLEFGPFSVTCEAEKRKSDYIIRTLKVKFNSET-------------RTIYQFHYKNWPDHDVPSS 145

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032733617  896 ALPVLTFVRRSSAARTPDMGPVVVHCSAGVGRTGTYIVIDSMLQQIKDK---STVNVLGFLKHIRTQRNYLVQTEEQYIF 972
Cdd:cd14602    146 IDPILELIWDVRCYQEDDSVPICIHCSAGCGRTGVICAIDYTWMLLKDGiipENFSVFSLIQEMRTQRPSLVQTKEQYEL 225


                   ....*..
gi 2032733617  973 IHDALLE 979
Cdd:cd14602    226 VYNAVIE 232
R-PTP-N2 cd14610
PTP-like domain of receptor-type tyrosine-protein phosphatase N2; Receptor-type ...
 700-981 4.05e-57

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: 199.51  E-value: 4.05e-57
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032733617  700 ELYSNNQHGFSEDFEEVQRCTADMNITAEhSNHPDNKHKNRYINILAYDHSRVKLRplpGKDSK-HSDYINANYV-DGYN 777
Cdd:cd14610     10 EDHLKNKNRLEKEWEALCAYQAEPNATNV-AQREENVQKNRSLAVLPYDHSRIILK---AENSHsHSDYINASPImDHDP 85

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032733617  778 KAKAYIATQGPLKSTFEDFWRMIWEQNTGIIVMITNLVEKGRRKCDQYWPTENSEEYGNIIVTLKSTNVHaC--YTVRRF 855
Cdd:cd14610     86 RNPAYIATQGPLPATVADFWQMVWESGCVVIVMLTPLAENGVKQCYHYWPDEGSNLYHIYEVNLVSEHIW-CedFLVRSF 164

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032733617  856 TVRNTKMkkgqkgnpkgrqNE-RTVIQYHYTQWPDMGVPEYALPVLTFVRRSSAARTPDMGPVVVHCSAGVGRTGTYIVI 934
Cdd:cd14610    165 YLKNLQT------------NEtRTVTQFHFLSWNDQGVPASTRSLLDFRRKVNKCYRGRSCPIIVHCSDGAGRSGTYILI 232

                          250       260       270       280
                   ....*....|....*....|....*....|....*....|....*...
gi 2032733617  935 DSMLQQI-KDKSTVNVLGFLKHIRTQRNYLVQTEEQYIFIHDALLEAI 981
Cdd:cd14610    233 DMVLNKMaKGAKEIDIAATLEHLRDQRPGMVQTKEQFEFALTAVAEEV 280
R-PTP-N cd14609
PTP-like domain of receptor-type tyrosine-protein phosphatase N; Receptor-type ...
 735-981 4.30e-57

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: 199.11  E-value: 4.30e-57
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032733617  735 NKHKNRYINILAYDHSRVKLRPlpGKDSKHSDYINAN-YVDGYNKAKAYIATQGPLKSTFEDFWRMIWEQNTGIIVMITN 813
Cdd:cd14609     42 NVKKNRNPDFVPYDHARIKLKA--ESNPSRSDYINASpIIEHDPRMPAYIATQGPLSHTIADFWQMVWENGCTVIVMLTP 119

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032733617  814 LVEKGRRKCDQYWPTENSEEYGNIIVTLKSTNVHaC--YTVRRFTVRNTKMkkgqkgnpkgrQNERTVIQYHYTQWPDMG 891
Cdd:cd14609    120 LVEDGVKQCDRYWPDEGSSLYHIYEVNLVSEHIW-CedFLVRSFYLKNVQT-----------QETRTLTQFHFLSWPAEG 187

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032733617  892 VPEYALPVLTFVRRSSAARTPDMGPVVVHCSAGVGRTGTYIVIDSMLQQI-KDKSTVNVLGFLKHIRTQRNYLVQTEEQY 970
Cdd:cd14609    188 IPSSTRPLLDFRRKVNKCYRGRSCPIIVHCSDGAGRTGTYILIDMVLNRMaKGVKEIDIAATLEHVRDQRPGMVRTKDQF 267

                          250
                   ....*....|.
gi 2032733617  971 IFIHDALLEAI 981
Cdd:cd14609    268 EFALTAVAEEV 278
PTPc-N21_14 cd14540
catalytic domain of tyrosine-protein phosphatase non-receptor type 21 and type 14; ...
 767-979 7.41e-57

catalytic domain of tyrosine-protein phosphatase non-receptor type 21 and type 14; Tyrosine-protein phosphatase non-receptor type 21 (PTPN21) and type 14 (PTPN14) belong to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. Both PTPN21 and PTPN14 contain an N-terminal FERM domain and a C-terminal catalytic PTP domain, separated by a long intervening sequence.


Pssm-ID: 350388 [Multi-domain]  Cd Length: 219  Bit Score: 196.14  E-value: 7.41e-57
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032733617  767 YINANYVDGY--NKAKAYIATQGPLKSTFEDFWRMIWEQNTGIIVMITNLVEKGRRKCDQYWPTENSEE----YGNIIVT 840
Cdd:cd14540      1 YINASHITATvgGKQRFYIAAQGPLQNTVGDFWQMVWEQGVYLVVMVTAEEEGGREKCFRYWPTLGGEHdaltFGEYKVS 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032733617  841 LKSTNVHACYTVRRFTVRNTkmkkgqkgnPKGRqnERTVIQYHYTQWPDMGVPEYALPVLTF------VRRSS----AAR 910
Cdd:cd14540     81 TKFSVSSGCYTTTGLRVKHT---------LSGQ--SRTVWHLQYTDWPDHGCPEDVSGFLDFleeinsVRRHTnqdvAGH 149

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2032733617  911 TPDmGPVVVHCSAGVGRTGTYIVIDSMLQQIKDKSTVNVLGFLKHIRTQRNYLVQTEEQYIFIHDALLE 979
Cdd:cd14540    150 NRN-PPTLVHCSAGVGRTGVVILADLMLYCLDHNEELDIPRVLALLRHQRMLLVQTLAQYKFVYNVLIQ 217
R-PTPc-A-2 cd14623
catalytic domain of receptor-type tyrosine-protein phosphatase A, repeat 2; Receptor-type ...
 740-979 8.55e-56

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: 193.72  E-value: 8.55e-56
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032733617  740 RYINILAYDHSRVKLRPLPGKDSkhSDYINANYVDGYNKAKAYIATQGPLKSTFEDFWRMIWEQNTGIIVMITNLVEKGR 819
Cdd:cd14623      1 RVLQIIPYEFNRVIIPVKRGEEN--TDYVNASFIDGYRQKDSYIASQGPLQHTIEDFWRMIWEWKSCSIVMLTELEERGQ 78

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032733617  820 RKCDQYWPTENSEEYGNIIVTLKSTNVHACYTVRRFTVRNTKMKKgqkgnpkgrqnERTVIQYHYTQWPDMGVPEYALPV 899
Cdd:cd14623     79 EKCAQYWPSDGSVSYGDITIELKKEEECESYTVRDLLVTNTRENK-----------SRQIRQFHFHGWPEVGIPSDGKGM 147

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032733617  900 LTFVRRSSAARTPDMG-PVVVHCSAGVGRTGTYIVIDSMLQQIKDKSTVNVLGFLKHIRTQRNYLVQTEEQYIFIHDALL 978
Cdd:cd14623    148 INIIAAVQKQQQQSGNhPITVHCSAGAGRTGTFCALSTVLERVKAEGILDVFQTVKSLRLQRPHMVQTLEQYEFCYKVVQ 227


                   .
gi 2032733617  979 E 979
Cdd:cd14623    228 E 228
R-PTP-N-N2 cd14546
PTP-like domain of receptor-type tyrosine-protein phosphatase-like N and N2; Receptor-type ...
 767-981 7.13e-54

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: 187.27  E-value: 7.13e-54
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032733617  767 YINANYVDGYN-KAKAYIATQGPLKSTFEDFWRMIWEQNTGIIVMITNLVEKGRRKCDQYWPTENSEEYGNIIVTLKSTN 845
Cdd:cd14546      1 YINASTIYDHDpRNPAYIATQGPLPHTIADFWQMIWEQGCVVIVMLTRLQENGVKQCARYWPEEGSEVYHIYEVHLVSEH 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032733617  846 V-HACYTVRRFTVRNTKmkkgqkgnpkgRQNERTVIQYHYTQWPDMGVPEYALPVLTFVRRSSAARTPDMGPVVVHCSAG 924
Cdd:cd14546     81 IwCDDYLVRSFYLKNLQ-----------TSETRTVTQFHFLSWPDEGIPASAKPLLEFRRKVNKSYRGRSCPIVVHCSDG 149

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 2032733617  925 VGRTGTYIVIDSMLQQI-KDKSTVNVLGFLKHIRTQRNYLVQTEEQYIFIHDALLEAI 981
Cdd:cd14546    150 AGRTGTYILIDMVLNRMaKGAKEIDIAATLEHLRDQRPGMVKTKDQFEFVLTAVAEEV 207
R-PTPc-E-2 cd14622
catalytic domain of receptor-type tyrosine-protein phosphatase E, repeat 2; Receptor-type ...
 766-974 2.94e-52

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: 182.51  E-value: 2.94e-52
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032733617  766 DYINANYVDGYNKAKAYIATQGPLKSTFEDFWRMIWEQNTGIIVMITNLVEKGRRKCDQYWPTENSEEYGNIIVTLKSTN 845
Cdd:cd14622      1 DYINASFIDGYRQKDYFIATQGPLAHTVEDFWRMVWEWKCHTIVMLTELQEREQEKCVQYWPSEGSVTHGEITIEIKNDT 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032733617  846 VHACYTVRRFTVRNTKMKKgqkgnpkgrqnERTVIQYHYTQWPDMGVPEYA---LPVLTFVRRSSaaRTPDMGPVVVHCS 922
Cdd:cd14622     81 LLETISIRDFLVTYNQEKQ-----------TRLVRQFHFHGWPEIGIPAEGkgmIDLIAAVQKQQ--QQTGNHPIVVHCS 147

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|..
gi 2032733617  923 AGVGRTGTYIVIDSMLQQIKDKSTVNVLGFLKHIRTQRNYLVQTEEQYIFIH 974
Cdd:cd14622    148 AGAGRTGTFIALSNILERVKAEGLLDVFQTVKSLRLQRPHMVQTLEQYEFCY 199
PTPc-N14 cd14599
catalytic domain of tyrosine-protein phosphatase non-receptor type 14; Tyrosine-protein ...
 709-979 1.91e-51

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: 183.27  E-value: 1.91e-51
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032733617  709 FSEdFEEVQRCTADMNITAehSNHPDNKHKNRYINILAYDHSRVKLrpLPGKDSkHSDYINANYVDGYNKAKA--YIATQ 786
Cdd:cd14599     15 FTE-YEQIPKKKADGVFTT--ATLPENAERNRIREVVPYEENRVEL--VPTKEN-NTGYINASHIKVTVGGEEwhYIATQ 88

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032733617  787 GPLKSTFEDFWRMIWEQNTGIIVMITNLVEKGRRKCDQYWP----TENSEEYGNIIVTLKSTNVHACYTVRRFTVRNtkM 862
Cdd:cd14599     89 GPLPHTCHDFWQMVWEQGVNVIAMVTAEEEGGRSKSHRYWPklgsKHSSATYGKFKVTTKFRTDSGCYATTGLKVKH--L 166

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032733617  863 KKGQkgnpkgrqnERTVIQYHYTQWPDMGVPEYALPVLTF------VRR-------SSAARTPdmgPVVVHCSAGVGRTG 929
Cdd:cd14599    167 LSGQ---------ERTVWHLQYTDWPDHGCPEEVQGFLSYleeiqsVRRhtnsmldSTKNCNP---PIVVHCSAGVGRTG 234

                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|
gi 2032733617  930 TYIVIDSMLQQIKDKSTVNVLGFLKHIRTQRNYLVQTEEQYIFIHDALLE 979
Cdd:cd14599    235 VVILTELMIGCLEHNEKVEVPVMLRHLREQRMFMIQTIAQYKFVYQVLIQ 284
R-PTP-LAR-2 cd14554
PTP-like domain of the LAR family receptor-type tyrosine-protein phosphatases, repeat 2; The ...
 1035-1269 2.20e-51

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


Pssm-ID: 350402 [Multi-domain]  Cd Length: 238  Bit Score: 181.18  E-value: 2.20e-51
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032733617 1035 CNKEKNRNSSVVPSERARVGLAPLPGMKGTDYINASYIMGYYRSNEFIITQHPLPHTTKDFWRMIWDHNAQIIVMLPDNQ 1114
Cdd:cd14554      5 CNKFKNRLVNILPYESTRVCLQPIRGVEGSDYINASFIDGYRQRGAYIATQGPLAETTEDFWRMLWEHNSTIIVMLTKLR 84

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032733617 1115 SLAEDE-FVYWPSrEESMNCEAFTVtliskDRLCLSNEEQIIIHDFILEATQDDYVLEVRHFQCPKWPNPDAPISST--F 1191
Cdd:cd14554     85 EMGREKcHQYWPA-ERSARYQYFVV-----DPMAEYNMPQYILREFKVTDARDGQSRTVRQFQFTDWPEQGVPKSGEgfI 158

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032733617 1192 ELINVIKE--EALTRDGPTIVHDEYGAVSAGTLCALTTLSQQLENENAVDVFQVAKMINLMRPGVFTDIEQYQFLYKAML 1269
Cdd:cd14554    159 DFIGQVHKtkEQFGQEGPITVHCSAGVGRTGVFITLSIVLERMRYEGVVDVFQTVKLLRTQRPAMVQTEDQYQFCYRAAL 238
PTPc_plant_PTP1 cd17658
protein tyrosine phosphatase 1 from Arabidopsis thaliana and similar plant PTPs; Arabidopsis ...
 767-974 3.08e-51

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: 179.58  E-value: 3.08e-51
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032733617  767 YINANYV--DGYNKAKAYIATQGPLKSTFEDFWRMIWEQNTGIIVMITNLVEKGRR-KCDQYWPTE--NSEEYGNIIVTL 841
Cdd:cd17658      1 YINASLVetPASESLPKFIATQGPLPHTFEDFWEMVIQQRCPVIIMLTRLVDNYSTaKCADYFPAEenESREFGRISVTN 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032733617  842 KSTNvhacytvrrfTVRNTKMKKGQKGNPKGRQNE-RTVIQYHYTQWPDMGVPEYALPVLTFVRRSSAArTPDMGPVVVH 920
Cdd:cd17658     81 KKLK----------HSQHSITLRVLEVQYIESEEPpLSVLHIQYPEWPDHGVPKDTRSVRELLKRLYGI-PPSAGPIVVH 149

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 2032733617  921 CSAGVGRTGTYIVIDSMLQQI--KDKSTVNVLGFLKHIRTQRNYLVQTEEQYIFIH 974
Cdd:cd17658    150 CSAGIGRTGAYCTIHNTIRRIleGDMSAVDLSKTVRKFRSQRIGMVQTQDQYIFCY 205
PTPc-N13 cd14597
catalytic domain of tyrosine-protein phosphatase non-receptor type 13; Tyrosine-protein ...
 734-978 5.59e-51

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: 180.03  E-value: 5.59e-51
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032733617  734 DNKHKNRYINILAYDHSRVKLrplpGKDSkhsDYINANYVD---GyNKAKAYIATQGPLKSTFEDFWRMIWEQNTGIIVM 810
Cdd:cd14597      2 ENRKKNRYKNILPYDTTRVPL----GDEG---GYINASFIKmpvG-DEEFVYIACQGPLPTTVADFWQMVWEQKSTVIAM 73

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032733617  811 ITNLVEKGRRKCDQYWPtensEEYGNIIVT---LKSTNVHAcYTVRRFTVRNTKMKKGQKGnpkgrqNERTVIQYHYTQW 887
Cdd:cd14597     74 MTQEVEGGKIKCQRYWP----EILGKTTMVdnrLQLTLVRM-QQLKNFVIRVLELEDIQTR------EVRHITHLNFTAW 142

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032733617  888 PDMGVPEYALPVLTFVrrSSAARTPDMGPVVVHCSAGVGRTGTYIVIDSMLQQIKDKSTVNVLGFLKHIRTQRNYLVQTE 967
Cdd:cd14597    143 PDHDTPSQPEQLLTFI--SYMRHIHKSGPIITHCSAGIGRSGTLICIDVVLGLISKDLDFDISDIVRTMRLQRHGMVQTE 220

                          250
                   ....*....|.
gi 2032733617  968 EQYIFIHDALL 978
Cdd:cd14597    221 DQYIFCYQVIL 231
R-PTP-D-2 cd14628
PTP-like domain of receptor-type tyrosine-protein phosphatase D, repeat 2; Receptor-type ...
 986-1274 7.94e-51

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: 181.47  E-value: 7.94e-51
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032733617  986 TEVSANQLHSYVNSILIPGIGGK-TRLEKQFKLVTQCNAKYVECFSAQKDCNKEKNRNSSVVPSERARVGLAPLPGMKGT 1064
Cdd:cd14628      1 TEVPARNLYAYIQKLTQIETGENvTGMELEFKRLASSKAHTSRFISANLPCNKFKNRLVNIMPYESTRVCLQPIRGVEGS 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032733617 1065 DYINASYIMGYYRSNEFIITQHPLPHTTKDFWRMIWDHNAQIIVMLPDNQSLAEDE-FVYWPSrEESMNCEAFTVtlisk 1143
Cdd:cd14628     81 DYINASFIDGYRQQKAYIATQGPLAETTEDFWRMLWEHNSTIVVMLTKLREMGREKcHQYWPA-ERSARYQYFVV----- 154

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032733617 1144 DRLCLSNEEQIIIHDFILEATQDDYVLEVRHFQCPKWPNPDAPISST--FELINVI--KEEALTRDGPTIVHDEYGAVSA 1219
Cdd:cd14628    155 DPMAEYNMPQYILREFKVTDARDGQSRTVRQFQFTDWPEQGVPKSGEgfIDFIGQVhkTKEQFGQDGPISVHCSAGVGRT 234

                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 2032733617 1220 GTLCALTTLSQQLENENAVDVFQVAKMINLMRPGVFTDIEQYQFLYKAMLSLVST 1274
Cdd:cd14628    235 GVFITLSIVLERMRYEGVVDIFQTVKMLRTQRPAMVQTEDQYQFCYRAALEYLGS 289
R-PTP-C-2 cd14558
PTP-like domain of receptor-type tyrosine-protein phosphatase C, repeat 2; Receptor-type ...
 767-975 5.90e-50

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


Pssm-ID: 350406 [Multi-domain]  Cd Length: 203  Bit Score: 175.66  E-value: 5.90e-50
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032733617  767 YINANYVDGYNKAKAYIATQGPLKSTFEDFWRMIWEQNTGIIVMITNLVEKGRRKCDQYWPtENSEEYGNIIVTLKSTNV 846
Cdd:cd14558      1 YINASFIDGYWGPKSLIATQGPLPDTIADFWQMIFQKKVKVIVMLTELKEGDQEQCAQYWG-DEKKTYGDIEVELKDTEK 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032733617  847 HACYTVRRFTVRNTKMKKgqkgnpkgrqnERTVIQYHYTQWPDMGVPEYALPVLTFVRR------SSAARTPDMGPVVVH 920
Cdd:cd14558     80 SPTYTVRVFEITHLKRKD-----------SRTVYQYQYHKWKGEELPEKPKDLVDMIKSikqklpYKNSKHGRSVPIVVH 148

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 2032733617  921 CSAGVGRTGTYIVIDSMLQQIKDKSTVNVLGFLKHIRTQRNYLVQTEEQYIFIHD 975
Cdd:cd14558    149 CSDGSSRTGIFCALWNLLESAETEKVVDVFQVVKALRKQRPGMVSTLEQYQFLYD 203
R-PTP-S-2 cd14627
PTP-like domain of receptor-type tyrosine-protein phosphatase S, repeat 2; Receptor-type ...
 986-1274 4.12e-49

PTP-like domain of receptor-type tyrosine-protein phosphatase S, repeat 2; Receptor-type tyrosine-protein phosphatase S (PTPRS), also known as receptor-type tyrosine-protein phosphatase sigma (R-PTP-sigma), belongs to the LAR (leukocyte common antigen-related) family of receptor-type tyrosine-protein phosphatases (RPTPs), which belong to the larger family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. PTPRS is a receptor for glycosaminoglycans, including heparan sulfate proteoglycan and neural chondroitin sulfate proteoglycans (CSPGs), which present a barrier to axon regeneration. It also plays a role in stimulating neurite outgrowth in response to the heparan sulfate proteoglycan GPC2. PTPRS contains an extracellular region with three immunoglobulin-like (Ig) domains and four to eight fibronectin type III (FN3) repeats (determined by alternative splicing), a single transmembrane domain, followed by an intracellular region with a membrane-proximal catalytic PTP domain (repeat 1, also called D1) and a membrane-distal non-catalytic PTP-like domain (repeat 2, also called D2). This model represents the non-catalytic PTP-like domain (repeat 2). Although described as non-catalytic, this domain contains the catalytic cysteine and the active site signature motif, HCSAGxGRxG.


Pssm-ID: 350475 [Multi-domain]  Cd Length: 290  Bit Score: 176.46  E-value: 4.12e-49
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032733617  986 TEVSANQLHSYVNSI--LIPGiGGKTRLEKQFKLVTQCNAKYVECFSAQKDCNKEKNRNSSVVPSERARVGLAPLPGMKG 1063
Cdd:cd14627      2 TEVPARNLYSYIQKLaqVEVG-EHVTGMELEFKRLANSKAHTSRFISANLPCNKFKNRLVNIMPYETTRVCLQPIRGVEG 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032733617 1064 TDYINASYIMGYYRSNEFIITQHPLPHTTKDFWRMIWDHNAQIIVMLPDNQSLAEDE-FVYWPSrEESMNCEAFTVtlis 1142
Cdd:cd14627     81 SDYINASFIDGYRQQKAYIATQGPLAETTEDFWRMLWENNSTIVVMLTKLREMGREKcHQYWPA-ERSARYQYFVV---- 155

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032733617 1143 kDRLCLSNEEQIIIHDFILEATQDDYVLEVRHFQCPKWPNPDAPISST--FELINVI--KEEALTRDGPTIVHDEYGAVS 1218
Cdd:cd14627    156 -DPMAEYNMPQYILREFKVTDARDGQSRTVRQFQFTDWPEQGVPKSGEgfIDFIGQVhkTKEQFGQDGPISVHCSAGVGR 234

                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 2032733617 1219 AGTLCALTTLSQQLENENAVDVFQVAKMINLMRPGVFTDIEQYQFLYKAMLSLVST 1274
Cdd:cd14627    235 TGVFITLSIVLERMRYEGVVDIFQTVKMLRTQRPAMVQTEDEYQFCYQAALEYLGS 290
PTPc-N4 cd14601
catalytic domain of tyrosine-protein phosphatase non-receptor type 4; Tyrosine-protein ...
 766-979 7.88e-49

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


Pssm-ID: 350449 [Multi-domain]  Cd Length: 212  Bit Score: 172.82  E-value: 7.88e-49
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032733617  766 DYINANYVDGYNKAKA----YIATQGPLKSTFEDFWRMIWEQNTGIIVMITNLVEKGRRKCDQYWP-TENSEEYGNIIVT 840
Cdd:cd14601      1 DYINANYINMEIPSSSiinrYIACQGPLPNTCSDFWQMTWEQGSSMVVMLTTQVERGRVKCHQYWPePSGSSSYGGFQVT 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032733617  841 LKSTNVHACYTVRRFTVRNTKMKKgqkgnpkgrqnERTVIQYHYTQWPDMGVPEYALPVLTFVRRSSAARTPDMGPVVVH 920
Cdd:cd14601     81 CHSEEGNPAYVFREMTLTNLEKNE-----------SRPLTQIQYIAWPDHGVPDDSSDFLDFVCLVRNKRAGKDEPVVVH 149

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 2032733617  921 CSAGVGRTGTYIVIDSMLQQIKDKSTVNVLGFLKHIRTQRNYLVQTEEQYIFIHDALLE 979
Cdd:cd14601    150 CSAGIGRTGVLITMETAMCLIECNQPVYPLDIVRTMRDQRAMMIQTPSQYRFVCEAILK 208
PTP-N23 cd14539
PTP-like domain of tyrosine-protein phosphatase non-receptor type 23; Tyrosine-protein ...
 767-975 1.39e-48

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: 171.80  E-value: 1.39e-48
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032733617  767 YINANYVDGY-NKAKAYIATQGPLKSTFEDFWRMIWEQNTGIIVMITNLVEKGRRKCDQYWPTE--NSEEYGNIIVTLKS 843
Cdd:cd14539      1 YINASLIEDLtPYCPRFIATQAPLPGTAADFWLMVYEQQVSVIVMLVSEQENEKQKVHRYWPTErgQALVYGAITVSLQS 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032733617  844 TNVHACYTVRRFTVRNtkmkKGQKGNpkgrqneRTVIQYHYTQWPDMGVPEYALPVLTFV---------RRSSAArtpdm 914
Cdd:cd14539     81 VRTTPTHVERIISIQH----KDTRLS-------RSVVHLQFTTWPELGLPDSPNPLLRFIeevhshylqQRSLQT----- 144

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2032733617  915 gPVVVHCSAGVGRTGTYIVIDSMLQQIK-DKSTVNVLGFLKHIRTQRNYLVQTEEQYIFIHD 975
Cdd:cd14539    145 -PIVVHCSSGVGRTGAFCLLYAAVQEIEaGNGIPDLPQLVRKMRQQRKYMLQEKEHLKFCYE 205
R-PTP-F-2 cd14629
PTP-like domain of receptor-type tyrosine-protein phosphatase F, repeat 2; Receptor-type ...
 986-1274 1.40e-48

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: 175.30  E-value: 1.40e-48
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032733617  986 TEVSANQLHSYVNSI-LIPGIGGKTRLEKQFKLVTQCNAKYVECFSAQKDCNKEKNRNSSVVPSERARVGLAPLPGMKGT 1064
Cdd:cd14629      2 TEVPARNLYAHIQKLtQVPPGESVTAMELEFKLLANSKAHTSRFISANLPCNKFKNRLVNIMPYELTRVCLQPIRGVEGS 81

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032733617 1065 DYINASYIMGYYRSNEFIITQHPLPHTTKDFWRMIWDHNAQIIVMLPDNQSLAEDE-FVYWPSrEESMNCEAFTVtlisk 1143
Cdd:cd14629     82 DYINASFIDGYRQQKAYIATQGPLAETTEDFWRMLWEHNSTIVVMLTKLREMGREKcHQYWPA-ERSARYQYFVV----- 155

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032733617 1144 DRLCLSNEEQIIIHDFILEATQDDYVLEVRHFQCPKWPNPDAPISST--FELINVI--KEEALTRDGPTIVHDEYGAVSA 1219
Cdd:cd14629    156 DPMAEYNMPQYILREFKVTDARDGQSRTIRQFQFTDWPEQGVPKTGEgfIDFIGQVhkTKEQFGQDGPITVHCSAGVGRT 235

                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 2032733617 1220 GTLCALTTLSQQLENENAVDVFQVAKMINLMRPGVFTDIEQYQFLYKAMLSLVST 1274
Cdd:cd14629    236 GVFITLSIVLERMRYEGVVDMFQTVKTLRTQRPAMVQTEDQYQLCYRAALEYLGS 290
alpha_CA_VI_IX_XII_XIV cd03123
Carbonic anhydrase alpha, isozymes VI, IX, XII and XIV. Carbonic anhydrases (CAs) are ...
 1-204 2.06e-48

Carbonic anhydrase alpha, isozymes VI, IX, XII and XIV. Carbonic anhydrases (CAs) are zinc-containing enzymes that catalyze the reversible hydration of carbon dioxide in a two-step mechanism: a nucleophilic attack of a zinc-bound hydroxide ion on carbon dioxide, followed by the regeneration of the active site by ionization of the zinc-bound water molecule and removal of a proton from the active site. They are ubiquitous enzymes involved in fundamental processes like photosynthesis, respiration, pH homeostasis and ion transport. There are three evolutionary distinct groups - alpha, beta and gamma carbonic anhydrases - which show no significant sequence identity or structural similarity. Alpha CAs are mostly monomeric enzymes. The zinc ion is complexed by three histidine residues. This sub-family comprises the secreted CA VI, which is found in saliva, for example, and the membrane proteins CA IX, XII, and XIV.


Pssm-ID: 239397 [Multi-domain]  Cd Length: 248  Bit Score: 172.88  E-value: 2.06e-48
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032733617    1 MKNTGKTVAILLKDDYFVSGaGLPGRFKAEKVEFHWGQSNGSAGSEHSINGKRFPVEMQIFFYNPDDFDSFGTAVLENRV 80
Cdd:cd03123     51 LTNNGHTVQLSLPPTMHIRG-GPGTEYTAAQLHLHWGGRGSLSGSEHTIDGIRFAAELHIVHYNSDKYSSFDEAADKPDG 129

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032733617   81 VGAMAVFFQVSQRDNSALDPIIHGLKGVVHHEKETFLDPFVLRELLPTSLGSYYRYTGSLTTPPCSEIVEWIVFRKPVPI 160
Cdd:cd03123    130 LAVLAILIEVGYPENTYYEKIISHLHEIKYKGQETTVPGFNVRELLPEDLSHYYRYEGSLTTPPCYESVLWTVFRDPVTL 209

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*
gi 2032733617  161 SYHQLEAFY-SIFTTEQQDhvksveyLRNNFRPQQSLNNRKVSKS 204
Cdd:cd03123    210 SKEQLETLEnTLMDTHNKT-------LQNNYRATQPLNGRVVEAS 247
PHA02738 PHA02738
hypothetical protein; Provisional
 712-977 1.20e-47

hypothetical protein; Provisional


Pssm-ID: 222923 [Multi-domain]  Cd Length: 320  Bit Score: 173.57  E-value: 1.20e-47
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032733617  712 DFEEVqrctadmnITAEH------------SNHPDNKHKNRYINILAYDHSRVKLRplpgKDSKHSDYINANYVDGYNKA 779
Cdd:PHA02738    22 DCEEV--------ITREHqkvisekvdgtfNAEKKNRKLNRYLDAVCFDHSRVILP----AERNRGDYINANYVDGFEYK 89

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032733617  780 KAYIATQGPLKSTFEDFWRMIWEQNTGIIVMITNLVEKGRRKCDQYWPT--ENSEEYGNIIVTLKSTNVHACYTVRRFTV 857
Cdd:PHA02738    90 KKFICGQAPTRQTCYDFYRMLWMEHVQIIVMLCKKKENGREKCFPYWSDveQGSIRFGKFKITTTQVETHPHYVKSTLLL 169

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032733617  858 RNtkmkkgqkgnpkGRQNERTVIQYHYTQWPDMGVPEYALPVLTFV------RRSSAARTPDMG-------PVVVHCSAG 924
Cdd:PHA02738   170 TD------------GTSATQTVTHFNFTAWPDHDVPKNTSEFLNFVlevrqcQKELAQESLQIGhnrlqppPIVVHCNAG 237

                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|...
gi 2032733617  925 VGRTGTYIVIDSMLQQIKDKSTVNVLGFLKHIRTQRNYLVQTEEQYIFIHDAL 977
Cdd:PHA02738   238 LGRTPCYCVVDISISRFDACATVSIPSIVSSIRNQRYYSLFIPFQYFFCYRAV 290
PHA02747 PHA02747
protein tyrosine phosphatase; Provisional
 714-974 6.90e-47

protein tyrosine phosphatase; Provisional


Pssm-ID: 165114 [Multi-domain]  Cd Length: 312  Bit Score: 170.95  E-value: 6.90e-47
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032733617  714 EEVQRCTADMNITAEHSNHPDNKHKNRYINILAYDHSRVKLRplpGKDSKHSDYINANYVDGYNKAKAYIATQGPLKSTF 793
Cdd:PHA02747    30 EHHQIILKPFDGLIANFEKPENQPKNRYWDIPCWDHNRVILD---SGGGSTSDYIHANWIDGFEDDKKFIATQGPFAETC 106

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032733617  794 EDFWRMIWEQNTGIIVMIT-NLVEKGRRKCDQYW-PTENS--EEYGNIIVTLKSTnVHACYTvrRFTVRNTKmkkgqkgn 869
Cdd:PHA02747   107 ADFWKAVWQEHCSIIVMLTpTKGTNGEEKCYQYWcLNEDGniDMEDFRIETLKTS-VRAKYI--LTLIEITD-------- 175

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032733617  870 pKGRQNERTVIQYHYTQWPDMGVPEYALPVLTFVRRSSAARTPDMG----------PVVVHCSAGVGRTGTYIVIDSMLQ 939
Cdd:PHA02747   176 -KILKDSRKISHFQCSEWFEDETPSDHPDFIKFIKIIDINRKKSGKlfnpkdallcPIVVHCSDGVGKTGIFCAVDICLN 254

                          250       260       270
                   ....*....|....*....|....*....|....*
gi 2032733617  940 QIKDKSTVNVLGFLKHIRTQRNYLVQTEEQYIFIH 974
Cdd:PHA02747   255 QLVKRKAICLAKTAEKIREQRHAGIMNFDDYLFIQ 289
PTPc-N20 cd14596
catalytic domain of tyrosine-protein phosphatase non-receptor type 20; Tyrosine-protein ...
 767-981 1.26e-46

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: 166.46  E-value: 1.26e-46
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032733617  767 YINANYVDGYNKAKA--YIATQGPLKSTFEDFWRMIWEQNTGIIVMITNLVEKGRRKCDQYWPTENSE--EYGNIIVTLK 842
Cdd:cd14596      1 YINASYITMPVGEEElfYIATQGPLPSTIDDFWQMVWENRSDVIAMMTREVERGKVKCHRYWPETLQEpmELENYQLRLE 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032733617  843 STNVhacytVRRFTVRNTKMKKGQKGnpkgrqNERTVIQYHYTQWPDMGVPEYALPVLTFVRrsSAARTPDMGPVVVHCS 922
Cdd:cd14596     81 NYQA-----LQYFIIRIIKLVEKETG------ENRLIKHLQFTTWPDHGTPQSSDQLVKFIC--YMRKVHNTGPIVVHCS 147

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 2032733617  923 AGVGRTGTYIVIDSMLQQIKDKSTVNVLGFLKHIRTQRNYLVQTEEQYIFIHDALLEAI 981
Cdd:cd14596    148 AGIGRAGVLICVDVLLSLIEKDLSFNIKDIVREMRQQRYGMIQTKDQYLFCYKVVLEVL 206
PHA02746 PHA02746
protein tyrosine phosphatase; Provisional
 726-982 1.60e-45

protein tyrosine phosphatase; Provisional


Pssm-ID: 165113 [Multi-domain]  Cd Length: 323  Bit Score: 167.51  E-value: 1.60e-45
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032733617  726 TAEHSNHPDNKHKNRYINILAYDHSRVKL-----------------RPLPGKDSKHSDYINANYVDGYNKAKAYIATQGP 788
Cdd:PHA02746    42 TTNHFLKKENLKKNRFHDIPCWDHSRVVInaheslkmfdvgdsdgkKIEVTSEDNAENYIHANFVDGFKEANKFICAQGP 121

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032733617  789 LKSTFEDFWRMIWEQNTGIIVMITNlVEKGRRKCDQYWPTENSEE--YGNIIVTLKSTNVHACYTVRRFTVRNtkmkkgq 866
Cdd:PHA02746   122 KEDTSEDFFKLISEHESQVIVSLTD-IDDDDEKCFELWTKEEDSElaFGRFVAKILDIIEELSFTKTRLMITD------- 193

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032733617  867 kgnpKGRQNERTVIQYHYTQWPDMGVPEYALPVLTFV-----RRSSAARTPD-----MGPVVVHCSAGVGRTGTYIVIDS 936
Cdd:PHA02746   194 ----KISDTSREIHHFWFPDWPDNGIPTGMAEFLELInkvneEQAELIKQADndpqtLGPIVVHCSAGIGRAGTFCAIDN 269

                          250       260       270       280
                   ....*....|....*....|....*....|....*....|....*.
gi 2032733617  937 MLQQIKDKSTVNVLGFLKHIRTQRNYLVQTEEQYIFIHDALLEAIL 982
Cdd:PHA02746   270 ALEQLEKEKEVCLGEIVLKIRKQRHSSVFLPEQYAFCYKALKYAII 315
alpha_CA_XII_XIV cd03126
Carbonic anhydrase alpha, isozymes XII and XIV. Carbonic anhydrases (CAs) are zinc-containing ...
 1-204 5.45e-45

Carbonic anhydrase alpha, isozymes XII and XIV. Carbonic anhydrases (CAs) are zinc-containing enzymes that catalyze the reversible hydration of carbon dioxide in a two-step mechanism: a nucleophilic attack of a zinc-bound hydroxide ion on carbon dioxide, followed by the regeneration of the active site by ionization of the zinc-bound water molecule and removal of a proton from the active site. They are ubiquitous enzymes involved in fundamental processes like photosynthesis, respiration, pH homeostasis and ion transport. There are three evolutionary distinct groups - alpha, beta and gamma carbonic anhydrases - which show no significant sequence identity or structural similarity. Most alpha CAs are monomeric enzymes. The zinc ion is complexed by three histidine residues. This sub-family comprises the membrane proteins CA XII and XIV.


Pssm-ID: 239400  Cd Length: 249  Bit Score: 163.08  E-value: 5.45e-45
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032733617    1 MKNTGKTVAILLKDDYFVSGagLPGRFKAEKVEFHWGQSNGSAGSEHSINGKRFPVEMQIFFYNPDDFDSFGTAVLENRV 80
Cdd:cd03126     51 LTNNGHTVQLSLPPTMHIGG--LPFKYTASQLHLHWGQRGSPEGSEHTISGKHFAAELHIVHYNSDKYPDISTAMNKSQG 128

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032733617   81 VGAMAVFFQVSQRdNSALDPIIHGLKGVVHHEKETFLDPFVLRELLPTSLGSYYRYTGSLTTPPCSEIVEWIVFRKPVPI 160
Cdd:cd03126    129 LAVLGILIEVGPF-NPSYEKIFSHLHEVKYKDQKVSVPGFNVQELLPKRLDEYYRYEGSLTTPPCYPSVLWTVFRNPVQI 207

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*
gi 2032733617  161 SYHQLEAFY-SIFTTEQQDHVKSVeylrNNFRPQQSLNNRKVSKS 204
Cdd:cd03126    208 SQEQLLALEtALYSTEEDESREMV----NNYRQVQPFNERLVFAS 248
R-PTPc-typeIIb-2 cd14556
PTP domain of type IIb (or R2B) subfamily receptor-type tyrosine-protein phosphatases, repeat ...
 1066-1265 8.98e-44

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: 157.95  E-value: 8.98e-44
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032733617 1066 YINASYIMGYYRSNEFIITQHPLPHTTKDFWRMIWDHNAQIIVMLPDNQSLAEDEFVYWPsrEESMNCEA-FTVTLISKD 1144
Cdd:cd14556      1 YINAALLDSYKQPAAFIVTQHPLPNTVTDFWRLVYDYGCTSIVMLNQLDPKDQSCPQYWP--DEGSGTYGpIQVEFVSTT 78

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032733617 1145 RlclsnEEQIIIHDFILEAT---QDDYVLeVRHFQCPKWP-NPDAPIS--STFELIN-VIKEEALTRDGPTIVHDEYGAV 1217
Cdd:cd14556     79 I-----DEDVISRIFRLQNTtrpQEGYRM-VQQFQFLGWPrDRDTPPSkrALLKLLSeVEKWQEQSGEGPIVVHCLNGVG 152

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*...
gi 2032733617 1218 SAGTLCALTTLSQQLENENAVDVFQVAKMINLMRPGVFTDIEQYQFLY 1265
Cdd:cd14556    153 RSGVFCAISSVCERIKVENVVDVFQAVKTLRNHRPNMVETEEQYKFCY 200
COG5599 COG5599
Protein tyrosine phosphatase [Signal transduction mechanisms];
729-973 6.43e-43

Protein tyrosine phosphatase [Signal transduction mechanisms];


Pssm-ID: 444335 [Multi-domain]  Cd Length: 282  Bit Score: 158.33  E-value: 6.43e-43
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032733617  729 HSNHPDNKHKNRYINILAYDHSRVklrplpGKDSKhsdYINANYVDGYNKaKAYIATQGPLKSTFEDFWRMIWEQNTGII 808
Cdd:COG5599     36 YLQNINGSPLNRFRDIQPYKETAL------RANLG---YLNANYIQVIGN-HRYIATQYPLEEQLEDFFQMLFDNNTPVL 105

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032733617  809 VMITNLVE--KGRRKCDQYWPTenSEEYGNIIVTLKSTNVHACYTvrRFTVRNTKMKKGQKGnpkgrQNERTVIQYHYTQ 886
Cdd:COG5599    106 VVLASDDEisKPKVKMPVYFRQ--DGEYGKYEVSSELTESIQLRD--GIEARTYVLTIKGTG-----QKKIEIPVLHVKN 176

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032733617  887 WPDMGVP--EYALPVLTFVRRSSAARTPDMGPVVVHCSAGVGRTGTYIVIDSMLQQIKDKS--TVNVLGFLKHIRTQRNY 962
Cdd:COG5599    177 WPDHGAIsaEALKNLADLIDKKEKIKDPDKLLPVVHCRAGVGRTGTLIACLALSKSINALVqiTLSVEEIVIDMRTSRNG 256

                          250
                   ....*....|..
gi 2032733617  963 -LVQTEEQYIFI 973
Cdd:COG5599    257 gMVQTSEQLDVL 268
R3-PTPc cd14548
catalytic domain of R3 subfamily receptor-type tyrosine-protein phosphatases and similar ...
 1041-1266 1.25e-42

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: 155.59  E-value: 1.25e-42
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032733617 1041 RNSSVVPSERARVGLAPLPGMKGTDYINASYIMGYYRSNEFIITQHPLPHTTKDFWRMIWDHNAQIIVMLP---DNQSLA 1117
Cdd:cd14548      1 RYTNILPYDHSRVKLIPINEEEGSDYINANYIPGYNSPREFIATQGPLPGTKDDFWRMVWEQNSHTIVMLTqcmEKGRVK 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032733617 1118 EDEfvYWPSREESMNCEAFTVTLISKDRLclsneEQIIIHDFILEatQDDYVLEVRHFQCPKWPN---PDAPISstfeLI 1194
Cdd:cd14548     81 CDH--YWPFDQDPVYYGDITVTMLSESVL-----PDWTIREFKLE--RGDEVRSVRQFHFTAWPDhgvPEAPDS----LL 147

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2032733617 1195 NVIKeeaLTRD------GPTIVHDEYGAVSAGTLCALTTLSQQLENENAVDVFQVAKMINLMRPGVFTDIEQYQFLYK 1266
Cdd:cd14548    148 RFVR---LVRDyikqekGPTIVHCSAGVGRTGTFIALDRLLQQIESEDYVDIFGIVYDLRKHRPLMVQTEAQYIFLHQ 222
PTPc-N21 cd14598
catalytic domain of tyrosine-protein phosphatase non-receptor type 21; Tyrosine-protein ...
 767-979 2.94e-42

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: 154.36  E-value: 2.94e-42
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032733617  767 YINANY--VDGYNKAKAYIATQGPLKSTFEDFWRMIWEQNTGIIVMITNLVEKGRRKCDQYWP----TENSEEYGNIIVT 840
Cdd:cd14598      1 YINASHikVTVGGKEWDYIATQGPLQNTCQDFWQMVWEQGVAIIAMVTAEEEGGREKSFRYWPrlgsRHNTVTYGRFKIT 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032733617  841 LKSTNVHACYTVRRFTVRNtkMKKGQkgnpkgrqnERTVIQYHYTQWPDMGVPEYALPVLTF------VRR----SSAAR 910
Cdd:cd14598     81 TRFRTDSGCYATTGLKIKH--LLTGQ---------ERTVWHLQYTDWPEHGCPEDLKGFLSYleeiqsVRRhtnsTIDPK 149

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2032733617  911 TPDMgPVVVHCSAGVGRTGTYIVIDSMLQQIKDKSTVNVLGFLKHIRTQRNYLVQTEEQYIFIHDALLE 979
Cdd:cd14598    150 SPNP-PVLVHCSAGVGRTGVVILSEIMIACLEHNEMLDIPRVLDMLRQQRMMMVQTLSQYTFVYKVLIQ 217
R-PTPc-A-E-2 cd14552
catalytic domain of receptor-type tyrosine-protein phosphatase A and E, repeat 2; ...
 1066-1268 4.96e-42

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: 153.19  E-value: 4.96e-42
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032733617 1066 YINASYIMGYYRSNEFIITQHPLPHTTKDFWRMIWDHNAQIIVMLPDNQSLAEDE-FVYWPSrEESMNCEAFTVTLiSKD 1144
Cdd:cd14552      1 YINASFIDGYRQKDAYIATQGPLDHTVEDFWRMIWEWKSCSIVMLTEIKERSQNKcAQYWPE-DGSVSSGDITVEL-KDQ 78

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032733617 1145 RLClsneEQIIIHDFILEATQDDYVLEVRHFQCPKWPNPDAPiSSTFELINVI----KEEALTRDGPTIVHDEYGAVSAG 1220
Cdd:cd14552     79 TDY----EDYTLRDFLVTKGKGGSTRTVRQFHFHGWPEVGIP-DNGKGMIDLIaavqKQQQQSGNHPITVHCSAGAGRTG 153

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*...
gi 2032733617 1221 TLCALTTLSQQLENENAVDVFQVAKMINLMRPGVFTDIEQYQFLYKAM 1268
Cdd:cd14552    154 TFCALSTVLERVKAEGVLDVFQVVKSLRLQRPHMVQTLEQYEFCYKVV 201
R-PTPc-typeIIb-2 cd14556
PTP domain of type IIb (or R2B) subfamily receptor-type tyrosine-protein phosphatases, repeat ...
 767-975 7.07e-42

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: 152.56  E-value: 7.07e-42
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032733617  767 YINANYVDGYNKAKAYIATQGPLKSTFEDFWRMIWEQNTGIIVMItNLVEKGRRKCDQYWPTENSEEYGNIIVTLKSTNV 846
Cdd:cd14556      1 YINAALLDSYKQPAAFIVTQHPLPNTVTDFWRLVYDYGCTSIVML-NQLDPKDQSCPQYWPDEGSGTYGPIQVEFVSTTI 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032733617  847 HACYTVRRFTVRNTKmkkgqkgnpkgRQNE--RTVIQYHYTQWPDMG----VPEYALPVLTFVRRSSAARtpDMGPVVVH 920
Cdd:cd14556     80 DEDVISRIFRLQNTT-----------RPQEgyRMVQQFQFLGWPRDRdtppSKRALLKLLSEVEKWQEQS--GEGPIVVH 146

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 2032733617  921 CSAGVGRTGTYIVIDSMLQQIKDKSTVNVLGFLKHIRTQRNYLVQTEEQYIFIHD 975
Cdd:cd14556    147 CLNGVGRSGVFCAISSVCERIKVENVVDVFQAVKTLRNHRPNMVETEEQYKFCYD 201
PHA02742 PHA02742
protein tyrosine phosphatase; Provisional
 735-979 1.04e-40

protein tyrosine phosphatase; Provisional


Pssm-ID: 165109 [Multi-domain]  Cd Length: 303  Bit Score: 152.85  E-value: 1.04e-40
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032733617  735 NKHKNRYINILAYDHSRVKLRPLPGKDskhsDYINANYVDGYNKAKAYIATQGPLKSTFEDFWRMIWEQNTGIIVMITNL 814
Cdd:PHA02742    52 NMKKCRYPDAPCFDRNRVILKIEDGGD----DFINASYVDGHNAKGRFICTQAPLEETALDFWQAIFQDQVRVIVMITKI 127

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032733617  815 VEKGRRKCDQYWPTENseeygniivtlKSTNVHACYTVRRFTV---RNTKMKKGQKGNPkgrqNERTVI---QYHYTQWP 888
Cdd:PHA02742   128 MEDGKEACYPYWMPHE-----------RGKATHGEFKIKTKKIksfRNYAVTNLCLTDT----NTGASLdikHFAYEDWP 192

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032733617  889 DMGVPEYALPVLTFV----RRSSAARTPDMG-------PVVVHCSAGVGRTGTYIVIDSMLQQIKDKSTVNVLGFLKHIR 957
Cdd:PHA02742   193 HGGLPRDPNKFLDFVlavrEADLKADVDIKGenivkepPILVHCSAGLDRAGAFCAIDICISKYNERAIIPLLSIVRDLR 272

                          250       260
                   ....*....|....*....|..
gi 2032733617  958 TQRNYLVQTEEQYIFIHDALLE 979
Cdd:PHA02742   273 KQRHNCLSLPQQYIFCYFIVLI 294
R-PTPc-E-2 cd14622
catalytic domain of receptor-type tyrosine-protein phosphatase E, repeat 2; Receptor-type ...
 1065-1268 5.27e-40

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: 147.46  E-value: 5.27e-40
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032733617 1065 DYINASYIMGYYRSNEFIITQHPLPHTTKDFWRMIWDHNAQIIVMLPDNQSLAEDE-FVYWPSrEESMNCEAFTVTlISK 1143
Cdd:cd14622      1 DYINASFIDGYRQKDYFIATQGPLAHTVEDFWRMVWEWKCHTIVMLTELQEREQEKcVQYWPS-EGSVTHGEITIE-IKN 78

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032733617 1144 DRLClsneEQIIIHDFILEATQDDYVLEVRHFQCPKWPNPDAPiSSTFELINVI----KEEALTRDGPTIVHDEYGAVSA 1219
Cdd:cd14622     79 DTLL----ETISIRDFLVTYNQEKQTRLVRQFHFHGWPEIGIP-AEGKGMIDLIaavqKQQQQTGNHPIVVHCSAGAGRT 153

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*....
gi 2032733617 1220 GTLCALTTLSQQLENENAVDVFQVAKMINLMRPGVFTDIEQYQFLYKAM 1268
Cdd:cd14622    154 GTFIALSNILERVKAEGLLDVFQTVKSLRLQRPHMVQTLEQYEFCYRVV 202
R-PTPc-H cd14619
catalytic domain of receptor-type tyrosine-protein phosphatase H; Receptor-type ...
 1040-1272 5.70e-40

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: 148.11  E-value: 5.70e-40
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032733617 1040 NRNSSVVPSERARVGLAPLPGMKGTDYINASYIMGYYRSNEFIITQHPLPHTTKDFWRMIWDHNAQIIVMLPDnqsLAED 1119
Cdd:cd14619      1 NRFRNVLPYDWSRVPLKPIHEEPGSDYINANYMPGYWSSQEFIATQGPLPQTVGDFWRMIWEQQSSTIVMLTN---CMEA 77

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032733617 1120 EFV----YWPSREESMNCEAFTVTLISKDRLclsneEQIIIHDFILEATQDDYVLEVRHFQCPKWPNPDAPiSSTFELI- 1194
Cdd:cd14619     78 GRVkcehYWPLDYTPCTYGHLRVTVVSEEVM-----ENWTVREFLLKQVEEQKTLSVRHFHFTAWPDHGVP-SSTDTLLa 151

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032733617 1195 --NVIKE--EALTRDGPTIVHDEYGAVSAGTLCALTTLSQQLENENAVDVFQVAKMINLMRPGVFTDIEQYQFLYKAMLS 1270
Cdd:cd14619    152 frRLLRQwlDQTMSGGPTVVHCSAGVGRTGTLIALDVLLQQLQSEGLLGPFSFVQKMRENRPLMVQTESQYVFLHQCILD 231


                   ..
gi 2032733617 1271 LV 1272
Cdd:cd14619    232 FL 233
R-PTP-C-2 cd14558
PTP-like domain of receptor-type tyrosine-protein phosphatase C, repeat 2; Receptor-type ...
 1066-1265 1.07e-39

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: 146.38  E-value: 1.07e-39
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032733617 1066 YINASYIMGYYRSNEFIITQHPLPHTTKDFWRMIWDHNAQIIVMLPD-NQSLAEDEFVYWPsrEESMNCEAFTVTLISKD 1144
Cdd:cd14558      1 YINASFIDGYWGPKSLIATQGPLPDTIADFWQMIFQKKVKVIVMLTElKEGDQEQCAQYWG--DEKKTYGDIEVELKDTE 78

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032733617 1145 rlclsNEEQIIIHDFILEATQDDYVLEVRHFQCPKWPNPDAPiSSTFELINVIKE---------EALTRDGPTIVHDEYG 1215
Cdd:cd14558     79 -----KSPTYTVRVFEITHLKRKDSRTVYQYQYHKWKGEELP-EKPKDLVDMIKSikqklpyknSKHGRSVPIVVHCSDG 152

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|
gi 2032733617 1216 AVSAGTLCALTTLSQQLENENAVDVFQVAKMINLMRPGVFTDIEQYQFLY 1265
Cdd:cd14558    153 SSRTGIFCALWNLLESAETEKVVDVFQVVKALRKQRPGMVSTLEQYQFLY 202
R-PTPc-J cd14615
catalytic domain of receptor-type tyrosine-protein phosphatase J; Receptor-type ...
 1040-1269 1.56e-39

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: 146.89  E-value: 1.56e-39
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032733617 1040 NRNSSVVPSERARVGLApLPGMKGTDYINASYIMGYYRSNEFIITQHPLPHTTKDFWRMIWDHNAQIIVMLPDNQSLAE- 1118
Cdd:cd14615      1 NRYNNVLPYDISRVKLS-VQSHSTDDYINANYMPGYNSKKEFIAAQGPLPNTVKDFWRMVWEKNVYAIVMLTKCVEQGRt 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032733617 1119 --DEfvYWPSrEESMNCEAFTVTLISKDRLclsneEQIIIHDFILEATQDDYVLEVRHFQCPKWPNPDAPiSSTFELIN- 1195
Cdd:cd14615     80 kcEE--YWPS-KQKKDYGDITVTMTSEIVL-----PEWTIRDFTVKNAQTNESRTVRHFHFTSWPDHGVP-ETTDLLINf 150

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2032733617 1196 --VIKE--EALTRDGPTIVHDEYGAVSAGTLCALTTLSQQLENENAVDVFQVAKMINLMRPGVFTDIEQYQFLYKAML 1269
Cdd:cd14615    151 rhLVREymKQNPPNSPILVHCSAGVGRTGTFIAIDRLIYQIENENVVDVYGIVYDLRMHRPLMVQTEDQYVFLNQCAL 228
PTPc_motif smart00404
Protein tyrosine phosphatase, catalytic domain motif;
878-979 3.35e-39

Protein tyrosine phosphatase, catalytic domain motif;


Pssm-ID: 214649 [Multi-domain]  Cd Length: 105  Bit Score: 140.96  E-value: 3.35e-39
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032733617   878 TVIQYHYTQWPDMGVPEYALPVLTFVR--RSSAARTPDMGPVVVHCSAGVGRTGTYIVIDSMLQQIKDKS-TVNVLGFLK 954
Cdd:smart00404    1 TVKHYHYTGWPDHGVPESPDSILELLRavKKNLNQSESSGPVVVHCSAGVGRTGTFVAIDILLQQLEAEAgEVDIFDTVK 80

                            90       100
                    ....*....|....*....|....*
gi 2032733617   955 HIRTQRNYLVQTEEQYIFIHDALLE 979
Cdd:smart00404   81 ELRSQRPGMVQTEEQYLFLYRALLE 105
PTPc_DSPc smart00012
Protein tyrosine phosphatase, catalytic domain, undefined specificity; Protein tyrosine ...
 878-979 3.35e-39

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: 140.96  E-value: 3.35e-39
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032733617   878 TVIQYHYTQWPDMGVPEYALPVLTFVR--RSSAARTPDMGPVVVHCSAGVGRTGTYIVIDSMLQQIKDKS-TVNVLGFLK 954
Cdd:smart00012    1 TVKHYHYTGWPDHGVPESPDSILELLRavKKNLNQSESSGPVVVHCSAGVGRTGTFVAIDILLQQLEAEAgEVDIFDTVK 80

                            90       100
                    ....*....|....*....|....*
gi 2032733617   955 HIRTQRNYLVQTEEQYIFIHDALLE 979
Cdd:smart00012   81 ELRSQRPGMVQTEEQYLFLYRALLE 105
R-PTPc-LAR-1 cd14553
catalytic domain of LAR family receptor-type tyrosine-protein phosphatases, repeat 1; The LAR ...
 1034-1273 8.78e-39

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: 144.85  E-value: 8.78e-39
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032733617 1034 DCNKEKNRNSSVVPSERARVGLAPLPGMKGTDYINASYIMGYYRSNEFIITQHPLPHTTKDFWRMIWDHNAQIIVMLpdn 1113
Cdd:cd14553      1 EVNKPKNRYANVIAYDHSRVILQPIEGVPGSDYINANYCDGYRKQNAYIATQGPLPETFGDFWRMVWEQRSATIVMM--- 77

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032733617 1114 QSLAEDEFV----YWPSReESMNCEAFTVTLIskDRLCLSNeeqIIIHDFILEATQDDYVLEVRHFQCPKWPN---PDAP 1186
Cdd:cd14553     78 TKLEERSRVkcdqYWPTR-GTETYGLIQVTLL--DTVELAT---YTVRTFALHKNGSSEKREVRQFQFTAWPDhgvPEHP 151

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032733617 1187 iSSTFELINVIKEEALTRDGPTIVHDEYGAVSAGTLCALTTLSQQLENENAVDVF-QVAKM---INLMrpgVFTDiEQYQ 1262
Cdd:cd14553    152 -TPFLAFLRRVKACNPPDAGPIVVHCSAGVGRTGCFIVIDSMLERIKHEKTVDIYgHVTCLraqRNYM---VQTE-DQYI 226

                          250
                   ....*....|.
gi 2032733617 1263 FLYKAMLSLVS 1273
Cdd:cd14553    227 FIHDALLEAVT 237
R-PTPc-A-2 cd14623
catalytic domain of receptor-type tyrosine-protein phosphatase A, repeat 2; Receptor-type ...
 1045-1268 9.03e-39

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: 144.80  E-value: 9.03e-39
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032733617 1045 VVPSERARVGLAPLPGMKGTDYINASYIMGYYRSNEFIITQHPLPHTTKDFWRMIWDHNAQIIVMLPDNQSLAEDEFV-Y 1123
Cdd:cd14623      5 IIPYEFNRVIIPVKRGEENTDYVNASFIDGYRQKDSYIASQGPLQHTIEDFWRMIWEWKSCSIVMLTELEERGQEKCAqY 84

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032733617 1124 WPSrEESMNCEAFTVTLiSKDRLClsneEQIIIHDFILEATQDDYVLEVRHFQCPKWPNPDAPiSSTFELINVI----KE 1199
Cdd:cd14623     85 WPS-DGSVSYGDITIEL-KKEEEC----ESYTVRDLLVTNTRENKSRQIRQFHFHGWPEVGIP-SDGKGMINIIaavqKQ 157

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2032733617 1200 EALTRDGPTIVHDEYGAVSAGTLCALTTLSQQLENENAVDVFQVAKMINLMRPGVFTDIEQYQFLYKAM 1268
Cdd:cd14623    158 QQQSGNHPITVHCSAGAGRTGTFCALSTVLERVKAEGILDVFQTVKSLRLQRPHMVQTLEQYEFCYKVV 226
R-PTPc-V cd14618
catalytic domain of receptor-type tyrosine-protein phosphatase V; Receptor-type ...
 1040-1269 2.90e-38

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: 143.16  E-value: 2.90e-38
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032733617 1040 NRNSSVVPSERARVGLAPLPGMKGTDYINASYIMGYYRSNEFIITQHPLPHTTKDFWRMIWDHNAQIIVMLP---DNQSL 1116
Cdd:cd14618      1 NRYPHVLPYDHSRVRLSQLGGEPHSDYINANFIPGYTSPQEFIATQGPLKKTIEDFWRLVWEQQVCNIIMLTvgmENGRV 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032733617 1117 AEDEfvYWPSREESMNCEAFTVTLISKdrlclSNEEQIIIHDFILEATQDDYVLEVRHFQCPKWPN---PDAPiSSTFEL 1193
Cdd:cd14618     81 LCDH--YWPSESTPVSYGHITVHLLAQ-----SSEDEWTRREFKLWHEDLRKERRVKHLHYTAWPDhgiPEST-SSLMAF 152

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2032733617 1194 INVIKEE--ALTRDGPTIVHDEYGAVSAGTLCALTTLSQQLENENAVDVFQVAKMINLMRPGVFTDIEQYQFLYKAML 1269
Cdd:cd14618    153 RELVREHvqATKGKGPTLVHCSAGVGRSGTFIALDRLLRQLKEEKVVDVFNTVYILRMHRYLMIQTLSQYIFLHSCIL 230
PTPc-N18 cd14603
catalytic domain of tyrosine-protein phosphatase non-receptor type 18; Tyrosine-protein ...
 1013-1268 3.02e-37

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: 141.50  E-value: 3.02e-37
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032733617 1013 KQFKLVTQCNAKYVE--CFSAQKDCNKE---KNRNSSVVPSERARVGLAPLPGMKGTDYINASYIMGYYRSNEFIITQHP 1087
Cdd:cd14603      2 GEFSEIRACSAAFKAdyVCSTVAGGRKEnvkKNRYKDILPYDQTRVILSLLQEEGHSDYINANFIKGVDGSRAYIATQGP 81

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032733617 1088 LPHTTKDFWRMIWDHNAQIIVMLPDNQSLAEDEF-VYWPSREESMNCEAFTVTLISKDRLclsNEEQIIihdFILEATQD 1166
Cdd:cd14603     82 LSHTVLDFWRMIWQYGVKVILMACREIEMGKKKCeRYWAQEQEPLQTGPFTITLVKEKRL---NEEVIL---RTLKVTFQ 155

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032733617 1167 DYVLEVRHFQCPKWPN---PDAPiSSTFELINVIKEEALTRDGPTIVHDEYGAVSAGTLCALTTLSQQLENENAVDVFQV 1243
Cdd:cd14603    156 KESRSVSHFQYMAWPDhgiPDSP-DCMLAMIELARRLQGSGPEPLCVHCSAGCGRTGVICTVDYVRQLLLTQRIPPDFSI 234

                          250       260
                   ....*....|....*....|....*...
gi 2032733617 1244 AKMINLM---RPGVFTDIEQYQFLYKAM 1268
Cdd:cd14603    235 FDVVLEMrkqRPAAVQTEEQYEFLYHTV 262
alpha_CA_prokaryotic_like cd03124
Carbonic anhydrase alpha, prokaryotic-like subfamily. Carbonic anhydrases (CAs) are ...
 1-201 1.53e-36

Carbonic anhydrase alpha, prokaryotic-like subfamily. Carbonic anhydrases (CAs) are zinc-containing enzymes that catalyze the reversible hydration of carbon dioxide in a two-step mechanism: a nucleophilic attack of a zinc-bound hydroxide ion on carbon dioxide, followed by the regeneration of the active site by ionization of the zinc-bound water molecule and removal of a proton from the active site. They are ubiquitous enzymes involved in fundamental processes like photosynthesis, respiration, pH homeostasis and ion transport. Most alpha CAs are monomeric enzymes. The zinc ion is complexed by three histidines. This sub-family includes bacterial carbonic anhydrase alpha, as well as plant enzymes such as tobacco nectarin III and yam dioscorin and, carbonic anhydrases from molluscs, such as nacrein, which are part of the organic matrix layer in shells. Other members of this family may be involved in maintaining pH balance, in facilitating transport of carbon dioxide or carbonic acid, or in sensing carbon dioxide levels in the environment. Dioscorin is the major storage protein of yam tubers and may play a role as an antioxidant. Tobacco Nectarin may play a role in the maintenace of pH and oxidative balance in nectar. Mollusc nacrein may participate in calcium carbonate crystal formation of the nacreous layer. This subfamily also includes three alpha carbonic anhydrases from Chlamydomonas reinhardtii (CAH 1-3). CAHs1-2 are localized in the periplasmic space. CAH1 faciliates the movement of carbon dioxide across the plasma membrane when the medium is alkaline. CAH3 is localized to the thylakoid lumen and provides CO2 to Rubisco.


Pssm-ID: 239398 [Multi-domain]  Cd Length: 216  Bit Score: 137.79  E-value: 1.53e-36
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032733617    1 MKNTGKTVAILLKDDyfVSGAGLPGR-FKAEKVEFHwgqsngsAGSEHSINGKRFPVEMQIFFYNPDDfdsfGTAVLenr 79
Cdd:cd03124     50 LVNNGHTIQVNFEGN--GGTLTIDGEtYQLLQFHFH-------SPSEHLINGKRYPLEAHLVHKSKDG----QLAVV--- 113

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032733617   80 vvgamAVFFQVSqRDNSALDPIIHGLKGVVhhEKETFLDPFV-LRELLPTSLgSYYRYTGSLTTPPCSEIVEWIVFRKPV 158
Cdd:cd03124    114 -----AVLFEEG-KENPFLKKILDNMPKKE--GTEVNLPAILdPNELLPESR-SYYRYEGSLTTPPCSEGVRWIVLKQPI 184

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|...
gi 2032733617  159 PISYHQLEAFysiftteqqdhvKSVEYLRNNfRPQQSLNNRKV 201
Cdd:cd03124    185 TISKEQLAKF------------RAAVYPNNA-RPVQPLNGREV 214
PTPc-N9 cd14543
catalytic domain of tyrosine-protein phosphatase non-receptor type 9; Tyrosine-protein ...
 1030-1266 2.41e-36

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: 139.04  E-value: 2.41e-36
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032733617 1030 SAQKDCNKEKNRNSSVVPSERARVGLAPLPGMKGTDYINASYIMGYYRSNEFIITQHPLPHTTKDFWRMIWDHNAQIIVM 1109
Cdd:cd14543     23 CSLAPANQEKNRYGDVLCLDQSRVKLPKRNGDERTDYINANFMDGYKQKNAYIATQGPLPKTYSDFWRMVWEQKVLVIVM 102

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032733617 1110 LpdnQSLAEDEFV----YWPSREES-MNCEAFTVTLISKDrlclsNEEQIIIHDFILEATQDDYVLEVRHFQCPKWPNPD 1184
Cdd:cd14543    103 T---TRVVERGRVkcgqYWPLEEGSsLRYGDLTVTNLSVE-----NKEHYKKTTLEIHNTETDESRQVTHFQFTSWPDFG 174

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032733617 1185 APiSSTFELIN----VIKEEAL------------TRDGPTIVHDEYGAVSAGTLCALTTLSQQLENENAVDVFQVAKMIN 1248
Cdd:cd14543    175 VP-SSAAALLDflgeVRQQQALavkamgdrwkghPPGPPIVVHCSAGIGRTGTFCTLDICLSQLEDVGTLNVMQTVRRMR 253

                          250
                   ....*....|....*...
gi 2032733617 1249 LMRPGVFTDIEQYQFLYK 1266
Cdd:cd14543    254 TQRAFSIQTPDQYYFCYK 271
alpha_CARP_X_XI_like cd03121
Carbonic anhydrase alpha related protein: groups X, XI and related proteins. This subgroup ...
 1-201 4.96e-36

Carbonic anhydrase alpha related protein: groups X, XI and related proteins. This subgroup contains carbonic anhydrase related proteins (CARPs) X and XI, which have been implicated in various biological processes of the central nervous system. CARPs are sequence similar to carbonic anhydrases. Carbonic anhydrases are zinc-containing enzymes that catalyze the reversible hydration of carbon dioxide in a two-step mechanism. CARPs have lost conserved histidines involved in zinc binding and consequently their catalytic activity. CARP XI plays a role in the development of gastrointestinal stromal tumors.


Pssm-ID: 239395 [Multi-domain]  Cd Length: 256  Bit Score: 137.54  E-value: 4.96e-36
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032733617    1 MKNTGKTVAILLKDDYFV--SGAGLPGRFKAEKVEFHWGQSNGsAGSEHSINGKRFPVEMQIFFYNPDDFDSFGTAVLEN 78
Cdd:cd03121     52 FYNTGRHVSFRPDKDPVVniSGGPLSYRYRLEEIRLHFGREDE-QGSEHTVNGQAFPGEVQLIHYNSELYPNFSEASKSP 130

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032733617   79 RVVGAMAVFFQVSQRDNSALDPIIHGLKG--VVHHEKETFLDPFVLRELLPTSlGSYYRYTGSLTTPPCSEIVEWIVFRK 156
Cdd:cd03121    131 NGLVIVSLFVKIGETSNPELRRLTNRDTItsIRYKGDAYFLQDLSIELLLPET-DHYITYEGSLTSPGCHETVTWIILNK 209

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*
gi 2032733617  157 PVPISYHQLEAFYSIfTTEQQDHVKSveYLRNNFRPQQSLNNRKV 201
Cdd:cd03121    210 PIYITKEQMHSLRLL-SQNSPSQEKA--PMSPNFRPVQPLNNRPV 251
R-PTPc-O cd14614
catalytic domain of receptor-type tyrosine-protein phosphatase O; Receptor-type ...
 1029-1269 1.20e-35

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: 136.17  E-value: 1.20e-35
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032733617 1029 FSAQKDCNKEKNRNSSVVPSERARVGLAPLPGMKGTDYINASYIMGYYRSNEFIITQHPLPHTTKDFWRMIWDHNAQIIV 1108
Cdd:cd14614      5 FAADLPVNRCKNRYTNILPYDFSRVKLVSMHEEEGSDYINANYIPGYNSPQEYIATQGPLPETRNDFWKMVLQQKSQIIV 84

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032733617 1109 MLP---DNQSLAEDEfvYWPSREESMNCEAFTVTLISKdrlclSNEEQIIIHDFILeaTQDDYVLEVRHFQCPKWPNPDA 1185
Cdd:cd14614     85 MLTqcnEKRRVKCDH--YWPFTEEPVAYGDITVEMLSE-----EEQPDWAIREFRV--SYADEVQDVMHFNYTAWPDHGV 155

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032733617 1186 P----ISSTFELINVIKEEALTRDGPTIVHDEYGAVSAGTLCALTTLSQQLENENAVDVFQVAKMINLMRPGVFTDIEQY 1261
Cdd:cd14614    156 PtanaAESILQFVQMVRQQAVKSKGPMIIHCSAGVGRTGTFIALDRLLQHIRDHEFVDILGLVSEMRSYRMSMVQTEEQY 235


                   ....*...
gi 2032733617 1262 QFLYKAML 1269
Cdd:cd14614    236 IFIHQCVQ 243
alpha_CA_V cd03118
Carbonic anhydrase alpha, CA isozyme V_like subgroup. Carbonic anhydrases (CAs) are ...
 14-204 2.03e-35

Carbonic anhydrase alpha, CA isozyme V_like subgroup. Carbonic anhydrases (CAs) are zinc-containing enzymes that catalyze the reversible hydration of carbon dioxide in a two-step mechanism: a nucleophilic attack of a zinc-bound hydroxide ion on carbon dioxide, followed by the regeneration of the active site by ionization of the zinc-bound water molecule and removal of a proton from the active site. They are ubiquitous enzymes involved in fundamental processes like photosynthesis, respiration, pH homeostasis and ion transport. Most alpha CAs are monomeric enzymes. The zinc ion is complexed by three histidines. This vertebrate subgroup comprises isozyme V. CA V is the mitochondrial isozyme, which may play a role in gluconeogenesis and ureagenesis and possibly also in lipogenesis.


Pssm-ID: 239392  Cd Length: 236  Bit Score: 135.36  E-value: 2.03e-35
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032733617   14 DDYFVSGAGLPGRFKAEKVEFHWGQSNgSAGSEHSINGKRFPVEMQIFFYNPDDFDSFGTAVLENRVVGAMAVFFQVSQR 93
Cdd:cd03118     51 DKSGISGGPLENHYRLKQFHFHWGANN-EWGSEHTVDGHTYPAELHLVHWNSVKYENFEEAVMEENGLAVIGVFLKLGAH 129

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032733617   94 dNSALDPIIHGLKGVVHHEKETFLDPFVLRELLPTSLgSYYRYTGSLTTPPCSEIVEWIVFRKPVPISYHQLEAFYSIFT 173
Cdd:cd03118    130 -HEGLQKLVDALPEVRHKDTVVEFNPFDPSCLLPACR-DYWTYPGSLTTPPLTESVTWIIQKQPIEVSPSQLSVFRTLLF 207

                          170       180       190
                   ....*....|....*....|....*....|.
gi 2032733617  174 TEQQDHVKsveYLRNNFRPQQSLNNRKVSKS 204
Cdd:cd03118    208 TSRGEEEK---VMVNNFRPLQPLMNRKVRSS 235
alpha_CA_VII cd03149
Carbonic anhydrase alpha, CA isozyme VII_like subgroup. Carbonic anhydrases (CAs) are ...
 1-204 8.14e-35

Carbonic anhydrase alpha, CA isozyme VII_like subgroup. Carbonic anhydrases (CAs) are zinc-containing enzymes that catalyze the reversible hydration of carbon dioxide in a two-step mechanism: a nucleophilic attack of a zinc-bound hydroxide ion on carbon dioxide, followed by the regeneration of the active site by ionization of the zinc-bound water molecule and removal of a proton from the active site. They are ubiquitous enzymes involved in fundamental processes like photosynthesis, respiration, pH homeostasis and ion transport. Most alpha CAs are monomeric enzymes. The zinc ion is complexed by three histidines. This vertebrate subgroup comprises isozyme VII. CA VII is the most active cytosolic enzyme after CA II, and may be highly expressed in the brain. Human CA VII may be a target of antiepileptic sulfonamides/sulfamates.


Pssm-ID: 239402  Cd Length: 236  Bit Score: 133.42  E-value: 8.14e-35
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032733617    1 MKNTGKTVAILLkDDY----FVSGAGLPGRFKAEKVEFHWGQSNGSaGSEHSINGKRFPVEMQIFFYNPDDFDSFGTAVL 76
Cdd:cd03149     35 ISNNGHSVMVEF-DDSddktVITGGPLENPYRLKQFHFHWGAKHGS-GSEHTVDGKTFPSELHLVHWNAKKYKSFGEAAA 112

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032733617   77 ENRVVGAMAVFFQVSQrDNSALDPIIHGLKGVVHHEKETFLDPFVLRELLPTSLgSYYRYTGSLTTPPCSEIVEWIVFRK 156
Cdd:cd03149    113 APDGLAVLGVFLETGD-EHPGLNRLTDALYMVRFKGTKAQFLDFNPKCLLPKSL-DYWTYPGSLTTPPLNESVTWIVLKE 190

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*....
gi 2032733617  157 PVPISYHQLEAFYS-IFTTEQQDHVKSVeylrNNFRPQQSLNNRKVSKS 204
Cdd:cd03149    191 PIPVSEKQMGKFRElLFTSEEDQRNHMV----NNFRPPQPLKGRTVRAS 235
Cah COG3338
Carbonic anhydrase [Inorganic ion transport and metabolism];
1-204 5.79e-34

Carbonic anhydrase [Inorganic ion transport and metabolism];


Pssm-ID: 442567 [Multi-domain]  Cd Length: 247  Bit Score: 131.16  E-value: 5.79e-34
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032733617    1 MKNTGKTVAILLKDDYFVSGAGLpgRFKAEKVEFHwgqsngsAGSEHSINGKRFPVEMQIFFYNPDDfdsfGTAVLenrv 80
Cdd:COG3338     82 IVNNGHTIQVNVDPGSTLTVDGK--RYELKQFHFH-------TPSEHTINGKSYPMEAHLVHKDADG----ELAVV---- 144

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032733617   81 vgamAVFFQVSQRdNSALDPIIHGL---KGvvhhEKETFLDPFVLRELLPTSLgSYYRYTGSLTTPPCSEIVEWIVFRKP 157
Cdd:COG3338    145 ----GVLFEEGAE-NPALAKLWANLpleAG----EEVALDATIDLNDLLPEDR-SYYRYSGSLTTPPCSEGVLWIVLKQP 214

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*..
gi 2032733617  158 VPISYHQLEAFYSIFtteqqdhvksveylRNNFRPQQSLNNRKVSKS 204
Cdd:COG3338    215 ITVSAEQIEAFARLY--------------PNNARPVQPLNGRLILES 247
R-PTPc-M-1 cd14633
catalytic domain of receptor-type tyrosine-protein phosphatase M, repeat 1; Receptor-type ...
 1030-1269 2.30e-33

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: 130.55  E-value: 2.30e-33
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032733617 1030 SAQKDCNKEKNRNSSVVPSERARVGLAPLPGMKGTDYINASYIMGYYRSNEFIITQHPLPHTTKDFWRMIWDHNAQIIVM 1109
Cdd:cd14633     34 SAKKDENRMKNRYGNIIAYDHSRVRLQPIEGETSSDYINGNYIDGYHRPNHYIATQGPMQETIYDFWRMVWHENTASIIM 113

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032733617 1110 LPDNQSLAEDEFV-YWPSREESMncEAFTVTLISKDRLclsneEQIIIHDFILEATQDDYVLEVRHFQCPKWPNPDAPIS 1188
Cdd:cd14633    114 VTNLVEVGRVKCCkYWPDDTEIY--KDIKVTLIETELL-----AEYVIRTFAVEKRGVHEIREIRQFHFTGWPDHGVPYH 186

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032733617 1189 ST--FELINVIKEEALTRDGPTIVHDEYGAVSAGTLCALTTLSQQLENENAVDVFQVAKMINLMRPGVFTDIEQYQFLYK 1266
Cdd:cd14633    187 ATglLGFVRQVKSKSPPNAGPLVVHCSAGAGRTGCFIVIDIMLDMAEREGVVDIYNCVRELRSRRVNMVQTEEQYVFIHD 266


                   ...
gi 2032733617 1267 AML 1269
Cdd:cd14633    267 AIL 269
R-PTPc-Q cd14616
catalytic domain of receptor-type tyrosine-protein phosphatase Q; Receptor-type ...
 1040-1266 4.03e-33

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: 128.10  E-value: 4.03e-33
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032733617 1040 NRNSSVVPSERARVGLAPLPGMKGTDYINASYIMGYYRSNEFIITQHPLPHTTKDFWRMIWDHNAQIIVMLpdNQSLAED 1119
Cdd:cd14616      1 NRFPNIKPYNNNRVKLIADAGVPGSDYINASYISGYLCPNEFIATQGPLPGTVGDFWRMVWETRAKTIVML--TQCFEKG 78

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032733617 1120 EF---VYWPsrEESMNCEAFTVTLISKdrlcLSNEEQI--IIHDFILEaTQDDYVLeVRHFQCPKWPNPDAPiSSTFELI 1194
Cdd:cd14616     79 RIrchQYWP--EDNKPVTVFGDIVITK----LMEDVQIdwTIRDLKIE-RHGDYMM-VRQCNFTSWPEHGVP-ESSAPLI 149

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2032733617 1195 NVIKEEALTRDG---PTIVHDEYGAVSAGTLCALTTLSQQLENENAVDVFQVAKMINLMRPGVFTDIEQYQFLYK 1266
Cdd:cd14616    150 HFVKLVRASRAHdntPMIVHCSAGVGRTGVFIALDHLTQHINDHDFVDIYGLVAELRSERMCMVQNLAQYIFLHQ 224
R-PTPc-T-1 cd14630
catalytic domain of receptor-type tyrosine-protein phosphatase T, repeat 1; Receptor-type ...
 1034-1269 4.65e-33

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: 128.60  E-value: 4.65e-33
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032733617 1034 DCNKEKNRNSSVVPSERARVGLAPLPGMKGTDYINASYIMGYYRSNEFIITQHPLPHTTKDFWRMIWDHNAQIIVMLPDN 1113
Cdd:cd14630      1 DENRNKNRYGNIISYDHSRVRLQLLDGDPHSDYINANYIDGYHRPRHYIATQGPMQETVKDFWRMIWQENSASVVMVTNL 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032733617 1114 QSLAEDEFV-YWPSREESMNceAFTVTLISKDRLClsneeQIIIHDFILEATQDDYVLEVRHFQCPKWPNPDAPISST-- 1190
Cdd:cd14630     81 VEVGRVKCVrYWPDDTEVYG--DIKVTLIETEPLA-----EYVIRTFTVQKKGYHEIREIRQFHFTSWPDHGVPCYATgl 153

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2032733617 1191 FELINVIKEEALTRDGPTIVHDEYGAVSAGTLCALTTLSQQLENENAVDVFQVAKMINLMRPGVFTDIEQYQFLYKAML 1269
Cdd:cd14630    154 LGFVRQVKFLNPPDAGPIVVHCSAGAGRTGCFIAIDIMLDMAENEGVVDIFNCVRELRAQRVNMVQTEEQYVFVHDAIL 232
PTPc-KIM cd14547
catalytic domain of the kinase interaction motif (KIM) family of protein-tyrosine phosphatases; ...
 1040-1265 4.81e-33

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: 127.90  E-value: 4.81e-33
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032733617 1040 NRNSSVVPSERARVGLAPLPGMKGTDYINASYIMGY-YRSNEFIITQHPLPHTTKDFWRMIWDHNAQIIVMLPDNQSLAE 1118
Cdd:cd14547      1 NRYKTILPNEHSRVCLPSVDDDPLSSYINANYIRGYdGEEKAYIATQGPLPNTVADFWRMVWQEKTPIIVMITNLTEAKE 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032733617 1119 DEFVYWPSrEESMNCEAFTVTLISKDRlclsnEEQIIIHDFILEatqddYVLEVR---HFQCPKWPN---PDAPiSSTFE 1192
Cdd:cd14547     81 KCAQYWPE-EENETYGDFEVTVQSVKE-----TDGYTVRKLTLK-----YGGEKRylkHYWYTSWPDhktPEAA-QPLLS 148

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2032733617 1193 LINVIKEEALTRD--GPTIVHDEYGAVSAGTLCALTTLSQQLENENAVDVFQVAKMINLMRPGVFTDIEQYQFLY 1265
Cdd:cd14547    149 LVQEVEEARQTEPhrGPIVVHCSAGIGRTGCFIATSIGCQQLREEGVVDVLGIVCQLRLDRGGMVQTAEQYEFVH 223
R-PTPc-B cd14617
catalytic domain of receptor-type tyrosine-protein phosphatase B; Receptor-type ...
 1040-1266 1.57e-32

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


Pssm-ID: 350465 [Multi-domain]  Cd Length: 228  Bit Score: 126.57  E-value: 1.57e-32
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032733617 1040 NRNSSVVPSERARVGLAPLPGMKGTDYINASYIMGYYRSNEFIITQHPLPHTTKDFWRMIWDHNAQIIVMLpdnQSLAED 1119
Cdd:cd14617      1 NRYNNILPYDSTRVKLSNVDDDPCSDYINASYIPGNNFRREYIATQGPLPGTKDDFWKMVWEQNVHNIVMV---TQCVEK 77

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032733617 1120 EFV----YWPSREESMNCEAFTVTLISKDRLclsneEQIIIHDF-ILEATQDDYVLEVRHFQCPKWPNPDAPiSSTFELI 1194
Cdd:cd14617     78 GRVkcdhYWPADQDSLYYGDLIVQMLSESVL-----PEWTIREFkICSEEQLDAPRLVRHFHYTVWPDHGVP-ETTQSLI 151

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032733617 1195 NVIKEealTRD--------GPTIVHDEYGAVSAGTLCALTTLSQQLENENAVDVFQVAKMINLMRPGVFTDIEQYQFLYK 1266
Cdd:cd14617    152 QFVRT---VRDyinrtpgsGPTVVHCSAGVGRTGTFIALDRILQQLDSKDSVDIYGAVHDLRLHRVHMVQTECQYVYLHQ 228
R-PTPc-F-1 cd14626
catalytic domain of receptor-type tyrosine-protein phosphatase F, repeat 1; Receptor-type ...
 1034-1273 1.83e-32

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: 127.84  E-value: 1.83e-32
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032733617 1034 DCNKEKNRNSSVVPSERARVGLAPLPGMKGTDYINASYIMGYYRSNEFIITQHPLPHTTKDFWRMIWDHNAQIIVMLpdn 1113
Cdd:cd14626     39 EVNKPKNRYANVIAYDHSRVILTSVDGVPGSDYINANYIDGYRKQNAYIATQGPLPETLSDFWRMVWEQRTATIVMM--- 115

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032733617 1114 QSLAEDEFV----YWPSReESMNCEAFTVTLISKDRLCLSNeeqiiIHDFILEATQDDYVLEVRHFQCPKWPN---PDAP 1186
Cdd:cd14626    116 TRLEEKSRVkcdqYWPIR-GTETYGMIQVTLLDTVELATYS-----VRTFALYKNGSSEKREVRQFQFMAWPDhgvPEYP 189

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032733617 1187 iSSTFELINVIKEEALTRDGPTIVHDEYGAVSAGTLCALTTLSQQLENENAVDVFQVAKMINLMRPGVFTDIEQYQFLYK 1266
Cdd:cd14626    190 -TPILAFLRRVKACNPPDAGPMVVHCSAGVGRTGCFIVIDAMLERMKHEKTVDIYGHVTCMRSQRNYMVQTEDQYIFIHE 268


                   ....*..
gi 2032733617 1267 AMLSLVS 1273
Cdd:cd14626    269 ALLEAAT 275
alpha_CA_IX cd03150
Carbonic anhydrase alpha, isozyme IX. Carbonic anhydrases (CAs) are zinc-containing enzymes ...
 24-204 1.85e-32

Carbonic anhydrase alpha, isozyme IX. Carbonic anhydrases (CAs) are zinc-containing enzymes that catalyze the reversible hydration of carbon dioxide in a two-step mechanism: a nucleophilic attack of a zinc-bound hydroxide ion on carbon dioxide, followed by the regeneration of the active site by ionization of the zinc-bound water molecule and removal of a proton from the active site. They are ubiquitous enzymes involved in fundamental processes like photosynthesis, respiration, pH homeostasis and ion transport. There are three evolutionary distinct groups - alpha, beta and gamma carbonic anhydrases - which show no significant sequence identity or structural similarity. Alpha CAs are strictly monomeric enzymes. The zinc ion is complexed by three histidine residues. This sub-family comprises the membrane protein CA IX. CA IX is functionally implicated in tumor growth and survival. CA IX is mainly present in solid tumors and its expression in normal tissues is limited to the mucosa of alimentary tract. CA IX is a transmembrane protein with two extracellular domains: carbonic anhydrase and, a proteoglycan-like segment mediating cell-cell adhesion. There is evidence for an involvement of the MAPK pathway in the regulation of CA9 expression.


Pssm-ID: 239403  Cd Length: 247  Bit Score: 126.99  E-value: 1.85e-32
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032733617   24 PGR-FKAEKVEFHWGQSnGSAGSEHSINGKRFPVEMQIFFYNpDDFDSFGTAVLENRVVGAMAVFFQVSQRDNSALDPII 102
Cdd:cd03150     72 PGQeYRALQLHLHWGAA-GRPGSEHTVDGHRFPAEIHVVHLS-TAFANLDEALGRPGGLAVLAAFLAEGLHENSAYEQLL 149

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032733617  103 HGLKGVVHHEKETFLDPFVLRELLPTSLGSYYRYTGSLTTPPCSEIVEWIVFRKPVPISYHQLEAFYSIFTTEQQdhvks 182
Cdd:cd03150    150 SRLSEISEEESETVVPGLDVSALLPSDLSRYFRYEGSLTTPPCAQGVIWTVFNQTVRLSAKQLHTLSDSLWGPHD----- 224

                          170       180
                   ....*....|....*....|..
gi 2032733617  183 vEYLRNNFRPQQSLNNRKVSKS 204
Cdd:cd03150    225 -SRLQLNFRATQPLNGRKIEAS 245
alpha_CA_I_II_III_XIII cd03119
Carbonic anhydrase alpha, isozymes I, II, and III and XIII. Carbonic anhydrases (CAs) are ...
 3-204 4.31e-32

Carbonic anhydrase alpha, isozymes I, II, and III and XIII. Carbonic anhydrases (CAs) are zinc-containing enzymes that catalyze the reversible hydration of carbon dioxide in a two-step mechanism: a nucleophilic attack of a zinc-bound hydroxide ion on carbon dioxide, followed by the regeneration of the active site by ionization of the zinc-bound water molecule and removal of a proton from the active site. They are ubiquitous enzymes involved in fundamental processes like photosynthesis, respiration, pH homeostasis and ion transport. Most alpha CAs are monomeric enzymes. The zinc ion is complexed by three histidines. This vertebrate subgroup comprises isozymes I, II, and III, which are cytoplasmic enzymes. CA I, for example, is expressed in erythrocyes of many vertebrates; CA II is the most active cytosolic isozyme; while it is being expressed nearly ubiquitously, it comprises 95% of the renal carbonic anhydrase and is required for renal acidification; CA III has been implicated in protection from the damaging effect of oxidizing agents in hepatocytes. CAXIII may play important physiological roles in several organs.


Pssm-ID: 239393 [Multi-domain]  Cd Length: 259  Bit Score: 126.40  E-value: 4.31e-32
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032733617    3 NTGKTVAILLKDDY---FVSGAGLPGRFKAEKVEFHWGQSNGSaGSEHSINGKRFPVEMQIFFYNPDdFDSFGTAVLENR 79
Cdd:cd03119     61 NNGHSFNVEFDDTDdrsVLRGGPLTGSYRLRQFHFHWGSSDDH-GSEHTVDGVKYAAELHLVHWNSK-YGSFGEAAKQPD 138

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032733617   80 VVGAMAVFFQVSqRDNSALDPIIHGLKGVVHHEKETFLDPFVLRELLPTSLgSYYRYTGSLTTPPCSEIVEWIVFRKPVP 159
Cdd:cd03119    139 GLAVVGVFLKVG-EANPELQKVLDALDSIKTKGKQAPFTNFDPSCLLPASL-DYWTYPGSLTTPPLLECVTWIVLKEPIS 216

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*
gi 2032733617  160 ISYHQLEAFYSIFTTEQQDhvkSVEYLRNNFRPQQSLNNRKVSKS 204
Cdd:cd03119    217 VSSEQMAKFRSLLFNAEGE---PPCPMVDNWRPPQPLKGRKVRAS 258
R5-PTP-2 cd14550
PTP-like domain of R5 subfamily receptor-type tyrosine-protein phosphatases, repeat 2; The R5 ...
 767-973 5.05e-32

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: 123.97  E-value: 5.05e-32
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032733617  767 YINANYVDGYNKAKAYIATQGPLKSTFEDFWRMIWEQNTGIIVMITNLVEKGrrKCDQYWPT-ENSEEYGNIIVTLKSTN 845
Cdd:cd14550      1 YINASYLQGYRRSNEFIITQHPLEHTIKDFWQMIWDHNSQTIVMLTDNELNE--DEPIYWPTkEKPLECETFKVTLSGED 78

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032733617  846 vHAC------YTVRRFTVRNTkmkkgqkgnpkgrQNER--TVIQYHYTQWPDMGVPEY-ALPVLTFVRRSSAARTpdmGP 916
Cdd:cd14550     79 -HSClsneirLIVRDFILEST-------------QDDYvlEVRQFQCPSWPNPCSPIHtVFELINTVQEWAQQRD---GP 141

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 2032733617  917 VVVHCSAGVGRTGTYIVIDSMLQQIKDKSTVNVLGFLKHIRTQRNYLVQTEEQYIFI 973
Cdd:cd14550    142 IVVHDRYGGVQAATFCALTTLHQQLEHESSVDVYQVAKLYHLMRPGVFTSKEDYQFL 198
alpha_CARP_VIII cd03120
Carbonic anhydrase alpha related protein, group VIII. Carbonic anhydrase related proteins ...
 3-201 1.23e-31

Carbonic anhydrase alpha related protein, group VIII. Carbonic anhydrase related proteins (CARPs) are sequence similar to carbonic anhydrases. Carbonic anhydrases are zinc-containing enzymes that catalyze the reversible hydration of carbon dioxide in a two-step mechanism. CARPs have lost conserved histidines involved in zinc binding and consequently their catalytic activity. CARP VIII may play roles in various biological processes of the central nervous system, and could be involved in protein-protein interactions. CARP VIII has been shown to bind inositol 1,4,5-triphosphate (IP3) receptor type I (IP3RI), reducing the affinity of the receptor for IP3. IP3RI is an intracellular IP3-gated Ca2+ channel located on intracellular Ca2+ stores. IP3RI converts IP3 signaling into Ca2+ signaling thereby participating in a variety of cell functions.


Pssm-ID: 239394  Cd Length: 256  Bit Score: 124.97  E-value: 1.23e-31
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032733617    3 NTGKTVAILLKDDYFVSGAGLP--GRFKAEKVEFHWGQSNgSAGSEHSINGKRFPVEMQIFFYNPDDFDSFGTAVLENRV 80
Cdd:cd03120     51 NDGHTIQIILKSKSVLSGGPLPqgHEFELAEVRFHWGREN-QRGSEHTVNFKAFPMELHLIHWNSTLYSSLEEAMGKPHG 129

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032733617   81 VGAMAVFFQVSqRDNSALDPIIHGLKGVVHHEKETFLDPFVLRELLPTS-LGSYYRYTGSLTTPPCSEIVEWIVFRKPVP 159
Cdd:cd03120    130 IAIIALFVQIG-KEHVGLKAVTEILQDIQYKGKSKTIPCFNPNTLLPDPlLRDYWVYEGSLTTPPCSEGVTWILFRYPLT 208

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*....
gi 2032733617  160 ISYHQLEAFYSIFTteqqdHVKSVEYLR-------NNFRPQQSLNNRKV 201
Cdd:cd03120    209 ISQSQIEEFRRLRT-----HVKGAELVEgcdgllgDNFRPTQPLSDRVI 252
R-PTPc-S-1 cd14625
catalytic domain of receptor-type tyrosine-protein phosphatase S, repeat 1; Receptor-type ...
 1034-1273 3.54e-31

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: 124.44  E-value: 3.54e-31
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032733617 1034 DCNKEKNRNSSVVPSERARVGLAPLPGMKGTDYINASYIMGYYRSNEFIITQHPLPHTTKDFWRMIWDHNAQIIVM---L 1110
Cdd:cd14625     45 EVNKPKNRYANVIAYDHSRVILQPIEGIMGSDYINANYIDGYRKQNAYIATQGPLPETFGDFWRMVWEQRSATVVMmtkL 124

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032733617 1111 PDNQSLAEDEfvYWPSREESmNCEAFTVTLISKDRLClsneeQIIIHDFILEATQDDYVLEVRHFQCPKWPNPDAPISST 1190
Cdd:cd14625    125 EEKSRIKCDQ--YWPSRGTE-TYGMIQVTLLDTIELA-----TFCVRTFSLHKNGSSEKREVRQFQFTAWPDHGVPEYPT 196

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032733617 1191 --FELINVIKEEALTRDGPTIVHDEYGAVSAGTLCALTTLSQQLENENAVDVFQVAKMINLMRPGVFTDIEQYQFLYKAM 1268
Cdd:cd14625    197 pfLAFLRRVKTCNPPDAGPIVVHCSAGVGRTGCFIVIDAMLERIKHEKTVDIYGHVTLMRSQRNYMVQTEDQYSFIHDAL 276


                   ....*
gi 2032733617 1269 LSLVS 1273
Cdd:cd14625    277 LEAVA 281
PTP_fungal cd18533
fungal protein tyrosine phosphatases; This subfamily contains Saccharomyces cerevisiae ...
 1066-1265 5.55e-31

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: 121.59  E-value: 5.55e-31
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032733617 1066 YINASYI-MGYYRSNEFIITQHPLPHTTKDFWRMIWDHNAQIIVML-PDNQSLAEDEFVYWPSREESMNCEAFTVTLISK 1143
Cdd:cd18533      1 YINASYItLPGTSSKRYIATQGPLPATIGDFWKMIWQNNVGVIVMLtPLVENGREKCDQYWPSGEYEGEYGDLTVELVSE 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032733617 1144 DRLclsNEEQIIIHDFILeATQDDYVLEVRHFQCPKWPNPDAP--ISSTFELINVIKE--EALTRDGPTIVHdeygaVSA 1219
Cdd:cd18533     81 EEN---DDGGFIVREFEL-SKEDGKVKKVYHIQYKSWPDFGVPdsPEDLLTLIKLKRElnDSASLDPPIIVH-----CSA 151

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2032733617 1220 -----GTLCALTTLSQQLEN--------ENAVDVfqVAKMINLM---RPGVFTDIEQYQFLY 1265
Cdd:cd18533    152 gvgrtGTFIALDSLLDELKRglsdsqdlEDSEDP--VYEIVNQLrkqRMSMVQTLRQYIFLY 211
PTPc-N7 cd14612
catalytic domain of tyrosine-protein phosphatase non-receptor type 7; Tyrosine-protein ...
 1039-1268 6.04e-31

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: 122.64  E-value: 6.04e-31
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032733617 1039 KNRNSSVVPSERARVGL-APLPGMKGTDYINASYIMGYY-RSNEFIITQHPLPHTTKDFWRMIWDHNAQIIVMLPDNQSL 1116
Cdd:cd14612     18 KDRYKTILPNPQSRVCLrRAGSQEEEGSYINANYIRGYDgKEKAYIATQGPMLNTVSDFWEMVWQEECPIIVMITKLKEK 97

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032733617 1117 AEDEFVYWPSREESMNceAFTVTlISKDRLClsneEQIIIHDFILEATQDDYvlEVRHFQCPKWPNPDAPIS--STFELI 1194
Cdd:cd14612     98 KEKCVHYWPEKEGTYG--RFEIR-VQDMKEC----DGYTIRDLTIQLEEESR--SVKHYWFSSWPDHQTPESagPLLRLV 168

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2032733617 1195 NVIKE--EALTRDGPTIVHDEYGAVSAGTLCALTTLSQQLENENAVDVFQVAKMINLMRPGVFTDIEQYQFLYKAM 1268
Cdd:cd14612    169 AEVEEsrQTAASPGPIVVHCSAGIGRTGCFIATSIGCQQLKDTGKVDILGIVCQLRLDRGGMIQTSEQYQFLHHTL 244
R-PTPc-T-2 cd14634
PTP domain of receptor-type tyrosine-protein phosphatase T, repeat 2; Receptor-type ...
 767-979 1.23e-30

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


Pssm-ID: 350482 [Multi-domain]  Cd Length: 206  Bit Score: 120.51  E-value: 1.23e-30
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032733617  767 YINANYVDGYNKAKAYIATQGPLKSTFEDFWRMIWEQNTGIIVMITNLveKGRRKCDQYWPTENSEEYGNIIVTLKSTNV 846
Cdd:cd14634      1 YINAALMDSHKQPAAFIVTQHPLPNTVADFWRLVFDYNCSSVVMLNEM--DAAQLCMQYWPEKTSCCYGPIQVEFVSADI 78

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032733617  847 HACYTVRRFTVRNtkMKKGQKGnpkgrqnERTVIQYHYTQWPDM-GVPEYALPVLTFVRRSSAARTP---DMGPVVVHCS 922
Cdd:cd14634     79 DEDIISRIFRICN--MARPQDG-------YRIVQHLQYIGWPAYrDTPPSKRSILKVVRRLEKWQEQydgREGRTVVHCL 149

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 2032733617  923 AGVGRTGTYIVIDSMLQQIKDKSTVNVLGFLKHIRTQRNYLVQTEEQYIFIHDALLE 979
Cdd:cd14634    150 NGGGRSGTFCAICSVCEMIQQQNIIDVFHTVKTLRNNKSNMVETLEQYKFVYEVALE 206
R-PTPc-E-1 cd14620
catalytic domain of receptor-type tyrosine-protein phosphatase E, repeat 1; Receptor-type ...
 1044-1269 2.09e-30

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: 120.43  E-value: 2.09e-30
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032733617 1044 SVVPSERARVGLAPLPGMKGTDYINASYIMGYYRSNEFIITQHPLPHTTKDFWRMIWDHNAQIIVMLPDNQSLAEDE-FV 1122
Cdd:cd14620      3 NILPYDHSRVILSQLDGIPCSDYINASYIDGYKEKNKFIAAQGPKQETVNDFWRMVWEQKSATIVMLTNLKERKEEKcYQ 82

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032733617 1123 YWPSReesmNCEAF-TVTLISKDRLCLSNeeqIIIHDFILEATQDDYVLEVR-----HFQcpKWPNPDAPIS--STFELI 1194
Cdd:cd14620     83 YWPDQ----GCWTYgNIRVAVEDCVVLVD---YTIRKFCIQPQLPDGCKAPRlvtqlHFT--SWPDFGVPFTpiGMLKFL 153

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2032733617 1195 NVIKEEALTRDGPTIVHDEYGAVSAGTLCALTTLSQQLENENAVDVFQVAKMINLMRPGVFTDIEQYQFLYKAML 1269
Cdd:cd14620    154 KKVKSVNPVHAGPIVVHCSAGVGRTGTFIVIDAMIDMMHAEQKVDVFEFVSRIRNQRPQMVQTDMQYSFIYQALL 228
alpha_CA_VI cd03125
Carbonic anhydrase alpha, isozyme VI. Carbonic anhydrases (CAs) are zinc-containing enzymes ...
 1-204 2.31e-30

Carbonic anhydrase alpha, isozyme VI. Carbonic anhydrases (CAs) are zinc-containing enzymes that catalyze the reversible hydration of carbon dioxide in a two-step mechanism: a nucleophilic attack of a zinc-bound hydroxide ion on carbon dioxide, followed by the regeneration of the active site by ionization of the zinc-bound water molecule and removal of a proton from the active site. They are ubiquitous enzymes involved in fundamental processes like photosynthesis, respiration, pH homeostasis and ion transport. There are three evolutionary distinct groups - alpha, beta and gamma carbonic anhydrases - which show no significant sequence identity or structural similarity. Most alpha CAs are monomeric enzymes. The zinc ion is complexed by three histidine residues. This sub-family comprises the secreted CA VI, which is found in saliva.


Pssm-ID: 239399  Cd Length: 249  Bit Score: 121.05  E-value: 2.31e-30
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032733617    1 MKNTGKTVAILLKDDYFVSgAGLPGRFKAEKVEFHWG-QSNGSAGSEHSINGKRFPVEMQIFFYNpDDFDSFGTAVLENR 79
Cdd:cd03125     50 MTNNGHTVQIDLPPTMSIT-TGDGTVYTAVQMHFHWGgRDSEISGSEHTIDGMRYVAELHIVHYN-SKYKSYEEAKDKPD 127

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032733617   80 VVGAMAVFFQVSQR-DNSALDPIIHGLKGVVHHEKETFLDPFVLRELLPTSLGSYYRYTGSLTTPPCSEIVEWIVFRKPV 158
Cdd:cd03125    128 GLAVLAFLYKVGHYaENTYYSDFISKLAKIKYAGQTTTLTSLDVRDMLPENLHHYYTYQGSLTTPPCTENVLWFVFDDPV 207

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*.
gi 2032733617  159 PISYHQLEafySIFTTEQQDHVKSveyLRNNFRPQQSLNNRKVSKS 204
Cdd:cd03125    208 TLSKTQIV---KLENTLMDHHNKT---IRNDYRRTQPLNHRVVEAN 247
PTPc-N5 cd14613
catalytic domain of tyrosine-protein phosphatase non-receptor type 5; Tyrosine-protein ...
 1039-1268 3.32e-30

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: 120.74  E-value: 3.32e-30
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032733617 1039 KNRNSSVVPSERARVGL-APLPGMKGTDYINASYIMGY-YRSNEFIITQHPLPHTTKDFWRMIWDHNAQIIVMLPDNQSL 1116
Cdd:cd14613     28 KNRYKTILPNPHSRVCLtSPDQDDPLSSYINANYIRGYgGEEKVYIATQGPTVNTVGDFWRMVWQERSPIIVMITNIEEM 107

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032733617 1117 AEDEFVYWPsrEESMNCEAFTVTLisKDRLClsnEEQIIIHDFILEATQDDYVLevRHFQCPKWPNPDAPISST--FELI 1194
Cdd:cd14613    108 NEKCTEYWP--EEQVTYEGIEITV--KQVIH---ADDYRLRLITLKSGGEERGL--KHYWYTSWPDQKTPDNAPplLQLV 178

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2032733617 1195 NVIKE---EALTRDGPTIVHDEYGAVSAGTLCALTTLSQQLENENAVDVFQVAKMINLMRPGVFTDIEQYQFLYKAM 1268
Cdd:cd14613    179 QEVEEarqQAEPNCGPVIVHCSAGIGRTGCFIATSICCKQLRNEGVVDILRTTCQLRLDRGGMIQTCEQYQFVHHVL 255
R-PTPc-G-1 cd17667
catalytic domain of receptor-type tyrosine-protein phosphatase G, repeat 1; Receptor-type ...
 1036-1272 6.08e-30

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: 120.53  E-value: 6.08e-30
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032733617 1036 NKEKNRNSSVVPSERARVGLAPLPGM--KGTDYINASYIMGYYRSNEFIITQHPLPHTTKDFWRMIWDHNAQIIVMLPDn 1113
Cdd:cd17667     27 NKHKNRYINILAYDHSRVKLRPLPGKdsKHSDYINANYVDGYNKAKAYIATQGPLKSTFEDFWRMIWEQNTGIIVMITN- 105

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032733617 1114 qsLAE------DEfvYWPSrEESMNCEAFTVTLIS-KDRLCLSneeqiiIHDFILEATQDDYVLE-----------VRHF 1175
Cdd:cd17667    106 --LVEkgrrkcDQ--YWPT-ENSEEYGNIIVTLKStKIHACYT------VRRFSIRNTKVKKGQKgnpkgrqnertVIQY 174

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032733617 1176 QCPKWPNPDAPISSTFELINVIKEEA--LTRDGPTIVHDEYGAVSAGTLCALTTLSQQLENENAVDVFQVAKMINLMRPG 1253
Cdd:cd17667    175 HYTQWPDMGVPEYALPVLTFVRRSSAarTPEMGPVLVHCSAGVGRTGTYIVIDSMLQQIKDKSTVNVLGFLKHIRTQRNY 254

                          250
                   ....*....|....*....
gi 2032733617 1254 VFTDIEQYQFLYKAMLSLV 1272
Cdd:cd17667    255 LVQTEEQYIFIHDALLEAI 273
R-PTP-N cd14609
PTP-like domain of receptor-type tyrosine-protein phosphatase N; Receptor-type ...
 1008-1268 9.36e-30

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: 120.14  E-value: 9.36e-30
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032733617 1008 KTRLEKQFKLVTQCNAKYVECFSAQKDCNKEKNRNSSVVPSERARVGLAPLPGMKGTDYINASYIMGY-YRSNEFIITQH 1086
Cdd:cd14609     14 RDRLAKEWQALCAYQAEPNTCSTAQGEANVKKNRNPDFVPYDHARIKLKAESNPSRSDYINASPIIEHdPRMPAYIATQG 93

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032733617 1087 PLPHTTKDFWRMIWDHNAQIIVMLpdnQSLAEDEFV----YWPSREESMNcEAFTVTLISKDRLClsneEQIIIHDFILE 1162
Cdd:cd14609     94 PLSHTIADFWQMVWENGCTVIVML---TPLVEDGVKqcdrYWPDEGSSLY-HIYEVNLVSEHIWC----EDFLVRSFYLK 165

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032733617 1163 ATQDDYVLEVRHFQCPKWPNPDAPiSSTFELINV---IKEEALTRDGPTIVHDEYGAVSAGTLCAL-TTLSQQLENENAV 1238
Cdd:cd14609    166 NVQTQETRTLTQFHFLSWPAEGIP-SSTRPLLDFrrkVNKCYRGRSCPIIVHCSDGAGRTGTYILIdMVLNRMAKGVKEI 244

                          250       260       270
                   ....*....|....*....|....*....|
gi 2032733617 1239 DVFQVAKMINLMRPGVFTDIEQYQFLYKAM 1268
Cdd:cd14609    245 DIAATLEHVRDQRPGMVRTKDQFEFALTAV 274
PTPc-N22 cd14602
catalytic domain of tyrosine-protein phosphatase non-receptor type 22; Tyrosine-protein ...
 1039-1271 1.03e-29

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: 118.79  E-value: 1.03e-29
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032733617 1039 KNRNSSVVPSERARVGLAPLPGMKGTDYINASYIMGYYRSNEFIITQHPLPHTTKDFWRMIWDHNAQIIVMlpdnqslAE 1118
Cdd:cd14602      1 KNRYKDILPYDHSRVELSLITSDEDSDYINANFIKGVYGPRAYIATQGPLSTTLLDFWRMIWEYSVLIIVM-------AC 73

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032733617 1119 DEFV--------YWP-SREESMNCEAFTVTLISKDrlclsNEEQIIIHdfILEATQDDYVLEVRHFQCPKWPNPDAP--I 1187
Cdd:cd14602     74 MEFEmgkkkcerYWAePGEMQLEFGPFSVTCEAEK-----RKSDYIIR--TLKVKFNSETRTIYQFHYKNWPDHDVPssI 146

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032733617 1188 SSTFELINVIKEEALTRDGPTIVHDEYGAVSAGTLCALTTLSQQLENENAVDVFQVAKMINLM---RPGVFTDIEQYQFL 1264
Cdd:cd14602    147 DPILELIWDVRCYQEDDSVPICIHCSAGCGRTGVICAIDYTWMLLKDGIIPENFSVFSLIQEMrtqRPSLVQTKEQYELV 226


                   ....*..
gi 2032733617 1265 YKAMLSL 1271
Cdd:cd14602    227 YNAVIEL 233
R-PTPc-D-1 cd14624
catalytic domain of receptor-type tyrosine-protein phosphatase D, repeat 1; Receptor-type ...
 1034-1273 1.23e-29

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: 120.22  E-value: 1.23e-29
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032733617 1034 DCNKEKNRNSSVVPSERARVGLAPLPGMKGTDYINASYIMGYYRSNEFIITQHPLPHTTKDFWRMIWDHNAQIIVM---L 1110
Cdd:cd14624     45 EVNKPKNRYANVIAYDHSRVLLSAIEGIPGSDYINANYIDGYRKQNAYIATQGALPETFGDFWRMIWEQRSATVVMmtkL 124

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032733617 1111 PDNQSLAEDEfvYWPSREESMNcEAFTVTLISKDRLClsneeQIIIHDFILEATQDDYVLEVRHFQCPKWPNPDAPISST 1190
Cdd:cd14624    125 EERSRVKCDQ--YWPSRGTETY-GLIQVTLLDTVELA-----TYCVRTFALYKNGSSEKREVRQFQFTAWPDHGVPEHPT 196

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032733617 1191 --FELINVIKEEALTRDGPTIVHDEYGAVSAGTLCALTTLSQQLENENAVDVFQVAKMINLMRPGVFTDIEQYQFLYKAM 1268
Cdd:cd14624    197 pfLAFLRRVKTCNPPDAGPMVVHCSAGVGRTGCFIVIDAMLERIKHEKTVDIYGHVTLMRAQRNYMVQTEDQYIFIHDAL 276


                   ....*
gi 2032733617 1269 LSLVS 1273
Cdd:cd14624    277 LEAVT 281
PTPc-N22_18_12 cd14542
catalytic domain of tyrosine-protein phosphatase non-receptor type 22, type 18 and type 12; ...
 1066-1266 1.49e-29

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: 117.14  E-value: 1.49e-29
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032733617 1066 YINASYIMGYYRSNEFIITQHPLPHTTKDFWRMIWDHNAQIIVMLPDNQSLAEDEFV-YWP-SREESMNCEAFTVTLISK 1143
Cdd:cd14542      1 YINANFIKGVSGSKAYIATQGPLPNTVLDFWRMIWEYNVQVIVMACREFEMGKKKCErYWPeEGEEQLQFGPFKISLEKE 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032733617 1144 DRLClsneEQIIIHDFILEATQDDYVleVRHFQCPKWPNPDAPISST--FELINVIKEEALTRDGPTIVHDEYGAVSAGT 1221
Cdd:cd14542     81 KRVG----PDFLIRTLKVTFQKESRT--VYQFHYTAWPDHGVPSSVDpiLDLVRLVRDYQGSEDVPICVHCSAGCGRTGT 154

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*....
gi 2032733617 1222 LCAL----TTLSQQLENENaVDVFQVAKMINLMRPGVFTDIEQYQFLYK 1266
Cdd:cd14542    155 ICAIdyvwNLLKTGKIPEE-FSLFDLVREMRKQRPAMVQTKEQYELVYR 202
R-PTP-N2 cd14610
PTP-like domain of receptor-type tyrosine-protein phosphatase N2; Receptor-type ...
 1008-1268 1.56e-29

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: 119.78  E-value: 1.56e-29
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032733617 1008 KTRLEKQFKLVTQCNAKYVECFSAQKDCNKEKNRNSSVVPSERARVGLAPLPGMKGTDYINASYIMGY-YRSNEFIITQH 1086
Cdd:cd14610     16 KNRLEKEWEALCAYQAEPNATNVAQREENVQKNRSLAVLPYDHSRIILKAENSHSHSDYINASPIMDHdPRNPAYIATQG 95

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032733617 1087 PLPHTTKDFWRMIWDHNAQIIVML-PDNQSLAEDEFVYWPSrEESMNCEAFTVTLISKDRLClsneEQIIIHDFILEATQ 1165
Cdd:cd14610     96 PLPATVADFWQMVWESGCVVIVMLtPLAENGVKQCYHYWPD-EGSNLYHIYEVNLVSEHIWC----EDFLVRSFYLKNLQ 170

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032733617 1166 DDYVLEVRHFQCPKWPNPDAPiSSTFELINV---IKEEALTRDGPTIVHDEYGAVSAGTLCAL-TTLSQQLENENAVDVF 1241
Cdd:cd14610    171 TNETRTVTQFHFLSWNDQGVP-ASTRSLLDFrrkVNKCYRGRSCPIIVHCSDGAGRSGTYILIdMVLNKMAKGAKEIDIA 249

                          250       260
                   ....*....|....*....|....*..
gi 2032733617 1242 QVAKMINLMRPGVFTDIEQYQFLYKAM 1268
Cdd:cd14610    250 ATLEHLRDQRPGMVQTKEQFEFALTAV 276
R-PTPc-T-2 cd14634
PTP domain of receptor-type tyrosine-protein phosphatase T, repeat 2; Receptor-type ...
 1066-1269 2.34e-29

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


Pssm-ID: 350482 [Multi-domain]  Cd Length: 206  Bit Score: 116.66  E-value: 2.34e-29
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032733617 1066 YINASYIMGYYRSNEFIITQHPLPHTTKDFWRMIWDHNAQIIVMLPDNQSlAEDEFVYWPsrEESMNCEA-FTVTLISKD 1144
Cdd:cd14634      1 YINAALMDSHKQPAAFIVTQHPLPNTVADFWRLVFDYNCSSVVMLNEMDA-AQLCMQYWP--EKTSCCYGpIQVEFVSAD 77

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032733617 1145 RlclsnEEQIIIHDFI---LEATQDDYVLeVRHFQCPKWPN-PDAPIS--STFELINVI---KEEALTRDGPTIVHDEYG 1215
Cdd:cd14634     78 I-----DEDIISRIFRicnMARPQDGYRI-VQHLQYIGWPAyRDTPPSkrSILKVVRRLekwQEQYDGREGRTVVHCLNG 151

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....
gi 2032733617 1216 AVSAGTLCALTTLSQQLENENAVDVFQVAKMINLMRPGVFTDIEQYQFLYKAML 1269
Cdd:cd14634    152 GGRSGTFCAICSVCEMIQQQNIIDVFHTVKTLRNNKSNMVETLEQYKFVYEVAL 205
R5-PTPc-1 cd14549
catalytic domain of R5 subfamily receptor-type tyrosine-protein phosphatases, repeat 1; The R5 ...
 1066-1265 2.63e-29

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: 116.30  E-value: 2.63e-29
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032733617 1066 YINASYIMGYYRSNEFIITQHPLPHTTKDFWRMIWDHNAQIIVMLPDnqsLAE------DEfvYWPSrEESMNCEAFTVT 1139
Cdd:cd14549      1 YINANYVDGYNKARAYIATQGPLPSTFDDFWRMVWEQNSAIIVMITN---LVErgrrkcDQ--YWPK-EGTETYGNIQVT 74

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032733617 1140 LISKD--------RLCLSNEEqiiihdfILEATQDDYVLEVRHFQCPKWPNPDAPiSSTFELINVIKEEALTRD---GPT 1208
Cdd:cd14549     75 LLSTEvlatytvrTFSLKNLK-------LKKVKGRSSERVVYQYHYTQWPDHGVP-DYTLPVLSFVRKSSAANPpgaGPI 146

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2032733617 1209 IVHDEYGAVSAGTLCALTTLSQQLENENAVDVFQVAKMI----NLMrpgVFTDiEQYQFLY 1265
Cdd:cd14549    147 VVHCSAGVGRTGTYIVIDSMLQQIQDKGTVNVFGFLKHIrtqrNYL---VQTE-EQYIFIH 203
R-PTPc-typeIIb-1 cd14555
catalytic domain of type IIb (or R2B) subfamily receptor-type tyrosine-protein phosphatases, ...
 1066-1269 5.50e-29

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: 115.78  E-value: 5.50e-29
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032733617 1066 YINASYIMGYYRSNEFIITQHPLPHTTKDFWRMIWDHNAQIIVMLPDnqsLAEDEFV----YWPSREESMNceAFTVTLI 1141
Cdd:cd14555      1 YINANYIDGYHRPNHYIATQGPMQETVYDFWRMVWQENSASIVMVTN---LVEVGRVkcsrYWPDDTEVYG--DIKVTLV 75

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032733617 1142 SKDRLClsneeQIIIHDFILEATQDDYVLEVRHFQCPKWPNPDAPISST--FELINVIKEEALTRDGPTIVHDEYGAVSA 1219
Cdd:cd14555     76 ETEPLA-----EYVVRTFALERRGYHEIREVRQFHFTGWPDHGVPYHATglLGFIRRVKASNPPSAGPIVVHCSAGAGRT 150

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|
gi 2032733617 1220 GTLCALTTLSQQLENENAVDVFQVAKMINLMRPGVFTDIEQYQFLYKAML 1269
Cdd:cd14555    151 GCYIVIDIMLDMAEREGVVDIYNCVKELRSRRVNMVQTEEQYIFIHDAIL 200
R-PTPc-A-1 cd14621
catalytic domain of receptor-type tyrosine-protein phosphatase A, repeat 1; Receptor-type ...
 1028-1269 9.53e-29

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: 117.82  E-value: 9.53e-29
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032733617 1028 CFSAQKDCNKEKNRNSSVVPSERARVGLAPLPGMKGTDYINASYIMGYYRSNEFIITQHPLPHTTKDFWRMIWDHNAQII 1107
Cdd:cd14621     44 CEAASKEENKEKNRYVNILPYDHSRVHLTPVEGVPDSDYINASFINGYQEKNKFIAAQGPKEETVNDFWRMIWEQNTATI 123

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032733617 1108 VMLPDNQSLAEDEFV-YWPSReesmNCEAFTVTLIS-KDRLCLSNeeqIIIHDFILEATQDDYVLE----VRHFQCPKWP 1181
Cdd:cd14621    124 VMVTNLKERKECKCAqYWPDQ----GCWTYGNIRVSvEDVTVLVD---YTVRKFCIQQVGDVTNKKpqrlITQFHFTSWP 196

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032733617 1182 N---PDAPIsSTFELINVIKEEALTRDGPTIVHDEYGAVSAGTLCALTTLSQQLENENAVDVFQVAKMINLMRPGVFTDI 1258
Cdd:cd14621    197 DfgvPFTPI-GMLKFLKKVKNCNPQYAGAIVVHCSAGVGRTGTFIVIDAMLDMMHAERKVDVYGFVSRIRAQRCQMVQTD 275

                          250
                   ....*....|.
gi 2032733617 1259 EQYQFLYKAML 1269
Cdd:cd14621    276 MQYVFIYQALL 286
R-PTPc-U-2 cd14637
PTP domain of receptor-type tyrosine-protein phosphatase U, repeat 2; Receptor-type ...
 1066-1269 1.94e-28

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


Pssm-ID: 350485 [Multi-domain]  Cd Length: 207  Bit Score: 114.24  E-value: 1.94e-28
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032733617 1066 YINASYIMGYYRSNEFIITQHPLPHTTKDFWRMIWDHNAQIIVMLPD-NQS-LAEDEFVYWPsreESMNCEaftVTLISK 1143
Cdd:cd14637      1 YINAALTDSYTRSAAFIVTLHPLQNTTTDFWRLVYDYGCTSVVMLNQlNQSnSAWPCLQYWP---EPGLQQ---YGPMEV 74

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032733617 1144 DRLCLSNEEQIIIHDFILE--ATQDDYVLEVRHFQCPKWP----NPDAPISSTFELINVIKEEALTRDGPTIVHDEYGAV 1217
Cdd:cd14637     75 EFVSGSADEDIVTRLFRVQniTRLQEGHLMVRHFQFLRWSayrdTPDSKKAFLHLLASVEKWQRESGEGRTVVHCLNGGG 154

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|..
gi 2032733617 1218 SAGTLCALTTLSQQLENENAVDVFQVAKMINLMRPGVFTDIEQYQFLYKAML 1269
Cdd:cd14637    155 RSGTYCASAMILEMIRCHNIVDVFYAVKTLRNYKPNMVETLEQYRFCYEIAL 206
PTPc-N12 cd14604
catalytic domain of tyrosine-protein phosphatase non-receptor type 12; Tyrosine-protein ...
 1032-1271 9.76e-27

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: 111.95  E-value: 9.76e-27
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032733617 1032 QKDCNKEKNRNSSVVPSERARVGLAPLPGMKGTDYINASYIMGYYRSNEFIITQHPLPHTTKDFWRMIWDHNAQIIVMlp 1111
Cdd:cd14604     53 EKEENVKKNRYKDILPFDHSRVKLTLKTSSQDSDYINANFIKGVYGPKAYIATQGPLANTVIDFWRMIWEYNVAIIVM-- 130

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032733617 1112 dnqslAEDEFV--------YWPSR-EESMNCEAFTVTliskdrlCLSNEEQI--IIHDFILEATQDDYVLEVRHFQcpKW 1180
Cdd:cd14604    131 -----ACREFEmgrkkcerYWPLYgEEPMTFGPFRIS-------CEAEQARTdyFIRTLLLEFQNETRRLYQFHYV--NW 196

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032733617 1181 PNPDAPIS--STFELINVIKEEALTRDGPTIVHDEYGAVSAGTLCALTTLSQQLENENAVDVFQVAKMINLMRPGVFTDI 1258
Cdd:cd14604    197 PDHDVPSSfdSILDMISLMRKYQEHEDVPICIHCSAGCGRTGAICAIDYTWNLLKAGKIPEEFNVFNLIQEMRTQRHSAV 276

                          250
                   ....*....|....*.
gi 2032733617 1259 ---EQYQFLYKAMLSL 1271
Cdd:cd14604    277 qtkEQYELVHRAIAQL 292
R-PTPc-K-1 cd14631
catalytic domain of receptor-type tyrosine-protein phosphatase K, repeat 1; Receptor-type ...
 1052-1269 1.01e-26

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: 109.72  E-value: 1.01e-26
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032733617 1052 RVGLAPLPGMKGTDYINASYIMGYYRSNEFIITQHPLPHTTKDFWRMIWDHNAQIIVMLPDNQSLAEDE-FVYWPSREES 1130
Cdd:cd14631      1 RVILQPVEDDPSSDYINANYIDGYQRPSHYIATQGPVHETVYDFWRMIWQEQSACIVMVTNLVEVGRVKcYKYWPDDTEV 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032733617 1131 MNceAFTVTLISKDRLClsneeQIIIHDFILEATQDDYVLEVRHFQCPKWPNPDAPISST--FELINVIKEEALTRDGPT 1208
Cdd:cd14631     81 YG--DFKVTCVEMEPLA-----EYVVRTFTLERRGYNEIREVKQFHFTGWPDHGVPYHATglLSFIRRVKLSNPPSAGPI 153

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2032733617 1209 IVHDEYGAVSAGTLCALTTLSQQLENENAVDVFQVAKMINLMRPGVFTDIEQYQFLYKAML 1269
Cdd:cd14631    154 VVHCSAGAGRTGCYIVIDIMLDMAEREGVVDIYNCVKALRSRRINMVQTEEQYIFIHDAIL 214
R-PTPc-U-1 cd14632
catalytic domain of receptor-type tyrosine-protein phosphatase U, repeat 1; Receptor-type ...
 1066-1269 1.03e-26

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: 108.99  E-value: 1.03e-26
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032733617 1066 YINASYIMGYYRSNEFIITQHPLPHTTKDFWRMIWDHNAQIIVMLpdnQSLAEDEFV----YWPsrEESMNCEAFTVTLI 1141
Cdd:cd14632      1 YINANYIDGYHRSNHFIATQGPKQEMVYDFWRMVWQEHCSSIVMI---TKLVEVGRVkcskYWP--DDSDTYGDIKITLL 75

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032733617 1142 SKDRLClsneeQIIIHDFILEATQDDYVLEVRHFQCPKWPNPDAPISST--FELINVIKEEALTRDGPTIVHDEYGAVSA 1219
Cdd:cd14632     76 KTETLA-----EYSVRTFALERRGYSARHEVKQFHFTSWPEHGVPYHATglLAFIRRVKASTPPDAGPVVVHCSAGAGRT 150

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|
gi 2032733617 1220 GTLCALTTLSQQLENENAVDVFQVAKMINLMRPGVFTDIEQYQFLYKAML 1269
Cdd:cd14632    151 GCYIVLDVMLDMAECEGVVDIYNCVKTLCSRRINMIQTEEQYIFIHDAIL 200
PTPc-N1 cd14608
catalytic domain of tyrosine-protein phosphatase non-receptor type 1; Tyrosine-protein ...
 1028-1269 1.81e-26

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: 110.50  E-value: 1.81e-26
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032733617 1028 CFSAQKDCNKEKNRNSSVVPSERARVGLAplpgMKGTDYINASYIMGYYRSNEFIITQHPLPHTTKDFWRMIWDHNAQII 1107
Cdd:cd14608     17 CRVAKLPKNKNRNRYRDVSPFDHSRIKLH----QEDNDYINASLIKMEEAQRSYILTQGPLPNTCGHFWEMVWEQKSRGV 92

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032733617 1108 VMLpdNQSLAEDEF---VYWPSREES---MNCEAFTVTLISKDRLCLSNEEQIIIHDFILEATQddyvlEVRHFQCPKWP 1181
Cdd:cd14608     93 VML--NRVMEKGSLkcaQYWPQKEEKemiFEDTNLKLTLISEDIKSYYTVRQLELENLTTQETR-----EILHFHYTTWP 165

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032733617 1182 N---PDAPISSTFELINVIKEEALTRD-GPTIVHDEYGAVSAGTLCALTT---LSQQLENENAVDVFQVAKMINLMRPGV 1254
Cdd:cd14608    166 DfgvPESPASFLNFLFKVRESGSLSPEhGPVVVHCSAGIGRSGTFCLADTcllLMDKRKDPSSVDIKKVLLEMRKFRMGL 245

                          250
                   ....*....|....*
gi 2032733617 1255 FTDIEQYQFLYKAML 1269
Cdd:cd14608    246 IQTADQLRFSYLAVI 260
PTPc-N1_2 cd14545
catalytic domain of tyrosine-protein phosphatase non-receptor type 1 and type 2; ...
 1039-1266 4.53e-26

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: 107.86  E-value: 4.53e-26
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032733617 1039 KNRNSSVVPSERARVGLAPLPGmkGTDYINASYIMGYYRSNEFIITQHPLPHTTKDFWRMIWDHNAQIIVMLpdnQSLAE 1118
Cdd:cd14545      1 LNRYRDRDPYDHDRSRVKLKQG--DNDYINASLVEVEEAKRSYILTQGPLPNTSGHFWQMVWEQNSKAVIML---NKLME 75

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032733617 1119 DE----FVYWPSREESMNC---EAFTVTLISKDRlclsnEEQIIIHDFILEATQDDYVLEVRHFQCPKWPN---PDAPIS 1188
Cdd:cd14545     76 KGqikcAQYWPQGEGNAMIfedTGLKVTLLSEED-----KSYYTVRTLELENLKTQETREVLHFHYTTWPDfgvPESPAA 150

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032733617 1189 STFELINVIKEEALTRD-GPTIVHDEYGAVSAGTLCALTTLSQQLENEN--AVDVFQVAKMINLMRPGVFTDIEQYQFLY 1265
Cdd:cd14545    151 FLNFLQKVRESGSLSSDvGPPVVHCSAGIGRSGTFCLVDTCLVLIEKGNpsSVDVKKVLLEMRKYRMGLIQTPDQLRFSY 230


                   .
gi 2032733617 1266 K 1266
Cdd:cd14545    231 L 231
R-PTPc-M-2 cd14635
PTP domain of receptor-type tyrosine-protein phosphatase M, repeat 2; Receptor-type ...
 1066-1269 5.47e-26

PTP domain of receptor-type tyrosine-protein phosphatase M, repeat 2; Receptor-type tyrosine-protein phosphatase M (PTPRM), also known as protein-tyrosine phosphatase mu (R-PTP-mu or PTPmu), belongs to the type IIb subfamily of receptor protein tyrosine phosphatases (RPTPs), which belong to the larger family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. PTPRM/PTPmu is a homophilic cell adhesion molecule expressed in CNS neurons and glia. It is required for E-, N-, and R-cadherin-dependent neurite outgrowth. Loss of PTPmu contributes to tumor cell migration and dispersal of human glioblastomas. PTPRM contains an extracellular region with an Meprin-A5 (neuropilin)-mu (MAM) domain, an immunoglobulin (Ig) domain, and four fibronectin type III (FN3) repeats, a transmembrane domain, and an intracellular segment with a juxtamembrane domain similar to the cytoplasmic domain of classical cadherins and two tandem PTP domains. This model represents the second (repeat 2) PTP domain.


Pssm-ID: 350483 [Multi-domain]  Cd Length: 206  Bit Score: 107.08  E-value: 5.47e-26
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032733617 1066 YINASYIMGYYRSNEFIITQHPLPHTTKDFWRMIWDHNAQIIVMLPDNQSlAEDEFVYWPSREESMNcEAFTVTLISKDR 1145
Cdd:cd14635      1 YINAALMDSYKQPSAFIVTQHPLPNTVKDFWRLVLDYHCTSIVMLNDVDP-AQLCPQYWPENGVHRH-GPIQVEFVSADL 78

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032733617 1146 lclsnEEQIIIHDF-ILEAT--QDDYVLeVRHFQCPKWP-NPDAPIS--STFELINVI---KEEALTRDGPTIVHDEYGA 1216
Cdd:cd14635     79 -----EEDIISRIFrIYNAArpQDGYRM-VQQFQFLGWPmYRDTPVSkrSFLKLIRQVdkwQEEYNGGEGRTVVHCLNGG 152

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|...
gi 2032733617 1217 VSAGTLCALTTLSQQLENENAVDVFQVAKMINLMRPGVFTDIEQYQFLYKAML 1269
Cdd:cd14635    153 GRSGTFCAISIVCEMLRHQRAVDVFHAVKTLRNNKPNMVDLLDQYKFCYEVAL 205
R-PTPc-Z-1 cd17668
catalytic domain of receptor-type tyrosine-protein phosphatase Z, repeat 1; Receptor-type ...
 1066-1269 8.75e-26

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: 106.60  E-value: 8.75e-26
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032733617 1066 YINASYIMGYYRSNEFIITQHPLPHTTKDFWRMIWDHNAQIIVMLPDnqsLAE------DEfvYWPSrEESMNCEAFTVT 1139
Cdd:cd17668      1 YINANYVDGYNKPKAYIAAQGPLKSTAEDFWRMIWEHNVEVIVMITN---LVEkgrrkcDQ--YWPA-DGSEEYGNFLVT 74

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032733617 1140 LISKDRLCLSNEEQIIIHDF-ILEATQDDYVLE--VRHFQCPKWPNPDAPiSSTFELINVIKEEALTRD---GPTIVHDE 1213
Cdd:cd17668     75 QKSVQVLAYYTVRNFTLRNTkIKKGSQKGRPSGrvVTQYHYTQWPDMGVP-EYTLPVLTFVRKASYAKRhavGPVVVHCS 153

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 2032733617 1214 YGAVSAGTLCALTTLSQQLENENAVDVFQVAKMINLMRPGVFTDIEQYQFLYKAML 1269
Cdd:cd17668    154 AGVGRTGTYIVLDSMLQQIQHEGTVNIFGFLKHIRSQRNYLVQTEEQYVFIHDALV 209
PTPc_DSPc smart00012
Protein tyrosine phosphatase, catalytic domain, undefined specificity; Protein tyrosine ...
 1171-1270 2.85e-25

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: 101.28  E-value: 2.85e-25
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032733617  1171 EVRHFQCPKWPNPDAPISST--FELINVIKEE--ALTRDGPTIVHDEYGAVSAGTLCALTTLSQQLENE-NAVDVFQVAK 1245
Cdd:smart00012    1 TVKHYHYTGWPDHGVPESPDsiLELLRAVKKNlnQSESSGPVVVHCSAGVGRTGTFVAIDILLQQLEAEaGEVDIFDTVK 80

                            90       100
                    ....*....|....*....|....*
gi 2032733617  1246 MINLMRPGVFTDIEQYQFLYKAMLS 1270
Cdd:smart00012   81 ELRSQRPGMVQTEEQYLFLYRALLE 105
PTPc_motif smart00404
Protein tyrosine phosphatase, catalytic domain motif;
1171-1270 2.85e-25

Protein tyrosine phosphatase, catalytic domain motif;


Pssm-ID: 214649 [Multi-domain]  Cd Length: 105  Bit Score: 101.28  E-value: 2.85e-25
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032733617  1171 EVRHFQCPKWPNPDAPISST--FELINVIKEE--ALTRDGPTIVHDEYGAVSAGTLCALTTLSQQLENE-NAVDVFQVAK 1245
Cdd:smart00404    1 TVKHYHYTGWPDHGVPESPDsiLELLRAVKKNlnQSESSGPVVVHCSAGVGRTGTFVAIDILLQQLEAEaGEVDIFDTVK 80

                            90       100
                    ....*....|....*....|....*
gi 2032733617  1246 MINLMRPGVFTDIEQYQFLYKAMLS 1270
Cdd:smart00404   81 ELRSQRPGMVQTEEQYLFLYRALLE 105
PHA02747 PHA02747
protein tyrosine phosphatase; Provisional
 987-1277 5.38e-25

protein tyrosine phosphatase; Provisional


Pssm-ID: 165114 [Multi-domain]  Cd Length: 312  Bit Score: 107.39  E-value: 5.38e-25
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032733617  987 EVSANQLHSYVNSILIPGIggkTRLEkQFKLVTQCNAKYVECFsaQKDCNKEKNRNSSVVPSERARVGLAPLPGmKGTDY 1066
Cdd:PHA02747     8 ECRAIDFLKRRNQLNCFGI---IRDE-HHQIILKPFDGLIANF--EKPENQPKNRYWDIPCWDHNRVILDSGGG-STSDY 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032733617 1067 INASYIMGYYRSNEFIITQHPLPHTTKDFWRMIWDHNAQIIVMLPDNQSLAEDE--FVYW-PSREESMNCEAFTVTLISK 1143
Cdd:PHA02747    81 IHANWIDGFEDDKKFIATQGPFAETCADFWKAVWQEHCSIIVMLTPTKGTNGEEkcYQYWcLNEDGNIDMEDFRIETLKT 160

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032733617 1144 DRLCLSNEEQIIIHDFILEATQddyvlEVRHFQCPKWPNPDAPISST-----FELINVIKEEALTRDG-------PTIVH 1211
Cdd:PHA02747   161 SVRAKYILTLIEITDKILKDSR-----KISHFQCSEWFEDETPSDHPdfikfIKIIDINRKKSGKLFNpkdallcPIVVH 235

                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2032733617 1212 DEYGAVSAGTLCALTTLSQQLENENAVDVFQVAKMINLMRPGVFTDIEQYQFL---YKAMLSLVSTKEN 1277
Cdd:PHA02747   236 CSDGVGKTGIFCAVDICLNQLVKRKAICLAKTAEKIREQRHAGIMNFDDYLFIqpgYEVLHYFLSKIKA 304
PHA02746 PHA02746
protein tyrosine phosphatase; Provisional
 1036-1268 6.10e-25

protein tyrosine phosphatase; Provisional


Pssm-ID: 165113 [Multi-domain]  Cd Length: 323  Bit Score: 107.42  E-value: 6.10e-25
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032733617 1036 NKEKNRNSSVVPSERARVGLAPLPGMKGTD-------------------YINASYIMGYYRSNEFIITQHPLPHTTKDFW 1096
Cdd:PHA02746    51 NLKKNRFHDIPCWDHSRVVINAHESLKMFDvgdsdgkkievtsednaenYIHANFVDGFKEANKFICAQGPKEDTSEDFF 130

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032733617 1097 RMIWDHNAQIIVMLPDNQSLAEDEFVYWPSREESMNCEAFTVTLISKDRLCLS-NEEQIIIHDFILEATQddyvlEVRHF 1175
Cdd:PHA02746   131 KLISEHESQVIVSLTDIDDDDEKCFELWTKEEDSELAFGRFVAKILDIIEELSfTKTRLMITDKISDTSR-----EIHHF 205

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032733617 1176 QCPKWP---NPDAPiSSTFELINVIKEEAL----------TRDGPTIVHDEYGAVSAGTLCALTTLSQQLENENAVDVFQ 1242
Cdd:PHA02746   206 WFPDWPdngIPTGM-AEFLELINKVNEEQAelikqadndpQTLGPIVVHCSAGIGRAGTFCAIDNALEQLEKEKEVCLGE 284

                          250       260
                   ....*....|....*....|....*.
gi 2032733617 1243 VAKMINLMRPGVFTDIEQYQFLYKAM 1268
Cdd:PHA02746   285 IVLKIRKQRHSSVFLPEQYAFCYKAL 310
R-PTPc-K-2 cd14636
PTP domain of receptor-type tyrosine-protein phosphatase K, repeat 2; Receptor-type ...
 1066-1269 7.94e-25

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: 103.57  E-value: 7.94e-25
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032733617 1066 YINASYIMGYYRSNEFIITQHPLPHTTKDFWRMIWDHNAQIIVMLpDNQSLAEDEFVYWPsrEESMnceaFTVTLISKDR 1145
Cdd:cd14636      1 YINAALMDSYRQPAAFIVTQHPLPNTVKDFWRLVYDYGCTSIVML-NEVDLAQGCPQYWP--EEGM----LRYGPIQVEC 73

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032733617 1146 LCLSNEEQIIIHDFI---LEATQDDYVLeVRHFQCPKWPNPDAPISSTFELINVI------KEEALTRDGPTIVHDEYGA 1216
Cdd:cd14636     74 MSCSMDCDVISRIFRicnLTRPQEGYLM-VQQFQYLGWASHREVPGSKRSFLKLIlqvekwQEECDEGEGRTIIHCLNGG 152

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|...
gi 2032733617 1217 VSAGTLCALTTLSQQLENENAVDVFQVAKMINLMRPGVFTDIEQYQFLYKAML 1269
Cdd:cd14636    153 GRSGMFCAISIVCEMIKRQNVVDVFHAVKTLRNSKPNMVETPEQYRFCYDVAL 205
R-PTPc-U-2 cd14637
PTP domain of receptor-type tyrosine-protein phosphatase U, repeat 2; Receptor-type ...
 767-979 1.38e-24

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: 103.06  E-value: 1.38e-24
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032733617  767 YINANYVDGYNKAKAYIATQGPLKSTFEDFWRMIWEQNTGIIVMITNLVEKGRR-KCDQYWPTENSEEYGNIIVTLKSTN 845
Cdd:cd14637      1 YINAALTDSYTRSAAFIVTLHPLQNTTTDFWRLVYDYGCTSVVMLNQLNQSNSAwPCLQYWPEPGLQQYGPMEVEFVSGS 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032733617  846 VHACYTVRRFTVRN-TKMKKGQkgnpkgrqneRTVIQYHYTQW-PDMGVPEYA---LPVLTFVRRSSaaRTPDMGPVVVH 920
Cdd:cd14637     81 ADEDIVTRLFRVQNiTRLQEGH----------LMVRHFQFLRWsAYRDTPDSKkafLHLLASVEKWQ--RESGEGRTVVH 148

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 2032733617  921 CSAGVGRTGTYIVIDSMLQQIKDKSTVNVLGFLKHIRTQRNYLVQTEEQYIFIHDALLE 979
Cdd:cd14637    149 CLNGGGRSGTYCASAMILEMIRCHNIVDVFYAVKTLRNYKPNMVETLEQYRFCYEIALE 207
R-PTPc-K-2 cd14636
PTP domain of receptor-type tyrosine-protein phosphatase K, repeat 2; Receptor-type ...
 767-979 1.60e-24

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


Pssm-ID: 350484 [Multi-domain]  Cd Length: 206  Bit Score: 102.80  E-value: 1.60e-24
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032733617  767 YINANYVDGYNKAKAYIATQGPLKSTFEDFWRMIWEQNTGIIVMITNL-VEKGrrkCDQYWPTENSEEYGNIIVTLKSTN 845
Cdd:cd14636      1 YINAALMDSYRQPAAFIVTQHPLPNTVKDFWRLVYDYGCTSIVMLNEVdLAQG---CPQYWPEEGMLRYGPIQVECMSCS 77

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032733617  846 VHACYTVRRFTVRNtkMKKGQKGnpkgrqnERTVIQYHYTQWPDM----GVPEYALPVLTFVRRSSAARTPDMGPVVVHC 921
Cdd:cd14636     78 MDCDVISRIFRICN--LTRPQEG-------YLMVQQFQYLGWASHrevpGSKRSFLKLILQVEKWQEECDEGEGRTIIHC 148

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 2032733617  922 SAGVGRTGTYIVIDSMLQQIKDKSTVNVLGFLKHIRTQRNYLVQTEEQYIFIHDALLE 979
Cdd:cd14636    149 LNGGGRSGMFCAISIVCEMIKRQNVVDVFHAVKTLRNSKPNMVETPEQYRFCYDVALE 206
R-PTPc-R cd14611
catalytic domain of receptor-type tyrosine-protein phosphatase R; Receptor-type ...
 1039-1265 1.71e-24

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: 103.46  E-value: 1.71e-24
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032733617 1039 KNRNSSVVPSERARVGLAPL-PGMKGTDYINASYIMGYY-RSNEFIITQHPLPHTTKDFWRMIWDHNAQIIVMLPDNQSL 1116
Cdd:cd14611      2 KNRYKTILPNPHSRVCLKPKnSNDSLSTYINANYIRGYGgKEKAFIATQGPMINTVNDFWQMVWQEDSPVIVMITKLKEK 81

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032733617 1117 AEDEFVYWPSREESMNCEAFTVTliskdrlCLSNEEQIIIHDFILEatQDDYVLEVRHFQCPKWPNPDAPISST--FELI 1194
Cdd:cd14611     82 NEKCVLYWPEKRGIYGKVEVLVN-------SVKECDNYTIRNLTLK--QGSQSRSVKHYWYTSWPDHKTPDSAQplLQLM 152

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2032733617 1195 NVIKEEAL--TRDGPTIVHDEYGAVSAGTLCALTTLSQQLENENAVDVFQVAKMINLMRPGVFTDIEQYQFLY 1265
Cdd:cd14611    153 LDVEEDRLasPGRGPVVVHCSAGIGRTGCFIATTIGCQQLKEEGVVDVLSIVCQLRVDRGGMVQTSEQYEFVH 225
PTPc-N20_13 cd14538
catalytic domain of tyrosine-protein phosphatase non-receptor type 20 and type 13; ...
 1066-1269 1.79e-24

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: 102.84  E-value: 1.79e-24
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032733617 1066 YINASYIM-----GYYRsneFIITQHPLPHTTKDFWRMIWDHNAQIIVMLPDNqslAEDEFV----YWP-SREESMNCEA 1135
Cdd:cd14538      1 YINASHIRipvggDTYH---YIACQGPLPNTTGDFWQMVWEQKSEVIAMVTQD---VEGGKVkchrYWPdSLNKPLICGG 74

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032733617 1136 -FTVTLISKDRLclsneEQIIIHDFILEATQDDYVLEVRHFQCPKWPNPDAPiSSTFELINVIKE-EALTRDGPTIVHDE 1213
Cdd:cd14538     75 rLEVSLEKYQSL-----QDFVIRRISLRDKETGEVHHITHLNFTTWPDHGTP-QSADPLLRFIRYmRRIHNSGPIVVHCS 148

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 2032733617 1214 YGAVSAGTLCALTTLSQQLENENAVDVFQVAKMINLMRPGVFTDIEQYQFLYKAML 1269
Cdd:cd14538    149 AGIGRTGVLITIDVALGLIERDLPFDIQDIVKDLREQRQGMIQTKDQYIFCYKACL 204
PTPc-N11_6 cd14544
catalytic domain of tyrosine-protein phosphatase non-receptor type 11 and type 6; ...
 1036-1268 2.00e-24

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: 103.70  E-value: 2.00e-24
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032733617 1036 NKEKNRNSSVVPSERARVGLAPL-PGMKGTDYINASYIM-----GYYRSNE--FIITQHPLPHTTKDFWRMIWDHNAQII 1107
Cdd:cd14544      1 NKGKNRYKNILPFDHTRVILKDRdPNVPGSDYINANYIRnenegPTTDENAktYIATQGCLENTVSDFWSMVWQENSRVI 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032733617 1108 VMLPDNQSLAEDEFV-YWPsreESMNCEAFtvtliskDRLCLSNEEQIIIHDFIL------EATQDDYVLEVRHFQCPKW 1180
Cdd:cd14544     81 VMTTKEVERGKNKCVrYWP---DEGMQKQY-------GPYRVQNVSEHDTTDYTLrelqvsKLDQGDPIREIWHYQYLSW 150

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032733617 1181 PN---PDAP--ISSTFELINViKEEALTRDGPTIVHDEYGAVSAGTLCALTTLSQQLENEN---AVDVFQVAKMINLMRP 1252
Cdd:cd14544    151 PDhgvPSDPggVLNFLEDVNQ-RQESLPHAGPIVVHCSAGIGRTGTFIVIDMLLDQIKRKGldcDIDIQKTIQMVRSQRS 229

                          250
                   ....*....|....*.
gi 2032733617 1253 GVFTDIEQYQFLYKAM 1268
Cdd:cd14544    230 GMVQTEAQYKFIYVAV 245
PTPc-N3 cd14600
catalytic domain of tyrosine-protein phosphatase non-receptor type 3; Tyrosine-protein ...
 1036-1269 4.43e-24

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: 103.39  E-value: 4.43e-24
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032733617 1036 NKEKNRNSSVVPSERARVGLAplpgmKGTDYINASY----IMGYYRSNEFIITQHPLPHTTKDFWRMIWDHNAQIIVMLp 1111
Cdd:cd14600     40 NMDKNRYKDVLPYDATRVVLQ-----GNEDYINASYvnmeIPSANIVNKYIATQGPLPHTCAQFWQVVWEQKLSLIVML- 113

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032733617 1112 dnQSLAEDEFV----YWPSREESMNCEAFTVTliskdrlCLSNEEQI--IIHDFILEATQDDYVLEVRHFQCPKWPNPDA 1185
Cdd:cd14600    114 --TTLTERGRTkchqYWPDPPDVMEYGGFRVQ-------CHSEDCTIayVFREMLLTNTQTGEERTVTHLQYVAWPDHGV 184

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032733617 1186 PISST--FELINVIKEEALTRDgPTIVHDEYGAVSAGTLCALTTLSQQLENENAVDVFQVAKMINLMRPGVFTDIEQYQF 1263
Cdd:cd14600    185 PDDSSdfLEFVNYVRSKRVENE-PVLVHCSAGIGRTGVLVTMETAMCLTERNQPVYPLDIVRKMRDQRAMMVQTSSQYKF 263


                   ....*.
gi 2032733617 1264 LYKAML 1269
Cdd:cd14600    264 VCEAIL 269
PTPc-N13 cd14597
catalytic domain of tyrosine-protein phosphatase non-receptor type 13; Tyrosine-protein ...
 1036-1269 1.36e-23

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: 101.06  E-value: 1.36e-23
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032733617 1036 NKEKNRNSSVVPSERARVGLaplpGMKGtDYINASYIMGYYRSNEF--IITQHPLPHTTKDFWRMIWDHNAQIIVMLPDN 1113
Cdd:cd14597      3 NRKKNRYKNILPYDTTRVPL----GDEG-GYINASFIKMPVGDEEFvyIACQGPLPTTVADFWQMVWEQKSTVIAMMTQE 77

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032733617 1114 qslAEDEFV----YWPsreesmncEAFTVTLISKDRLCLS-----NEEQIIIHDFILEATQDDYVLEVRHFQCPKWPNPD 1184
Cdd:cd14597     78 ---VEGGKIkcqrYWP--------EILGKTTMVDNRLQLTlvrmqQLKNFVIRVLELEDIQTREVRHITHLNFTAWPDHD 146

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032733617 1185 APiSSTFELINVIK-EEALTRDGPTIVHDEYGAVSAGTL-C---ALTTLSQQLEnenaVDVFQVAKMINLMRPGVFTDIE 1259
Cdd:cd14597    147 TP-SQPEQLLTFISyMRHIHKSGPIITHCSAGIGRSGTLiCidvVLGLISKDLD----FDISDIVRTMRLQRHGMVQTED 221

                          250
                   ....*....|
gi 2032733617 1260 QYQFLYKAML 1269
Cdd:cd14597    222 QYIFCYQVIL 231
PTPc-N3_4 cd14541
catalytic domain of tyrosine-protein phosphatase non-receptor type 21 and type 14; ...
 1065-1270 5.52e-23

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: 98.56  E-value: 5.52e-23
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032733617 1065 DYINASYI-MGYYRS---NEFIITQHPLPHTTKDFWRMIWDHNAQIIVMLpdnQSLAEDEFV----YWPSREESMNCEAF 1136
Cdd:cd14541      1 DYINANYVnMEIPGSgivNRYIAAQGPLPNTCADFWQMVWEQKSTLIVML---TTLVERGRVkchqYWPDLGETMQFGNL 77

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032733617 1137 TVTliskdrlCLSNEEQI--IIHDFILEATQDDYVLEVRHFQCPKWPNPDAPISSTfELINVIKEEALTRDG---PTIVH 1211
Cdd:cd14541     78 QIT-------CVSEEVTPsfAFREFILTNTNTGEERHITQMQYLAWPDHGVPDDSS-DFLDFVKRVRQNRVGmvePTVVH 149

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 2032733617 1212 DEYGAVSAGTLCALTTLSQQLENENAVDVFQVAKMINLMRPGVFTDIEQYQFLYKAMLS 1270
Cdd:cd14541    150 CSAGIGRTGVLITMETAMCLIEANEPVYPLDIVRTMRDQRAMLIQTPSQYRFVCEAILR 208
R-PTP-Z-2 cd17669
catalytic domain of receptor-type tyrosine-protein phosphatase Z, repeat 2; Receptor-type ...
 767-978 5.93e-23

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: 98.14  E-value: 5.93e-23
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032733617  767 YINANYVDGYNKAKAYIATQGPLKSTFEDFWRMIWEQNTGIIVMITNLVEKGRRKCdQYWPteNSEEYGN---IIVTLKS 843
Cdd:cd17669      1 YINASYIMGYYQSNEFIITQHPLLHTIKDFWRMIWDHNAQLIVMLPDGQNMAEDEF-VYWP--NKDEPINcetFKVTLIA 77

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032733617  844 TNvHACYT------VRRFTVRNTkmkkgqkgnpkgrQNERTVIQYHYT--QWPDMGVP-EYALPVLTFVRRSSAARTpdm 914
Cdd:cd17669     78 EE-HKCLSneekliIQDFILEAT-------------QDDYVLEVRHFQcpKWPNPDSPiSKTFELISIIKEEAANRD--- 140

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2032733617  915 GPVVVHCSAGVGRTGTYIVIDSMLQQIKDKSTVNVLGFLKHIRTQRNYLVQTEEQYIFIHDALL 978
Cdd:cd17669    141 GPMIVHDEHGGVTAGTFCALTTLMHQLEKENSVDVYQVAKMINLMRPGVFTDIEQYQFLYKAIL 204
PHA02738 PHA02738
hypothetical protein; Provisional
 1029-1268 6.91e-23

hypothetical protein; Provisional


Pssm-ID: 222923 [Multi-domain]  Cd Length: 320  Bit Score: 101.15  E-value: 6.91e-23
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032733617 1029 FSAQKDcNKEKNRNSSVVPSERARVGLaPLPGMKGtDYINASYIMGYYRSNEFIITQHPLPHTTKDFWRMIWDHNAQIIV 1108
Cdd:PHA02738    43 FNAEKK-NRKLNRYLDAVCFDHSRVIL-PAERNRG-DYINANYVDGFEYKKKFICGQAPTRQTCYDFYRMLWMEHVQIIV 119

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032733617 1109 ML-PDNQSLAEDEFVYWPSREE-SMNCEAFTVTLISKDRLCLSNEEQIIIHDFIlEATQddyvlEVRHFQCPKWPNPDAP 1186
Cdd:PHA02738   120 MLcKKKENGREKCFPYWSDVEQgSIRFGKFKITTTQVETHPHYVKSTLLLTDGT-SATQ-----TVTHFNFTAWPDHDVP 193

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032733617 1187 iSSTFELINVI----------KEEAL------TRDGPTIVHDEYGAVSAGTLCALTTLSQQLENENAVDVFQVAKMINLM 1250
Cdd:PHA02738   194 -KNTSEFLNFVlevrqcqkelAQESLqighnrLQPPPIVVHCNAGLGRTPCYCVVDISISRFDACATVSIPSIVSSIRNQ 272

                          250
                   ....*....|....*...
gi 2032733617 1251 RPGVFTDIEQYQFLYKAM 1268
Cdd:PHA02738   273 RYYSLFIPFQYFFCYRAV 290
PTPc-N6 cd14606
catalytic domain of tyrosine-protein phosphatase non-receptor type 6; Tyrosine-protein ...
 1032-1274 1.89e-22

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: 98.41  E-value: 1.89e-22
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032733617 1032 QKDCNKEKNRNSSVVPSERARVGLAPL-PGMKGTDYINASYIMGYYRSNE-----FIITQHPLPHTTKDFWRMIWDHNAQ 1105
Cdd:cd14606     14 QRPENKSKNRYKNILPFDHSRVILQGRdSNIPGSDYINANYVKNQLLGPDenaktYIASQGCLEATVNDFWQMAWQENSR 93

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032733617 1106 IIVMLPDNQSLAEDEFV-YWPSREESMNCEAFTVTLIS-------KDR-LCLSneeqiIIHDfileatqDDYVLEVRHFQ 1176
Cdd:cd14606     94 VIVMTTREVEKGRNKCVpYWPEVGMQRAYGPYSVTNCGehdtteyKLRtLQVS-----PLDN-------GELIREIWHYQ 161

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032733617 1177 CPKWPNPDAP-----ISSTFELINViKEEALTRDGPTIVHDEYGAVSAGTLCALTTLSQQLENENA---VDVFQVAKMIN 1248
Cdd:cd14606    162 YLSWPDHGVPsepggVLSFLDQINQ-RQESLPHAGPIIVHCSAGIGRTGTIIVIDMLMENISTKGLdcdIDIQKTIQMVR 240

                          250       260
                   ....*....|....*....|....*.
gi 2032733617 1249 LMRPGVFTDIEQYQFLYKAMLSLVST 1274
Cdd:cd14606    241 AQRSGMVQTEAQYKFIYVAIAQFIET 266
R-PTPc-M-2 cd14635
PTP domain of receptor-type tyrosine-protein phosphatase M, repeat 2; Receptor-type ...
 767-979 2.26e-22

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: 96.68  E-value: 2.26e-22
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032733617  767 YINANYVDGYNKAKAYIATQGPLKSTFEDFWRMIWEQNTGIIVMITNLveKGRRKCDQYWPTENSEEYGNIIVTLKSTNV 846
Cdd:cd14635      1 YINAALMDSYKQPSAFIVTQHPLPNTVKDFWRLVLDYHCTSIVMLNDV--DPAQLCPQYWPENGVHRHGPIQVEFVSADL 78

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032733617  847 HACYTVRRFTVRNTKmkkgqkgnpKGRQNERTVIQYHYTQWPDM-GVPEYALPVLTFVRRSSAARTP---DMGPVVVHCS 922
Cdd:cd14635     79 EEDIISRIFRIYNAA---------RPQDGYRMVQQFQFLGWPMYrDTPVSKRSFLKLIRQVDKWQEEyngGEGRTVVHCL 149

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 2032733617  923 AGVGRTGTYIVIDSMLQQIKDKSTVNVLGFLKHIRTQRNYLVQTEEQYIFIHDALLE 979
Cdd:cd14635    150 NGGGRSGTFCAISIVCEMLRHQRAVDVFHAVKTLRNNKPNMVDLLDQYKFCYEVALE 206
R-PTPc-C-1 cd14557
catalytic domain of receptor-type tyrosine-protein phosphatase C, repeat 1; Receptor-type ...
 1066-1266 2.41e-22

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: 96.43  E-value: 2.41e-22
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032733617 1066 YINASYIMGYYRSNEFIITQHPLPHTTKDFWRMIWDHNAQIIVMLPDNQSLAEDE-FVYWPSREESMNCEAFTVTLISKD 1144
Cdd:cd14557      1 YINASYIDGFKEPRKYIAAQGPKDETVDDFWRMIWEQKSTVIVMVTRCEEGNRNKcAQYWPSMEEGSRAFGDVVVKINEE 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032733617 1145 RLClsnEEQIIIHDFILEATQDDYVLEVRHFQCPKWPNPDAPISSTFELINVIKEEALTR--DGPTIVHDEYGAVSAGTL 1222
Cdd:cd14557     81 KIC---PDYIIRKLNINNKKEKGSGREVTHIQFTSWPDHGVPEDPHLLLKLRRRVNAFNNffSGPIVVHCSAGVGRTGTY 157

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....
gi 2032733617 1223 CALTTLSQQLENENAVDVFQVAKMINLMRPGVFTDIEQYQFLYK 1266
Cdd:cd14557    158 IGIDAMLEGLEAEGRVDVYGYVVKLRRQRCLMVQVEAQYILIHQ 201
R-PTP-G-2 cd17670
PTP-like domain of receptor-type tyrosine-protein phosphatase G, repeat 2; Receptor-type ...
 767-978 4.74e-22

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


Pssm-ID: 350508 [Multi-domain]  Cd Length: 205  Bit Score: 95.52  E-value: 4.74e-22
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032733617  767 YINANYVDGYNKAKAYIATQGPLKSTFEDFWRMIWEQNTGIIVMITN---LVEkgrrkcDQ--YWPT-ENSEEYGNIIVT 840
Cdd:cd17670      1 YINASYIMGYYRSNEFIITQHPLPHTTKDFWRMIWDHNAQIIVMLPDnqgLAE------DEfvYWPSrEESMNCEAFTVT 74

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032733617  841 LKSTNVHACYTVRRFTVRNTKMKKGQkgnpkgrqnERTVIQYHYTQ---WPDMGVP-EYALPVLTFVRRSSAARTpdmGP 916
Cdd:cd17670     75 LISKDRLCLSNEEQIIIHDFILEATQ---------DDYVLEVRHFQcpkWPNPDAPiSSTFELINVIKEEALTRD---GP 142

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2032733617  917 VVVHCSAGVGRTGTYIVIDSMLQQIKDKSTVNVLGFLKHIRTQRNYLVQTEEQYIFIHDALL 978
Cdd:cd17670    143 TIVHDEFGAVSAGTLCALTTLSQQLENENAVDVYQVAKMINLMRPGVFTDIEQYQFLYKAML 204
PTPc-N14 cd14599
catalytic domain of tyrosine-protein phosphatase non-receptor type 14; Tyrosine-protein ...
 1036-1272 5.18e-22

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: 97.76  E-value: 5.18e-22
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032733617 1036 NKEKNRNSSVVPSERARVGLAPLPgMKGTDYINASYIMGYYRSNE--FIITQHPLPHTTKDFWRMIWDHNAQIIVMLPdn 1113
Cdd:cd14599     38 NAERNRIREVVPYEENRVELVPTK-ENNTGYINASHIKVTVGGEEwhYIATQGPLPHTCHDFWQMVWEQGVNVIAMVT-- 114

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032733617 1114 qslAEDE------FVYWP---SREESMNCEAFTVTL-ISKDRLCLSNEEQIIIHdfiLEATQDDYVLevrHFQCPKWPNP 1183
Cdd:cd14599    115 ---AEEEggrsksHRYWPklgSKHSSATYGKFKVTTkFRTDSGCYATTGLKVKH---LLSGQERTVW---HLQYTDWPDH 185

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032733617 1184 DAP------------ISSTFELINVIKEEALTRDGPTIVHDEYGAVSAGTLCALTTLSQQLENENAVDVFQVAKMINLMR 1251
Cdd:cd14599    186 GCPeevqgflsyleeIQSVRRHTNSMLDSTKNCNPPIVVHCSAGVGRTGVVILTELMIGCLEHNEKVEVPVMLRHLREQR 265

                          250       260
                   ....*....|....*....|.
gi 2032733617 1252 PGVFTDIEQYQFLYKAMLSLV 1272
Cdd:cd14599    266 MFMIQTIAQYKFVYQVLIQFL 286
PTP-N23 cd14539
PTP-like domain of tyrosine-protein phosphatase non-receptor type 23; Tyrosine-protein ...
 1066-1266 5.96e-22

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: 95.14  E-value: 5.96e-22
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032733617 1066 YINASYIMGYYR-SNEFIITQHPLPHTTKDFWRMIWDHNAQIIVMLPDNQSLAEDEFV-YWPS-REESMNCEAFTVTLIS 1142
Cdd:cd14539      1 YINASLIEDLTPyCPRFIATQAPLPGTAADFWLMVYEQQVSVIVMLVSEQENEKQKVHrYWPTeRGQALVYGAITVSLQS 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032733617 1143 KDRLCLSNEEQIII--HDFILEATqddyvleVRHFQCPKWP---NPDAPiSSTFELINVIKEEALTRDG---PTIVHDEY 1214
Cdd:cd14539     81 VRTTPTHVERIISIqhKDTRLSRS-------VVHLQFTTWPelgLPDSP-NPLLRFIEEVHSHYLQQRSlqtPIVVHCSS 152

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|...
gi 2032733617 1215 GAVSAGTLCALTTLSQQLENENAV-DVFQVAKMINLMRPGVFTDIEQYQFLYK 1266
Cdd:cd14539    153 GVGRTGAFCLLYAAVQEIEAGNGIpDLPQLVRKMRQQRKYMLQEKEHLKFCYE 205
R-PTPc-A-E-1 cd14551
catalytic domain of receptor-type tyrosine-protein phosphatase A and E, repeat 1; ...
 1066-1266 1.03e-21

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: 94.59  E-value: 1.03e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032733617 1066 YINASYIMGYYRSNEFIITQHPLPHTTKDFWRMIWDHNAQIIVMLPDNQSLAEDEFV-YWPSReesmNCEAFtvtliSKD 1144
Cdd:cd14551      1 YINASYIDGYQEKNKFIAAQGPKDETVNDFWRMIWEQGSATIVMVTNLKERKEKKCSqYWPDQ----GCWTY-----GNL 71

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032733617 1145 RLCLSNEEQIIIH---DFILEATQDDY----VLEVRHFQCPKWPN---PDAPIsSTFELINVIKEEALTRDGPTIVHDEY 1214
Cdd:cd14551     72 RVRVEDTVVLVDYttrKFCIQKVNRGIgekrVRLVTQFHFTSWPDfgvPFTPI-GMLKFLKKVKSANPPRAGPIVVHCSA 150

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|..
gi 2032733617 1215 GAVSAGTLCALTTLSQQLENENAVDVFQVAKMINLMRPGVFTDIEQYQFLYK 1266
Cdd:cd14551    151 GVGRTGTFIVIDAMLDMMHAEGKVDVFGFVSRIRQQRSQMVQTDMQYVFIYQ 202
PTPc-N11 cd14605
catalytic domain of tyrosine-protein phosphatase non-receptor type 11; Tyrosine-protein ...
 1036-1274 1.06e-21

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: 95.85  E-value: 1.06e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032733617 1036 NKEKNRNSSVVPSERARVGLAP-LPGMKGTDYINASYIMGYYRSN--------EFIITQHPLPHTTKDFWRMIWDHNAQI 1106
Cdd:cd14605      2 NKNKNRYKNILPFDHTRVVLHDgDPNEPVSDYINANIIMPEFETKcnnskpkkSYIATQGCLQNTVNDFWRMVFQENSRV 81

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032733617 1107 IVMLPDNQSLAEDEFV-YWPsreESMNCEAFTVTLIskdrlclSNEEQIIIHDFIL------EATQDDYVLEVRHFQCPK 1179
Cdd:cd14605     82 IVMTTKEVERGKSKCVkYWP---DEYALKEYGVMRV-------RNVKESAAHDYILrelklsKVGQGNTERTVWQYHFRT 151

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032733617 1180 WPNPDAP-----ISSTFELINvIKEEALTRDGPTIVHDEYGAVSAGTLCALTTLSQQLENENA---VDVFQVAKMINLMR 1251
Cdd:cd14605    152 WPDHGVPsdpggVLDFLEEVH-HKQESIMDAGPVVVHCSAGIGRTGTFIVIDILIDIIREKGVdcdIDVPKTIQMVRSQR 230

                          250       260
                   ....*....|....*....|...
gi 2032733617 1252 PGVFTDIEQYQFLYKAMLSLVST 1274
Cdd:cd14605    231 SGMVQTEAQYRFIYMAVQHYIET 253
PTPc-N2 cd14607
catalytic domain of tyrosine-protein phosphatase non-receptor type 2; Tyrosine-protein ...
 1023-1268 1.39e-21

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: 95.80  E-value: 1.39e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032733617 1023 AKYVEcfsaqkdcNKEKNRNSSVVPSERARVGLAPLPgmkgTDYINASYIMGYYRSNEFIITQHPLPHTTKDFWRMIWDH 1102
Cdd:cd14607     19 AKYPE--------NRNRNRYRDVSPYDHSRVKLQNTE----NDYINASLVVIEEAQRSYILTQGPLPNTCCHFWLMVWQQ 86

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032733617 1103 NAQIIVMLpdnQSLAEDEFV----YWPSREESM---NCEAFTVTLISKDRlclsnEEQIIIHDFILEATQDDYVLEVRHF 1175
Cdd:cd14607     87 KTKAVVML---NRIVEKDSVkcaqYWPTDEEEVlsfKETGFSVKLLSEDV-----KSYYTVHLLQLENINSGETRTISHF 158

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032733617 1176 QCPKWPN---PDAPISSTFELINVIKEEALTRD-GPTIVHDEYGAVSAGTLCALTTLSQQLENEN--AVDVFQVAKMINL 1249
Cdd:cd14607    159 HYTTWPDfgvPESPASFLNFLFKVRESGSLSPEhGPAVVHCSAGIGRSGTFSLVDTCLVLMEKKDpdSVDIKQVLLDMRK 238

                          250
                   ....*....|....*....
gi 2032733617 1250 MRPGVFTDIEQYQFLYKAM 1268
Cdd:cd14607    239 YRMGLIQTPDQLRFSYMAV 257
R-PTP-N-N2 cd14546
PTP-like domain of receptor-type tyrosine-protein phosphatase-like N and N2; Receptor-type ...
 1066-1267 7.10e-21

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: 92.12  E-value: 7.10e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032733617 1066 YINASYIMGYY-RSNEFIITQHPLPHTTKDFWRMIWDHNAQIIVMLPDNQSLAEDEFV-YWPsrEESMNC-EAFTVTLIS 1142
Cdd:cd14546      1 YINASTIYDHDpRNPAYIATQGPLPHTIADFWQMIWEQGCVVIVMLTRLQENGVKQCArYWP--EEGSEVyHIYEVHLVS 78

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032733617 1143 KDRLClsneEQIIIHDFILEATQDDYVLEVRHFQCPKWPNPDAPISST--FELINVIKEEALTRDGPTIVHDEYGAVSAG 1220
Cdd:cd14546     79 EHIWC----DDYLVRSFYLKNLQTSETRTVTQFHFLSWPDEGIPASAKplLEFRRKVNKSYRGRSCPIVVHCSDGAGRTG 154

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*...
gi 2032733617 1221 TLCAL-TTLSQQLENENAVDVFQVAKMINLMRPGVFTDIEQYQFLYKA 1267
Cdd:cd14546    155 TYILIdMVLNRMAKGAKEIDIAATLEHLRDQRPGMVKTKDQFEFVLTA 202
PTPc-N20 cd14596
catalytic domain of tyrosine-protein phosphatase non-receptor type 20; Tyrosine-protein ...
 1066-1269 2.61e-20

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: 90.58  E-value: 2.61e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032733617 1066 YINASYIMGYYRSNE--FIITQHPLPHTTKDFWRMIWDHNAQIIVMLPDNQSLAEDE-FVYWP-SREESMNCEAFTVTLI 1141
Cdd:cd14596      1 YINASYITMPVGEEElfYIATQGPLPSTIDDFWQMVWENRSDVIAMMTREVERGKVKcHRYWPeTLQEPMELENYQLRLE 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032733617 1142 SKDRLclsneEQIIIHDFILEATQDDYVLEVRHFQCPKWPNPDAPISSTfELINVIK-EEALTRDGPTIVHDEYGAVSAG 1220
Cdd:cd14596     81 NYQAL-----QYFIIRIIKLVEKETGENRLIKHLQFTTWPDHGTPQSSD-QLVKFICyMRKVHNTGPIVVHCSAGIGRAG 154

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*....
gi 2032733617 1221 TLCALTTLSQQLENENAVDVFQVAKMINLMRPGVFTDIEQYQFLYKAML 1269
Cdd:cd14596    155 VLICVDVLLSLIEKDLSFNIKDIVREMRQQRYGMIQTKDQYLFCYKVVL 203
PTPc-N21_14 cd14540
catalytic domain of tyrosine-protein phosphatase non-receptor type 21 and type 14; ...
 1066-1269 4.86e-19

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: 87.13  E-value: 4.86e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032733617 1066 YINASYIMGYYRSNE--FIITQHPLPHTTKDFWRMIWDHNAQIIVMLPDNQSLA-EDEFVYWP---SREESMNCEAFTVT 1139
Cdd:cd14540      1 YINASHITATVGGKQrfYIAAQGPLQNTVGDFWQMVWEQGVYLVVMVTAEEEGGrEKCFRYWPtlgGEHDALTFGEYKVS 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032733617 1140 L-ISKDRLCLsneeqiIIHDFILEATQDDYVLEVRHFQCPKWPN---PDAPIS--STFELINVIKEEAL------TRDGP 1207
Cdd:cd14540     81 TkFSVSSGCY------TTTGLRVKHTLSGQSRTVWHLQYTDWPDhgcPEDVSGflDFLEEINSVRRHTNqdvaghNRNPP 154

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2032733617 1208 TIVHDEYGAVSAGTLCALTTLSQQLENENAVDVFQVAKMINLMRPGVFTDIEQYQFLYKAML 1269
Cdd:cd14540    155 TLVHCSAGVGRTGVVILADLMLYCLDHNEELDIPRVLALLRHQRMLLVQTLAQYKFVYNVLI 216
PHA02742 PHA02742
protein tyrosine phosphatase; Provisional
 1011-1275 5.78e-19

protein tyrosine phosphatase; Provisional


Pssm-ID: 165109 [Multi-domain]  Cd Length: 303  Bit Score: 89.29  E-value: 5.78e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032733617 1011 LEKQFKLVTQCNAKYvECFSAQKDCNKEKNRNSSVVPSERARVGLAPLPGmkGTDYINASYIMGYYRSNEFIITQHPLPH 1090
Cdd:PHA02742    28 LKEEHEHIMQEIVAF-SCNESLELKNMKKCRYPDAPCFDRNRVILKIEDG--GDDFINASYVDGHNAKGRFICTQAPLEE 104

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032733617 1091 TTKDFWRMIWDHNAQIIVMLP----DNQslaEDEFVYWPSREESMNCEA-FTV-TLISKD-------RLCLSNeeqiiih 1157
Cdd:PHA02742   105 TALDFWQAIFQDQVRVIVMITkimeDGK---EACYPYWMPHERGKATHGeFKIkTKKIKSfrnyavtNLCLTD------- 174

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032733617 1158 dfileaTQDDYVLEVRHFQCPKWPNPDAP--ISSTFELINVIKEEALTRD-----------GPTIVHDEYGAVSAGTLCA 1224
Cdd:PHA02742   175 ------TNTGASLDIKHFAYEDWPHGGLPrdPNKFLDFVLAVREADLKADvdikgenivkePPILVHCSAGLDRAGAFCA 248

                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 2032733617 1225 LtTLSQQLENENA-VDVFQVAKMINLMRPGVFTDIEQYQFLYKAML---SLVSTK 1275
Cdd:PHA02742   249 I-DICISKYNERAiIPLLSIVRDLRKQRHNCLSLPQQYIFCYFIVLifaKLMADK 302
PHA02740 PHA02740
protein tyrosine phosphatase; Provisional
 730-977 1.65e-17

protein tyrosine phosphatase; Provisional


Pssm-ID: 165107 [Multi-domain]  Cd Length: 298  Bit Score: 84.63  E-value: 1.65e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032733617  730 SNHPDNKHK--NRYINILAYDHSRVKLRplpgKDSKhsdYINANYVDGYNKAKAYIATQGPLKSTFEDFWRMIWEQNTGI 807
Cdd:PHA02740    46 CAQAENKAKdeNLALHITRLLHRRIKLF----NDEK---VLDARFVDGYDFEQKFICIINLCEDACDKFLQALSDNKVQI 118

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032733617  808 IVMITNLVEKgrrKC-DQYWPTENS--EEYGNI-IVTLK-STNVHACYTVRRFTvrntkMKKGQkgnpkgrqnERTVIQY 882
Cdd:PHA02740   119 IVLISRHADK---KCfNQFWSLKEGcvITSDKFqIETLEiIIKPHFNLTLLSLT-----DKFGQ---------AQKISHF 181

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032733617  883 HYTQWPDMGVPEYALPVLTF----------VRRSSAARtpDMGPVVVHCSAGVGRTGTYIVIDSMLQQIKDKSTVNVLGF 952
Cdd:PHA02740   182 QYTAWPADGFSHDPDAFIDFfcniddlcadLEKHKADG--KIAPIIIDCIDGISSSAVFCVFDICATEFDKTGMLSIANA 259

                          250       260
                   ....*....|....*....|....*
gi 2032733617  953 LKHIRTQRNYLVQTEEQYIFIHDAL 977
Cdd:PHA02740   260 LKKVRQKKYGCMNCLDDYVFCYHLI 284
PTPc-N4 cd14601
catalytic domain of tyrosine-protein phosphatase non-receptor type 4; Tyrosine-protein ...
 1065-1269 9.03e-17

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: 80.37  E-value: 9.03e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032733617 1065 DYINASYIMGYYRS----NEFIITQHPLPHTTKDFWRMIWDHNAQIIVMLPDNQSLAEDE-FVYWPSREESMNCEAFTVT 1139
Cdd:cd14601      1 DYINANYINMEIPSssiiNRYIACQGPLPNTCSDFWQMTWEQGSSMVVMLTTQVERGRVKcHQYWPEPSGSSSYGGFQVT 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032733617 1140 liskdrlCLSNE--EQIIIHDFILEATQDDYVLEVRHFQCPKWPNPDAPISST--FELINVIKEEALTRDGPTIVHDEYG 1215
Cdd:cd14601     81 -------CHSEEgnPAYVFREMTLTNLEKNESRPLTQIQYIAWPDHGVPDDSSdfLDFVCLVRNKRAGKDEPVVVHCSAG 153

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....
gi 2032733617 1216 AVSAGTLCALTTLSQQLENENAVDVFQVAKMINLMRPGVFTDIEQYQFLYKAML 1269
Cdd:cd14601    154 IGRTGVLITMETAMCLIECNQPVYPLDIVRTMRDQRAMMIQTPSQYRFVCEAIL 207
PTPc_plant_PTP1 cd17658
protein tyrosine phosphatase 1 from Arabidopsis thaliana and similar plant PTPs; Arabidopsis ...
 1066-1265 1.20e-16

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: 79.82  E-value: 1.20e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032733617 1066 YINASYIMGYYRSN--EFIITQHPLPHTTKDFWRMIWDHNAQIIVMLP---DNQSLAEDEFVYWPSREESMNCEAFTVTL 1140
Cdd:cd17658      1 YINASLVETPASESlpKFIATQGPLPHTFEDFWEMVIQQRCPVIIMLTrlvDNYSTAKCADYFPAEENESREFGRISVTN 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032733617 1141 ISkdrlcLSNEEQIIIHDFiLEATQ---DDYVLEVRHFQCPKWPNPDAPiSSTFELINVIKEEALTRD--GPTIVHDEYG 1215
Cdd:cd17658     81 KK-----LKHSQHSITLRV-LEVQYiesEEPPLSVLHIQYPEWPDHGVP-KDTRSVRELLKRLYGIPPsaGPIVVHCSAG 153

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|..
gi 2032733617 1216 AVSAGTLCAL-TTLSQQLENE-NAVDVFQVAKMINLMRPGVFTDIEQYQFLY 1265
Cdd:cd17658    154 IGRTGAYCTIhNTIRRILEGDmSAVDLSKTVRKFRSQRIGMVQTQDQYIFCY 205
PTPc-N21 cd14598
catalytic domain of tyrosine-protein phosphatase non-receptor type 21; Tyrosine-protein ...
 1066-1272 2.35e-16

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: 79.63  E-value: 2.35e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032733617 1066 YINASYIMGYYRSNE--FIITQHPLPHTTKDFWRMIWDHNAQIIVMLP-DNQSLAEDEFVYWP---SREESMNCEAFTVT 1139
Cdd:cd14598      1 YINASHIKVTVGGKEwdYIATQGPLQNTCQDFWQMVWEQGVAIIAMVTaEEEGGREKSFRYWPrlgSRHNTVTYGRFKIT 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032733617 1140 L-ISKDRLCLSNEEQIIIHdfiLEATQDDYVLevrHFQCPKWPNPDAP------ISSTFELINVIKEEALTRD-----GP 1207
Cdd:cd14598     81 TrFRTDSGCYATTGLKIKH---LLTGQERTVW---HLQYTDWPEHGCPedlkgfLSYLEEIQSVRRHTNSTIDpkspnPP 154

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2032733617 1208 TIVHDEYGAVSAGTLCALTTLSQQLENENAVDVFQVAKMINLMRPGVFTDIEQYQFLYKAMLSLV 1272
Cdd:cd14598    155 VLVHCSAGVGRTGVVILSEIMIACLEHNEMLDIPRVLDMLRQQRMMMVQTLSQYTFVYKVLIQFL 219
PTP_YopH-like cd14559
YopH and related bacterial protein tyrosine phosphatases; Yersinia outer protein H (YopH) ...
 739-979 9.47e-15

YopH and related bacterial protein tyrosine phosphatases; Yersinia outer protein H (YopH) belongs to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. YopH is an essential virulence determinant of the pathogenic bacterium by dephosphorylating several focal adhesion proteins including p130Cas in human epithelial cells, resulting in the disruption of focal adhesions and cell detachment from the extracellular matrix. It contains an N-terminal domain that contains signals required for TTSS-mediated delivery of YopH into host cells and a C-terminal catalytic PTP domain.


Pssm-ID: 350407 [Multi-domain]  Cd Length: 227  Bit Score: 75.13  E-value: 9.47e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032733617  739 NRYINIlaydHSRVKLrpLPGKDskhsdyINANYVDGYNKAKAyIATQGPLKSTFEDFWRMIWEQNTGIIVMITNLVEKG 818
Cdd:cd14559      1 NRFTNI----QTRVST--PVGKN------LNANRVQIGNKNVA-IACQYPKNEQLEDHLKMLADNRTPCLVVLASNKDIQ 67

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032733617  819 RRKCDQYWptENSEEYGNIIVTLKSTNvhACYTVRRFTVRNTKMKKgqkgnpKGRQNERTVIQYHYTQWPDMG-VPEYAL 897
Cdd:cd14559     68 RKGLPPYF--RQSGTYGSVTVKSKKTG--KDELVDGLKADMYNLKI------TDGNKTITIPVVHVTNWPDHTaISSEGL 137

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032733617  898 PVLT--------------FVRRSSAARTPDMGPVVVHCSAGVGRTGTYIvidSMLQQIKDKSTVNVLGFLKHIRTQRN-Y 962
Cdd:cd14559    138 KELAdlvnksaeekrnfyKSKGSSAINDKNKLLPVIHCRAGVGRTGQLA---AAMELNKSPNNLSVEDIVSDMRTSRNgK 214

                          250
                   ....*....|....*..
gi 2032733617  963 LVQTEEQYifihDALLE 979
Cdd:cd14559    215 MVQKDEQL----DTLKE 227
PHA02740 PHA02740
protein tyrosine phosphatase; Provisional
 1067-1275 8.02e-11

protein tyrosine phosphatase; Provisional


Pssm-ID: 165107 [Multi-domain]  Cd Length: 298  Bit Score: 64.60  E-value: 8.02e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032733617 1067 INASYIMGYYRSNEFIITQHPLPHTTKDFWRMIWDHNAQIIVMLpdnQSLAEDE--FVYWPSREEsmnceaftvTLISKD 1144
Cdd:PHA02740    79 LDARFVDGYDFEQKFICIINLCEDACDKFLQALSDNKVQIIVLI---SRHADKKcfNQFWSLKEG---------CVITSD 146

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032733617 1145 RLCLSNEEQIIIHDFILE----ATQDDYVLEVRHFQCPKWP------NPDAPISSTFEL----INVIKEEALTRDGPTIV 1210
Cdd:PHA02740   147 KFQIETLEIIIKPHFNLTllslTDKFGQAQKISHFQYTAWPadgfshDPDAFIDFFCNIddlcADLEKHKADGKIAPIII 226

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2032733617 1211 HDEYGAVSAGTLCALTTLSQQLENENAVDVFQVAKMINLMRPGVFTDIEQYQFLYKAMLSLVSTK 1275
Cdd:PHA02740   227 DCIDGISSSAVFCVFDICATEFDKTGMLSIANALKKVRQKKYGCMNCLDDYVFCYHLIAAYLKEK 291
PLN02179 PLN02179
carbonic anhydrase
 15-156 9.06e-10

carbonic anhydrase


Pssm-ID: 177835  Cd Length: 235  Bit Score: 60.38  E-value: 9.06e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032733617   15 DYFVSGAGLPGRFKAEKVEFHWGQSNGSAGSEHSINGKRFPVEMQIFFynpddfdsfGTAVLENRVVGamaVFFQVSQRD 94
Cdd:PLN02179   101 DVMVSWKGDAGKITIHQTDYKLVQCHWHSPSEHTINGTSYDLELHMVH---------TSASGKTAVVG---VLYKLGEPD 168

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2032733617   95 nSALDPIIHGLKGVVHHEKET-FLDPFVLRellpTSLGSYYRYTGSLTTPPCSEIVEWIVFRK 156
Cdd:PLN02179   169 -EFLTKLLNGIKGVGKKEINLgIVDPRDIR----FETNNFYRYIGSLTIPPCTEGVIWTVVKR 226
FN3 cd00063
Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein ...
 233-322 1.35e-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: 53.27  E-value: 1.35e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032733617  233 PPVNMKVQPVNRTALLVTWNQPETIyHPPIMNYMISYSWTKNEDEKEktFTKDSDKDLKAIISHVSPDILYLFRVQAVcR 312
Cdd:cd00063      3 PPTNLRVTDVTSTSVTLSWTPPEDD-GGPITGYVVEYREKGSGDWKE--VEVTPGSETSYTLTGLKPGTEYEFRVRAV-N 78

                           90
                   ....*....|
gi 2032733617  313 NEMRSDFSQT 322
Cdd:cd00063     79 GGGESPPSES 88
FN3 smart00060
Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, ...
 233-310 1.41e-08

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: 53.00  E-value: 1.41e-08
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2032733617   233 PPVNMKVQPVNRTALLVTWNQPEtiyHPPIMNYMISYSWTKNEDEKEKTFTKDSDKDLKAIISHVSPDILYLFRVQAV 310
Cdd:smart00060    3 PPSNLRVTDVTSTSVTLSWEPPP---DDGITGYIVGYRVEYREEGSEWKEVNVTPSSTSYTLTGLKPGTEYEFRVRAV 77
PLN02202 PLN02202
carbonate dehydratase
 133-201 2.62e-08

carbonate dehydratase


Pssm-ID: 177853 [Multi-domain]  Cd Length: 284  Bit Score: 56.99  E-value: 2.62e-08
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2032733617  133 YYRYTGSLTTPPCSEIVEWIVFRKPVPISYHQLEAFYSIFTTEqqdhvksveyLRNNFRPQQSLNNRKV 201
Cdd:PLN02202   204 YFRYIGSLTTPPCSENVSWTILGKVRSMSKEQVELLRSPLDKS----------FKNNSRPCQPLNGRRV 262
CDC14 COG2453
Protein-tyrosine phosphatase [Signal transduction mechanisms];
880-975 4.99e-08

Protein-tyrosine phosphatase [Signal transduction mechanisms];


Pssm-ID: 441989 [Multi-domain]  Cd Length: 140  Bit Score: 53.05  E-value: 4.99e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032733617  880 IQYHYTQWPDMGVPEYA--LPVLTFVRRSSAARtpdmGPVVVHCSAGVGRTGT----YIVIDSM-LQQIkdkstvnvlgf 952
Cdd:COG2453     48 LEYLHLPIPDFGAPDDEqlQEAVDFIDEALREG----KKVLVHCRGGIGRTGTvaaaYLVLLGLsAEEA----------- 112

                           90       100
                   ....*....|....*....|...
gi 2032733617  953 LKHIRTQRNYLVQTEEQYIFIHD 975
Cdd:COG2453    113 LARVRAARPGAVETPAQRAFLER 135
fn3 pfam00041
Fibronectin type III domain;
233-310 1.26e-07

Fibronectin type III domain;


Pssm-ID: 394996 [Multi-domain]  Cd Length: 85  Bit Score: 50.49  E-value: 1.26e-07
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2032733617  233 PPVNMKVQPVNRTALLVTWNQPETiYHPPIMNYMISYsWTKNEDEKEKTFTKDSDKDlKAIISHVSPDILYLFRVQAV 310
Cdd:pfam00041    2 APSNLTVTDVTSTSLTVSWTPPPD-GNGPITGYEVEY-RPKNSGEPWNEITVPGTTT-SVTLTGLKPGTEYEVRVQAV 76
PTP_DSP_cys cd14494
cys-based protein tyrosine phosphatase and dual-specificity phosphatase superfamily; This ...
 915-975 7.19e-07

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: 49.27  E-value: 7.19e-07
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2032733617  915 GPVVVHCSAGVGRTGTYIVIDSMLQQIKDkstvnVLGFLKHIRTQR-NYLVQTEEQYIFIHD 975
Cdd:cd14494     57 EPVLVHCKAGVGRTGTLVACYLVLLGGMS-----AEEAVRIVRLIRpGGIPQTIEQLDFLIK 113
CDKN3-like cd14505
cyclin-dependent kinase inhibitor 3 and similar proteins; This family is composed of ...
 880-975 5.96e-06

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


Pssm-ID: 350355 [Multi-domain]  Cd Length: 163  Bit Score: 47.64  E-value: 5.96e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032733617  880 IQYHYTQWPDMGVP---EYALPVLTFVR-RSSAARTpdmgpVVVHCSAGVGRTGTyiVIDSMLQQIKDKSTVNVLgfLKH 955
Cdd:cd14505     73 ITWHHLPIPDGGVPsdiAQWQELLEELLsALENGKK-----VLIHCKGGLGRTGL--IAACLLLELGDTLDPEQA--IAA 143

                           90       100
                   ....*....|....*....|
gi 2032733617  956 IRTQRNYLVQTEEQYIFIHD 975
Cdd:cd14505    144 VRALRPGAIQTPKQENFLHQ 163
PTP_PTPDC1 cd14506
protein tyrosine phosphatase domain of PTP domain-containing protein 1; protein tyrosine ...
 880-975 3.13e-05

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: 46.57  E-value: 3.13e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032733617  880 IQYHYTQWPDMGVPEYALpVLTFVR-RSSAARTPdmGPVVVHCSAGVGRTGtyIVIDSMLQQIKDKSTVNVLGFlkhIRT 958
Cdd:cd14506     77 IYFYNFGWKDYGVPSLTT-ILDIVKvMAFALQEG--GKVAVHCHAGLGRTG--VLIACYLVYALRMSADQAIRL---VRS 148

                           90
                   ....*....|....*..
gi 2032733617  959 QRNYLVQTEEQYIFIHD 975
Cdd:cd14506    149 KRPNSIQTRGQVLCVRE 165
DUSP23 cd14504
dual specificity phosphatase 23; Dual specificity phosphatase 23 (DUSP23), also known as ...
 880-973 8.89e-05

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: 43.81  E-value: 8.89e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032733617  880 IQYHYTQWPDMGVPEYALpVLTFVRRSSAARTPDmGPVVVHCSAGVGRTGT----YIVIDSMLQQIKDkstvnvlgfLKH 955
Cdd:cd14504     50 LRYHHIPIEDYTPPTLEQ-IDEFLDIVEEANAKN-EAVLVHCLAGKGRTGTmlacYLVKTGKISAVDA---------INE 118

                           90
                   ....*....|....*...
gi 2032733617  956 IRTQRNYLVQTEEQYIFI 973
Cdd:cd14504    119 IRRIRPGSIETSEQEKFV 136
DSPc smart00195
Dual specificity phosphatase, catalytic domain;
915-957 4.27e-03

Dual specificity phosphatase, catalytic domain;


Pssm-ID: 214551 [Multi-domain]  Cd Length: 138  Bit Score: 38.80  E-value: 4.27e-03
                            10        20        30        40
                    ....*....|....*....|....*....|....*....|...
gi 2032733617   915 GPVVVHCSAGVGRTGTYIVidSMLQQIKDKSTVNVLGFLKHIR 957
Cdd:smart00195   79 GKVLVHCQAGVSRSATLII--AYLMKTRNMSLNDAYDFVKDRR 119
 
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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