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Conserved domains on  [gi|1823416726|ref|XP_032927298|]
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receptor-type tyrosine-protein phosphatase gamma [Catharus ustulatus]

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 ...
 825-1098 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: 641.32  E-value: 0e+00
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823416726  825 FSEDFEEVQRCTADMNITAEHSNHPDNKHKNRYINILAYDHSRVKLRPLPGKDSKHSDYINANYVDGYNKAKAYIATQGP 904
Cdd:cd17667      1 FSEDFEEVQRCTADMNITAEHSNHPDNKHKNRYINILAYDHSRVKLRPLPGKDSKHSDYINANYVDGYNKAKAYIATQGP 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823416726  905 LKSTFEDFWRMIWEQNTGIIVMITNLVEKGRRKCDQYWPTENSEEYGNIIVTLKSTNVHACYTVRRFTIRNTKMKKGQKG 984
Cdd:cd17667     81 LKSTFEDFWRMIWEQNTGIIVMITNLVEKGRRKCDQYWPTENSEEYGNIIVTLKSTKIHACYTVRRFSIRNTKVKKGQKG 160

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823416726  985 NPKGRQNERTVIQYHYTQWPDMGVPEYALPVLTFVRRSSAARTPDMGPVVVHCSAGVGRTGTYIVIDSMLQQIKDKSTVN 1064
Cdd:cd17667    161 NPKGRQNERTVIQYHYTQWPDMGVPEYALPVLTFVRRSSAARTPEMGPVLVHCSAGVGRTGTYIVIDSMLQQIKDKSTVN 240

                          250       260       270
                   ....*....|....*....|....*....|....
gi 1823416726 1065 VLGFLKHIRTQRNYLVQTEEQYIFIHDALLEAIL 1098
Cdd:cd17667    241 VLGFLKHIRTQRNYLVQTEEQYIFIHDALLEAIL 274
R-PTP-G-2 cd17670
PTP-like domain of receptor-type tyrosine-protein phosphatase G, repeat 2; Receptor-type ...
 1182-1386 8.21e-158

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: 8.21e-158
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823416726 1182 YINASYIMGYYRSNEFIITQHPLPHTTKDFWRMIWDHNAQIIVMLPDNQSLAEDEFVYWPSREESMNCEAFTVTLISKDR 1261
Cdd:cd17670      1 YINASYIMGYYRSNEFIITQHPLPHTTKDFWRMIWDHNAQIIVMLPDNQGLAEDEFVYWPSREESMNCEAFTVTLISKDR 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823416726 1262 LCLSNEEQIIIHDFILEATQDDYVLEVRHFQCPKWPNPDAPISSTFELINVIKEEALTRDGPTIVHDEYGAVSAGTLCAL 1341
Cdd:cd17670     81 LCLSNEEQIIIHDFILEATQDDYVLEVRHFQCPKWPNPDAPISSTFELINVIKEEALTRDGPTIVHDEFGAVSAGTLCAL 160

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*
gi 1823416726 1342 TTLSQQLENENAVDVFQVAKMINLMRPGVFTDIEQYQFLYKAMLS 1386
Cdd:cd17670    161 TTLSQQLENENAVDVYQVAKMINLMRPGVFTDIEQYQFLYKAMLS 205
alpha_CARP_receptor_like cd03122
Carbonic anhydrase alpha related protein, receptor_like subfamily. Carbonic anhydrase related ...
 67-319 1.43e-119

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: 373.61  E-value: 1.43e-119
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823416726   67 GPEHWVTSSEKCG-GSHQSPIDIMDHLAHVGDEYQELQLDGFDNESsNKTWMKNTGKTVAILLKD---DYFVSGAGLPGR 142
Cdd:cd03122      1 NPKHWAKKYPACGeGRQQSPIDIVEDTQVQRQGLQPLHFDGYEELT-ASTTLENTGKTVILRLEGnssDPFVSGGPLLGR 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823416726  143 FKAEKVEFHWGQSNgSAGSEHSINGKRFPVEMQIYFYNPDDFDSFgTAVLENRVVGAMAVFFQVSPRDNSALDPIIHGLK 222
Cdd:cd03122     80 YKFSEITFHWGTCN-SDGSEHSIDGHKFPLEMQILHRNTDFFDSF-EAIKSPGGVLALAYLFELSHEDNPFLDPIIEGLR 157

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823416726  223 GVVHHEKETFLDPFVLRELLPTSLGSYYRYTGSLTTPPCSEIVEWIVFRKPVPISYHQLEAFYSIFTTEQQDhVKSVEYL 302
Cdd:cd03122    158 NVSRPGKEVELPPFPLSDLLPPFTDKYYSYEGSLTTPPCSETVEWIVFREPVPISSRQLEAFRELLTRRQDG-VMSGDYL 236

                          250
                   ....*....|....*..
gi 1823416726  303 RNNFRPQQRLNNRKVSK 319
Cdd:cd03122    237 PNNGRPQQPLGSRTVFS 253
FN3 cd00063
Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein ...
 349-438 1.42e-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: 53.65  E-value: 1.42e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823416726  349 PPVNMKVQPVNRTALLVTWNQPETIyHPPIMNYMISYSWTKNEDEKEktFTKDSDKDLKAIISHVSPDILYLFRVQAVcR 428
Cdd:cd00063      3 PPTNLRVTDVTSTSVTLSWTPPEDD-GGPITGYVVEYREKGSGDWKE--VEVTPGSETSYTLTGLKPGTEYEFRVRAV-N 78

                           90
                   ....*....|
gi 1823416726  429 NEMRSDFSQT 438
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 ...
 825-1098 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: 641.32  E-value: 0e+00
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823416726  825 FSEDFEEVQRCTADMNITAEHSNHPDNKHKNRYINILAYDHSRVKLRPLPGKDSKHSDYINANYVDGYNKAKAYIATQGP 904
Cdd:cd17667      1 FSEDFEEVQRCTADMNITAEHSNHPDNKHKNRYINILAYDHSRVKLRPLPGKDSKHSDYINANYVDGYNKAKAYIATQGP 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823416726  905 LKSTFEDFWRMIWEQNTGIIVMITNLVEKGRRKCDQYWPTENSEEYGNIIVTLKSTNVHACYTVRRFTIRNTKMKKGQKG 984
Cdd:cd17667     81 LKSTFEDFWRMIWEQNTGIIVMITNLVEKGRRKCDQYWPTENSEEYGNIIVTLKSTKIHACYTVRRFSIRNTKVKKGQKG 160

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823416726  985 NPKGRQNERTVIQYHYTQWPDMGVPEYALPVLTFVRRSSAARTPDMGPVVVHCSAGVGRTGTYIVIDSMLQQIKDKSTVN 1064
Cdd:cd17667    161 NPKGRQNERTVIQYHYTQWPDMGVPEYALPVLTFVRRSSAARTPEMGPVLVHCSAGVGRTGTYIVIDSMLQQIKDKSTVN 240

                          250       260       270
                   ....*....|....*....|....*....|....
gi 1823416726 1065 VLGFLKHIRTQRNYLVQTEEQYIFIHDALLEAIL 1098
Cdd:cd17667    241 VLGFLKHIRTQRNYLVQTEEQYIFIHDALLEAIL 274
R-PTP-G-2 cd17670
PTP-like domain of receptor-type tyrosine-protein phosphatase G, repeat 2; Receptor-type ...
 1182-1386 8.21e-158

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: 8.21e-158
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823416726 1182 YINASYIMGYYRSNEFIITQHPLPHTTKDFWRMIWDHNAQIIVMLPDNQSLAEDEFVYWPSREESMNCEAFTVTLISKDR 1261
Cdd:cd17670      1 YINASYIMGYYRSNEFIITQHPLPHTTKDFWRMIWDHNAQIIVMLPDNQGLAEDEFVYWPSREESMNCEAFTVTLISKDR 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823416726 1262 LCLSNEEQIIIHDFILEATQDDYVLEVRHFQCPKWPNPDAPISSTFELINVIKEEALTRDGPTIVHDEYGAVSAGTLCAL 1341
Cdd:cd17670     81 LCLSNEEQIIIHDFILEATQDDYVLEVRHFQCPKWPNPDAPISSTFELINVIKEEALTRDGPTIVHDEFGAVSAGTLCAL 160

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*
gi 1823416726 1342 TTLSQQLENENAVDVFQVAKMINLMRPGVFTDIEQYQFLYKAMLS 1386
Cdd:cd17670    161 TTLSQQLENENAVDVYQVAKMINLMRPGVFTDIEQYQFLYKAMLS 205
alpha_CARP_receptor_like cd03122
Carbonic anhydrase alpha related protein, receptor_like subfamily. Carbonic anhydrase related ...
 67-319 1.43e-119

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: 373.61  E-value: 1.43e-119
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823416726   67 GPEHWVTSSEKCG-GSHQSPIDIMDHLAHVGDEYQELQLDGFDNESsNKTWMKNTGKTVAILLKD---DYFVSGAGLPGR 142
Cdd:cd03122      1 NPKHWAKKYPACGeGRQQSPIDIVEDTQVQRQGLQPLHFDGYEELT-ASTTLENTGKTVILRLEGnssDPFVSGGPLLGR 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823416726  143 FKAEKVEFHWGQSNgSAGSEHSINGKRFPVEMQIYFYNPDDFDSFgTAVLENRVVGAMAVFFQVSPRDNSALDPIIHGLK 222
Cdd:cd03122     80 YKFSEITFHWGTCN-SDGSEHSIDGHKFPLEMQILHRNTDFFDSF-EAIKSPGGVLALAYLFELSHEDNPFLDPIIEGLR 157

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823416726  223 GVVHHEKETFLDPFVLRELLPTSLGSYYRYTGSLTTPPCSEIVEWIVFRKPVPISYHQLEAFYSIFTTEQQDhVKSVEYL 302
Cdd:cd03122    158 NVSRPGKEVELPPFPLSDLLPPFTDKYYSYEGSLTTPPCSETVEWIVFREPVPISSRQLEAFRELLTRRQDG-VMSGDYL 236

                          250
                   ....*....|....*..
gi 1823416726  303 RNNFRPQQRLNNRKVSK 319
Cdd:cd03122    237 PNNGRPQQPLGSRTVFS 253
PTPc smart00194
Protein tyrosine phosphatase, catalytic domain;
824-1095 2.16e-119

Protein tyrosine phosphatase, catalytic domain;


Pssm-ID: 214550 [Multi-domain]  Cd Length: 259  Bit Score: 373.53  E-value: 2.16e-119
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823416726   824 GFSEDFEEVQRCTADMnITAEHSNHPDNKHKNRYINILAYDHSRVKLRPLPGKDSkhsDYINANYVDGYNKAKAYIATQG 903
Cdd:smart00194    1 GLEEEFEKLDRLKPDD-ESCTVAAFPENRDKNRYKDVLPYDHTRVKLKPPPGEGS---DYINASYIDGPNGPKAYIATQG 76

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823416726   904 PLKSTFEDFWRMIWEQNTGIIVMITNLVEKGRRKCDQYWPTENSE--EYGNIIVTLKSTNVHACYTVRRFTIRNTkmkkg 981
Cdd:smart00194   77 PLPSTVEDFWRMVWEQKVTVIVMLTELVEKGREKCAQYWPDEEGEplTYGDITVTLKSVEKVDDYTIRTLEVTNT----- 151

                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823416726   982 qkgnpkGRQNERTVIQYHYTQWPDMGVPEYALPVLTFVRRSSAARTPDMGPVVVHCSAGVGRTGTYIVIDSMLQQIKDKS 1061
Cdd:smart00194  152 ------GCSETRTVTHYHYTNWPDHGVPESPESILDLIRAVRKSQSTSTGPIVVHCSAGVGRTGTFIAIDILLQQLEAGK 225

                           250       260       270
                    ....*....|....*....|....*....|....
gi 1823416726  1062 TVNVLGFLKHIRTQRNYLVQTEEQYIFIHDALLE 1095
Cdd:smart00194  226 EVDIFEIVKELRSQRPGMVQTEEQYIFLYRAILE 259
Y_phosphatase pfam00102
Protein-tyrosine phosphatase;
851-1095 1.49e-112

Protein-tyrosine phosphatase;


Pssm-ID: 459674 [Multi-domain]  Cd Length: 234  Bit Score: 353.86  E-value: 1.49e-112
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823416726  851 NKHKNRYINILAYDHSRVKLRPLPGkdskHSDYINANYVDGYNKAKAYIATQGPLKSTFEDFWRMIWEQNTGIIVMITNL 930
Cdd:pfam00102    1 NLEKNRYKDVLPYDHTRVKLTGDPG----PSDYINASYIDGYKKPKKYIATQGPLPNTVEDFWRMVWEEKVTIIVMLTEL 76

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823416726  931 VEKGRRKCDQYWPTEN--SEEYGNIIVTLKSTNVH-ACYTVRRFTIRNtkmkkgqkgnpKGRQNERTVIQYHYTQWPDMG 1007
Cdd:pfam00102   77 EEKGREKCAQYWPEEEgeSLEYGDFTVTLKKEKEDeKDYTVRTLEVSN-----------GGSEETRTVKHFHYTGWPDHG 145

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823416726 1008 VPEYALPVLTFVRR-SSAARTPDMGPVVVHCSAGVGRTGTYIVIDSMLQQIKDKSTVNVLGFLKHIRTQRNYLVQTEEQY 1086
Cdd:pfam00102  146 VPESPNSLLDLLRKvRKSSLDGRSGPIVVHCSAGIGRTGTFIAIDIALQQLEAEGEVDIFQIVKELRSQRPGMVQTLEQY 225


                   ....*....
gi 1823416726 1087 IFIHDALLE 1095
Cdd:pfam00102  226 IFLYDAILE 234
Carb_anhydrase smart01057
Eukaryotic-type carbonic anhydrase; Carbonic anhydrases are zinc metalloenzymes which catalyse ...
 60-316 3.54e-96

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: 309.24  E-value: 3.54e-96
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823416726    60 WAYSGTYGPEHWVTSS-EKCGGSHQSPIDIMDHLAHVGDEYQELQldgFDNESSNKTWMKNTGKTVAILLKDD-YFVSGA 137
Cdd:smart01057    1 WGYEGKNGPEHWGKLDpPFCGGKRQSPIDIVTAEAQYDPSLKPLK---LSYDQPTAKRILNNGHTVQVNFDDDgSTLSGG 77

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823416726   138 GLPGRFKAEKVEFHWGqSNGSAGSEHSINGKRFPVEMQIYFYNPDDfdSFGTAVLENRVVGAMAVFFQVSPRDNSALDPI 217
Cdd:smart01057   78 PLPGRYRLKQFHFHWG-GSDSEGSEHTIDGKRFPLELHLVHYNSKG--SFSEAVSKPGGLAVVAVFFKVGAEENPALQAI 154

                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823416726   218 IHGLKGVVHHEKETFLDPFVLRELLPTSLGSYYRYTGSLTTPPCSEIVEWIVFRKPVPISYHQLEAFYSIFTTEQQdhvk 297
Cdd:smart01057  155 LDHLPLIKYKGQETELTPFDLSSLLPASTRHYYTYNGSLTTPPCSEGVTWIVFKEPITISTEQLEKFRTLLPMEGN---- 230

                           250
                    ....*....|....*....
gi 1823416726   298 svEYLRNNFRPQQRLNNRK 316
Cdd:smart01057  231 --EPLVNNARPLQPLNGRV 247
Carb_anhydrase pfam00194
Eukaryotic-type carbonic anhydrase;
67-320 7.05e-94

Eukaryotic-type carbonic anhydrase;


Pssm-ID: 459707 [Multi-domain]  Cd Length: 252  Bit Score: 303.03  E-value: 7.05e-94
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823416726   67 GPEHWVTSSEKCGGSHQSPIDIMDHLAHVGDEYQELQLDGFDNESSNKTwMKNTGKTVAILLKDDY--FVSGAGLPGRFK 144
Cdd:pfam00194    2 GPEHWGKVYPSCGGKRQSPINIDTRKVRYDPSLPPLTFQGYDVPPGKNT-LTNNGHTVQVSLDDGDpsTISGGPLATRYR 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823416726  145 AEKVEFHWGqSNGSAGSEHSINGKRFPVEMQIYFYNpDDFDSFGTAVLENRVVGAMAVFFQVSPRDNSALDPIIHGLKGV 224
Cdd:pfam00194   81 LVQFHFHWG-STDSRGSEHTIDGKRYPAELHIVHYN-SKYKSFDEAAKHPDGLAVLGVFFEVGDENNPYLQPIVSALDNI 158

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823416726  225 VHHEKETFLDPFVLRELLPTSLGSYYRYTGSLTTPPCSEIVEWIVFRKPVPISYHQLEAFYSIFTTEQQDHvksVEYLRN 304
Cdd:pfam00194  159 KYKGKSVLLPPFDLSDLLPEDLTSYYTYNGSLTTPPCSESVTWIVFKEPISISEEQLEAFRTLLFSDGGEE---PRPLVN 235

                          250
                   ....*....|....*.
gi 1823416726  305 NFRPQQRLNNRKVSKS 320
Cdd:pfam00194  236 NFRPTQPLNGRVVFAS 251
PTPc smart00194
Protein tyrosine phosphatase, catalytic domain;
1127-1385 2.73e-80

Protein tyrosine phosphatase, catalytic domain;


Pssm-ID: 214550 [Multi-domain]  Cd Length: 259  Bit Score: 264.91  E-value: 2.73e-80
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823416726  1127 LEKQFKLVTQCNAKYVECFSAQKDCNKEKNRNSSVVPSERARVGLAPLPGmKGTDYINASYIMGYYRSNEFIITQHPLPH 1206
Cdd:smart00194    2 LEEEFEKLDRLKPDDESCTVAAFPENRDKNRYKDVLPYDHTRVKLKPPPG-EGSDYINASYIDGPNGPKAYIATQGPLPS 80

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823416726  1207 TTKDFWRMIWDHNAQIIVMLPDNQSL-AEDEFVYWPSRE-ESMNCEAFTVTLISKDRLclsneEQIIIHDFILEATQDDY 1284
Cdd:smart00194   81 TVEDFWRMVWEQKVTVIVMLTELVEKgREKCAQYWPDEEgEPLTYGDITVTLKSVEKV-----DDYTIRTLEVTNTGCSE 155

                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823416726  1285 VLEVRHFQCPKWPNPDAP--ISSTFELINVIKEEALTRDGPTIVHDEYGAVSAGTLCALTTLSQQLENENAVDVFQVAKM 1362
Cdd:smart00194  156 TRTVTHYHYTNWPDHGVPesPESILDLIRAVRKSQSTSTGPIVVHCSAGVGRTGTFIAIDILLQQLEAGKEVDIFEIVKE 235

                           250       260
                    ....*....|....*....|...
gi 1823416726  1363 INLMRPGVFTDIEQYQFLYKAML 1385
Cdd:smart00194  236 LRSQRPGMVQTEEQYIFLYRAIL 258
Y_phosphatase pfam00102
Protein-tyrosine phosphatase;
1152-1385 3.24e-79

Protein-tyrosine phosphatase;


Pssm-ID: 459674 [Multi-domain]  Cd Length: 234  Bit Score: 261.02  E-value: 3.24e-79
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823416726 1152 NKEKNRNSSVVPSERARVGLAPLPGmkGTDYINASYIMGYYRSNEFIITQHPLPHTTKDFWRMIWDHNAQIIVMLPDNQS 1231
Cdd:pfam00102    1 NLEKNRYKDVLPYDHTRVKLTGDPG--PSDYINASYIDGYKKPKKYIATQGPLPNTVEDFWRMVWEEKVTIIVMLTELEE 78

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823416726 1232 LA-EDEFVYWP-SREESMNCEAFTVTLISKDrlclSNEEQIIIHDFILEATQDDYVLEVRHFQCPKWPNPDAP--ISSTF 1307
Cdd:pfam00102   79 KGrEKCAQYWPeEEGESLEYGDFTVTLKKEK----EDEKDYTVRTLEVSNGGSEETRTVKHFHYTGWPDHGVPesPNSLL 154

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1823416726 1308 ELINVIKEEALT-RDGPTIVHDEYGAVSAGTLCALTTLSQQLENENAVDVFQVAKMINLMRPGVFTDIEQYQFLYKAML 1385
Cdd:pfam00102  155 DLLRKVRKSSLDgRSGPIVVHCSAGIGRTGTFIAIDIALQQLEAEGEVDIFQIVKELRSQRPGMVQTLEQYIFLYDAIL 233
PHA02738 PHA02738
hypothetical protein; Provisional
 828-1093 9.49e-48

hypothetical protein; Provisional


Pssm-ID: 222923 [Multi-domain]  Cd Length: 320  Bit Score: 173.96  E-value: 9.49e-48
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823416726  828 DFEEVqrctadmnITAEH------------SNHPDNKHKNRYINILAYDHSRVKLRplpgKDSKHSDYINANYVDGYNKA 895
Cdd:PHA02738    22 DCEEV--------ITREHqkvisekvdgtfNAEKKNRKLNRYLDAVCFDHSRVILP----AERNRGDYINANYVDGFEYK 89

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823416726  896 KAYIATQGPLKSTFEDFWRMIWEQNTGIIVMITNLVEKGRRKCDQYWPT--ENSEEYGNIIVTLKSTNVHACYTvrRFTI 973
Cdd:PHA02738    90 KKFICGQAPTRQTCYDFYRMLWMEHVQIIVMLCKKKENGREKCFPYWSDveQGSIRFGKFKITTTQVETHPHYV--KSTL 167

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823416726  974 RNTkmkkgqkgnpKGRQNERTVIQYHYTQWPDMGVPEYALPVLTFV------RRSSAARTPDMG-------PVVVHCSAG 1040
Cdd:PHA02738   168 LLT----------DGTSATQTVTHFNFTAWPDHDVPKNTSEFLNFVlevrqcQKELAQESLQIGhnrlqppPIVVHCNAG 237

                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|...
gi 1823416726 1041 VGRTGTYIVIDSMLQQIKDKSTVNVLGFLKHIRTQRNYLVQTEEQYIFIHDAL 1093
Cdd:PHA02738   238 LGRTPCYCVVDISISRFDACATVSIPSIVSSIRNQRYYSLFIPFQYFFCYRAV 290
Cah COG3338
Carbonic anhydrase [Inorganic ion transport and metabolism];
53-320 5.75e-46

Carbonic anhydrase [Inorganic ion transport and metabolism];


Pssm-ID: 442567 [Multi-domain]  Cd Length: 247  Bit Score: 166.21  E-value: 5.75e-46
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823416726   53 KASGDPYWAYSGTYGPEHWVTSSEK---CG-GSHQSPIDIMDHlahVGDEYQELQldgFDNESSNKTwMKNTGKTVAILL 128
Cdd:COG3338     21 AAASAPHWSYEGETGPEHWGELSPEfatCAtGKNQSPIDIRTA---IKADLPPLK---FDYKPTPLE-IVNNGHTIQVNV 93

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823416726  129 KDDYFVSGAGLpgRFKAEKVEFHwgqsngsAGSEHSINGKRFPVEMQIYFYNPDDfdsfGTAVLenrvvgamAVFFQVSp 208
Cdd:COG3338     94 DPGSTLTVDGK--RYELKQFHFH-------TPSEHTINGKSYPMEAHLVHKDADG----ELAVV--------GVLFEEG- 151

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823416726  209 RDNSALDPIIHGL---KGvvhhEKETFLDPFVLRELLPTSLgSYYRYTGSLTTPPCSEIVEWIVFRKPVPISYHQLEAFY 285
Cdd:COG3338    152 AENPALAKLWANLpleAG----EEVALDATIDLNDLLPEDR-SYYRYSGSLTTPPCSEGVLWIVLKQPITVSAEQIEAFA 226

                          250       260       270
                   ....*....|....*....|....*....|....*
gi 1823416726  286 SIFtteqqdhvksveylRNNFRPQQRLNNRKVSKS 320
Cdd:COG3338    227 RLY--------------PNNARPVQPLNGRLILES 247
COG5599 COG5599
Protein tyrosine phosphatase [Signal transduction mechanisms];
845-1089 3.96e-43

Protein tyrosine phosphatase [Signal transduction mechanisms];


Pssm-ID: 444335 [Multi-domain]  Cd Length: 282  Bit Score: 159.10  E-value: 3.96e-43
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823416726  845 HSNHPDNKHKNRYINILAYDHSRVklrplpGKDSKhsdYINANYVDGYNKaKAYIATQGPLKSTFEDFWRMIWEQNTGII 924
Cdd:COG5599     36 YLQNINGSPLNRFRDIQPYKETAL------RANLG---YLNANYIQVIGN-HRYIATQYPLEEQLEDFFQMLFDNNTPVL 105

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823416726  925 VMITNLVE--KGRRKCDQYWPTenSEEYGNIIVTLKSTNVHACYTvrRFTIRNTKMKKGQKGnpkgrQNERTVIQYHYTQ 1002
Cdd:COG5599    106 VVLASDDEisKPKVKMPVYFRQ--DGEYGKYEVSSELTESIQLRD--GIEARTYVLTIKGTG-----QKKIEIPVLHVKN 176

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823416726 1003 WPDMGVP--EYALPVLTFVRRSSAARTPDMGPVVVHCSAGVGRTGTYIVIDSMLQQIKDKS--TVNVLGFLKHIRTQRNY 1078
Cdd:COG5599    177 WPDHGAIsaEALKNLADLIDKKEKIKDPDKLLPVVHCRAGVGRTGTLIACLALSKSINALVqiTLSVEEIVIDMRTSRNG 256

                          250
                   ....*....|..
gi 1823416726 1079 -LVQTEEQYIFI 1089
Cdd:COG5599    257 gMVQTSEQLDVL 268
PHA02747 PHA02747
protein tyrosine phosphatase; Provisional
 1103-1393 5.74e-25

protein tyrosine phosphatase; Provisional


Pssm-ID: 165114 [Multi-domain]  Cd Length: 312  Bit Score: 107.39  E-value: 5.74e-25
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823416726 1103 EVSANQLHSYVNSILIPGIggkTRLEkQFKLVTQCNAKYVECFsaQKDCNKEKNRNSSVVPSERARVGLAPLPGmKGTDY 1182
Cdd:PHA02747     8 ECRAIDFLKRRNQLNCFGI---IRDE-HHQIILKPFDGLIANF--EKPENQPKNRYWDIPCWDHNRVILDSGGG-STSDY 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823416726 1183 INASYIMGYYRSNEFIITQHPLPHTTKDFWRMIWDHNAQIIVMLPDNQSLAEDE--FVYW-PSREESMNCEAFTVTLISK 1259
Cdd:PHA02747    81 IHANWIDGFEDDKKFIATQGPFAETCADFWKAVWQEHCSIIVMLTPTKGTNGEEkcYQYWcLNEDGNIDMEDFRIETLKT 160

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823416726 1260 DRLCLSNEEQIIIHDFILEATQddyvlEVRHFQCPKWPNPDAPISST-----FELINVIKEEALTRDG-------PTIVH 1327
Cdd:PHA02747   161 SVRAKYILTLIEITDKILKDSR-----KISHFQCSEWFEDETPSDHPdfikfIKIIDINRKKSGKLFNpkdallcPIVVH 235

                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1823416726 1328 DEYGAVSAGTLCALTTLSQQLENENAVDVFQVAKMINLMRPGVFTDIEQYQFL---YKAMLSLVSTKEN 1393
Cdd:PHA02747   236 CSDGVGKTGIFCAVDICLNQLVKRKAICLAKTAEKIREQRHAGIMNFDDYLFIqpgYEVLHYFLSKIKA 304
PLN02179 PLN02179
carbonic anhydrase
 17-272 4.98e-11

carbonic anhydrase


Pssm-ID: 177835  Cd Length: 235  Bit Score: 64.23  E-value: 4.98e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823416726   17 TSSVLHDVVCFPALTEGYVGSLHESRHGSS--VQIRRRKASGDPYWaysGTYGPeHWVTSSEkcgGSHQSPIDIMDH--- 91
Cdd:PLN02179     5 TKTIFFFVVFFIDLFFPNILLVYAREIGNKplFTYKQKTEKGPAEW---GKLNP-QWKVCST---GKYQSPIDLTDErvs 77

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823416726   92 LAHvgdeyqelqldgfdnessNKTWMKNTGKTVAILLK--DDYFVSGAGLPGRFKAEKVEFHWGQSNGSAGSEHSINGKR 169
Cdd:PLN02179    78 LIH------------------DQALSRHYKPAPAVIQSrgHDVMVSWKGDAGKITIHQTDYKLVQCHWHSPSEHTINGTS 139

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823416726  170 FPVEMQIYFynpddfdsfGTAVLENRVVGamaVFFQVSpRDNSALDPIIHGLKGVVHHEKET-FLDPFVLRellpTSLGS 248
Cdd:PLN02179   140 YDLELHMVH---------TSASGKTAVVG---VLYKLG-EPDEFLTKLLNGIKGVGKKEINLgIVDPRDIR----FETNN 202

                          250       260
                   ....*....|....*....|....
gi 1823416726  249 YYRYTGSLTTPPCSEIVEWIVFRK 272
Cdd:PLN02179   203 FYRYIGSLTIPPCTEGVIWTVVKR 226
FN3 cd00063
Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein ...
 349-438 1.42e-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: 53.65  E-value: 1.42e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823416726  349 PPVNMKVQPVNRTALLVTWNQPETIyHPPIMNYMISYSWTKNEDEKEktFTKDSDKDLKAIISHVSPDILYLFRVQAVcR 428
Cdd:cd00063      3 PPTNLRVTDVTSTSVTLSWTPPEDD-GGPITGYVVEYREKGSGDWKE--VEVTPGSETSYTLTGLKPGTEYEFRVRAV-N 78

                           90
                   ....*....|
gi 1823416726  429 NEMRSDFSQT 438
Cdd:cd00063     79 GGGESPPSES 88
FN3 smart00060
Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, ...
 349-426 1.54e-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: 1.54e-08
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1823416726   349 PPVNMKVQPVNRTALLVTWNQPEtiyHPPIMNYMISYSWTKNEDEKEKTFTKDSDKDLKAIISHVSPDILYLFRVQAV 426
Cdd:smart00060    3 PPSNLRVTDVTSTSVTLSWEPPP---DDGITGYIVGYRVEYREEGSEWKEVNVTPSSTSYTLTGLKPGTEYEFRVRAV 77
fn3 pfam00041
Fibronectin type III domain;
349-426 1.37e-07

Fibronectin type III domain;


Pssm-ID: 394996 [Multi-domain]  Cd Length: 85  Bit Score: 50.49  E-value: 1.37e-07
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1823416726  349 PPVNMKVQPVNRTALLVTWNQPETiYHPPIMNYMISYsWTKNEDEKEKTFTKDSDKDlKAIISHVSPDILYLFRVQAV 426
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 ...
 825-1098 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: 641.32  E-value: 0e+00
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823416726  825 FSEDFEEVQRCTADMNITAEHSNHPDNKHKNRYINILAYDHSRVKLRPLPGKDSKHSDYINANYVDGYNKAKAYIATQGP 904
Cdd:cd17667      1 FSEDFEEVQRCTADMNITAEHSNHPDNKHKNRYINILAYDHSRVKLRPLPGKDSKHSDYINANYVDGYNKAKAYIATQGP 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823416726  905 LKSTFEDFWRMIWEQNTGIIVMITNLVEKGRRKCDQYWPTENSEEYGNIIVTLKSTNVHACYTVRRFTIRNTKMKKGQKG 984
Cdd:cd17667     81 LKSTFEDFWRMIWEQNTGIIVMITNLVEKGRRKCDQYWPTENSEEYGNIIVTLKSTKIHACYTVRRFSIRNTKVKKGQKG 160

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823416726  985 NPKGRQNERTVIQYHYTQWPDMGVPEYALPVLTFVRRSSAARTPDMGPVVVHCSAGVGRTGTYIVIDSMLQQIKDKSTVN 1064
Cdd:cd17667    161 NPKGRQNERTVIQYHYTQWPDMGVPEYALPVLTFVRRSSAARTPEMGPVLVHCSAGVGRTGTYIVIDSMLQQIKDKSTVN 240

                          250       260       270
                   ....*....|....*....|....*....|....
gi 1823416726 1065 VLGFLKHIRTQRNYLVQTEEQYIFIHDALLEAIL 1098
Cdd:cd17667    241 VLGFLKHIRTQRNYLVQTEEQYIFIHDALLEAIL 274
R-PTP-G-2 cd17670
PTP-like domain of receptor-type tyrosine-protein phosphatase G, repeat 2; Receptor-type ...
 1182-1386 8.21e-158

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: 8.21e-158
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823416726 1182 YINASYIMGYYRSNEFIITQHPLPHTTKDFWRMIWDHNAQIIVMLPDNQSLAEDEFVYWPSREESMNCEAFTVTLISKDR 1261
Cdd:cd17670      1 YINASYIMGYYRSNEFIITQHPLPHTTKDFWRMIWDHNAQIIVMLPDNQGLAEDEFVYWPSREESMNCEAFTVTLISKDR 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823416726 1262 LCLSNEEQIIIHDFILEATQDDYVLEVRHFQCPKWPNPDAPISSTFELINVIKEEALTRDGPTIVHDEYGAVSAGTLCAL 1341
Cdd:cd17670     81 LCLSNEEQIIIHDFILEATQDDYVLEVRHFQCPKWPNPDAPISSTFELINVIKEEALTRDGPTIVHDEFGAVSAGTLCAL 160

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*
gi 1823416726 1342 TTLSQQLENENAVDVFQVAKMINLMRPGVFTDIEQYQFLYKAMLS 1386
Cdd:cd17670    161 TTLSQQLENENAVDVYQVAKMINLMRPGVFTDIEQYQFLYKAMLS 205
R5-PTPc-1 cd14549
catalytic domain of R5 subfamily receptor-type tyrosine-protein phosphatases, repeat 1; The R5 ...
 883-1091 9.59e-150

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: 452.19  E-value: 9.59e-150
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823416726  883 YINANYVDGYNKAKAYIATQGPLKSTFEDFWRMIWEQNTGIIVMITNLVEKGRRKCDQYWPTENSEEYGNIIVTLKSTNV 962
Cdd:cd14549      1 YINANYVDGYNKARAYIATQGPLPSTFDDFWRMVWEQNSAIIVMITNLVERGRRKCDQYWPKEGTETYGNIQVTLLSTEV 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823416726  963 HACYTVRRFTIRNTKMKKgqkgnPKGRQNERTVIQYHYTQWPDMGVPEYALPVLTFVRRSSAARTPDMGPVVVHCSAGVG 1042
Cdd:cd14549     81 LATYTVRTFSLKNLKLKK-----VKGRSSERVVYQYHYTQWPDHGVPDYTLPVLSFVRKSSAANPPGAGPIVVHCSAGVG 155

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*....
gi 1823416726 1043 RTGTYIVIDSMLQQIKDKSTVNVLGFLKHIRTQRNYLVQTEEQYIFIHD 1091
Cdd:cd14549    156 RTGTYIVIDSMLQQIQDKGTVNVFGFLKHIRTQRNYLVQTEEQYIFIHD 204
R-PTP-Z-2 cd17669
catalytic domain of receptor-type tyrosine-protein phosphatase Z, repeat 2; Receptor-type ...
 1182-1385 1.13e-138

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: 1.13e-138
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823416726 1182 YINASYIMGYYRSNEFIITQHPLPHTTKDFWRMIWDHNAQIIVMLPDNQSLAEDEFVYWPSREESMNCEAFTVTLISKDR 1261
Cdd:cd17669      1 YINASYIMGYYQSNEFIITQHPLLHTIKDFWRMIWDHNAQLIVMLPDGQNMAEDEFVYWPNKDEPINCETFKVTLIAEEH 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823416726 1262 LCLSNEEQIIIHDFILEATQDDYVLEVRHFQCPKWPNPDAPISSTFELINVIKEEALTRDGPTIVHDEYGAVSAGTLCAL 1341
Cdd:cd17669     81 KCLSNEEKLIIQDFILEATQDDYVLEVRHFQCPKWPNPDSPISKTFELISIIKEEAANRDGPMIVHDEHGGVTAGTFCAL 160

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....
gi 1823416726 1342 TTLSQQLENENAVDVFQVAKMINLMRPGVFTDIEQYQFLYKAML 1385
Cdd:cd17669    161 TTLMHQLEKENSVDVYQVAKMINLMRPGVFTDIEQYQFLYKAIL 204
R-PTPc-Z-1 cd17668
catalytic domain of receptor-type tyrosine-protein phosphatase Z, repeat 1; Receptor-type ...
 883-1094 3.48e-136

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: 416.30  E-value: 3.48e-136
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823416726  883 YINANYVDGYNKAKAYIATQGPLKSTFEDFWRMIWEQNTGIIVMITNLVEKGRRKCDQYWPTENSEEYGNIIVTLKSTNV 962
Cdd:cd17668      1 YINANYVDGYNKPKAYIAAQGPLKSTAEDFWRMIWEHNVEVIVMITNLVEKGRRKCDQYWPADGSEEYGNFLVTQKSVQV 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823416726  963 HACYTVRRFTIRNTKMKKGQKgnpKGRQNERTVIQYHYTQWPDMGVPEYALPVLTFVRRSSAARTPDMGPVVVHCSAGVG 1042
Cdd:cd17668     81 LAYYTVRNFTLRNTKIKKGSQ---KGRPSGRVVTQYHYTQWPDMGVPEYTLPVLTFVRKASYAKRHAVGPVVVHCSAGVG 157

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|..
gi 1823416726 1043 RTGTYIVIDSMLQQIKDKSTVNVLGFLKHIRTQRNYLVQTEEQYIFIHDALL 1094
Cdd:cd17668    158 RTGTYIVLDSMLQQIQHEGTVNIFGFLKHIRSQRNYLVQTEEQYVFIHDALV 209
R5-PTP-2 cd14550
PTP-like domain of R5 subfamily receptor-type tyrosine-protein phosphatases, repeat 2; The R5 ...
 1182-1382 2.88e-126

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: 389.37  E-value: 2.88e-126
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823416726 1182 YINASYIMGYYRSNEFIITQHPLPHTTKDFWRMIWDHNAQIIVMLPDNQsLAEDEFVYWPSREESMNCEAFTVTLISKDR 1261
Cdd:cd14550      1 YINASYLQGYRRSNEFIITQHPLEHTIKDFWQMIWDHNSQTIVMLTDNE-LNEDEPIYWPTKEKPLECETFKVTLSGEDH 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823416726 1262 LCLSNEEQIIIHDFILEATQDDYVLEVRHFQCPKWPNPDAPISSTFELINVIKEEALTRDGPTIVHDEYGAVSAGTLCAL 1341
Cdd:cd14550     80 SCLSNEIRLIVRDFILESTQDDYVLEVRQFQCPSWPNPCSPIHTVFELINTVQEWAQQRDGPIVVHDRYGGVQAATFCAL 159

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|.
gi 1823416726 1342 TTLSQQLENENAVDVFQVAKMINLMRPGVFTDIEQYQFLYK 1382
Cdd:cd14550    160 TTLHQQLEHESSVDVYQVAKLYHLMRPGVFTSKEDYQFLYK 200
alpha_CARP_receptor_like cd03122
Carbonic anhydrase alpha related protein, receptor_like subfamily. Carbonic anhydrase related ...
 67-319 1.43e-119

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: 373.61  E-value: 1.43e-119
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823416726   67 GPEHWVTSSEKCG-GSHQSPIDIMDHLAHVGDEYQELQLDGFDNESsNKTWMKNTGKTVAILLKD---DYFVSGAGLPGR 142
Cdd:cd03122      1 NPKHWAKKYPACGeGRQQSPIDIVEDTQVQRQGLQPLHFDGYEELT-ASTTLENTGKTVILRLEGnssDPFVSGGPLLGR 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823416726  143 FKAEKVEFHWGQSNgSAGSEHSINGKRFPVEMQIYFYNPDDFDSFgTAVLENRVVGAMAVFFQVSPRDNSALDPIIHGLK 222
Cdd:cd03122     80 YKFSEITFHWGTCN-SDGSEHSIDGHKFPLEMQILHRNTDFFDSF-EAIKSPGGVLALAYLFELSHEDNPFLDPIIEGLR 157

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823416726  223 GVVHHEKETFLDPFVLRELLPTSLGSYYRYTGSLTTPPCSEIVEWIVFRKPVPISYHQLEAFYSIFTTEQQDhVKSVEYL 302
Cdd:cd03122    158 NVSRPGKEVELPPFPLSDLLPPFTDKYYSYEGSLTTPPCSETVEWIVFREPVPISSRQLEAFRELLTRRQDG-VMSGDYL 236

                          250
                   ....*....|....*..
gi 1823416726  303 RNNFRPQQRLNNRKVSK 319
Cdd:cd03122    237 PNNGRPQQPLGSRTVFS 253
PTPc smart00194
Protein tyrosine phosphatase, catalytic domain;
824-1095 2.16e-119

Protein tyrosine phosphatase, catalytic domain;


Pssm-ID: 214550 [Multi-domain]  Cd Length: 259  Bit Score: 373.53  E-value: 2.16e-119
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823416726   824 GFSEDFEEVQRCTADMnITAEHSNHPDNKHKNRYINILAYDHSRVKLRPLPGKDSkhsDYINANYVDGYNKAKAYIATQG 903
Cdd:smart00194    1 GLEEEFEKLDRLKPDD-ESCTVAAFPENRDKNRYKDVLPYDHTRVKLKPPPGEGS---DYINASYIDGPNGPKAYIATQG 76

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823416726   904 PLKSTFEDFWRMIWEQNTGIIVMITNLVEKGRRKCDQYWPTENSE--EYGNIIVTLKSTNVHACYTVRRFTIRNTkmkkg 981
Cdd:smart00194   77 PLPSTVEDFWRMVWEQKVTVIVMLTELVEKGREKCAQYWPDEEGEplTYGDITVTLKSVEKVDDYTIRTLEVTNT----- 151

                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823416726   982 qkgnpkGRQNERTVIQYHYTQWPDMGVPEYALPVLTFVRRSSAARTPDMGPVVVHCSAGVGRTGTYIVIDSMLQQIKDKS 1061
Cdd:smart00194  152 ------GCSETRTVTHYHYTNWPDHGVPESPESILDLIRAVRKSQSTSTGPIVVHCSAGVGRTGTFIAIDILLQQLEAGK 225

                           250       260       270
                    ....*....|....*....|....*....|....
gi 1823416726  1062 TVNVLGFLKHIRTQRNYLVQTEEQYIFIHDALLE 1095
Cdd:smart00194  226 EVDIFEIVKELRSQRPGMVQTEEQYIFLYRAILE 259
R-PTPc-LAR-1 cd14553
catalytic domain of LAR family receptor-type tyrosine-protein phosphatases, repeat 1; The LAR ...
 851-1097 2.60e-118

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: 369.42  E-value: 2.60e-118
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823416726  851 NKHKNRYINILAYDHSRVKLRPLPGKDSkhSDYINANYVDGYNKAKAYIATQGPLKSTFEDFWRMIWEQNTGIIVMITNL 930
Cdd:cd14553      3 NKPKNRYANVIAYDHSRVILQPIEGVPG--SDYINANYCDGYRKQNAYIATQGPLPETFGDFWRMVWEQRSATIVMMTKL 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823416726  931 VEKGRRKCDQYWPTENSEEYGNIIVTLKSTNVHACYTVRRFTIRNTkmkkgqkgnpkGRQNERTVIQYHYTQWPDMGVPE 1010
Cdd:cd14553     81 EERSRVKCDQYWPTRGTETYGLIQVTLLDTVELATYTVRTFALHKN-----------GSSEKREVRQFQFTAWPDHGVPE 149

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823416726 1011 YALPVLTFVRRSSAARTPDMGPVVVHCSAGVGRTGTYIVIDSMLQQIKDKSTVNVLGFLKHIRTQRNYLVQTEEQYIFIH 1090
Cdd:cd14553    150 HPTPFLAFLRRVKACNPPDAGPIVVHCSAGVGRTGCFIVIDSMLERIKHEKTVDIYGHVTCLRAQRNYMVQTEDQYIFIH 229


                   ....*..
gi 1823416726 1091 DALLEAI 1097
Cdd:cd14553    230 DALLEAV 236
Y_phosphatase pfam00102
Protein-tyrosine phosphatase;
851-1095 1.49e-112

Protein-tyrosine phosphatase;


Pssm-ID: 459674 [Multi-domain]  Cd Length: 234  Bit Score: 353.86  E-value: 1.49e-112
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823416726  851 NKHKNRYINILAYDHSRVKLRPLPGkdskHSDYINANYVDGYNKAKAYIATQGPLKSTFEDFWRMIWEQNTGIIVMITNL 930
Cdd:pfam00102    1 NLEKNRYKDVLPYDHTRVKLTGDPG----PSDYINASYIDGYKKPKKYIATQGPLPNTVEDFWRMVWEEKVTIIVMLTEL 76

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823416726  931 VEKGRRKCDQYWPTEN--SEEYGNIIVTLKSTNVH-ACYTVRRFTIRNtkmkkgqkgnpKGRQNERTVIQYHYTQWPDMG 1007
Cdd:pfam00102   77 EEKGREKCAQYWPEEEgeSLEYGDFTVTLKKEKEDeKDYTVRTLEVSN-----------GGSEETRTVKHFHYTGWPDHG 145

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823416726 1008 VPEYALPVLTFVRR-SSAARTPDMGPVVVHCSAGVGRTGTYIVIDSMLQQIKDKSTVNVLGFLKHIRTQRNYLVQTEEQY 1086
Cdd:pfam00102  146 VPESPNSLLDLLRKvRKSSLDGRSGPIVVHCSAGIGRTGTFIAIDIALQQLEAEGEVDIFQIVKELRSQRPGMVQTLEQY 225


                   ....*....
gi 1823416726 1087 IFIHDALLE 1095
Cdd:pfam00102  226 IFLYDAILE 234
R-PTPc-F-1 cd14626
catalytic domain of receptor-type tyrosine-protein phosphatase F, repeat 1; Receptor-type ...
 813-1097 1.25e-101

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: 325.45  E-value: 1.25e-101
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823416726  813 HISELYSNNQHGFSEDFEEVQrctADMNITAEHSNHPDNKHKNRYINILAYDHSRVKLRPLPGKDSkhSDYINANYVDGY 892
Cdd:cd14626      6 NIERLKANDGLKFSQEYESID---PGQQFTWENSNLEVNKPKNRYANVIAYDHSRVILTSVDGVPG--SDYINANYIDGY 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823416726  893 NKAKAYIATQGPLKSTFEDFWRMIWEQNTGIIVMITNLVEKGRRKCDQYWPTENSEEYGNIIVTLKSTNVHACYTVRRFT 972
Cdd:cd14626     81 RKQNAYIATQGPLPETLSDFWRMVWEQRTATIVMMTRLEEKSRVKCDQYWPIRGTETYGMIQVTLLDTVELATYSVRTFA 160

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823416726  973 IRNTkmkkgqkgnpkGRQNERTVIQYHYTQWPDMGVPEYALPVLTFVRRSSAARTPDMGPVVVHCSAGVGRTGTYIVIDS 1052
Cdd:cd14626    161 LYKN-----------GSSEKREVRQFQFMAWPDHGVPEYPTPILAFLRRVKACNPPDAGPMVVHCSAGVGRTGCFIVIDA 229

                          250       260       270       280
                   ....*....|....*....|....*....|....*....|....*
gi 1823416726 1053 MLQQIKDKSTVNVLGFLKHIRTQRNYLVQTEEQYIFIHDALLEAI 1097
Cdd:cd14626    230 MLERMKHEKTVDIYGHVTCMRSQRNYMVQTEDQYIFIHEALLEAA 274
R-PTPc-S-1 cd14625
catalytic domain of receptor-type tyrosine-protein phosphatase S, repeat 1; Receptor-type ...
 805-1097 1.56e-97

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: 1.56e-97
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823416726  805 IPVKQFVKHISELYSNNQHGFSEDFEEVQrctADMNITAEHSNHPDNKHKNRYINILAYDHSRVKLRPLPGKDSkhSDYI 884
Cdd:cd14625      4 IPISELAEHTERLKANDNLKLSQEYESID---PGQQFTWEHSNLEVNKPKNRYANVIAYDHSRVILQPIEGIMG--SDYI 78

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823416726  885 NANYVDGYNKAKAYIATQGPLKSTFEDFWRMIWEQNTGIIVMITNLVEKGRRKCDQYWPTENSEEYGNIIVTLKSTNVHA 964
Cdd:cd14625     79 NANYIDGYRKQNAYIATQGPLPETFGDFWRMVWEQRSATVVMMTKLEEKSRIKCDQYWPSRGTETYGMIQVTLLDTIELA 158

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823416726  965 CYTVRRFTIRNTkmkkgqkgnpkGRQNERTVIQYHYTQWPDMGVPEYALPVLTFVRRSSAARTPDMGPVVVHCSAGVGRT 1044
Cdd:cd14625    159 TFCVRTFSLHKN-----------GSSEKREVRQFQFTAWPDHGVPEYPTPFLAFLRRVKTCNPPDAGPIVVHCSAGVGRT 227

                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|...
gi 1823416726 1045 GTYIVIDSMLQQIKDKSTVNVLGFLKHIRTQRNYLVQTEEQYIFIHDALLEAI 1097
Cdd:cd14625    228 GCFIVIDAMLERIKHEKTVDIYGHVTLMRSQRNYMVQTEDQYSFIHDALLEAV 280
PTPc cd00047
catalytic domain of protein tyrosine phosphatases; Protein tyrosine phosphatases (PTP, EC 3.1. ...
 883-1091 2.87e-96

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: 307.29  E-value: 2.87e-96
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823416726  883 YINANYVDGYNKAKAYIATQGPLKSTFEDFWRMIWEQNTGIIVMITNLVEKGRRKCDQYWPTENSE--EYGNIIVTLKST 960
Cdd:cd00047      1 YINASYIDGYRGPKEYIATQGPLPNTVEDFWRMVWEQKVSVIVMLTNLVEKGREKCERYWPEEGGKplEYGDITVTLVSE 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823416726  961 NVHACYTVRRFTIRNtkmkkgqkgnpKGRQNERTVIQYHYTQWPDMGVPEYALPVLTFVRRSSAARTPDMGPVVVHCSAG 1040
Cdd:cd00047     81 EELSDYTIRTLELSP-----------KGCSESREVTHLHYTGWPDHGVPSSPEDLLALVRRVRKEARKPNGPIVVHCSAG 149

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|.
gi 1823416726 1041 VGRTGTYIVIDSMLQQIKDKSTVNVLGFLKHIRTQRNYLVQTEEQYIFIHD 1091
Cdd:cd00047    150 VGRTGTFIAIDILLERLEAEGEVDVFEIVKALRKQRPGMVQTLEQYEFIYE 200
Carb_anhydrase smart01057
Eukaryotic-type carbonic anhydrase; Carbonic anhydrases are zinc metalloenzymes which catalyse ...
 60-316 3.54e-96

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: 309.24  E-value: 3.54e-96
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823416726    60 WAYSGTYGPEHWVTSS-EKCGGSHQSPIDIMDHLAHVGDEYQELQldgFDNESSNKTWMKNTGKTVAILLKDD-YFVSGA 137
Cdd:smart01057    1 WGYEGKNGPEHWGKLDpPFCGGKRQSPIDIVTAEAQYDPSLKPLK---LSYDQPTAKRILNNGHTVQVNFDDDgSTLSGG 77

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823416726   138 GLPGRFKAEKVEFHWGqSNGSAGSEHSINGKRFPVEMQIYFYNPDDfdSFGTAVLENRVVGAMAVFFQVSPRDNSALDPI 217
Cdd:smart01057   78 PLPGRYRLKQFHFHWG-GSDSEGSEHTIDGKRFPLELHLVHYNSKG--SFSEAVSKPGGLAVVAVFFKVGAEENPALQAI 154

                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823416726   218 IHGLKGVVHHEKETFLDPFVLRELLPTSLGSYYRYTGSLTTPPCSEIVEWIVFRKPVPISYHQLEAFYSIFTTEQQdhvk 297
Cdd:smart01057  155 LDHLPLIKYKGQETELTPFDLSSLLPASTRHYYTYNGSLTTPPCSEGVTWIVFKEPITISTEQLEKFRTLLPMEGN---- 230

                           250
                    ....*....|....*....
gi 1823416726   298 svEYLRNNFRPQQRLNNRK 316
Cdd:smart01057  231 --EPLVNNARPLQPLNGRV 247
R-PTPc-D-1 cd14624
catalytic domain of receptor-type tyrosine-protein phosphatase D, repeat 1; Receptor-type ...
 805-1097 2.67e-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: 308.20  E-value: 2.67e-95
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823416726  805 IPVKQFVKHISELYSNNQHGFSEDFEEVQrctADMNITAEHSNHPDNKHKNRYINILAYDHSRVKLRPLPGKDSkhSDYI 884
Cdd:cd14624      4 IPILELADHIERLKANDNLKFSQEYESID---PGQQFTWEHSNLEVNKPKNRYANVIAYDHSRVLLSAIEGIPG--SDYI 78

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823416726  885 NANYVDGYNKAKAYIATQGPLKSTFEDFWRMIWEQNTGIIVMITNLVEKGRRKCDQYWPTENSEEYGNIIVTLKSTNVHA 964
Cdd:cd14624     79 NANYIDGYRKQNAYIATQGALPETFGDFWRMIWEQRSATVVMMTKLEERSRVKCDQYWPSRGTETYGLIQVTLLDTVELA 158

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823416726  965 CYTVRRFTIRNTkmkkgqkgnpkGRQNERTVIQYHYTQWPDMGVPEYALPVLTFVRRSSAARTPDMGPVVVHCSAGVGRT 1044
Cdd:cd14624    159 TYCVRTFALYKN-----------GSSEKREVRQFQFTAWPDHGVPEHPTPFLAFLRRVKTCNPPDAGPMVVHCSAGVGRT 227

                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|...
gi 1823416726 1045 GTYIVIDSMLQQIKDKSTVNVLGFLKHIRTQRNYLVQTEEQYIFIHDALLEAI 1097
Cdd:cd14624    228 GCFIVIDAMLERIKHEKTVDIYGHVTLMRAQRNYMVQTEDQYIFIHDALLEAV 280
Carb_anhydrase pfam00194
Eukaryotic-type carbonic anhydrase;
67-320 7.05e-94

Eukaryotic-type carbonic anhydrase;


Pssm-ID: 459707 [Multi-domain]  Cd Length: 252  Bit Score: 303.03  E-value: 7.05e-94
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823416726   67 GPEHWVTSSEKCGGSHQSPIDIMDHLAHVGDEYQELQLDGFDNESSNKTwMKNTGKTVAILLKDDY--FVSGAGLPGRFK 144
Cdd:pfam00194    2 GPEHWGKVYPSCGGKRQSPINIDTRKVRYDPSLPPLTFQGYDVPPGKNT-LTNNGHTVQVSLDDGDpsTISGGPLATRYR 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823416726  145 AEKVEFHWGqSNGSAGSEHSINGKRFPVEMQIYFYNpDDFDSFGTAVLENRVVGAMAVFFQVSPRDNSALDPIIHGLKGV 224
Cdd:pfam00194   81 LVQFHFHWG-STDSRGSEHTIDGKRYPAELHIVHYN-SKYKSFDEAAKHPDGLAVLGVFFEVGDENNPYLQPIVSALDNI 158

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823416726  225 VHHEKETFLDPFVLRELLPTSLGSYYRYTGSLTTPPCSEIVEWIVFRKPVPISYHQLEAFYSIFTTEQQDHvksVEYLRN 304
Cdd:pfam00194  159 KYKGKSVLLPPFDLSDLLPEDLTSYYTYNGSLTTPPCSESVTWIVFKEPISISEEQLEAFRTLLFSDGGEE---PRPLVN 235

                          250
                   ....*....|....*.
gi 1823416726  305 NFRPQQRLNNRKVSKS 320
Cdd:pfam00194  236 NFRPTQPLNGRVVFAS 251
R3-PTPc cd14548
catalytic domain of R3 subfamily receptor-type tyrosine-protein phosphatases and similar ...
 856-1090 1.00e-93

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


Pssm-ID: 350396 [Multi-domain]  Cd Length: 222  Bit Score: 301.20  E-value: 1.00e-93
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823416726  856 RYINILAYDHSRVKLRPLPgkDSKHSDYINANYVDGYNKAKAYIATQGPLKSTFEDFWRMIWEQNTGIIVMITNLVEKGR 935
Cdd:cd14548      1 RYTNILPYDHSRVKLIPIN--EEEGSDYINANYIPGYNSPREFIATQGPLPGTKDDFWRMVWEQNSHTIVMLTQCMEKGR 78

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823416726  936 RKCDQYWPTENSE-EYGNIIVTLKSTNVHACYTVRRFTIrntkmkkgqkgnpKGRQNERTVIQYHYTQWPDMGVPEYALP 1014
Cdd:cd14548     79 VKCDHYWPFDQDPvYYGDITVTMLSESVLPDWTIREFKL-------------ERGDEVRSVRQFHFTAWPDHGVPEAPDS 145

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1823416726 1015 VLTFVRRSSAARTPDMGPVVVHCSAGVGRTGTYIVIDSMLQQIKDKSTVNVLGFLKHIRTQRNYLVQTEEQYIFIH 1090
Cdd:cd14548    146 LLRFVRLVRDYIKQEKGPTIVHCSAGVGRTGTFIALDRLLQQIESEDYVDIFGIVYDLRKHRPLMVQTEAQYIFLH 221
PTPc-N9 cd14543
catalytic domain of tyrosine-protein phosphatase non-receptor type 9; Tyrosine-protein ...
 822-1090 1.78e-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: 296.97  E-value: 1.78e-91
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823416726  822 QHGFSEDFEEVQRCTADMniTAEHSNHPDNKHKNRYINILAYDHSRVKLRPLPGKDSkhSDYINANYVDGYNKAKAYIAT 901
Cdd:cd14543      2 KRGIYEEYEDIRREPPAG--TFLCSLAPANQEKNRYGDVLCLDQSRVKLPKRNGDER--TDYINANFMDGYKQKNAYIAT 77

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823416726  902 QGPLKSTFEDFWRMIWEQNTGIIVMITNLVEKGRRKCDQYWPTE--NSEEYGNIIVTLKSTNVHACYTVRRFTIRNTKMK 979
Cdd:cd14543     78 QGPLPKTYSDFWRMVWEQKVLVIVMTTRVVERGRVKCGQYWPLEegSSLRYGDLTVTNLSVENKEHYKKTTLEIHNTETD 157

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823416726  980 KGqkgnpkgrqneRTVIQYHYTQWPDMGVPEYALPVLTF---VRRSSAARTPDMG----------PVVVHCSAGVGRTGT 1046
Cdd:cd14543    158 ES-----------RQVTHFQFTSWPDFGVPSSAAALLDFlgeVRQQQALAVKAMGdrwkghppgpPIVVHCSAGIGRTGT 226

                          250       260       270       280
                   ....*....|....*....|....*....|....*....|....
gi 1823416726 1047 YIVIDSMLQQIKDKSTVNVLGFLKHIRTQRNYLVQTEEQYIFIH 1090
Cdd:cd14543    227 FCTLDICLSQLEDVGTLNVMQTVRRMRTQRAFSIQTPDQYYFCY 270
R-PTPc-T-1 cd14630
catalytic domain of receptor-type tyrosine-protein phosphatase T, repeat 1; Receptor-type ...
 850-1098 4.71e-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: 280.37  E-value: 4.71e-86
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823416726  850 DNKHKNRYINILAYDHSRVKLRPLPGkdSKHSDYINANYVDGYNKAKAYIATQGPLKSTFEDFWRMIWEQNTGIIVMITN 929
Cdd:cd14630      2 ENRNKNRYGNIISYDHSRVRLQLLDG--DPHSDYINANYIDGYHRPRHYIATQGPMQETVKDFWRMIWQENSASVVMVTN 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823416726  930 LVEKGRRKCDQYWPtENSEEYGNIIVTLKSTNVHACYTVRRFTIRNtkmkkgqkgnpKGRQNERTVIQYHYTQWPDMGVP 1009
Cdd:cd14630     80 LVEVGRVKCVRYWP-DDTEVYGDIKVTLIETEPLAEYVIRTFTVQK-----------KGYHEIREIRQFHFTSWPDHGVP 147

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823416726 1010 EYALPVLTFVRRSSAARTPDMGPVVVHCSAGVGRTGTYIVIDSMLQQIKDKSTVNVLGFLKHIRTQRNYLVQTEEQYIFI 1089
Cdd:cd14630    148 CYATGLLGFVRQVKFLNPPDAGPIVVHCSAGAGRTGCFIAIDIMLDMAENEGVVDIFNCVRELRAQRVNMVQTEEQYVFV 227


                   ....*....
gi 1823416726 1090 HDALLEAIL 1098
Cdd:cd14630    228 HDAILEACL 236
R-PTPc-A-1 cd14621
catalytic domain of receptor-type tyrosine-protein phosphatase A, repeat 1; Receptor-type ...
 805-1104 1.06e-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: 276.13  E-value: 1.06e-83
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823416726  805 IPVKQFVKHISELYSNNQHGFSEDFEEVQRCTadMNITAEHSNHPDNKHKNRYINILAYDHSRVKLRPLPGkdSKHSDYI 884
Cdd:cd14621      8 LPVDKLEEEINRRMADDNKLFREEFNALPACP--IQATCEAASKEENKEKNRYVNILPYDHSRVHLTPVEG--VPDSDYI 83

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823416726  885 NANYVDGYNKAKAYIATQGPLKSTFEDFWRMIWEQNTGIIVMITNLVEKGRRKCDQYWPTENSEEYGNIIVTLKSTNVHA 964
Cdd:cd14621     84 NASFINGYQEKNKFIAAQGPKEETVNDFWRMIWEQNTATIVMVTNLKERKECKCAQYWPDQGCWTYGNIRVSVEDVTVLV 163

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823416726  965 CYTVRRFTIRntkmkkgQKGNPKGRQNERTVIQYHYTQWPDMGVPEYALPVLTFVRRSSAARTPDMGPVVVHCSAGVGRT 1044
Cdd:cd14621    164 DYTVRKFCIQ-------QVGDVTNKKPQRLITQFHFTSWPDFGVPFTPIGMLKFLKKVKNCNPQYAGAIVVHCSAGVGRT 236

                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823416726 1045 GTYIVIDSMLQQIKDKSTVNVLGFLKHIRTQRNYLVQTEEQYIFIHDALLEAILGKETEV 1104
Cdd:cd14621    237 GTFIVIDAMLDMMHAERKVDVYGFVSRIRAQRCQMVQTDMQYVFIYQALLEHYLYGDTEL 296
alpha_CA cd00326
Carbonic anhydrase alpha (vertebrate-like) group. Carbonic anhydrases (CAs) are ...
 80-317 2.21e-82

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: 269.54  E-value: 2.21e-82
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823416726   80 GSHQSPIDIMDHLAHVGDEYQELQLDGFDNESsnkTWMKNTGKTVAILLKDD-YFVSGAGLPGRFKAEKVEFHWGqSNGS 158
Cdd:cd00326      1 GKRQSPINIVTSAVVYDPSLPPLNFDYYPTTS---LTLVNNGHTVQVNFDDDgGTLSGGGLPGRYKLVQFHFHWG-SENS 76

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823416726  159 AGSEHSINGKRFPVEMQIYFYNPDDFDSfgTAVLENRVVGAMAVFFQVSPRDNSALDPIIHGLKGVVHHEKETFLDPFVL 238
Cdd:cd00326     77 PGSEHTIDGKRYPLELHLVHYNSDYYSS--EAAKKPGGLAVLGVFFEVGEKENPFLKKILDALPKIKYKGKETTLPPFDL 154

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1823416726  239 RELLPTSLGSYYRYTGSLTTPPCSEIVEWIVFRKPVPISYHQLEAFYSIFTTEqqdhvksVEYLRNNFRPQQRLNNRKV 317
Cdd:cd00326    155 SDLLPSSLRDYYTYEGSLTTPPCSEGVTWIVFKEPITISKEQLEAFRSLLDRE-------GKPLVNNYRPVQPLNGRVV 226
R-PTPc-M-1 cd14633
catalytic domain of receptor-type tyrosine-protein phosphatase M, repeat 1; Receptor-type ...
 810-1098 1.02e-80

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: 266.91  E-value: 1.02e-80
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823416726  810 FVKHISELYSNNQHGFSEDFE---EVQRCTADmnitaeHSNHPDNKHKNRYINILAYDHSRVKLRPLPGKdsKHSDYINA 886
Cdd:cd14633      2 LLQHITQMKCAEGYGFKEEYEsffEGQSAPWD------SAKKDENRMKNRYGNIIAYDHSRVRLQPIEGE--TSSDYING 73

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823416726  887 NYVDGYNKAKAYIATQGPLKSTFEDFWRMIWEQNTGIIVMITNLVEKGRRKCDQYWPtENSEEYGNIIVTLKSTNVHACY 966
Cdd:cd14633     74 NYIDGYHRPNHYIATQGPMQETIYDFWRMVWHENTASIIMVTNLVEVGRVKCCKYWP-DDTEIYKDIKVTLIETELLAEY 152

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823416726  967 TVRRFTIRNtkmkkgqkgnpKGRQNERTVIQYHYTQWPDMGVPEYALPVLTFVRRSSAARTPDMGPVVVHCSAGVGRTGT 1046
Cdd:cd14633    153 VIRTFAVEK-----------RGVHEIREIRQFHFTGWPDHGVPYHATGLLGFVRQVKSKSPPNAGPLVVHCSAGAGRTGC 221

                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|..
gi 1823416726 1047 YIVIDSMLQQIKDKSTVNVLGFLKHIRTQRNYLVQTEEQYIFIHDALLEAIL 1098
Cdd:cd14633    222 FIVIDIMLDMAEREGVVDIYNCVRELRSRRVNMVQTEEQYVFIHDAILEACL 273
PTPc smart00194
Protein tyrosine phosphatase, catalytic domain;
1127-1385 2.73e-80

Protein tyrosine phosphatase, catalytic domain;


Pssm-ID: 214550 [Multi-domain]  Cd Length: 259  Bit Score: 264.91  E-value: 2.73e-80
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823416726  1127 LEKQFKLVTQCNAKYVECFSAQKDCNKEKNRNSSVVPSERARVGLAPLPGmKGTDYINASYIMGYYRSNEFIITQHPLPH 1206
Cdd:smart00194    2 LEEEFEKLDRLKPDDESCTVAAFPENRDKNRYKDVLPYDHTRVKLKPPPG-EGSDYINASYIDGPNGPKAYIATQGPLPS 80

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823416726  1207 TTKDFWRMIWDHNAQIIVMLPDNQSL-AEDEFVYWPSRE-ESMNCEAFTVTLISKDRLclsneEQIIIHDFILEATQDDY 1284
Cdd:smart00194   81 TVEDFWRMVWEQKVTVIVMLTELVEKgREKCAQYWPDEEgEPLTYGDITVTLKSVEKV-----DDYTIRTLEVTNTGCSE 155

                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823416726  1285 VLEVRHFQCPKWPNPDAP--ISSTFELINVIKEEALTRDGPTIVHDEYGAVSAGTLCALTTLSQQLENENAVDVFQVAKM 1362
Cdd:smart00194  156 TRTVTHYHYTNWPDHGVPesPESILDLIRAVRKSQSTSTGPIVVHCSAGVGRTGTFIAIDILLQQLEAGKEVDIFEIVKE 235

                           250       260
                    ....*....|....*....|...
gi 1823416726  1363 INLMRPGVFTDIEQYQFLYKAML 1385
Cdd:smart00194  236 LRSQRPGMVQTEEQYIFLYRAIL 258
R-PTPc-B cd14617
catalytic domain of receptor-type tyrosine-protein phosphatase B; Receptor-type ...
 855-1090 8.80e-80

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: 262.16  E-value: 8.80e-80
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823416726  855 NRYINILAYDHSRVKLRPLpgKDSKHSDYINANYVDGYNKAKAYIATQGPLKSTFEDFWRMIWEQNTGIIVMITNLVEKG 934
Cdd:cd14617      1 NRYNNILPYDSTRVKLSNV--DDDPCSDYINASYIPGNNFRREYIATQGPLPGTKDDFWKMVWEQNVHNIVMVTQCVEKG 78

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823416726  935 RRKCDQYWPTE-NSEEYGNIIVTLKSTNVHACYTVRRFTIRNtkmkKGQKGNPkgrqneRTVIQYHYTQWPDMGVPEYAL 1013
Cdd:cd14617     79 RVKCDHYWPADqDSLYYGDLIVQMLSESVLPEWTIREFKICS----EEQLDAP------RLVRHFHYTVWPDHGVPETTQ 148

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1823416726 1014 PVLTFVR--RSSAARTPDMGPVVVHCSAGVGRTGTYIVIDSMLQQIKDKSTVNVLGFLKHIRTQRNYLVQTEEQYIFIH 1090
Cdd:cd14617    149 SLIQFVRtvRDYINRTPGSGPTVVHCSAGVGRTGTFIALDRILQQLDSKDSVDIYGAVHDLRLHRVHMVQTECQYVYLH 227
Y_phosphatase pfam00102
Protein-tyrosine phosphatase;
1152-1385 3.24e-79

Protein-tyrosine phosphatase;


Pssm-ID: 459674 [Multi-domain]  Cd Length: 234  Bit Score: 261.02  E-value: 3.24e-79
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823416726 1152 NKEKNRNSSVVPSERARVGLAPLPGmkGTDYINASYIMGYYRSNEFIITQHPLPHTTKDFWRMIWDHNAQIIVMLPDNQS 1231
Cdd:pfam00102    1 NLEKNRYKDVLPYDHTRVKLTGDPG--PSDYINASYIDGYKKPKKYIATQGPLPNTVEDFWRMVWEEKVTIIVMLTELEE 78

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823416726 1232 LA-EDEFVYWP-SREESMNCEAFTVTLISKDrlclSNEEQIIIHDFILEATQDDYVLEVRHFQCPKWPNPDAP--ISSTF 1307
Cdd:pfam00102   79 KGrEKCAQYWPeEEGESLEYGDFTVTLKKEK----EDEKDYTVRTLEVSNGGSEETRTVKHFHYTGWPDHGVPesPNSLL 154

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1823416726 1308 ELINVIKEEALT-RDGPTIVHDEYGAVSAGTLCALTTLSQQLENENAVDVFQVAKMINLMRPGVFTDIEQYQFLYKAML 1385
Cdd:pfam00102  155 DLLRKVRKSSLDgRSGPIVVHCSAGIGRTGTFIAIDIALQQLEAEGEVDIFQIVKELRSQRPGMVQTLEQYIFLYDAIL 233
R-PTPc-J cd14615
catalytic domain of receptor-type tyrosine-protein phosphatase J; Receptor-type ...
 855-1095 8.50e-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: 259.36  E-value: 8.50e-79
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823416726  855 NRYINILAYDHSRVKLRPLpgkDSKHSDYINANYVDGYNKAKAYIATQGPLKSTFEDFWRMIWEQNTGIIVMITNLVEKG 934
Cdd:cd14615      1 NRYNNVLPYDISRVKLSVQ---SHSTDDYINANYMPGYNSKKEFIAAQGPLPNTVKDFWRMVWEKNVYAIVMLTKCVEQG 77

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823416726  935 RRKCDQYWPTENSEEYGNIIVTLKSTNVHACYTVRRFTIRNtkMKKGQKgnpkgrqneRTVIQYHYTQWPDMGVPEYALP 1014
Cdd:cd14615     78 RTKCEEYWPSKQKKDYGDITVTMTSEIVLPEWTIRDFTVKN--AQTNES---------RTVRHFHFTSWPDHGVPETTDL 146

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823416726 1015 VLTF--VRRSSAARTPDMGPVVVHCSAGVGRTGTYIVIDSMLQQIKDKSTVNVLGFLKHIRTQRNYLVQTEEQYIFIHDA 1092
Cdd:cd14615    147 LINFrhLVREYMKQNPPNSPILVHCSAGVGRTGTFIAIDRLIYQIENENVVDVYGIVYDLRMHRPLMVQTEDQYVFLNQC 226


                   ...
gi 1823416726 1093 LLE 1095
Cdd:cd14615    227 ALD 229
R-PTPc-typeIIb-1 cd14555
catalytic domain of type IIb (or R2B) subfamily receptor-type tyrosine-protein phosphatases, ...
 883-1098 2.25e-77

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: 254.46  E-value: 2.25e-77
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823416726  883 YINANYVDGYNKAKAYIATQGPLKSTFEDFWRMIWEQNTGIIVMITNLVEKGRRKCDQYWPtENSEEYGNIIVTLKSTNV 962
Cdd:cd14555      1 YINANYIDGYHRPNHYIATQGPMQETVYDFWRMVWQENSASIVMVTNLVEVGRVKCSRYWP-DDTEVYGDIKVTLVETEP 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823416726  963 HACYTVRRFTIRNtkmkkgqkgnpKGRQNERTVIQYHYTQWPDMGVPEYALPVLTFVRRSSAARTPDMGPVVVHCSAGVG 1042
Cdd:cd14555     80 LAEYVVRTFALER-----------RGYHEIREVRQFHFTGWPDHGVPYHATGLLGFIRRVKASNPPSAGPIVVHCSAGAG 148

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 1823416726 1043 RTGTYIVIDSMLQQIKDKSTVNVLGFLKHIRTQRNYLVQTEEQYIFIHDALLEAIL 1098
Cdd:cd14555    149 RTGCYIVIDIMLDMAEREGVVDIYNCVKELRSRRVNMVQTEEQYIFIHDAILEACL 204
PTPc-KIM cd14547
catalytic domain of the kinase interaction motif (KIM) family of protein-tyrosine phosphatases; ...
 855-1090 9.52e-77

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: 253.47  E-value: 9.52e-77
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823416726  855 NRYINILAYDHSRVKLRPLPgkDSKHSDYINANYVDGYN-KAKAYIATQGPLKSTFEDFWRMIWEQNTGIIVMITNLVEK 933
Cdd:cd14547      1 NRYKTILPNEHSRVCLPSVD--DDPLSSYINANYIRGYDgEEKAYIATQGPLPNTVADFWRMVWQEKTPIIVMITNLTEA 78

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823416726  934 gRRKCDQYWPTENSEEYGNIIVTLKSTNVHACYTVRRFTIRNtkmkkgqkgnpkgRQNERTVIQYHYTQWPDMGVPEYAL 1013
Cdd:cd14547     79 -KEKCAQYWPEEENETYGDFEVTVQSVKETDGYTVRKLTLKY-------------GGEKRYLKHYWYTSWPDHKTPEAAQ 144

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1823416726 1014 PVLTFVRR--SSAARTPDMGPVVVHCSAGVGRTGTYIVIDSMLQQIKDKSTVNVLGFLKHIRTQRNYLVQTEEQYIFIH 1090
Cdd:cd14547    145 PLLSLVQEveEARQTEPHRGPIVVHCSAGIGRTGCFIATSIGCQQLREEGVVDVLGIVCQLRLDRGGMVQTAEQYEFVH 223
R-PTPc-H cd14619
catalytic domain of receptor-type tyrosine-protein phosphatase H; Receptor-type ...
 855-1097 2.01e-75

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: 250.19  E-value: 2.01e-75
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823416726  855 NRYINILAYDHSRVKLRPLpgKDSKHSDYINANYVDGYNKAKAYIATQGPLKSTFEDFWRMIWEQNTGIIVMITNLVEKG 934
Cdd:cd14619      1 NRFRNVLPYDWSRVPLKPI--HEEPGSDYINANYMPGYWSSQEFIATQGPLPQTVGDFWRMIWEQQSSTIVMLTNCMEAG 78

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823416726  935 RRKCDQYWPTENSE-EYGNIIVTLKSTNVHACYTVRRFTIRNTKmkkgqkgnpkgRQNERTVIQYHYTQWPDMGVPEYAL 1013
Cdd:cd14619     79 RVKCEHYWPLDYTPcTYGHLRVTVVSEEVMENWTVREFLLKQVE-----------EQKTLSVRHFHFTAWPDHGVPSSTD 147

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823416726 1014 PVLTFVR--RSSAARTPDMGPVVVHCSAGVGRTGTYIVIDSMLQQIKDKSTVNVLGFLKHIRTQRNYLVQTEEQYIFIHD 1091
Cdd:cd14619    148 TLLAFRRllRQWLDQTMSGGPTVVHCSAGVGRTGTLIALDVLLQQLQSEGLLGPFSFVQKMRENRPLMVQTESQYVFLHQ 227


                   ....*.
gi 1823416726 1092 ALLEAI 1097
Cdd:cd14619    228 CILDFL 233
R-PTPc-E-1 cd14620
catalytic domain of receptor-type tyrosine-protein phosphatase E, repeat 1; Receptor-type ...
 857-1095 3.09e-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: 249.47  E-value: 3.09e-75
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823416726  857 YINILAYDHSRVKLRPLPGKDSkhSDYINANYVDGYNKAKAYIATQGPLKSTFEDFWRMIWEQNTGIIVMITNLVEKGRR 936
Cdd:cd14620      1 YPNILPYDHSRVILSQLDGIPC--SDYINASYIDGYKEKNKFIAAQGPKQETVNDFWRMVWEQKSATIVMLTNLKERKEE 78

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823416726  937 KCDQYWPTENSEEYGNIIVTLKSTNVHACYTVRRFTIrntkmkkgQKGNPKGRQNERTVIQYHYTQWPDMGVPEYALPVL 1016
Cdd:cd14620     79 KCYQYWPDQGCWTYGNIRVAVEDCVVLVDYTIRKFCI--------QPQLPDGCKAPRLVTQLHFTSWPDFGVPFTPIGML 150

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1823416726 1017 TFVRRSSAARTPDMGPVVVHCSAGVGRTGTYIVIDSMLQQIKDKSTVNVLGFLKHIRTQRNYLVQTEEQYIFIHDALLE 1095
Cdd:cd14620    151 KFLKKVKSVNPVHAGPIVVHCSAGVGRTGTFIVIDAMIDMMHAEQKVDVFEFVSRIRNQRPQMVQTDMQYSFIYQALLE 229
R-PTP-LAR-2 cd14554
PTP-like domain of the LAR family receptor-type tyrosine-protein phosphatases, repeat 2; The ...
 846-1094 3.01e-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: 247.05  E-value: 3.01e-74
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823416726  846 SNHPDNKHKNRYINILAYDHSRVKLRPLPGKDSkhSDYINANYVDGYNKAKAYIATQGPLKSTFEDFWRMIWEQNTGIIV 925
Cdd:cd14554      1 ANLPCNKFKNRLVNILPYESTRVCLQPIRGVEG--SDYINASFIDGYRQRGAYIATQGPLAETTEDFWRMLWEHNSTIIV 78

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823416726  926 MITNLVEKGRRKCDQYWPTENSEEYGNIIVtlkstNVHACYTVRRFTIRNTKMKKGQKGnpkgrqNERTVIQYHYTQWPD 1005
Cdd:cd14554     79 MLTKLREMGREKCHQYWPAERSARYQYFVV-----DPMAEYNMPQYILREFKVTDARDG------QSRTVRQFQFTDWPE 147

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823416726 1006 MGVPEYALPVLTFVRR--SSAARTPDMGPVVVHCSAGVGRTGTYIVIDSMLQQIKDKSTVNVLGFLKHIRTQRNYLVQTE 1083
Cdd:cd14554    148 QGVPKSGEGFIDFIGQvhKTKEQFGQEGPITVHCSAGVGRTGVFITLSIVLERMRYEGVVDVFQTVKLLRTQRPAMVQTE 227

                          250
                   ....*....|.
gi 1823416726 1084 EQYIFIHDALL 1094
Cdd:cd14554    228 DQYQFCYRAAL 238
PTPc-N11_6 cd14544
catalytic domain of tyrosine-protein phosphatase non-receptor type 11 and type 6; ...
 851-1093 5.06e-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: 246.99  E-value: 5.06e-74
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823416726  851 NKHKNRYINILAYDHSRVKLRPLPgKDSKHSDYINANYVDGYN-------KAKAYIATQGPLKSTFEDFWRMIWEQNTGI 923
Cdd:cd14544      1 NKGKNRYKNILPFDHTRVILKDRD-PNVPGSDYINANYIRNENegpttdeNAKTYIATQGCLENTVSDFWSMVWQENSRV 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823416726  924 IVMITNLVEKGRRKCDQYWPTE-NSEEYGNIIVTLKSTNVHACYTVRRFtirntKMKKGQKGNPkgrqnERTVIQYHYTQ 1002
Cdd:cd14544     80 IVMTTKEVERGKNKCVRYWPDEgMQKQYGPYRVQNVSEHDTTDYTLREL-----QVSKLDQGDP-----IREIWHYQYLS 149

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823416726 1003 WPDMGVPEYALPVLTFV----RRSSAarTPDMGPVVVHCSAGVGRTGTYIVIDSMLQQIKDKS---TVNVLGFLKHIRTQ 1075
Cdd:cd14544    150 WPDHGVPSDPGGVLNFLedvnQRQES--LPHAGPIVVHCSAGIGRTGTFIVIDMLLDQIKRKGldcDIDIQKTIQMVRSQ 227

                          250
                   ....*....|....*...
gi 1823416726 1076 RNYLVQTEEQYIFIHDAL 1093
Cdd:cd14544    228 RSGMVQTEAQYKFIYVAV 245
R-PTPc-O cd14614
catalytic domain of receptor-type tyrosine-protein phosphatase O; Receptor-type ...
 840-1090 1.15e-72

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


Pssm-ID: 350462 [Multi-domain]  Cd Length: 245  Bit Score: 242.87  E-value: 1.15e-72
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823416726  840 NITAEHSNHPDNKHKNRYINILAYDHSRVKLRPLpgKDSKHSDYINANYVDGYNKAKAYIATQGPLKSTFEDFWRMIWEQ 919
Cdd:cd14614      1 DIPHFAADLPVNRCKNRYTNILPYDFSRVKLVSM--HEEEGSDYINANYIPGYNSPQEYIATQGPLPETRNDFWKMVLQQ 78

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823416726  920 NTGIIVMITNLVEKGRRKCDQYWP-TENSEEYGNIIVTLKSTNVHACYTVRRFTIRNTkmkkgqkgnpkgrQNERTVIQY 998
Cdd:cd14614     79 KSQIIVMLTQCNEKRRVKCDHYWPfTEEPVAYGDITVEMLSEEEQPDWAIREFRVSYA-------------DEVQDVMHF 145

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823416726  999 HYTQWPDMGVP--EYALPVLTFVR--RSSAARTPdmGPVVVHCSAGVGRTGTYIVIDSMLQQIKDKSTVNVLGFLKHIRT 1074
Cdd:cd14614    146 NYTAWPDHGVPtaNAAESILQFVQmvRQQAVKSK--GPMIIHCSAGVGRTGTFIALDRLLQHIRDHEFVDILGLVSEMRS 223

                          250
                   ....*....|....*.
gi 1823416726 1075 QRNYLVQTEEQYIFIH 1090
Cdd:cd14614    224 YRMSMVQTEEQYIFIH 239
R-PTPc-U-1 cd14632
catalytic domain of receptor-type tyrosine-protein phosphatase U, repeat 1; Receptor-type ...
 883-1098 1.34e-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: 1.34e-72
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823416726  883 YINANYVDGYNKAKAYIATQGPLKSTFEDFWRMIWEQNTGIIVMITNLVEKGRRKCDQYWPtENSEEYGNIIVTLKSTNV 962
Cdd:cd14632      1 YINANYIDGYHRSNHFIATQGPKQEMVYDFWRMVWQEHCSSIVMITKLVEVGRVKCSKYWP-DDSDTYGDIKITLLKTET 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823416726  963 HACYTVRRFTIRNtkmkkgqkgnpKGRQNERTVIQYHYTQWPDMGVPEYALPVLTFVRRSSAARTPDMGPVVVHCSAGVG 1042
Cdd:cd14632     80 LAEYSVRTFALER-----------RGYSARHEVKQFHFTSWPEHGVPYHATGLLAFIRRVKASTPPDAGPVVVHCSAGAG 148

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 1823416726 1043 RTGTYIVIDSMLQQIKDKSTVNVLGFLKHIRTQRNYLVQTEEQYIFIHDALLEAIL 1098
Cdd:cd14632    149 RTGCYIVLDVMLDMAECEGVVDIYNCVKTLCSRRINMIQTEEQYIFIHDAILEACL 204
R-PTPc-V cd14618
catalytic domain of receptor-type tyrosine-protein phosphatase V; Receptor-type ...
 855-1094 1.40e-72

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: 241.77  E-value: 1.40e-72
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823416726  855 NRYINILAYDHSRVKLRPLPGKdsKHSDYINANYVDGYNKAKAYIATQGPLKSTFEDFWRMIWEQNTGIIVMITNLVEKG 934
Cdd:cd14618      1 NRYPHVLPYDHSRVRLSQLGGE--PHSDYINANFIPGYTSPQEFIATQGPLKKTIEDFWRLVWEQQVCNIIMLTVGMENG 78

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823416726  935 RRKCDQYWPTENSE-EYGNIIVTLKSTNVHACYTVRRFTIRNtkmkkgqkgnpKGRQNERTVIQYHYTQWPDMGVPEYAL 1013
Cdd:cd14618     79 RVLCDHYWPSESTPvSYGHITVHLLAQSSEDEWTRREFKLWH-----------EDLRKERRVKHLHYTAWPDHGIPESTS 147

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823416726 1014 PVLTFVR--RSSAARTPDMGPVVVHCSAGVGRTGTYIVIDSMLQQIKDKSTVNVLGFLKHIRTQRNYLVQTEEQYIFIHD 1091
Cdd:cd14618    148 SLMAFRElvREHVQATKGKGPTLVHCSAGVGRSGTFIALDRLLRQLKEEKVVDVFNTVYILRMHRYLMIQTLSQYIFLHS 227


                   ...
gi 1823416726 1092 ALL 1094
Cdd:cd14618    228 CIL 230
R-PTPc-K-1 cd14631
catalytic domain of receptor-type tyrosine-protein phosphatase K, repeat 1; Receptor-type ...
 867-1098 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: 241.08  E-value: 1.78e-72
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823416726  867 RVKLRPLpgKDSKHSDYINANYVDGYNKAKAYIATQGPLKSTFEDFWRMIWEQNTGIIVMITNLVEKGRRKCDQYWPtEN 946
Cdd:cd14631      1 RVILQPV--EDDPSSDYINANYIDGYQRPSHYIATQGPVHETVYDFWRMIWQEQSACIVMVTNLVEVGRVKCYKYWP-DD 77

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823416726  947 SEEYGNIIVTLKSTNVHACYTVRRFTIRNtkmkkgqkgnpKGRQNERTVIQYHYTQWPDMGVPEYALPVLTFVRRSSAAR 1026
Cdd:cd14631     78 TEVYGDFKVTCVEMEPLAEYVVRTFTLER-----------RGYNEIREVKQFHFTGWPDHGVPYHATGLLSFIRRVKLSN 146

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1823416726 1027 TPDMGPVVVHCSAGVGRTGTYIVIDSMLQQIKDKSTVNVLGFLKHIRTQRNYLVQTEEQYIFIHDALLEAIL 1098
Cdd:cd14631    147 PPSAGPIVVHCSAGAGRTGCYIVIDIMLDMAEREGVVDIYNCVKALRSRRINMVQTEEQYIFIHDAILEACL 218
PTP_fungal cd18533
fungal protein tyrosine phosphatases; This subfamily contains Saccharomyces cerevisiae ...
 883-1091 4.99e-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: 239.46  E-value: 4.99e-72
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823416726  883 YINANYVD-GYNKAKAYIATQGPLKSTFEDFWRMIWEQNTGIIVMITNLVEKGRRKCDQYWPTENSE-EYGNIIVTL--K 958
Cdd:cd18533      1 YINASYITlPGTSSKRYIATQGPLPATIGDFWKMIWQNNVGVIVMLTPLVENGREKCDQYWPSGEYEgEYGDLTVELvsE 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823416726  959 STNVHACYTVRRFTIRNTKMKKgqkgnpkgrqneRTVIQYHYTQWPDMGVPEYALPVLTFVRRSSA--ARTPDMGPVVVH 1036
Cdd:cd18533     81 EENDDGGFIVREFELSKEDGKV------------KKVYHIQYKSWPDFGVPDSPEDLLTLIKLKRElnDSASLDPPIIVH 148

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1823416726 1037 CSAGVGRTGTYIVIDSMLQQIKDKSTVN---------VLGFLKHIRTQRNYLVQTEEQYIFIHD 1091
Cdd:cd18533    149 CSAGVGRTGTFIALDSLLDELKRGLSDSqdledsedpVYEIVNQLRKQRMSMVQTLRQYIFLYD 212
R-PTPc-A-E-1 cd14551
catalytic domain of receptor-type tyrosine-protein phosphatase A and E, repeat 1; ...
 883-1090 1.98e-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: 237.50  E-value: 1.98e-71
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823416726  883 YINANYVDGYNKAKAYIATQGPLKSTFEDFWRMIWEQNTGIIVMITNLVEKGRRKCDQYWPTENSEEYGNIIVTLKSTNV 962
Cdd:cd14551      1 YINASYIDGYQEKNKFIAAQGPKDETVNDFWRMIWEQGSATIVMVTNLKERKEKKCSQYWPDQGCWTYGNLRVRVEDTVV 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823416726  963 HACYTVRRFTIRntkmkkgQKGNPKGRQNERTVIQYHYTQWPDMGVPEYALPVLTFVRRSSAARTPDMGPVVVHCSAGVG 1042
Cdd:cd14551     81 LVDYTTRKFCIQ-------KVNRGIGEKRVRLVTQFHFTSWPDFGVPFTPIGMLKFLKKVKSANPPRAGPIVVHCSAGVG 153

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*...
gi 1823416726 1043 RTGTYIVIDSMLQQIKDKSTVNVLGFLKHIRTQRNYLVQTEEQYIFIH 1090
Cdd:cd14551    154 RTGTFIVIDAMLDMMHAEGKVDVFGFVSRIRQQRSQMVQTDMQYVFIY 201
alpha_CA_IV_XV_like cd03117
Carbonic anhydrase alpha, CA_IV, CA_XV, like isozymes. Carbonic anhydrases (CAs) are ...
 80-319 2.17e-66

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: 224.07  E-value: 2.17e-66
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823416726   80 GSHQSPIDIMDHLAHVGDEYQELQLDGFDNESSNKtWMKNTGKTVAILLKDDYFVSGAGLPGRFKAEKVEFHWGqSNGSA 159
Cdd:cd03117      1 GKRQSPINIVTKKVQYDENLTPFTFTGYDDTTTNW-TITNNGHTVQVTLPDGAKISGGGLPGTYKALQFHFHWG-SNGSP 78

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823416726  160 GSEHSINGKRFPVEMQIYFYNpDDFDSFGTAVLENRVVGAMAVFFQVSPRDNSALDPIIHGLKGVVHHEKETFLDPFVLR 239
Cdd:cd03117     79 GSEHTIDGERYPMELHIVHIK-ESYNSLLEALKDSDGLAVLGFFIEEGEEENTNFDPLISALSNIPQKGGSTNLTPFSLR 157

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823416726  240 ELLPT-SLGSYYRYTGSLTTPPCSEIVEWIVFRKPVPISYHQLEAFYSI--FTTEQQDHVKsveylrNNFRPQQRLNNRK 316
Cdd:cd03117    158 SLLPSvLLTKYYRYNGSLTTPGCNEAVIWTVFEEPIPISRAQLDAFSTVlfFDTDNGQPMV------NNFRPVQPLNGRV 231


                   ...
gi 1823416726  317 VSK 319
Cdd:cd03117    232 VYA 234
R-PTP-D-2 cd14628
PTP-like domain of receptor-type tyrosine-protein phosphatase D, repeat 2; Receptor-type ...
 805-1095 8.35e-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: 8.35e-66
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823416726  805 IPVKQFVKHISELYS----NNQHGFSEDFEEVQRCTADMN--ITAehsNHPDNKHKNRYINILAYDHSRVKLRPLPGKDS 878
Cdd:cd14628      3 VPARNLYAYIQKLTQietgENVTGMELEFKRLASSKAHTSrfISA---NLPCNKFKNRLVNIMPYESTRVCLQPIRGVEG 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823416726  879 khSDYINANYVDGYNKAKAYIATQGPLKSTFEDFWRMIWEQNTGIIVMITNLVEKGRRKCDQYWPTENSEEYGNIIVtlk 958
Cdd:cd14628     80 --SDYINASFIDGYRQQKAYIATQGPLAETTEDFWRMLWEHNSTIVVMLTKLREMGREKCHQYWPAERSARYQYFVV--- 154

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823416726  959 stNVHACYTVRRFTIRNTKMKKGQKGnpkgrqNERTVIQYHYTQWPDMGVPEYALPVLTFVRRSSAARTP--DMGPVVVH 1036
Cdd:cd14628    155 --DPMAEYNMPQYILREFKVTDARDG------QSRTVRQFQFTDWPEQGVPKSGEGFIDFIGQVHKTKEQfgQDGPISVH 226

                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 1823416726 1037 CSAGVGRTGTYIVIDSMLQQIKDKSTVNVLGFLKHIRTQRNYLVQTEEQYIFIHDALLE 1095
Cdd:cd14628    227 CSAGVGRTGVFITLSIVLERMRYEGVVDIFQTVKMLRTQRPAMVQTEDQYQFCYRAALE 285
R-PTP-S-2 cd14627
PTP-like domain of receptor-type tyrosine-protein phosphatase S, repeat 2; Receptor-type ...
 846-1095 2.06e-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: 2.06e-65
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823416726  846 SNHPDNKHKNRYINILAYDHSRVKLRPLPGKDSkhSDYINANYVDGYNKAKAYIATQGPLKSTFEDFWRMIWEQNTGIIV 925
Cdd:cd14627     48 ANLPCNKFKNRLVNIMPYETTRVCLQPIRGVEG--SDYINASFIDGYRQQKAYIATQGPLAETTEDFWRMLWENNSTIVV 125

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823416726  926 MITNLVEKGRRKCDQYWPTENSEEYGNIIVtlkstNVHACYTVRRFTIRNTKMKKGQKGnpkgrqNERTVIQYHYTQWPD 1005
Cdd:cd14627    126 MLTKLREMGREKCHQYWPAERSARYQYFVV-----DPMAEYNMPQYILREFKVTDARDG------QSRTVRQFQFTDWPE 194

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823416726 1006 MGVPEYALPVLTFVRRSSAARTP--DMGPVVVHCSAGVGRTGTYIVIDSMLQQIKDKSTVNVLGFLKHIRTQRNYLVQTE 1083
Cdd:cd14627    195 QGVPKSGEGFIDFIGQVHKTKEQfgQDGPISVHCSAGVGRTGVFITLSIVLERMRYEGVVDIFQTVKMLRTQRPAMVQTE 274

                          250
                   ....*....|..
gi 1823416726 1084 EQYIFIHDALLE 1095
Cdd:cd14627    275 DEYQFCYQAALE 286
PTPc-N1_2 cd14545
catalytic domain of tyrosine-protein phosphatase non-receptor type 1 and type 2; ...
 852-1088 7.56e-65

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: 219.57  E-value: 7.56e-65
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823416726  852 KHKNRYINILAYDHSRVKLRplpgkdSKHSDYINANYVDGYNKAKAYIATQGPLKSTFEDFWRMIWEQNTGIIVMITNLV 931
Cdd:cd14545      1 LNRYRDRDPYDHDRSRVKLK------QGDNDYINASLVEVEEAKRSYILTQGPLPNTSGHFWQMVWEQNSKAVIMLNKLM 74

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823416726  932 EKGRRKCDQYWPTENSE----EYGNIIVTLKSTNVHACYTVRRFTIRNTKMkkgqkgnpkgrQNERTVIQYHYTQWPDMG 1007
Cdd:cd14545     75 EKGQIKCAQYWPQGEGNamifEDTGLKVTLLSEEDKSYYTVRTLELENLKT-----------QETREVLHFHYTTWPDFG 143

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823416726 1008 VPEYALPVLTFVR--RSSAARTPDMGPVVVHCSAGVGRTGTYIVIDSMLQQIKDK--STVNVLGFLKHIRTQRNYLVQTE 1083
Cdd:cd14545    144 VPESPAAFLNFLQkvRESGSLSSDVGPPVVHCSAGIGRSGTFCLVDTCLVLIEKGnpSSVDVKKVLLEMRKYRMGLIQTP 223


                   ....*
gi 1823416726 1084 EQYIF 1088
Cdd:cd14545    224 DQLRF 228
R-PTPc-C-1 cd14557
catalytic domain of receptor-type tyrosine-protein phosphatase C, repeat 1; Receptor-type ...
 883-1090 2.06e-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: 217.39  E-value: 2.06e-64
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823416726  883 YINANYVDGYNKAKAYIATQGPLKSTFEDFWRMIWEQNTGIIVMITNLVEKGRRKCDQYWPT--ENSEEYGNIIVTLKST 960
Cdd:cd14557      1 YINASYIDGFKEPRKYIAAQGPKDETVDDFWRMIWEQKSTVIVMVTRCEEGNRNKCAQYWPSmeEGSRAFGDVVVKINEE 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823416726  961 NVHACYTVRRFTIRNTKMKKGqkgnpkgrqnERTVIQYHYTQWPDMGVPEYALPVLTFVRRSSAARTPDMGPVVVHCSAG 1040
Cdd:cd14557     81 KICPDYIIRKLNINNKKEKGS----------GREVTHIQFTSWPDHGVPEDPHLLLKLRRRVNAFNNFFSGPIVVHCSAG 150

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|
gi 1823416726 1041 VGRTGTYIVIDSMLQQIKDKSTVNVLGFLKHIRTQRNYLVQTEEQYIFIH 1090
Cdd:cd14557    151 VGRTGTYIGIDAMLEGLEAEGRVDVYGYVVKLRRQRCLMVQVEAQYILIH 200
R-PTP-F-2 cd14629
PTP-like domain of receptor-type tyrosine-protein phosphatase F, repeat 2; Receptor-type ...
 846-1095 8.63e-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: 8.63e-64
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823416726  846 SNHPDNKHKNRYINILAYDHSRVKLRPLPGKDSkhSDYINANYVDGYNKAKAYIATQGPLKSTFEDFWRMIWEQNTGIIV 925
Cdd:cd14629     48 ANLPCNKFKNRLVNIMPYELTRVCLQPIRGVEG--SDYINASFIDGYRQQKAYIATQGPLAETTEDFWRMLWEHNSTIVV 125

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823416726  926 MITNLVEKGRRKCDQYWPTENSEEYGNIIVtlkstNVHACYTVRRFTIRNTKMKKGQKGnpkgrqNERTVIQYHYTQWPD 1005
Cdd:cd14629    126 MLTKLREMGREKCHQYWPAERSARYQYFVV-----DPMAEYNMPQYILREFKVTDARDG------QSRTIRQFQFTDWPE 194

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823416726 1006 MGVPEYALPVLTFVRRSSAARTP--DMGPVVVHCSAGVGRTGTYIVIDSMLQQIKDKSTVNVLGFLKHIRTQRNYLVQTE 1083
Cdd:cd14629    195 QGVPKTGEGFIDFIGQVHKTKEQfgQDGPITVHCSAGVGRTGVFITLSIVLERMRYEGVVDMFQTVKTLRTQRPAMVQTE 274

                          250
                   ....*....|..
gi 1823416726 1084 EQYIFIHDALLE 1095
Cdd:cd14629    275 DQYQLCYRAALE 286
PTPc-N11 cd14605
catalytic domain of tyrosine-protein phosphatase non-receptor type 11; Tyrosine-protein ...
 850-1097 8.71e-64

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: 217.58  E-value: 8.71e-64
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823416726  850 DNKHKNRYINILAYDHSRVKLRPlPGKDSKHSDYINANYVDGYNKA--------KAYIATQGPLKSTFEDFWRMIWEQNT 921
Cdd:cd14605      1 ENKNKNRYKNILPFDHTRVVLHD-GDPNEPVSDYINANIIMPEFETkcnnskpkKSYIATQGCLQNTVNDFWRMVFQENS 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823416726  922 GIIVMITNLVEKGRRKCDQYWPTENS-EEYGNIIV-TLKSTNVHacytvrRFTIRNTKMKKGQKGNpkgrqNERTVIQYH 999
Cdd:cd14605     80 RVIVMTTKEVERGKSKCVKYWPDEYAlKEYGVMRVrNVKESAAH------DYILRELKLSKVGQGN-----TERTVWQYH 148

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823416726 1000 YTQWPDMGVPEYALPVLTFVRRSSAAR--TPDMGPVVVHCSAGVGRTGTYIVIDSMLQQIKDKST---VNVLGFLKHIRT 1074
Cdd:cd14605    149 FRTWPDHGVPSDPGGVLDFLEEVHHKQesIMDAGPVVVHCSAGIGRTGTFIVIDILIDIIREKGVdcdIDVPKTIQMVRS 228

                          250       260
                   ....*....|....*....|...
gi 1823416726 1075 QRNYLVQTEEQYIFIHDALLEAI 1097
Cdd:cd14605    229 QRSGMVQTEAQYRFIYMAVQHYI 251
PTPc-N6 cd14606
catalytic domain of tyrosine-protein phosphatase non-receptor type 6; Tyrosine-protein ...
 849-1097 3.62e-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: 3.62e-62
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823416726  849 PDNKHKNRYINILAYDHSRVKLRplpGKDSK--HSDYINANYVDGY-----NKAKAYIATQGPLKSTFEDFWRMIWEQNT 921
Cdd:cd14606     16 PENKSKNRYKNILPFDHSRVILQ---GRDSNipGSDYINANYVKNQllgpdENAKTYIASQGCLEATVNDFWQMAWQENS 92

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823416726  922 GIIVMITNLVEKGRRKCDQYWPTENSE-EYGNIIVTLKSTNVHACYTVRrfTIRNTKMKKGQKgnpkgrqnERTVIQYHY 1000
Cdd:cd14606     93 RVIVMTTREVEKGRNKCVPYWPEVGMQrAYGPYSVTNCGEHDTTEYKLR--TLQVSPLDNGEL--------IREIWHYQY 162

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823416726 1001 TQWPDMGVPEYALPVLTFVRRSSAART--PDMGPVVVHCSAGVGRTGTYIVIDSMLQQIKDK---STVNVLGFLKHIRTQ 1075
Cdd:cd14606    163 LSWPDHGVPSEPGGVLSFLDQINQRQEslPHAGPIIVHCSAGIGRTGTIIVIDMLMENISTKgldCDIDIQKTIQMVRAQ 242

                          250       260
                   ....*....|....*....|..
gi 1823416726 1076 RNYLVQTEEQYIFIHDALLEAI 1097
Cdd:cd14606    243 RSGMVQTEAQYKFIYVAIAQFI 264
alpha_CA_VI_IX_XII_XIV cd03123
Carbonic anhydrase alpha, isozymes VI, IX, XII and XIV. Carbonic anhydrases (CAs) are ...
 67-320 6.87e-62

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: 211.78  E-value: 6.87e-62
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823416726   67 GPEHWVTSSEKCGGSHQSPIDIMDHLAHVGDEYQELQLDGFDNESSNKTWMKNTGKTVAILLKDDYFVSGaGLPGRFKAE 146
Cdd:cd03123      1 GEDHWPKKYPACGGKRQSPIDIQTDIVQFDPSLPPLELVGYDLPGTEEFTLTNNGHTVQLSLPPTMHIRG-GPGTEYTAA 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823416726  147 KVEFHWGQSNGSAGSEHSINGKRFPVEMQIYFYNPDDFDSFGTAVLENRVVGAMAVFFQVSPRDNSALDPIIHGLKGVVH 226
Cdd:cd03123     80 QLHLHWGGRGSLSGSEHTIDGIRFAAELHIVHYNSDKYSSFDEAADKPDGLAVLAILIEVGYPENTYYEKIISHLHEIKY 159

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823416726  227 HEKETFLDPFVLRELLPTSLGSYYRYTGSLTTPPCSEIVEWIVFRKPVPISYHQLEAFY-SIFTTEQQDhvksveyLRNN 305
Cdd:cd03123    160 KGQETTVPGFNVRELLPEDLSHYYRYEGSLTTPPCYESVLWTVFRDPVTLSKEQLETLEnTLMDTHNKT-------LQNN 232

                          250
                   ....*....|....*
gi 1823416726  306 FRPQQRLNNRKVSKS 320
Cdd:cd03123    233 YRATQPLNGRVVEAS 247
R-PTPc-Q cd14616
catalytic domain of receptor-type tyrosine-protein phosphatase Q; Receptor-type ...
 855-1090 1.26e-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: 1.26e-61
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823416726  855 NRYINILAYDHSRVKLRPLPGkdSKHSDYINANYVDGYNKAKAYIATQGPLKSTFEDFWRMIWEQNTGIIVMITNLVEKG 934
Cdd:cd14616      1 NRFPNIKPYNNNRVKLIADAG--VPGSDYINASYISGYLCPNEFIATQGPLPGTVGDFWRMVWETRAKTIVMLTQCFEKG 78

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823416726  935 RRKCDQYWPTENS--EEYGNIIVTLKSTNVHACYTVRRFTIRntkmKKGqkgnpkgrqNERTVIQYHYTQWPDMGVPEYA 1012
Cdd:cd14616     79 RIRCHQYWPEDNKpvTVFGDIVITKLMEDVQIDWTIRDLKIE----RHG---------DYMMVRQCNFTSWPEHGVPESS 145

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1823416726 1013 LPVLTFVRRSSAARTPDMGPVVVHCSAGVGRTGTYIVIDSMLQQIKDKSTVNVLGFLKHIRTQRNYLVQTEEQYIFIH 1090
Cdd:cd14616    146 APLIHFVKLVRASRAHDNTPMIVHCSAGVGRTGVFIALDHLTQHINDHDFVDIYGLVAELRSERMCMVQNLAQYIFLH 223
PTPc-N3_4 cd14541
catalytic domain of tyrosine-protein phosphatase non-receptor type 21 and type 14; ...
 882-1096 3.05e-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: 3.05e-61
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823416726  882 DYINANYVD----GYNKAKAYIATQGPLKSTFEDFWRMIWEQNTGIIVMITNLVEKGRRKCDQYWPTEN-SEEYGNIIVT 956
Cdd:cd14541      1 DYINANYVNmeipGSGIVNRYIAAQGPLPNTCADFWQMVWEQKSTLIVMLTTLVERGRVKCHQYWPDLGeTMQFGNLQIT 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823416726  957 LKSTNVHACYTVRRFTIRNTKMKKgqkgnpkgrqnERTVIQYHYTQWPDMGVPEYALPVLTFVRRSSAARTPDMGPVVVH 1036
Cdd:cd14541     81 CVSEEVTPSFAFREFILTNTNTGE-----------ERHITQMQYLAWPDHGVPDDSSDFLDFVKRVRQNRVGMVEPTVVH 149

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823416726 1037 CSAGVGRTGTYIVIDSMLQQIKDKSTVNVLGFLKHIRTQRNYLVQTEEQYIFIHDALLEA 1096
Cdd:cd14541    150 CSAGIGRTGVLITMETAMCLIEANEPVYPLDIVRTMRDQRAMLIQTPSQYRFVCEAILRV 209
PTPc-N7 cd14612
catalytic domain of tyrosine-protein phosphatase non-receptor type 7; Tyrosine-protein ...
 841-1093 3.47e-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: 3.47e-61
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823416726  841 ITAEHSNHPDNKHKNRYINILAYDHSRVKLRPlPGKDSKHSDYINANYVDGYN-KAKAYIATQGPLKSTFEDFWRMIWEQ 919
Cdd:cd14612      5 VSPEELDIPGHASKDRYKTILPNPQSRVCLRR-AGSQEEEGSYINANYIRGYDgKEKAYIATQGPMLNTVSDFWEMVWQE 83

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823416726  920 NTGIIVMITNLVEKgRRKCDQYWPtENSEEYGNIIVTLKSTNVHACYTVRRFTIrntkmkkgqkgnpKGRQNERTVIQYH 999
Cdd:cd14612     84 ECPIIVMITKLKEK-KEKCVHYWP-EKEGTYGRFEIRVQDMKECDGYTIRDLTI-------------QLEEESRSVKHYW 148

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823416726 1000 YTQWPDMGVPEYALPVLTFVRRSSAAR--TPDMGPVVVHCSAGVGRTGTYIVIDSMLQQIKDKSTVNVLGFLKHIRTQRN 1077
Cdd:cd14612    149 FSSWPDHQTPESAGPLLRLVAEVEESRqtAASPGPIVVHCSAGIGRTGCFIATSIGCQQLKDTGKVDILGIVCQLRLDRG 228

                          250
                   ....*....|....*.
gi 1823416726 1078 YLVQTEEQYIFIHDAL 1093
Cdd:cd14612    229 GMIQTSEQYQFLHHTL 244
PTPc-N1 cd14608
catalytic domain of tyrosine-protein phosphatase non-receptor type 1; Tyrosine-protein ...
 846-1095 4.31e-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: 207.96  E-value: 4.31e-60
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823416726  846 SNHPDNKHKNRYINILAYDHSRVKLRplpgkdSKHSDYINANYVDGYNKAKAYIATQGPLKSTFEDFWRMIWEQNTGIIV 925
Cdd:cd14608     20 AKLPKNKNRNRYRDVSPFDHSRIKLH------QEDNDYINASLIKMEEAQRSYILTQGPLPNTCGHFWEMVWEQKSRGVV 93

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823416726  926 MITNLVEKGRRKCDQYWPTENSEEY----GNIIVTLKSTNVHACYTVRRFTIRNTKMkkgqkgnpkgrQNERTVIQYHYT 1001
Cdd:cd14608     94 MLNRVMEKGSLKCAQYWPQKEEKEMifedTNLKLTLISEDIKSYYTVRQLELENLTT-----------QETREILHFHYT 162

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823416726 1002 QWPDMGVPEYALPVLTFV--RRSSAARTPDMGPVVVHCSAGVGRTGTYIVIDS---MLQQIKDKSTVNVLGFLKHIRTQR 1076
Cdd:cd14608    163 TWPDFGVPESPASFLNFLfkVRESGSLSPEHGPVVVHCSAGIGRSGTFCLADTcllLMDKRKDPSSVDIKKVLLEMRKFR 242

                          250
                   ....*....|....*....
gi 1823416726 1077 NYLVQTEEQYIFIHDALLE 1095
Cdd:cd14608    243 MGLIQTADQLRFSYLAVIE 261
PTPc cd00047
catalytic domain of protein tyrosine phosphatases; Protein tyrosine phosphatases (PTP, EC 3.1. ...
 1182-1382 7.05e-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: 204.06  E-value: 7.05e-60
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823416726 1182 YINASYIMGYYRSNEFIITQHPLPHTTKDFWRMIWDHNAQIIVMLPDNQSLAEDEFV-YWPSR-EESMNCEAFTVTLISK 1259
Cdd:cd00047      1 YINASYIDGYRGPKEYIATQGPLPNTVEDFWRMVWEQKVSVIVMLTNLVEKGREKCErYWPEEgGKPLEYGDITVTLVSE 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823416726 1260 DRLclsneEQIIIHDFILEATQDDYVLEVRHFQCPKWPNPDAP--ISSTFELINVIKEEALTRDGPTIVHDEYGAVSAGT 1337
Cdd:cd00047     81 EEL-----SDYTIRTLELSPKGCSESREVTHLHYTGWPDHGVPssPEDLLALVRRVRKEARKPNGPIVVHCSAGVGRTGT 155

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*
gi 1823416726 1338 LCALTTLSQQLENENAVDVFQVAKMINLMRPGVFTDIEQYQFLYK 1382
Cdd:cd00047    156 FIAIDILLERLEAEGEVDVFEIVKALRKQRPGMVQTLEQYEFIYE 200
PTPc-N5 cd14613
catalytic domain of tyrosine-protein phosphatase non-receptor type 5; Tyrosine-protein ...
 854-1093 8.37e-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: 206.25  E-value: 8.37e-60
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823416726  854 KNRYINILAYDHSRVKLRPlPGKDSKHSDYINANYVDGYN-KAKAYIATQGPLKSTFEDFWRMIWEQNTGIIVMITNLVE 932
Cdd:cd14613     28 KNRYKTILPNPHSRVCLTS-PDQDDPLSSYINANYIRGYGgEEKVYIATQGPTVNTVGDFWRMVWQERSPIIVMITNIEE 106

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823416726  933 KGRrKCDQYWPtENSEEYGNIIVTLKSTNVHACYTVRRFTirntkMKKGQKgnpkgrqnERTVIQYHYTQWPDMGVPEYA 1012
Cdd:cd14613    107 MNE-KCTEYWP-EEQVTYEGIEITVKQVIHADDYRLRLIT-----LKSGGE--------ERGLKHYWYTSWPDQKTPDNA 171

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823416726 1013 LPVLTFVRRSSAART---PDMGPVVVHCSAGVGRTGTYIVIDSMLQQIKDKSTVNVLGFLKHIRTQRNYLVQTEEQYIFI 1089
Cdd:cd14613    172 PPLLQLVQEVEEARQqaePNCGPVIVHCSAGIGRTGCFIATSICCKQLRNEGVVDILRTTCQLRLDRGGMIQTCEQYQFV 251


                   ....
gi 1823416726 1090 HDAL 1093
Cdd:cd14613    252 HHVL 255
PTPc-N18 cd14603
catalytic domain of tyrosine-protein phosphatase non-receptor type 18; Tyrosine-protein ...
 826-1095 1.39e-59

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: 205.83  E-value: 1.39e-59
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823416726  826 SEDFEEVQRCTA----DMNITAEHSNHPDNKHKNRYINILAYDHSRVKLRPLpgKDSKHSDYINANYVDGYNKAKAYIAT 901
Cdd:cd14603      1 AGEFSEIRACSAafkaDYVCSTVAGGRKENVKKNRYKDILPYDQTRVILSLL--QEEGHSDYINANFIKGVDGSRAYIAT 78

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823416726  902 QGPLKSTFEDFWRMIWEQNTGIIVMITNLVEKGRRKCDQYWP-TENSEEYGNIIVT-LKSTNVHACYTVRRFTIrntkmk 979
Cdd:cd14603     79 QGPLSHTVLDFWRMIWQYGVKVILMACREIEMGKKKCERYWAqEQEPLQTGPFTITlVKEKRLNEEVILRTLKV------ 152

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823416726  980 kgqkgnpKGRQNERTVIQYHYTQWPDMGVPEYALPVLTFVRRSSAARTPDMGPVVVHCSAGVGRTGTYIVIDS-----ML 1054
Cdd:cd14603    153 -------TFQKESRSVSHFQYMAWPDHGIPDSPDCMLAMIELARRLQGSGPEPLCVHCSAGCGRTGVICTVDYvrqllLT 225

                          250       260       270       280
                   ....*....|....*....|....*....|....*....|.
gi 1823416726 1055 QQIKDKstVNVLGFLKHIRTQRNYLVQTEEQYIFIHDALLE 1095
Cdd:cd14603    226 QRIPPD--FSIFDVVLEMRKQRPAAVQTEEQYEFLYHTVAQ 264
PTPc-N12 cd14604
catalytic domain of tyrosine-protein phosphatase non-receptor type 12; Tyrosine-protein ...
 807-1101 1.41e-59

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: 207.09  E-value: 1.41e-59
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823416726  807 VKQFVKHISELYSNNQHG---FSEDFEEVQRCTADM-------NITAEHSnhpDNKHKNRYINILAYDHSRVKLR-PLPG 875
Cdd:cd14604      6 LKKFIERVQAMKSTDHNGednFASDFMRLRRLSTKYrtekiypTATGEKE---ENVKKNRYKDILPFDHSRVKLTlKTSS 82

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823416726  876 KDSkhsDYINANYVDGYNKAKAYIATQGPLKSTFEDFWRMIWEQNTGIIVMITNLVEKGRRKCDQYWPT--ENSEEYGNI 953
Cdd:cd14604     83 QDS---DYINANFIKGVYGPKAYIATQGPLANTVIDFWRMIWEYNVAIIVMACREFEMGRKKCERYWPLygEEPMTFGPF 159

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823416726  954 IVTLKSTNVHACYTVRRFTIRntkmkkgqkgnpkgRQNE-RTVIQYHYTQWPDMGVPEYALPVLTFVRRSSAARTPDMGP 1032
Cdd:cd14604    160 RISCEAEQARTDYFIRTLLLE--------------FQNEtRRLYQFHYVNWPDHDVPSSFDSILDMISLMRKYQEHEDVP 225

                          250       260       270       280       290       300       310
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1823416726 1033 VVVHCSAGVGRTGTYIVID---SMLQQIKDKSTVNVLGFLKHIRTQRNYLVQTEEQYIFIHDALLEaILGKE 1101
Cdd:cd14604    226 ICIHCSAGCGRTGAICAIDytwNLLKAGKIPEEFNVFNLIQEMRTQRHSAVQTKEQYELVHRAIAQ-LFEKQ 296
PTPc-N20_13 cd14538
catalytic domain of tyrosine-protein phosphatase non-receptor type 20 and type 13; ...
 883-1097 3.38e-59

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


Pssm-ID: 350386 [Multi-domain]  Cd Length: 207  Bit Score: 202.60  E-value: 3.38e-59
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823416726  883 YINANYV--DGYNKAKAYIATQGPLKSTFEDFWRMIWEQNTGIIVMITNLVEKGRRKCDQYWPtENSEE----YGNIIVT 956
Cdd:cd14538      1 YINASHIriPVGGDTYHYIACQGPLPNTTGDFWQMVWEQKSEVIAMVTQDVEGGKVKCHRYWP-DSLNKplicGGRLEVS 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823416726  957 LKSTNVHACYTVRRFTIRNTKMKKgqkgnpkgrqnERTVIQYHYTQWPDMGVPEYALPVLTFVR--RSSAartpDMGPVV 1034
Cdd:cd14538     80 LEKYQSLQDFVIRRISLRDKETGE-----------VHHITHLNFTTWPDHGTPQSADPLLRFIRymRRIH----NSGPIV 144

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1823416726 1035 VHCSAGVGRTGTYIVIDSMLQQIKDKSTVNVLGFLKHIRTQRNYLVQTEEQYIFIHDALLEAI 1097
Cdd:cd14538    145 VHCSAGIGRTGVLITIDVALGLIERDLPFDIQDIVKDLREQRQGMIQTKDQYIFCYKACLEVL 207
R-PTPc-A-E-2 cd14552
catalytic domain of receptor-type tyrosine-protein phosphatase A and E, repeat 2; ...
 883-1093 6.47e-59

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


Pssm-ID: 350400 [Multi-domain]  Cd Length: 202  Bit Score: 201.73  E-value: 6.47e-59
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823416726  883 YINANYVDGYNKAKAYIATQGPLKSTFEDFWRMIWEQNTGIIVMITNLVEKGRRKCDQYWPTENSEEYGNIIVTLKSTNV 962
Cdd:cd14552      1 YINASFIDGYRQKDAYIATQGPLDHTVEDFWRMIWEWKSCSIVMLTEIKERSQNKCAQYWPEDGSVSSGDITVELKDQTD 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823416726  963 HACYTVRRFTIRNTKMKKgqkgnpkgrqnERTVIQYHYTQWPDMGVPEYALPVLTFVRR-SSAARTPDMGPVVVHCSAGV 1041
Cdd:cd14552     81 YEDYTLRDFLVTKGKGGS-----------TRTVRQFHFHGWPEVGIPDNGKGMIDLIAAvQKQQQQSGNHPITVHCSAGA 149

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|..
gi 1823416726 1042 GRTGTYIVIDSMLQQIKDKSTVNVLGFLKHIRTQRNYLVQTEEQYIFIHDAL 1093
Cdd:cd14552    150 GRTGTFCALSTVLERVKAEGVLDVFQVVKSLRLQRPHMVQTLEQYEFCYKVV 201
PTPc-N3 cd14600
catalytic domain of tyrosine-protein phosphatase non-receptor type 3; Tyrosine-protein ...
 829-1094 1.44e-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: 203.54  E-value: 1.44e-58
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823416726  829 FEEVQRCTADMNITAehSNHPDNKHKNRYINILAYDHSRVKLRplpGKDskhsDYINANYVD----GYNKAKAYIATQGP 904
Cdd:cd14600     20 FEQLYRKKPGLAITC--AKLPQNMDKNRYKDVLPYDATRVVLQ---GNE----DYINASYVNmeipSANIVNKYIATQGP 90

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823416726  905 LKSTFEDFWRMIWEQNTGIIVMITNLVEKGRRKCDQYWP-TENSEEYGNIIVTLKSTNVHACYTVRRFTIRNTkmKKGQk 983
Cdd:cd14600     91 LPHTCAQFWQVVWEQKLSLIVMLTTLTERGRTKCHQYWPdPPDVMEYGGFRVQCHSEDCTIAYVFREMLLTNT--QTGE- 167

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823416726  984 gnpkgrqnERTVIQYHYTQWPDMGVPEYALPVLTFVRRSSAARTpDMGPVVVHCSAGVGRTGTYIVIDSMLQQIKDKSTV 1063
Cdd:cd14600    168 --------ERTVTHLQYVAWPDHGVPDDSSDFLEFVNYVRSKRV-ENEPVLVHCSAGIGRTGVLVTMETAMCLTERNQPV 238

                          250       260       270
                   ....*....|....*....|....*....|.
gi 1823416726 1064 NVLGFLKHIRTQRNYLVQTEEQYIFIHDALL 1094
Cdd:cd14600    239 YPLDIVRKMRDQRAMMVQTSSQYKFVCEAIL 269
R-PTPc-R cd14611
catalytic domain of receptor-type tyrosine-protein phosphatase R; Receptor-type ...
 854-1090 3.12e-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: 3.12e-58
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823416726  854 KNRYINILAYDHSRVKLRPLPGKDSKhSDYINANYVDGY-NKAKAYIATQGPLKSTFEDFWRMIWEQNTGIIVMITNLVE 932
Cdd:cd14611      2 KNRYKTILPNPHSRVCLKPKNSNDSL-STYINANYIRGYgGKEKAFIATQGPMINTVNDFWQMVWQEDSPVIVMITKLKE 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823416726  933 KGRrKCDQYWPtENSEEYGNIIVTLKSTNVHACYTVRRFTIRNtkmkkgqkgnpkGRQNeRTVIQYHYTQWPDMGVPEYA 1012
Cdd:cd14611     81 KNE-KCVLYWP-EKRGIYGKVEVLVNSVKECDNYTIRNLTLKQ------------GSQS-RSVKHYWYTSWPDHKTPDSA 145

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823416726 1013 LPVLTFV------RRSSAARtpdmGPVVVHCSAGVGRTGTYIVIDSMLQQIKDKSTVNVLGFLKHIRTQRNYLVQTEEQY 1086
Cdd:cd14611    146 QPLLQLMldveedRLASPGR----GPVVVHCSAGIGRTGCFIATTIGCQQLKEEGVVDVLSIVCQLRVDRGGMVQTSEQY 221


                   ....
gi 1823416726 1087 IFIH 1090
Cdd:cd14611    222 EFVH 225
PTPc-N2 cd14607
catalytic domain of tyrosine-protein phosphatase non-receptor type 2; Tyrosine-protein ...
 846-1093 2.05e-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: 199.42  E-value: 2.05e-57
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823416726  846 SNHPDNKHKNRYINILAYDHSRVKLRplpgkdSKHSDYINANYVDGYNKAKAYIATQGPLKSTFEDFWRMIWEQNTGIIV 925
Cdd:cd14607     19 AKYPENRNRNRYRDVSPYDHSRVKLQ------NTENDYINASLVVIEEAQRSYILTQGPLPNTCCHFWLMVWQQKTKAVV 92

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823416726  926 MITNLVEKGRRKCDQYWPTENSEEYG----NIIVTLKSTNVHACYTVRRFTIRNtkMKKGQKgnpkgrqneRTVIQYHYT 1001
Cdd:cd14607     93 MLNRIVEKDSVKCAQYWPTDEEEVLSfketGFSVKLLSEDVKSYYTVHLLQLEN--INSGET---------RTISHFHYT 161

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823416726 1002 QWPDMGVPEYALPVLTFV--RRSSAARTPDMGPVVVHCSAGVGRTGTYIVIDS--MLQQIKDKSTVNVLGFLKHIRTQRN 1077
Cdd:cd14607    162 TWPDFGVPESPASFLNFLfkVRESGSLSPEHGPAVVHCSAGIGRSGTFSLVDTclVLMEKKDPDSVDIKQVLLDMRKYRM 241

                          250
                   ....*....|....*.
gi 1823416726 1078 YLVQTEEQYIFIHDAL 1093
Cdd:cd14607    242 GLIQTPDQLRFSYMAV 257
R-PTP-N2 cd14610
PTP-like domain of receptor-type tyrosine-protein phosphatase N2; Receptor-type ...
 816-1097 3.46e-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: 199.90  E-value: 3.46e-57
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823416726  816 ELYSNNQHGFSEDFEEVQRCTADMNITAEhSNHPDNKHKNRYINILAYDHSRVKLRplpGKDSK-HSDYINANYV-DGYN 893
Cdd:cd14610     10 EDHLKNKNRLEKEWEALCAYQAEPNATNV-AQREENVQKNRSLAVLPYDHSRIILK---AENSHsHSDYINASPImDHDP 85

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823416726  894 KAKAYIATQGPLKSTFEDFWRMIWEQNTGIIVMITNLVEKGRRKCDQYWPTENSEEYGNIIVTLKSTNVHaC--YTVRRF 971
Cdd:cd14610     86 RNPAYIATQGPLPATVADFWQMVWESGCVVIVMLTPLAENGVKQCYHYWPDEGSNLYHIYEVNLVSEHIW-CedFLVRSF 164

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823416726  972 TIRNTKMkkgqkgnpkgrqNE-RTVIQYHYTQWPDMGVPEYALPVLTFVRRSSAARTPDMGPVVVHCSAGVGRTGTYIVI 1050
Cdd:cd14610    165 YLKNLQT------------NEtRTVTQFHFLSWNDQGVPASTRSLLDFRRKVNKCYRGRSCPIIVHCSDGAGRSGTYILI 232

                          250       260       270       280
                   ....*....|....*....|....*....|....*....|....*...
gi 1823416726 1051 DSMLQQI-KDKSTVNVLGFLKHIRTQRNYLVQTEEQYIFIHDALLEAI 1097
Cdd:cd14610    233 DMVLNKMaKGAKEIDIAATLEHLRDQRPGMVQTKEQFEFALTAVAEEV 280
PTPc-N22_18_12 cd14542
catalytic domain of tyrosine-protein phosphatase non-receptor type 22, type 18 and type 12; ...
 883-1090 3.60e-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: 196.49  E-value: 3.60e-57
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823416726  883 YINANYVDGYNKAKAYIATQGPLKSTFEDFWRMIWEQNTGIIVMITNLVEKGRRKCDQYWPTENSEE--YGNIIVTLKST 960
Cdd:cd14542      1 YINANFIKGVSGSKAYIATQGPLPNTVLDFWRMIWEYNVQVIVMACREFEMGKKKCERYWPEEGEEQlqFGPFKISLEKE 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823416726  961 NvhacYTVRRFTIRNTKMKKGQKgnpkgrqnERTVIQYHYTQWPDMGVPEYALPVLTFVRRSSAARTPDMGPVVVHCSAG 1040
Cdd:cd14542     81 K----RVGPDFLIRTLKVTFQKE--------SRTVYQFHYTAWPDHGVPSSVDPILDLVRLVRDYQGSEDVPICVHCSAG 148

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|...
gi 1823416726 1041 VGRTGTYIVID---SMLQQIKDKSTVNVLGFLKHIRTQRNYLVQTEEQYIFIH 1090
Cdd:cd14542    149 CGRTGTICAIDyvwNLLKTGKIPEEFSLFDLVREMRKQRPAMVQTKEQYELVY 201
R-PTP-N cd14609
PTP-like domain of receptor-type tyrosine-protein phosphatase N; Receptor-type ...
 851-1097 3.71e-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: 199.49  E-value: 3.71e-57
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823416726  851 NKHKNRYINILAYDHSRVKLRPlpGKDSKHSDYINAN-YVDGYNKAKAYIATQGPLKSTFEDFWRMIWEQNTGIIVMITN 929
Cdd:cd14609     42 NVKKNRNPDFVPYDHARIKLKA--ESNPSRSDYINASpIIEHDPRMPAYIATQGPLSHTIADFWQMVWENGCTVIVMLTP 119

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823416726  930 LVEKGRRKCDQYWPTENSEEYGNIIVTLKSTNVHaC--YTVRRFTIRNTKMkkgqkgnpkgrQNERTVIQYHYTQWPDMG 1007
Cdd:cd14609    120 LVEDGVKQCDRYWPDEGSSLYHIYEVNLVSEHIW-CedFLVRSFYLKNVQT-----------QETRTLTQFHFLSWPAEG 187

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823416726 1008 VPEYALPVLTFVRRSSAARTPDMGPVVVHCSAGVGRTGTYIVIDSMLQQI-KDKSTVNVLGFLKHIRTQRNYLVQTEEQY 1086
Cdd:cd14609    188 IPSSTRPLLDFRRKVNKCYRGRSCPIIVHCSDGAGRTGTYILIDMVLNRMaKGVKEIDIAATLEHVRDQRPGMVRTKDQF 267

                          250
                   ....*....|.
gi 1823416726 1087 IFIHDALLEAI 1097
Cdd:cd14609    268 EFALTAVAEEV 278
alpha_CA_XII_XIV cd03126
Carbonic anhydrase alpha, isozymes XII and XIV. Carbonic anhydrases (CAs) are zinc-containing ...
 67-320 7.29e-57

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: 197.37  E-value: 7.29e-57
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823416726   67 GPEHWVTSSEKCGGSHQSPIDIMDHLAHVGDEYQELQLDGFDNESSNKTWMKNTGKTVAILLKDDYFVSGagLPGRFKAE 146
Cdd:cd03126      1 GENSWPKKYPFCGGVAQSPIDIHTDILQYDSSLPPLEFHGYNVSGTEQFTLTNNGHTVQLSLPPTMHIGG--LPFKYTAS 78

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823416726  147 KVEFHWGQSNGSAGSEHSINGKRFPVEMQIYFYNPDDFDSFGTAVLENRVVGAMAVFFQVSPRdNSALDPIIHGLKGVVH 226
Cdd:cd03126     79 QLHLHWGQRGSPEGSEHTISGKHFAAELHIVHYNSDKYPDISTAMNKSQGLAVLGILIEVGPF-NPSYEKIFSHLHEVKY 157

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823416726  227 HEKETFLDPFVLRELLPTSLGSYYRYTGSLTTPPCSEIVEWIVFRKPVPISYHQLEAFY-SIFTTEQQDHVKSVeylrNN 305
Cdd:cd03126    158 KDQKVSVPGFNVQELLPKRLDEYYRYEGSLTTPPCYPSVLWTVFRNPVQISQEQLLALEtALYSTEEDESREMV----NN 233

                          250
                   ....*....|....*
gi 1823416726  306 FRPQQRLNNRKVSKS 320
Cdd:cd03126    234 YRQVQPFNERLVFAS 248
PTPc-N22 cd14602
catalytic domain of tyrosine-protein phosphatase non-receptor type 22; Tyrosine-protein ...
 854-1095 1.60e-56

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: 195.83  E-value: 1.60e-56
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823416726  854 KNRYINILAYDHSRVKLRPLPGKDSkhSDYINANYVDGYNKAKAYIATQGPLKSTFEDFWRMIWEQNTGIIVMITNLVEK 933
Cdd:cd14602      1 KNRYKDILPYDHSRVELSLITSDED--SDYINANFIKGVYGPRAYIATQGPLSTTLLDFWRMIWEYSVLIIVMACMEFEM 78

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823416726  934 GRRKCDQYW--PTENSEEYGNIIVTLKSTNVHACYTVRRFTIRNTKMKkgqkgnpkgrqneRTVIQYHYTQWPDMGVPEY 1011
Cdd:cd14602     79 GKKKCERYWaePGEMQLEFGPFSVTCEAEKRKSDYIIRTLKVKFNSET-------------RTIYQFHYKNWPDHDVPSS 145

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823416726 1012 ALPVLTFVRRSSAARTPDMGPVVVHCSAGVGRTGTYIVIDSMLQQIKDK---STVNVLGFLKHIRTQRNYLVQTEEQYIF 1088
Cdd:cd14602    146 IDPILELIWDVRCYQEDDSVPICIHCSAGCGRTGVICAIDYTWMLLKDGiipENFSVFSLIQEMRTQRPSLVQTKEQYEL 225


                   ....*..
gi 1823416726 1089 IHDALLE 1095
Cdd:cd14602    226 VYNAVIE 232
PTPc-N21_14 cd14540
catalytic domain of tyrosine-protein phosphatase non-receptor type 21 and type 14; ...
 883-1095 2.43e-56

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


Pssm-ID: 350388 [Multi-domain]  Cd Length: 219  Bit Score: 194.98  E-value: 2.43e-56
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823416726  883 YINANYVDGY--NKAKAYIATQGPLKSTFEDFWRMIWEQNTGIIVMITNLVEKGRRKCDQYWPTENSEE----YGNIIVT 956
Cdd:cd14540      1 YINASHITATvgGKQRFYIAAQGPLQNTVGDFWQMVWEQGVYLVVMVTAEEEGGREKCFRYWPTLGGEHdaltFGEYKVS 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823416726  957 LKSTNVHACYTVRRFTIRNTkmkkgqkgnPKGRqnERTVIQYHYTQWPDMGVPEYALPVLTF------VRRSS----AAR 1026
Cdd:cd14540     81 TKFSVSSGCYTTTGLRVKHT---------LSGQ--SRTVWHLQYTDWPDHGCPEDVSGFLDFleeinsVRRHTnqdvAGH 149

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1823416726 1027 TPDmGPVVVHCSAGVGRTGTYIVIDSMLQQIKDKSTVNVLGFLKHIRTQRNYLVQTEEQYIFIHDALLE 1095
Cdd:cd14540    150 NRN-PPTLVHCSAGVGRTGVVILADLMLYCLDHNEELDIPRVLALLRHQRMLLVQTLAQYKFVYNVLIQ 217
R-PTPc-A-2 cd14623
catalytic domain of receptor-type tyrosine-protein phosphatase A, repeat 2; Receptor-type ...
 856-1095 1.63e-55

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


Pssm-ID: 350471 [Multi-domain]  Cd Length: 228  Bit Score: 192.95  E-value: 1.63e-55
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823416726  856 RYINILAYDHSRVKLRPLPGKDSkhSDYINANYVDGYNKAKAYIATQGPLKSTFEDFWRMIWEQNTGIIVMITNLVEKGR 935
Cdd:cd14623      1 RVLQIIPYEFNRVIIPVKRGEEN--TDYVNASFIDGYRQKDSYIASQGPLQHTIEDFWRMIWEWKSCSIVMLTELEERGQ 78

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823416726  936 RKCDQYWPTENSEEYGNIIVTLKSTNVHACYTVRRFTIRNTKMKKgqkgnpkgrqnERTVIQYHYTQWPDMGVPEYALPV 1015
Cdd:cd14623     79 EKCAQYWPSDGSVSYGDITIELKKEEECESYTVRDLLVTNTRENK-----------SRQIRQFHFHGWPEVGIPSDGKGM 147

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823416726 1016 LTFVRRSSAARTPDMG-PVVVHCSAGVGRTGTYIVIDSMLQQIKDKSTVNVLGFLKHIRTQRNYLVQTEEQYIFIHDALL 1094
Cdd:cd14623    148 INIIAAVQKQQQQSGNhPITVHCSAGAGRTGTFCALSTVLERVKAEGILDVFQTVKSLRLQRPHMVQTLEQYEFCYKVVQ 227


                   .
gi 1823416726 1095 E 1095
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 ...
 883-1097 1.05e-53

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: 186.88  E-value: 1.05e-53
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823416726  883 YINANYVDGYN-KAKAYIATQGPLKSTFEDFWRMIWEQNTGIIVMITNLVEKGRRKCDQYWPTENSEEYGNIIVTLKSTN 961
Cdd:cd14546      1 YINASTIYDHDpRNPAYIATQGPLPHTIADFWQMIWEQGCVVIVMLTRLQENGVKQCARYWPEEGSEVYHIYEVHLVSEH 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823416726  962 V-HACYTVRRFTIRNTKmkkgqkgnpkgRQNERTVIQYHYTQWPDMGVPEYALPVLTFVRRSSAARTPDMGPVVVHCSAG 1040
Cdd:cd14546     81 IwCDDYLVRSFYLKNLQ-----------TSETRTVTQFHFLSWPDEGIPASAKPLLEFRRKVNKSYRGRSCPIVVHCSDG 149

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 1823416726 1041 VGRTGTYIVIDSMLQQI-KDKSTVNVLGFLKHIRTQRNYLVQTEEQYIFIHDALLEAI 1097
Cdd:cd14546    150 AGRTGTYILIDMVLNRMaKGAKEIDIAATLEHLRDQRPGMVKTKDQFEFVLTAVAEEV 207
R-PTPc-E-2 cd14622
catalytic domain of receptor-type tyrosine-protein phosphatase E, repeat 2; Receptor-type ...
 882-1090 5.51e-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: 181.74  E-value: 5.51e-52
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823416726  882 DYINANYVDGYNKAKAYIATQGPLKSTFEDFWRMIWEQNTGIIVMITNLVEKGRRKCDQYWPTENSEEYGNIIVTLKSTN 961
Cdd:cd14622      1 DYINASFIDGYRQKDYFIATQGPLAHTVEDFWRMVWEWKCHTIVMLTELQEREQEKCVQYWPSEGSVTHGEITIEIKNDT 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823416726  962 VHACYTVRRFTIRNTKMKKgqkgnpkgrqnERTVIQYHYTQWPDMGVPEYA---LPVLTFVRRSSaaRTPDMGPVVVHCS 1038
Cdd:cd14622     81 LLETISIRDFLVTYNQEKQ-----------TRLVRQFHFHGWPEIGIPAEGkgmIDLIAAVQKQQ--QQTGNHPIVVHCS 147

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|..
gi 1823416726 1039 AGVGRTGTYIVIDSMLQQIKDKSTVNVLGFLKHIRTQRNYLVQTEEQYIFIH 1090
Cdd:cd14622    148 AGAGRTGTFIALSNILERVKAEGLLDVFQTVKSLRLQRPHMVQTLEQYEFCY 199
R-PTP-LAR-2 cd14554
PTP-like domain of the LAR family receptor-type tyrosine-protein phosphatases, repeat 2; The ...
 1151-1385 2.45e-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: 2.45e-51
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823416726 1151 CNKEKNRNSSVVPSERARVGLAPLPGMKGTDYINASYIMGYYRSNEFIITQHPLPHTTKDFWRMIWDHNAQIIVMLPDNQ 1230
Cdd:cd14554      5 CNKFKNRLVNILPYESTRVCLQPIRGVEGSDYINASFIDGYRQRGAYIATQGPLAETTEDFWRMLWEHNSTIIVMLTKLR 84

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823416726 1231 SLAEDE-FVYWPSrEESMNCEAFTVtliskDRLCLSNEEQIIIHDFILEATQDDYVLEVRHFQCPKWPNPDAPISST--F 1307
Cdd:cd14554     85 EMGREKcHQYWPA-ERSARYQYFVV-----DPMAEYNMPQYILREFKVTDARDGQSRTVRQFQFTDWPEQGVPKSGEgfI 158

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823416726 1308 ELINVIKE--EALTRDGPTIVHDEYGAVSAGTLCALTTLSQQLENENAVDVFQVAKMINLMRPGVFTDIEQYQFLYKAML 1385
Cdd:cd14554    159 DFIGQVHKtkEQFGQEGPITVHCSAGVGRTGVFITLSIVLERMRYEGVVDVFQTVKLLRTQRPAMVQTEDQYQFCYRAAL 238
PTPc_plant_PTP1 cd17658
protein tyrosine phosphatase 1 from Arabidopsis thaliana and similar plant PTPs; Arabidopsis ...
 883-1090 3.84e-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: 3.84e-51
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823416726  883 YINANYV--DGYNKAKAYIATQGPLKSTFEDFWRMIWEQNTGIIVMITNLVEKGRR-KCDQYWPTE--NSEEYGNIIVTL 957
Cdd:cd17658      1 YINASLVetPASESLPKFIATQGPLPHTFEDFWEMVIQQRCPVIIMLTRLVDNYSTaKCADYFPAEenESREFGRISVTN 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823416726  958 KSTNvhacYTVRRFTIRNTKMKKGQKGNPKgrqneRTVIQYHYTQWPDMGVPEYALPVLTFVRRSSAArTPDMGPVVVHC 1037
Cdd:cd17658     81 KKLK----HSQHSITLRVLEVQYIESEEPP-----LSVLHIQYPEWPDHGVPKDTRSVRELLKRLYGI-PPSAGPIVVHC 150

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1823416726 1038 SAGVGRTGTYIVIDSMLQQI--KDKSTVNVLGFLKHIRTQRNYLVQTEEQYIFIH 1090
Cdd:cd17658    151 SAGIGRTGAYCTIHNTIRRIleGDMSAVDLSKTVRKFRSQRIGMVQTQDQYIFCY 205
PTPc-N13 cd14597
catalytic domain of tyrosine-protein phosphatase non-receptor type 13; Tyrosine-protein ...
 850-1094 3.99e-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: 180.41  E-value: 3.99e-51
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823416726  850 DNKHKNRYINILAYDHSRVKLrplpGKDSkhsDYINANYVD---GyNKAKAYIATQGPLKSTFEDFWRMIWEQNTGIIVM 926
Cdd:cd14597      2 ENRKKNRYKNILPYDTTRVPL----GDEG---GYINASFIKmpvG-DEEFVYIACQGPLPTTVADFWQMVWEQKSTVIAM 73

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823416726  927 ITNLVEKGRRKCDQYWPtensEEYGNIIVT---LKSTNVHAcYTVRRFTIRNTKMKKGQKGnpkgrqNERTVIQYHYTQW 1003
Cdd:cd14597     74 MTQEVEGGKIKCQRYWP----EILGKTTMVdnrLQLTLVRM-QQLKNFVIRVLELEDIQTR------EVRHITHLNFTAW 142

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823416726 1004 PDMGVPEYALPVLTFVrrSSAARTPDMGPVVVHCSAGVGRTGTYIVIDSMLQQIKDKSTVNVLGFLKHIRTQRNYLVQTE 1083
Cdd:cd14597    143 PDHDTPSQPEQLLTFI--SYMRHIHKSGPIITHCSAGIGRSGTLICIDVVLGLISKDLDFDISDIVRTMRLQRHGMVQTE 220

                          250
                   ....*....|.
gi 1823416726 1084 EQYIFIHDALL 1094
Cdd:cd14597    221 DQYIFCYQVIL 231
PTPc-N14 cd14599
catalytic domain of tyrosine-protein phosphatase non-receptor type 14; Tyrosine-protein ...
 825-1095 4.47e-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: 182.12  E-value: 4.47e-51
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823416726  825 FSEdFEEVQRCTADMNITAehSNHPDNKHKNRYINILAYDHSRVKLrpLPGKDSkHSDYINANYVDGYNKAKA--YIATQ 902
Cdd:cd14599     15 FTE-YEQIPKKKADGVFTT--ATLPENAERNRIREVVPYEENRVEL--VPTKEN-NTGYINASHIKVTVGGEEwhYIATQ 88

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823416726  903 GPLKSTFEDFWRMIWEQNTGIIVMITNLVEKGRRKCDQYWP----TENSEEYGNIIVTLKSTNVHACYTVRRFTIRNtkM 978
Cdd:cd14599     89 GPLPHTCHDFWQMVWEQGVNVIAMVTAEEEGGRSKSHRYWPklgsKHSSATYGKFKVTTKFRTDSGCYATTGLKVKH--L 166

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823416726  979 KKGQkgnpkgrqnERTVIQYHYTQWPDMGVPEYALPVLTF------VRR-------SSAARTPdmgPVVVHCSAGVGRTG 1045
Cdd:cd14599    167 LSGQ---------ERTVWHLQYTDWPDHGCPEEVQGFLSYleeiqsVRRhtnsmldSTKNCNP---PIVVHCSAGVGRTG 234

                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|
gi 1823416726 1046 TYIVIDSMLQQIKDKSTVNVLGFLKHIRTQRNYLVQTEEQYIFIHDALLE 1095
Cdd:cd14599    235 VVILTELMIGCLEHNEKVEVPVMLRHLREQRMFMIQTIAQYKFVYQVLIQ 284
R-PTP-D-2 cd14628
PTP-like domain of receptor-type tyrosine-protein phosphatase D, repeat 2; Receptor-type ...
 1102-1390 8.45e-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: 181.85  E-value: 8.45e-51
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823416726 1102 TEVSANQLHSYVNSILIPGIGGK-TRLEKQFKLVTQCNAKYVECFSAQKDCNKEKNRNSSVVPSERARVGLAPLPGMKGT 1180
Cdd:cd14628      1 TEVPARNLYAYIQKLTQIETGENvTGMELEFKRLASSKAHTSRFISANLPCNKFKNRLVNIMPYESTRVCLQPIRGVEGS 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823416726 1181 DYINASYIMGYYRSNEFIITQHPLPHTTKDFWRMIWDHNAQIIVMLPDNQSLAEDE-FVYWPSrEESMNCEAFTVtlisk 1259
Cdd:cd14628     81 DYINASFIDGYRQQKAYIATQGPLAETTEDFWRMLWEHNSTIVVMLTKLREMGREKcHQYWPA-ERSARYQYFVV----- 154

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823416726 1260 DRLCLSNEEQIIIHDFILEATQDDYVLEVRHFQCPKWPNPDAPISST--FELINVI--KEEALTRDGPTIVHDEYGAVSA 1335
Cdd:cd14628    155 DPMAEYNMPQYILREFKVTDARDGQSRTVRQFQFTDWPEQGVPKSGEgfIDFIGQVhkTKEQFGQDGPISVHCSAGVGRT 234

                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1823416726 1336 GTLCALTTLSQQLENENAVDVFQVAKMINLMRPGVFTDIEQYQFLYKAMLSLVST 1390
Cdd:cd14628    235 GVFITLSIVLERMRYEGVVDIFQTVKMLRTQRPAMVQTEDQYQFCYRAALEYLGS 289
R-PTP-C-2 cd14558
PTP-like domain of receptor-type tyrosine-protein phosphatase C, repeat 2; Receptor-type ...
 883-1091 3.23e-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: 176.81  E-value: 3.23e-50
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823416726  883 YINANYVDGYNKAKAYIATQGPLKSTFEDFWRMIWEQNTGIIVMITNLVEKGRRKCDQYWPtENSEEYGNIIVTLKSTNV 962
Cdd:cd14558      1 YINASFIDGYWGPKSLIATQGPLPDTIADFWQMIFQKKVKVIVMLTELKEGDQEQCAQYWG-DEKKTYGDIEVELKDTEK 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823416726  963 HACYTVRRFTIRNTKMKKgqkgnpkgrqnERTVIQYHYTQWPDMGVPEYALPVLTFVRR------SSAARTPDMGPVVVH 1036
Cdd:cd14558     80 SPTYTVRVFEITHLKRKD-----------SRTVYQYQYHKWKGEELPEKPKDLVDMIKSikqklpYKNSKHGRSVPIVVH 148

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1823416726 1037 CSAGVGRTGTYIVIDSMLQQIKDKSTVNVLGFLKHIRTQRNYLVQTEEQYIFIHD 1091
Cdd:cd14558    149 CSDGSSRTGIFCALWNLLESAETEKVVDVFQVVKALRKQRPGMVSTLEQYQFLYD 203
R-PTP-S-2 cd14627
PTP-like domain of receptor-type tyrosine-protein phosphatase S, repeat 2; Receptor-type ...
 1102-1390 3.76e-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: 176.85  E-value: 3.76e-49
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823416726 1102 TEVSANQLHSYVNSI--LIPGiGGKTRLEKQFKLVTQCNAKYVECFSAQKDCNKEKNRNSSVVPSERARVGLAPLPGMKG 1179
Cdd:cd14627      2 TEVPARNLYSYIQKLaqVEVG-EHVTGMELEFKRLANSKAHTSRFISANLPCNKFKNRLVNIMPYETTRVCLQPIRGVEG 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823416726 1180 TDYINASYIMGYYRSNEFIITQHPLPHTTKDFWRMIWDHNAQIIVMLPDNQSLAEDE-FVYWPSrEESMNCEAFTVtlis 1258
Cdd:cd14627     81 SDYINASFIDGYRQQKAYIATQGPLAETTEDFWRMLWENNSTIVVMLTKLREMGREKcHQYWPA-ERSARYQYFVV---- 155

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823416726 1259 kDRLCLSNEEQIIIHDFILEATQDDYVLEVRHFQCPKWPNPDAPISST--FELINVI--KEEALTRDGPTIVHDEYGAVS 1334
Cdd:cd14627    156 -DPMAEYNMPQYILREFKVTDARDGQSRTVRQFQFTDWPEQGVPKSGEgfIDFIGQVhkTKEQFGQDGPISVHCSAGVGR 234

                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 1823416726 1335 AGTLCALTTLSQQLENENAVDVFQVAKMINLMRPGVFTDIEQYQFLYKAMLSLVST 1390
Cdd:cd14627    235 TGVFITLSIVLERMRYEGVVDIFQTVKMLRTQRPAMVQTEDEYQFCYQAALEYLGS 290
PTPc-N4 cd14601
catalytic domain of tyrosine-protein phosphatase non-receptor type 4; Tyrosine-protein ...
 882-1095 7.21e-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: 173.21  E-value: 7.21e-49
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823416726  882 DYINANYVDGYNKAKA----YIATQGPLKSTFEDFWRMIWEQNTGIIVMITNLVEKGRRKCDQYWP-TENSEEYGNIIVT 956
Cdd:cd14601      1 DYINANYINMEIPSSSiinrYIACQGPLPNTCSDFWQMTWEQGSSMVVMLTTQVERGRVKCHQYWPePSGSSSYGGFQVT 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823416726  957 LKSTNVHACYTVRRFTIRNTKMKKgqkgnpkgrqnERTVIQYHYTQWPDMGVPEYALPVLTFVRRSSAARTPDMGPVVVH 1036
Cdd:cd14601     81 CHSEEGNPAYVFREMTLTNLEKNE-----------SRPLTQIQYIAWPDHGVPDDSSDFLDFVCLVRNKRAGKDEPVVVH 149

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 1823416726 1037 CSAGVGRTGTYIVIDSMLQQIKDKSTVNVLGFLKHIRTQRNYLVQTEEQYIFIHDALLE 1095
Cdd:cd14601    150 CSAGIGRTGVLITMETAMCLIECNQPVYPLDIVRTMRDQRAMMIQTPSQYRFVCEAILK 208
PTP-N23 cd14539
PTP-like domain of tyrosine-protein phosphatase non-receptor type 23; Tyrosine-protein ...
 883-1091 8.31e-49

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: 172.57  E-value: 8.31e-49
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823416726  883 YINANYVDGY-NKAKAYIATQGPLKSTFEDFWRMIWEQNTGIIVMITNLVEKGRRKCDQYWPTE--NSEEYGNIIVTLKS 959
Cdd:cd14539      1 YINASLIEDLtPYCPRFIATQAPLPGTAADFWLMVYEQQVSVIVMLVSEQENEKQKVHRYWPTErgQALVYGAITVSLQS 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823416726  960 TNVHACYTVRRFTIRNtkmkKGQKGNpkgrqneRTVIQYHYTQWPDMGVPEYALPVLTFV---------RRSSAArtpdm 1030
Cdd:cd14539     81 VRTTPTHVERIISIQH----KDTRLS-------RSVVHLQFTTWPELGLPDSPNPLLRFIeevhshylqQRSLQT----- 144

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1823416726 1031 gPVVVHCSAGVGRTGTYIVIDSMLQQIK-DKSTVNVLGFLKHIRTQRNYLVQTEEQYIFIHD 1091
Cdd:cd14539    145 -PIVVHCSSGVGRTGAFCLLYAAVQEIEaGNGIPDLPQLVRKMRQQRKYMLQEKEHLKFCYE 205
R-PTP-F-2 cd14629
PTP-like domain of receptor-type tyrosine-protein phosphatase F, repeat 2; Receptor-type ...
 1102-1390 1.38e-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: 1.38e-48
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823416726 1102 TEVSANQLHSYVNSI-LIPGIGGKTRLEKQFKLVTQCNAKYVECFSAQKDCNKEKNRNSSVVPSERARVGLAPLPGMKGT 1180
Cdd:cd14629      2 TEVPARNLYAHIQKLtQVPPGESVTAMELEFKLLANSKAHTSRFISANLPCNKFKNRLVNIMPYELTRVCLQPIRGVEGS 81

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823416726 1181 DYINASYIMGYYRSNEFIITQHPLPHTTKDFWRMIWDHNAQIIVMLPDNQSLAEDE-FVYWPSrEESMNCEAFTVtlisk 1259
Cdd:cd14629     82 DYINASFIDGYRQQKAYIATQGPLAETTEDFWRMLWEHNSTIVVMLTKLREMGREKcHQYWPA-ERSARYQYFVV----- 155

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823416726 1260 DRLCLSNEEQIIIHDFILEATQDDYVLEVRHFQCPKWPNPDAPISST--FELINVI--KEEALTRDGPTIVHDEYGAVSA 1335
Cdd:cd14629    156 DPMAEYNMPQYILREFKVTDARDGQSRTIRQFQFTDWPEQGVPKTGEgfIDFIGQVhkTKEQFGQDGPITVHCSAGVGRT 235

                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1823416726 1336 GTLCALTTLSQQLENENAVDVFQVAKMINLMRPGVFTDIEQYQFLYKAMLSLVST 1390
Cdd:cd14629    236 GVFITLSIVLERMRYEGVVDMFQTVKTLRTQRPAMVQTEDQYQLCYRAALEYLGS 290
PHA02738 PHA02738
hypothetical protein; Provisional
 828-1093 9.49e-48

hypothetical protein; Provisional


Pssm-ID: 222923 [Multi-domain]  Cd Length: 320  Bit Score: 173.96  E-value: 9.49e-48
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823416726  828 DFEEVqrctadmnITAEH------------SNHPDNKHKNRYINILAYDHSRVKLRplpgKDSKHSDYINANYVDGYNKA 895
Cdd:PHA02738    22 DCEEV--------ITREHqkvisekvdgtfNAEKKNRKLNRYLDAVCFDHSRVILP----AERNRGDYINANYVDGFEYK 89

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823416726  896 KAYIATQGPLKSTFEDFWRMIWEQNTGIIVMITNLVEKGRRKCDQYWPT--ENSEEYGNIIVTLKSTNVHACYTvrRFTI 973
Cdd:PHA02738    90 KKFICGQAPTRQTCYDFYRMLWMEHVQIIVMLCKKKENGREKCFPYWSDveQGSIRFGKFKITTTQVETHPHYV--KSTL 167

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823416726  974 RNTkmkkgqkgnpKGRQNERTVIQYHYTQWPDMGVPEYALPVLTFV------RRSSAARTPDMG-------PVVVHCSAG 1040
Cdd:PHA02738   168 LLT----------DGTSATQTVTHFNFTAWPDHDVPKNTSEFLNFVlevrqcQKELAQESLQIGhnrlqppPIVVHCNAG 237

                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|...
gi 1823416726 1041 VGRTGTYIVIDSMLQQIKDKSTVNVLGFLKHIRTQRNYLVQTEEQYIFIHDAL 1093
Cdd:PHA02738   238 LGRTPCYCVVDISISRFDACATVSIPSIVSSIRNQRYYSLFIPFQYFFCYRAV 290
PHA02747 PHA02747
protein tyrosine phosphatase; Provisional
 830-1090 3.42e-47

protein tyrosine phosphatase; Provisional


Pssm-ID: 165114 [Multi-domain]  Cd Length: 312  Bit Score: 172.11  E-value: 3.42e-47
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823416726  830 EEVQRCTADMNITAEHSNHPDNKHKNRYINILAYDHSRVKLRplpGKDSKHSDYINANYVDGYNKAKAYIATQGPLKSTF 909
Cdd:PHA02747    30 EHHQIILKPFDGLIANFEKPENQPKNRYWDIPCWDHNRVILD---SGGGSTSDYIHANWIDGFEDDKKFIATQGPFAETC 106

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823416726  910 EDFWRMIWEQNTGIIVMIT-NLVEKGRRKCDQYW-PTENS--EEYGNIIVTLKSTnVHACYTvrRFTIRNTKmkkgqkgn 985
Cdd:PHA02747   107 ADFWKAVWQEHCSIIVMLTpTKGTNGEEKCYQYWcLNEDGniDMEDFRIETLKTS-VRAKYI--LTLIEITD-------- 175

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823416726  986 pKGRQNERTVIQYHYTQWPDMGVPEYALPVLTFVRRSSAARTPDMG----------PVVVHCSAGVGRTGTYIVIDSMLQ 1055
Cdd:PHA02747   176 -KILKDSRKISHFQCSEWFEDETPSDHPDFIKFIKIIDINRKKSGKlfnpkdallcPIVVHCSDGVGKTGIFCAVDICLN 254

                          250       260       270
                   ....*....|....*....|....*....|....*
gi 1823416726 1056 QIKDKSTVNVLGFLKHIRTQRNYLVQTEEQYIFIH 1090
Cdd:PHA02747   255 QLVKRKAICLAKTAEKIREQRHAGIMNFDDYLFIQ 289
PTPc-N20 cd14596
catalytic domain of tyrosine-protein phosphatase non-receptor type 20; Tyrosine-protein ...
 883-1097 7.82e-47

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


Pssm-ID: 350444 [Multi-domain]  Cd Length: 207  Bit Score: 167.23  E-value: 7.82e-47
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823416726  883 YINANYVDGYNKAKA--YIATQGPLKSTFEDFWRMIWEQNTGIIVMITNLVEKGRRKCDQYWPTENSE--EYGNIIVTLK 958
Cdd:cd14596      1 YINASYITMPVGEEElfYIATQGPLPSTIDDFWQMVWENRSDVIAMMTREVERGKVKCHRYWPETLQEpmELENYQLRLE 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823416726  959 STNVhacytVRRFTIRNTKMKKGQKGnpkgrqNERTVIQYHYTQWPDMGVPEYALPVLTFVRrsSAARTPDMGPVVVHCS 1038
Cdd:cd14596     81 NYQA-----LQYFIIRIIKLVEKETG------ENRLIKHLQFTTWPDHGTPQSSDQLVKFIC--YMRKVHNTGPIVVHCS 147

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 1823416726 1039 AGVGRTGTYIVIDSMLQQIKDKSTVNVLGFLKHIRTQRNYLVQTEEQYIFIHDALLEAI 1097
Cdd:cd14596    148 AGIGRAGVLICVDVLLSLIEKDLSFNIKDIVREMRQQRYGMIQTKDQYLFCYKVVLEVL 206
Cah COG3338
Carbonic anhydrase [Inorganic ion transport and metabolism];
53-320 5.75e-46

Carbonic anhydrase [Inorganic ion transport and metabolism];


Pssm-ID: 442567 [Multi-domain]  Cd Length: 247  Bit Score: 166.21  E-value: 5.75e-46
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823416726   53 KASGDPYWAYSGTYGPEHWVTSSEK---CG-GSHQSPIDIMDHlahVGDEYQELQldgFDNESSNKTwMKNTGKTVAILL 128
Cdd:COG3338     21 AAASAPHWSYEGETGPEHWGELSPEfatCAtGKNQSPIDIRTA---IKADLPPLK---FDYKPTPLE-IVNNGHTIQVNV 93

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823416726  129 KDDYFVSGAGLpgRFKAEKVEFHwgqsngsAGSEHSINGKRFPVEMQIYFYNPDDfdsfGTAVLenrvvgamAVFFQVSp 208
Cdd:COG3338     94 DPGSTLTVDGK--RYELKQFHFH-------TPSEHTINGKSYPMEAHLVHKDADG----ELAVV--------GVLFEEG- 151

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823416726  209 RDNSALDPIIHGL---KGvvhhEKETFLDPFVLRELLPTSLgSYYRYTGSLTTPPCSEIVEWIVFRKPVPISYHQLEAFY 285
Cdd:COG3338    152 AENPALAKLWANLpleAG----EEVALDATIDLNDLLPEDR-SYYRYSGSLTTPPCSEGVLWIVLKQPITVSAEQIEAFA 226

                          250       260       270
                   ....*....|....*....|....*....|....*
gi 1823416726  286 SIFtteqqdhvksveylRNNFRPQQRLNNRKVSKS 320
Cdd:COG3338    227 RLY--------------PNNARPVQPLNGRLILES 247
PHA02746 PHA02746
protein tyrosine phosphatase; Provisional
 842-1098 9.20e-46

protein tyrosine phosphatase; Provisional


Pssm-ID: 165113 [Multi-domain]  Cd Length: 323  Bit Score: 168.28  E-value: 9.20e-46
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823416726  842 TAEHSNHPDNKHKNRYINILAYDHSRVKL-----------------RPLPGKDSKHSDYINANYVDGYNKAKAYIATQGP 904
Cdd:PHA02746    42 TTNHFLKKENLKKNRFHDIPCWDHSRVVInaheslkmfdvgdsdgkKIEVTSEDNAENYIHANFVDGFKEANKFICAQGP 121

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823416726  905 LKSTFEDFWRMIWEQNTGIIVMITNlVEKGRRKCDQYWPTENSEE--YGNIIVTLKSTNVHACYTVRRFTIRNtkmkkgq 982
Cdd:PHA02746   122 KEDTSEDFFKLISEHESQVIVSLTD-IDDDDEKCFELWTKEEDSElaFGRFVAKILDIIEELSFTKTRLMITD------- 193

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823416726  983 kgnpKGRQNERTVIQYHYTQWPDMGVPEYALPVLTFV-----RRSSAARTPD-----MGPVVVHCSAGVGRTGTYIVIDS 1052
Cdd:PHA02746   194 ----KISDTSREIHHFWFPDWPDNGIPTGMAEFLELInkvneEQAELIKQADndpqtLGPIVVHCSAGIGRAGTFCAIDN 269

                          250       260       270       280
                   ....*....|....*....|....*....|....*....|....*.
gi 1823416726 1053 MLQQIKDKSTVNVLGFLKHIRTQRNYLVQTEEQYIFIHDALLEAIL 1098
Cdd:PHA02746   270 ALEQLEKEKEVCLGEIVLKIRKQRHSSVFLPEQYAFCYKALKYAII 315
alpha_CA_IX cd03150
Carbonic anhydrase alpha, isozyme IX. Carbonic anhydrases (CAs) are zinc-containing enzymes ...
 67-320 1.12e-44

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: 162.43  E-value: 1.12e-44
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823416726   67 GPEHWVTSSEKCGGSHQSPIDIMDHLAHVGDEYQELQLDGFDNESSNKTWMKNTGKTVAILLKDDYFVSGAglPGR-FKA 145
Cdd:cd03150      1 GQPPWPSVSPACAGRFQSPVDIRPHLVAFCPALRPLELLGFDLPPSPSLRLLNNGHTVQLSLPSGLRMALG--PGQeYRA 78

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823416726  146 EKVEFHWGQSnGSAGSEHSINGKRFPVEMQIYFYNpDDFDSFGTAVLENRVVGAMAVFFQVSPRDNSALDPIIHGLKGVV 225
Cdd:cd03150     79 LQLHLHWGAA-GRPGSEHTVDGHRFPAEIHVVHLS-TAFANLDEALGRPGGLAVLAAFLAEGLHENSAYEQLLSRLSEIS 156

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823416726  226 HHEKETFLDPFVLRELLPTSLGSYYRYTGSLTTPPCSEIVEWIVFRKPVPISYHQLEAFYSIFTTEQQdhvksvEYLRNN 305
Cdd:cd03150    157 EEESETVVPGLDVSALLPSDLSRYFRYEGSLTTPPCAQGVIWTVFNQTVRLSAKQLHTLSDSLWGPHD------SRLQLN 230

                          250
                   ....*....|....*
gi 1823416726  306 FRPQQRLNNRKVSKS 320
Cdd:cd03150    231 FRATQPLNGRKIEAS 245
R-PTPc-typeIIb-2 cd14556
PTP domain of type IIb (or R2B) subfamily receptor-type tyrosine-protein phosphatases, repeat ...
 1182-1381 1.24e-43

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: 157.57  E-value: 1.24e-43
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823416726 1182 YINASYIMGYYRSNEFIITQHPLPHTTKDFWRMIWDHNAQIIVMLPDNQSLAEDEFVYWPsrEESMNCEA-FTVTLISKD 1260
Cdd:cd14556      1 YINAALLDSYKQPAAFIVTQHPLPNTVTDFWRLVYDYGCTSIVMLNQLDPKDQSCPQYWP--DEGSGTYGpIQVEFVSTT 78

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823416726 1261 RlclsnEEQIIIHDFILEAT---QDDYVLeVRHFQCPKWP-NPDAPIS--STFELIN-VIKEEALTRDGPTIVHDEYGAV 1333
Cdd:cd14556     79 I-----DEDVISRIFRLQNTtrpQEGYRM-VQQFQFLGWPrDRDTPPSkrALLKLLSeVEKWQEQSGEGPIVVHCLNGVG 152

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*...
gi 1823416726 1334 SAGTLCALTTLSQQLENENAVDVFQVAKMINLMRPGVFTDIEQYQFLY 1381
Cdd:cd14556    153 RSGVFCAISSVCERIKVENVVDVFQAVKTLRNHRPNMVETEEQYKFCY 200
alpha_CA_prokaryotic_like cd03124
Carbonic anhydrase alpha, prokaryotic-like subfamily. Carbonic anhydrases (CAs) are ...
 67-317 1.27e-43

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: 158.20  E-value: 1.27e-43
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823416726   67 GPEHWVTSSEK---CG-GSHQSPIDImdHLAHVGDEyQELQLDgFDNESSNKTwMKNTGKTVAILLKDDyfVSGAGLPGR 142
Cdd:cd03124      1 GPEHWGNLDPEfalCAtGKNQSPIDI--TTKAVVSD-KLPPLN-YNYKPTSAT-LVNNGHTIQVNFEGN--GGTLTIDGE 73

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823416726  143 -FKAEKVEFHwgqsngsAGSEHSINGKRFPVEMQIYFYNPDDfdsfGTAVLenrvvgamAVFFQVSPrDNSALDPIIHGL 221
Cdd:cd03124     74 tYQLLQFHFH-------SPSEHLINGKRYPLEAHLVHKSKDG----QLAVV--------AVLFEEGK-ENPFLKKILDNM 133

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823416726  222 KGVVhhEKETFLDPFV-LRELLPTSLgSYYRYTGSLTTPPCSEIVEWIVFRKPVPISYHQLEAFysiftteqqdhvKSVE 300
Cdd:cd03124    134 PKKE--GTEVNLPAILdPNELLPESR-SYYRYEGSLTTPPCSEGVRWIVLKQPITISKEQLAKF------------RAAV 198

                          250
                   ....*....|....*..
gi 1823416726  301 YLRNNfRPQQRLNNRKV 317
Cdd:cd03124    199 YPNNA-RPVQPLNGREV 214
COG5599 COG5599
Protein tyrosine phosphatase [Signal transduction mechanisms];
845-1089 3.96e-43

Protein tyrosine phosphatase [Signal transduction mechanisms];


Pssm-ID: 444335 [Multi-domain]  Cd Length: 282  Bit Score: 159.10  E-value: 3.96e-43
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823416726  845 HSNHPDNKHKNRYINILAYDHSRVklrplpGKDSKhsdYINANYVDGYNKaKAYIATQGPLKSTFEDFWRMIWEQNTGII 924
Cdd:COG5599     36 YLQNINGSPLNRFRDIQPYKETAL------RANLG---YLNANYIQVIGN-HRYIATQYPLEEQLEDFFQMLFDNNTPVL 105

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823416726  925 VMITNLVE--KGRRKCDQYWPTenSEEYGNIIVTLKSTNVHACYTvrRFTIRNTKMKKGQKGnpkgrQNERTVIQYHYTQ 1002
Cdd:COG5599    106 VVLASDDEisKPKVKMPVYFRQ--DGEYGKYEVSSELTESIQLRD--GIEARTYVLTIKGTG-----QKKIEIPVLHVKN 176

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823416726 1003 WPDMGVP--EYALPVLTFVRRSSAARTPDMGPVVVHCSAGVGRTGTYIVIDSMLQQIKDKS--TVNVLGFLKHIRTQRNY 1078
Cdd:COG5599    177 WPDHGAIsaEALKNLADLIDKKEKIKDPDKLLPVVHCRAGVGRTGTLIACLALSKSINALVqiTLSVEEIVIDMRTSRNG 256

                          250
                   ....*....|..
gi 1823416726 1079 -LVQTEEQYIFI 1089
Cdd:COG5599    257 gMVQTSEQLDVL 268
PTPc-N21 cd14598
catalytic domain of tyrosine-protein phosphatase non-receptor type 21; Tyrosine-protein ...
 883-1095 1.43e-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: 155.52  E-value: 1.43e-42
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823416726  883 YINANY--VDGYNKAKAYIATQGPLKSTFEDFWRMIWEQNTGIIVMITNLVEKGRRKCDQYWP----TENSEEYGNIIVT 956
Cdd:cd14598      1 YINASHikVTVGGKEWDYIATQGPLQNTCQDFWQMVWEQGVAIIAMVTAEEEGGREKSFRYWPrlgsRHNTVTYGRFKIT 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823416726  957 LKSTNVHACYTVRRFTIRNtkMKKGQkgnpkgrqnERTVIQYHYTQWPDMGVPEYALPVLTF------VRR----SSAAR 1026
Cdd:cd14598     81 TRFRTDSGCYATTGLKIKH--LLTGQ---------ERTVWHLQYTDWPEHGCPEDLKGFLSYleeiqsVRRhtnsTIDPK 149

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1823416726 1027 TPDMgPVVVHCSAGVGRTGTYIVIDSMLQQIKDKSTVNVLGFLKHIRTQRNYLVQTEEQYIFIHDALLE 1095
Cdd:cd14598    150 SPNP-PVLVHCSAGVGRTGVVILSEIMIACLEHNEMLDIPRVLDMLRQQRMMMVQTLSQYTFVYKVLIQ 217
R3-PTPc cd14548
catalytic domain of R3 subfamily receptor-type tyrosine-protein phosphatases and similar ...
 1157-1382 2.28e-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: 154.82  E-value: 2.28e-42
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823416726 1157 RNSSVVPSERARVGLAPLPGMKGTDYINASYIMGYYRSNEFIITQHPLPHTTKDFWRMIWDHNAQIIVMLP---DNQSLA 1233
Cdd:cd14548      1 RYTNILPYDHSRVKLIPINEEEGSDYINANYIPGYNSPREFIATQGPLPGTKDDFWRMVWEQNSHTIVMLTqcmEKGRVK 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823416726 1234 EDEfvYWPSREESMNCEAFTVTLISKDRLclsneEQIIIHDFILEatQDDYVLEVRHFQCPKWPN---PDAPISstfeLI 1310
Cdd:cd14548     81 CDH--YWPFDQDPVYYGDITVTMLSESVL-----PDWTIREFKLE--RGDEVRSVRQFHFTAWPDhgvPEAPDS----LL 147

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1823416726 1311 NVIKeeaLTRD------GPTIVHDEYGAVSAGTLCALTTLSQQLENENAVDVFQVAKMINLMRPGVFTDIEQYQFLYK 1382
Cdd:cd14548    148 RFVR---LVRDyikqekGPTIVHCSAGVGRTGTFIALDRLLQQIESEDYVDIFGIVYDLRKHRPLMVQTEAQYIFLHQ 222
R-PTPc-typeIIb-2 cd14556
PTP domain of type IIb (or R2B) subfamily receptor-type tyrosine-protein phosphatases, repeat ...
 883-1091 4.93e-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: 152.95  E-value: 4.93e-42
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823416726  883 YINANYVDGYNKAKAYIATQGPLKSTFEDFWRMIWEQNTGIIVMItNLVEKGRRKCDQYWPTENSEEYGNIIVTLKSTNV 962
Cdd:cd14556      1 YINAALLDSYKQPAAFIVTQHPLPNTVTDFWRLVYDYGCTSIVML-NQLDPKDQSCPQYWPDEGSGTYGPIQVEFVSTTI 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823416726  963 HACYTVRRFTIRNTKmkkgqkgnpkgRQNE--RTVIQYHYTQWPDMG----VPEYALPVLTFVRRSSAARtpDMGPVVVH 1036
Cdd:cd14556     80 DEDVISRIFRLQNTT-----------RPQEgyRMVQQFQFLGWPRDRdtppSKRALLKLLSEVEKWQEQS--GEGPIVVH 146

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1823416726 1037 CSAGVGRTGTYIVIDSMLQQIKDKSTVNVLGFLKHIRTQRNYLVQTEEQYIFIHD 1091
Cdd:cd14556    147 CLNGVGRSGVFCAISSVCERIKVENVVDVFQAVKTLRNHRPNMVETEEQYKFCYD 201
R-PTPc-A-E-2 cd14552
catalytic domain of receptor-type tyrosine-protein phosphatase A and E, repeat 2; ...
 1182-1384 5.45e-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: 5.45e-42
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823416726 1182 YINASYIMGYYRSNEFIITQHPLPHTTKDFWRMIWDHNAQIIVMLPDNQSLAEDE-FVYWPSrEESMNCEAFTVTLiSKD 1260
Cdd:cd14552      1 YINASFIDGYRQKDAYIATQGPLDHTVEDFWRMIWEWKSCSIVMLTEIKERSQNKcAQYWPE-DGSVSSGDITVEL-KDQ 78

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823416726 1261 RLClsneEQIIIHDFILEATQDDYVLEVRHFQCPKWPNPDAPiSSTFELINVI----KEEALTRDGPTIVHDEYGAVSAG 1336
Cdd:cd14552     79 TDY----EDYTLRDFLVTKGKGGSTRTVRQFHFHGWPEVGIP-DNGKGMIDLIaavqKQQQQSGNHPITVHCSAGAGRTG 153

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*...
gi 1823416726 1337 TLCALTTLSQQLENENAVDVFQVAKMINLMRPGVFTDIEQYQFLYKAM 1384
Cdd:cd14552    154 TFCALSTVLERVKAEGVLDVFQVVKSLRLQRPHMVQTLEQYEFCYKVV 201
PHA02742 PHA02742
protein tyrosine phosphatase; Provisional
 851-1095 4.60e-41

protein tyrosine phosphatase; Provisional


Pssm-ID: 165109 [Multi-domain]  Cd Length: 303  Bit Score: 154.00  E-value: 4.60e-41
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823416726  851 NKHKNRYINILAYDHSRVKLRPLPGKDskhsDYINANYVDGYNKAKAYIATQGPLKSTFEDFWRMIWEQNTGIIVMITNL 930
Cdd:PHA02742    52 NMKKCRYPDAPCFDRNRVILKIEDGGD----DFINASYVDGHNAKGRFICTQAPLEETALDFWQAIFQDQVRVIVMITKI 127

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823416726  931 VEKGRRKCDQYWPTENseeygniivtlKSTNVHACYTVRRFTI---RNTKMKKGQKGNPkgrqNERTVI---QYHYTQWP 1004
Cdd:PHA02742   128 MEDGKEACYPYWMPHE-----------RGKATHGEFKIKTKKIksfRNYAVTNLCLTDT----NTGASLdikHFAYEDWP 192

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823416726 1005 DMGVPEYALPVLTFV----RRSSAARTPDMG-------PVVVHCSAGVGRTGTYIVIDSMLQQIKDKSTVNVLGFLKHIR 1073
Cdd:PHA02742   193 HGGLPRDPNKFLDFVlavrEADLKADVDIKGenivkepPILVHCSAGLDRAGAFCAIDICISKYNERAIIPLLSIVRDLR 272

                          250       260
                   ....*....|....*....|..
gi 1823416726 1074 TQRNYLVQTEEQYIFIHDALLE 1095
Cdd:PHA02742   273 KQRHNCLSLPQQYIFCYFIVLI 294
R-PTPc-E-2 cd14622
catalytic domain of receptor-type tyrosine-protein phosphatase E, repeat 2; Receptor-type ...
 1181-1384 5.79e-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: 5.79e-40
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823416726 1181 DYINASYIMGYYRSNEFIITQHPLPHTTKDFWRMIWDHNAQIIVMLPDNQSLAEDE-FVYWPSrEESMNCEAFTVTlISK 1259
Cdd:cd14622      1 DYINASFIDGYRQKDYFIATQGPLAHTVEDFWRMVWEWKCHTIVMLTELQEREQEKcVQYWPS-EGSVTHGEITIE-IKN 78

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823416726 1260 DRLClsneEQIIIHDFILEATQDDYVLEVRHFQCPKWPNPDAPiSSTFELINVI----KEEALTRDGPTIVHDEYGAVSA 1335
Cdd:cd14622     79 DTLL----ETISIRDFLVTYNQEKQTRLVRQFHFHGWPEIGIP-AEGKGMIDLIaavqKQQQQTGNHPIVVHCSAGAGRT 153

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*....
gi 1823416726 1336 GTLCALTTLSQQLENENAVDVFQVAKMINLMRPGVFTDIEQYQFLYKAM 1384
Cdd:cd14622    154 GTFIALSNILERVKAEGLLDVFQTVKSLRLQRPHMVQTLEQYEFCYRVV 202
R-PTPc-H cd14619
catalytic domain of receptor-type tyrosine-protein phosphatase H; Receptor-type ...
 1156-1388 7.99e-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: 7.99e-40
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823416726 1156 NRNSSVVPSERARVGLAPLPGMKGTDYINASYIMGYYRSNEFIITQHPLPHTTKDFWRMIWDHNAQIIVMLPDnqsLAED 1235
Cdd:cd14619      1 NRFRNVLPYDWSRVPLKPIHEEPGSDYINANYMPGYWSSQEFIATQGPLPQTVGDFWRMIWEQQSSTIVMLTN---CMEA 77

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823416726 1236 EFV----YWPSREESMNCEAFTVTLISKDRLclsneEQIIIHDFILEATQDDYVLEVRHFQCPKWPNPDAPiSSTFELI- 1310
Cdd:cd14619     78 GRVkcehYWPLDYTPCTYGHLRVTVVSEEVM-----ENWTVREFLLKQVEEQKTLSVRHFHFTAWPDHGVP-SSTDTLLa 151

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823416726 1311 --NVIKE--EALTRDGPTIVHDEYGAVSAGTLCALTTLSQQLENENAVDVFQVAKMINLMRPGVFTDIEQYQFLYKAMLS 1386
Cdd:cd14619    152 frRLLRQwlDQTMSGGPTVVHCSAGVGRTGTLIALDVLLQQLQSEGLLGPFSFVQKMRENRPLMVQTESQYVFLHQCILD 231


                   ..
gi 1823416726 1387 LV 1388
Cdd:cd14619    232 FL 233
R-PTP-C-2 cd14558
PTP-like domain of receptor-type tyrosine-protein phosphatase C, repeat 2; Receptor-type ...
 1182-1381 1.53e-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: 146.00  E-value: 1.53e-39
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823416726 1182 YINASYIMGYYRSNEFIITQHPLPHTTKDFWRMIWDHNAQIIVMLPD-NQSLAEDEFVYWPsrEESMNCEAFTVTLISKD 1260
Cdd:cd14558      1 YINASFIDGYWGPKSLIATQGPLPDTIADFWQMIFQKKVKVIVMLTElKEGDQEQCAQYWG--DEKKTYGDIEVELKDTE 78

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823416726 1261 rlclsNEEQIIIHDFILEATQDDYVLEVRHFQCPKWPNPDAPiSSTFELINVIKE---------EALTRDGPTIVHDEYG 1331
Cdd:cd14558     79 -----KSPTYTVRVFEITHLKRKDSRTVYQYQYHKWKGEELP-EKPKDLVDMIKSikqklpyknSKHGRSVPIVVHCSDG 152

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|
gi 1823416726 1332 AVSAGTLCALTTLSQQLENENAVDVFQVAKMINLMRPGVFTDIEQYQFLY 1381
Cdd:cd14558    153 SSRTGIFCALWNLLESAETEKVVDVFQVVKALRKQRPGMVSTLEQYQFLY 202
R-PTPc-J cd14615
catalytic domain of receptor-type tyrosine-protein phosphatase J; Receptor-type ...
 1156-1385 1.78e-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: 1.78e-39
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823416726 1156 NRNSSVVPSERARVGLApLPGMKGTDYINASYIMGYYRSNEFIITQHPLPHTTKDFWRMIWDHNAQIIVMLPDNQSLAE- 1234
Cdd:cd14615      1 NRYNNVLPYDISRVKLS-VQSHSTDDYINANYMPGYNSKKEFIAAQGPLPNTVKDFWRMVWEKNVYAIVMLTKCVEQGRt 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823416726 1235 --DEfvYWPSrEESMNCEAFTVTLISKDRLclsneEQIIIHDFILEATQDDYVLEVRHFQCPKWPNPDAPiSSTFELIN- 1311
Cdd:cd14615     80 kcEE--YWPS-KQKKDYGDITVTMTSEIVL-----PEWTIRDFTVKNAQTNESRTVRHFHFTSWPDHGVP-ETTDLLINf 150

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1823416726 1312 --VIKE--EALTRDGPTIVHDEYGAVSAGTLCALTTLSQQLENENAVDVFQVAKMINLMRPGVFTDIEQYQFLYKAML 1385
Cdd:cd14615    151 rhLVREymKQNPPNSPILVHCSAGVGRTGTFIAIDRLIYQIENENVVDVYGIVYDLRMHRPLMVQTEDQYVFLNQCAL 228
alpha_CA_I_II_III_XIII cd03119
Carbonic anhydrase alpha, isozymes I, II, and III and XIII. Carbonic anhydrases (CAs) are ...
 58-320 2.38e-39

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: 147.59  E-value: 2.38e-39
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823416726   58 PYWAYSGTYGPEHWVTSSEKCGGSHQSPIDIMDHLAHVGDEYQELQLDGfdNESSNKTwMKNTGKTVAILLKDDY---FV 134
Cdd:cd03119      3 HHWGYDSHNGPEHWHELFPIAKGDRQSPIDIKTKDAKHDPSLKPLSVSY--DPATAKT-ILNNGHSFNVEFDDTDdrsVL 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823416726  135 SGAGLPGRFKAEKVEFHWGQSNGSaGSEHSINGKRFPVEMQIYFYNPDdFDSFGTAVLENRVVGAMAVFFQVSpRDNSAL 214
Cdd:cd03119     80 RGGPLTGSYRLRQFHFHWGSSDDH-GSEHTVDGVKYAAELHLVHWNSK-YGSFGEAAKQPDGLAVVGVFLKVG-EANPEL 156

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823416726  215 DPIIHGLKGVVHHEKETFLDPFVLRELLPTSLgSYYRYTGSLTTPPCSEIVEWIVFRKPVPISYHQLEAFYSIFTTEQQD 294
Cdd:cd03119    157 QKVLDALDSIKTKGKQAPFTNFDPSCLLPASL-DYWTYPGSLTTPPLLECVTWIVLKEPISVSSEQMAKFRSLLFNAEGE 235

                          250       260
                   ....*....|....*....|....*.
gi 1823416726  295 hvkSVEYLRNNFRPQQRLNNRKVSKS 320
Cdd:cd03119    236 ---PPCPMVDNWRPPQPLKGRKVRAS 258
PTPc_DSPc smart00012
Protein tyrosine phosphatase, catalytic domain, undefined specificity; Protein tyrosine ...
 994-1095 3.65e-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: 3.65e-39
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823416726   994 TVIQYHYTQWPDMGVPEYALPVLTFVR--RSSAARTPDMGPVVVHCSAGVGRTGTYIVIDSMLQQIKDKS-TVNVLGFLK 1070
Cdd:smart00012    1 TVKHYHYTGWPDHGVPESPDSILELLRavKKNLNQSESSGPVVVHCSAGVGRTGTFVAIDILLQQLEAEAgEVDIFDTVK 80

                            90       100
                    ....*....|....*....|....*
gi 1823416726  1071 HIRTQRNYLVQTEEQYIFIHDALLE 1095
Cdd:smart00012   81 ELRSQRPGMVQTEEQYLFLYRALLE 105
PTPc_motif smart00404
Protein tyrosine phosphatase, catalytic domain motif;
994-1095 3.65e-39

Protein tyrosine phosphatase, catalytic domain motif;


Pssm-ID: 214649 [Multi-domain]  Cd Length: 105  Bit Score: 140.96  E-value: 3.65e-39
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823416726   994 TVIQYHYTQWPDMGVPEYALPVLTFVR--RSSAARTPDMGPVVVHCSAGVGRTGTYIVIDSMLQQIKDKS-TVNVLGFLK 1070
Cdd:smart00404    1 TVKHYHYTGWPDHGVPESPDSILELLRavKKNLNQSESSGPVVVHCSAGVGRTGTFVAIDILLQQLEAEAgEVDIFDTVK 80

                            90       100
                    ....*....|....*....|....*
gi 1823416726  1071 HIRTQRNYLVQTEEQYIFIHDALLE 1095
Cdd:smart00404   81 ELRSQRPGMVQTEEQYLFLYRALLE 105
alpha_CA_VI cd03125
Carbonic anhydrase alpha, isozyme VI. Carbonic anhydrases (CAs) are zinc-containing enzymes ...
 67-320 5.82e-39

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: 146.08  E-value: 5.82e-39
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823416726   67 GPEHWVTSSEKCGGSHQSPIDIMDHLAHVGDEYQELQLDGFDNESSNKTwMKNTGKTVAILLKDDYFVSgAGLPGRFKAE 146
Cdd:cd03125      1 DESHWPEKYPACGGKRQSPIDIQRREVRFNPSLLQLELVGYEKEQGEFT-MTNNGHTVQIDLPPTMSIT-TGDGTVYTAV 78

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823416726  147 KVEFHWG-QSNGSAGSEHSINGKRFPVEMQIYFYNpDDFDSFGTAVLENRVVGAMAVFFQV-SPRDNSALDPIIHGLKGV 224
Cdd:cd03125     79 QMHFHWGgRDSEISGSEHTIDGMRYVAELHIVHYN-SKYKSYEEAKDKPDGLAVLAFLYKVgHYAENTYYSDFISKLAKI 157

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823416726  225 VHHEKETFLDPFVLRELLPTSLGSYYRYTGSLTTPPCSEIVEWIVFRKPVPISYHQLEafySIFTTEQQDHVKSveyLRN 304
Cdd:cd03125    158 KYAGQTTTLTSLDVRDMLPENLHHYYTYQGSLTTPPCTENVLWFVFDDPVTLSKTQIV---KLENTLMDHHNKT---IRN 231

                          250
                   ....*....|....*.
gi 1823416726  305 NFRPQQRLNNRKVSKS 320
Cdd:cd03125    232 DYRRTQPLNHRVVEAN 247
R-PTPc-A-2 cd14623
catalytic domain of receptor-type tyrosine-protein phosphatase A, repeat 2; Receptor-type ...
 1161-1384 9.95e-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: 9.95e-39
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823416726 1161 VVPSERARVGLAPLPGMKGTDYINASYIMGYYRSNEFIITQHPLPHTTKDFWRMIWDHNAQIIVMLPDNQSLAEDEFV-Y 1239
Cdd:cd14623      5 IIPYEFNRVIIPVKRGEENTDYVNASFIDGYRQKDSYIASQGPLQHTIEDFWRMIWEWKSCSIVMLTELEERGQEKCAqY 84

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823416726 1240 WPSrEESMNCEAFTVTLiSKDRLClsneEQIIIHDFILEATQDDYVLEVRHFQCPKWPNPDAPiSSTFELINVI----KE 1315
Cdd:cd14623     85 WPS-DGSVSYGDITIEL-KKEEEC----ESYTVRDLLVTNTRENKSRQIRQFHFHGWPEVGIP-SDGKGMINIIaavqKQ 157

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1823416726 1316 EALTRDGPTIVHDEYGAVSAGTLCALTTLSQQLENENAVDVFQVAKMINLMRPGVFTDIEQYQFLYKAM 1384
Cdd:cd14623    158 QQQSGNHPITVHCSAGAGRTGTFCALSTVLERVKAEGILDVFQTVKSLRLQRPHMVQTLEQYEFCYKVV 226
R-PTPc-LAR-1 cd14553
catalytic domain of LAR family receptor-type tyrosine-protein phosphatases, repeat 1; The LAR ...
 1150-1389 1.14e-38

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: 1.14e-38
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823416726 1150 DCNKEKNRNSSVVPSERARVGLAPLPGMKGTDYINASYIMGYYRSNEFIITQHPLPHTTKDFWRMIWDHNAQIIVMLpdn 1229
Cdd:cd14553      1 EVNKPKNRYANVIAYDHSRVILQPIEGVPGSDYINANYCDGYRKQNAYIATQGPLPETFGDFWRMVWEQRSATIVMM--- 77

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823416726 1230 QSLAEDEFV----YWPSReESMNCEAFTVTLIskDRLCLSNeeqIIIHDFILEATQDDYVLEVRHFQCPKWPN---PDAP 1302
Cdd:cd14553     78 TKLEERSRVkcdqYWPTR-GTETYGLIQVTLL--DTVELAT---YTVRTFALHKNGSSEKREVRQFQFTAWPDhgvPEHP 151

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823416726 1303 iSSTFELINVIKEEALTRDGPTIVHDEYGAVSAGTLCALTTLSQQLENENAVDVF-QVAKM---INLMrpgVFTDiEQYQ 1378
Cdd:cd14553    152 -TPFLAFLRRVKACNPPDAGPIVVHCSAGVGRTGCFIVIDSMLERIKHEKTVDIYgHVTCLraqRNYM---VQTE-DQYI 226

                          250
                   ....*....|.
gi 1823416726 1379 FLYKAMLSLVS 1389
Cdd:cd14553    227 FIHDALLEAVT 237
R-PTPc-V cd14618
catalytic domain of receptor-type tyrosine-protein phosphatase V; Receptor-type ...
 1156-1385 6.84e-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: 142.39  E-value: 6.84e-38
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823416726 1156 NRNSSVVPSERARVGLAPLPGMKGTDYINASYIMGYYRSNEFIITQHPLPHTTKDFWRMIWDHNAQIIVMLP---DNQSL 1232
Cdd:cd14618      1 NRYPHVLPYDHSRVRLSQLGGEPHSDYINANFIPGYTSPQEFIATQGPLKKTIEDFWRLVWEQQVCNIIMLTvgmENGRV 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823416726 1233 AEDEfvYWPSREESMNCEAFTVTLISKdrlclSNEEQIIIHDFILEATQDDYVLEVRHFQCPKWPN---PDAPiSSTFEL 1309
Cdd:cd14618     81 LCDH--YWPSESTPVSYGHITVHLLAQ-----SSEDEWTRREFKLWHEDLRKERRVKHLHYTAWPDhgiPEST-SSLMAF 152

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1823416726 1310 INVIKEE--ALTRDGPTIVHDEYGAVSAGTLCALTTLSQQLENENAVDVFQVAKMINLMRPGVFTDIEQYQFLYKAML 1385
Cdd:cd14618    153 RELVREHvqATKGKGPTLVHCSAGVGRSGTFIALDRLLRQLKEEKVVDVFNTVYILRMHRYLMIQTLSQYIFLHSCIL 230
alpha_CARP_X_XI_like cd03121
Carbonic anhydrase alpha related protein: groups X, XI and related proteins. This subgroup ...
 80-317 7.35e-38

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: 142.94  E-value: 7.35e-38
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823416726   80 GSHQSPIDI-MDHLahVGDEY-QELQLDGfdNESSNKTwMKNTGKTVAILLKDDYFV--SGAGLPGRFKAEKVEFHWGQS 155
Cdd:cd03121     18 GRRQSPVDIePSRL--LFDPFlTPLRIDT--GRKVSGT-FYNTGRHVSFRPDKDPVVniSGGPLSYRYRLEEIRLHFGRE 92

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823416726  156 NGsAGSEHSINGKRFPVEMQIYFYNPDDFDSFGTAVLENRVVGAMAVFFQVSPRDNSALDPIIHGLKG--VVHHEKETFL 233
Cdd:cd03121     93 DE-QGSEHTVNGQAFPGEVQLIHYNSELYPNFSEASKSPNGLVIVSLFVKIGETSNPELRRLTNRDTItsIRYKGDAYFL 171

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823416726  234 DPFVLRELLPTSlGSYYRYTGSLTTPPCSEIVEWIVFRKPVPISYHQLEAFYSIfTTEQQDHVKSveYLRNNFRPQQRLN 313
Cdd:cd03121    172 QDLSIELLLPET-DHYITYEGSLTSPGCHETVTWIILNKPIYITKEQMHSLRLL-SQNSPSQEKA--PMSPNFRPVQPLN 247


                   ....
gi 1823416726  314 NRKV 317
Cdd:cd03121    248 NRPV 251
alpha_CA_VII cd03149
Carbonic anhydrase alpha, CA isozyme VII_like subgroup. Carbonic anhydrases (CAs) are ...
 80-320 1.41e-37

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: 141.51  E-value: 1.41e-37
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823416726   80 GSHQSPIDIMDHLAHVGDEYQELQLDgFDNESSNKtwMKNTGKTVAILLkDDY----FVSGAGLPGRFKAEKVEFHWGQS 155
Cdd:cd03149      1 GNRQSPIDIVSSEAVYDPKLKPLSLS-YDPCTSLS--ISNNGHSVMVEF-DDSddktVITGGPLENPYRLKQFHFHWGAK 76

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823416726  156 NGSaGSEHSINGKRFPVEMQIYFYNPDDFDSFGTAVLENRVVGAMAVFFQVSpRDNSALDPIIHGLKGVVHHEKETFLDP 235
Cdd:cd03149     77 HGS-GSEHTVDGKTFPSELHLVHWNAKKYKSFGEAAAAPDGLAVLGVFLETG-DEHPGLNRLTDALYMVRFKGTKAQFLD 154

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823416726  236 FVLRELLPTSLgSYYRYTGSLTTPPCSEIVEWIVFRKPVPISYHQLEAFYS-IFTTEQQDHVKSVeylrNNFRPQQRLNN 314
Cdd:cd03149    155 FNPKCLLPKSL-DYWTYPGSLTTPPLNESVTWIVLKEPIPVSEKQMGKFRElLFTSEEDQRNHMV----NNFRPPQPLKG 229


                   ....*.
gi 1823416726  315 RKVSKS 320
Cdd:cd03149    230 RTVRAS 235
PTPc-N18 cd14603
catalytic domain of tyrosine-protein phosphatase non-receptor type 18; Tyrosine-protein ...
 1129-1384 3.33e-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: 3.33e-37
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823416726 1129 KQFKLVTQCNAKYVE--CFSAQKDCNKE---KNRNSSVVPSERARVGLAPLPGMKGTDYINASYIMGYYRSNEFIITQHP 1203
Cdd:cd14603      2 GEFSEIRACSAAFKAdyVCSTVAGGRKEnvkKNRYKDILPYDQTRVILSLLQEEGHSDYINANFIKGVDGSRAYIATQGP 81

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823416726 1204 LPHTTKDFWRMIWDHNAQIIVMLPDNQSLAEDEF-VYWPSREESMNCEAFTVTLISKDRLclsNEEQIIihdFILEATQD 1282
Cdd:cd14603     82 LSHTVLDFWRMIWQYGVKVILMACREIEMGKKKCeRYWAQEQEPLQTGPFTITLVKEKRL---NEEVIL---RTLKVTFQ 155

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823416726 1283 DYVLEVRHFQCPKWPN---PDAPiSSTFELINVIKEEALTRDGPTIVHDEYGAVSAGTLCALTTLSQQLENENAVDVFQV 1359
Cdd:cd14603    156 KESRSVSHFQYMAWPDhgiPDSP-DCMLAMIELARRLQGSGPEPLCVHCSAGCGRTGVICTVDYVRQLLLTQRIPPDFSI 234

                          250       260
                   ....*....|....*....|....*...
gi 1823416726 1360 AKMINLM---RPGVFTDIEQYQFLYKAM 1384
Cdd:cd14603    235 FDVVLEMrkqRPAAVQTEEQYEFLYHTV 262
alpha_CA_V cd03118
Carbonic anhydrase alpha, CA isozyme V_like subgroup. Carbonic anhydrases (CAs) are ...
 80-320 6.49e-37

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: 139.59  E-value: 6.49e-37
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823416726   80 GSHQSPIDImdhlaHVGDEYQELQLD----GFDNESSNKTWmkNTGKTVAILLKD---DYFVSGAGLPGRFKAEKVEFHW 152
Cdd:cd03118      1 GTRQSPINI-----QWRDSVYDPQLAplrvSYDPATCLYIW--NNGYSFQVEFDDstdKSGISGGPLENHYRLKQFHFHW 73

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823416726  153 GQSNgSAGSEHSINGKRFPVEMQIYFYNPDDFDSFGTAVLENRVVGAMAVFFQVSPRdNSALDPIIHGLKGVVHHEKETF 232
Cdd:cd03118     74 GANN-EWGSEHTVDGHTYPAELHLVHWNSVKYENFEEAVMEENGLAVIGVFLKLGAH-HEGLQKLVDALPEVRHKDTVVE 151

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823416726  233 LDPFVLRELLPTSLgSYYRYTGSLTTPPCSEIVEWIVFRKPVPISYHQLEAFYSIFTTEQQDHVKsveYLRNNFRPQQRL 312
Cdd:cd03118    152 FNPFDPSCLLPACR-DYWTYPGSLTTPPLTESVTWIIQKQPIEVSPSQLSVFRTLLFTSRGEEEK---VMVNNFRPLQPL 227


                   ....*...
gi 1823416726  313 NNRKVSKS 320
Cdd:cd03118    228 MNRKVRSS 235
PTPc-N9 cd14543
catalytic domain of tyrosine-protein phosphatase non-receptor type 9; Tyrosine-protein ...
 1146-1382 2.67e-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: 2.67e-36
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823416726 1146 SAQKDCNKEKNRNSSVVPSERARVGLAPLPGMKGTDYINASYIMGYYRSNEFIITQHPLPHTTKDFWRMIWDHNAQIIVM 1225
Cdd:cd14543     23 CSLAPANQEKNRYGDVLCLDQSRVKLPKRNGDERTDYINANFMDGYKQKNAYIATQGPLPKTYSDFWRMVWEQKVLVIVM 102

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823416726 1226 LpdnQSLAEDEFV----YWPSREES-MNCEAFTVTLISKDrlclsNEEQIIIHDFILEATQDDYVLEVRHFQCPKWPNPD 1300
Cdd:cd14543    103 T---TRVVERGRVkcgqYWPLEEGSsLRYGDLTVTNLSVE-----NKEHYKKTTLEIHNTETDESRQVTHFQFTSWPDFG 174

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823416726 1301 APiSSTFELIN----VIKEEAL------------TRDGPTIVHDEYGAVSAGTLCALTTLSQQLENENAVDVFQVAKMIN 1364
Cdd:cd14543    175 VP-SSAAALLDflgeVRQQQALavkamgdrwkghPPGPPIVVHCSAGIGRTGTFCTLDICLSQLEDVGTLNVMQTVRRMR 253

                          250
                   ....*....|....*...
gi 1823416726 1365 LMRPGVFTDIEQYQFLYK 1382
Cdd:cd14543    254 TQRAFSIQTPDQYYFCYK 271
R-PTPc-O cd14614
catalytic domain of receptor-type tyrosine-protein phosphatase O; Receptor-type ...
 1145-1385 1.57e-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: 135.79  E-value: 1.57e-35
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823416726 1145 FSAQKDCNKEKNRNSSVVPSERARVGLAPLPGMKGTDYINASYIMGYYRSNEFIITQHPLPHTTKDFWRMIWDHNAQIIV 1224
Cdd:cd14614      5 FAADLPVNRCKNRYTNILPYDFSRVKLVSMHEEEGSDYINANYIPGYNSPQEYIATQGPLPETRNDFWKMVLQQKSQIIV 84

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823416726 1225 MLP---DNQSLAEDEfvYWPSREESMNCEAFTVTLISKdrlclSNEEQIIIHDFILeaTQDDYVLEVRHFQCPKWPNPDA 1301
Cdd:cd14614     85 MLTqcnEKRRVKCDH--YWPFTEEPVAYGDITVEMLSE-----EEQPDWAIREFRV--SYADEVQDVMHFNYTAWPDHGV 155

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823416726 1302 P----ISSTFELINVIKEEALTRDGPTIVHDEYGAVSAGTLCALTTLSQQLENENAVDVFQVAKMINLMRPGVFTDIEQY 1377
Cdd:cd14614    156 PtanaAESILQFVQMVRQQAVKSKGPMIIHCSAGVGRTGTFIALDRLLQHIRDHEFVDILGLVSEMRSYRMSMVQTEEQY 235


                   ....*...
gi 1823416726 1378 QFLYKAML 1385
Cdd:cd14614    236 IFIHQCVQ 243
R-PTPc-M-1 cd14633
catalytic domain of receptor-type tyrosine-protein phosphatase M, repeat 1; Receptor-type ...
 1146-1385 2.99e-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: 130.16  E-value: 2.99e-33
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823416726 1146 SAQKDCNKEKNRNSSVVPSERARVGLAPLPGMKGTDYINASYIMGYYRSNEFIITQHPLPHTTKDFWRMIWDHNAQIIVM 1225
Cdd:cd14633     34 SAKKDENRMKNRYGNIIAYDHSRVRLQPIEGETSSDYINGNYIDGYHRPNHYIATQGPMQETIYDFWRMVWHENTASIIM 113

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823416726 1226 LPDNQSLAEDEFV-YWPSREESMncEAFTVTLISKDRLclsneEQIIIHDFILEATQDDYVLEVRHFQCPKWPNPDAPIS 1304
Cdd:cd14633    114 VTNLVEVGRVKCCkYWPDDTEIY--KDIKVTLIETELL-----AEYVIRTFAVEKRGVHEIREIRQFHFTGWPDHGVPYH 186

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823416726 1305 ST--FELINVIKEEALTRDGPTIVHDEYGAVSAGTLCALTTLSQQLENENAVDVFQVAKMINLMRPGVFTDIEQYQFLYK 1382
Cdd:cd14633    187 ATglLGFVRQVKSKSPPNAGPLVVHCSAGAGRTGCFIVIDIMLDMAEREGVVDIYNCVRELRSRRVNMVQTEEQYVFIHD 266


                   ...
gi 1823416726 1383 AML 1385
Cdd:cd14633    267 AIL 269
R-PTPc-Q cd14616
catalytic domain of receptor-type tyrosine-protein phosphatase Q; Receptor-type ...
 1156-1382 5.22e-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: 5.22e-33
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823416726 1156 NRNSSVVPSERARVGLAPLPGMKGTDYINASYIMGYYRSNEFIITQHPLPHTTKDFWRMIWDHNAQIIVMLpdNQSLAED 1235
Cdd:cd14616      1 NRFPNIKPYNNNRVKLIADAGVPGSDYINASYISGYLCPNEFIATQGPLPGTVGDFWRMVWETRAKTIVML--TQCFEKG 78

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823416726 1236 EF---VYWPsrEESMNCEAFTVTLISKdrlcLSNEEQI--IIHDFILEaTQDDYVLeVRHFQCPKWPNPDAPiSSTFELI 1310
Cdd:cd14616     79 RIrchQYWP--EDNKPVTVFGDIVITK----LMEDVQIdwTIRDLKIE-RHGDYMM-VRQCNFTSWPEHGVP-ESSAPLI 149

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1823416726 1311 NVIKEEALTRDG---PTIVHDEYGAVSAGTLCALTTLSQQLENENAVDVFQVAKMINLMRPGVFTDIEQYQFLYK 1382
Cdd:cd14616    150 HFVKLVRASRAHdntPMIVHCSAGVGRTGVFIALDHLTQHINDHDFVDIYGLVAELRSERMCMVQNLAQYIFLHQ 224
PTPc-KIM cd14547
catalytic domain of the kinase interaction motif (KIM) family of protein-tyrosine phosphatases; ...
 1156-1381 5.30e-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: 5.30e-33
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823416726 1156 NRNSSVVPSERARVGLAPLPGMKGTDYINASYIMGY-YRSNEFIITQHPLPHTTKDFWRMIWDHNAQIIVMLPDNQSLAE 1234
Cdd:cd14547      1 NRYKTILPNEHSRVCLPSVDDDPLSSYINANYIRGYdGEEKAYIATQGPLPNTVADFWRMVWQEKTPIIVMITNLTEAKE 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823416726 1235 DEFVYWPSrEESMNCEAFTVTLISKDRlclsnEEQIIIHDFILEatqddYVLEVR---HFQCPKWPN---PDAPiSSTFE 1308
Cdd:cd14547     81 KCAQYWPE-EENETYGDFEVTVQSVKE-----TDGYTVRKLTLK-----YGGEKRylkHYWYTSWPDhktPEAA-QPLLS 148

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1823416726 1309 LINVIKEEALTRD--GPTIVHDEYGAVSAGTLCALTTLSQQLENENAVDVFQVAKMINLMRPGVFTDIEQYQFLY 1381
Cdd:cd14547    149 LVQEVEEARQTEPhrGPIVVHCSAGIGRTGCFIATSIGCQQLREEGVVDVLGIVCQLRLDRGGMVQTAEQYEFVH 223
R-PTPc-T-1 cd14630
catalytic domain of receptor-type tyrosine-protein phosphatase T, repeat 1; Receptor-type ...
 1150-1385 6.34e-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: 128.22  E-value: 6.34e-33
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823416726 1150 DCNKEKNRNSSVVPSERARVGLAPLPGMKGTDYINASYIMGYYRSNEFIITQHPLPHTTKDFWRMIWDHNAQIIVMLPDN 1229
Cdd:cd14630      1 DENRNKNRYGNIISYDHSRVRLQLLDGDPHSDYINANYIDGYHRPRHYIATQGPMQETVKDFWRMIWQENSASVVMVTNL 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823416726 1230 QSLAEDEFV-YWPSREESMNceAFTVTLISKDRLClsneeQIIIHDFILEATQDDYVLEVRHFQCPKWPNPDAPISST-- 1306
Cdd:cd14630     81 VEVGRVKCVrYWPDDTEVYG--DIKVTLIETEPLA-----EYVIRTFTVQKKGYHEIREIRQFHFTSWPDHGVPCYATgl 153

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1823416726 1307 FELINVIKEEALTRDGPTIVHDEYGAVSAGTLCALTTLSQQLENENAVDVFQVAKMINLMRPGVFTDIEQYQFLYKAML 1385
Cdd:cd14630    154 LGFVRQVKFLNPPDAGPIVVHCSAGAGRTGCFIAIDIMLDMAENEGVVDIFNCVRELRAQRVNMVQTEEQYVFVHDAIL 232
R-PTPc-B cd14617
catalytic domain of receptor-type tyrosine-protein phosphatase B; Receptor-type ...
 1156-1382 1.73e-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: 1.73e-32
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823416726 1156 NRNSSVVPSERARVGLAPLPGMKGTDYINASYIMGYYRSNEFIITQHPLPHTTKDFWRMIWDHNAQIIVMLpdnQSLAED 1235
Cdd:cd14617      1 NRYNNILPYDSTRVKLSNVDDDPCSDYINASYIPGNNFRREYIATQGPLPGTKDDFWKMVWEQNVHNIVMV---TQCVEK 77

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823416726 1236 EFV----YWPSREESMNCEAFTVTLISKDRLclsneEQIIIHDF-ILEATQDDYVLEVRHFQCPKWPNPDAPiSSTFELI 1310
Cdd:cd14617     78 GRVkcdhYWPADQDSLYYGDLIVQMLSESVL-----PEWTIREFkICSEEQLDAPRLVRHFHYTVWPDHGVP-ETTQSLI 151

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823416726 1311 NVIKEealTRD--------GPTIVHDEYGAVSAGTLCALTTLSQQLENENAVDVFQVAKMINLMRPGVFTDIEQYQFLYK 1382
Cdd:cd14617    152 QFVRT---VRDyinrtpgsGPTVVHCSAGVGRTGTFIALDRILQQLDSKDSVDIYGAVHDLRLHRVHMVQTECQYVYLHQ 228
R-PTPc-F-1 cd14626
catalytic domain of receptor-type tyrosine-protein phosphatase F, repeat 1; Receptor-type ...
 1150-1389 2.03e-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: 2.03e-32
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823416726 1150 DCNKEKNRNSSVVPSERARVGLAPLPGMKGTDYINASYIMGYYRSNEFIITQHPLPHTTKDFWRMIWDHNAQIIVMLpdn 1229
Cdd:cd14626     39 EVNKPKNRYANVIAYDHSRVILTSVDGVPGSDYINANYIDGYRKQNAYIATQGPLPETLSDFWRMVWEQRTATIVMM--- 115

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823416726 1230 QSLAEDEFV----YWPSReESMNCEAFTVTLISKDRLCLSNeeqiiIHDFILEATQDDYVLEVRHFQCPKWPN---PDAP 1302
Cdd:cd14626    116 TRLEEKSRVkcdqYWPIR-GTETYGMIQVTLLDTVELATYS-----VRTFALYKNGSSEKREVRQFQFMAWPDhgvPEYP 189

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823416726 1303 iSSTFELINVIKEEALTRDGPTIVHDEYGAVSAGTLCALTTLSQQLENENAVDVFQVAKMINLMRPGVFTDIEQYQFLYK 1382
Cdd:cd14626    190 -TPILAFLRRVKACNPPDAGPMVVHCSAGVGRTGCFIVIDAMLERMKHEKTVDIYGHVTCMRSQRNYMVQTEDQYIFIHE 268


                   ....*..
gi 1823416726 1383 AMLSLVS 1389
Cdd:cd14626    269 ALLEAAT 275
R5-PTP-2 cd14550
PTP-like domain of R5 subfamily receptor-type tyrosine-protein phosphatases, repeat 2; The R5 ...
 883-1089 2.09e-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: 125.51  E-value: 2.09e-32
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823416726  883 YINANYVDGYNKAKAYIATQGPLKSTFEDFWRMIWEQNTGIIVMITNLVEKGrrKCDQYWPT-ENSEEYGNIIVTLKSTN 961
Cdd:cd14550      1 YINASYLQGYRRSNEFIITQHPLEHTIKDFWQMIWDHNSQTIVMLTDNELNE--DEPIYWPTkEKPLECETFKVTLSGED 78

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823416726  962 vHAC------YTVRRFTIRNTkmkkgqkgnpkgrQNER--TVIQYHYTQWPDMGVPEY-ALPVLTFVRRSSAARTpdmGP 1032
Cdd:cd14550     79 -HSClsneirLIVRDFILEST-------------QDDYvlEVRQFQCPSWPNPCSPIHtVFELINTVQEWAQQRD---GP 141

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 1823416726 1033 VVVHCSAGVGRTGTYIVIDSMLQQIKDKSTVNVLGFLKHIRTQRNYLVQTEEQYIFI 1089
Cdd:cd14550    142 IVVHDRYGGVQAATFCALTTLHQQLEHESSVDVYQVAKLYHLMRPGVFTSKEDYQFL 198
alpha_CARP_VIII cd03120
Carbonic anhydrase alpha related protein, group VIII. Carbonic anhydrase related proteins ...
 80-317 1.31e-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: 1.31e-31
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823416726   80 GSHQSPIDIMDHLAHVGDEYQELQLdgfdneSSNKTWMK-----NTGKTVAILLKDDYFVSGAGLP--GRFKAEKVEFHW 152
Cdd:cd03120     13 GEYQSPINLNSREARYDPSLLEVRL------SPNYVVCRdceviNDGHTIQIILKSKSVLSGGPLPqgHEFELAEVRFHW 86

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823416726  153 GQSNgSAGSEHSINGKRFPVEMQIYFYNPDDFDSFGTAVLENRVVGAMAVFFQVSpRDNSALDPIIHGLKGVVHHEKETF 232
Cdd:cd03120     87 GREN-QRGSEHTVNFKAFPMELHLIHWNSTLYSSLEEAMGKPHGIAIIALFVQIG-KEHVGLKAVTEILQDIQYKGKSKT 164

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823416726  233 LDPFVLRELLPTS-LGSYYRYTGSLTTPPCSEIVEWIVFRKPVPISYHQLEAFYSIFTteqqdHVKSVEYLR-------N 304
Cdd:cd03120    165 IPCFNPNTLLPDPlLRDYWVYEGSLTTPPCSEGVTWILFRYPLTISQSQIEEFRRLRT-----HVKGAELVEgcdgllgD 239

                          250
                   ....*....|...
gi 1823416726  305 NFRPQQRLNNRKV 317
Cdd:cd03120    240 NFRPTQPLSDRVI 252
R-PTPc-S-1 cd14625
catalytic domain of receptor-type tyrosine-protein phosphatase S, repeat 1; Receptor-type ...
 1150-1389 4.06e-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: 4.06e-31
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823416726 1150 DCNKEKNRNSSVVPSERARVGLAPLPGMKGTDYINASYIMGYYRSNEFIITQHPLPHTTKDFWRMIWDHNAQIIVM---L 1226
Cdd:cd14625     45 EVNKPKNRYANVIAYDHSRVILQPIEGIMGSDYINANYIDGYRKQNAYIATQGPLPETFGDFWRMVWEQRSATVVMmtkL 124

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823416726 1227 PDNQSLAEDEfvYWPSREESmNCEAFTVTLISKDRLClsneeQIIIHDFILEATQDDYVLEVRHFQCPKWPNPDAPISST 1306
Cdd:cd14625    125 EEKSRIKCDQ--YWPSRGTE-TYGMIQVTLLDTIELA-----TFCVRTFSLHKNGSSEKREVRQFQFTAWPDHGVPEYPT 196

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823416726 1307 --FELINVIKEEALTRDGPTIVHDEYGAVSAGTLCALTTLSQQLENENAVDVFQVAKMINLMRPGVFTDIEQYQFLYKAM 1384
Cdd:cd14625    197 pfLAFLRRVKTCNPPDAGPIVVHCSAGVGRTGCFIVIDAMLERIKHEKTVDIYGHVTLMRSQRNYMVQTEDQYSFIHDAL 276


                   ....*
gi 1823416726 1385 LSLVS 1389
Cdd:cd14625    277 LEAVA 281
R-PTPc-T-2 cd14634
PTP domain of receptor-type tyrosine-protein phosphatase T, repeat 2; Receptor-type ...
 883-1095 6.37e-31

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: 121.28  E-value: 6.37e-31
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823416726  883 YINANYVDGYNKAKAYIATQGPLKSTFEDFWRMIWEQNTGIIVMITNLveKGRRKCDQYWPTENSEEYGNIIVTLKSTNV 962
Cdd:cd14634      1 YINAALMDSHKQPAAFIVTQHPLPNTVADFWRLVFDYNCSSVVMLNEM--DAAQLCMQYWPEKTSCCYGPIQVEFVSADI 78

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823416726  963 HACYTVRRFTIRNtkMKKGQKGnpkgrqnERTVIQYHYTQWPDM-GVPEYALPVLTFVRRSSAARTP---DMGPVVVHCS 1038
Cdd:cd14634     79 DEDIISRIFRICN--MARPQDG-------YRIVQHLQYIGWPAYrDTPPSKRSILKVVRRLEKWQEQydgREGRTVVHCL 149

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 1823416726 1039 AGVGRTGTYIVIDSMLQQIKDKSTVNVLGFLKHIRTQRNYLVQTEEQYIFIHDALLE 1095
Cdd:cd14634    150 NGGGRSGTFCAICSVCEMIQQQNIIDVFHTVKTLRNNKSNMVETLEQYKFVYEVALE 206
PTP_fungal cd18533
fungal protein tyrosine phosphatases; This subfamily contains Saccharomyces cerevisiae ...
 1182-1381 7.19e-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: 121.20  E-value: 7.19e-31
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823416726 1182 YINASYI-MGYYRSNEFIITQHPLPHTTKDFWRMIWDHNAQIIVML-PDNQSLAEDEFVYWPSREESMNCEAFTVTLISK 1259
Cdd:cd18533      1 YINASYItLPGTSSKRYIATQGPLPATIGDFWKMIWQNNVGVIVMLtPLVENGREKCDQYWPSGEYEGEYGDLTVELVSE 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823416726 1260 DRLclsNEEQIIIHDFILeATQDDYVLEVRHFQCPKWPNPDAP--ISSTFELINVIKE--EALTRDGPTIVHdeygaVSA 1335
Cdd:cd18533     81 EEN---DDGGFIVREFEL-SKEDGKVKKVYHIQYKSWPDFGVPdsPEDLLTLIKLKRElnDSASLDPPIIVH-----CSA 151

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1823416726 1336 -----GTLCALTTLSQQLEN--------ENAVDVfqVAKMINLM---RPGVFTDIEQYQFLY 1381
Cdd:cd18533    152 gvgrtGTFIALDSLLDELKRglsdsqdlEDSEDP--VYEIVNQLrkqRMSMVQTLRQYIFLY 211
PTPc-N7 cd14612
catalytic domain of tyrosine-protein phosphatase non-receptor type 7; Tyrosine-protein ...
 1155-1384 9.31e-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: 122.25  E-value: 9.31e-31
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823416726 1155 KNRNSSVVPSERARVGL-APLPGMKGTDYINASYIMGYY-RSNEFIITQHPLPHTTKDFWRMIWDHNAQIIVMLPDNQSL 1232
Cdd:cd14612     18 KDRYKTILPNPQSRVCLrRAGSQEEEGSYINANYIRGYDgKEKAYIATQGPMLNTVSDFWEMVWQEECPIIVMITKLKEK 97

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823416726 1233 AEDEFVYWPSREESMNceAFTVTlISKDRLClsneEQIIIHDFILEATQDDYvlEVRHFQCPKWPNPDAPIS--STFELI 1310
Cdd:cd14612     98 KEKCVHYWPEKEGTYG--RFEIR-VQDMKEC----DGYTIRDLTIQLEEESR--SVKHYWFSSWPDHQTPESagPLLRLV 168

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1823416726 1311 NVIKE--EALTRDGPTIVHDEYGAVSAGTLCALTTLSQQLENENAVDVFQVAKMINLMRPGVFTDIEQYQFLYKAM 1384
Cdd:cd14612    169 AEVEEsrQTAASPGPIVVHCSAGIGRTGCFIATSIGCQQLKDTGKVDILGIVCQLRLDRGGMIQTSEQYQFLHHTL 244
R-PTPc-E-1 cd14620
catalytic domain of receptor-type tyrosine-protein phosphatase E, repeat 1; Receptor-type ...
 1160-1385 2.33e-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: 2.33e-30
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823416726 1160 SVVPSERARVGLAPLPGMKGTDYINASYIMGYYRSNEFIITQHPLPHTTKDFWRMIWDHNAQIIVMLPDNQSLAEDE-FV 1238
Cdd:cd14620      3 NILPYDHSRVILSQLDGIPCSDYINASYIDGYKEKNKFIAAQGPKQETVNDFWRMVWEQKSATIVMLTNLKERKEEKcYQ 82

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823416726 1239 YWPSReesmNCEAF-TVTLISKDRLCLSNeeqIIIHDFILEATQDDYVLEVR-----HFQcpKWPNPDAPIS--STFELI 1310
Cdd:cd14620     83 YWPDQ----GCWTYgNIRVAVEDCVVLVD---YTIRKFCIQPQLPDGCKAPRlvtqlHFT--SWPDFGVPFTpiGMLKFL 153

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1823416726 1311 NVIKEEALTRDGPTIVHDEYGAVSAGTLCALTTLSQQLENENAVDVFQVAKMINLMRPGVFTDIEQYQFLYKAML 1385
Cdd:cd14620    154 KKVKSVNPVHAGPIVVHCSAGVGRTGTFIVIDAMIDMMHAEQKVDVFEFVSRIRNQRPQMVQTDMQYSFIYQALL 228
PTPc-N5 cd14613
catalytic domain of tyrosine-protein phosphatase non-receptor type 5; Tyrosine-protein ...
 1155-1384 3.81e-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: 3.81e-30
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823416726 1155 KNRNSSVVPSERARVGL-APLPGMKGTDYINASYIMGY-YRSNEFIITQHPLPHTTKDFWRMIWDHNAQIIVMLPDNQSL 1232
Cdd:cd14613     28 KNRYKTILPNPHSRVCLtSPDQDDPLSSYINANYIRGYgGEEKVYIATQGPTVNTVGDFWRMVWQERSPIIVMITNIEEM 107

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823416726 1233 AEDEFVYWPsrEESMNCEAFTVTLisKDRLClsnEEQIIIHDFILEATQDDYVLevRHFQCPKWPNPDAPISST--FELI 1310
Cdd:cd14613    108 NEKCTEYWP--EEQVTYEGIEITV--KQVIH---ADDYRLRLITLKSGGEERGL--KHYWYTSWPDQKTPDNAPplLQLV 178

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1823416726 1311 NVIKE---EALTRDGPTIVHDEYGAVSAGTLCALTTLSQQLENENAVDVFQVAKMINLMRPGVFTDIEQYQFLYKAM 1384
Cdd:cd14613    179 QEVEEarqQAEPNCGPVIVHCSAGIGRTGCFIATSICCKQLRNEGVVDILRTTCQLRLDRGGMIQTCEQYQFVHHVL 255
R-PTPc-G-1 cd17667
catalytic domain of receptor-type tyrosine-protein phosphatase G, repeat 1; Receptor-type ...
 1152-1388 6.28e-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: 6.28e-30
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823416726 1152 NKEKNRNSSVVPSERARVGLAPLPGM--KGTDYINASYIMGYYRSNEFIITQHPLPHTTKDFWRMIWDHNAQIIVMLPDn 1229
Cdd:cd17667     27 NKHKNRYINILAYDHSRVKLRPLPGKdsKHSDYINANYVDGYNKAKAYIATQGPLKSTFEDFWRMIWEQNTGIIVMITN- 105

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823416726 1230 qsLAE------DEfvYWPSrEESMNCEAFTVTLIS-KDRLCLSneeqiiIHDFILEATQDDYVLE-----------VRHF 1291
Cdd:cd17667    106 --LVEkgrrkcDQ--YWPT-ENSEEYGNIIVTLKStKIHACYT------VRRFSIRNTKVKKGQKgnpkgrqnertVIQY 174

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823416726 1292 QCPKWPNPDAPISSTFELINVIKEEA--LTRDGPTIVHDEYGAVSAGTLCALTTLSQQLENENAVDVFQVAKMINLMRPG 1369
Cdd:cd17667    175 HYTQWPDMGVPEYALPVLTFVRRSSAarTPEMGPVLVHCSAGVGRTGTYIVIDSMLQQIKDKSTVNVLGFLKHIRTQRNY 254

                          250
                   ....*....|....*....
gi 1823416726 1370 VFTDIEQYQFLYKAMLSLV 1388
Cdd:cd17667    255 LVQTEEQYIFIHDALLEAI 273
R-PTP-N cd14609
PTP-like domain of receptor-type tyrosine-protein phosphatase N; Receptor-type ...
 1124-1384 1.03e-29

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: 1.03e-29
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823416726 1124 KTRLEKQFKLVTQCNAKYVECFSAQKDCNKEKNRNSSVVPSERARVGLAPLPGMKGTDYINASYIMGY-YRSNEFIITQH 1202
Cdd:cd14609     14 RDRLAKEWQALCAYQAEPNTCSTAQGEANVKKNRNPDFVPYDHARIKLKAESNPSRSDYINASPIIEHdPRMPAYIATQG 93

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823416726 1203 PLPHTTKDFWRMIWDHNAQIIVMLpdnQSLAEDEFV----YWPSREESMNcEAFTVTLISKDRLClsneEQIIIHDFILE 1278
Cdd:cd14609     94 PLSHTIADFWQMVWENGCTVIVML---TPLVEDGVKqcdrYWPDEGSSLY-HIYEVNLVSEHIWC----EDFLVRSFYLK 165

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823416726 1279 ATQDDYVLEVRHFQCPKWPNPDAPiSSTFELINV---IKEEALTRDGPTIVHDEYGAVSAGTLCAL-TTLSQQLENENAV 1354
Cdd:cd14609    166 NVQTQETRTLTQFHFLSWPAEGIP-SSTRPLLDFrrkVNKCYRGRSCPIIVHCSDGAGRTGTYILIdMVLNRMAKGVKEI 244

                          250       260       270
                   ....*....|....*....|....*....|
gi 1823416726 1355 DVFQVAKMINLMRPGVFTDIEQYQFLYKAM 1384
Cdd:cd14609    245 DIAATLEHVRDQRPGMVRTKDQFEFALTAV 274
R-PTPc-D-1 cd14624
catalytic domain of receptor-type tyrosine-protein phosphatase D, repeat 1; Receptor-type ...
 1150-1389 1.54e-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: 119.84  E-value: 1.54e-29
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823416726 1150 DCNKEKNRNSSVVPSERARVGLAPLPGMKGTDYINASYIMGYYRSNEFIITQHPLPHTTKDFWRMIWDHNAQIIVM---L 1226
Cdd:cd14624     45 EVNKPKNRYANVIAYDHSRVLLSAIEGIPGSDYINANYIDGYRKQNAYIATQGALPETFGDFWRMIWEQRSATVVMmtkL 124

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823416726 1227 PDNQSLAEDEfvYWPSREESMNcEAFTVTLISKDRLClsneeQIIIHDFILEATQDDYVLEVRHFQCPKWPNPDAPISST 1306
Cdd:cd14624    125 EERSRVKCDQ--YWPSRGTETY-GLIQVTLLDTVELA-----TYCVRTFALYKNGSSEKREVRQFQFTAWPDHGVPEHPT 196

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823416726 1307 --FELINVIKEEALTRDGPTIVHDEYGAVSAGTLCALTTLSQQLENENAVDVFQVAKMINLMRPGVFTDIEQYQFLYKAM 1384
Cdd:cd14624    197 pfLAFLRRVKTCNPPDAGPMVVHCSAGVGRTGCFIVIDAMLERIKHEKTVDIYGHVTLMRAQRNYMVQTEDQYIFIHDAL 276


                   ....*
gi 1823416726 1385 LSLVS 1389
Cdd:cd14624    277 LEAVT 281
PTPc-N22 cd14602
catalytic domain of tyrosine-protein phosphatase non-receptor type 22; Tyrosine-protein ...
 1155-1387 1.63e-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: 118.40  E-value: 1.63e-29
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823416726 1155 KNRNSSVVPSERARVGLAPLPGMKGTDYINASYIMGYYRSNEFIITQHPLPHTTKDFWRMIWDHNAQIIVMlpdnqslAE 1234
Cdd:cd14602      1 KNRYKDILPYDHSRVELSLITSDEDSDYINANFIKGVYGPRAYIATQGPLSTTLLDFWRMIWEYSVLIIVM-------AC 73

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823416726 1235 DEFV--------YWP-SREESMNCEAFTVTLISKDrlclsNEEQIIIHdfILEATQDDYVLEVRHFQCPKWPNPDAP--I 1303
Cdd:cd14602     74 MEFEmgkkkcerYWAePGEMQLEFGPFSVTCEAEK-----RKSDYIIR--TLKVKFNSETRTIYQFHYKNWPDHDVPssI 146

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823416726 1304 SSTFELINVIKEEALTRDGPTIVHDEYGAVSAGTLCALTTLSQQLENENAVDVFQVAKMINLM---RPGVFTDIEQYQFL 1380
Cdd:cd14602    147 DPILELIWDVRCYQEDDSVPICIHCSAGCGRTGVICAIDYTWMLLKDGIIPENFSVFSLIQEMrtqRPSLVQTKEQYELV 226


                   ....*..
gi 1823416726 1381 YKAMLSL 1387
Cdd:cd14602    227 YNAVIEL 233
R-PTP-N2 cd14610
PTP-like domain of receptor-type tyrosine-protein phosphatase N2; Receptor-type ...
 1124-1384 1.72e-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: 1.72e-29
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823416726 1124 KTRLEKQFKLVTQCNAKYVECFSAQKDCNKEKNRNSSVVPSERARVGLAPLPGMKGTDYINASYIMGY-YRSNEFIITQH 1202
Cdd:cd14610     16 KNRLEKEWEALCAYQAEPNATNVAQREENVQKNRSLAVLPYDHSRIILKAENSHSHSDYINASPIMDHdPRNPAYIATQG 95

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823416726 1203 PLPHTTKDFWRMIWDHNAQIIVML-PDNQSLAEDEFVYWPSrEESMNCEAFTVTLISKDRLClsneEQIIIHDFILEATQ 1281
Cdd:cd14610     96 PLPATVADFWQMVWESGCVVIVMLtPLAENGVKQCYHYWPD-EGSNLYHIYEVNLVSEHIWC----EDFLVRSFYLKNLQ 170

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823416726 1282 DDYVLEVRHFQCPKWPNPDAPiSSTFELINV---IKEEALTRDGPTIVHDEYGAVSAGTLCAL-TTLSQQLENENAVDVF 1357
Cdd:cd14610    171 TNETRTVTQFHFLSWNDQGVP-ASTRSLLDFrrkVNKCYRGRSCPIIVHCSDGAGRSGTYILIdMVLNKMAKGAKEIDIA 249

                          250       260
                   ....*....|....*....|....*..
gi 1823416726 1358 QVAKMINLMRPGVFTDIEQYQFLYKAM 1384
Cdd:cd14610    250 ATLEHLRDQRPGMVQTKEQFEFALTAV 276
PTPc-N22_18_12 cd14542
catalytic domain of tyrosine-protein phosphatase non-receptor type 22, type 18 and type 12; ...
 1182-1382 2.21e-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: 116.75  E-value: 2.21e-29
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823416726 1182 YINASYIMGYYRSNEFIITQHPLPHTTKDFWRMIWDHNAQIIVMLPDNQSLAEDEFV-YWP-SREESMNCEAFTVTLISK 1259
Cdd:cd14542      1 YINANFIKGVSGSKAYIATQGPLPNTVLDFWRMIWEYNVQVIVMACREFEMGKKKCErYWPeEGEEQLQFGPFKISLEKE 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823416726 1260 DRLClsneEQIIIHDFILEATQDDYVleVRHFQCPKWPNPDAPISST--FELINVIKEEALTRDGPTIVHDEYGAVSAGT 1337
Cdd:cd14542     81 KRVG----PDFLIRTLKVTFQKESRT--VYQFHYTAWPDHGVPSSVDpiLDLVRLVRDYQGSEDVPICVHCSAGCGRTGT 154

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*....
gi 1823416726 1338 LCAL----TTLSQQLENENaVDVFQVAKMINLMRPGVFTDIEQYQFLYK 1382
Cdd:cd14542    155 ICAIdyvwNLLKTGKIPEE-FSLFDLVREMRKQRPAMVQTKEQYELVYR 202
R-PTPc-T-2 cd14634
PTP domain of receptor-type tyrosine-protein phosphatase T, repeat 2; Receptor-type ...
 1182-1385 2.57e-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: 2.57e-29
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823416726 1182 YINASYIMGYYRSNEFIITQHPLPHTTKDFWRMIWDHNAQIIVMLPDNQSlAEDEFVYWPsrEESMNCEA-FTVTLISKD 1260
Cdd:cd14634      1 YINAALMDSHKQPAAFIVTQHPLPNTVADFWRLVFDYNCSSVVMLNEMDA-AQLCMQYWP--EKTSCCYGpIQVEFVSAD 77

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823416726 1261 RlclsnEEQIIIHDFI---LEATQDDYVLeVRHFQCPKWPN-PDAPIS--STFELINVI---KEEALTRDGPTIVHDEYG 1331
Cdd:cd14634     78 I-----DEDIISRIFRicnMARPQDGYRI-VQHLQYIGWPAyRDTPPSkrSILKVVRRLekwQEQYDGREGRTVVHCLNG 151

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....
gi 1823416726 1332 AVSAGTLCALTTLSQQLENENAVDVFQVAKMINLMRPGVFTDIEQYQFLYKAML 1385
Cdd:cd14634    152 GGRSGTFCAICSVCEMIQQQNIIDVFHTVKTLRNNKSNMVETLEQYKFVYEVAL 205
R5-PTPc-1 cd14549
catalytic domain of R5 subfamily receptor-type tyrosine-protein phosphatases, repeat 1; The R5 ...
 1182-1381 3.19e-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: 3.19e-29
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823416726 1182 YINASYIMGYYRSNEFIITQHPLPHTTKDFWRMIWDHNAQIIVMLPDnqsLAE------DEfvYWPSrEESMNCEAFTVT 1255
Cdd:cd14549      1 YINANYVDGYNKARAYIATQGPLPSTFDDFWRMVWEQNSAIIVMITN---LVErgrrkcDQ--YWPK-EGTETYGNIQVT 74

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823416726 1256 LISKD--------RLCLSNEEqiiihdfILEATQDDYVLEVRHFQCPKWPNPDAPiSSTFELINVIKEEALTRD---GPT 1324
Cdd:cd14549     75 LLSTEvlatytvrTFSLKNLK-------LKKVKGRSSERVVYQYHYTQWPDHGVP-DYTLPVLSFVRKSSAANPpgaGPI 146

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1823416726 1325 IVHDEYGAVSAGTLCALTTLSQQLENENAVDVFQVAKMI----NLMrpgVFTDiEQYQFLY 1381
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, ...
 1182-1385 6.53e-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: 115.40  E-value: 6.53e-29
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823416726 1182 YINASYIMGYYRSNEFIITQHPLPHTTKDFWRMIWDHNAQIIVMLPDnqsLAEDEFV----YWPSREESMNceAFTVTLI 1257
Cdd:cd14555      1 YINANYIDGYHRPNHYIATQGPMQETVYDFWRMVWQENSASIVMVTN---LVEVGRVkcsrYWPDDTEVYG--DIKVTLV 75

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823416726 1258 SKDRLClsneeQIIIHDFILEATQDDYVLEVRHFQCPKWPNPDAPISST--FELINVIKEEALTRDGPTIVHDEYGAVSA 1335
Cdd:cd14555     76 ETEPLA-----EYVVRTFALERRGYHEIREVRQFHFTGWPDHGVPYHATglLGFIRRVKASNPPSAGPIVVHCSAGAGRT 150

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|
gi 1823416726 1336 GTLCALTTLSQQLENENAVDVFQVAKMINLMRPGVFTDIEQYQFLYKAML 1385
Cdd:cd14555    151 GCYIVIDIMLDMAEREGVVDIYNCVKELRSRRVNMVQTEEQYIFIHDAIL 200
R-PTPc-A-1 cd14621
catalytic domain of receptor-type tyrosine-protein phosphatase A, repeat 1; Receptor-type ...
 1144-1385 9.50e-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: 9.50e-29
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823416726 1144 CFSAQKDCNKEKNRNSSVVPSERARVGLAPLPGMKGTDYINASYIMGYYRSNEFIITQHPLPHTTKDFWRMIWDHNAQII 1223
Cdd:cd14621     44 CEAASKEENKEKNRYVNILPYDHSRVHLTPVEGVPDSDYINASFINGYQEKNKFIAAQGPKEETVNDFWRMIWEQNTATI 123

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823416726 1224 VMLPDNQSLAEDEFV-YWPSReesmNCEAFTVTLIS-KDRLCLSNeeqIIIHDFILEATQDDYVLE----VRHFQCPKWP 1297
Cdd:cd14621    124 VMVTNLKERKECKCAqYWPDQ----GCWTYGNIRVSvEDVTVLVD---YTVRKFCIQQVGDVTNKKpqrlITQFHFTSWP 196

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823416726 1298 NPDAPIS--STFELINVIKEEALTRDGPTIVHDEYGAVSAGTLCALTTLSQQLENENAVDVFQVAKMINLMRPGVFTDIE 1375
Cdd:cd14621    197 DFGVPFTpiGMLKFLKKVKNCNPQYAGAIVVHCSAGVGRTGTFIVIDAMLDMMHAERKVDVYGFVSRIRAQRCQMVQTDM 276

                          250
                   ....*....|
gi 1823416726 1376 QYQFLYKAML 1385
Cdd:cd14621    277 QYVFIYQALL 286
R-PTPc-U-2 cd14637
PTP domain of receptor-type tyrosine-protein phosphatase U, repeat 2; Receptor-type ...
 1182-1385 2.82e-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: 113.85  E-value: 2.82e-28
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823416726 1182 YINASYIMGYYRSNEFIITQHPLPHTTKDFWRMIWDHNAQIIVMLPD-NQS-LAEDEFVYWPsreESMNCEaftVTLISK 1259
Cdd:cd14637      1 YINAALTDSYTRSAAFIVTLHPLQNTTTDFWRLVYDYGCTSVVMLNQlNQSnSAWPCLQYWP---EPGLQQ---YGPMEV 74

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823416726 1260 DRLCLSNEEQIIIHDFILE--ATQDDYVLEVRHFQCPKWP----NPDAPISSTFELINVIKEEALTRDGPTIVHDEYGAV 1333
Cdd:cd14637     75 EFVSGSADEDIVTRLFRVQniTRLQEGHLMVRHFQFLRWSayrdTPDSKKAFLHLLASVEKWQRESGEGRTVVHCLNGGG 154

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|..
gi 1823416726 1334 SAGTLCALTTLSQQLENENAVDVFQVAKMINLMRPGVFTDIEQYQFLYKAML 1385
Cdd:cd14637    155 RSGTYCASAMILEMIRCHNIVDVFYAVKTLRNYKPNMVETLEQYRFCYEIAL 206
PTPc-N12 cd14604
catalytic domain of tyrosine-protein phosphatase non-receptor type 12; Tyrosine-protein ...
 1148-1387 1.08e-26

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: 1.08e-26
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823416726 1148 QKDCNKEKNRNSSVVPSERARVGLAPLPGMKGTDYINASYIMGYYRSNEFIITQHPLPHTTKDFWRMIWDHNAQIIVMlp 1227
Cdd:cd14604     53 EKEENVKKNRYKDILPFDHSRVKLTLKTSSQDSDYINANFIKGVYGPKAYIATQGPLANTVIDFWRMIWEYNVAIIVM-- 130

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823416726 1228 dnqslAEDEFV--------YWPSR-EESMNCEAFTVTliskdrlCLSNEEQI--IIHDFILEATQDDYVLEVRHFQcpKW 1296
Cdd:cd14604    131 -----ACREFEmgrkkcerYWPLYgEEPMTFGPFRIS-------CEAEQARTdyFIRTLLLEFQNETRRLYQFHYV--NW 196

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823416726 1297 PNPDAPIS--STFELINVIKEEALTRDGPTIVHDEYGAVSAGTLCALTTLSQQLENENAVDVFQVAKMINLMRPGVFTDI 1374
Cdd:cd14604    197 PDHDVPSSfdSILDMISLMRKYQEHEDVPICIHCSAGCGRTGAICAIDYTWNLLKAGKIPEEFNVFNLIQEMRTQRHSAV 276

                          250
                   ....*....|....*.
gi 1823416726 1375 ---EQYQFLYKAMLSL 1387
Cdd:cd14604    277 qtkEQYELVHRAIAQL 292
R-PTPc-K-1 cd14631
catalytic domain of receptor-type tyrosine-protein phosphatase K, repeat 1; Receptor-type ...
 1168-1385 1.13e-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: 109.34  E-value: 1.13e-26
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823416726 1168 RVGLAPLPGMKGTDYINASYIMGYYRSNEFIITQHPLPHTTKDFWRMIWDHNAQIIVMLPDNQSLAEDE-FVYWPSREES 1246
Cdd:cd14631      1 RVILQPVEDDPSSDYINANYIDGYQRPSHYIATQGPVHETVYDFWRMIWQEQSACIVMVTNLVEVGRVKcYKYWPDDTEV 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823416726 1247 MNceAFTVTLISKDRLClsneeQIIIHDFILEATQDDYVLEVRHFQCPKWPNPDAPISST--FELINVIKEEALTRDGPT 1324
Cdd:cd14631     81 YG--DFKVTCVEMEPLA-----EYVVRTFTLERRGYNEIREVKQFHFTGWPDHGVPYHATglLSFIRRVKLSNPPSAGPI 153

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1823416726 1325 IVHDEYGAVSAGTLCALTTLSQQLENENAVDVFQVAKMINLMRPGVFTDIEQYQFLYKAML 1385
Cdd:cd14631    154 VVHCSAGAGRTGCYIVIDIMLDMAEREGVVDIYNCVKALRSRRINMVQTEEQYIFIHDAIL 214
R-PTPc-U-1 cd14632
catalytic domain of receptor-type tyrosine-protein phosphatase U, repeat 1; Receptor-type ...
 1182-1385 1.14e-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: 1.14e-26
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823416726 1182 YINASYIMGYYRSNEFIITQHPLPHTTKDFWRMIWDHNAQIIVMLpdnQSLAEDEFV----YWPsrEESMNCEAFTVTLI 1257
Cdd:cd14632      1 YINANYIDGYHRSNHFIATQGPKQEMVYDFWRMVWQEHCSSIVMI---TKLVEVGRVkcskYWP--DDSDTYGDIKITLL 75

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823416726 1258 SKDRLClsneeQIIIHDFILEATQDDYVLEVRHFQCPKWPNPDAPISST--FELINVIKEEALTRDGPTIVHDEYGAVSA 1335
Cdd:cd14632     76 KTETLA-----EYSVRTFALERRGYSARHEVKQFHFTSWPEHGVPYHATglLAFIRRVKASTPPDAGPVVVHCSAGAGRT 150

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|
gi 1823416726 1336 GTLCALTTLSQQLENENAVDVFQVAKMINLMRPGVFTDIEQYQFLYKAML 1385
Cdd:cd14632    151 GCYIVLDVMLDMAECEGVVDIYNCVKTLCSRRINMIQTEEQYIFIHDAIL 200
PTPc-N1 cd14608
catalytic domain of tyrosine-protein phosphatase non-receptor type 1; Tyrosine-protein ...
 1144-1385 2.00e-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: 2.00e-26
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823416726 1144 CFSAQKDCNKEKNRNSSVVPSERARVGLAplpgMKGTDYINASYIMGYYRSNEFIITQHPLPHTTKDFWRMIWDHNAQII 1223
Cdd:cd14608     17 CRVAKLPKNKNRNRYRDVSPFDHSRIKLH----QEDNDYINASLIKMEEAQRSYILTQGPLPNTCGHFWEMVWEQKSRGV 92

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823416726 1224 VMLpdNQSLAEDEF---VYWPSREES---MNCEAFTVTLISKDRLCLSNEEQIIIHDFILEATQddyvlEVRHFQCPKWP 1297
Cdd:cd14608     93 VML--NRVMEKGSLkcaQYWPQKEEKemiFEDTNLKLTLISEDIKSYYTVRQLELENLTTQETR-----EILHFHYTTWP 165

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823416726 1298 N---PDAPISSTFELINVIKEEALTRD-GPTIVHDEYGAVSAGTLCALTT---LSQQLENENAVDVFQVAKMINLMRPGV 1370
Cdd:cd14608    166 DfgvPESPASFLNFLFKVRESGSLSPEhGPVVVHCSAGIGRSGTFCLADTcllLMDKRKDPSSVDIKKVLLEMRKFRMGL 245

                          250
                   ....*....|....*
gi 1823416726 1371 FTDIEQYQFLYKAML 1385
Cdd:cd14608    246 IQTADQLRFSYLAVI 260
PTPc-N1_2 cd14545
catalytic domain of tyrosine-protein phosphatase non-receptor type 1 and type 2; ...
 1155-1382 4.99e-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: 4.99e-26
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823416726 1155 KNRNSSVVPSERARVGLAPLPGmkGTDYINASYIMGYYRSNEFIITQHPLPHTTKDFWRMIWDHNAQIIVMLpdnQSLAE 1234
Cdd:cd14545      1 LNRYRDRDPYDHDRSRVKLKQG--DNDYINASLVEVEEAKRSYILTQGPLPNTSGHFWQMVWEQNSKAVIML---NKLME 75

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823416726 1235 DE----FVYWPSREESMNC---EAFTVTLISKDRlclsnEEQIIIHDFILEATQDDYVLEVRHFQCPKWPN---PDAPIS 1304
Cdd:cd14545     76 KGqikcAQYWPQGEGNAMIfedTGLKVTLLSEED-----KSYYTVRTLELENLKTQETREVLHFHYTTWPDfgvPESPAA 150

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823416726 1305 STFELINVIKEEALTRD-GPTIVHDEYGAVSAGTLCALTTLSQQLENEN--AVDVFQVAKMINLMRPGVFTDIEQYQFLY 1381
Cdd:cd14545    151 FLNFLQKVRESGSLSSDvGPPVVHCSAGIGRSGTFCLVDTCLVLIEKGNpsSVDVKKVLLEMRKYRMGLIQTPDQLRFSY 230


                   .
gi 1823416726 1382 K 1382
Cdd:cd14545    231 L 231
R-PTPc-M-2 cd14635
PTP domain of receptor-type tyrosine-protein phosphatase M, repeat 2; Receptor-type ...
 1182-1385 7.57e-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: 106.70  E-value: 7.57e-26
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823416726 1182 YINASYIMGYYRSNEFIITQHPLPHTTKDFWRMIWDHNAQIIVMLPDNQSlAEDEFVYWPSREESMNcEAFTVTLISKDR 1261
Cdd:cd14635      1 YINAALMDSYKQPSAFIVTQHPLPNTVKDFWRLVLDYHCTSIVMLNDVDP-AQLCPQYWPENGVHRH-GPIQVEFVSADL 78

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823416726 1262 lclsnEEQIIIHDF-ILEAT--QDDYVLeVRHFQCPKWP-NPDAPIS--STFELINVI---KEEALTRDGPTIVHDEYGA 1332
Cdd:cd14635     79 -----EEDIISRIFrIYNAArpQDGYRM-VQQFQFLGWPmYRDTPVSkrSFLKLIRQVdkwQEEYNGGEGRTVVHCLNGG 152

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|...
gi 1823416726 1333 VSAGTLCALTTLSQQLENENAVDVFQVAKMINLMRPGVFTDIEQYQFLYKAML 1385
Cdd:cd14635    153 GRSGTFCAISIVCEMLRHQRAVDVFHAVKTLRNNKPNMVDLLDQYKFCYEVAL 205
R-PTPc-Z-1 cd17668
catalytic domain of receptor-type tyrosine-protein phosphatase Z, repeat 1; Receptor-type ...
 1182-1385 1.00e-25

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: 1.00e-25
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823416726 1182 YINASYIMGYYRSNEFIITQHPLPHTTKDFWRMIWDHNAQIIVMLPDnqsLAE------DEfvYWPSrEESMNCEAFTVT 1255
Cdd:cd17668      1 YINANYVDGYNKPKAYIAAQGPLKSTAEDFWRMIWEHNVEVIVMITN---LVEkgrrkcDQ--YWPA-DGSEEYGNFLVT 74

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823416726 1256 LISKDRLCLSNEEQIIIHDF-ILEATQDDYVLE--VRHFQCPKWPNPDAPiSSTFELINVIKEEALTRD---GPTIVHDE 1329
Cdd:cd17668     75 QKSVQVLAYYTVRNFTLRNTkIKKGSQKGRPSGrvVTQYHYTQWPDMGVP-EYTLPVLTFVRKASYAKRhavGPVVVHCS 153

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 1823416726 1330 YGAVSAGTLCALTTLSQQLENENAVDVFQVAKMINLMRPGVFTDIEQYQFLYKAML 1385
Cdd:cd17668    154 AGVGRTGTYIVLDSMLQQIQHEGTVNIFGFLKHIRSQRNYLVQTEEQYVFIHDALV 209
PTPc_DSPc smart00012
Protein tyrosine phosphatase, catalytic domain, undefined specificity; Protein tyrosine ...
 1287-1386 3.12e-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: 3.12e-25
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823416726  1287 EVRHFQCPKWPNPDAPISST--FELINVIKEE--ALTRDGPTIVHDEYGAVSAGTLCALTTLSQQLENE-NAVDVFQVAK 1361
Cdd:smart00012    1 TVKHYHYTGWPDHGVPESPDsiLELLRAVKKNlnQSESSGPVVVHCSAGVGRTGTFVAIDILLQQLEAEaGEVDIFDTVK 80

                            90       100
                    ....*....|....*....|....*
gi 1823416726  1362 MINLMRPGVFTDIEQYQFLYKAMLS 1386
Cdd:smart00012   81 ELRSQRPGMVQTEEQYLFLYRALLE 105
PTPc_motif smart00404
Protein tyrosine phosphatase, catalytic domain motif;
1287-1386 3.12e-25

Protein tyrosine phosphatase, catalytic domain motif;


Pssm-ID: 214649 [Multi-domain]  Cd Length: 105  Bit Score: 101.28  E-value: 3.12e-25
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823416726  1287 EVRHFQCPKWPNPDAPISST--FELINVIKEE--ALTRDGPTIVHDEYGAVSAGTLCALTTLSQQLENE-NAVDVFQVAK 1361
Cdd:smart00404    1 TVKHYHYTGWPDHGVPESPDsiLELLRAVKKNlnQSESSGPVVVHCSAGVGRTGTFVAIDILLQQLEAEaGEVDIFDTVK 80

                            90       100
                    ....*....|....*....|....*
gi 1823416726  1362 MINLMRPGVFTDIEQYQFLYKAMLS 1386
Cdd:smart00404   81 ELRSQRPGMVQTEEQYLFLYRALLE 105
PHA02747 PHA02747
protein tyrosine phosphatase; Provisional
 1103-1393 5.74e-25

protein tyrosine phosphatase; Provisional


Pssm-ID: 165114 [Multi-domain]  Cd Length: 312  Bit Score: 107.39  E-value: 5.74e-25
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823416726 1103 EVSANQLHSYVNSILIPGIggkTRLEkQFKLVTQCNAKYVECFsaQKDCNKEKNRNSSVVPSERARVGLAPLPGmKGTDY 1182
Cdd:PHA02747     8 ECRAIDFLKRRNQLNCFGI---IRDE-HHQIILKPFDGLIANF--EKPENQPKNRYWDIPCWDHNRVILDSGGG-STSDY 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823416726 1183 INASYIMGYYRSNEFIITQHPLPHTTKDFWRMIWDHNAQIIVMLPDNQSLAEDE--FVYW-PSREESMNCEAFTVTLISK 1259
Cdd:PHA02747    81 IHANWIDGFEDDKKFIATQGPFAETCADFWKAVWQEHCSIIVMLTPTKGTNGEEkcYQYWcLNEDGNIDMEDFRIETLKT 160

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823416726 1260 DRLCLSNEEQIIIHDFILEATQddyvlEVRHFQCPKWPNPDAPISST-----FELINVIKEEALTRDG-------PTIVH 1327
Cdd:PHA02747   161 SVRAKYILTLIEITDKILKDSR-----KISHFQCSEWFEDETPSDHPdfikfIKIIDINRKKSGKLFNpkdallcPIVVH 235

                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1823416726 1328 DEYGAVSAGTLCALTTLSQQLENENAVDVFQVAKMINLMRPGVFTDIEQYQFL---YKAMLSLVSTKEN 1393
Cdd:PHA02747   236 CSDGVGKTGIFCAVDICLNQLVKRKAICLAKTAEKIREQRHAGIMNFDDYLFIqpgYEVLHYFLSKIKA 304
PHA02746 PHA02746
protein tyrosine phosphatase; Provisional
 1152-1384 6.70e-25

protein tyrosine phosphatase; Provisional


Pssm-ID: 165113 [Multi-domain]  Cd Length: 323  Bit Score: 107.42  E-value: 6.70e-25
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823416726 1152 NKEKNRNSSVVPSERARVGLAPLPGMKGTD-------------------YINASYIMGYYRSNEFIITQHPLPHTTKDFW 1212
Cdd:PHA02746    51 NLKKNRFHDIPCWDHSRVVINAHESLKMFDvgdsdgkkievtsednaenYIHANFVDGFKEANKFICAQGPKEDTSEDFF 130

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823416726 1213 RMIWDHNAQIIVMLPDNQSLAEDEFVYWPSREESMNCEAFTVTLISKDRLCLS-NEEQIIIHDFILEATQddyvlEVRHF 1291
Cdd:PHA02746   131 KLISEHESQVIVSLTDIDDDDEKCFELWTKEEDSELAFGRFVAKILDIIEELSfTKTRLMITDKISDTSR-----EIHHF 205

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823416726 1292 QCPKWP---NPDAPiSSTFELINVIKEEAL----------TRDGPTIVHDEYGAVSAGTLCALTTLSQQLENENAVDVFQ 1358
Cdd:PHA02746   206 WFPDWPdngIPTGM-AEFLELINKVNEEQAelikqadndpQTLGPIVVHCSAGIGRAGTFCAIDNALEQLEKEKEVCLGE 284

                          250       260
                   ....*....|....*....|....*.
gi 1823416726 1359 VAKMINLMRPGVFTDIEQYQFLYKAM 1384
Cdd:PHA02746   285 IVLKIRKQRHSSVFLPEQYAFCYKAL 310
R-PTPc-K-2 cd14636
PTP domain of receptor-type tyrosine-protein phosphatase K, repeat 2; Receptor-type ...
 1182-1385 8.73e-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: 8.73e-25
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823416726 1182 YINASYIMGYYRSNEFIITQHPLPHTTKDFWRMIWDHNAQIIVMLpDNQSLAEDEFVYWPsrEESMnceaFTVTLISKDR 1261
Cdd:cd14636      1 YINAALMDSYRQPAAFIVTQHPLPNTVKDFWRLVYDYGCTSIVML-NEVDLAQGCPQYWP--EEGM----LRYGPIQVEC 73

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823416726 1262 LCLSNEEQIIIHDFI---LEATQDDYVLeVRHFQCPKWPNPDAPISSTFELINVI------KEEALTRDGPTIVHDEYGA 1332
Cdd:cd14636     74 MSCSMDCDVISRIFRicnLTRPQEGYLM-VQQFQYLGWASHREVPGSKRSFLKLIlqvekwQEECDEGEGRTIIHCLNGG 152

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|...
gi 1823416726 1333 VSAGTLCALTTLSQQLENENAVDVFQVAKMINLMRPGVFTDIEQYQFLYKAML 1385
Cdd:cd14636    153 GRSGMFCAISIVCEMIKRQNVVDVFHAVKTLRNSKPNMVETPEQYRFCYDVAL 205
R-PTPc-K-2 cd14636
PTP domain of receptor-type tyrosine-protein phosphatase K, repeat 2; Receptor-type ...
 883-1095 9.34e-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: 9.34e-25
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823416726  883 YINANYVDGYNKAKAYIATQGPLKSTFEDFWRMIWEQNTGIIVMITNL-VEKGrrkCDQYWPTENSEEYGNIIVTLKSTN 961
Cdd:cd14636      1 YINAALMDSYRQPAAFIVTQHPLPNTVKDFWRLVYDYGCTSIVMLNEVdLAQG---CPQYWPEEGMLRYGPIQVECMSCS 77

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823416726  962 VHACYTVRRFTIRNtkMKKGQKGnpkgrqnERTVIQYHYTQWPDM----GVPEYALPVLTFVRRSSAARTPDMGPVVVHC 1037
Cdd:cd14636     78 MDCDVISRIFRICN--LTRPQEG-------YLMVQQFQYLGWASHrevpGSKRSFLKLILQVEKWQEECDEGEGRTIIHC 148

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 1823416726 1038 SAGVGRTGTYIVIDSMLQQIKDKSTVNVLGFLKHIRTQRNYLVQTEEQYIFIHDALLE 1095
Cdd:cd14636    149 LNGGGRSGMFCAISIVCEMIKRQNVVDVFHAVKTLRNSKPNMVETPEQYRFCYDVALE 206
PTPc-N20_13 cd14538
catalytic domain of tyrosine-protein phosphatase non-receptor type 20 and type 13; ...
 1182-1385 1.97e-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: 1.97e-24
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823416726 1182 YINASYIM-----GYYRsneFIITQHPLPHTTKDFWRMIWDHNAQIIVMLPDNqslAEDEFV----YWP-SREESMNCEA 1251
Cdd:cd14538      1 YINASHIRipvggDTYH---YIACQGPLPNTTGDFWQMVWEQKSEVIAMVTQD---VEGGKVkchrYWPdSLNKPLICGG 74

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823416726 1252 -FTVTLISKDRLclsneEQIIIHDFILEATQDDYVLEVRHFQCPKWPNPDAPiSSTFELINVIKE-EALTRDGPTIVHDE 1329
Cdd:cd14538     75 rLEVSLEKYQSL-----QDFVIRRISLRDKETGEVHHITHLNFTTWPDHGTP-QSADPLLRFIRYmRRIHNSGPIVVHCS 148

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 1823416726 1330 YGAVSAGTLCALTTLSQQLENENAVDVFQVAKMINLMRPGVFTDIEQYQFLYKAML 1385
Cdd:cd14538    149 AGIGRTGVLITIDVALGLIERDLPFDIQDIVKDLREQRQGMIQTKDQYIFCYKACL 204
R-PTPc-R cd14611
catalytic domain of receptor-type tyrosine-protein phosphatase R; Receptor-type ...
 1155-1381 2.14e-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: 103.07  E-value: 2.14e-24
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823416726 1155 KNRNSSVVPSERARVGLAPL-PGMKGTDYINASYIMGYY-RSNEFIITQHPLPHTTKDFWRMIWDHNAQIIVMLPDNQSL 1232
Cdd:cd14611      2 KNRYKTILPNPHSRVCLKPKnSNDSLSTYINANYIRGYGgKEKAFIATQGPMINTVNDFWQMVWQEDSPVIVMITKLKEK 81

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823416726 1233 AEDEFVYWPSREESMNCEAFTVTliskdrlCLSNEEQIIIHDFILEatQDDYVLEVRHFQCPKWPNPDAPISST--FELI 1310
Cdd:cd14611     82 NEKCVLYWPEKRGIYGKVEVLVN-------SVKECDNYTIRNLTLK--QGSQSRSVKHYWYTSWPDHKTPDSAQplLQLM 152

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1823416726 1311 NVIKEEAL--TRDGPTIVHDEYGAVSAGTLCALTTLSQQLENENAVDVFQVAKMINLMRPGVFTDIEQYQFLY 1381
Cdd:cd14611    153 LDVEEDRLasPGRGPVVVHCSAGIGRTGCFIATTIGCQQLKEEGVVDVLSIVCQLRVDRGGMVQTSEQYEFVH 225
PTPc-N11_6 cd14544
catalytic domain of tyrosine-protein phosphatase non-receptor type 11 and type 6; ...
 1152-1384 2.20e-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: 2.20e-24
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823416726 1152 NKEKNRNSSVVPSERARVGLAPL-PGMKGTDYINASYIM-----GYYRSNE--FIITQHPLPHTTKDFWRMIWDHNAQII 1223
Cdd:cd14544      1 NKGKNRYKNILPFDHTRVILKDRdPNVPGSDYINANYIRnenegPTTDENAktYIATQGCLENTVSDFWSMVWQENSRVI 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823416726 1224 VMLPDNQSLAEDEFV-YWPsreESMNCEAFtvtliskDRLCLSNEEQIIIHDFIL------EATQDDYVLEVRHFQCPKW 1296
Cdd:cd14544     81 VMTTKEVERGKNKCVrYWP---DEGMQKQY-------GPYRVQNVSEHDTTDYTLrelqvsKLDQGDPIREIWHYQYLSW 150

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823416726 1297 PN---PDAP--ISSTFELINViKEEALTRDGPTIVHDEYGAVSAGTLCALTTLSQQLENEN---AVDVFQVAKMINLMRP 1368
Cdd:cd14544    151 PDhgvPSDPggVLNFLEDVNQ-RQESLPHAGPIVVHCSAGIGRTGTFIVIDMLLDQIKRKGldcDIDIQKTIQMVRSQRS 229

                          250
                   ....*....|....*.
gi 1823416726 1369 GVFTDIEQYQFLYKAM 1384
Cdd:cd14544    230 GMVQTEAQYKFIYVAV 245
PTPc-N3 cd14600
catalytic domain of tyrosine-protein phosphatase non-receptor type 3; Tyrosine-protein ...
 1152-1385 4.16e-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: 103.78  E-value: 4.16e-24
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823416726 1152 NKEKNRNSSVVPSERARVGLAplpgmKGTDYINASY----IMGYYRSNEFIITQHPLPHTTKDFWRMIWDHNAQIIVMLp 1227
Cdd:cd14600     40 NMDKNRYKDVLPYDATRVVLQ-----GNEDYINASYvnmeIPSANIVNKYIATQGPLPHTCAQFWQVVWEQKLSLIVML- 113

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823416726 1228 dnQSLAEDEFV----YWPSREESMNCEAFTVTliskdrlCLSNEEQI--IIHDFILEATQDDYVLEVRHFQCPKWPNPDA 1301
Cdd:cd14600    114 --TTLTERGRTkchqYWPDPPDVMEYGGFRVQ-------CHSEDCTIayVFREMLLTNTQTGEERTVTHLQYVAWPDHGV 184

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823416726 1302 PISST--FELINVIKEEALTRDgPTIVHDEYGAVSAGTLCALTTLSQQLENENAVDVFQVAKMINLMRPGVFTDIEQYQF 1379
Cdd:cd14600    185 PDDSSdfLEFVNYVRSKRVENE-PVLVHCSAGIGRTGVLVTMETAMCLTERNQPVYPLDIVRKMRDQRAMMVQTSSQYKF 263


                   ....*.
gi 1823416726 1380 LYKAML 1385
Cdd:cd14600    264 VCEAIL 269
R-PTPc-U-2 cd14637
PTP domain of receptor-type tyrosine-protein phosphatase U, repeat 2; Receptor-type ...
 883-1095 4.19e-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: 101.91  E-value: 4.19e-24
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823416726  883 YINANYVDGYNKAKAYIATQGPLKSTFEDFWRMIWEQNTGIIVMITNLVEKGRR-KCDQYWPTENSEEYGNIIVTLKSTN 961
Cdd:cd14637      1 YINAALTDSYTRSAAFIVTLHPLQNTTTDFWRLVYDYGCTSVVMLNQLNQSNSAwPCLQYWPEPGLQQYGPMEVEFVSGS 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823416726  962 VHACYTVRRFTIRN-TKMKKGQkgnpkgrqneRTVIQYHYTQW-PDMGVPEYA---LPVLTFVRRSSaaRTPDMGPVVVH 1036
Cdd:cd14637     81 ADEDIVTRLFRVQNiTRLQEGH----------LMVRHFQFLRWsAYRDTPDSKkafLHLLASVEKWQ--RESGEGRTVVH 148

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 1823416726 1037 CSAGVGRTGTYIVIDSMLQQIKDKSTVNVLGFLKHIRTQRNYLVQTEEQYIFIHDALLE 1095
Cdd:cd14637    149 CLNGGGRSGTYCASAMILEMIRCHNIVDVFYAVKTLRNYKPNMVETLEQYRFCYEIALE 207
PTPc-N13 cd14597
catalytic domain of tyrosine-protein phosphatase non-receptor type 13; Tyrosine-protein ...
 1152-1385 1.94e-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: 100.67  E-value: 1.94e-23
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823416726 1152 NKEKNRNSSVVPSERARVGLaplpGMKGtDYINASYIMGYYRSNEF--IITQHPLPHTTKDFWRMIWDHNAQIIVMLPDN 1229
Cdd:cd14597      3 NRKKNRYKNILPYDTTRVPL----GDEG-GYINASFIKMPVGDEEFvyIACQGPLPTTVADFWQMVWEQKSTVIAMMTQE 77

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823416726 1230 qslAEDEFV----YWPsreesmncEAFTVTLISKDRLCLS-----NEEQIIIHDFILEATQDDYVLEVRHFQCPKWPNPD 1300
Cdd:cd14597     78 ---VEGGKIkcqrYWP--------EILGKTTMVDNRLQLTlvrmqQLKNFVIRVLELEDIQTREVRHITHLNFTAWPDHD 146

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823416726 1301 APiSSTFELINVIK-EEALTRDGPTIVHDEYGAVSAGTL-C---ALTTLSQQLEnenaVDVFQVAKMINLMRPGVFTDIE 1375
Cdd:cd14597    147 TP-SQPEQLLTFISyMRHIHKSGPIITHCSAGIGRSGTLiCidvVLGLISKDLD----FDISDIVRTMRLQRHGMVQTED 221

                          250
                   ....*....|
gi 1823416726 1376 QYQFLYKAML 1385
Cdd:cd14597    222 QYIFCYQVIL 231
R-PTP-Z-2 cd17669
catalytic domain of receptor-type tyrosine-protein phosphatase Z, repeat 2; Receptor-type ...
 883-1094 5.08e-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: 98.53  E-value: 5.08e-23
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823416726  883 YINANYVDGYNKAKAYIATQGPLKSTFEDFWRMIWEQNTGIIVMITNLVEKGRRKCdQYWPteNSEEYGN---IIVTLKS 959
Cdd:cd17669      1 YINASYIMGYYQSNEFIITQHPLLHTIKDFWRMIWDHNAQLIVMLPDGQNMAEDEF-VYWP--NKDEPINcetFKVTLIA 77

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823416726  960 TNvHACYT------VRRFTIRNTkmkkgqkgnpkgrQNERTVIQYHYT--QWPDMGVP-EYALPVLTFVRRSSAARTpdm 1030
Cdd:cd17669     78 EE-HKCLSneekliIQDFILEAT-------------QDDYVLEVRHFQcpKWPNPDSPiSKTFELISIIKEEAANRD--- 140

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1823416726 1031 GPVVVHCSAGVGRTGTYIVIDSMLQQIKDKSTVNVLGFLKHIRTQRNYLVQTEEQYIFIHDALL 1094
Cdd:cd17669    141 GPMIVHDEHGGVTAGTFCALTTLMHQLEKENSVDVYQVAKMINLMRPGVFTDIEQYQFLYKAIL 204
PHA02738 PHA02738
hypothetical protein; Provisional
 1145-1384 5.78e-23

hypothetical protein; Provisional


Pssm-ID: 222923 [Multi-domain]  Cd Length: 320  Bit Score: 101.54  E-value: 5.78e-23
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823416726 1145 FSAQKDcNKEKNRNSSVVPSERARVGLaPLPGMKGtDYINASYIMGYYRSNEFIITQHPLPHTTKDFWRMIWDHNAQIIV 1224
Cdd:PHA02738    43 FNAEKK-NRKLNRYLDAVCFDHSRVIL-PAERNRG-DYINANYVDGFEYKKKFICGQAPTRQTCYDFYRMLWMEHVQIIV 119

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823416726 1225 ML-PDNQSLAEDEFVYWPSREE-SMNCEAFTVTLISKDRLCLSNEEQIIIHDFIlEATQddyvlEVRHFQCPKWPNPDAP 1302
Cdd:PHA02738   120 MLcKKKENGREKCFPYWSDVEQgSIRFGKFKITTTQVETHPHYVKSTLLLTDGT-SATQ-----TVTHFNFTAWPDHDVP 193

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823416726 1303 iSSTFELINVI----------KEEAL------TRDGPTIVHDEYGAVSAGTLCALTTLSQQLENENAVDVFQVAKMINLM 1366
Cdd:PHA02738   194 -KNTSEFLNFVlevrqcqkelAQESLqighnrLQPPPIVVHCNAGLGRTPCYCVVDISISRFDACATVSIPSIVSSIRNQ 272

                          250
                   ....*....|....*...
gi 1823416726 1367 RPGVFTDIEQYQFLYKAM 1384
Cdd:PHA02738   273 RYYSLFIPFQYFFCYRAV 290
PTPc-N3_4 cd14541
catalytic domain of tyrosine-protein phosphatase non-receptor type 21 and type 14; ...
 1181-1386 6.13e-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: 6.13e-23
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823416726 1181 DYINASYI-MGYYRS---NEFIITQHPLPHTTKDFWRMIWDHNAQIIVMLpdnQSLAEDEFV----YWPSREESMNCEAF 1252
Cdd:cd14541      1 DYINANYVnMEIPGSgivNRYIAAQGPLPNTCADFWQMVWEQKSTLIVML---TTLVERGRVkchqYWPDLGETMQFGNL 77

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823416726 1253 TVTliskdrlCLSNEEQI--IIHDFILEATQDDYVLEVRHFQCPKWPNPDAPISSTfELINVIKEEALTRDG---PTIVH 1327
Cdd:cd14541     78 QIT-------CVSEEVTPsfAFREFILTNTNTGEERHITQMQYLAWPDHGVPDDSS-DFLDFVKRVRQNRVGmvePTVVH 149

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 1823416726 1328 DEYGAVSAGTLCALTTLSQQLENENAVDVFQVAKMINLMRPGVFTDIEQYQFLYKAMLS 1386
Cdd:cd14541    150 CSAGIGRTGVLITMETAMCLIEANEPVYPLDIVRTMRDQRAMLIQTPSQYRFVCEAILR 208
R-PTPc-M-2 cd14635
PTP domain of receptor-type tyrosine-protein phosphatase M, repeat 2; Receptor-type ...
 883-1095 1.76e-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: 97.07  E-value: 1.76e-22
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823416726  883 YINANYVDGYNKAKAYIATQGPLKSTFEDFWRMIWEQNTGIIVMITNLveKGRRKCDQYWPTENSEEYGNIIVTLKSTNV 962
Cdd:cd14635      1 YINAALMDSYKQPSAFIVTQHPLPNTVKDFWRLVLDYHCTSIVMLNDV--DPAQLCPQYWPENGVHRHGPIQVEFVSADL 78

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823416726  963 HACYTVRRFTIRNTKmkkgqkgnpKGRQNERTVIQYHYTQWPDM-GVPEYALPVLTFVRRSSAARTP---DMGPVVVHCS 1038
Cdd:cd14635     79 EEDIISRIFRIYNAA---------RPQDGYRMVQQFQFLGWPMYrDTPVSKRSFLKLIRQVDKWQEEyngGEGRTVVHCL 149

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 1823416726 1039 AGVGRTGTYIVIDSMLQQIKDKSTVNVLGFLKHIRTQRNYLVQTEEQYIFIHDALLE 1095
Cdd:cd14635    150 NGGGRSGTFCAISIVCEMLRHQRAVDVFHAVKTLRNNKPNMVDLLDQYKFCYEVALE 206
PTPc-N6 cd14606
catalytic domain of tyrosine-protein phosphatase non-receptor type 6; Tyrosine-protein ...
 1148-1390 2.05e-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: 2.05e-22
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823416726 1148 QKDCNKEKNRNSSVVPSERARVGLAPL-PGMKGTDYINASYIMGYYRSNE-----FIITQHPLPHTTKDFWRMIWDHNAQ 1221
Cdd:cd14606     14 QRPENKSKNRYKNILPFDHSRVILQGRdSNIPGSDYINANYVKNQLLGPDenaktYIASQGCLEATVNDFWQMAWQENSR 93

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823416726 1222 IIVMLPDNQSLAEDEFV-YWPSREESMNCEAFTVTLIS-------KDR-LCLSneeqiIIHDfileatqDDYVLEVRHFQ 1292
Cdd:cd14606     94 VIVMTTREVEKGRNKCVpYWPEVGMQRAYGPYSVTNCGehdtteyKLRtLQVS-----PLDN-------GELIREIWHYQ 161

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823416726 1293 CPKWPNPDAP-----ISSTFELINViKEEALTRDGPTIVHDEYGAVSAGTLCALTTLSQQLENENA---VDVFQVAKMIN 1364
Cdd:cd14606    162 YLSWPDHGVPsepggVLSFLDQINQ-RQESLPHAGPIIVHCSAGIGRTGTIIVIDMLMENISTKGLdcdIDIQKTIQMVR 240

                          250       260
                   ....*....|....*....|....*.
gi 1823416726 1365 LMRPGVFTDIEQYQFLYKAMLSLVST 1390
Cdd:cd14606    241 AQRSGMVQTEAQYKFIYVAIAQFIET 266
R-PTP-G-2 cd17670
PTP-like domain of receptor-type tyrosine-protein phosphatase G, repeat 2; Receptor-type ...
 883-1094 2.61e-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: 96.67  E-value: 2.61e-22
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823416726  883 YINANYVDGYNKAKAYIATQGPLKSTFEDFWRMIWEQNTGIIVMITN---LVEkgrrkcDQ--YWPT-ENSEEYGNIIVT 956
Cdd:cd17670      1 YINASYIMGYYRSNEFIITQHPLPHTTKDFWRMIWDHNAQIIVMLPDnqgLAE------DEfvYWPSrEESMNCEAFTVT 74

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823416726  957 LKSTNVHACYTVRRFTIRNTKMKKGQkgnpkgrqnERTVIQYHYTQ---WPDMGVP-EYALPVLTFVRRSSAARTpdmGP 1032
Cdd:cd17670     75 LISKDRLCLSNEEQIIIHDFILEATQ---------DDYVLEVRHFQcpkWPNPDAPiSSTFELINVIKEEALTRD---GP 142

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1823416726 1033 VVVHCSAGVGRTGTYIVIDSMLQQIKDKSTVNVLGFLKHIRTQRNYLVQTEEQYIFIHDALL 1094
Cdd:cd17670    143 TIVHDEFGAVSAGTLCALTTLSQQLENENAVDVYQVAKMINLMRPGVFTDIEQYQFLYKAML 204
R-PTPc-C-1 cd14557
catalytic domain of receptor-type tyrosine-protein phosphatase C, repeat 1; Receptor-type ...
 1182-1382 3.34e-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: 96.05  E-value: 3.34e-22
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823416726 1182 YINASYIMGYYRSNEFIITQHPLPHTTKDFWRMIWDHNAQIIVMLPDNQSLAEDE-FVYWPSREESMNCEAFTVTLISKD 1260
Cdd:cd14557      1 YINASYIDGFKEPRKYIAAQGPKDETVDDFWRMIWEQKSTVIVMVTRCEEGNRNKcAQYWPSMEEGSRAFGDVVVKINEE 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823416726 1261 RLClsnEEQIIIHDFILEATQDDYVLEVRHFQCPKWPNPDAPISSTFELINVIKEEALTR--DGPTIVHDEYGAVSAGTL 1338
Cdd:cd14557     81 KIC---PDYIIRKLNINNKKEKGSGREVTHIQFTSWPDHGVPEDPHLLLKLRRRVNAFNNffSGPIVVHCSAGVGRTGTY 157

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....
gi 1823416726 1339 CALTTLSQQLENENAVDVFQVAKMINLMRPGVFTDIEQYQFLYK 1382
Cdd:cd14557    158 IGIDAMLEGLEAEGRVDVYGYVVKLRRQRCLMVQVEAQYILIHQ 201
PTPc-N14 cd14599
catalytic domain of tyrosine-protein phosphatase non-receptor type 14; Tyrosine-protein ...
 1152-1388 6.79e-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: 6.79e-22
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823416726 1152 NKEKNRNSSVVPSERARVGLAPLPgMKGTDYINASYIMGYYRSNE--FIITQHPLPHTTKDFWRMIWDHNAQIIVMLPdn 1229
Cdd:cd14599     38 NAERNRIREVVPYEENRVELVPTK-ENNTGYINASHIKVTVGGEEwhYIATQGPLPHTCHDFWQMVWEQGVNVIAMVT-- 114

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823416726 1230 qslAEDE------FVYWP---SREESMNCEAFTVTL-ISKDRLCLSNEEQIIIHdfiLEATQDDYVLevrHFQCPKWPNP 1299
Cdd:cd14599    115 ---AEEEggrsksHRYWPklgSKHSSATYGKFKVTTkFRTDSGCYATTGLKVKH---LLSGQERTVW---HLQYTDWPDH 185

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823416726 1300 DAP------------ISSTFELINVIKEEALTRDGPTIVHDEYGAVSAGTLCALTTLSQQLENENAVDVFQVAKMINLMR 1367
Cdd:cd14599    186 GCPeevqgflsyleeIQSVRRHTNSMLDSTKNCNPPIVVHCSAGVGRTGVVILTELMIGCLEHNEKVEVPVMLRHLREQR 265

                          250       260
                   ....*....|....*....|.
gi 1823416726 1368 PGVFTDIEQYQFLYKAMLSLV 1388
Cdd:cd14599    266 MFMIQTIAQYKFVYQVLIQFL 286
PTP-N23 cd14539
PTP-like domain of tyrosine-protein phosphatase non-receptor type 23; Tyrosine-protein ...
 1182-1382 8.02e-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: 8.02e-22
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823416726 1182 YINASYIMGYYR-SNEFIITQHPLPHTTKDFWRMIWDHNAQIIVMLPDNQSLAEDEFV-YWPS-REESMNCEAFTVTLIS 1258
Cdd:cd14539      1 YINASLIEDLTPyCPRFIATQAPLPGTAADFWLMVYEQQVSVIVMLVSEQENEKQKVHrYWPTeRGQALVYGAITVSLQS 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823416726 1259 KDRLCLSNEEQIII--HDFILEATqddyvleVRHFQCPKWP---NPDAPiSSTFELINVIKEEALTRDG---PTIVHDEY 1330
Cdd:cd14539     81 VRTTPTHVERIISIqhKDTRLSRS-------VVHLQFTTWPelgLPDSP-NPLLRFIEEVHSHYLQQRSlqtPIVVHCSS 152

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|...
gi 1823416726 1331 GAVSAGTLCALTTLSQQLENENAV-DVFQVAKMINLMRPGVFTDIEQYQFLYK 1382
Cdd:cd14539    153 GVGRTGAFCLLYAAVQEIEAGNGIpDLPQLVRKMRQQRKYMLQEKEHLKFCYE 205
R-PTPc-A-E-1 cd14551
catalytic domain of receptor-type tyrosine-protein phosphatase A and E, repeat 1; ...
 1182-1382 1.09e-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: 1.09e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823416726 1182 YINASYIMGYYRSNEFIITQHPLPHTTKDFWRMIWDHNAQIIVMLPDNQSLAEDEFV-YWPSReesmNCEAFtvtliSKD 1260
Cdd:cd14551      1 YINASYIDGYQEKNKFIAAQGPKDETVNDFWRMIWEQGSATIVMVTNLKERKEKKCSqYWPDQ----GCWTY-----GNL 71

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823416726 1261 RLCLSNEEQIIIH---DFILEATQDDY----VLEVRHFQCPKWPN---PDAPIsSTFELINVIKEEALTRDGPTIVHDEY 1330
Cdd:cd14551     72 RVRVEDTVVLVDYttrKFCIQKVNRGIgekrVRLVTQFHFTSWPDfgvPFTPI-GMLKFLKKVKSANPPRAGPIVVHCSA 150

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|..
gi 1823416726 1331 GAVSAGTLCALTTLSQQLENENAVDVFQVAKMINLMRPGVFTDIEQYQFLYK 1382
Cdd:cd14551    151 GVGRTGTFIVIDAMLDMMHAEGKVDVFGFVSRIRQQRSQMVQTDMQYVFIYQ 202
PTPc-N11 cd14605
catalytic domain of tyrosine-protein phosphatase non-receptor type 11; Tyrosine-protein ...
 1152-1390 1.17e-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: 1.17e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823416726 1152 NKEKNRNSSVVPSERARVGLAP-LPGMKGTDYINASYIMGYYRSN--------EFIITQHPLPHTTKDFWRMIWDHNAQI 1222
Cdd:cd14605      2 NKNKNRYKNILPFDHTRVVLHDgDPNEPVSDYINANIIMPEFETKcnnskpkkSYIATQGCLQNTVNDFWRMVFQENSRV 81

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823416726 1223 IVMLPDNQSLAEDEFV-YWPsreESMNCEAFTVTLIskdrlclSNEEQIIIHDFIL------EATQDDYVLEVRHFQCPK 1295
Cdd:cd14605     82 IVMTTKEVERGKSKCVkYWP---DEYALKEYGVMRV-------RNVKESAAHDYILrelklsKVGQGNTERTVWQYHFRT 151

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823416726 1296 WPNPDAP-----ISSTFELINvIKEEALTRDGPTIVHDEYGAVSAGTLCALTTLSQQLENENA---VDVFQVAKMINLMR 1367
Cdd:cd14605    152 WPDHGVPsdpggVLDFLEEVH-HKQESIMDAGPVVVHCSAGIGRTGTFIVIDILIDIIREKGVdcdIDVPKTIQMVRSQR 230

                          250       260
                   ....*....|....*....|...
gi 1823416726 1368 PGVFTDIEQYQFLYKAMLSLVST 1390
Cdd:cd14605    231 SGMVQTEAQYRFIYMAVQHYIET 253
PTPc-N2 cd14607
catalytic domain of tyrosine-protein phosphatase non-receptor type 2; Tyrosine-protein ...
 1139-1384 1.62e-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: 1.62e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823416726 1139 AKYVEcfsaqkdcNKEKNRNSSVVPSERARVGLAPLPgmkgTDYINASYIMGYYRSNEFIITQHPLPHTTKDFWRMIWDH 1218
Cdd:cd14607     19 AKYPE--------NRNRNRYRDVSPYDHSRVKLQNTE----NDYINASLVVIEEAQRSYILTQGPLPNTCCHFWLMVWQQ 86

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823416726 1219 NAQIIVMLpdnQSLAEDEFV----YWPSREESM---NCEAFTVTLISKDRlclsnEEQIIIHDFILEATQDDYVLEVRHF 1291
Cdd:cd14607     87 KTKAVVML---NRIVEKDSVkcaqYWPTDEEEVlsfKETGFSVKLLSEDV-----KSYYTVHLLQLENINSGETRTISHF 158

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823416726 1292 QCPKWPN---PDAPISSTFELINVIKEEALTRD-GPTIVHDEYGAVSAGTLCALTTLSQQLENEN--AVDVFQVAKMINL 1365
Cdd:cd14607    159 HYTTWPDfgvPESPASFLNFLFKVRESGSLSPEhGPAVVHCSAGIGRSGTFSLVDTCLVLMEKKDpdSVDIKQVLLDMRK 238

                          250
                   ....*....|....*....
gi 1823416726 1366 MRPGVFTDIEQYQFLYKAM 1384
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 ...
 1182-1383 1.07e-20

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: 91.74  E-value: 1.07e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823416726 1182 YINASYIMGYY-RSNEFIITQHPLPHTTKDFWRMIWDHNAQIIVMLPDNQSLAEDEFV-YWPsrEESMNC-EAFTVTLIS 1258
Cdd:cd14546      1 YINASTIYDHDpRNPAYIATQGPLPHTIADFWQMIWEQGCVVIVMLTRLQENGVKQCArYWP--EEGSEVyHIYEVHLVS 78

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823416726 1259 KDRLClsneEQIIIHDFILEATQDDYVLEVRHFQCPKWPNPDAPISST--FELINVIKEEALTRDGPTIVHDEYGAVSAG 1336
Cdd:cd14546     79 EHIWC----DDYLVRSFYLKNLQTSETRTVTQFHFLSWPDEGIPASAKplLEFRRKVNKSYRGRSCPIVVHCSDGAGRTG 154

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*...
gi 1823416726 1337 TLCAL-TTLSQQLENENAVDVFQVAKMINLMRPGVFTDIEQYQFLYKA 1383
Cdd:cd14546    155 TYILIdMVLNRMAKGAKEIDIAATLEHLRDQRPGMVKTKDQFEFVLTA 202
PTPc-N20 cd14596
catalytic domain of tyrosine-protein phosphatase non-receptor type 20; Tyrosine-protein ...
 1182-1385 3.57e-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: 90.19  E-value: 3.57e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823416726 1182 YINASYIMGYYRSNE--FIITQHPLPHTTKDFWRMIWDHNAQIIVMLPDNQSLAEDE-FVYWP-SREESMNCEAFTVTLI 1257
Cdd:cd14596      1 YINASYITMPVGEEElfYIATQGPLPSTIDDFWQMVWENRSDVIAMMTREVERGKVKcHRYWPeTLQEPMELENYQLRLE 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823416726 1258 SKDRLclsneEQIIIHDFILEATQDDYVLEVRHFQCPKWPNPDAPISSTfELINVIK-EEALTRDGPTIVHDEYGAVSAG 1336
Cdd:cd14596     81 NYQAL-----QYFIIRIIKLVEKETGENRLIKHLQFTTWPDHGTPQSSD-QLVKFICyMRKVHNTGPIVVHCSAGIGRAG 154

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*....
gi 1823416726 1337 TLCALTTLSQQLENENAVDVFQVAKMINLMRPGVFTDIEQYQFLYKAML 1385
Cdd:cd14596    155 VLICVDVLLSLIEKDLSFNIKDIVREMRQQRYGMIQTKDQYLFCYKVVL 203
PTPc-N21_14 cd14540
catalytic domain of tyrosine-protein phosphatase non-receptor type 21 and type 14; ...
 1182-1385 5.15e-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: 87.51  E-value: 5.15e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823416726 1182 YINASYIMGYYRSNE--FIITQHPLPHTTKDFWRMIWDHNAQIIVMLPDNQSLA-EDEFVYWP---SREESMNCEAFTVT 1255
Cdd:cd14540      1 YINASHITATVGGKQrfYIAAQGPLQNTVGDFWQMVWEQGVYLVVMVTAEEEGGrEKCFRYWPtlgGEHDALTFGEYKVS 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823416726 1256 L-ISKDRLCLsneeqiIIHDFILEATQDDYVLEVRHFQCPKWPN---PDAPIS--STFELINVIKEEAL------TRDGP 1323
Cdd:cd14540     81 TkFSVSSGCY------TTTGLRVKHTLSGQSRTVWHLQYTDWPDhgcPEDVSGflDFLEEINSVRRHTNqdvaghNRNPP 154

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1823416726 1324 TIVHDEYGAVSAGTLCALTTLSQQLENENAVDVFQVAKMINLMRPGVFTDIEQYQFLYKAML 1385
Cdd:cd14540    155 TLVHCSAGVGRTGVVILADLMLYCLDHNEELDIPRVLALLRHQRMLLVQTLAQYKFVYNVLI 216
PHA02742 PHA02742
protein tyrosine phosphatase; Provisional
 1127-1391 5.99e-19

protein tyrosine phosphatase; Provisional


Pssm-ID: 165109 [Multi-domain]  Cd Length: 303  Bit Score: 89.29  E-value: 5.99e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823416726 1127 LEKQFKLVTQCNAKYvECFSAQKDCNKEKNRNSSVVPSERARVGLAPLPGmkGTDYINASYIMGYYRSNEFIITQHPLPH 1206
Cdd:PHA02742    28 LKEEHEHIMQEIVAF-SCNESLELKNMKKCRYPDAPCFDRNRVILKIEDG--GDDFINASYVDGHNAKGRFICTQAPLEE 104

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823416726 1207 TTKDFWRMIWDHNAQIIVMLP----DNQslaEDEFVYWPSREESMNCEA-FTV-TLISKD-------RLCLSNeeqiiih 1273
Cdd:PHA02742   105 TALDFWQAIFQDQVRVIVMITkimeDGK---EACYPYWMPHERGKATHGeFKIkTKKIKSfrnyavtNLCLTD------- 174

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823416726 1274 dfileaTQDDYVLEVRHFQCPKWPNPDAP--ISSTFELINVIKEEALTRD-----------GPTIVHDEYGAVSAGTLCA 1340
Cdd:PHA02742   175 ------TNTGASLDIKHFAYEDWPHGGLPrdPNKFLDFVLAVREADLKADvdikgenivkePPILVHCSAGLDRAGAFCA 248

                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1823416726 1341 LtTLSQQLENENA-VDVFQVAKMINLMRPGVFTDIEQYQFLYKAML---SLVSTK 1391
Cdd:PHA02742   249 I-DICISKYNERAiIPLLSIVRDLRKQRHNCLSLPQQYIFCYFIVLifaKLMADK 302
PHA02740 PHA02740
protein tyrosine phosphatase; Provisional
 846-1093 1.82e-17

protein tyrosine phosphatase; Provisional


Pssm-ID: 165107 [Multi-domain]  Cd Length: 298  Bit Score: 84.63  E-value: 1.82e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823416726  846 SNHPDNKHK--NRYINILAYDHSRVKLRplpgKDSKhsdYINANYVDGYNKAKAYIATQGPLKSTFEDFWRMIWEQNTGI 923
Cdd:PHA02740    46 CAQAENKAKdeNLALHITRLLHRRIKLF----NDEK---VLDARFVDGYDFEQKFICIINLCEDACDKFLQALSDNKVQI 118

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823416726  924 IVMITNLVEKgrrKC-DQYWPTENS--EEYGNI-IVTLK-STNVHACYTVRRFTirntkMKKGQkgnpkgrqnERTVIQY 998
Cdd:PHA02740   119 IVLISRHADK---KCfNQFWSLKEGcvITSDKFqIETLEiIIKPHFNLTLLSLT-----DKFGQ---------AQKISHF 181

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823416726  999 HYTQWPDMGVPEYALPVLTF----------VRRSSAARtpDMGPVVVHCSAGVGRTGTYIVIDSMLQQIKDKSTVNVLGF 1068
Cdd:PHA02740   182 QYTAWPADGFSHDPDAFIDFfcniddlcadLEKHKADG--KIAPIIIDCIDGISSSAVFCVFDICATEFDKTGMLSIANA 259

                          250       260
                   ....*....|....*....|....*
gi 1823416726 1069 LKHIRTQRNYLVQTEEQYIFIHDAL 1093
Cdd:PHA02740   260 LKKVRQKKYGCMNCLDDYVFCYHLI 284
PTPc-N4 cd14601
catalytic domain of tyrosine-protein phosphatase non-receptor type 4; Tyrosine-protein ...
 1181-1385 1.04e-16

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: 1.04e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823416726 1181 DYINASYIMGYYRS----NEFIITQHPLPHTTKDFWRMIWDHNAQIIVMLPDNQSLAEDE-FVYWPSREESMNCEAFTVT 1255
Cdd:cd14601      1 DYINANYINMEIPSssiiNRYIACQGPLPNTCSDFWQMTWEQGSSMVVMLTTQVERGRVKcHQYWPEPSGSSSYGGFQVT 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823416726 1256 liskdrlCLSNE--EQIIIHDFILEATQDDYVLEVRHFQCPKWPNPDAPISST--FELINVIKEEALTRDGPTIVHDEYG 1331
Cdd:cd14601     81 -------CHSEEgnPAYVFREMTLTNLEKNESRPLTQIQYIAWPDHGVPDDSSdfLDFVCLVRNKRAGKDEPVVVHCSAG 153

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....
gi 1823416726 1332 AVSAGTLCALTTLSQQLENENAVDVFQVAKMINLMRPGVFTDIEQYQFLYKAML 1385
Cdd:cd14601    154 IGRTGVLITMETAMCLIECNQPVYPLDIVRTMRDQRAMMIQTPSQYRFVCEAIL 207
PTPc_plant_PTP1 cd17658
protein tyrosine phosphatase 1 from Arabidopsis thaliana and similar plant PTPs; Arabidopsis ...
 1182-1381 1.42e-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: 1.42e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823416726 1182 YINASYIMGYYRSN--EFIITQHPLPHTTKDFWRMIWDHNAQIIVMLP---DNQSLAEDEFVYWPSREESMNCEAFTVTL 1256
Cdd:cd17658      1 YINASLVETPASESlpKFIATQGPLPHTFEDFWEMVIQQRCPVIIMLTrlvDNYSTAKCADYFPAEENESREFGRISVTN 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823416726 1257 ISkdrlcLSNEEQIIIHDFiLEATQ---DDYVLEVRHFQCPKWPNPDAPiSSTFELINVIKEEALTRD--GPTIVHDEYG 1331
Cdd:cd17658     81 KK-----LKHSQHSITLRV-LEVQYiesEEPPLSVLHIQYPEWPDHGVP-KDTRSVRELLKRLYGIPPsaGPIVVHCSAG 153

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|..
gi 1823416726 1332 AVSAGTLCAL-TTLSQQLENE-NAVDVFQVAKMINLMRPGVFTDIEQYQFLY 1381
Cdd:cd17658    154 IGRTGAYCTIhNTIRRILEGDmSAVDLSKTVRKFRSQRIGMVQTQDQYIFCY 205
PTPc-N21 cd14598
catalytic domain of tyrosine-protein phosphatase non-receptor type 21; Tyrosine-protein ...
 1182-1388 2.59e-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: 2.59e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823416726 1182 YINASYIMGYYRSNE--FIITQHPLPHTTKDFWRMIWDHNAQIIVMLP-DNQSLAEDEFVYWP---SREESMNCEAFTVT 1255
Cdd:cd14598      1 YINASHIKVTVGGKEwdYIATQGPLQNTCQDFWQMVWEQGVAIIAMVTaEEEGGREKSFRYWPrlgSRHNTVTYGRFKIT 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823416726 1256 L-ISKDRLCLSNEEQIIIHdfiLEATQDDYVLevrHFQCPKWPNPDAP------ISSTFELINVIKEEALTRD-----GP 1323
Cdd:cd14598     81 TrFRTDSGCYATTGLKIKH---LLTGQERTVW---HLQYTDWPEHGCPedlkgfLSYLEEIQSVRRHTNSTIDpkspnPP 154

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1823416726 1324 TIVHDEYGAVSAGTLCALTTLSQQLENENAVDVFQVAKMINLMRPGVFTDIEQYQFLYKAMLSLV 1388
Cdd:cd14598    155 VLVHCSAGVGRTGVVILSEIMIACLEHNEMLDIPRVLDMLRQQRMMMVQTLSQYTFVYKVLIQFL 219
PTP_YopH-like cd14559
YopH and related bacterial protein tyrosine phosphatases; Yersinia outer protein H (YopH) ...
 855-1095 7.01e-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: 75.51  E-value: 7.01e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823416726  855 NRYINIlaydHSRVKLrpLPGKDskhsdyINANYVDGYNKAKAyIATQGPLKSTFEDFWRMIWEQNTGIIVMITNLVEKG 934
Cdd:cd14559      1 NRFTNI----QTRVST--PVGKN------LNANRVQIGNKNVA-IACQYPKNEQLEDHLKMLADNRTPCLVVLASNKDIQ 67

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823416726  935 RRKCDQYWptENSEEYGNIIVTLKSTNvhACYTVRRFTIRNTKMKKgqkgnpKGRQNERTVIQYHYTQWPDMG-VPEYAL 1013
Cdd:cd14559     68 RKGLPPYF--RQSGTYGSVTVKSKKTG--KDELVDGLKADMYNLKI------TDGNKTITIPVVHVTNWPDHTaISSEGL 137

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823416726 1014 PVLT--------------FVRRSSAARTPDMGPVVVHCSAGVGRTGTYIvidSMLQQIKDKSTVNVLGFLKHIRTQRN-Y 1078
Cdd:cd14559    138 KELAdlvnksaeekrnfyKSKGSSAINDKNKLLPVIHCRAGVGRTGQLA---AAMELNKSPNNLSVEDIVSDMRTSRNgK 214

                          250
                   ....*....|....*..
gi 1823416726 1079 LVQTEEQYifihDALLE 1095
Cdd:cd14559    215 MVQKDEQL----DTLKE 227
PLN02179 PLN02179
carbonic anhydrase
 17-272 4.98e-11

carbonic anhydrase


Pssm-ID: 177835  Cd Length: 235  Bit Score: 64.23  E-value: 4.98e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823416726   17 TSSVLHDVVCFPALTEGYVGSLHESRHGSS--VQIRRRKASGDPYWaysGTYGPeHWVTSSEkcgGSHQSPIDIMDH--- 91
Cdd:PLN02179     5 TKTIFFFVVFFIDLFFPNILLVYAREIGNKplFTYKQKTEKGPAEW---GKLNP-QWKVCST---GKYQSPIDLTDErvs 77

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823416726   92 LAHvgdeyqelqldgfdnessNKTWMKNTGKTVAILLK--DDYFVSGAGLPGRFKAEKVEFHWGQSNGSAGSEHSINGKR 169
Cdd:PLN02179    78 LIH------------------DQALSRHYKPAPAVIQSrgHDVMVSWKGDAGKITIHQTDYKLVQCHWHSPSEHTINGTS 139

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823416726  170 FPVEMQIYFynpddfdsfGTAVLENRVVGamaVFFQVSpRDNSALDPIIHGLKGVVHHEKET-FLDPFVLRellpTSLGS 248
Cdd:PLN02179   140 YDLELHMVH---------TSASGKTAVVG---VLYKLG-EPDEFLTKLLNGIKGVGKKEINLgIVDPRDIR----FETNN 202

                          250       260
                   ....*....|....*....|....
gi 1823416726  249 YYRYTGSLTTPPCSEIVEWIVFRK 272
Cdd:PLN02179   203 FYRYIGSLTIPPCTEGVIWTVVKR 226
PHA02740 PHA02740
protein tyrosine phosphatase; Provisional
 1183-1391 8.85e-11

protein tyrosine phosphatase; Provisional


Pssm-ID: 165107 [Multi-domain]  Cd Length: 298  Bit Score: 64.60  E-value: 8.85e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823416726 1183 INASYIMGYYRSNEFIITQHPLPHTTKDFWRMIWDHNAQIIVMLpdnQSLAEDE--FVYWPSREEsmnceaftvTLISKD 1260
Cdd:PHA02740    79 LDARFVDGYDFEQKFICIINLCEDACDKFLQALSDNKVQIIVLI---SRHADKKcfNQFWSLKEG---------CVITSD 146

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823416726 1261 RLCLSNEEQIIIHDFILE----ATQDDYVLEVRHFQCPKWP------NPDAPISSTFEL----INVIKEEALTRDGPTIV 1326
Cdd:PHA02740   147 KFQIETLEIIIKPHFNLTllslTDKFGQAQKISHFQYTAWPadgfshDPDAFIDFFCNIddlcADLEKHKADGKIAPIII 226

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1823416726 1327 HDEYGAVSAGTLCALTTLSQQLENENAVDVFQVAKMINLMRPGVFTDIEQYQFLYKAMLSLVSTK 1391
Cdd:PHA02740   227 DCIDGISSSAVFCVFDICATEFDKTGMLSIANALKKVRQKKYGCMNCLDDYVFCYHLIAAYLKEK 291
FN3 cd00063
Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein ...
 349-438 1.42e-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: 53.65  E-value: 1.42e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823416726  349 PPVNMKVQPVNRTALLVTWNQPETIyHPPIMNYMISYSWTKNEDEKEktFTKDSDKDLKAIISHVSPDILYLFRVQAVcR 428
Cdd:cd00063      3 PPTNLRVTDVTSTSVTLSWTPPEDD-GGPITGYVVEYREKGSGDWKE--VEVTPGSETSYTLTGLKPGTEYEFRVRAV-N 78

                           90
                   ....*....|
gi 1823416726  429 NEMRSDFSQT 438
Cdd:cd00063     79 GGGESPPSES 88
FN3 smart00060
Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, ...
 349-426 1.54e-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: 1.54e-08
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1823416726   349 PPVNMKVQPVNRTALLVTWNQPEtiyHPPIMNYMISYSWTKNEDEKEKTFTKDSDKDLKAIISHVSPDILYLFRVQAV 426
Cdd:smart00060    3 PPSNLRVTDVTSTSVTLSWEPPP---DDGITGYIVGYRVEYREEGSEWKEVNVTPSSTSYTLTGLKPGTEYEFRVRAV 77
PLN02202 PLN02202
carbonate dehydratase
 249-317 4.26e-08

carbonate dehydratase


Pssm-ID: 177853 [Multi-domain]  Cd Length: 284  Bit Score: 56.22  E-value: 4.26e-08
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1823416726  249 YYRYTGSLTTPPCSEIVEWIVFRKPVPISYHQLEAFYSIFTTEqqdhvksveyLRNNFRPQQRLNNRKV 317
Cdd:PLN02202   204 YFRYIGSLTTPPCSENVSWTILGKVRSMSKEQVELLRSPLDKS----------FKNNSRPCQPLNGRRV 262
CDC14 COG2453
Protein-tyrosine phosphatase [Signal transduction mechanisms];
996-1091 5.47e-08

Protein-tyrosine phosphatase [Signal transduction mechanisms];


Pssm-ID: 441989 [Multi-domain]  Cd Length: 140  Bit Score: 53.05  E-value: 5.47e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823416726  996 IQYHYTQWPDMGVPEYA--LPVLTFVRRSSAARtpdmGPVVVHCSAGVGRTGT----YIVIDSM-LQQIkdkstvnvlgf 1068
Cdd:COG2453     48 LEYLHLPIPDFGAPDDEqlQEAVDFIDEALREG----KKVLVHCRGGIGRTGTvaaaYLVLLGLsAEEA----------- 112

                           90       100
                   ....*....|....*....|...
gi 1823416726 1069 LKHIRTQRNYLVQTEEQYIFIHD 1091
Cdd:COG2453    113 LARVRAARPGAVETPAQRAFLER 135
fn3 pfam00041
Fibronectin type III domain;
349-426 1.37e-07

Fibronectin type III domain;


Pssm-ID: 394996 [Multi-domain]  Cd Length: 85  Bit Score: 50.49  E-value: 1.37e-07
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1823416726  349 PPVNMKVQPVNRTALLVTWNQPETiYHPPIMNYMISYsWTKNEDEKEKTFTKDSDKDlKAIISHVSPDILYLFRVQAV 426
Cdd:pfam00041    2 APSNLTVTDVTSTSLTVSWTPPPD-GNGPITGYEVEY-RPKNSGEPWNEITVPGTTT-SVTLTGLKPGTEYEVRVQAV 76
PTP_DSP_cys cd14494
cys-based protein tyrosine phosphatase and dual-specificity phosphatase superfamily; This ...
 1031-1091 7.86e-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: 7.86e-07
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1823416726 1031 GPVVVHCSAGVGRTGTYIVIDSMLQQIKDkstvnVLGFLKHIRTQR-NYLVQTEEQYIFIHD 1091
Cdd:cd14494     57 EPVLVHCKAGVGRTGTLVACYLVLLGGMS-----AEEAVRIVRLIRpGGIPQTIEQLDFLIK 113
CDKN3-like cd14505
cyclin-dependent kinase inhibitor 3 and similar proteins; This family is composed of ...
 996-1091 6.53e-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: 6.53e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823416726  996 IQYHYTQWPDMGVP---EYALPVLTFVR-RSSAARTpdmgpVVVHCSAGVGRTGTyiVIDSMLQQIKDKSTVNVLgfLKH 1071
Cdd:cd14505     73 ITWHHLPIPDGGVPsdiAQWQELLEELLsALENGKK-----VLIHCKGGLGRTGL--IAACLLLELGDTLDPEQA--IAA 143

                           90       100
                   ....*....|....*....|
gi 1823416726 1072 IRTQRNYLVQTEEQYIFIHD 1091
Cdd:cd14505    144 VRALRPGAIQTPKQENFLHQ 163
PTP_PTPDC1 cd14506
protein tyrosine phosphatase domain of PTP domain-containing protein 1; protein tyrosine ...
 996-1091 3.43e-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: 3.43e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823416726  996 IQYHYTQWPDMGVPEYALpVLTFVR-RSSAARTPdmGPVVVHCSAGVGRTGtyIVIDSMLQQIKDKSTVNVLGFlkhIRT 1074
Cdd:cd14506     77 IYFYNFGWKDYGVPSLTT-ILDIVKvMAFALQEG--GKVAVHCHAGLGRTG--VLIACYLVYALRMSADQAIRL---VRS 148

                           90
                   ....*....|....*..
gi 1823416726 1075 QRNYLVQTEEQYIFIHD 1091
Cdd:cd14506    149 KRPNSIQTRGQVLCVRE 165
DUSP23 cd14504
dual specificity phosphatase 23; Dual specificity phosphatase 23 (DUSP23), also known as ...
 996-1089 9.73e-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: 9.73e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823416726  996 IQYHYTQWPDMGVPEYALpVLTFVRRSSAARTPDmGPVVVHCSAGVGRTGT----YIVIDSMLQQIKDkstvnvlgfLKH 1071
Cdd:cd14504     50 LRYHHIPIEDYTPPTLEQ-IDEFLDIVEEANAKN-EAVLVHCLAGKGRTGTmlacYLVKTGKISAVDA---------INE 118

                           90
                   ....*....|....*...
gi 1823416726 1072 IRTQRNYLVQTEEQYIFI 1089
Cdd:cd14504    119 IRRIRPGSIETSEQEKFV 136
DSPc smart00195
Dual specificity phosphatase, catalytic domain;
1031-1073 4.45e-03

Dual specificity phosphatase, catalytic domain;


Pssm-ID: 214551 [Multi-domain]  Cd Length: 138  Bit Score: 38.80  E-value: 4.45e-03
                            10        20        30        40
                    ....*....|....*....|....*....|....*....|...
gi 1823416726  1031 GPVVVHCSAGVGRTGTYIVidSMLQQIKDKSTVNVLGFLKHIR 1073
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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