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Conserved domains on  [gi|1925147141|ref|XP_036813487|]
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receptor-type tyrosine-protein phosphatase zeta isoform X2 [Oncorhynchus mykiss]

Protein Classification

fibronectin type III domain-containing protein; tyrosine-protein phosphatase( domain architecture ID 12931150)

fibronectin type III (FN3) domain-containing protein may be involved in specific interactions with other molecules through its FN3 domain| tyrosine-protein phosphatase catalyzes the dephosphorylation of O-phosphotyrosine groups in phosphoproteins; has a C-terminal GNAT-family acetyltransferase domain

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
PTP_DSP_cys super family cl28904
cys-based protein tyrosine phosphatase and dual-specificity phosphatase superfamily; This ...
840-1105 8.18e-158

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.


The actual alignment was detected with superfamily member cd17667:

Pssm-ID: 475123 [Multi-domain]  Cd Length: 274  Bit Score: 476.84  E-value: 8.18e-158
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1925147141  840 FSKEFEEVQSCTVEMGITTDSSNHPDNKNKNRYINIMAYDHSRVKLL----EEGKGGDYINANFVDGFERTRAYIAAQGP 915
Cdd:cd17667      1 FSEDFEEVQRCTADMNITAEHSNHPDNKHKNRYINILAYDHSRVKLRplpgKDSKHSDYINANYVDGYNKAKAYIATQGP 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1925147141  916 LKSGTEDFWRMVWQENVGVIVMITNLLEKGRRKCDQYWPMENQEEYGHFLVTLKDTKTLAYYTLRTFTLRDTS----QKA 991
Cdd:cd17667     81 LKSTFEDFWRMIWEQNTGIIVMITNLVEKGRRKCDQYWPTENSEEYGNIIVTLKSTKIHACYTVRRFSIRNTKvkkgQKG 160
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1925147141  992 SQRGRCAERTVVQYHYTQWPDMGVPEYTLPVLSFVRASTQARTQDMGPVLVHCSAGVGRTGTYIVLDSMLQQIQDQGTVN 1071
Cdd:cd17667    161 NPKGRQNERTVIQYHYTQWPDMGVPEYALPVLTFVRRSSAARTPEMGPVLVHCSAGVGRTGTYIVIDSMLQQIKDKSTVN 240
                          250       260       270
                   ....*....|....*....|....*....|....
gi 1925147141 1072 ILGFLKHVRTQRNYLVQTEEQYVFIHDALVEAIV 1105
Cdd:cd17667    241 VLGFLKHIRTQRNYLVQTEEQYIFIHDALLEAIL 274
R5-PTP-2 cd14550
PTP-like domain of R5 subfamily receptor-type tyrosine-protein phosphatases, repeat 2; The R5 ...
1189-1391 2.82e-109

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: 343.53  E-value: 2.82e-109
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1925147141 1189 YINASYIMGYHKSREFILTQSPLPSTVSDFWRMVWDHNSQLIISLPDTHTAqregEESCAYWPSKDQPISCEGFIVSFSG 1268
Cdd:cd14550      1 YINASYLQGYRRSNEFIITQHPLEHTIKDFWQMIWDHNSQTIVMLTDNELN----EDEPIYWPTKEKPLECETFKVTLSG 76
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1925147141 1269 EDHMCLANEERLVVHDFLLEATQDNYVLEVRQYMSPCWPNPDSPVSGTFQLLNIITEDSRQREGTIVVHDRLGGSVAGLF 1348
Cdd:cd14550     77 EDHSCLSNEIRLIVRDFILESTQDDYVLEVRQFQCPSWPNPCSPIHTVFELINTVQEWAQQRDGPIVVHDRYGGVQAATF 156
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|...
gi 1925147141 1349 CALTTLAQQLEHQGSVDVYQVARMTNLMRPGVFNDMEQYQFMY 1391
Cdd:cd14550    157 CALTTLHQQLEHESSVDVYQVAKLYHLMRPGVFTSKEDYQFLY 199
alpha_CARP_receptor_like cd03122
Carbonic anhydrase alpha related protein, receptor_like subfamily. Carbonic anhydrase related ...
48-301 2.25e-102

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


:

Pssm-ID: 239396 [Multi-domain]  Cd Length: 253  Bit Score: 326.62  E-value: 2.25e-102
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1925147141   48 NQKIWGKRYPACNNAR-QSPIDIDETfTQVRVE-YQGLQLEGWEkNTPETTTINNDGNTVVLGLDG---EYYVSGGGLST 122
Cdd:cd03122      1 NPKHWAKKYPACGEGRqQSPIDIVED-TQVQRQgLQPLHFDGYE-ELTASTTLENTGKTVILRLEGnssDPFVSGGPLLG 78
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1925147141  123 RFRLGRMTFHWGRCNasSDGSEHSLNGLKFPLEMQILCYeSGLYQSIDDAVRDGGRIAALAVLFETSLDNNDNYNTILEG 202
Cdd:cd03122     79 RYKFSEITFHWGTCN--SDGSEHSIDGHKFPLEMQILHR-NTDFFDSFEAIKSPGGVLALAYLFELSHEDNPFLDPIIEG 155
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1925147141  203 VNSVNRFGKTGNVEPFSLLALLPNSTDKYYTYNGSLTSPPCSETVEWIVFKHTVPISETQLEVFCEVMTMQQAGyVMLMD 282
Cdd:cd03122    156 LRNVSRPGKEVELPPFPLSDLLPPFTDKYYSYEGSLTTPPCSETVEWIVFREPVPISSRQLEAFRELLTRRQDG-VMSGD 234
                          250
                   ....*....|....*....
gi 1925147141  283 YLQNNFREQQQQFLGQVFS 301
Cdd:cd03122    235 YLPNNGRPQQPLGSRTVFS 253
fn3 pfam00041
Fibronectin type III domain;
316-404 5.99e-12

Fibronectin type III domain;


:

Pssm-ID: 394996 [Multi-domain]  Cd Length: 85  Bit Score: 62.82  E-value: 5.99e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1925147141  316 SEPQNMQADAQNETTIMVMWERPRVVyDTTIDWYSVTYQRlQDQNQPKHEYRTDGDQDvGAIIPGLLSNSSYVVQVVAVC 395
Cdd:pfam00041    1 SAPSNLTVTDVTSTSLTVSWTPPPDG-NGPITGYEVEYRP-KNSGEPWNEITVPGTTT-SVTLTGLKPGTEYEVRVQAVN 77

                   ....*....
gi 1925147141  396 TNGLtGRWS 404
Cdd:pfam00041   78 GGGE-GPPS 85
 
Name Accession Description Interval E-value
R-PTPc-G-1 cd17667
catalytic domain of receptor-type tyrosine-protein phosphatase G, repeat 1; Receptor-type ...
840-1105 8.18e-158

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: 476.84  E-value: 8.18e-158
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1925147141  840 FSKEFEEVQSCTVEMGITTDSSNHPDNKNKNRYINIMAYDHSRVKLL----EEGKGGDYINANFVDGFERTRAYIAAQGP 915
Cdd:cd17667      1 FSEDFEEVQRCTADMNITAEHSNHPDNKHKNRYINILAYDHSRVKLRplpgKDSKHSDYINANYVDGYNKAKAYIATQGP 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1925147141  916 LKSGTEDFWRMVWQENVGVIVMITNLLEKGRRKCDQYWPMENQEEYGHFLVTLKDTKTLAYYTLRTFTLRDTS----QKA 991
Cdd:cd17667     81 LKSTFEDFWRMIWEQNTGIIVMITNLVEKGRRKCDQYWPTENSEEYGNIIVTLKSTKIHACYTVRRFSIRNTKvkkgQKG 160
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1925147141  992 SQRGRCAERTVVQYHYTQWPDMGVPEYTLPVLSFVRASTQARTQDMGPVLVHCSAGVGRTGTYIVLDSMLQQIQDQGTVN 1071
Cdd:cd17667    161 NPKGRQNERTVIQYHYTQWPDMGVPEYALPVLTFVRRSSAARTPEMGPVLVHCSAGVGRTGTYIVIDSMLQQIKDKSTVN 240
                          250       260       270
                   ....*....|....*....|....*....|....
gi 1925147141 1072 ILGFLKHVRTQRNYLVQTEEQYVFIHDALVEAIV 1105
Cdd:cd17667    241 VLGFLKHIRTQRNYLVQTEEQYIFIHDALLEAIL 274
PTPc smart00194
Protein tyrosine phosphatase, catalytic domain;
840-1102 1.05e-112

Protein tyrosine phosphatase, catalytic domain;


Pssm-ID: 214550 [Multi-domain]  Cd Length: 259  Bit Score: 355.43  E-value: 1.05e-112
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1925147141   840 FSKEFEEVQSCTVEMgITTDSSNHPDNKNKNRYINIMAYDHSRVKL-LEEGKGGDYINANFVDGFERTRAYIAAQGPLKS 918
Cdd:smart00194    2 LEEEFEKLDRLKPDD-ESCTVAAFPENRDKNRYKDVLPYDHTRVKLkPPPGEGSDYINASYIDGPNGPKAYIATQGPLPS 80
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1925147141   919 GTEDFWRMVWQENVGVIVMITNLLEKGRRKCDQYWPMENQE--EYGHFLVTLKDTKTLAYYTLRTFTLRDTSQKASqrgr 996
Cdd:smart00194   81 TVEDFWRMVWEQKVTVIVMLTELVEKGREKCAQYWPDEEGEplTYGDITVTLKSVEKVDDYTIRTLEVTNTGCSET---- 156
                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1925147141   997 caeRTVVQYHYTQWPDMGVPEYTLPVLSFVRASTQARTQDMGPVLVHCSAGVGRTGTYIVLDSMLQQIQDQGTVNILGFL 1076
Cdd:smart00194  157 ---RTVTHYHYTNWPDHGVPESPESILDLIRAVRKSQSTSTGPIVVHCSAGVGRTGTFIAIDILLQQLEAGKEVDIFEIV 233
                           250       260
                    ....*....|....*....|....*.
gi 1925147141  1077 KHVRTQRNYLVQTEEQYVFIHDALVE 1102
Cdd:smart00194  234 KELRSQRPGMVQTEEQYIFLYRAILE 259
R5-PTP-2 cd14550
PTP-like domain of R5 subfamily receptor-type tyrosine-protein phosphatases, repeat 2; The R5 ...
1189-1391 2.82e-109

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: 343.53  E-value: 2.82e-109
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1925147141 1189 YINASYIMGYHKSREFILTQSPLPSTVSDFWRMVWDHNSQLIISLPDTHTAqregEESCAYWPSKDQPISCEGFIVSFSG 1268
Cdd:cd14550      1 YINASYLQGYRRSNEFIITQHPLEHTIKDFWQMIWDHNSQTIVMLTDNELN----EDEPIYWPTKEKPLECETFKVTLSG 76
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1925147141 1269 EDHMCLANEERLVVHDFLLEATQDNYVLEVRQYMSPCWPNPDSPVSGTFQLLNIITEDSRQREGTIVVHDRLGGSVAGLF 1348
Cdd:cd14550     77 EDHSCLSNEIRLIVRDFILESTQDDYVLEVRQFQCPSWPNPCSPIHTVFELINTVQEWAQQRDGPIVVHDRYGGVQAATF 156
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|...
gi 1925147141 1349 CALTTLAQQLEHQGSVDVYQVARMTNLMRPGVFNDMEQYQFMY 1391
Cdd:cd14550    157 CALTTLHQQLEHESSVDVYQVAKLYHLMRPGVFTSKEDYQFLY 199
Y_phosphatase pfam00102
Protein-tyrosine phosphatase;
866-1102 2.51e-106

Protein-tyrosine phosphatase;


Pssm-ID: 459674 [Multi-domain]  Cd Length: 234  Bit Score: 336.91  E-value: 2.51e-106
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1925147141  866 NKNKNRYINIMAYDHSRVKLLEEGKGGDYINANFVDGFERTRAYIAAQGPLKSGTEDFWRMVWQENVGVIVMITNLLEKG 945
Cdd:pfam00102    1 NLEKNRYKDVLPYDHTRVKLTGDPGPSDYINASYIDGYKKPKKYIATQGPLPNTVEDFWRMVWEEKVTIIVMLTELEEKG 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1925147141  946 RRKCDQYWP--MENQEEYGHFLVTLKDTKT-LAYYTLRTFTLRDTSQKasqrgrcAERTVVQYHYTQWPDMGVPEYTLPV 1022
Cdd:pfam00102   81 REKCAQYWPeeEGESLEYGDFTVTLKKEKEdEKDYTVRTLEVSNGGSE-------ETRTVKHFHYTGWPDHGVPESPNSL 153
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1925147141 1023 LSFVRA-STQARTQDMGPVLVHCSAGVGRTGTYIVLDSMLQQIQDQGTVNILGFLKHVRTQRNYLVQTEEQYVFIHDALV 1101
Cdd:pfam00102  154 LDLLRKvRKSSLDGRSGPIVVHCSAGIGRTGTFIAIDIALQQLEAEGEVDIFQIVKELRSQRPGMVQTLEQYIFLYDAIL 233

                   .
gi 1925147141 1102 E 1102
Cdd:pfam00102  234 E 234
alpha_CARP_receptor_like cd03122
Carbonic anhydrase alpha related protein, receptor_like subfamily. Carbonic anhydrase related ...
48-301 2.25e-102

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


Pssm-ID: 239396 [Multi-domain]  Cd Length: 253  Bit Score: 326.62  E-value: 2.25e-102
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1925147141   48 NQKIWGKRYPACNNAR-QSPIDIDETfTQVRVE-YQGLQLEGWEkNTPETTTINNDGNTVVLGLDG---EYYVSGGGLST 122
Cdd:cd03122      1 NPKHWAKKYPACGEGRqQSPIDIVED-TQVQRQgLQPLHFDGYE-ELTASTTLENTGKTVILRLEGnssDPFVSGGPLLG 78
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1925147141  123 RFRLGRMTFHWGRCNasSDGSEHSLNGLKFPLEMQILCYeSGLYQSIDDAVRDGGRIAALAVLFETSLDNNDNYNTILEG 202
Cdd:cd03122     79 RYKFSEITFHWGTCN--SDGSEHSIDGHKFPLEMQILHR-NTDFFDSFEAIKSPGGVLALAYLFELSHEDNPFLDPIIEG 155
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1925147141  203 VNSVNRFGKTGNVEPFSLLALLPNSTDKYYTYNGSLTSPPCSETVEWIVFKHTVPISETQLEVFCEVMTMQQAGyVMLMD 282
Cdd:cd03122    156 LRNVSRPGKEVELPPFPLSDLLPPFTDKYYSYEGSLTTPPCSETVEWIVFREPVPISSRQLEAFRELLTRRQDG-VMSGD 234
                          250
                   ....*....|....*....
gi 1925147141  283 YLQNNFREQQQQFLGQVFS 301
Cdd:cd03122    235 YLPNNGRPQQPLGSRTVFS 253
Carb_anhydrase pfam00194
Eukaryotic-type carbonic anhydrase;
52-303 2.58e-85

Eukaryotic-type carbonic anhydrase;


Pssm-ID: 459707 [Multi-domain]  Cd Length: 252  Bit Score: 278.77  E-value: 2.58e-85
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1925147141   52 WGKRYPACNNARQSPIDIDETFTQVRVEYQGLQLEGWEkNTPETTTINNDGNTVVLGLDGEY--YVSGGGLSTRFRLGRM 129
Cdd:pfam00194    6 WGKVYPSCGGKRQSPINIDTRKVRYDPSLPPLTFQGYD-VPPGKNTLTNNGHTVQVSLDDGDpsTISGGPLATRYRLVQF 84
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1925147141  130 TFHWGRCNasSDGSEHSLNGLKFPLEMQILCYESGlYQSIDDAVRDGGRIAALAVLFETSLDNNDNYNTILEGVNSVNRF 209
Cdd:pfam00194   85 HFHWGSTD--SRGSEHTIDGKRYPAELHIVHYNSK-YKSFDEAAKHPDGLAVLGVFFEVGDENNPYLQPIVSALDNIKYK 161
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1925147141  210 GKTGNVEPFSLLALLPNSTDKYYTYNGSLTSPPCSETVEWIVFKHTVPISETQLEVFCEVMTMQQAGYvmlMDYLQNNFR 289
Cdd:pfam00194  162 GKSVLLPPFDLSDLLPEDLTSYYTYNGSLTTPPCSESVTWIVFKEPISISEEQLEAFRTLLFSDGGEE---PRPLVNNFR 238
                          250
                   ....*....|....
gi 1925147141  290 EQQQQFLGQVFSSY 303
Cdd:pfam00194  239 PTQPLNGRVVFASF 252
Carb_anhydrase smart01057
Eukaryotic-type carbonic anhydrase; Carbonic anhydrases are zinc metalloenzymes which catalyse ...
41-292 6.34e-81

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: 266.49  E-value: 6.34e-81
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1925147141    41 WSYTGQLNQKIWGK-RYPACNNARQSPIDIDETFTQVRVEYQGLQlegWEKNTPETTTINNDGNTVVLGLDGE-YYVSGG 118
Cdd:smart01057    1 WGYEGKNGPEHWGKlDPPFCGGKRQSPIDIVTAEAQYDPSLKPLK---LSYDQPTAKRILNNGHTVQVNFDDDgSTLSGG 77
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1925147141   119 GLSTRFRLGRMTFHWGRCNasSDGSEHSLNGLKFPLEMQILCYESGlyQSIDDAVRDGGRIAALAVLFETSLDNNDNYNT 198
Cdd:smart01057   78 PLPGRYRLKQFHFHWGGSD--SEGSEHTIDGKRFPLELHLVHYNSK--GSFSEAVSKPGGLAVVAVFFKVGAEENPALQA 153
                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1925147141   199 ILEGVNSVNRFGKTGNVEPFSLLALLPNSTDKYYTYNGSLTSPPCSETVEWIVFKHTVPISETQLEVFCEVMTMQQAgyv 278
Cdd:smart01057  154 ILDHLPLIKYKGQETELTPFDLSSLLPASTRHYYTYNGSLTTPPCSEGVTWIVFKEPITISTEQLEKFRTLLPMEGN--- 230
                           250
                    ....*....|....
gi 1925147141   279 mlmDYLQNNFREQQ 292
Cdd:smart01057  231 ---EPLVNNARPLQ 241
PTPc smart00194
Protein tyrosine phosphatase, catalytic domain;
1154-1395 1.38e-61

Protein tyrosine phosphatase, catalytic domain;


Pssm-ID: 214550 [Multi-domain]  Cd Length: 259  Bit Score: 211.36  E-value: 1.38e-61
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1925147141  1154 ALREGNDDKNRTSSLMPVERSRVCLScPVEGESSDYINASYIMGYHKSREFILTQSPLPSTVSDFWRMVWDHNSQLIISL 1233
Cdd:smart00194   22 AAFPENRDKNRYKDVLPYDHTRVKLK-PPPGEGSDYINASYIDGPNGPKAYIATQGPLPSTVEDFWRMVWEQKVTVIVML 100
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1925147141  1234 PDTHTAQREGEEScaYWPSK-DQPISCEGFIVSFSGEDHMclaneERLVVHDFLLEATQDNYVLEVRQYMSPCWP---NP 1309
Cdd:smart00194  101 TELVEKGREKCAQ--YWPDEeGEPLTYGDITVTLKSVEKV-----DDYTIRTLEVTNTGCSETRTVTHYHYTNWPdhgVP 173
                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1925147141  1310 DSPvSGTFQLLNIITEDSRQREGTIVVHDRLGGSVAGLFCALTTLAQQLEHQGSVDVYQVARMTNLMRPGVFNDMEQYQF 1389
Cdd:smart00194  174 ESP-ESILDLIRAVRKSQSTSTGPIVVHCSAGVGRTGTFIAIDILLQQLEAGKEVDIFEIVKELRSQRPGMVQTEEQYIF 252

                    ....*.
gi 1925147141  1390 MYRAVL 1395
Cdd:smart00194  253 LYRAIL 258
Y_phosphatase pfam00102
Protein-tyrosine phosphatase;
1159-1395 1.27e-59

Protein-tyrosine phosphatase;


Pssm-ID: 459674 [Multi-domain]  Cd Length: 234  Bit Score: 204.78  E-value: 1.27e-59
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1925147141 1159 NDDKNRTSSLMPVERSRVCLscPVEGESSDYINASYIMGYHKSREFILTQSPLPSTVSDFWRMVWDHNSQLIISLpdthT 1238
Cdd:pfam00102    1 NLEKNRYKDVLPYDHTRVKL--TGDPGPSDYINASYIDGYKKPKKYIATQGPLPNTVEDFWRMVWEEKVTIIVML----T 74
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1925147141 1239 AQRE-GEESCA-YWPSK-DQPISCEGFIVSFSGEDhmclANEERLVVHDFLLEATQDNYVLEVRQYMSPCWPNPDSPVSg 1315
Cdd:pfam00102   75 ELEEkGREKCAqYWPEEeGESLEYGDFTVTLKKEK----EDEKDYTVRTLEVSNGGSEETRTVKHFHYTGWPDHGVPES- 149
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1925147141 1316 TFQLLNII----TEDSRQREGTIVVHDRLGGSVAGLFCALTTLAQQLEHQGSVDVYQVARMTNLMRPGVFNDMEQYQFMY 1391
Cdd:pfam00102  150 PNSLLDLLrkvrKSSLDGRSGPIVVHCSAGIGRTGTFIAIDIALQQLEAEGEVDIFQIVKELRSQRPGMVQTLEQYIFLY 229

                   ....
gi 1925147141 1392 RAVL 1395
Cdd:pfam00102  230 DAIL 233
PHA02738 PHA02738
hypothetical protein; Provisional
819-1116 1.64e-54

hypothetical protein; Provisional


Pssm-ID: 222923 [Multi-domain]  Cd Length: 320  Bit Score: 193.22  E-value: 1.64e-54
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1925147141  819 HEALSVKQFVKHVAELHQTNTFSKEFEEVQSCTVEMGITTDSSNhpdnKNKNRYINIMAYDHSRVKLLEEGKGGDYINAN 898
Cdd:PHA02738     6 FRELKYAEFLALMEKSDCEEVITREHQKVISEKVDGTFNAEKKN----RKLNRYLDAVCFDHSRVILPAERNRGDYINAN 81
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1925147141  899 FVDGFERTRAYIAAQGPLKSGTEDFWRMVWQENVGVIVMITNLLEKGRRKCDQYWPMENQEE--YGHFLVTLKDTKTLAY 976
Cdd:PHA02738    82 YVDGFEYKKKFICGQAPTRQTCYDFYRMLWMEHVQIIVMLCKKKENGREKCFPYWSDVEQGSirFGKFKITTTQVETHPH 161
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1925147141  977 YTLRTFTLRDtsqkasqrGRCAERTVVQYHYTQWPDMGVPEYTLPVLSFVRASTQARTQ------DMG-------PVLVH 1043
Cdd:PHA02738   162 YVKSTLLLTD--------GTSATQTVTHFNFTAWPDHDVPKNTSEFLNFVLEVRQCQKElaqeslQIGhnrlqppPIVVH 233
                          250       260       270       280       290       300       310
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1925147141 1044 CSAGVGRTGTYIVLDSMLQQIQDQGTVNILGFLKHVRTQRNYLVQTEEQYVFIHDALVEAIVSRDTLVTSDLV 1116
Cdd:PHA02738   234 CNAGLGRTPCYCVVDISISRFDACATVSIPSIVSSIRNQRYYSLFIPFQYFFCYRAVKRYVNLTVNKVSKKLI 306
COG5599 COG5599
Protein tyrosine phosphatase [Signal transduction mechanisms];
842-1096 4.79e-42

Protein tyrosine phosphatase [Signal transduction mechanisms];


Pssm-ID: 444335 [Multi-domain]  Cd Length: 282  Bit Score: 156.02  E-value: 4.79e-42
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1925147141  842 KEFEEVQSCTVEMGITTDSSNHPDNKN---KNRYINIMAYDHSRVklleeGKGGDYINANFVDGFERTRaYIAAQGPLKS 918
Cdd:COG5599     15 KINSRLSTLTNELAPSHNDPQYLQNINgspLNRFRDIQPYKETAL-----RANLGYLNANYIQVIGNHR-YIATQYPLEE 88
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1925147141  919 GTEDFWRMVWQENVGVIVMITNLLE--KGRRKCDQYWPMenQEEYGHFLV--TLKDTKTLA-YYTLRTFTL--RDTSQKa 991
Cdd:COG5599     89 QLEDFFQMLFDNNTPVLVVLASDDEisKPKVKMPVYFRQ--DGEYGKYEVssELTESIQLRdGIEARTYVLtiKGTGQK- 165
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1925147141  992 sqrgrcaERTVVQYHYTQWPDMGVP--EYTLPVLSFVRASTQARTQDMGPVLVHCSAGVGRTGTYIVLDSMLQQIQD--Q 1067
Cdd:COG5599    166 -------KIEIPVLHVKNWPDHGAIsaEALKNLADLIDKKEKIKDPDKLLPVVHCRAGVGRTGTLIACLALSKSINAlvQ 238
                          250       260       270
                   ....*....|....*....|....*....|
gi 1925147141 1068 GTVNILGFLKHVRTQRNY-LVQTEEQYVFI 1096
Cdd:COG5599    239 ITLSVEEIVIDMRTSRNGgMVQTSEQLDVL 268
Cah COG3338
Carbonic anhydrase [Inorganic ion transport and metabolism];
37-266 2.22e-33

Carbonic anhydrase [Inorganic ion transport and metabolism];


Pssm-ID: 442567 [Multi-domain]  Cd Length: 247  Bit Score: 129.62  E-value: 2.22e-33
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1925147141   37 DDIDWSYTGQLNQKIWGK---RYPACNN-ARQSPIDIDETftqVRVEYQGLQLEgwekNTPETTTINNDGNTVVLGLDGE 112
Cdd:COG3338     24 SAPHWSYEGETGPEHWGElspEFATCATgKNQSPIDIRTA---IKADLPPLKFD----YKPTPLEIVNNGHTIQVNVDPG 96
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1925147141  113 YYVSGGGlsTRFRLGRMTFHwgrcnassDGSEHSLNGLKFPLEMQiLCYESglyqsiddavrDGGRIAALAVLFETSlDN 192
Cdd:COG3338     97 STLTVDG--KRYELKQFHFH--------TPSEHTINGKSYPMEAH-LVHKD-----------ADGELAVVGVLFEEG-AE 153
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1925147141  193 NDNYNTILEGVNSVNRFGKTGNVePFSLLALLPNSTDkYYTYNGSLTSPPCSETVEWIVFKHTVPISETQLEVF 266
Cdd:COG3338    154 NPALAKLWANLPLEAGEEVALDA-TIDLNDLLPEDRS-YYRYSGSLTTPPCSEGVLWIVLKQPITVSAEQIEAF 225
PHA02746 PHA02746
protein tyrosine phosphatase; Provisional
1155-1394 2.64e-24

protein tyrosine phosphatase; Provisional


Pssm-ID: 165113 [Multi-domain]  Cd Length: 323  Bit Score: 105.50  E-value: 2.64e-24
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1925147141 1155 LREGNDDKNRTSSLMPVERSRVCLSC-------------------PVEGESSDYINASYIMGYHKSREFILTQSPLPSTV 1215
Cdd:PHA02746    47 LKKENLKKNRFHDIPCWDHSRVVINAheslkmfdvgdsdgkkievTSEDNAENYIHANFVDGFKEANKFICAQGPKEDTS 126
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1925147141 1216 SDFWRMVWDHNSQLIISLPDThtaQREGEESCAYWPS-KDQPISCEGFIVSFSGEDHMCLANEERLVVHDFLLEATQdny 1294
Cdd:PHA02746   127 EDFFKLISEHESQVIVSLTDI---DDDDEKCFELWTKeEDSELAFGRFVAKILDIIEELSFTKTRLMITDKISDTSR--- 200
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1925147141 1295 vlEVRQYMSPCWPNPDSPvSGTFQLLNIIT-------------EDSRQREGTIVVHDRLGGSVAGLFCALTTLAQQLEHQ 1361
Cdd:PHA02746   201 --EIHHFWFPDWPDNGIP-TGMAEFLELINkvneeqaelikqaDNDPQTLGPIVVHCSAGIGRAGTFCAIDNALEQLEKE 277
                          250       260       270
                   ....*....|....*....|....*....|...
gi 1925147141 1362 GSVDVYQVARMTNLMRPGVFNDMEQYQFMYRAV 1394
Cdd:PHA02746   278 KEVCLGEIVLKIRKQRHSSVFLPEQYAFCYKAL 310
PLN02179 PLN02179
carbonic anhydrase
52-256 3.50e-12

carbonic anhydrase


Pssm-ID: 177835  Cd Length: 235  Bit Score: 67.70  E-value: 3.50e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1925147141   52 WGKRYP---ACNNAR-QSPIDIdetfTQVRVEYqgLQLEGWEKN-TPETTTINNDGNTVVLGLDGEyyvsGGGLS---TR 123
Cdd:PLN02179    50 WGKLNPqwkVCSTGKyQSPIDL----TDERVSL--IHDQALSRHyKPAPAVIQSRGHDVMVSWKGD----AGKITihqTD 119
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1925147141  124 FRLgrMTFHWgrcnasSDGSEHSLNGLKFPLEMQILCYESGlyqsiddavrdgGRIAALAVLFEtsLDNNDNYNT-ILEG 202
Cdd:PLN02179   120 YKL--VQCHW------HSPSEHTINGTSYDLELHMVHTSAS------------GKTAVVGVLYK--LGEPDEFLTkLLNG 177
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1925147141  203 VNSV-NRFGKTGNVEPFSLLAllpnSTDKYYTYNGSLTSPPCSETVEWIVFKHTV 256
Cdd:PLN02179   178 IKGVgKKEINLGIVDPRDIRF----ETNNFYRYIGSLTIPPCTEGVIWTVVKRVV 228
fn3 pfam00041
Fibronectin type III domain;
316-404 5.99e-12

Fibronectin type III domain;


Pssm-ID: 394996 [Multi-domain]  Cd Length: 85  Bit Score: 62.82  E-value: 5.99e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1925147141  316 SEPQNMQADAQNETTIMVMWERPRVVyDTTIDWYSVTYQRlQDQNQPKHEYRTDGDQDvGAIIPGLLSNSSYVVQVVAVC 395
Cdd:pfam00041    1 SAPSNLTVTDVTSTSLTVSWTPPPDG-NGPITGYEVEYRP-KNSGEPWNEITVPGTTT-SVTLTGLKPGTEYEVRVQAVN 77

                   ....*....
gi 1925147141  396 TNGLtGRWS 404
Cdd:pfam00041   78 GGGE-GPPS 85
FN3 cd00063
Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein ...
316-409 5.29e-07

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


Pssm-ID: 238020 [Multi-domain]  Cd Length: 93  Bit Score: 49.03  E-value: 5.29e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1925147141  316 SEPQNMQADAQNETTIMVMWERPRVvYDTTIDWYSVTYQRLQDQNQpkHEYRTDGDQDVGAIIPGLLSNSSYVVQVVAVC 395
Cdd:cd00063      2 SPPTNLRVTDVTSTSVTLSWTPPED-DGGPITGYVVEYREKGSGDW--KEVEVTPGSETSYTLTGLKPGTEYEFRVRAVN 78
                           90
                   ....*....|....
gi 1925147141  396 TNGlTGRWSDQIIV 409
Cdd:cd00063     79 GGG-ESPPSESVTV 91
FN3 smart00060
Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, ...
316-398 2.79e-06

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: 46.84  E-value: 2.79e-06
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1925147141   316 SEPQNMQADAQNETTIMVMWERPRvvyDTTIDWYSVTYQRLQDQNQPKHEYRTDGDQDVGAIIPGLLSNSSYVVQVVAVC 395
Cdd:smart00060    2 SPPSNLRVTDVTSTSVTLSWEPPP---DDGITGYIVGYRVEYREEGSEWKEVNVTPSSTSYTLTGLKPGTEYEFRVRAVN 78

                    ...
gi 1925147141   396 TNG 398
Cdd:smart00060   79 GAG 81
 
Name Accession Description Interval E-value
R-PTPc-G-1 cd17667
catalytic domain of receptor-type tyrosine-protein phosphatase G, repeat 1; Receptor-type ...
840-1105 8.18e-158

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: 476.84  E-value: 8.18e-158
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1925147141  840 FSKEFEEVQSCTVEMGITTDSSNHPDNKNKNRYINIMAYDHSRVKLL----EEGKGGDYINANFVDGFERTRAYIAAQGP 915
Cdd:cd17667      1 FSEDFEEVQRCTADMNITAEHSNHPDNKHKNRYINILAYDHSRVKLRplpgKDSKHSDYINANYVDGYNKAKAYIATQGP 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1925147141  916 LKSGTEDFWRMVWQENVGVIVMITNLLEKGRRKCDQYWPMENQEEYGHFLVTLKDTKTLAYYTLRTFTLRDTS----QKA 991
Cdd:cd17667     81 LKSTFEDFWRMIWEQNTGIIVMITNLVEKGRRKCDQYWPTENSEEYGNIIVTLKSTKIHACYTVRRFSIRNTKvkkgQKG 160
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1925147141  992 SQRGRCAERTVVQYHYTQWPDMGVPEYTLPVLSFVRASTQARTQDMGPVLVHCSAGVGRTGTYIVLDSMLQQIQDQGTVN 1071
Cdd:cd17667    161 NPKGRQNERTVIQYHYTQWPDMGVPEYALPVLTFVRRSSAARTPEMGPVLVHCSAGVGRTGTYIVIDSMLQQIKDKSTVN 240
                          250       260       270
                   ....*....|....*....|....*....|....
gi 1925147141 1072 ILGFLKHVRTQRNYLVQTEEQYVFIHDALVEAIV 1105
Cdd:cd17667    241 VLGFLKHIRTQRNYLVQTEEQYIFIHDALLEAIL 274
R-PTPc-Z-1 cd17668
catalytic domain of receptor-type tyrosine-protein phosphatase Z, repeat 1; Receptor-type ...
894-1101 1.59e-132

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: 406.67  E-value: 1.59e-132
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1925147141  894 YINANFVDGFERTRAYIAAQGPLKSGTEDFWRMVWQENVGVIVMITNLLEKGRRKCDQYWPMENQEEYGHFLVTLKDTKT 973
Cdd:cd17668      1 YINANYVDGYNKPKAYIAAQGPLKSTAEDFWRMIWEHNVEVIVMITNLVEKGRRKCDQYWPADGSEEYGNFLVTQKSVQV 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1925147141  974 LAYYTLRTFTLRDTS-QKASQRGRCAERTVVQYHYTQWPDMGVPEYTLPVLSFVRASTQARTQDMGPVLVHCSAGVGRTG 1052
Cdd:cd17668     81 LAYYTVRNFTLRNTKiKKGSQKGRPSGRVVTQYHYTQWPDMGVPEYTLPVLTFVRKASYAKRHAVGPVVVHCSAGVGRTG 160
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*....
gi 1925147141 1053 TYIVLDSMLQQIQDQGTVNILGFLKHVRTQRNYLVQTEEQYVFIHDALV 1101
Cdd:cd17668    161 TYIVLDSMLQQIQHEGTVNIFGFLKHIRSQRNYLVQTEEQYVFIHDALV 209
R5-PTPc-1 cd14549
catalytic domain of R5 subfamily receptor-type tyrosine-protein phosphatases, repeat 1; The R5 ...
894-1098 9.74e-129

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: 396.34  E-value: 9.74e-129
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1925147141  894 YINANFVDGFERTRAYIAAQGPLKSGTEDFWRMVWQENVGVIVMITNLLEKGRRKCDQYWPMENQEEYGHFLVTLKDTKT 973
Cdd:cd14549      1 YINANYVDGYNKARAYIATQGPLPSTFDDFWRMVWEQNSAIIVMITNLVERGRRKCDQYWPKEGTETYGNIQVTLLSTEV 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1925147141  974 LAYYTLRTFTLRDTSQKaSQRGRCAERTVVQYHYTQWPDMGVPEYTLPVLSFVRASTQARTQDMGPVLVHCSAGVGRTGT 1053
Cdd:cd14549     81 LATYTVRTFSLKNLKLK-KVKGRSSERVVYQYHYTQWPDHGVPDYTLPVLSFVRKSSAANPPGAGPIVVHCSAGVGRTGT 159
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*
gi 1925147141 1054 YIVLDSMLQQIQDQGTVNILGFLKHVRTQRNYLVQTEEQYVFIHD 1098
Cdd:cd14549    160 YIVIDSMLQQIQDKGTVNVFGFLKHIRTQRNYLVQTEEQYIFIHD 204
PTPc smart00194
Protein tyrosine phosphatase, catalytic domain;
840-1102 1.05e-112

Protein tyrosine phosphatase, catalytic domain;


Pssm-ID: 214550 [Multi-domain]  Cd Length: 259  Bit Score: 355.43  E-value: 1.05e-112
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1925147141   840 FSKEFEEVQSCTVEMgITTDSSNHPDNKNKNRYINIMAYDHSRVKL-LEEGKGGDYINANFVDGFERTRAYIAAQGPLKS 918
Cdd:smart00194    2 LEEEFEKLDRLKPDD-ESCTVAAFPENRDKNRYKDVLPYDHTRVKLkPPPGEGSDYINASYIDGPNGPKAYIATQGPLPS 80
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1925147141   919 GTEDFWRMVWQENVGVIVMITNLLEKGRRKCDQYWPMENQE--EYGHFLVTLKDTKTLAYYTLRTFTLRDTSQKASqrgr 996
Cdd:smart00194   81 TVEDFWRMVWEQKVTVIVMLTELVEKGREKCAQYWPDEEGEplTYGDITVTLKSVEKVDDYTIRTLEVTNTGCSET---- 156
                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1925147141   997 caeRTVVQYHYTQWPDMGVPEYTLPVLSFVRASTQARTQDMGPVLVHCSAGVGRTGTYIVLDSMLQQIQDQGTVNILGFL 1076
Cdd:smart00194  157 ---RTVTHYHYTNWPDHGVPESPESILDLIRAVRKSQSTSTGPIVVHCSAGVGRTGTFIAIDILLQQLEAGKEVDIFEIV 233
                           250       260
                    ....*....|....*....|....*.
gi 1925147141  1077 KHVRTQRNYLVQTEEQYVFIHDALVE 1102
Cdd:smart00194  234 KELRSQRPGMVQTEEQYIFLYRAILE 259
R5-PTP-2 cd14550
PTP-like domain of R5 subfamily receptor-type tyrosine-protein phosphatases, repeat 2; The R5 ...
1189-1391 2.82e-109

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: 343.53  E-value: 2.82e-109
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1925147141 1189 YINASYIMGYHKSREFILTQSPLPSTVSDFWRMVWDHNSQLIISLPDTHTAqregEESCAYWPSKDQPISCEGFIVSFSG 1268
Cdd:cd14550      1 YINASYLQGYRRSNEFIITQHPLEHTIKDFWQMIWDHNSQTIVMLTDNELN----EDEPIYWPTKEKPLECETFKVTLSG 76
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1925147141 1269 EDHMCLANEERLVVHDFLLEATQDNYVLEVRQYMSPCWPNPDSPVSGTFQLLNIITEDSRQREGTIVVHDRLGGSVAGLF 1348
Cdd:cd14550     77 EDHSCLSNEIRLIVRDFILESTQDDYVLEVRQFQCPSWPNPCSPIHTVFELINTVQEWAQQRDGPIVVHDRYGGVQAATF 156
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|...
gi 1925147141 1349 CALTTLAQQLEHQGSVDVYQVARMTNLMRPGVFNDMEQYQFMY 1391
Cdd:cd14550    157 CALTTLHQQLEHESSVDVYQVAKLYHLMRPGVFTSKEDYQFLY 199
R-PTP-Z-2 cd17669
catalytic domain of receptor-type tyrosine-protein phosphatase Z, repeat 2; Receptor-type ...
1189-1395 4.09e-107

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: 337.74  E-value: 4.09e-107
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1925147141 1189 YINASYIMGYHKSREFILTQSPLPSTVSDFWRMVWDHNSQLIISLPDThtaQREGEESCAYWPSKDQPISCEGFIVSFSG 1268
Cdd:cd17669      1 YINASYIMGYYQSNEFIITQHPLLHTIKDFWRMIWDHNAQLIVMLPDG---QNMAEDEFVYWPNKDEPINCETFKVTLIA 77
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1925147141 1269 EDHMCLANEERLVVHDFLLEATQDNYVLEVRQYMSPCWPNPDSPVSGTFQLLNIITEDSRQREGTIVVHDRLGGSVAGLF 1348
Cdd:cd17669     78 EEHKCLSNEEKLIIQDFILEATQDDYVLEVRHFQCPKWPNPDSPISKTFELISIIKEEAANRDGPMIVHDEHGGVTAGTF 157
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*..
gi 1925147141 1349 CALTTLAQQLEHQGSVDVYQVARMTNLMRPGVFNDMEQYQFMYRAVL 1395
Cdd:cd17669    158 CALTTLMHQLEKENSVDVYQVAKMINLMRPGVFTDIEQYQFLYKAIL 204
Y_phosphatase pfam00102
Protein-tyrosine phosphatase;
866-1102 2.51e-106

Protein-tyrosine phosphatase;


Pssm-ID: 459674 [Multi-domain]  Cd Length: 234  Bit Score: 336.91  E-value: 2.51e-106
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1925147141  866 NKNKNRYINIMAYDHSRVKLLEEGKGGDYINANFVDGFERTRAYIAAQGPLKSGTEDFWRMVWQENVGVIVMITNLLEKG 945
Cdd:pfam00102    1 NLEKNRYKDVLPYDHTRVKLTGDPGPSDYINASYIDGYKKPKKYIATQGPLPNTVEDFWRMVWEEKVTIIVMLTELEEKG 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1925147141  946 RRKCDQYWP--MENQEEYGHFLVTLKDTKT-LAYYTLRTFTLRDTSQKasqrgrcAERTVVQYHYTQWPDMGVPEYTLPV 1022
Cdd:pfam00102   81 REKCAQYWPeeEGESLEYGDFTVTLKKEKEdEKDYTVRTLEVSNGGSE-------ETRTVKHFHYTGWPDHGVPESPNSL 153
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1925147141 1023 LSFVRA-STQARTQDMGPVLVHCSAGVGRTGTYIVLDSMLQQIQDQGTVNILGFLKHVRTQRNYLVQTEEQYVFIHDALV 1101
Cdd:pfam00102  154 LDLLRKvRKSSLDGRSGPIVVHCSAGIGRTGTFIAIDIALQQLEAEGEVDIFQIVKELRSQRPGMVQTLEQYIFLYDAIL 233

                   .
gi 1925147141 1102 E 1102
Cdd:pfam00102  234 E 234
R-PTPc-LAR-1 cd14553
catalytic domain of LAR family receptor-type tyrosine-protein phosphatases, repeat 1; The LAR ...
866-1106 2.48e-104

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: 331.28  E-value: 2.48e-104
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1925147141  866 NKNKNRYINIMAYDHSRVKL--LEEGKGGDYINANFVDGFERTRAYIAAQGPLKSGTEDFWRMVWQENVGVIVMITNLLE 943
Cdd:cd14553      3 NKPKNRYANVIAYDHSRVILqpIEGVPGSDYINANYCDGYRKQNAYIATQGPLPETFGDFWRMVWEQRSATIVMMTKLEE 82
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1925147141  944 KGRRKCDQYWPMENQEEYGHFLVTLKDTKTLAYYTLRTFTLrdTSQKASQRgrcaeRTVVQYHYTQWPDMGVPEYTLPVL 1023
Cdd:cd14553     83 RSRVKCDQYWPTRGTETYGLIQVTLLDTVELATYTVRTFAL--HKNGSSEK-----REVRQFQFTAWPDHGVPEHPTPFL 155
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1925147141 1024 SFVRASTQARTQDMGPVLVHCSAGVGRTGTYIVLDSMLQQIQDQGTVNILGFLKHVRTQRNYLVQTEEQYVFIHDALVEA 1103
Cdd:cd14553    156 AFLRRVKACNPPDAGPIVVHCSAGVGRTGCFIVIDSMLERIKHEKTVDIYGHVTCLRAQRNYMVQTEDQYIFIHDALLEA 235

                   ...
gi 1925147141 1104 IVS 1106
Cdd:cd14553    236 VTC 238
alpha_CARP_receptor_like cd03122
Carbonic anhydrase alpha related protein, receptor_like subfamily. Carbonic anhydrase related ...
48-301 2.25e-102

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


Pssm-ID: 239396 [Multi-domain]  Cd Length: 253  Bit Score: 326.62  E-value: 2.25e-102
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1925147141   48 NQKIWGKRYPACNNAR-QSPIDIDETfTQVRVE-YQGLQLEGWEkNTPETTTINNDGNTVVLGLDG---EYYVSGGGLST 122
Cdd:cd03122      1 NPKHWAKKYPACGEGRqQSPIDIVED-TQVQRQgLQPLHFDGYE-ELTASTTLENTGKTVILRLEGnssDPFVSGGPLLG 78
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1925147141  123 RFRLGRMTFHWGRCNasSDGSEHSLNGLKFPLEMQILCYeSGLYQSIDDAVRDGGRIAALAVLFETSLDNNDNYNTILEG 202
Cdd:cd03122     79 RYKFSEITFHWGTCN--SDGSEHSIDGHKFPLEMQILHR-NTDFFDSFEAIKSPGGVLALAYLFELSHEDNPFLDPIIEG 155
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1925147141  203 VNSVNRFGKTGNVEPFSLLALLPNSTDKYYTYNGSLTSPPCSETVEWIVFKHTVPISETQLEVFCEVMTMQQAGyVMLMD 282
Cdd:cd03122    156 LRNVSRPGKEVELPPFPLSDLLPPFTDKYYSYEGSLTTPPCSETVEWIVFREPVPISSRQLEAFRELLTRRQDG-VMSGD 234
                          250
                   ....*....|....*....
gi 1925147141  283 YLQNNFREQQQQFLGQVFS 301
Cdd:cd03122    235 YLPNNGRPQQPLGSRTVFS 253
R-PTP-G-2 cd17670
PTP-like domain of receptor-type tyrosine-protein phosphatase G, repeat 2; Receptor-type ...
1189-1396 1.39e-100

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: 319.70  E-value: 1.39e-100
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1925147141 1189 YINASYIMGYHKSREFILTQSPLPSTVSDFWRMVWDHNSQLIISLPDThtaQREGEESCAYWPSKDQPISCEGFIVSFSG 1268
Cdd:cd17670      1 YINASYIMGYYRSNEFIITQHPLPHTTKDFWRMIWDHNAQIIVMLPDN---QGLAEDEFVYWPSREESMNCEAFTVTLIS 77
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1925147141 1269 EDHMCLANEERLVVHDFLLEATQDNYVLEVRQYMSPCWPNPDSPVSGTFQLLNIITEDSRQREGTIVVHDRLGGSVAGLF 1348
Cdd:cd17670     78 KDRLCLSNEEQIIIHDFILEATQDDYVLEVRHFQCPKWPNPDAPISSTFELINVIKEEALTRDGPTIVHDEFGAVSAGTL 157
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*...
gi 1925147141 1349 CALTTLAQQLEHQGSVDVYQVARMTNLMRPGVFNDMEQYQFMYRAVLS 1396
Cdd:cd17670    158 CALTTLSQQLENENAVDVYQVAKMINLMRPGVFTDIEQYQFLYKAMLS 205
PTPc cd00047
catalytic domain of protein tyrosine phosphatases; Protein tyrosine phosphatases (PTP, EC 3.1. ...
894-1098 1.25e-90

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: 291.88  E-value: 1.25e-90
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1925147141  894 YINANFVDGFERTRAYIAAQGPLKSGTEDFWRMVWQENVGVIVMITNLLEKGRRKCDQYWPMENQE--EYGHFLVTLKDT 971
Cdd:cd00047      1 YINASYIDGYRGPKEYIATQGPLPNTVEDFWRMVWEQKVSVIVMLTNLVEKGREKCERYWPEEGGKplEYGDITVTLVSE 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1925147141  972 KTLAYYTLRTFTLRDTSQKASqrgrcaeRTVVQYHYTQWPDMGVPEYTLPVLSFVRASTQARTQDMGPVLVHCSAGVGRT 1051
Cdd:cd00047     81 EELSDYTIRTLELSPKGCSES-------REVTHLHYTGWPDHGVPSSPEDLLALVRRVRKEARKPNGPIVVHCSAGVGRT 153
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*..
gi 1925147141 1052 GTYIVLDSMLQQIQDQGTVNILGFLKHVRTQRNYLVQTEEQYVFIHD 1098
Cdd:cd00047    154 GTFIAIDILLERLEAEGEVDVFEIVKALRKQRPGMVQTLEQYEFIYE 200
R-PTPc-F-1 cd14626
catalytic domain of receptor-type tyrosine-protein phosphatase F, repeat 1; Receptor-type ...
840-1105 2.72e-89

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: 291.17  E-value: 2.72e-89
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1925147141  840 FSKEFEEVQSctvEMGITTDSSNHPDNKNKNRYINIMAYDHSRVKL--LEEGKGGDYINANFVDGFERTRAYIAAQGPLK 917
Cdd:cd14626     18 FSQEYESIDP---GQQFTWENSNLEVNKPKNRYANVIAYDHSRVILtsVDGVPGSDYINANYIDGYRKQNAYIATQGPLP 94
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1925147141  918 SGTEDFWRMVWQENVGVIVMITNLLEKGRRKCDQYWPMENQEEYGHFLVTLKDTKTLAYYTLRTFTLRdtsqkasQRGRC 997
Cdd:cd14626     95 ETLSDFWRMVWEQRTATIVMMTRLEEKSRVKCDQYWPIRGTETYGMIQVTLLDTVELATYSVRTFALY-------KNGSS 167
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1925147141  998 AERTVVQYHYTQWPDMGVPEYTLPVLSFVRASTQARTQDMGPVLVHCSAGVGRTGTYIVLDSMLQQIQDQGTVNILGFLK 1077
Cdd:cd14626    168 EKREVRQFQFMAWPDHGVPEYPTPILAFLRRVKACNPPDAGPMVVHCSAGVGRTGCFIVIDAMLERMKHEKTVDIYGHVT 247
                          250       260
                   ....*....|....*....|....*...
gi 1925147141 1078 HVRTQRNYLVQTEEQYVFIHDALVEAIV 1105
Cdd:cd14626    248 CMRSQRNYMVQTEDQYIFIHEALLEAAT 275
Carb_anhydrase pfam00194
Eukaryotic-type carbonic anhydrase;
52-303 2.58e-85

Eukaryotic-type carbonic anhydrase;


Pssm-ID: 459707 [Multi-domain]  Cd Length: 252  Bit Score: 278.77  E-value: 2.58e-85
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1925147141   52 WGKRYPACNNARQSPIDIDETFTQVRVEYQGLQLEGWEkNTPETTTINNDGNTVVLGLDGEY--YVSGGGLSTRFRLGRM 129
Cdd:pfam00194    6 WGKVYPSCGGKRQSPINIDTRKVRYDPSLPPLTFQGYD-VPPGKNTLTNNGHTVQVSLDDGDpsTISGGPLATRYRLVQF 84
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1925147141  130 TFHWGRCNasSDGSEHSLNGLKFPLEMQILCYESGlYQSIDDAVRDGGRIAALAVLFETSLDNNDNYNTILEGVNSVNRF 209
Cdd:pfam00194   85 HFHWGSTD--SRGSEHTIDGKRYPAELHIVHYNSK-YKSFDEAAKHPDGLAVLGVFFEVGDENNPYLQPIVSALDNIKYK 161
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1925147141  210 GKTGNVEPFSLLALLPNSTDKYYTYNGSLTSPPCSETVEWIVFKHTVPISETQLEVFCEVMTMQQAGYvmlMDYLQNNFR 289
Cdd:pfam00194  162 GKSVLLPPFDLSDLLPEDLTSYYTYNGSLTTPPCSESVTWIVFKEPISISEEQLEAFRTLLFSDGGEE---PRPLVNNFR 238
                          250
                   ....*....|....
gi 1925147141  290 EQQQQFLGQVFSSY 303
Cdd:pfam00194  239 PTQPLNGRVVFASF 252
R-PTPc-S-1 cd14625
catalytic domain of receptor-type tyrosine-protein phosphatase S, repeat 1; Receptor-type ...
819-1104 3.37e-85

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: 280.06  E-value: 3.37e-85
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1925147141  819 HEALSVKQFVKHVAELHQTNTFsKEFEEVQSCTVEMGITTDSSNHPDNKNKNRYINIMAYDHSRVKLLE-EG-KGGDYIN 896
Cdd:cd14625      1 HPPIPISELAEHTERLKANDNL-KLSQEYESIDPGQQFTWEHSNLEVNKPKNRYANVIAYDHSRVILQPiEGiMGSDYIN 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1925147141  897 ANFVDGFERTRAYIAAQGPLKSGTEDFWRMVWQENVGVIVMITNLLEKGRRKCDQYWPMENQEEYGHFLVTLKDTKTLAY 976
Cdd:cd14625     80 ANYIDGYRKQNAYIATQGPLPETFGDFWRMVWEQRSATVVMMTKLEEKSRIKCDQYWPSRGTETYGMIQVTLLDTIELAT 159
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1925147141  977 YTLRTFTLRdtsqkasQRGRCAERTVVQYHYTQWPDMGVPEYTLPVLSFVRASTQARTQDMGPVLVHCSAGVGRTGTYIV 1056
Cdd:cd14625    160 FCVRTFSLH-------KNGSSEKREVRQFQFTAWPDHGVPEYPTPFLAFLRRVKTCNPPDAGPIVVHCSAGVGRTGCFIV 232
                          250       260       270       280
                   ....*....|....*....|....*....|....*....|....*...
gi 1925147141 1057 LDSMLQQIQDQGTVNILGFLKHVRTQRNYLVQTEEQYVFIHDALVEAI 1104
Cdd:cd14625    233 IDAMLERIKHEKTVDIYGHVTLMRSQRNYMVQTEDQYSFIHDALLEAV 280
R3-PTPc cd14548
catalytic domain of R3 subfamily receptor-type tyrosine-protein phosphatases and similar ...
871-1097 1.65e-83

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: 272.69  E-value: 1.65e-83
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1925147141  871 RYINIMAYDHSRVKL--LEEGKGGDYINANFVDGFERTRAYIAAQGPLKSGTEDFWRMVWQENVGVIVMITNLLEKGRRK 948
Cdd:cd14548      1 RYTNILPYDHSRVKLipINEEEGSDYINANYIPGYNSPREFIATQGPLPGTKDDFWRMVWEQNSHTIVMLTQCMEKGRVK 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1925147141  949 CDQYWPMENQE-EYGHFLVTLKDTKTLAYYTLRTFTLrdtsqkaSQRGRCaeRTVVQYHYTQWPDMGVPEYTLPVLSFVR 1027
Cdd:cd14548     81 CDHYWPFDQDPvYYGDITVTMLSESVLPDWTIREFKL-------ERGDEV--RSVRQFHFTAWPDHGVPEAPDSLLRFVR 151
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1925147141 1028 ASTQARTQDMGPVLVHCSAGVGRTGTYIVLDSMLQQIQDQGTVNILGFLKHVRTQRNYLVQTEEQYVFIH 1097
Cdd:cd14548    152 LVRDYIKQEKGPTIVHCSAGVGRTGTFIALDRLLQQIESEDYVDIFGIVYDLRKHRPLMVQTEAQYIFLH 221
R-PTPc-D-1 cd14624
catalytic domain of receptor-type tyrosine-protein phosphatase D, repeat 1; Receptor-type ...
819-1104 1.70e-82

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: 272.38  E-value: 1.70e-82
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1925147141  819 HEALSVKQFVKHVAELHQTNT--FSKEFEEVQSctvEMGITTDSSNHPDNKNKNRYINIMAYDHSRVKL--LEEGKGGDY 894
Cdd:cd14624      1 HPPIPILELADHIERLKANDNlkFSQEYESIDP---GQQFTWEHSNLEVNKPKNRYANVIAYDHSRVLLsaIEGIPGSDY 77
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1925147141  895 INANFVDGFERTRAYIAAQGPLKSGTEDFWRMVWQENVGVIVMITNLLEKGRRKCDQYWPMENQEEYGHFLVTLKDTKTL 974
Cdd:cd14624     78 INANYIDGYRKQNAYIATQGALPETFGDFWRMIWEQRSATVVMMTKLEERSRVKCDQYWPSRGTETYGLIQVTLLDTVEL 157
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1925147141  975 AYYTLRTFTLRdtsqkasQRGRCAERTVVQYHYTQWPDMGVPEYTLPVLSFVRASTQARTQDMGPVLVHCSAGVGRTGTY 1054
Cdd:cd14624    158 ATYCVRTFALY-------KNGSSEKREVRQFQFTAWPDHGVPEHPTPFLAFLRRVKTCNPPDAGPMVVHCSAGVGRTGCF 230
                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|
gi 1925147141 1055 IVLDSMLQQIQDQGTVNILGFLKHVRTQRNYLVQTEEQYVFIHDALVEAI 1104
Cdd:cd14624    231 IVIDAMLERIKHEKTVDIYGHVTLMRAQRNYMVQTEDQYIFIHDALLEAV 280
PTPc-N9 cd14543
catalytic domain of tyrosine-protein phosphatase non-receptor type 9; Tyrosine-protein ...
842-1097 3.39e-82

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: 270.77  E-value: 3.39e-82
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1925147141  842 KEFEEVQSCTVEMgiTTDSSNHPDNKNKNRYINIMAYDHSRVKL--LEEGKGGDYINANFVDGFERTRAYIAAQGPLKSG 919
Cdd:cd14543      7 EEYEDIRREPPAG--TFLCSLAPANQEKNRYGDVLCLDQSRVKLpkRNGDERTDYINANFMDGYKQKNAYIATQGPLPKT 84
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1925147141  920 TEDFWRMVWQENVGVIVMITNLLEKGRRKCDQYWPME--NQEEYGHFLVTLKDTKTLAYYTLRTFTLRDTSQKASqrgrc 997
Cdd:cd14543     85 YSDFWRMVWEQKVLVIVMTTRVVERGRVKCGQYWPLEegSSLRYGDLTVTNLSVENKEHYKKTTLEIHNTETDES----- 159
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1925147141  998 aeRTVVQYHYTQWPDMGVPEYTLPVLSFVRA--STQART-QDMG----------PVLVHCSAGVGRTGTYIVLDSMLQQI 1064
Cdd:cd14543    160 --RQVTHFQFTSWPDFGVPSSAAALLDFLGEvrQQQALAvKAMGdrwkghppgpPIVVHCSAGIGRTGTFCTLDICLSQL 237
                          250       260       270
                   ....*....|....*....|....*....|...
gi 1925147141 1065 QDQGTVNILGFLKHVRTQRNYLVQTEEQYVFIH 1097
Cdd:cd14543    238 EDVGTLNVMQTVRRMRTQRAFSIQTPDQYYFCY 270
R-PTPc-T-1 cd14630
catalytic domain of receptor-type tyrosine-protein phosphatase T, repeat 1; Receptor-type ...
865-1103 4.97e-81

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: 266.12  E-value: 4.97e-81
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1925147141  865 DNKNKNRYINIMAYDHSRVKL--LEEGKGGDYINANFVDGFERTRAYIAAQGPLKSGTEDFWRMVWQENVGVIVMITNLL 942
Cdd:cd14630      2 ENRNKNRYGNIISYDHSRVRLqlLDGDPHSDYINANYIDGYHRPRHYIATQGPMQETVKDFWRMIWQENSASVVMVTNLV 81
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1925147141  943 EKGRRKCDQYWPmENQEEYGHFLVTLKDTKTLAYYTLRTFTLRdtsqkasQRGRCAERTVVQYHYTQWPDMGVPEYTLPV 1022
Cdd:cd14630     82 EVGRVKCVRYWP-DDTEVYGDIKVTLIETEPLAEYVIRTFTVQ-------KKGYHEIREIRQFHFTSWPDHGVPCYATGL 153
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1925147141 1023 LSFVRASTQARTQDMGPVLVHCSAGVGRTGTYIVLDSMLQQIQDQGTVNILGFLKHVRTQRNYLVQTEEQYVFIHDALVE 1102
Cdd:cd14630    154 LGFVRQVKFLNPPDAGPIVVHCSAGAGRTGCFIAIDIMLDMAENEGVVDIFNCVRELRAQRVNMVQTEEQYVFVHDAILE 233

                   .
gi 1925147141 1103 A 1103
Cdd:cd14630    234 A 234
Carb_anhydrase smart01057
Eukaryotic-type carbonic anhydrase; Carbonic anhydrases are zinc metalloenzymes which catalyse ...
41-292 6.34e-81

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: 266.49  E-value: 6.34e-81
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1925147141    41 WSYTGQLNQKIWGK-RYPACNNARQSPIDIDETFTQVRVEYQGLQlegWEKNTPETTTINNDGNTVVLGLDGE-YYVSGG 118
Cdd:smart01057    1 WGYEGKNGPEHWGKlDPPFCGGKRQSPIDIVTAEAQYDPSLKPLK---LSYDQPTAKRILNNGHTVQVNFDDDgSTLSGG 77
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1925147141   119 GLSTRFRLGRMTFHWGRCNasSDGSEHSLNGLKFPLEMQILCYESGlyQSIDDAVRDGGRIAALAVLFETSLDNNDNYNT 198
Cdd:smart01057   78 PLPGRYRLKQFHFHWGGSD--SEGSEHTIDGKRFPLELHLVHYNSK--GSFSEAVSKPGGLAVVAVFFKVGAEENPALQA 153
                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1925147141   199 ILEGVNSVNRFGKTGNVEPFSLLALLPNSTDKYYTYNGSLTSPPCSETVEWIVFKHTVPISETQLEVFCEVMTMQQAgyv 278
Cdd:smart01057  154 ILDHLPLIKYKGQETELTPFDLSSLLPASTRHYYTYNGSLTTPPCSEGVTWIVFKEPITISTEQLEKFRTLLPMEGN--- 230
                           250
                    ....*....|....
gi 1925147141   279 mlmDYLQNNFREQQ 292
Cdd:smart01057  231 ---EPLVNNARPLQ 241
R-PTPc-typeIIb-1 cd14555
catalytic domain of type IIb (or R2B) subfamily receptor-type tyrosine-protein phosphatases, ...
894-1103 1.54e-74

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: 246.37  E-value: 1.54e-74
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1925147141  894 YINANFVDGFERTRAYIAAQGPLKSGTEDFWRMVWQENVGVIVMITNLLEKGRRKCDQYWPmENQEEYGHFLVTLKDTKT 973
Cdd:cd14555      1 YINANYIDGYHRPNHYIATQGPMQETVYDFWRMVWQENSASIVMVTNLVEVGRVKCSRYWP-DDTEVYGDIKVTLVETEP 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1925147141  974 LAYYTLRTFTLRdtsqkasQRGRCAERTVVQYHYTQWPDMGVPEYTLPVLSFVRASTQARTQDMGPVLVHCSAGVGRTGT 1053
Cdd:cd14555     80 LAEYVVRTFALE-------RRGYHEIREVRQFHFTGWPDHGVPYHATGLLGFIRRVKASNPPSAGPIVVHCSAGAGRTGC 152
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|
gi 1925147141 1054 YIVLDSMLQQIQDQGTVNILGFLKHVRTQRNYLVQTEEQYVFIHDALVEA 1103
Cdd:cd14555    153 YIVIDIMLDMAEREGVVDIYNCVKELRSRRVNMVQTEEQYIFIHDAILEA 202
alpha_CA cd00326
Carbonic anhydrase alpha (vertebrate-like) group. Carbonic anhydrases (CAs) are ...
63-292 2.90e-74

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


Pssm-ID: 238200  Cd Length: 227  Bit Score: 246.43  E-value: 2.90e-74
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1925147141   63 RQSPIDIDETftQVRVEYQGLQLEgWEKNTPETTTINNDGNTVVLGLDGE-YYVSGGGLSTRFRLGRMTFHWGRCNasSD 141
Cdd:cd00326      3 RQSPINIVTS--AVVYDPSLPPLN-FDYYPTTSLTLVNNGHTVQVNFDDDgGTLSGGGLPGRYKLVQFHFHWGSEN--SP 77
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1925147141  142 GSEHSLNGLKFPLEMQILCYESGLYQSidDAVRDGGRIAALAVLFETSLDNNDNYNTILEGVNSVNRFGKTGNVEPFSLL 221
Cdd:cd00326     78 GSEHTIDGKRYPLELHLVHYNSDYYSS--EAAKKPGGLAVLGVFFEVGEKENPFLKKILDALPKIKYKGKETTLPPFDLS 155
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1925147141  222 ALLPNSTDKYYTYNGSLTSPPCSETVEWIVFKHTVPISETQLEVFCEVMTMQqagyvmlMDYLQNNFREQQ 292
Cdd:cd00326    156 DLLPSSLRDYYTYEGSLTTPPCSEGVTWIVFKEPITISKEQLEAFRSLLDRE-------GKPLVNNYRPVQ 219
R-PTPc-M-1 cd14633
catalytic domain of receptor-type tyrosine-protein phosphatase M, repeat 1; Receptor-type ...
859-1103 7.79e-74

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: 247.26  E-value: 7.79e-74
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1925147141  859 DSSNHPDNKNKNRYINIMAYDHSRVKL--LEEGKGGDYINANFVDGFERTRAYIAAQGPLKSGTEDFWRMVWQENVGVIV 936
Cdd:cd14633     33 DSAKKDENRMKNRYGNIIAYDHSRVRLqpIEGETSSDYINGNYIDGYHRPNHYIATQGPMQETIYDFWRMVWHENTASII 112
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1925147141  937 MITNLLEKGRRKCDQYWPmENQEEYGHFLVTLKDTKTLAYYTLRTFTLRdtsqkasQRGRCAERTVVQYHYTQWPDMGVP 1016
Cdd:cd14633    113 MVTNLVEVGRVKCCKYWP-DDTEIYKDIKVTLIETELLAEYVIRTFAVE-------KRGVHEIREIRQFHFTGWPDHGVP 184
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1925147141 1017 EYTLPVLSFVRASTQARTQDMGPVLVHCSAGVGRTGTYIVLDSMLQQIQDQGTVNILGFLKHVRTQRNYLVQTEEQYVFI 1096
Cdd:cd14633    185 YHATGLLGFVRQVKSKSPPNAGPLVVHCSAGAGRTGCFIVIDIMLDMAEREGVVDIYNCVRELRSRRVNMVQTEEQYVFI 264

                   ....*..
gi 1925147141 1097 HDALVEA 1103
Cdd:cd14633    265 HDAILEA 271
R-PTPc-A-1 cd14621
catalytic domain of receptor-type tyrosine-protein phosphatase A, repeat 1; Receptor-type ...
840-1109 1.06e-73

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: 247.63  E-value: 1.06e-73
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1925147141  840 FSKEFEEVQSCTVEMgiTTDSSNHPDNKNKNRYINIMAYDHSRVKL--LEEGKGGDYINANFVDGFERTRAYIAAQGPLK 917
Cdd:cd14621     28 FREEFNALPACPIQA--TCEAASKEENKEKNRYVNILPYDHSRVHLtpVEGVPDSDYINASFINGYQEKNKFIAAQGPKE 105
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1925147141  918 SGTEDFWRMVWQENVGVIVMITNLLEKGRRKCDQYWPMENQEEYGHFLVTLKDTKTLAYYTLRTFTLRdtsQKASQRGRC 997
Cdd:cd14621    106 ETVNDFWRMIWEQNTATIVMVTNLKERKECKCAQYWPDQGCWTYGNIRVSVEDVTVLVDYTVRKFCIQ---QVGDVTNKK 182
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1925147141  998 AERTVVQYHYTQWPDMGVPEYTLPVLSFVRASTQARTQDMGPVLVHCSAGVGRTGTYIVLDSMLQQIQDQGTVNILGFLK 1077
Cdd:cd14621    183 PQRLITQFHFTSWPDFGVPFTPIGMLKFLKKVKNCNPQYAGAIVVHCSAGVGRTGTFIVIDAMLDMMHAERKVDVYGFVS 262
                          250       260       270
                   ....*....|....*....|....*....|..
gi 1925147141 1078 HVRTQRNYLVQTEEQYVFIHDALVEAIVSRDT 1109
Cdd:cd14621    263 RIRAQRCQMVQTDMQYVFIYQALLEHYLYGDT 294
R-PTPc-B cd14617
catalytic domain of receptor-type tyrosine-protein phosphatase B; Receptor-type ...
870-1097 2.76e-72

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: 240.98  E-value: 2.76e-72
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1925147141  870 NRYINIMAYDHSRVKL--LEEGKGGDYINANFVDGFERTRAYIAAQGPLKSGTEDFWRMVWQENVGVIVMITNLLEKGRR 947
Cdd:cd14617      1 NRYNNILPYDSTRVKLsnVDDDPCSDYINASYIPGNNFRREYIATQGPLPGTKDDFWKMVWEQNVHNIVMVTQCVEKGRV 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1925147141  948 KCDQYWPMENQE-EYGHFLVTLKDTKTLAYYTLRTFTLRDTSQKAsqrgrcAERTVVQYHYTQWPDMGVPEYTLPVLSFV 1026
Cdd:cd14617     81 KCDHYWPADQDSlYYGDLIVQMLSESVLPEWTIREFKICSEEQLD------APRLVRHFHYTVWPDHGVPETTQSLIQFV 154
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1925147141 1027 RASTQ--ARTQDMGPVLVHCSAGVGRTGTYIVLDSMLQQIQDQGTVNILGFLKHVRTQRNYLVQTEEQYVFIH 1097
Cdd:cd14617    155 RTVRDyiNRTPGSGPTVVHCSAGVGRTGTFIALDRILQQLDSKDSVDIYGAVHDLRLHRVHMVQTECQYVYLH 227
R-PTPc-U-1 cd14632
catalytic domain of receptor-type tyrosine-protein phosphatase U, repeat 1; Receptor-type ...
894-1103 3.58e-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: 239.57  E-value: 3.58e-72
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1925147141  894 YINANFVDGFERTRAYIAAQGPLKSGTEDFWRMVWQENVGVIVMITNLLEKGRRKCDQYWPmENQEEYGHFLVTLKDTKT 973
Cdd:cd14632      1 YINANYIDGYHRSNHFIATQGPKQEMVYDFWRMVWQEHCSSIVMITKLVEVGRVKCSKYWP-DDSDTYGDIKITLLKTET 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1925147141  974 LAYYTLRTFTLRdtsqkasQRGRCAERTVVQYHYTQWPDMGVPEYTLPVLSFVRASTQARTQDMGPVLVHCSAGVGRTGT 1053
Cdd:cd14632     80 LAEYSVRTFALE-------RRGYSARHEVKQFHFTSWPEHGVPYHATGLLAFIRRVKASTPPDAGPVVVHCSAGAGRTGC 152
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|
gi 1925147141 1054 YIVLDSMLQQIQDQGTVNILGFLKHVRTQRNYLVQTEEQYVFIHDALVEA 1103
Cdd:cd14632    153 YIVLDVMLDMAECEGVVDIYNCVKTLCSRRINMIQTEEQYIFIHDAILEA 202
PTPc-N11_6 cd14544
catalytic domain of tyrosine-protein phosphatase non-receptor type 11 and type 6; ...
866-1104 7.59e-72

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: 240.44  E-value: 7.59e-72
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1925147141  866 NKNKNRYINIMAYDHSRVKLLE---EGKGGDYINANFV-------DGFERTRAYIAAQGPLKSGTEDFWRMVWQENVGVI 935
Cdd:cd14544      1 NKGKNRYKNILPFDHTRVILKDrdpNVPGSDYINANYIrnenegpTTDENAKTYIATQGCLENTVSDFWSMVWQENSRVI 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1925147141  936 VMITNLLEKGRRKCDQYWPME-NQEEYGHFLVTLKDTKTLAYYTLRTFTLRDTSQKASqrgrcaERTVVQYHYTQWPDMG 1014
Cdd:cd14544     81 VMTTKEVERGKNKCVRYWPDEgMQKQYGPYRVQNVSEHDTTDYTLRELQVSKLDQGDP------IREIWHYQYLSWPDHG 154
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1925147141 1015 VPEYTLPVLSFVRA--STQARTQDMGPVLVHCSAGVGRTGTYIVLDSMLQQIQDQG---TVNILGFLKHVRTQRNYLVQT 1089
Cdd:cd14544    155 VPSDPGGVLNFLEDvnQRQESLPHAGPIVVHCSAGIGRTGTFIVIDMLLDQIKRKGldcDIDIQKTIQMVRSQRSGMVQT 234
                          250
                   ....*....|....*
gi 1925147141 1090 EEQYVFIHDALVEAI 1104
Cdd:cd14544    235 EAQYKFIYVAVAQYI 249
R-PTPc-J cd14615
catalytic domain of receptor-type tyrosine-protein phosphatase J; Receptor-type ...
870-1096 2.32e-71

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: 238.18  E-value: 2.32e-71
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1925147141  870 NRYINIMAYDHSRVKLLEEG-KGGDYINANFVDGFERTRAYIAAQGPLKSGTEDFWRMVWQENVGVIVMITNLLEKGRRK 948
Cdd:cd14615      1 NRYNNVLPYDISRVKLSVQShSTDDYINANYMPGYNSKKEFIAAQGPLPNTVKDFWRMVWEKNVYAIVMLTKCVEQGRTK 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1925147141  949 CDQYWPMENQEEYGHFLVTLKDTKTLAYYTLRTFTLrdTSQKASQRgrcaeRTVVQYHYTQWPDMGVPEYTLPVLSF--- 1025
Cdd:cd14615     81 CEEYWPSKQKKDYGDITVTMTSEIVLPEWTIRDFTV--KNAQTNES-----RTVRHFHFTSWPDHGVPETTDLLINFrhl 153
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1925147141 1026 VRASTQARTQDmGPVLVHCSAGVGRTGTYIVLDSMLQQIQDQGTVNILGFLKHVRTQRNYLVQTEEQYVFI 1096
Cdd:cd14615    154 VREYMKQNPPN-SPILVHCSAGVGRTGTFIAIDRLIYQIENENVVDVYGIVYDLRMHRPLMVQTEDQYVFL 223
PTPc-KIM cd14547
catalytic domain of the kinase interaction motif (KIM) family of protein-tyrosine phosphatases; ...
870-1097 4.80e-71

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: 237.29  E-value: 4.80e-71
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1925147141  870 NRYINIMAYDHSRVKL--LEEGKGGDYINANFVDGFE-RTRAYIAAQGPLKSGTEDFWRMVWQENVGVIVMITNLLEKgR 946
Cdd:cd14547      1 NRYKTILPNEHSRVCLpsVDDDPLSSYINANYIRGYDgEEKAYIATQGPLPNTVADFWRMVWQEKTPIIVMITNLTEA-K 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1925147141  947 RKCDQYWPMENQEEYGHFLVTLKDTKTLAYYTLRTFTLRDTSQKasqrgrcaeRTVVQYHYTQWPDMGVPEYTLPVLSFV 1026
Cdd:cd14547     80 EKCAQYWPEEENETYGDFEVTVQSVKETDGYTVRKLTLKYGGEK---------RYLKHYWYTSWPDHKTPEAAQPLLSLV 150
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1925147141 1027 RASTQARTQDM--GPVLVHCSAGVGRTGTYIVLDSMLQQIQDQGTVNILGFLKHVRTQRNYLVQTEEQYVFIH 1097
Cdd:cd14547    151 QEVEEARQTEPhrGPIVVHCSAGIGRTGCFIATSIGCQQLREEGVVDVLGIVCQLRLDRGGMVQTAEQYEFVH 223
R-PTPc-H cd14619
catalytic domain of receptor-type tyrosine-protein phosphatase H; Receptor-type ...
870-1104 4.81e-71

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: 237.48  E-value: 4.81e-71
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1925147141  870 NRYINIMAYDHSRVKL--LEEGKGGDYINANFVDGFERTRAYIAAQGPLKSGTEDFWRMVWQENVGVIVMITNLLEKGRR 947
Cdd:cd14619      1 NRFRNVLPYDWSRVPLkpIHEEPGSDYINANYMPGYWSSQEFIATQGPLPQTVGDFWRMIWEQQSSTIVMLTNCMEAGRV 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1925147141  948 KCDQYWPMENQE-EYGHFLVTLKDTKTLAYYTLRTFTLRDTSQKASqrgrcaeRTVVQYHYTQWPDMGVPEYTLPVLSFV 1026
Cdd:cd14619     81 KCEHYWPLDYTPcTYGHLRVTVVSEEVMENWTVREFLLKQVEEQKT-------LSVRHFHFTAWPDHGVPSSTDTLLAFR 153
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1925147141 1027 RASTQARTQDM--GPVLVHCSAGVGRTGTYIVLDSMLQQIQDQGTVNILGFLKHVRTQRNYLVQTEEQYVFIHDALVEAI 1104
Cdd:cd14619    154 RLLRQWLDQTMsgGPTVVHCSAGVGRTGTLIALDVLLQQLQSEGLLGPFSFVQKMRENRPLMVQTESQYVFLHQCILDFL 233
R-PTPc-O cd14614
catalytic domain of receptor-type tyrosine-protein phosphatase O; Receptor-type ...
856-1097 8.00e-69

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: 231.70  E-value: 8.00e-69
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1925147141  856 ITTDSSNHPDNKNKNRYINIMAYDHSRVKL--LEEGKGGDYINANFVDGFERTRAYIAAQGPLKSGTEDFWRMVWQENVG 933
Cdd:cd14614      2 IPHFAADLPVNRCKNRYTNILPYDFSRVKLvsMHEEEGSDYINANYIPGYNSPQEYIATQGPLPETRNDFWKMVLQQKSQ 81
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1925147141  934 VIVMITNLLEKGRRKCDQYWPM-ENQEEYGHFLVTLKDTKTLAYYTLRTFtlRDTSQKASQRgrcaertVVQYHYTQWPD 1012
Cdd:cd14614     82 IIVMLTQCNEKRRVKCDHYWPFtEEPVAYGDITVEMLSEEEQPDWAIREF--RVSYADEVQD-------VMHFNYTAWPD 152
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1925147141 1013 MGVPEYTL--PVLSFVRASTQARTQDMGPVLVHCSAGVGRTGTYIVLDSMLQQIQDQGTVNILGFLKHVRTQRNYLVQTE 1090
Cdd:cd14614    153 HGVPTANAaeSILQFVQMVRQQAVKSKGPMIIHCSAGVGRTGTFIALDRLLQHIRDHEFVDILGLVSEMRSYRMSMVQTE 232

                   ....*..
gi 1925147141 1091 EQYVFIH 1097
Cdd:cd14614    233 EQYIFIH 239
R-PTPc-K-1 cd14631
catalytic domain of receptor-type tyrosine-protein phosphatase K, repeat 1; Receptor-type ...
886-1103 1.09e-68

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: 230.29  E-value: 1.09e-68
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1925147141  886 LEEGKGGDYINANFVDGFERTRAYIAAQGPLKSGTEDFWRMVWQENVGVIVMITNLLEKGRRKCDQYWPmENQEEYGHFL 965
Cdd:cd14631      7 VEDDPSSDYINANYIDGYQRPSHYIATQGPVHETVYDFWRMIWQEQSACIVMVTNLVEVGRVKCYKYWP-DDTEVYGDFK 85
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1925147141  966 VTLKDTKTLAYYTLRTFTLrdtsqkaSQRGRCAERTVVQYHYTQWPDMGVPEYTLPVLSFVRASTQARTQDMGPVLVHCS 1045
Cdd:cd14631     86 VTCVEMEPLAEYVVRTFTL-------ERRGYNEIREVKQFHFTGWPDHGVPYHATGLLSFIRRVKLSNPPSAGPIVVHCS 158
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 1925147141 1046 AGVGRTGTYIVLDSMLQQIQDQGTVNILGFLKHVRTQRNYLVQTEEQYVFIHDALVEA 1103
Cdd:cd14631    159 AGAGRTGCYIVIDIMLDMAEREGVVDIYNCVKALRSRRINMVQTEEQYIFIHDAILEA 216
R-PTP-LAR-2 cd14554
PTP-like domain of the LAR family receptor-type tyrosine-protein phosphatases, repeat 2; The ...
861-1099 5.96e-68

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: 228.95  E-value: 5.96e-68
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1925147141  861 SNHPDNKNKNRYINIMAYDHSRV--KLLEEGKGGDYINANFVDGFERTRAYIAAQGPLKSGTEDFWRMVWQENVGVIVMI 938
Cdd:cd14554      1 ANLPCNKFKNRLVNILPYESTRVclQPIRGVEGSDYINASFIDGYRQRGAYIATQGPLAETTEDFWRMLWEHNSTIIVML 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1925147141  939 TNLLEKGRRKCDQYWPMENQEEYGHFLVTLKDTKTLAYYTLRTFTLRDTSQKASqrgrcaeRTVVQYHYTQWPDMGVPEY 1018
Cdd:cd14554     81 TKLREMGREKCHQYWPAERSARYQYFVVDPMAEYNMPQYILREFKVTDARDGQS-------RTVRQFQFTDWPEQGVPKS 153
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1925147141 1019 TLPVLSFVRASTQARTQ--DMGPVLVHCSAGVGRTGTYIVLDSMLQQIQDQGTVNILGFLKHVRTQRNYLVQTEEQYVFI 1096
Cdd:cd14554    154 GEGFIDFIGQVHKTKEQfgQEGPITVHCSAGVGRTGVFITLSIVLERMRYEGVVDVFQTVKLLRTQRPAMVQTEDQYQFC 233

                   ...
gi 1925147141 1097 HDA 1099
Cdd:cd14554    234 YRA 236
R-PTPc-E-1 cd14620
catalytic domain of receptor-type tyrosine-protein phosphatase E, repeat 1; Receptor-type ...
872-1102 2.39e-67

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: 226.75  E-value: 2.39e-67
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1925147141  872 YINIMAYDHSRVKL--LEEGKGGDYINANFVDGFERTRAYIAAQGPLKSGTEDFWRMVWQENVGVIVMITNLLEKGRRKC 949
Cdd:cd14620      1 YPNILPYDHSRVILsqLDGIPCSDYINASYIDGYKEKNKFIAAQGPKQETVNDFWRMVWEQKSATIVMLTNLKERKEEKC 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1925147141  950 DQYWPMENQEEYGHFLVTLKDTKTLAYYTLRTFTLrdtsQKASQRGRCAERTVVQYHYTQWPDMGVPEYTLPVLSFVRAS 1029
Cdd:cd14620     81 YQYWPDQGCWTYGNIRVAVEDCVVLVDYTIRKFCI----QPQLPDGCKAPRLVTQLHFTSWPDFGVPFTPIGMLKFLKKV 156
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1925147141 1030 TQARTQDMGPVLVHCSAGVGRTGTYIVLDSMLQQIQDQGTVNILGFLKHVRTQRNYLVQTEEQYVFIHDALVE 1102
Cdd:cd14620    157 KSVNPVHAGPIVVHCSAGVGRTGTFIVIDAMIDMMHAEQKVDVFEFVSRIRNQRPQMVQTDMQYSFIYQALLE 229
R-PTPc-V cd14618
catalytic domain of receptor-type tyrosine-protein phosphatase V; Receptor-type ...
870-1101 4.50e-67

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: 225.98  E-value: 4.50e-67
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1925147141  870 NRYINIMAYDHSRVKL--LEEGKGGDYINANFVDGFERTRAYIAAQGPLKSGTEDFWRMVWQENVGVIVMITNLLEKGRR 947
Cdd:cd14618      1 NRYPHVLPYDHSRVRLsqLGGEPHSDYINANFIPGYTSPQEFIATQGPLKKTIEDFWRLVWEQQVCNIIMLTVGMENGRV 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1925147141  948 KCDQYWPMENQE-EYGHFLVTLKDTKTLAYYTLRTFTLRDTSQKasqrgrcAERTVVQYHYTQWPDMGVPEYTLPVLSF- 1025
Cdd:cd14618     81 LCDHYWPSESTPvSYGHITVHLLAQSSEDEWTRREFKLWHEDLR-------KERRVKHLHYTAWPDHGIPESTSSLMAFr 153
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1925147141 1026 --VRASTQArTQDMGPVLVHCSAGVGRTGTYIVLDSMLQQIQDQGTVNILGFLKHVRTQRNYLVQTEEQYVFIHDALV 1101
Cdd:cd14618    154 elVREHVQA-TKGKGPTLVHCSAGVGRSGTFIALDRLLRQLKEEKVVDVFNTVYILRMHRYLMIQTLSQYIFLHSCIL 230
R-PTPc-A-E-1 cd14551
catalytic domain of receptor-type tyrosine-protein phosphatase A and E, repeat 1; ...
894-1097 1.54e-65

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: 220.55  E-value: 1.54e-65
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1925147141  894 YINANFVDGFERTRAYIAAQGPLKSGTEDFWRMVWQENVGVIVMITNLLEKGRRKCDQYWPMENQEEYGHFLVTLKDTKT 973
Cdd:cd14551      1 YINASYIDGYQEKNKFIAAQGPKDETVNDFWRMIWEQGSATIVMVTNLKERKEKKCSQYWPDQGCWTYGNLRVRVEDTVV 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1925147141  974 LAYYTLRTFTLRdtsQKASQRGRCAERTVVQYHYTQWPDMGVPEYTLPVLSFVRASTQARTQDMGPVLVHCSAGVGRTGT 1053
Cdd:cd14551     81 LVDYTTRKFCIQ---KVNRGIGEKRVRLVTQFHFTSWPDFGVPFTPIGMLKFLKKVKSANPPRAGPIVVHCSAGVGRTGT 157
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....
gi 1925147141 1054 YIVLDSMLQQIQDQGTVNILGFLKHVRTQRNYLVQTEEQYVFIH 1097
Cdd:cd14551    158 FIVIDAMLDMMHAEGKVDVFGFVSRIRQQRSQMVQTDMQYVFIY 201
PTP_fungal cd18533
fungal protein tyrosine phosphatases; This subfamily contains Saccharomyces cerevisiae ...
894-1098 6.00e-65

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: 219.04  E-value: 6.00e-65
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1925147141  894 YINANFVD-GFERTRAYIAAQGPLKSGTEDFWRMVWQENVGVIVMITNLLEKGRRKCDQYWPM-ENQEEYGHFLVTLKDT 971
Cdd:cd18533      1 YINASYITlPGTSSKRYIATQGPLPATIGDFWKMIWQNNVGVIVMLTPLVENGREKCDQYWPSgEYEGEYGDLTVELVSE 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1925147141  972 KTL--AYYTLRTFTLRDTSQKasqrgrcaERTVVQYHYTQWPDMGVPEYTLPVLS---FVRASTQArTQDMGPVLVHCSA 1046
Cdd:cd18533     81 EENddGGFIVREFELSKEDGK--------VKKVYHIQYKSWPDFGVPDSPEDLLTlikLKRELNDS-ASLDPPIIVHCSA 151
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1925147141 1047 GVGRTGTYIVLDSMLQQIQDQG---------------TVNILgflkhvRTQRNYLVQTEEQYVFIHD 1098
Cdd:cd18533    152 GVGRTGTFIALDSLLDELKRGLsdsqdledsedpvyeIVNQL------RKQRMSMVQTLRQYIFLYD 212
R-PTP-D-2 cd14628
PTP-like domain of receptor-type tyrosine-protein phosphatase D, repeat 2; Receptor-type ...
860-1108 9.28e-65

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: 221.91  E-value: 9.28e-65
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1925147141  860 SSNHPDNKNKNRYINIMAYDHSRVKL--LEEGKGGDYINANFVDGFERTRAYIAAQGPLKSGTEDFWRMVWQENVGVIVM 937
Cdd:cd14628     46 SANLPCNKFKNRLVNIMPYESTRVCLqpIRGVEGSDYINASFIDGYRQQKAYIATQGPLAETTEDFWRMLWEHNSTIVVM 125
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1925147141  938 ITNLLEKGRRKCDQYWPMENQEEYGHFLVTLKDTKTLAYYTLRTFTLRDTSQKASqrgrcaeRTVVQYHYTQWPDMGVPE 1017
Cdd:cd14628    126 LTKLREMGREKCHQYWPAERSARYQYFVVDPMAEYNMPQYILREFKVTDARDGQS-------RTVRQFQFTDWPEQGVPK 198
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1925147141 1018 YTLPVLSFVRASTQARTQ--DMGPVLVHCSAGVGRTGTYIVLDSMLQQIQDQGTVNILGFLKHVRTQRNYLVQTEEQYVF 1095
Cdd:cd14628    199 SGEGFIDFIGQVHKTKEQfgQDGPISVHCSAGVGRTGVFITLSIVLERMRYEGVVDIFQTVKMLRTQRPAMVQTEDQYQF 278
                          250
                   ....*....|...
gi 1925147141 1096 IHDALVEAIVSRD 1108
Cdd:cd14628    279 CYRAALEYLGSFD 291
R-PTP-S-2 cd14627
PTP-like domain of receptor-type tyrosine-protein phosphatase S, repeat 2; Receptor-type ...
860-1106 2.47e-64

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: 220.76  E-value: 2.47e-64
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1925147141  860 SSNHPDNKNKNRYINIMAYDHSRVKL--LEEGKGGDYINANFVDGFERTRAYIAAQGPLKSGTEDFWRMVWQENVGVIVM 937
Cdd:cd14627     47 SANLPCNKFKNRLVNIMPYETTRVCLqpIRGVEGSDYINASFIDGYRQQKAYIATQGPLAETTEDFWRMLWENNSTIVVM 126
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1925147141  938 ITNLLEKGRRKCDQYWPMENQEEYGHFLVTLKDTKTLAYYTLRTFTLRDTSQKASqrgrcaeRTVVQYHYTQWPDMGVPE 1017
Cdd:cd14627    127 LTKLREMGREKCHQYWPAERSARYQYFVVDPMAEYNMPQYILREFKVTDARDGQS-------RTVRQFQFTDWPEQGVPK 199
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1925147141 1018 YTLPVLSFVRASTQARTQ--DMGPVLVHCSAGVGRTGTYIVLDSMLQQIQDQGTVNILGFLKHVRTQRNYLVQTEEQYVF 1095
Cdd:cd14627    200 SGEGFIDFIGQVHKTKEQfgQDGPISVHCSAGVGRTGVFITLSIVLERMRYEGVVDIFQTVKMLRTQRPAMVQTEDEYQF 279
                          250
                   ....*....|.
gi 1925147141 1096 IHDALVEAIVS 1106
Cdd:cd14627    280 CYQAALEYLGS 290
R-PTP-F-2 cd14629
PTP-like domain of receptor-type tyrosine-protein phosphatase F, repeat 2; Receptor-type ...
860-1106 3.59e-63

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: 217.29  E-value: 3.59e-63
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1925147141  860 SSNHPDNKNKNRYINIMAYDHSRVKL--LEEGKGGDYINANFVDGFERTRAYIAAQGPLKSGTEDFWRMVWQENVGVIVM 937
Cdd:cd14629     47 SANLPCNKFKNRLVNIMPYELTRVCLqpIRGVEGSDYINASFIDGYRQQKAYIATQGPLAETTEDFWRMLWEHNSTIVVM 126
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1925147141  938 ITNLLEKGRRKCDQYWPMENQEEYGHFLVTLKDTKTLAYYTLRTFTLRDTSQKASqrgrcaeRTVVQYHYTQWPDMGVPE 1017
Cdd:cd14629    127 LTKLREMGREKCHQYWPAERSARYQYFVVDPMAEYNMPQYILREFKVTDARDGQS-------RTIRQFQFTDWPEQGVPK 199
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1925147141 1018 YTLPVLSFVRASTQARTQ--DMGPVLVHCSAGVGRTGTYIVLDSMLQQIQDQGTVNILGFLKHVRTQRNYLVQTEEQYVF 1095
Cdd:cd14629    200 TGEGFIDFIGQVHKTKEQfgQDGPITVHCSAGVGRTGVFITLSIVLERMRYEGVVDMFQTVKTLRTQRPAMVQTEDQYQL 279
                          250
                   ....*....|.
gi 1925147141 1096 IHDALVEAIVS 1106
Cdd:cd14629    280 CYRAALEYLGS 290
PTPc-N18 cd14603
catalytic domain of tyrosine-protein phosphatase non-receptor type 18; Tyrosine-protein ...
841-1102 2.18e-62

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: 213.92  E-value: 2.18e-62
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1925147141  841 SKEFEEVQSCTVEM----GITTDSSNHPDNKNKNRYINIMAYDHSRV--KLLEEGKGGDYINANFVDGFERTRAYIAAQG 914
Cdd:cd14603      1 AGEFSEIRACSAAFkadyVCSTVAGGRKENVKKNRYKDILPYDQTRVilSLLQEEGHSDYINANFIKGVDGSRAYIATQG 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1925147141  915 PLKSGTEDFWRMVWQENVGVIVMITNLLEKGRRKCDQYWPMENQE-EYGHFLVT-LKDTKTLAYYTLRTFTLrdTSQKAS 992
Cdd:cd14603     81 PLSHTVLDFWRMIWQYGVKVILMACREIEMGKKKCERYWAQEQEPlQTGPFTITlVKEKRLNEEVILRTLKV--TFQKES 158
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1925147141  993 qrgrcaeRTVVQYHYTQWPDMGVPEYTLPVLSFVRASTQARTQDMGPVLVHCSAGVGRTGTYIVLDS-----MLQQIQDQ 1067
Cdd:cd14603    159 -------RSVSHFQYMAWPDHGIPDSPDCMLAMIELARRLQGSGPEPLCVHCSAGCGRTGVICTVDYvrqllLTQRIPPD 231
                          250       260       270
                   ....*....|....*....|....*....|....*
gi 1925147141 1068 gtVNILGFLKHVRTQRNYLVQTEEQYVFIHDALVE 1102
Cdd:cd14603    232 --FSIFDVVLEMRKQRPAAVQTEEQYEFLYHTVAQ 264
PTPc smart00194
Protein tyrosine phosphatase, catalytic domain;
1154-1395 1.38e-61

Protein tyrosine phosphatase, catalytic domain;


Pssm-ID: 214550 [Multi-domain]  Cd Length: 259  Bit Score: 211.36  E-value: 1.38e-61
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1925147141  1154 ALREGNDDKNRTSSLMPVERSRVCLScPVEGESSDYINASYIMGYHKSREFILTQSPLPSTVSDFWRMVWDHNSQLIISL 1233
Cdd:smart00194   22 AAFPENRDKNRYKDVLPYDHTRVKLK-PPPGEGSDYINASYIDGPNGPKAYIATQGPLPSTVEDFWRMVWEQKVTVIVML 100
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1925147141  1234 PDTHTAQREGEEScaYWPSK-DQPISCEGFIVSFSGEDHMclaneERLVVHDFLLEATQDNYVLEVRQYMSPCWP---NP 1309
Cdd:smart00194  101 TELVEKGREKCAQ--YWPDEeGEPLTYGDITVTLKSVEKV-----DDYTIRTLEVTNTGCSETRTVTHYHYTNWPdhgVP 173
                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1925147141  1310 DSPvSGTFQLLNIITEDSRQREGTIVVHDRLGGSVAGLFCALTTLAQQLEHQGSVDVYQVARMTNLMRPGVFNDMEQYQF 1389
Cdd:smart00194  174 ESP-ESILDLIRAVRKSQSTSTGPIVVHCSAGVGRTGTFIAIDILLQQLEAGKEVDIFEIVKELRSQRPGMVQTEEQYIF 252

                    ....*.
gi 1925147141  1390 MYRAVL 1395
Cdd:smart00194  253 LYRAIL 258
PTPc-N11 cd14605
catalytic domain of tyrosine-protein phosphatase non-receptor type 11; Tyrosine-protein ...
865-1100 2.74e-61

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: 210.26  E-value: 2.74e-61
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1925147141  865 DNKNKNRYINIMAYDHSRVkLLEEG----KGGDYINANFV-DGFER-------TRAYIAAQGPLKSGTEDFWRMVWQENV 932
Cdd:cd14605      1 ENKNKNRYKNILPFDHTRV-VLHDGdpnePVSDYINANIImPEFETkcnnskpKKSYIATQGCLQNTVNDFWRMVFQENS 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1925147141  933 GVIVMITNLLEKGRRKCDQYWPMENQ-EEYGHFLVtlKDTK-TLAY-YTLRTFTLRDTSQKASqrgrcaERTVVQYHYTQ 1009
Cdd:cd14605     80 RVIVMTTKEVERGKSKCVKYWPDEYAlKEYGVMRV--RNVKeSAAHdYILRELKLSKVGQGNT------ERTVWQYHFRT 151
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1925147141 1010 WPDMGVPEYTLPVLSFVRA--STQARTQDMGPVLVHCSAGVGRTGTYIVLDSMLQQIQDQGT---VNILGFLKHVRTQRN 1084
Cdd:cd14605    152 WPDHGVPSDPGGVLDFLEEvhHKQESIMDAGPVVVHCSAGIGRTGTFIVIDILIDIIREKGVdcdIDVPKTIQMVRSQRS 231
                          250
                   ....*....|....*.
gi 1925147141 1085 YLVQTEEQYVFIHDAL 1100
Cdd:cd14605    232 GMVQTEAQYRFIYMAV 247
PTPc-N1_2 cd14545
catalytic domain of tyrosine-protein phosphatase non-receptor type 1 and type 2; ...
867-1095 5.52e-61

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: 208.79  E-value: 5.52e-61
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1925147141  867 KNKNRYINImaYDHSRVKLLEEGKGGDYINANFVDGFERTRAYIAAQGPLKSGTEDFWRMVWQENVGVIVMITNLLEKGR 946
Cdd:cd14545      1 LNRYRDRDP--YDHDRSRVKLKQGDNDYINASLVEVEEAKRSYILTQGPLPNTSGHFWQMVWEQNSKAVIMLNKLMEKGQ 78
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1925147141  947 RKCDQYWPmeNQEEYGH------FLVTLKDTKTLAYYTLRTFTLRDtsqKASQRgrcaERTVVQYHYTQWPDMGVPEYTL 1020
Cdd:cd14545     79 IKCAQYWP--QGEGNAMifedtgLKVTLLSEEDKSYYTVRTLELEN---LKTQE----TREVLHFHYTTWPDFGVPESPA 149
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1925147141 1021 PVLSF---VRaSTQARTQDMGPVLVHCSAGVGRTGTYIVLDSMLQQIQDQGT--VNILGFLKHVRTQRNYLVQTEEQYVF 1095
Cdd:cd14545    150 AFLNFlqkVR-ESGSLSSDVGPPVVHCSAGIGRSGTFCLVDTCLVLIEKGNPssVDVKKVLLEMRKYRMGLIQTPDQLRF 228
PTPc-N6 cd14606
catalytic domain of tyrosine-protein phosphatase non-receptor type 6; Tyrosine-protein ...
859-1106 9.04e-61

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: 209.35  E-value: 9.04e-61
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1925147141  859 DSSNHPDNKNKNRYINIMAYDHSRVkLLEEGK----GGDYINANFVDG-----FERTRAYIAAQGPLKSGTEDFWRMVWQ 929
Cdd:cd14606     11 LEGQRPENKSKNRYKNILPFDHSRV-ILQGRDsnipGSDYINANYVKNqllgpDENAKTYIASQGCLEATVNDFWQMAWQ 89
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1925147141  930 ENVGVIVMITNLLEKGRRKCDQYWP-MENQEEYGHFLVTLKDTKTLAYYTLRtfTLRDTSQKASQrgrcAERTVVQYHYT 1008
Cdd:cd14606     90 ENSRVIVMTTREVEKGRNKCVPYWPeVGMQRAYGPYSVTNCGEHDTTEYKLR--TLQVSPLDNGE----LIREIWHYQYL 163
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1925147141 1009 QWPDMGVPEYTLPVLSFVRA--STQARTQDMGPVLVHCSAGVGRTGTYIVLDSMLQQIQDQGT---VNILGFLKHVRTQR 1083
Cdd:cd14606    164 SWPDHGVPSEPGGVLSFLDQinQRQESLPHAGPIIVHCSAGIGRTGTIIVIDMLMENISTKGLdcdIDIQKTIQMVRAQR 243
                          250       260
                   ....*....|....*....|...
gi 1925147141 1084 NYLVQTEEQYVFIHDALVEAIVS 1106
Cdd:cd14606    244 SGMVQTEAQYKFIYVAIAQFIET 266
Y_phosphatase pfam00102
Protein-tyrosine phosphatase;
1159-1395 1.27e-59

Protein-tyrosine phosphatase;


Pssm-ID: 459674 [Multi-domain]  Cd Length: 234  Bit Score: 204.78  E-value: 1.27e-59
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1925147141 1159 NDDKNRTSSLMPVERSRVCLscPVEGESSDYINASYIMGYHKSREFILTQSPLPSTVSDFWRMVWDHNSQLIISLpdthT 1238
Cdd:pfam00102    1 NLEKNRYKDVLPYDHTRVKL--TGDPGPSDYINASYIDGYKKPKKYIATQGPLPNTVEDFWRMVWEEKVTIIVML----T 74
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1925147141 1239 AQRE-GEESCA-YWPSK-DQPISCEGFIVSFSGEDhmclANEERLVVHDFLLEATQDNYVLEVRQYMSPCWPNPDSPVSg 1315
Cdd:pfam00102   75 ELEEkGREKCAqYWPEEeGESLEYGDFTVTLKKEK----EDEKDYTVRTLEVSNGGSEETRTVKHFHYTGWPDHGVPES- 149
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1925147141 1316 TFQLLNII----TEDSRQREGTIVVHDRLGGSVAGLFCALTTLAQQLEHQGSVDVYQVARMTNLMRPGVFNDMEQYQFMY 1391
Cdd:pfam00102  150 PNSLLDLLrkvrKSSLDGRSGPIVVHCSAGIGRTGTFIAIDIALQQLEAEGEVDIFQIVKELRSQRPGMVQTLEQYIFLY 229

                   ....
gi 1925147141 1392 RAVL 1395
Cdd:pfam00102  230 DAIL 233
R-PTPc-C-1 cd14557
catalytic domain of receptor-type tyrosine-protein phosphatase C, repeat 1; Receptor-type ...
894-1097 1.69e-59

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: 203.13  E-value: 1.69e-59
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1925147141  894 YINANFVDGFERTRAYIAAQGPLKSGTEDFWRMVWQENVGVIVMITNLLEKGRRKCDQYWPM--ENQEEYGHFLVTLKDT 971
Cdd:cd14557      1 YINASYIDGFKEPRKYIAAQGPKDETVDDFWRMIWEQKSTVIVMVTRCEEGNRNKCAQYWPSmeEGSRAFGDVVVKINEE 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1925147141  972 KTLAYYTLRTFTLRDTSQKASqrgrcaERTVVQYHYTQWPDMGVPEYTLPVLSFVRASTQARTQDMGPVLVHCSAGVGRT 1051
Cdd:cd14557     81 KICPDYIIRKLNINNKKEKGS------GREVTHIQFTSWPDHGVPEDPHLLLKLRRRVNAFNNFFSGPIVVHCSAGVGRT 154
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*.
gi 1925147141 1052 GTYIVLDSMLQQIQDQGTVNILGFLKHVRTQRNYLVQTEEQYVFIH 1097
Cdd:cd14557    155 GTYIGIDAMLEGLEAEGRVDVYGYVVKLRRQRCLMVQVEAQYILIH 200
PTPc-N7 cd14612
catalytic domain of tyrosine-protein phosphatase non-receptor type 7; Tyrosine-protein ...
856-1100 5.29e-59

catalytic domain of tyrosine-protein phosphatase non-receptor type 7; Tyrosine-protein phosphatase non-receptor type 7 (PTPN7), also called hematopoietic protein-tyrosine phosphatase (HePTP) or LC-PTP. belongs to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. PTPN7/HePTP is a kinase interaction motif (KIM)-PTP, characterized by the presence of a 16-amino-acid KIM that binds specifically to members of the MAPK (mitogen-activated protein kinase) family. PTPN7/HePTP is found exclusively in the white blood cells in bone marrow, thymus, spleen, lymph nodes and all myeloid and lymphoid cell lines. It negatively regulates T-cell activation and proliferation, and is often dysregulated in the preleukemic disorder myelodysplastic syndrome, as well as in acute myelogenous leukemia.


Pssm-ID: 350460 [Multi-domain]  Cd Length: 247  Bit Score: 203.53  E-value: 5.29e-59
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1925147141  856 ITTDSSNHPDNKNKNRYINIMAYDHSRVKLLEEG---KGGDYINANFVDGFE-RTRAYIAAQGPLKSGTEDFWRMVWQEN 931
Cdd:cd14612      5 VSPEELDIPGHASKDRYKTILPNPQSRVCLRRAGsqeEEGSYINANYIRGYDgKEKAYIATQGPMLNTVSDFWEMVWQEE 84
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1925147141  932 VGVIVMITNLLEKgRRKCDQYWPmENQEEYGHFLVTLKDTKTLAYYTLRTFTLrdtsQKASQRgrcaeRTVVQYHYTQWP 1011
Cdd:cd14612     85 CPIIVMITKLKEK-KEKCVHYWP-EKEGTYGRFEIRVQDMKECDGYTIRDLTI----QLEEES-----RSVKHYWFSSWP 153
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1925147141 1012 DMGVPEYTLPVLSFVRASTQAR--TQDMGPVLVHCSAGVGRTGTYIVLDSMLQQIQDQGTVNILGFLKHVRTQRNYLVQT 1089
Cdd:cd14612    154 DHQTPESAGPLLRLVAEVEESRqtAASPGPIVVHCSAGIGRTGCFIATSIGCQQLKDTGKVDILGIVCQLRLDRGGMIQT 233
                          250
                   ....*....|.
gi 1925147141 1090 EEQYVFIHDAL 1100
Cdd:cd14612    234 SEQYQFLHHTL 244
R-PTPc-Q cd14616
catalytic domain of receptor-type tyrosine-protein phosphatase Q; Receptor-type ...
870-1097 6.01e-58

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: 199.75  E-value: 6.01e-58
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1925147141  870 NRYINIMAYDHSRVKLLEEG--KGGDYINANFVDGFERTRAYIAAQGPLKSGTEDFWRMVWQENVGVIVMITNLLEKGRR 947
Cdd:cd14616      1 NRFPNIKPYNNNRVKLIADAgvPGSDYINASYISGYLCPNEFIATQGPLPGTVGDFWRMVWETRAKTIVMLTQCFEKGRI 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1925147141  948 KCDQYWPMENQ--EEYGHFLVTLKDTKTLAYYTLRTFtlrdtsqKASQRGRCAerTVVQYHYTQWPDMGVPEYTLPVLSF 1025
Cdd:cd14616     81 RCHQYWPEDNKpvTVFGDIVITKLMEDVQIDWTIRDL-------KIERHGDYM--MVRQCNFTSWPEHGVPESSAPLIHF 151
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1925147141 1026 VRASTQARTQDMGPVLVHCSAGVGRTGTYIVLDSMLQQIQDQGTVNILGFLKHVRTQRNYLVQTEEQYVFIH 1097
Cdd:cd14616    152 VKLVRASRAHDNTPMIVHCSAGVGRTGVFIALDHLTQHINDHDFVDIYGLVAELRSERMCMVQNLAQYIFLH 223
PTPc-N12 cd14604
catalytic domain of tyrosine-protein phosphatase non-receptor type 12; Tyrosine-protein ...
824-1102 4.41e-57

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: 200.16  E-value: 4.41e-57
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1925147141  824 VKQFVKHVAELHQT-----NTFSKEFEEVQSCTV----EMGITTDSSNHPDNKNKNRYINIMAYDHSRVKLL--EEGKGG 892
Cdd:cd14604      6 LKKFIERVQAMKSTdhngeDNFASDFMRLRRLSTkyrtEKIYPTATGEKEENVKKNRYKDILPFDHSRVKLTlkTSSQDS 85
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1925147141  893 DYINANFVDGFERTRAYIAAQGPLKSGTEDFWRMVWQENVGVIVMITNLLEKGRRKCDQYWPMENQE--EYGHFLVTLKD 970
Cdd:cd14604     86 DYINANFIKGVYGPKAYIATQGPLANTVIDFWRMIWEYNVAIIVMACREFEMGRKKCERYWPLYGEEpmTFGPFRISCEA 165
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1925147141  971 TKTLAYYTLRTFTLRDTSQKasqrgrcaeRTVVQYHYTQWPDMGVPEYTLPVLSFVRASTQARTQDMGPVLVHCSAGVGR 1050
Cdd:cd14604    166 EQARTDYFIRTLLLEFQNET---------RRLYQFHYVNWPDHDVPSSFDSILDMISLMRKYQEHEDVPICIHCSAGCGR 236
                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1925147141 1051 TGTYIVLD---SMLQQIQDQGTVNILGFLKHVRTQRNYLVQTEEQYVFIHDALVE 1102
Cdd:cd14604    237 TGAICAIDytwNLLKAGKIPEEFNVFNLIQEMRTQRHSAVQTKEQYELVHRAIAQ 291
alpha_CA_IV_XV_like cd03117
Carbonic anhydrase alpha, CA_IV, CA_XV, like isozymes. Carbonic anhydrases (CAs) are ...
63-293 1.08e-56

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: 196.34  E-value: 1.08e-56
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1925147141   63 RQSPIDIDETFTQVRVEYQGLQLEGWEKNTPeTTTINNDGNTVVLGLDGEYYVSGGGLSTRFRLGRMTFHWGrcNASSDG 142
Cdd:cd03117      3 RQSPINIVTKKVQYDENLTPFTFTGYDDTTT-NWTITNNGHTVQVTLPDGAKISGGGLPGTYKALQFHFHWG--SNGSPG 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1925147141  143 SEHSLNGLKFPLEMQILCYESGlYQSIDDAVRDGGRIAALAVLFETSLDNNDNYNTILEGVNSVNRFGKTGNVEPFSLLA 222
Cdd:cd03117     80 SEHTIDGERYPMELHIVHIKES-YNSLLEALKDSDGLAVLGFFIEEGEEENTNFDPLISALSNIPQKGGSTNLTPFSLRS 158
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1925147141  223 LLP-NSTDKYYTYNGSLTSPPCSETVEWIVFKHTVPISETQLEVFCEVMTMQQAGYVMLMdylqNNFREQQQ 293
Cdd:cd03117    159 LLPsVLLTKYYRYNGSLTTPGCNEAVIWTVFEEPIPISRAQLDAFSTVLFFDTDNGQPMV----NNFRPVQP 226
PTPc-N5 cd14613
catalytic domain of tyrosine-protein phosphatase non-receptor type 5; Tyrosine-protein ...
869-1100 1.67e-56

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: 197.01  E-value: 1.67e-56
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1925147141  869 KNRYINIMAYDHSRVKLLEEGKG---GDYINANFVDGF-ERTRAYIAAQGPLKSGTEDFWRMVWQENVGVIVMITNLLEK 944
Cdd:cd14613     28 KNRYKTILPNPHSRVCLTSPDQDdplSSYINANYIRGYgGEEKVYIATQGPTVNTVGDFWRMVWQERSPIIVMITNIEEM 107
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1925147141  945 GRrKCDQYWPmENQEEYGHFLVTLKDTKTLAYYTLRTFTLRDTSQkasqrgrcaERTVVQYHYTQWPDMGVPEYTLPVLS 1024
Cdd:cd14613    108 NE-KCTEYWP-EEQVTYEGIEITVKQVIHADDYRLRLITLKSGGE---------ERGLKHYWYTSWPDQKTPDNAPPLLQ 176
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1925147141 1025 FVRASTQARTQ---DMGPVLVHCSAGVGRTGTYIVLDSMLQQIQDQGTVNILGFLKHVRTQRNYLVQTEEQYVFIHDAL 1100
Cdd:cd14613    177 LVQEVEEARQQaepNCGPVIVHCSAGIGRTGCFIATSICCKQLRNEGVVDILRTTCQLRLDRGGMIQTCEQYQFVHHVL 255
PTPc-N22 cd14602
catalytic domain of tyrosine-protein phosphatase non-receptor type 22; Tyrosine-protein ...
869-1102 1.84e-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: 1.84e-56
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1925147141  869 KNRYINIMAYDHSRVKL--LEEGKGGDYINANFVDGFERTRAYIAAQGPLKSGTEDFWRMVWQENVGVIVMITNLLEKGR 946
Cdd:cd14602      1 KNRYKDILPYDHSRVELslITSDEDSDYINANFIKGVYGPRAYIATQGPLSTTLLDFWRMIWEYSVLIIVMACMEFEMGK 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1925147141  947 RKCDQYW--PMENQEEYGHFLVTLKDTKTLAYYTLRtfTLRDTSQKASqrgrcaeRTVVQYHYTQWPDMGVPEYTLPVLS 1024
Cdd:cd14602     81 KKCERYWaePGEMQLEFGPFSVTCEAEKRKSDYIIR--TLKVKFNSET-------RTIYQFHYKNWPDHDVPSSIDPILE 151
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1925147141 1025 FVRASTQARTQDMGPVLVHCSAGVGRTGTYIVLDSMLQQIQDqGTV----NILGFLKHVRTQRNYLVQTEEQYVFIHDAL 1100
Cdd:cd14602    152 LIWDVRCYQEDDSVPICIHCSAGCGRTGVICAIDYTWMLLKD-GIIpenfSVFSLIQEMRTQRPSLVQTKEQYELVYNAV 230

                   ..
gi 1925147141 1101 VE 1102
Cdd:cd14602    231 IE 232
PTPc-N22_18_12 cd14542
catalytic domain of tyrosine-protein phosphatase non-receptor type 22, type 18 and type 12; ...
894-1097 4.83e-56

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


Pssm-ID: 350390 [Multi-domain]  Cd Length: 202  Bit Score: 193.41  E-value: 4.83e-56
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1925147141  894 YINANFVDGFERTRAYIAAQGPLKSGTEDFWRMVWQENVGVIVMITNLLEKGRRKCDQYWP--MENQEEYGHFLVTLKDT 971
Cdd:cd14542      1 YINANFIKGVSGSKAYIATQGPLPNTVLDFWRMIWEYNVQVIVMACREFEMGKKKCERYWPeeGEEQLQFGPFKISLEKE 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1925147141  972 KTLAY-YTLRTFTLRDTSQkasqrgrcaERTVVQYHYTQWPDMGVPEYTLPVLSFVRASTQARTQDMGPVLVHCSAGVGR 1050
Cdd:cd14542     81 KRVGPdFLIRTLKVTFQKE---------SRTVYQFHYTAWPDHGVPSSVDPILDLVRLVRDYQGSEDVPICVHCSAGCGR 151
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|
gi 1925147141 1051 TGTYIVLDSMLQQIQDQG---TVNILGFLKHVRTQRNYLVQTEEQYVFIH 1097
Cdd:cd14542    152 TGTICAIDYVWNLLKTGKipeEFSLFDLVREMRKQRPAMVQTKEQYELVY 201
R-PTPc-A-E-2 cd14552
catalytic domain of receptor-type tyrosine-protein phosphatase A and E, repeat 2; ...
894-1101 5.61e-56

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


Pssm-ID: 350400 [Multi-domain]  Cd Length: 202  Bit Score: 193.25  E-value: 5.61e-56
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1925147141  894 YINANFVDGFERTRAYIAAQGPLKSGTEDFWRMVWQENVGVIVMITNLLEKGRRKCDQYWPMENQEEYGHFLVTLKDTKT 973
Cdd:cd14552      1 YINASFIDGYRQKDAYIATQGPLDHTVEDFWRMIWEWKSCSIVMLTEIKERSQNKCAQYWPEDGSVSSGDITVELKDQTD 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1925147141  974 LAYYTLRTFTLRDTSQKASqrgrcaeRTVVQYHYTQWPDMGVPEYTLPVLSFVrASTQARTQDMG--PVLVHCSAGVGRT 1051
Cdd:cd14552     81 YEDYTLRDFLVTKGKGGST-------RTVRQFHFHGWPEVGIPDNGKGMIDLI-AAVQKQQQQSGnhPITVHCSAGAGRT 152
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|
gi 1925147141 1052 GTYIVLDSMLQQIQDQGTVNILGFLKHVRTQRNYLVQTEEQYVFIHDALV 1101
Cdd:cd14552    153 GTFCALSTVLERVKAEGVLDVFQVVKSLRLQRPHMVQTLEQYEFCYKVVQ 202
PTPc-N20_13 cd14538
catalytic domain of tyrosine-protein phosphatase non-receptor type 20 and type 13; ...
894-1104 1.47e-55

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: 192.20  E-value: 1.47e-55
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1925147141  894 YINANFV--DGFERTRAYIAAQGPLKSGTEDFWRMVWQENVGVIVMITNLLEKGRRKCDQYWP---MENQEEYGHFLVTL 968
Cdd:cd14538      1 YINASHIriPVGGDTYHYIACQGPLPNTTGDFWQMVWEQKSEVIAMVTQDVEGGKVKCHRYWPdslNKPLICGGRLEVSL 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1925147141  969 KDTKTLAYYTLRTFTLRDTSQKASqrgrcaeRTVVQYHYTQWPDMGVPEYTLPVLSFVRASTqaRTQDMGPVLVHCSAGV 1048
Cdd:cd14538     81 EKYQSLQDFVIRRISLRDKETGEV-------HHITHLNFTTWPDHGTPQSADPLLRFIRYMR--RIHNSGPIVVHCSAGI 151
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 1925147141 1049 GRTGTYIVLDSMLQQIQDQGTVNILGFLKHVRTQRNYLVQTEEQYVFIHDALVEAI 1104
Cdd:cd14538    152 GRTGVLITIDVALGLIERDLPFDIQDIVKDLREQRQGMIQTKDQYIFCYKACLEVL 207
PTPc-N1 cd14608
catalytic domain of tyrosine-protein phosphatase non-receptor type 1; Tyrosine-protein ...
861-1102 5.61e-55

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: 193.32  E-value: 5.61e-55
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1925147141  861 SNHPDNKNKNRYINIMAYDHSRVKLLEEGKggDYINANFVDGFERTRAYIAAQGPLKSGTEDFWRMVWQENVGVIVMITN 940
Cdd:cd14608     20 AKLPKNKNRNRYRDVSPFDHSRIKLHQEDN--DYINASLIKMEEAQRSYILTQGPLPNTCGHFWEMVWEQKSRGVVMLNR 97
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1925147141  941 LLEKGRRKCDQYWPMENQEEY----GHFLVTLKDTKTLAYYTLRTFTLRDTSQKASqrgrcaeRTVVQYHYTQWPDMGVP 1016
Cdd:cd14608     98 VMEKGSLKCAQYWPQKEEKEMifedTNLKLTLISEDIKSYYTVRQLELENLTTQET-------REILHFHYTTWPDFGVP 170
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1925147141 1017 EYTLPVLSF---VRASTqARTQDMGPVLVHCSAGVGRTGTYIVLDS---MLQQIQDQGTVNILGFLKHVRTQRNYLVQTE 1090
Cdd:cd14608    171 ESPASFLNFlfkVRESG-SLSPEHGPVVVHCSAGIGRSGTFCLADTcllLMDKRKDPSSVDIKKVLLEMRKFRMGLIQTA 249
                          250
                   ....*....|..
gi 1925147141 1091 EQYVFIHDALVE 1102
Cdd:cd14608    250 DQLRFSYLAVIE 261
PTPc-N3_4 cd14541
catalytic domain of tyrosine-protein phosphatase non-receptor type 21 and type 14; ...
893-1103 5.89e-55

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: 190.62  E-value: 5.89e-55
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1925147141  893 DYINANFVD----GFERTRAYIAAQGPLKSGTEDFWRMVWQENVGVIVMITNLLEKGRRKCDQYWP-MENQEEYGHFLVT 967
Cdd:cd14541      1 DYINANYVNmeipGSGIVNRYIAAQGPLPNTCADFWQMVWEQKSTLIVMLTTLVERGRVKCHQYWPdLGETMQFGNLQIT 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1925147141  968 LKDTKTLAYYTLRTFTLRDTSQKAsqrgrcaERTVVQYHYTQWPDMGVPEYTLPVLSFVRASTQARTQDMGPVLVHCSAG 1047
Cdd:cd14541     81 CVSEEVTPSFAFREFILTNTNTGE-------ERHITQMQYLAWPDHGVPDDSSDFLDFVKRVRQNRVGMVEPTVVHCSAG 153
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 1925147141 1048 VGRTGTYIVLDSMLQQIQDQGTVNILGFLKHVRTQRNYLVQTEEQYVFIHDALVEA 1103
Cdd:cd14541    154 IGRTGVLITMETAMCLIEANEPVYPLDIVRTMRDQRAMLIQTPSQYRFVCEAILRV 209
PHA02738 PHA02738
hypothetical protein; Provisional
819-1116 1.64e-54

hypothetical protein; Provisional


Pssm-ID: 222923 [Multi-domain]  Cd Length: 320  Bit Score: 193.22  E-value: 1.64e-54
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1925147141  819 HEALSVKQFVKHVAELHQTNTFSKEFEEVQSCTVEMGITTDSSNhpdnKNKNRYINIMAYDHSRVKLLEEGKGGDYINAN 898
Cdd:PHA02738     6 FRELKYAEFLALMEKSDCEEVITREHQKVISEKVDGTFNAEKKN----RKLNRYLDAVCFDHSRVILPAERNRGDYINAN 81
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1925147141  899 FVDGFERTRAYIAAQGPLKSGTEDFWRMVWQENVGVIVMITNLLEKGRRKCDQYWPMENQEE--YGHFLVTLKDTKTLAY 976
Cdd:PHA02738    82 YVDGFEYKKKFICGQAPTRQTCYDFYRMLWMEHVQIIVMLCKKKENGREKCFPYWSDVEQGSirFGKFKITTTQVETHPH 161
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1925147141  977 YTLRTFTLRDtsqkasqrGRCAERTVVQYHYTQWPDMGVPEYTLPVLSFVRASTQARTQ------DMG-------PVLVH 1043
Cdd:PHA02738   162 YVKSTLLLTD--------GTSATQTVTHFNFTAWPDHDVPKNTSEFLNFVLEVRQCQKElaqeslQIGhnrlqppPIVVH 233
                          250       260       270       280       290       300       310
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1925147141 1044 CSAGVGRTGTYIVLDSMLQQIQDQGTVNILGFLKHVRTQRNYLVQTEEQYVFIHDALVEAIVSRDTLVTSDLV 1116
Cdd:PHA02738   234 CNAGLGRTPCYCVVDISISRFDACATVSIPSIVSSIRNQRYYSLFIPFQYFFCYRAVKRYVNLTVNKVSKKLI 306
alpha_CA_VI_IX_XII_XIV cd03123
Carbonic anhydrase alpha, isozymes VI, IX, XII and XIV. Carbonic anhydrases (CAs) are ...
49-303 5.58e-54

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: 189.06  E-value: 5.58e-54
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1925147141   49 QKIWGKRYPACNNARQSPIDIDETFTQVRVEYQGLQLEGWEKNTPETTTINNDGNTVVLGLDGEYYVsGGGLSTRFRLGR 128
Cdd:cd03123      2 EDHWPKKYPACGGKRQSPIDIQTDIVQFDPSLPPLELVGYDLPGTEEFTLTNNGHTVQLSLPPTMHI-RGGPGTEYTAAQ 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1925147141  129 MTFHWGRCNASSdGSEHSLNGLKFPLEMQILCYESGLYQSIDDAVRDGGRIAALAVLFETSLDNNDNYNTILEGVNSVNR 208
Cdd:cd03123     81 LHLHWGGRGSLS-GSEHTIDGIRFAAELHIVHYNSDKYSSFDEAADKPDGLAVLAILIEVGYPENTYYEKIISHLHEIKY 159
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1925147141  209 FGKTGNVEPFSLLALLPNSTDKYYTYNGSLTSPPCSETVEWIVFKHTVPISETQLEvfcevmTMQQAgyvmLMDY----L 284
Cdd:cd03123    160 KGQETTVPGFNVRELLPEDLSHYYRYEGSLTTPPCYESVLWTVFRDPVTLSKEQLE------TLENT----LMDThnktL 229
                          250       260
                   ....*....|....*....|.
gi 1925147141  285 QNNFReqQQQFLGQ--VFSSY 303
Cdd:cd03123    230 QNNYR--ATQPLNGrvVEASF 248
PTPc-N2 cd14607
catalytic domain of tyrosine-protein phosphatase non-receptor type 2; Tyrosine-protein ...
861-1100 7.05e-54

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: 189.41  E-value: 7.05e-54
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1925147141  861 SNHPDNKNKNRYINIMAYDHSRVKLleEGKGGDYINANFVDGFERTRAYIAAQGPLKSGTEDFWRMVWQENVGVIVMITN 940
Cdd:cd14607     19 AKYPENRNRNRYRDVSPYDHSRVKL--QNTENDYINASLVVIEEAQRSYILTQGPLPNTCCHFWLMVWQQKTKAVVMLNR 96
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1925147141  941 LLEKGRRKCDQYWPMENQEEYGH----FLVTLKDTKTLAYYTLRTFTLRDTSQKASqrgrcaeRTVVQYHYTQWPDMGVP 1016
Cdd:cd14607     97 IVEKDSVKCAQYWPTDEEEVLSFketgFSVKLLSEDVKSYYTVHLLQLENINSGET-------RTISHFHYTTWPDFGVP 169
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1925147141 1017 EYTLPVLSFVRASTQARTQDM--GPVLVHCSAGVGRTGTYIVLDS--MLQQIQDQGTVNILGFLKHVRTQRNYLVQTEEQ 1092
Cdd:cd14607    170 ESPASFLNFLFKVRESGSLSPehGPAVVHCSAGIGRSGTFSLVDTclVLMEKKDPDSVDIKQVLLDMRKYRMGLIQTPDQ 249

                   ....*...
gi 1925147141 1093 YVFIHDAL 1100
Cdd:cd14607    250 LRFSYMAV 257
R-PTP-N cd14609
PTP-like domain of receptor-type tyrosine-protein phosphatase N; Receptor-type ...
834-1104 1.19e-53

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: 189.48  E-value: 1.19e-53
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1925147141  834 LHQTNTFSKEFEEVQSCTVEMGiTTDSSNHPDNKNKNRYINIMAYDHSRVKLLEEGK--GGDYINAN-FVDGFERTRAYI 910
Cdd:cd14609     11 LRNRDRLAKEWQALCAYQAEPN-TCSTAQGEANVKKNRNPDFVPYDHARIKLKAESNpsRSDYINASpIIEHDPRMPAYI 89
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1925147141  911 AAQGPLKSGTEDFWRMVWQENVGVIVMITNLLEKGRRKCDQYWPMENQEEYGHFLVTLKDTKTLAY-YTLRTFTLRDTSQ 989
Cdd:cd14609     90 ATQGPLSHTIADFWQMVWENGCTVIVMLTPLVEDGVKQCDRYWPDEGSSLYHIYEVNLVSEHIWCEdFLVRSFYLKNVQT 169
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1925147141  990 KASqrgrcaeRTVVQYHYTQWPDMGVPEYTLPVLSFVRASTQARTQDMGPVLVHCSAGVGRTGTYIVLDSMLQQI-QDQG 1068
Cdd:cd14609    170 QET-------RTLTQFHFLSWPAEGIPSSTRPLLDFRRKVNKCYRGRSCPIIVHCSDGAGRTGTYILIDMVLNRMaKGVK 242
                          250       260       270
                   ....*....|....*....|....*....|....*.
gi 1925147141 1069 TVNILGFLKHVRTQRNYLVQTEEQYVFIHDALVEAI 1104
Cdd:cd14609    243 EIDIAATLEHVRDQRPGMVRTKDQFEFALTAVAEEV 278
R-PTP-N2 cd14610
PTP-like domain of receptor-type tyrosine-protein phosphatase N2; Receptor-type ...
834-1104 5.64e-53

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: 187.57  E-value: 5.64e-53
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1925147141  834 LHQTNTFSKEFEEVQSCTVEMGITTdSSNHPDNKNKNRYINIMAYDHSRVKLLEEGK--GGDYINAN-FVDGFERTRAYI 910
Cdd:cd14610     13 LKNKNRLEKEWEALCAYQAEPNATN-VAQREENVQKNRSLAVLPYDHSRIILKAENShsHSDYINASpIMDHDPRNPAYI 91
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1925147141  911 AAQGPLKSGTEDFWRMVWQENVGVIVMITNLLEKGRRKCDQYWPMENQEEYGHFLVTLKDTKTLAY-YTLRTFTLRDTSQ 989
Cdd:cd14610     92 ATQGPLPATVADFWQMVWESGCVVIVMLTPLAENGVKQCYHYWPDEGSNLYHIYEVNLVSEHIWCEdFLVRSFYLKNLQT 171
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1925147141  990 KASqrgrcaeRTVVQYHYTQWPDMGVPEYTLPVLSFVRASTQARTQDMGPVLVHCSAGVGRTGTYIVLDSMLQQI-QDQG 1068
Cdd:cd14610    172 NET-------RTVTQFHFLSWNDQGVPASTRSLLDFRRKVNKCYRGRSCPIIVHCSDGAGRSGTYILIDMVLNKMaKGAK 244
                          250       260       270
                   ....*....|....*....|....*....|....*.
gi 1925147141 1069 TVNILGFLKHVRTQRNYLVQTEEQYVFIHDALVEAI 1104
Cdd:cd14610    245 EIDIAATLEHLRDQRPGMVQTKEQFEFALTAVAEEV 280
R-PTPc-R cd14611
catalytic domain of receptor-type tyrosine-protein phosphatase R; Receptor-type ...
869-1097 1.10e-52

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


Pssm-ID: 350459 [Multi-domain]  Cd Length: 226  Bit Score: 184.74  E-value: 1.10e-52
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1925147141  869 KNRYINIMAYDHSRVKLLEEGKG---GDYINANFVDGFE-RTRAYIAAQGPLKSGTEDFWRMVWQENVGVIVMITNLLEK 944
Cdd:cd14611      2 KNRYKTILPNPHSRVCLKPKNSNdslSTYINANYIRGYGgKEKAFIATQGPMINTVNDFWQMVWQEDSPVIVMITKLKEK 81
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1925147141  945 GRrKCDQYWPmENQEEYGHFLVTLKDTKTLAYYTLRTFTLRDTSQKasqrgrcaeRTVVQYHYTQWPDMGVPEYTLPVLS 1024
Cdd:cd14611     82 NE-KCVLYWP-EKRGIYGKVEVLVNSVKECDNYTIRNLTLKQGSQS---------RSVKHYWYTSWPDHKTPDSAQPLLQ 150
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1925147141 1025 FVRASTQAR--TQDMGPVLVHCSAGVGRTGTYIVLDSMLQQIQDQGTVNILGFLKHVRTQRNYLVQTEEQYVFIH 1097
Cdd:cd14611    151 LMLDVEEDRlaSPGRGPVVVHCSAGIGRTGCFIATTIGCQQLKEEGVVDVLSIVCQLRVDRGGMVQTSEQYEFVH 225
R-PTPc-A-2 cd14623
catalytic domain of receptor-type tyrosine-protein phosphatase A, repeat 2; Receptor-type ...
871-1102 1.21e-52

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: 184.48  E-value: 1.21e-52
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1925147141  871 RYINIMAYDHSRVKL-LEEGK-GGDYINANFVDGFERTRAYIAAQGPLKSGTEDFWRMVWQENVGVIVMITNLLEKGRRK 948
Cdd:cd14623      1 RVLQIIPYEFNRVIIpVKRGEeNTDYVNASFIDGYRQKDSYIASQGPLQHTIEDFWRMIWEWKSCSIVMLTELEERGQEK 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1925147141  949 CDQYWPMENQEEYGHFLVTLKDTKTLAYYTLRTFTLRDTSQKASqrgrcaeRTVVQYHYTQWPDMGVPEYTLPVLSFVrA 1028
Cdd:cd14623     81 CAQYWPSDGSVSYGDITIELKKEEECESYTVRDLLVTNTRENKS-------RQIRQFHFHGWPEVGIPSDGKGMINII-A 152
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1925147141 1029 STQARTQDMG--PVLVHCSAGVGRTGTYIVLDSMLQQIQDQGTVNILGFLKHVRTQRNYLVQTEEQYVFIHDALVE 1102
Cdd:cd14623    153 AVQKQQQQSGnhPITVHCSAGAGRTGTFCALSTVLERVKAEGILDVFQTVKSLRLQRPHMVQTLEQYEFCYKVVQE 228
PTPc-N3 cd14600
catalytic domain of tyrosine-protein phosphatase non-receptor type 3; Tyrosine-protein ...
836-1101 1.63e-52

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: 185.82  E-value: 1.63e-52
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1925147141  836 QTNTFSKEFEEVQSCTVEMGITTdsSNHPDNKNKNRYINIMAYDHSRVkLLEEGKggDYINANFVD----GFERTRAYIA 911
Cdd:cd14600     12 ESGTVLIQFEQLYRKKPGLAITC--AKLPQNMDKNRYKDVLPYDATRV-VLQGNE--DYINASYVNmeipSANIVNKYIA 86
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1925147141  912 AQGPLKSGTEDFWRMVWQENVGVIVMITNLLEKGRRKCDQYWP-MENQEEYGHFLVTLKDTKTLAYYTLRTFTLRDTsqk 990
Cdd:cd14600     87 TQGPLPHTCAQFWQVVWEQKLSLIVMLTTLTERGRTKCHQYWPdPPDVMEYGGFRVQCHSEDCTIAYVFREMLLTNT--- 163
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1925147141  991 asQRGRcaERTVVQYHYTQWPDMGVPEYTLPVLSFVRASTQARtQDMGPVLVHCSAGVGRTGTYIVLDSMLQQIQDQGTV 1070
Cdd:cd14600    164 --QTGE--ERTVTHLQYVAWPDHGVPDDSSDFLEFVNYVRSKR-VENEPVLVHCSAGIGRTGVLVTMETAMCLTERNQPV 238
                          250       260       270
                   ....*....|....*....|....*....|.
gi 1925147141 1071 NILGFLKHVRTQRNYLVQTEEQYVFIHDALV 1101
Cdd:cd14600    239 YPLDIVRKMRDQRAMMVQTSSQYKFVCEAIL 269
PTPc-N21_14 cd14540
catalytic domain of tyrosine-protein phosphatase non-receptor type 21 and type 14; ...
894-1102 6.22e-52

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: 182.27  E-value: 6.22e-52
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1925147141  894 YINANFVDGFE--RTRAYIAAQGPLKSGTEDFWRMVWQENVGVIVMITNLLEKGRRKCDQYWPMENQEE----YGHFLVT 967
Cdd:cd14540      1 YINASHITATVggKQRFYIAAQGPLQNTVGDFWQMVWEQGVYLVVMVTAEEEGGREKCFRYWPTLGGEHdaltFGEYKVS 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1925147141  968 LKDTKTLAYYTLRTFTLRDTSQkasqrgrCAERTVVQYHYTQWPDMGVPEYTLPVLSF---VRASTQARTQDMG------ 1038
Cdd:cd14540     81 TKFSVSSGCYTTTGLRVKHTLS-------GQSRTVWHLQYTDWPDHGCPEDVSGFLDFleeINSVRRHTNQDVAghnrnp 153
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1925147141 1039 PVLVHCSAGVGRTGTYIVLDSMLQQIQDQGTVNILGFLKHVRTQRNYLVQTEEQYVFIHDALVE 1102
Cdd:cd14540    154 PTLVHCSAGVGRTGVVILADLMLYCLDHNEELDIPRVLALLRHQRMLLVQTLAQYKFVYNVLIQ 217
R-PTPc-E-2 cd14622
catalytic domain of receptor-type tyrosine-protein phosphatase E, repeat 2; Receptor-type ...
893-1097 4.97e-51

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: 179.05  E-value: 4.97e-51
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1925147141  893 DYINANFVDGFERTRAYIAAQGPLKSGTEDFWRMVWQENVGVIVMITNLLEKGRRKCDQYWPMENQEEYGHFLVTLKDTK 972
Cdd:cd14622      1 DYINASFIDGYRQKDYFIATQGPLAHTVEDFWRMVWEWKCHTIVMLTELQEREQEKCVQYWPSEGSVTHGEITIEIKNDT 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1925147141  973 TLAYYTLRTFTLRDTSQKASqrgrcaeRTVVQYHYTQWPDMGVPEYTLPVLSFVrASTQARTQDMG--PVLVHCSAGVGR 1050
Cdd:cd14622     81 LLETISIRDFLVTYNQEKQT-------RLVRQFHFHGWPEIGIPAEGKGMIDLI-AAVQKQQQQTGnhPIVVHCSAGAGR 152
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*..
gi 1925147141 1051 TGTYIVLDSMLQQIQDQGTVNILGFLKHVRTQRNYLVQTEEQYVFIH 1097
Cdd:cd14622    153 TGTFIALSNILERVKAEGLLDVFQTVKSLRLQRPHMVQTLEQYEFCY 199
R-PTP-N-N2 cd14546
PTP-like domain of receptor-type tyrosine-protein phosphatase-like N and N2; Receptor-type ...
894-1104 9.46e-50

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: 175.33  E-value: 9.46e-50
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1925147141  894 YINANFV-DGFERTRAYIAAQGPLKSGTEDFWRMVWQENVGVIVMITNLLEKGRRKCDQYWPMENQEEYGHFLVTLKDTK 972
Cdd:cd14546      1 YINASTIyDHDPRNPAYIATQGPLPHTIADFWQMIWEQGCVVIVMLTRLQENGVKQCARYWPEEGSEVYHIYEVHLVSEH 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1925147141  973 TL-AYYTLRTFTLRD--TSQKasqrgrcaeRTVVQYHYTQWPDMGVPEYTLPVLSFVRASTQARTQDMGPVLVHCSAGVG 1049
Cdd:cd14546     81 IWcDDYLVRSFYLKNlqTSET---------RTVTQFHFLSWPDEGIPASAKPLLEFRRKVNKSYRGRSCPIVVHCSDGAG 151
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 1925147141 1050 RTGTYIVLDSMLQQIQdQGT--VNILGFLKHVRTQRNYLVQTEEQYVFIHDALVEAI 1104
Cdd:cd14546    152 RTGTYILIDMVLNRMA-KGAkeIDIAATLEHLRDQRPGMVKTKDQFEFVLTAVAEEV 207
PTPc-N13 cd14597
catalytic domain of tyrosine-protein phosphatase non-receptor type 13; Tyrosine-protein ...
865-1095 7.27e-49

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: 173.86  E-value: 7.27e-49
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1925147141  865 DNKNKNRYINIMAYDHSRVKLleeGKGGDYINANFVD---GFERTrAYIAAQGPLKSGTEDFWRMVWQENVGVIVMITNL 941
Cdd:cd14597      2 ENRKKNRYKNILPYDTTRVPL---GDEGGYINASFIKmpvGDEEF-VYIACQGPLPTTVADFWQMVWEQKSTVIAMMTQE 77
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1925147141  942 LEKGRRKCDQYWPmenqEEYGHFL-------VTLKDTKTLAYYTLRTFTLRDTSQKASQRgrcaertVVQYHYTQWPDMG 1014
Cdd:cd14597     78 VEGGKIKCQRYWP----EILGKTTmvdnrlqLTLVRMQQLKNFVIRVLELEDIQTREVRH-------ITHLNFTAWPDHD 146
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1925147141 1015 VPEYTLPVLSFVraSTQARTQDMGPVLVHCSAGVGRTGTYIVLDSMLQQIQDQGTVNILGFLKHVRTQRNYLVQTEEQYV 1094
Cdd:cd14597    147 TPSQPEQLLTFI--SYMRHIHKSGPIITHCSAGIGRSGTLICIDVVLGLISKDLDFDISDIVRTMRLQRHGMVQTEDQYI 224

                   .
gi 1925147141 1095 F 1095
Cdd:cd14597    225 F 225
R-PTP-C-2 cd14558
PTP-like domain of receptor-type tyrosine-protein phosphatase C, repeat 2; Receptor-type ...
894-1098 2.30e-47

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: 168.34  E-value: 2.30e-47
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1925147141  894 YINANFVDGFERTRAYIAAQGPLKSGTEDFWRMVWQENVGVIVMITNLLEKGRRKCDQYWPmENQEEYGHFLVTLKDTKT 973
Cdd:cd14558      1 YINASFIDGYWGPKSLIATQGPLPDTIADFWQMIFQKKVKVIVMLTELKEGDQEQCAQYWG-DEKKTYGDIEVELKDTEK 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1925147141  974 LAYYTLRTFTLRDTSQKASqrgrcaeRTVVQYHYTQWPDMGVPEYTLPVLSFVRA------STQARTQDMGPVLVHCSAG 1047
Cdd:cd14558     80 SPTYTVRVFEITHLKRKDS-------RTVYQYQYHKWKGEELPEKPKDLVDMIKSikqklpYKNSKHGRSVPIVVHCSDG 152
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|.
gi 1925147141 1048 VGRTGTYIVLDSMLQQIQDQGTVNILGFLKHVRTQRNYLVQTEEQYVFIHD 1098
Cdd:cd14558    153 SSRTGIFCALWNLLESAETEKVVDVFQVVKALRKQRPGMVSTLEQYQFLYD 203
alpha_CA_XII_XIV cd03126
Carbonic anhydrase alpha, isozymes XII and XIV. Carbonic anhydrases (CAs) are zinc-containing ...
49-303 6.88e-47

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: 168.86  E-value: 6.88e-47
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1925147141   49 QKIWGKRYPACNNARQSPIDIDETFTQVRVEYQGLQLEGWEKNTPETTTINNDGNTVVLGLDGEYYVsgGGLSTRFRLGR 128
Cdd:cd03126      2 ENSWPKKYPFCGGVAQSPIDIHTDILQYDSSLPPLEFHGYNVSGTEQFTLTNNGHTVQLSLPPTMHI--GGLPFKYTASQ 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1925147141  129 MTFHWGRCNaSSDGSEHSLNGLKFPLEMQILCYESGLYQSIDDAVRDGGRIAALAVLFETSlDNNDNYNTILEGVNSVNR 208
Cdd:cd03126     80 LHLHWGQRG-SPEGSEHTISGKHFAAELHIVHYNSDKYPDISTAMNKSQGLAVLGILIEVG-PFNPSYEKIFSHLHEVKY 157
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1925147141  209 FGKTGNVEPFSLLALLPNSTDKYYTYNGSLTSPPCSETVEWIVFKHTVPISETQLEvfcevmTMQQAGYVMLMD---YLQ 285
Cdd:cd03126    158 KDQKVSVPGFNVQELLPKRLDEYYRYEGSLTTPPCYPSVLWTVFRNPVQISQEQLL------ALETALYSTEEDesrEMV 231
                          250       260
                   ....*....|....*....|
gi 1925147141  286 NNFReqQQQFLGQ--VFSSY 303
Cdd:cd03126    232 NNYR--QVQPFNErlVFASF 249
PTPc cd00047
catalytic domain of protein tyrosine phosphatases; Protein tyrosine phosphatases (PTP, EC 3.1. ...
1189-1392 2.55e-46

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: 165.15  E-value: 2.55e-46
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1925147141 1189 YINASYIMGYHKSREFILTQSPLPSTVSDFWRMVWDHNSQLIISLpdthTAQRE-GEESCA-YWPSK-DQPISCEGFIVS 1265
Cdd:cd00047      1 YINASYIDGYRGPKEYIATQGPLPNTVEDFWRMVWEQKVSVIVML----TNLVEkGREKCErYWPEEgGKPLEYGDITVT 76
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1925147141 1266 FSGEDHMclaneERLVVHDFLLEATQDNYVLEVRQYMSPCWPN---PDSPvSGTFQLLNIITEDSRQREGTIVVHDRLGG 1342
Cdd:cd00047     77 LVSEEEL-----SDYTIRTLELSPKGCSESREVTHLHYTGWPDhgvPSSP-EDLLALVRRVRKEARKPNGPIVVHCSAGV 150
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|
gi 1925147141 1343 SVAGLFCALTTLAQQLEHQGSVDVYQVARMTNLMRPGVFNDMEQYQFMYR 1392
Cdd:cd00047    151 GRTGTFIAIDILLERLEAEGEVDVFEIVKALRKQRPGMVQTLEQYEFIYE 200
PTP-N23 cd14539
PTP-like domain of tyrosine-protein phosphatase non-receptor type 23; Tyrosine-protein ...
894-1098 5.42e-46

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: 164.48  E-value: 5.42e-46
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1925147141  894 YINANFVDGFERTRA-YIAAQGPLKSGTEDFWRMVWQENVGVIVMITNLLEKGRRKCDQYWPME--NQEEYGHFLVTLKD 970
Cdd:cd14539      1 YINASLIEDLTPYCPrFIATQAPLPGTAADFWLMVYEQQVSVIVMLVSEQENEKQKVHRYWPTErgQALVYGAITVSLQS 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1925147141  971 TKTLAYYTLRTFTL--RDTSQKasqrgrcaeRTVVQYHYTQWPDMGVPEYTLPVLSF---VRASTQARTQDMGPVLVHCS 1045
Cdd:cd14539     81 VRTTPTHVERIISIqhKDTRLS---------RSVVHLQFTTWPELGLPDSPNPLLRFieeVHSHYLQQRSLQTPIVVHCS 151
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....
gi 1925147141 1046 AGVGRTGTYIVLDSMLQQIQ-DQGTVNILGFLKHVRTQRNYLVQTEEQYVFIHD 1098
Cdd:cd14539    152 SGVGRTGAFCLLYAAVQEIEaGNGIPDLPQLVRKMRQQRKYMLQEKEHLKFCYE 205
PHA02747 PHA02747
protein tyrosine phosphatase; Provisional
820-1097 1.42e-45

protein tyrosine phosphatase; Provisional


Pssm-ID: 165114 [Multi-domain]  Cd Length: 312  Bit Score: 167.49  E-value: 1.42e-45
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1925147141  820 EALSVKQFVKHVAELHQTNTFSKEFEEVqsCTVEMGITTDSSNHPDNKNKNRYINIMAYDHSRVKL-LEEGKGGDYINAN 898
Cdd:PHA02747     7 AECRAIDFLKRRNQLNCFGIIRDEHHQI--ILKPFDGLIANFEKPENQPKNRYWDIPCWDHNRVILdSGGGSTSDYIHAN 84
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1925147141  899 FVDGFERTRAYIAAQGPLKSGTEDFWRMVWQENVGVIVMIT-NLLEKGRRKCDQYW-PMENQE-EYGHFLVTLKDTKTLA 975
Cdd:PHA02747    85 WIDGFEDDKKFIATQGPFAETCADFWKAVWQEHCSIIVMLTpTKGTNGEEKCYQYWcLNEDGNiDMEDFRIETLKTSVRA 164
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1925147141  976 YYTLRTFTLRDTSQKASQRgrcaertVVQYHYTQWPDMGVPEYTLPVLSFVRASTQARTQDMG----------PVLVHCS 1045
Cdd:PHA02747   165 KYILTLIEITDKILKDSRK-------ISHFQCSEWFEDETPSDHPDFIKFIKIIDINRKKSGKlfnpkdallcPIVVHCS 237
                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|..
gi 1925147141 1046 AGVGRTGTYIVLDSMLQQIQDQGTVNILGFLKHVRTQRNYLVQTEEQYVFIH 1097
Cdd:PHA02747   238 DGVGKTGIFCAVDICLNQLVKRKAICLAKTAEKIREQRHAGIMNFDDYLFIQ 289
PTPc_plant_PTP1 cd17658
protein tyrosine phosphatase 1 from Arabidopsis thaliana and similar plant PTPs; Arabidopsis ...
894-1097 1.50e-45

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: 163.40  E-value: 1.50e-45
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1925147141  894 YINANFV--DGFERTRAYIAAQGPLKSGTEDFWRMVWQENVGVIVMITNLLEKGRR-KCDQYWPME--NQEEYGHFLVTL 968
Cdd:cd17658      1 YINASLVetPASESLPKFIATQGPLPHTFEDFWEMVIQQRCPVIIMLTRLVDNYSTaKCADYFPAEenESREFGRISVTN 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1925147141  969 KDTKTLAY-YTLRTFtlrDTSQKASQRgrcAERTVVQYHYTQWPDMGVPEYTLPVLSFVRASTQArTQDMGPVLVHCSAG 1047
Cdd:cd17658     81 KKLKHSQHsITLRVL---EVQYIESEE---PPLSVLHIQYPEWPDHGVPKDTRSVRELLKRLYGI-PPSAGPIVVHCSAG 153
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|..
gi 1925147141 1048 VGRTGTYIVLDSMLQQIQ--DQGTVNILGFLKHVRTQRNYLVQTEEQYVFIH 1097
Cdd:cd17658    154 IGRTGAYCTIHNTIRRILegDMSAVDLSKTVRKFRSQRIGMVQTQDQYIFCY 205
R-PTP-D-2 cd14628
PTP-like domain of receptor-type tyrosine-protein phosphatase D, repeat 2; Receptor-type ...
1109-1400 4.65e-45

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


Pssm-ID: 350476 [Multi-domain]  Cd Length: 292  Bit Score: 165.29  E-value: 4.65e-45
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1925147141 1109 TLVTSDLVHSYVSDL--LTTGPSgRTRMERQFKLVSQRRARQADYAAALREGNDDKNRTSSLMPVERSRVCLScPVEG-E 1185
Cdd:cd14628      1 TEVPARNLYAYIQKLtqIETGEN-VTGMELEFKRLASSKAHTSRFISANLPCNKFKNRLVNIMPYESTRVCLQ-PIRGvE 78
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1925147141 1186 SSDYINASYIMGYHKSREFILTQSPLPSTVSDFWRMVWDHNSQLIISLpdthTAQRE-GEESC-AYWPSkDQPISCEGFI 1263
Cdd:cd14628     79 GSDYINASFIDGYRQQKAYIATQGPLAETTEDFWRMLWEHNSTIVVML----TKLREmGREKChQYWPA-ERSARYQYFV 153
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1925147141 1264 VsfsgeDHMCLANEERLVVHDFLLEATQDNYVLEVRQYMSPCWPNPDSPVSGTfQLLNIITEDSRQRE-----GTIVVHD 1338
Cdd:cd14628    154 V-----DPMAEYNMPQYILREFKVTDARDGQSRTVRQFQFTDWPEQGVPKSGE-GFIDFIGQVHKTKEqfgqdGPISVHC 227
                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1925147141 1339 RLGGSVAGLFCALTTLAQQLEHQGSVDVYQVARMTNLMRPGVFNDMEQYQFMYRAVLSLVDS 1400
Cdd:cd14628    228 SAGVGRTGVFITLSIVLERMRYEGVVDIFQTVKMLRTQRPAMVQTEDQYQFCYRAALEYLGS 289
PTPc-N14 cd14599
catalytic domain of tyrosine-protein phosphatase non-receptor type 14; Tyrosine-protein ...
843-1102 5.04e-45

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: 164.79  E-value: 5.04e-45
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1925147141  843 EFEEVQSCTVEMGITTdsSNHPDNKNKNRYINIMAYDHSRVKLL--EEGKGGdYINANFVDGFERTRA--YIAAQGPLKS 918
Cdd:cd14599     17 EYEQIPKKKADGVFTT--ATLPENAERNRIREVVPYEENRVELVptKENNTG-YINASHIKVTVGGEEwhYIATQGPLPH 93
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1925147141  919 GTEDFWRMVWQENVGVIVMITNLLEKGRRKCDQYWPM----ENQEEYGHFLVTLK-DTKTLAYYTlrtftlrdTSQKASQ 993
Cdd:cd14599     94 TCHDFWQMVWEQGVNVIAMVTAEEEGGRSKSHRYWPKlgskHSSATYGKFKVTTKfRTDSGCYAT--------TGLKVKH 165
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1925147141  994 RGRCAERTVVQYHYTQWPDMGVPEYTLPVLSFVRA--STQARTQDM--------GPVLVHCSAGVGRTGTYIVLDSMLQQ 1063
Cdd:cd14599    166 LLSGQERTVWHLQYTDWPDHGCPEEVQGFLSYLEEiqSVRRHTNSMldstkncnPPIVVHCSAGVGRTGVVILTELMIGC 245
                          250       260       270
                   ....*....|....*....|....*....|....*....
gi 1925147141 1064 IQDQGTVNILGFLKHVRTQRNYLVQTEEQYVFIHDALVE 1102
Cdd:cd14599    246 LEHNEKVEVPVMLRHLREQRMFMIQTIAQYKFVYQVLIQ 284
R-PTP-LAR-2 cd14554
PTP-like domain of the LAR family receptor-type tyrosine-protein phosphatases, repeat 2; The ...
1159-1395 9.79e-45

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: 162.31  E-value: 9.79e-45
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1925147141 1159 NDDKNRTSSLMPVERSRVCLScPVEG-ESSDYINASYIMGYHKSREFILTQSPLPSTVSDFWRMVWDHNSQLIISLpdTH 1237
Cdd:cd14554      6 NKFKNRLVNILPYESTRVCLQ-PIRGvEGSDYINASFIDGYRQRGAYIATQGPLAETTEDFWRMLWEHNSTIIVML--TK 82
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1925147141 1238 TAQREGEESCAYWPSkDQPISCEGFIVsfsgeDHMCLANEERLVVHDFLLEATQDNYVLEVRQYMSPCWPNPDSPVSGTf 1317
Cdd:cd14554     83 LREMGREKCHQYWPA-ERSARYQYFVV-----DPMAEYNMPQYILREFKVTDARDGQSRTVRQFQFTDWPEQGVPKSGE- 155
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1925147141 1318 QLLNIITEDSRQRE-----GTIVVHDRLGGSVAGLFCALTTLAQQLEHQGSVDVYQVARMTNLMRPGVFNDMEQYQFMYR 1392
Cdd:cd14554    156 GFIDFIGQVHKTKEqfgqeGPITVHCSAGVGRTGVFITLSIVLERMRYEGVVDVFQTVKLLRTQRPAMVQTEDQYQFCYR 235

                   ...
gi 1925147141 1393 AVL 1395
Cdd:cd14554    236 AAL 238
PHA02742 PHA02742
protein tyrosine phosphatase; Provisional
865-1095 1.64e-44

protein tyrosine phosphatase; Provisional


Pssm-ID: 165109 [Multi-domain]  Cd Length: 303  Bit Score: 164.02  E-value: 1.64e-44
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1925147141  865 DNKN--KNRYINIMAYDHSRVKLLEEGKGGDYINANFVDGFERTRAYIAAQGPLKSGTEDFWRMVWQENVGVIVMITNLL 942
Cdd:PHA02742    49 ELKNmkKCRYPDAPCFDRNRVILKIEDGGDDFINASYVDGHNAKGRFICTQAPLEETALDFWQAIFQDQVRVIVMITKIM 128
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1925147141  943 EKGRRKCDQYWPMENQEE--YGHFLVTLKDTKTLAYYTLRTFTLRDTSQKASQrgrcaerTVVQYHYTQWPDMGVPEYTL 1020
Cdd:PHA02742   129 EDGKEACYPYWMPHERGKatHGEFKIKTKKIKSFRNYAVTNLCLTDTNTGASL-------DIKHFAYEDWPHGGLPRDPN 201
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1925147141 1021 PVLSFVRASTQARTQ-----------DMGPVLVHCSAGVGRTGTYIVLDSMLQQIQDQGTVNILGFLKHVRTQRNYLVQT 1089
Cdd:PHA02742   202 KFLDFVLAVREADLKadvdikgenivKEPPILVHCSAGLDRAGAFCAIDICISKYNERAIIPLLSIVRDLRKQRHNCLSL 281

                   ....*.
gi 1925147141 1090 EEQYVF 1095
Cdd:PHA02742   282 PQQYIF 287
R-PTP-S-2 cd14627
PTP-like domain of receptor-type tyrosine-protein phosphatase S, repeat 2; Receptor-type ...
1108-1400 4.19e-44

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: 162.21  E-value: 4.19e-44
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1925147141 1108 DTLVTSDLVHSYVSDLLTTGPSGR-TRMERQFKLVSQRRARQADYAAALREGNDDKNRTSSLMPVERSRVCLScPVEG-E 1185
Cdd:cd14627      1 NTEVPARNLYSYIQKLAQVEVGEHvTGMELEFKRLANSKAHTSRFISANLPCNKFKNRLVNIMPYETTRVCLQ-PIRGvE 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1925147141 1186 SSDYINASYIMGYHKSREFILTQSPLPSTVSDFWRMVWDHNSQLIISLpdthTAQRE-GEESC-AYWPSkDQPISCEGFI 1263
Cdd:cd14627     80 GSDYINASFIDGYRQQKAYIATQGPLAETTEDFWRMLWENNSTIVVML----TKLREmGREKChQYWPA-ERSARYQYFV 154
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1925147141 1264 VsfsgeDHMCLANEERLVVHDFLLEATQDNYVLEVRQYMSPCWPNPDSPVSGTfQLLNIITEDSRQRE-----GTIVVHD 1338
Cdd:cd14627    155 V-----DPMAEYNMPQYILREFKVTDARDGQSRTVRQFQFTDWPEQGVPKSGE-GFIDFIGQVHKTKEqfgqdGPISVHC 228
                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1925147141 1339 RLGGSVAGLFCALTTLAQQLEHQGSVDVYQVARMTNLMRPGVFNDMEQYQFMYRAVLSLVDS 1400
Cdd:cd14627    229 SAGVGRTGVFITLSIVLERMRYEGVVDIFQTVKMLRTQRPAMVQTEDEYQFCYQAALEYLGS 290
PTPc-N20 cd14596
catalytic domain of tyrosine-protein phosphatase non-receptor type 20; Tyrosine-protein ...
894-1104 9.80e-44

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: 158.37  E-value: 9.80e-44
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1925147141  894 YINANFVD---GfERTRAYIAAQGPLKSGTEDFWRMVWQENVGVIVMITNLLEKGRRKCDQYWPMENQE--EYGHFLVTL 968
Cdd:cd14596      1 YINASYITmpvG-EEELFYIATQGPLPSTIDDFWQMVWENRSDVIAMMTREVERGKVKCHRYWPETLQEpmELENYQLRL 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1925147141  969 KDTKTLAYYTLRTFTLRDTSQKASqrgrcaeRTVVQYHYTQWPDMGVPEYTLPVLSFVRASTqaRTQDMGPVLVHCSAGV 1048
Cdd:cd14596     80 ENYQALQYFIIRIIKLVEKETGEN-------RLIKHLQFTTWPDHGTPQSSDQLVKFICYMR--KVHNTGPIVVHCSAGI 150
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 1925147141 1049 GRTGTYIVLDSMLQQIQDQGTVNILGFLKHVRTQRNYLVQTEEQYVFIHDALVEAI 1104
Cdd:cd14596    151 GRAGVLICVDVLLSLIEKDLSFNIKDIVREMRQQRYGMIQTKDQYLFCYKVVLEVL 206
PHA02746 PHA02746
protein tyrosine phosphatase; Provisional
845-1105 1.96e-43

protein tyrosine phosphatase; Provisional


Pssm-ID: 165113 [Multi-domain]  Cd Length: 323  Bit Score: 161.35  E-value: 1.96e-43
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1925147141  845 EEVQSCTVEMGITTDSSNHPDNKNKNRYINIMAYDHSRVKLLEEGKG-----GD----------------YINANFVDGF 903
Cdd:PHA02746    30 EHAEVMDIPIRGTTNHFLKKENLKKNRFHDIPCWDHSRVVINAHESLkmfdvGDsdgkkievtsednaenYIHANFVDGF 109
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1925147141  904 ERTRAYIAAQGPLKSGTEDFWRMVWQENVGVIVMITNlLEKGRRKCDQYWPMENQEE--YGHFLVTLKDTKTLAYYTLRT 981
Cdd:PHA02746   110 KEANKFICAQGPKEDTSEDFFKLISEHESQVIVSLTD-IDDDDEKCFELWTKEEDSElaFGRFVAKILDIIEELSFTKTR 188
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1925147141  982 FTLRDTSQKASqrgrcaeRTVVQYHYTQWPDMGVPEYTLPVLSFVRASTQAR----------TQDMGPVLVHCSAGVGRT 1051
Cdd:PHA02746   189 LMITDKISDTS-------REIHHFWFPDWPDNGIPTGMAEFLELINKVNEEQaelikqadndPQTLGPIVVHCSAGIGRA 261
                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|....
gi 1925147141 1052 GTYIVLDSMLQQIQDQGTVNILGFLKHVRTQRNYLVQTEEQYVFIHDALVEAIV 1105
Cdd:PHA02746   262 GTFCAIDNALEQLEKEKEVCLGEIVLKIRKQRHSSVFLPEQYAFCYKALKYAII 315
PTPc-N4 cd14601
catalytic domain of tyrosine-protein phosphatase non-receptor type 4; Tyrosine-protein ...
893-1102 5.49e-43

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


Pssm-ID: 350449 [Multi-domain]  Cd Length: 212  Bit Score: 156.26  E-value: 5.49e-43
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1925147141  893 DYINANFVD----GFERTRAYIAAQGPLKSGTEDFWRMVWQENVGVIVMITNLLEKGRRKCDQYWP-MENQEEYGHFLVT 967
Cdd:cd14601      1 DYINANYINmeipSSSIINRYIACQGPLPNTCSDFWQMTWEQGSSMVVMLTTQVERGRVKCHQYWPePSGSSSYGGFQVT 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1925147141  968 LKDTKTLAYYTLRTFTLRDTSQKASqrgrcaeRTVVQYHYTQWPDMGVPEYTLPVLSFVRASTQARTQDMGPVLVHCSAG 1047
Cdd:cd14601     81 CHSEEGNPAYVFREMTLTNLEKNES-------RPLTQIQYIAWPDHGVPDDSSDFLDFVCLVRNKRAGKDEPVVVHCSAG 153
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1925147141 1048 VGRTGTYIVLDSMLQQIQDQGTVNILGFLKHVRTQRNYLVQTEEQYVFIHDALVE 1102
Cdd:cd14601    154 IGRTGVLITMETAMCLIECNQPVYPLDIVRTMRDQRAMMIQTPSQYRFVCEAILK 208
R-PTP-F-2 cd14629
PTP-like domain of receptor-type tyrosine-protein phosphatase F, repeat 2; Receptor-type ...
1128-1400 6.72e-43

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: 158.74  E-value: 6.72e-43
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1925147141 1128 PSGR--TRMERQFKLVSQRRARQADYAAALREGNDDKNRTSSLMPVERSRVCLScPVEG-ESSDYINASYIMGYHKSREF 1204
Cdd:cd14629     20 PPGEsvTAMELEFKLLANSKAHTSRFISANLPCNKFKNRLVNIMPYELTRVCLQ-PIRGvEGSDYINASFIDGYRQQKAY 98
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1925147141 1205 ILTQSPLPSTVSDFWRMVWDHNSQLIISLpdthTAQRE-GEESC-AYWPSkDQPISCEGFIVsfsgeDHMCLANEERLVV 1282
Cdd:cd14629     99 IATQGPLAETTEDFWRMLWEHNSTIVVML----TKLREmGREKChQYWPA-ERSARYQYFVV-----DPMAEYNMPQYIL 168
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1925147141 1283 HDFLLEATQDNYVLEVRQYMSPCWPNPDSPVSGTfQLLNIITEDSRQRE-----GTIVVHDRLGGSVAGLFCALTTLAQQ 1357
Cdd:cd14629    169 REFKVTDARDGQSRTIRQFQFTDWPEQGVPKTGE-GFIDFIGQVHKTKEqfgqdGPITVHCSAGVGRTGVFITLSIVLER 247
                          250       260       270       280
                   ....*....|....*....|....*....|....*....|...
gi 1925147141 1358 LEHQGSVDVYQVARMTNLMRPGVFNDMEQYQFMYRAVLSLVDS 1400
Cdd:cd14629    248 MRYEGVVDMFQTVKTLRTQRPAMVQTEDQYQLCYRAALEYLGS 290
COG5599 COG5599
Protein tyrosine phosphatase [Signal transduction mechanisms];
842-1096 4.79e-42

Protein tyrosine phosphatase [Signal transduction mechanisms];


Pssm-ID: 444335 [Multi-domain]  Cd Length: 282  Bit Score: 156.02  E-value: 4.79e-42
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1925147141  842 KEFEEVQSCTVEMGITTDSSNHPDNKN---KNRYINIMAYDHSRVklleeGKGGDYINANFVDGFERTRaYIAAQGPLKS 918
Cdd:COG5599     15 KINSRLSTLTNELAPSHNDPQYLQNINgspLNRFRDIQPYKETAL-----RANLGYLNANYIQVIGNHR-YIATQYPLEE 88
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1925147141  919 GTEDFWRMVWQENVGVIVMITNLLE--KGRRKCDQYWPMenQEEYGHFLV--TLKDTKTLA-YYTLRTFTL--RDTSQKa 991
Cdd:COG5599     89 QLEDFFQMLFDNNTPVLVVLASDDEisKPKVKMPVYFRQ--DGEYGKYEVssELTESIQLRdGIEARTYVLtiKGTGQK- 165
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1925147141  992 sqrgrcaERTVVQYHYTQWPDMGVP--EYTLPVLSFVRASTQARTQDMGPVLVHCSAGVGRTGTYIVLDSMLQQIQD--Q 1067
Cdd:COG5599    166 -------KIEIPVLHVKNWPDHGAIsaEALKNLADLIDKKEKIKDPDKLLPVVHCRAGVGRTGTLIACLALSKSINAlvQ 238
                          250       260       270
                   ....*....|....*....|....*....|
gi 1925147141 1068 GTVNILGFLKHVRTQRNY-LVQTEEQYVFI 1096
Cdd:COG5599    239 ITLSVEEIVIDMRTSRNGgMVQTSEQLDVL 268
PTPc-N21 cd14598
catalytic domain of tyrosine-protein phosphatase non-receptor type 21; Tyrosine-protein ...
894-1102 2.34e-39

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: 146.27  E-value: 2.34e-39
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1925147141  894 YINANF----VDGFERTraYIAAQGPLKSGTEDFWRMVWQENVGVIVMITNLLEKGRRKCDQYWP----MENQEEYGHFL 965
Cdd:cd14598      1 YINASHikvtVGGKEWD--YIATQGPLQNTCQDFWQMVWEQGVAIIAMVTAEEEGGREKSFRYWPrlgsRHNTVTYGRFK 78
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1925147141  966 VTLK-DTKTLAYYTlrtftlrdTSQKASQRGRCAERTVVQYHYTQWPDMGVPEYTLPVLSF------VRASTQARTQDMG 1038
Cdd:cd14598     79 ITTRfRTDSGCYAT--------TGLKIKHLLTGQERTVWHLQYTDWPEHGCPEDLKGFLSYleeiqsVRRHTNSTIDPKS 150
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1925147141 1039 ---PVLVHCSAGVGRTGTYIVLDSMLQQIQDQGTVNILGFLKHVRTQRNYLVQTEEQYVFIHDALVE 1102
Cdd:cd14598    151 pnpPVLVHCSAGVGRTGVVILSEIMIACLEHNEMLDIPRVLDMLRQQRMMMVQTLSQYTFVYKVLIQ 217
R-PTPc-A-2 cd14623
catalytic domain of receptor-type tyrosine-protein phosphatase A, repeat 2; Receptor-type ...
1164-1394 7.95e-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: 7.95e-39
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1925147141 1164 RTSSLMPVERSRVCLSCPVEGESSDYINASYIMGYHKSREFILTQSPLPSTVSDFWRMVWDHNSQLIISLPDThtaQREG 1243
Cdd:cd14623      1 RVLQIIPYEFNRVIIPVKRGEENTDYVNASFIDGYRQKDSYIASQGPLQHTIEDFWRMIWEWKSCSIVMLTEL---EERG 77
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1925147141 1244 EESCA-YWPSkDQPISCEGFIVSFSGEDHMclaneERLVVHDFLLEATQDNYVLEVRQYMSPCWPNPDSPVSGTfQLLNI 1322
Cdd:cd14623     78 QEKCAqYWPS-DGSVSYGDITIELKKEEEC-----ESYTVRDLLVTNTRENKSRQIRQFHFHGWPEVGIPSDGK-GMINI 150
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1925147141 1323 ITEDSRQREGT----IVVHDRLGGSVAGLFCALTTLAQQLEHQGSVDVYQVARMTNLMRPGVFNDMEQYQFMYRAV 1394
Cdd:cd14623    151 IAAVQKQQQQSgnhpITVHCSAGAGRTGTFCALSTVLERVKAEGILDVFQTVKSLRLQRPHMVQTLEQYEFCYKVV 226
R3-PTPc cd14548
catalytic domain of R3 subfamily receptor-type tyrosine-protein phosphatases and similar ...
1164-1391 1.54e-38

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: 143.65  E-value: 1.54e-38
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1925147141 1164 RTSSLMPVERSRVCLSCPVEGESSDYINASYIMGYHKSREFILTQSPLPSTVSDFWRMVWDHNSQLIISLpdthTAQRE- 1242
Cdd:cd14548      1 RYTNILPYDHSRVKLIPINEEEGSDYINANYIPGYNSPREFIATQGPLPGTKDDFWRMVWEQNSHTIVML----TQCMEk 76
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1925147141 1243 GEESCA-YWPSKDQPISCEGFIVSFSGEDHMclaneERLVVHDFLLEATQDnyVLEVRQYMSPCWPN---PDSPVSgtfq 1318
Cdd:cd14548     77 GRVKCDhYWPFDQDPVYYGDITVTMLSESVL-----PDWTIREFKLERGDE--VRSVRQFHFTAWPDhgvPEAPDS---- 145
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1925147141 1319 LLNII--TEDSRQRE-GTIVVHDRLGGSVAGLFCALTTLAQQLEHQGSVDVYQVARMTNLMRPGVFNDMEQYQFMY 1391
Cdd:cd14548    146 LLRFVrlVRDYIKQEkGPTIVHCSAGVGRTGTFIALDRLLQQIESEDYVDIFGIVYDLRKHRPLMVQTEAQYIFLH 221
R-PTPc-A-E-2 cd14552
catalytic domain of receptor-type tyrosine-protein phosphatase A and E, repeat 2; ...
1189-1394 1.95e-38

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: 142.79  E-value: 1.95e-38
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1925147141 1189 YINASYIMGYHKSREFILTQSPLPSTVSDFWRMVWDHNSQLIISLPDThtaQREGEESCA-YWPSkDQPISCEGFIVSFS 1267
Cdd:cd14552      1 YINASFIDGYRQKDAYIATQGPLDHTVEDFWRMIWEWKSCSIVMLTEI---KERSQNKCAqYWPE-DGSVSSGDITVELK 76
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1925147141 1268 GEDhmclaNEERLVVHDFLLEATQDNYVLEVRQYMSPCWPNPDSPVSGTfQLLNIITEDSRQRE----GTIVVHDRLGGS 1343
Cdd:cd14552     77 DQT-----DYEDYTLRDFLVTKGKGGSTRTVRQFHFHGWPEVGIPDNGK-GMIDLIAAVQKQQQqsgnHPITVHCSAGAG 150
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|.
gi 1925147141 1344 VAGLFCALTTLAQQLEHQGSVDVYQVARMTNLMRPGVFNDMEQYQFMYRAV 1394
Cdd:cd14552    151 RTGTFCALSTVLERVKAEGVLDVFQVVKSLRLQRPHMVQTLEQYEFCYKVV 201
alpha_CA_VI cd03125
Carbonic anhydrase alpha, isozyme VI. Carbonic anhydrases (CAs) are zinc-containing enzymes ...
52-292 2.55e-38

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: 144.16  E-value: 2.55e-38
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1925147141   52 WGKRYPACNNARQSPIDIDETFTQVRVEYQGLQLEGWEKNTPETTTINNdGNTVVLGLDGEYYVSGGgLSTRFRLGRMTF 131
Cdd:cd03125      5 WPEKYPACGGKRQSPIDIQRREVRFNPSLLQLELVGYEKEQGEFTMTNN-GHTVQIDLPPTMSITTG-DGTVYTAVQMHF 82
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1925147141  132 HWGRCNASSDGSEHSLNGLKFPLEMQILCYESGlYQSIDDAVRDGGRIAALAVLFET-SLDNNDNYNTILEGVNSVNRFG 210
Cdd:cd03125     83 HWGGRDSEISGSEHTIDGMRYVAELHIVHYNSK-YKSYEEAKDKPDGLAVLAFLYKVgHYAENTYYSDFISKLAKIKYAG 161
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1925147141  211 KTGNVEPFSLLALLPNSTDKYYTYNGSLTSPPCSETVEWIVFKHTVPISETQLEvfcevmTMQQAgyvmLMDY----LQN 286
Cdd:cd03125    162 QTTTLTSLDVRDMLPENLHHYYTYQGSLTTPPCTENVLWFVFDDPVTLSKTQIV------KLENT----LMDHhnktIRN 231

                   ....*.
gi 1925147141  287 NFREQQ 292
Cdd:cd03125    232 DYRRTQ 237
PTPc_motif smart00404
Protein tyrosine phosphatase, catalytic domain motif;
1001-1102 5.10e-38

Protein tyrosine phosphatase, catalytic domain motif;


Pssm-ID: 214649 [Multi-domain]  Cd Length: 105  Bit Score: 137.88  E-value: 5.10e-38
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1925147141  1001 TVVQYHYTQWPDMGVPEYTLPVLSFVRASTQARTQDM--GPVLVHCSAGVGRTGTYIVLDSMLQQIQD-QGTVNILGFLK 1077
Cdd:smart00404    1 TVKHYHYTGWPDHGVPESPDSILELLRAVKKNLNQSEssGPVVVHCSAGVGRTGTFVAIDILLQQLEAeAGEVDIFDTVK 80
                            90       100
                    ....*....|....*....|....*
gi 1925147141  1078 HVRTQRNYLVQTEEQYVFIHDALVE 1102
Cdd:smart00404   81 ELRSQRPGMVQTEEQYLFLYRALLE 105
PTPc_DSPc smart00012
Protein tyrosine phosphatase, catalytic domain, undefined specificity; Protein tyrosine ...
1001-1102 5.10e-38

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


Pssm-ID: 214469 [Multi-domain]  Cd Length: 105  Bit Score: 137.88  E-value: 5.10e-38
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1925147141  1001 TVVQYHYTQWPDMGVPEYTLPVLSFVRASTQARTQDM--GPVLVHCSAGVGRTGTYIVLDSMLQQIQD-QGTVNILGFLK 1077
Cdd:smart00012    1 TVKHYHYTGWPDHGVPESPDSILELLRAVKKNLNQSEssGPVVVHCSAGVGRTGTFVAIDILLQQLEAeAGEVDIFDTVK 80
                            90       100
                    ....*....|....*....|....*
gi 1925147141  1078 HVRTQRNYLVQTEEQYVFIHDALVE 1102
Cdd:smart00012   81 ELRSQRPGMVQTEEQYLFLYRALLE 105
PTPc-N7 cd14612
catalytic domain of tyrosine-protein phosphatase non-receptor type 7; Tyrosine-protein ...
1158-1392 1.03e-37

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: 142.28  E-value: 1.03e-37
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1925147141 1158 GNDDKNRTSSLMPVERSRVCLSCP-VEGESSDYINASYIMGYH-KSREFILTQSPLPSTVSDFWRMVWDHNSQLIISLpd 1235
Cdd:cd14612     14 GHASKDRYKTILPNPQSRVCLRRAgSQEEEGSYINANYIRGYDgKEKAYIATQGPMLNTVSDFWEMVWQEECPIIVMI-- 91
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1925147141 1236 thTAQREGEESCA-YWPSKDQPISCEGFIVSFSGEdhmClaneERLVVHDFLLEATQDNYvlEVRQYMSPCWPNPDSPVS 1314
Cdd:cd14612     92 --TKLKEKKEKCVhYWPEKEGTYGRFEIRVQDMKE---C----DGYTIRDLTIQLEEESR--SVKHYWFSSWPDHQTPES 160
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1925147141 1315 GTfQLLNIITEDSRQRE-----GTIVVHDRLGGSVAGLFCALTTLAQQLEHQGSVDVYQVARMTNLMRPGVFNDMEQYQF 1389
Cdd:cd14612    161 AG-PLLRLVAEVEESRQtaaspGPIVVHCSAGIGRTGCFIATSIGCQQLKDTGKVDILGIVCQLRLDRGGMIQTSEQYQF 239

                   ...
gi 1925147141 1390 MYR 1392
Cdd:cd14612    240 LHH 242
alpha_CA_IX cd03150
Carbonic anhydrase alpha, isozyme IX. Carbonic anhydrases (CAs) are zinc-containing enzymes ...
48-292 1.44e-37

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: 142.02  E-value: 1.44e-37
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1925147141   48 NQKIWGKRYPACNNARQSPIDIDETFTQVRVEYQGLQLEGWEKNTPETTTINNDGNTVVLGLDGEYYVSGGgLSTRFRLG 127
Cdd:cd03150      1 GQPPWPSVSPACAGRFQSPVDIRPHLVAFCPALRPLELLGFDLPPSPSLRLLNNGHTVQLSLPSGLRMALG-PGQEYRAL 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1925147141  128 RMTFHWGrcNASSDGSEHSLNGLKFPLEMQILCYESGlYQSIDDAVRDGGRIAALAVLFETSLDNNDNYNTILEGVNSVN 207
Cdd:cd03150     80 QLHLHWG--AAGRPGSEHTVDGHRFPAEIHVVHLSTA-FANLDEALGRPGGLAVLAAFLAEGLHENSAYEQLLSRLSEIS 156
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1925147141  208 RFGKTGNVEPFSLLALLPNSTDKYYTYNGSLTSPPCSETVEWIVFKHTVPISETQLEVFCEVMTMQQAgyvmlmDYLQNN 287
Cdd:cd03150    157 EEESETVVPGLDVSALLPSDLSRYFRYEGSLTTPPCAQGVIWTVFNQTVRLSAKQLHTLSDSLWGPHD------SRLQLN 230

                   ....*
gi 1925147141  288 FREQQ 292
Cdd:cd03150    231 FRATQ 235
R-PTPc-E-2 cd14622
catalytic domain of receptor-type tyrosine-protein phosphatase E, repeat 2; Receptor-type ...
1188-1394 1.87e-37

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: 140.14  E-value: 1.87e-37
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1925147141 1188 DYINASYIMGYHKSREFILTQSPLPSTVSDFWRMVWDHNSQLIISLpdTHTAQREGEESCAYWPSKDQpiSCEGFIVSFS 1267
Cdd:cd14622      1 DYINASFIDGYRQKDYFIATQGPLAHTVEDFWRMVWEWKCHTIVML--TELQEREQEKCVQYWPSEGS--VTHGEITIEI 76
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1925147141 1268 GEDHMClaneERLVVHDFLLEATQDNYVLEVRQYMSPCWPNPDSPVSGTfQLLNIITEDSRQREGT----IVVHDRLGGS 1343
Cdd:cd14622     77 KNDTLL----ETISIRDFLVTYNQEKQTRLVRQFHFHGWPEIGIPAEGK-GMIDLIAAVQKQQQQTgnhpIVVHCSAGAG 151
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|.
gi 1925147141 1344 VAGLFCALTTLAQQLEHQGSVDVYQVARMTNLMRPGVFNDMEQYQFMYRAV 1394
Cdd:cd14622    152 RTGTFIALSNILERVKAEGLLDVFQTVKSLRLQRPHMVQTLEQYEFCYRVV 202
R-PTPc-H cd14619
catalytic domain of receptor-type tyrosine-protein phosphatase H; Receptor-type ...
1163-1398 1.02e-36

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: 138.87  E-value: 1.02e-36
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1925147141 1163 NRTSSLMPVERSRVCLSCPVEGESSDYINASYIMGYHKSREFILTQSPLPSTVSDFWRMVWDHNSQLIISLPDTHTAQRE 1242
Cdd:cd14619      1 NRFRNVLPYDWSRVPLKPIHEEPGSDYINANYMPGYWSSQEFIATQGPLPQTVGDFWRMIWEQQSSTIVMLTNCMEAGRV 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1925147141 1243 GEEScaYWPSKDQPISCEGFIVSFSGEDHMclaneERLVVHDFLLEATQDNYVLEVRQYMSPCWPNPDSPVSGT--FQLL 1320
Cdd:cd14619     81 KCEH--YWPLDYTPCTYGHLRVTVVSEEVM-----ENWTVREFLLKQVEEQKTLSVRHFHFTAWPDHGVPSSTDtlLAFR 153
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1925147141 1321 NIITE--DSRQREGTIVVHDRLGGSVAGLFCALTTLAQQLEHQGSVDVYQVARMTNLMRPGVFNDMEQYQFMYRAVLSLV 1398
Cdd:cd14619    154 RLLRQwlDQTMSGGPTVVHCSAGVGRTGTLIALDVLLQQLQSEGLLGPFSFVQKMRENRPLMVQTESQYVFLHQCILDFL 233
PTPc-KIM cd14547
catalytic domain of the kinase interaction motif (KIM) family of protein-tyrosine phosphatases; ...
1163-1392 1.08e-36

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: 138.68  E-value: 1.08e-36
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1925147141 1163 NRTSSLMPVERSRVCLSCPVEGESSDYINASYIMGY-HKSREFILTQSPLPSTVSDFWRMVWDHNSQLIISLpdthTAQR 1241
Cdd:cd14547      1 NRYKTILPNEHSRVCLPSVDDDPLSSYINANYIRGYdGEEKAYIATQGPLPNTVADFWRMVWQEKTPIIVMI----TNLT 76
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1925147141 1242 EGEESCA-YWPSKdQPISCEGFIVSFsgedhmclaneERLVVHD----FLLEATQDNYVLEVRQYMSPCWPNPDSPVSgT 1316
Cdd:cd14547     77 EAKEKCAqYWPEE-ENETYGDFEVTV-----------QSVKETDgytvRKLTLKYGGEKRYLKHYWYTSWPDHKTPEA-A 143
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1925147141 1317 FQLLNIITE--DSRQRE---GTIVVHDRLGGSVAGLFCALTTLAQQLEHQGSVDVYQVARMTNLMRPGVFNDMEQYQFMY 1391
Cdd:cd14547    144 QPLLSLVQEveEARQTEphrGPIVVHCSAGIGRTGCFIATSIGCQQLREEGVVDVLGIVCQLRLDRGGMVQTAEQYEFVH 223

                   .
gi 1925147141 1392 R 1392
Cdd:cd14547    224 R 224
R-PTPc-typeIIb-2 cd14556
PTP domain of type IIb (or R2B) subfamily receptor-type tyrosine-protein phosphatases, repeat ...
894-1098 5.84e-36

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


Pssm-ID: 350404 [Multi-domain]  Cd Length: 201  Bit Score: 135.61  E-value: 5.84e-36
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1925147141  894 YINANFVDGFERTRAYIAAQGPLKSGTEDFWRMVWQENVGVIVMItNLLEKGRRKCDQYWPMENQEEYGHFLVTLKDTKT 973
Cdd:cd14556      1 YINAALLDSYKQPAAFIVTQHPLPNTVTDFWRLVYDYGCTSIVML-NQLDPKDQSCPQYWPDEGSGTYGPIQVEFVSTTI 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1925147141  974 LAYYTLRTFTLRDTsqKASQRGRcaeRTVVQYHYTQWPDMG-VPEYTLPVLSFVRASTQARTQ-DMGPVLVHCSAGVGRT 1051
Cdd:cd14556     80 DEDVISRIFRLQNT--TRPQEGY---RMVQQFQFLGWPRDRdTPPSKRALLKLLSEVEKWQEQsGEGPIVVHCLNGVGRS 154
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*..
gi 1925147141 1052 GTYIVLDSMLQQIQDQGTVNILGFLKHVRTQRNYLVQTEEQYVFIHD 1098
Cdd:cd14556    155 GVFCAISSVCERIKVENVVDVFQAVKTLRNHRPNMVETEEQYKFCYD 201
R-PTPc-J cd14615
catalytic domain of receptor-type tyrosine-protein phosphatase J; Receptor-type ...
1163-1395 1.44e-35

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: 135.71  E-value: 1.44e-35
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1925147141 1163 NRTSSLMPVERSRVCLSCPvEGESSDYINASYIMGYHKSREFILTQSPLPSTVSDFWRMVWDHNSQLIISLPdthTAQRE 1242
Cdd:cd14615      1 NRYNNVLPYDISRVKLSVQ-SHSTDDYINANYMPGYNSKKEFIAAQGPLPNTVKDFWRMVWEKNVYAIVMLT---KCVEQ 76
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1925147141 1243 GEESC-AYWPSKdQPISCEGFIVSFSGEDHMclaneERLVVHDFLLEATQDNYVLEVRQYMSPCWpnPDSPVSGTFQLL- 1320
Cdd:cd14615     77 GRTKCeEYWPSK-QKKDYGDITVTMTSEIVL-----PEWTIRDFTVKNAQTNESRTVRHFHFTSW--PDHGVPETTDLLi 148
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1925147141 1321 ---NIITEDSRQ--REGTIVVHDRLGGSVAGLFCALTTLAQQLEHQGSVDVYQVARMTNLMRPGVFNDMEQYQFMYRAVL 1395
Cdd:cd14615    149 nfrHLVREYMKQnpPNSPILVHCSAGVGRTGTFIAIDRLIYQIENENVVDVYGIVYDLRMHRPLMVQTEDQYVFLNQCAL 228
alpha_CARP_X_XI_like cd03121
Carbonic anhydrase alpha related protein: groups X, XI and related proteins. This subgroup ...
52-292 1.88e-35

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: 136.00  E-value: 1.88e-35
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1925147141   52 WGKRYPA---CNNA-RQSPIDI-------DETFTQVRVEyQGLQLEGwekntpettTINNDGNTVVLGLDGEY--YVSGG 118
Cdd:cd03121      5 WGLVNSAwnlCSKGrRQSPVDIepsrllfDPFLTPLRID-TGRKVSG---------TFYNTGRHVSFRPDKDPvvNISGG 74
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1925147141  119 GLSTRFRLGRMTFHWGRCNasSDGSEHSLNGLKFPLEMQILCYESGLYQSIDDAVRDGGRIAALAVLFETSLDNNDNYN- 197
Cdd:cd03121     75 PLSYRYRLEEIRLHFGRED--EQGSEHTVNGQAFPGEVQLIHYNSELYPNFSEASKSPNGLVIVSLFVKIGETSNPELRr 152
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1925147141  198 -TILEGVNSVNRFGKTGNVEPFSLLALLPNsTDKYYTYNGSLTSPPCSETVEWIVFKHTVPISETQLEvfcEVMTMQQAG 276
Cdd:cd03121    153 lTNRDTITSIRYKGDAYFLQDLSIELLLPE-TDHYITYEGSLTSPGCHETVTWIILNKPIYITKEQMH---SLRLLSQNS 228
                          250
                   ....*....|....*.
gi 1925147141  277 YVMLMDYLQNNFREQQ 292
Cdd:cd03121    229 PSQEKAPMSPNFRPVQ 244
R-PTP-C-2 cd14558
PTP-like domain of receptor-type tyrosine-protein phosphatase C, repeat 2; Receptor-type ...
1189-1391 1.88e-34

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: 131.36  E-value: 1.88e-34
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1925147141 1189 YINASYIMGYHKSREFILTQSPLPSTVSDFWRMVWDHNSQLIISLPDthTAQREGEESCAYWPSKDQPIscegfivsfsG 1268
Cdd:cd14558      1 YINASFIDGYWGPKSLIATQGPLPDTIADFWQMIFQKKVKVIVMLTE--LKEGDQEQCAQYWGDEKKTY----------G 68
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1925147141 1269 EDHMCLANEER---LVVHDFLLEATQDNYVLEVRQYMSPCWPNPDSPVSGTfQLLNIItEDSRQREGT----------IV 1335
Cdd:cd14558     69 DIEVELKDTEKsptYTVRVFEITHLKRKDSRTVYQYQYHKWKGEELPEKPK-DLVDMI-KSIKQKLPYknskhgrsvpIV 146
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 1925147141 1336 VHDRLGGSVAGLFCALTTLAQQLEHQGSVDVYQVARMTNLMRPGVFNDMEQYQFMY 1391
Cdd:cd14558    147 VHCSDGSSRTGIFCALWNLLESAETEKVVDVFQVVKALRKQRPGMVSTLEQYQFLY 202
alpha_CA_prokaryotic_like cd03124
Carbonic anhydrase alpha, prokaryotic-like subfamily. Carbonic anhydrases (CAs) are ...
52-270 2.52e-34

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: 131.63  E-value: 2.52e-34
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1925147141   52 WG---KRYPACNN-ARQSPIDIDETFTQVRveyqglQLEGWEKN-TPETTTINNDGNTVVLGLDGEyyvsGGGLS---TR 123
Cdd:cd03124      5 WGnldPEFALCATgKNQSPIDITTKAVVSD------KLPPLNYNyKPTSATLVNNGHTIQVNFEGN----GGTLTidgET 74
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1925147141  124 FRLGRMTFHwgrcnassDGSEHSLNGLKFPLEMQILcyesglYQSIDdavrdgGRIAALAVLFETSlDNNDNYNTILEGV 203
Cdd:cd03124     75 YQLLQFHFH--------SPSEHLINGKRYPLEAHLV------HKSKD------GQLAVVAVLFEEG-KENPFLKKILDNM 133
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1925147141  204 NSVNRfGKTGNVEPFSLLALLPNSTDkYYTYNGSLTSPPCSETVEWIVFKHTVPISETQLEVFCEVM 270
Cdd:cd03124    134 PKKEG-TEVNLPAILDPNELLPESRS-YYRYEGSLTTPPCSEGVRWIVLKQPITISKEQLAKFRAAV 198
R-PTPc-typeIIb-2 cd14556
PTP domain of type IIb (or R2B) subfamily receptor-type tyrosine-protein phosphatases, repeat ...
1189-1391 3.43e-34

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: 130.60  E-value: 3.43e-34
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1925147141 1189 YINASYIMGYHKSREFILTQSPLPSTVSDFWRMVWDHNSQLIISLPDTHTAqregEESCA-YWPSKDQ----PISCEgfi 1263
Cdd:cd14556      1 YINAALLDSYKQPAAFIVTQHPLPNTVTDFWRLVYDYGCTSIVMLNQLDPK----DQSCPqYWPDEGSgtygPIQVE--- 73
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1925147141 1264 vsfsgedHMCLANEERLVVHDFLLEAT---QDNYVLeVRQYMSPCWPN----PDSPVSgTFQLLNIITEDSRQR-EGTIV 1335
Cdd:cd14556     74 -------FVSTTIDEDVISRIFRLQNTtrpQEGYRM-VQQFQFLGWPRdrdtPPSKRA-LLKLLSEVEKWQEQSgEGPIV 144
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 1925147141 1336 VHDRLGGSVAGLFCALTTLAQQLEHQGSVDVYQVARMTNLMRPGVFNDMEQYQFMY 1391
Cdd:cd14556    145 VHCLNGVGRSGVFCAISSVCERIKVENVVDVFQAVKTLRNHRPNMVETEEQYKFCY 200
Cah COG3338
Carbonic anhydrase [Inorganic ion transport and metabolism];
37-266 2.22e-33

Carbonic anhydrase [Inorganic ion transport and metabolism];


Pssm-ID: 442567 [Multi-domain]  Cd Length: 247  Bit Score: 129.62  E-value: 2.22e-33
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1925147141   37 DDIDWSYTGQLNQKIWGK---RYPACNN-ARQSPIDIDETftqVRVEYQGLQLEgwekNTPETTTINNDGNTVVLGLDGE 112
Cdd:COG3338     24 SAPHWSYEGETGPEHWGElspEFATCATgKNQSPIDIRTA---IKADLPPLKFD----YKPTPLEIVNNGHTIQVNVDPG 96
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1925147141  113 YYVSGGGlsTRFRLGRMTFHwgrcnassDGSEHSLNGLKFPLEMQiLCYESglyqsiddavrDGGRIAALAVLFETSlDN 192
Cdd:COG3338     97 STLTVDG--KRYELKQFHFH--------TPSEHTINGKSYPMEAH-LVHKD-----------ADGELAVVGVLFEEG-AE 153
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1925147141  193 NDNYNTILEGVNSVNRFGKTGNVePFSLLALLPNSTDkYYTYNGSLTSPPCSETVEWIVFKHTVPISETQLEVF 266
Cdd:COG3338    154 NPALAKLWANLPLEAGEEVALDA-TIDLNDLLPEDRS-YYRYSGSLTTPPCSEGVLWIVLKQPITVSAEQIEAF 225
PTPc-N18 cd14603
catalytic domain of tyrosine-protein phosphatase non-receptor type 18; Tyrosine-protein ...
1137-1394 5.45e-33

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: 129.17  E-value: 5.45e-33
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1925147141 1137 QFKLVSQRRAR-QADYA----AALREGNDDKNRTSSLMPVERSRVCLSCPVEGESSDYINASYIMGYHKSREFILTQSPL 1211
Cdd:cd14603      3 EFSEIRACSAAfKADYVcstvAGGRKENVKKNRYKDILPYDQTRVILSLLQEEGHSDYINANFIKGVDGSRAYIATQGPL 82
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1925147141 1212 PSTVSDFWRMVWDHNSQLIIslpdthTAQRE---GEESCA-YWPSKDQPISCEGFIVSFSGEDHMclaNEErLVVHDFLL 1287
Cdd:cd14603     83 SHTVLDFWRMIWQYGVKVIL------MACREiemGKKKCErYWAQEQEPLQTGPFTITLVKEKRL---NEE-VILRTLKV 152
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1925147141 1288 EATQDNYVLEVRQYMSpcWPN---PDSPvSGTFQLLNIITEdsRQREGT--IVVHDRLGGSVAGLFCALTTLAQQLEHQG 1362
Cdd:cd14603    153 TFQKESRSVSHFQYMA--WPDhgiPDSP-DCMLAMIELARR--LQGSGPepLCVHCSAGCGRTGVICTVDYVRQLLLTQR 227
                          250       260       270
                   ....*....|....*....|....*....|....*
gi 1925147141 1363 SVDVYQVARMTNLM---RPGVFNDMEQYQFMYRAV 1394
Cdd:cd14603    228 IPPDFSIFDVVLEMrkqRPAAVQTEEQYEFLYHTV 262
alpha_CA_VII cd03149
Carbonic anhydrase alpha, CA isozyme VII_like subgroup. Carbonic anhydrases (CAs) are ...
63-292 1.91e-31

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: 123.79  E-value: 1.91e-31
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1925147141   63 RQSPIDI-------DETFTQVRVEYqglqlegwekNTPETTTINNDGNTVVLGL---DGEYYVSGGGLSTRFRLGRMTFH 132
Cdd:cd03149      3 RQSPIDIvsseavyDPKLKPLSLSY----------DPCTSLSISNNGHSVMVEFddsDDKTVITGGPLENPYRLKQFHFH 72
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1925147141  133 WGRcnASSDGSEHSLNGLKFPLEMQILCYESGLYQSIDDAVRDGGRIAALAVLFETSlDNNDNYNTILEGVNSVNRFGKT 212
Cdd:cd03149     73 WGA--KHGSGSEHTVDGKTFPSELHLVHWNAKKYKSFGEAAAAPDGLAVLGVFLETG-DEHPGLNRLTDALYMVRFKGTK 149
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1925147141  213 GNVEPFSLLALLPNSTDkYYTYNGSLTSPPCSETVEWIVFKHTVPISETQLEVFCEVMTMQQAGYVMLMdylQNNFREQQ 292
Cdd:cd03149    150 AQFLDFNPKCLLPKSLD-YWTYPGSLTTPPLNESVTWIVLKEPIPVSEKQMGKFRELLFTSEEDQRNHM---VNNFRPPQ 225
PTPc-N5 cd14613
catalytic domain of tyrosine-protein phosphatase non-receptor type 5; Tyrosine-protein ...
1162-1397 3.28e-31

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: 123.82  E-value: 3.28e-31
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1925147141 1162 KNRTSSLMPVERSRVCLSCPVEGES-SDYINASYIMGY-HKSREFILTQSPLPSTVSDFWRMVWDHNSQLIISLpdthTA 1239
Cdd:cd14613     28 KNRYKTILPNPHSRVCLTSPDQDDPlSSYINANYIRGYgGEEKVYIATQGPTVNTVGDFWRMVWQERSPIIVMI----TN 103
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1925147141 1240 QREGEESCA-YWPSKDqpISCEGFIVSFSGEDHmclanEERLVVHDFLLEATQDNYVLevRQYMSPCWPNPDSPVSGTfQ 1318
Cdd:cd14613    104 IEEMNEKCTeYWPEEQ--VTYEGIEITVKQVIH-----ADDYRLRLITLKSGGEERGL--KHYWYTSWPDQKTPDNAP-P 173
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1925147141 1319 LLNII--TEDSRQRE----GTIVVHDRLGGSVAGLFCALTTLAQQLEHQGSVDVYQVARMTNLMRPGVFNDMEQYQFMYR 1392
Cdd:cd14613    174 LLQLVqeVEEARQQAepncGPVIVHCSAGIGRTGCFIATSICCKQLRNEGVVDILRTTCQLRLDRGGMIQTCEQYQFVHH 253

                   ....*
gi 1925147141 1393 aVLSL 1397
Cdd:cd14613    254 -VLSL 257
R-PTPc-LAR-1 cd14553
catalytic domain of LAR family receptor-type tyrosine-protein phosphatases, repeat 1; The LAR ...
1157-1400 3.63e-31

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: 123.28  E-value: 3.63e-31
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1925147141 1157 EGNDDKNRTSSLMPVERSRVCLScPVEG-ESSDYINASYIMGYHKSREFILTQSPLPSTVSDFWRMVWDHNSQLIISLpd 1235
Cdd:cd14553      1 EVNKPKNRYANVIAYDHSRVILQ-PIEGvPGSDYINANYCDGYRKQNAYIATQGPLPETFGDFWRMVWEQRSATIVMM-- 77
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1925147141 1236 THTAQREGEESCAYWPSKDQPiSCEGFIVSFSgeDHMCLANeerLVVHDFLLEATQDNYVLEVRQYMSPCWPN---PDSP 1312
Cdd:cd14553     78 TKLEERSRVKCDQYWPTRGTE-TYGLIQVTLL--DTVELAT---YTVRTFALHKNGSSEKREVRQFQFTAWPDhgvPEHP 151
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1925147141 1313 VSGTFQLLNIITEDSRQrEGTIVVHDRLGGSVAGLFCALTTLAQQLEHQGSVDVY-QVARMTNlMRPGVFNDMEQYQFMY 1391
Cdd:cd14553    152 TPFLAFLRRVKACNPPD-AGPIVVHCSAGVGRTGCFIVIDSMLERIKHEKTVDIYgHVTCLRA-QRNYMVQTEDQYIFIH 229

                   ....*....
gi 1925147141 1392 RAVLSLVDS 1400
Cdd:cd14553    230 DALLEAVTC 238
R-PTP-N2 cd14610
PTP-like domain of receptor-type tyrosine-protein phosphatase N2; Receptor-type ...
1112-1400 7.77e-31

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: 123.63  E-value: 7.77e-31
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1925147141 1112 TSDLVHSYVSDLLttgpSGRTRMERQFKLVSQRRARQADYAAALREGNDDKNRTSSLMPVERSRVCLSCPVEGESSDYIN 1191
Cdd:cd14610      1 TGHMILSYMEDHL----KNKNRLEKEWEALCAYQAEPNATNVAQREENVQKNRSLAVLPYDHSRIILKAENSHSHSDYIN 76
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1925147141 1192 ASYIMGyHKSRE--FILTQSPLPSTVSDFWRMVWDHNSQLIISLpdTHTAQREGEESCAYWPSKDQPIScEGFIVSFSGE 1269
Cdd:cd14610     77 ASPIMD-HDPRNpaYIATQGPLPATVADFWQMVWESGCVVIVML--TPLAENGVKQCYHYWPDEGSNLY-HIYEVNLVSE 152
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1925147141 1270 DHMClaneERLVVHDFLLEATQDNYVLEVRQYMSPCWPNPDSPVSgTFQLLNI---ITEDSRQREGTIVVHDRLGGSVAG 1346
Cdd:cd14610    153 HIWC----EDFLVRSFYLKNLQTNETRTVTQFHFLSWNDQGVPAS-TRSLLDFrrkVNKCYRGRSCPIIVHCSDGAGRSG 227
                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 1925147141 1347 LFCALTTLAQQLEhQGSVDVYQVARMTNL--MRPGVFNDMEQYQFMYRAVLSLVDS 1400
Cdd:cd14610    228 TYILIDMVLNKMA-KGAKEIDIAATLEHLrdQRPGMVQTKEQFEFALTAVAEEVNA 282
R-PTPc-V cd14618
catalytic domain of receptor-type tyrosine-protein phosphatase V; Receptor-type ...
1163-1395 2.62e-30

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: 120.43  E-value: 2.62e-30
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1925147141 1163 NRTSSLMPVERSRVCLSCPVEGESSDYINASYIMGYHKSREFILTQSPLPSTVSDFWRMVWDHNSQLIISLPdthTAQRE 1242
Cdd:cd14618      1 NRYPHVLPYDHSRVRLSQLGGEPHSDYINANFIPGYTSPQEFIATQGPLKKTIEDFWRLVWEQQVCNIIMLT---VGMEN 77
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1925147141 1243 GEESCA-YWPSKDQPISCEGFIVSFSGEDhmclaNEERLVVHDFLLEATQDNYVLEVRQYMSPCWPN---PDSPVS-GTF 1317
Cdd:cd14618     78 GRVLCDhYWPSESTPVSYGHITVHLLAQS-----SEDEWTRREFKLWHEDLRKERRVKHLHYTAWPDhgiPESTSSlMAF 152
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1925147141 1318 QLLNIITEDSRQREGTIVVHDRLGGSVAGLFCALTTLAQQLEHQGSVDVYQVARMTNLMRPGVFNDMEQYQFMYRAVL 1395
Cdd:cd14618    153 RELVREHVQATKGKGPTLVHCSAGVGRSGTFIALDRLLRQLKEEKVVDVFNTVYILRMHRYLMIQTLSQYIFLHSCIL 230
alpha_CARP_VIII cd03120
Carbonic anhydrase alpha related protein, group VIII. Carbonic anhydrase related proteins ...
52-292 4.48e-30

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: 120.73  E-value: 4.48e-30
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1925147141   52 WGKRYPACNNARQSPIDI-------DETFTQVRVEYQGLQLEGWEkntpetttINNDGNTVVLGLDGEYYVSGGGL--ST 122
Cdd:cd03120      4 WGLLFPEANGEYQSPINLnsrearyDPSLLEVRLSPNYVVCRDCE--------VINDGHTIQIILKSKSVLSGGPLpqGH 75
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1925147141  123 RFRLGRMTFHWGRCNasSDGSEHSLNGLKFPLEMQILCYESGLYQSIDDAVRDGGRIAALAvLFETSLDNNDNYNTILEG 202
Cdd:cd03120     76 EFELAEVRFHWGREN--QRGSEHTVNFKAFPMELHLIHWNSTLYSSLEEAMGKPHGIAIIA-LFVQIGKEHVGLKAVTEI 152
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1925147141  203 VNSVNRFGKTGNVEPFSLLALLPNSTDK-YYTYNGSLTSPPCSETVEWIVFKHTVPISETQLEVFCEVMT-MQQAGYVML 280
Cdd:cd03120    153 LQDIQYKGKSKTIPCFNPNTLLPDPLLRdYWVYEGSLTTPPCSEGVTWILFRYPLTISQSQIEEFRRLRThVKGAELVEG 232
                          250
                   ....*....|...
gi 1925147141  281 MDY-LQNNFREQQ 292
Cdd:cd03120    233 CDGlLGDNFRPTQ 245
alpha_CA_I_II_III_XIII cd03119
Carbonic anhydrase alpha, isozymes I, II, and III and XIII. Carbonic anhydrases (CAs) are ...
40-266 1.99e-29

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: 118.70  E-value: 1.99e-29
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1925147141   40 DWSYTGQLNQKIWGKRYPACNNARQSPIDIDETFTQVRVEYQGLQLegweKNTPETT-TINNDGNTVVLGLDGEYYVS-- 116
Cdd:cd03119      4 HWGYDSHNGPEHWHELFPIAKGDRQSPIDIKTKDAKHDPSLKPLSV----SYDPATAkTILNNGHSFNVEFDDTDDRSvl 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1925147141  117 -GGGLSTRFRLGRMTFHWGRCNasSDGSEHSLNGLKFPLEMQILCYESGlYQSIDDAVRDGGRIAALAVLFETSlDNNDN 195
Cdd:cd03119     80 rGGPLTGSYRLRQFHFHWGSSD--DHGSEHTVDGVKYAAELHLVHWNSK-YGSFGEAAKQPDGLAVVGVFLKVG-EANPE 155
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1925147141  196 YNTILEGVNSVNRFGKTGNVEPFSLLALLPNSTDkYYTYNGSLTSPPCSETVEWIVFKHTVPISETQLEVF 266
Cdd:cd03119    156 LQKVLDALDSIKTKGKQAPFTNFDPSCLLPASLD-YWTYPGSLTTPPLLECVTWIVLKEPISVSSEQMAKF 225
R-PTPc-O cd14614
catalytic domain of receptor-type tyrosine-protein phosphatase O; Receptor-type ...
1159-1395 2.50e-29

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: 118.07  E-value: 2.50e-29
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1925147141 1159 NDDKNRTSSLMPVERSRVCLSCPVEGESSDYINASYIMGYHKSREFILTQSPLPSTVSDFWRMVWDHNSQLIISLpdTHT 1238
Cdd:cd14614     12 NRCKNRYTNILPYDFSRVKLVSMHEEEGSDYINANYIPGYNSPQEYIATQGPLPETRNDFWKMVLQQKSQIIVML--TQC 89
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1925147141 1239 AQREGEESCAYWPSKDQPISCEGFIVSFSGEDhmclaNEERLVVHDFLL---EATQDnyvleVRQYMSPCWPNPDSPVSG 1315
Cdd:cd14614     90 NEKRRVKCDHYWPFTEEPVAYGDITVEMLSEE-----EQPDWAIREFRVsyaDEVQD-----VMHFNYTAWPDHGVPTAN 159
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1925147141 1316 T----FQLLNIITEDSRQREGTIVVHDRLGGSVAGLFCALTTLAQQLEHQGSVDVYQVARMTNLMRPGVFNDMEQYQFMY 1391
Cdd:cd14614    160 AaesiLQFVQMVRQQAVKSKGPMIIHCSAGVGRTGTFIALDRLLQHIRDHEFVDILGLVSEMRSYRMSMVQTEEQYIFIH 239

                   ....
gi 1925147141 1392 RAVL 1395
Cdd:cd14614    240 QCVQ 243
PTPc-N12 cd14604
catalytic domain of tyrosine-protein phosphatase non-receptor type 12; Tyrosine-protein ...
1156-1401 6.13e-29

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: 118.50  E-value: 6.13e-29
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1925147141 1156 REGNDDKNRTSSLMPVERSRVCLSCPVEGESSDYINASYIMGYHKSREFILTQSPLPSTVSDFWRMVWDHNSQLIIslpd 1235
Cdd:cd14604     54 KEENVKKNRYKDILPFDHSRVKLTLKTSSQDSDYINANFIKGVYGPKAYIATQGPLANTVIDFWRMIWEYNVAIIV---- 129
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1925147141 1236 thTAQRE---GEESCA-YWPS-KDQPISCEGFIVSfsgedhmCLANEER--LVVHDFLLEATQDNYVLEVRQYMSpcWPN 1308
Cdd:cd14604    130 --MACREfemGRKKCErYWPLyGEEPMTFGPFRIS-------CEAEQARtdYFIRTLLLEFQNETRRLYQFHYVN--WPD 198
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1925147141 1309 PDSPVS--GTFQLLNIITEDSRQREGTIVVHDRLGGSVAGLFCALtTLAQQLEHQGSV----DVYQVARMTNLMRPGVFN 1382
Cdd:cd14604    199 HDVPSSfdSILDMISLMRKYQEHEDVPICIHCSAGCGRTGAICAI-DYTWNLLKAGKIpeefNVFNLIQEMRTQRHSAVQ 277
                          250
                   ....*....|....*....
gi 1925147141 1383 DMEQYQFMYRAVLSLVDSQ 1401
Cdd:cd14604    278 TKEQYELVHRAIAQLFEKQ 296
R5-PTP-2 cd14550
PTP-like domain of R5 subfamily receptor-type tyrosine-protein phosphatases, repeat 2; The R5 ...
894-1096 9.70e-29

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


Pssm-ID: 350398 [Multi-domain]  Cd Length: 200  Bit Score: 114.73  E-value: 9.70e-29
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1925147141  894 YINANFVDGFERTRAYIAAQGPLKSGTEDFWRMVWQENVGVIVMITNLLEKGrrKCDQYWPMENQE-EYGHFLVTLKDTK 972
Cdd:cd14550      1 YINASYLQGYRRSNEFIITQHPLEHTIKDFWQMIWDHNSQTIVMLTDNELNE--DEPIYWPTKEKPlECETFKVTLSGED 78
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1925147141  973 TLAYYTLRTFTLRDTSQKASQRGRcaERTVVQYHYTQWPDMGVPEYTlpVLSFVRASTQARTQDMGPVLVHCSAGVGRTG 1052
Cdd:cd14550     79 HSCLSNEIRLIVRDFILESTQDDY--VLEVRQFQCPSWPNPCSPIHT--VFELINTVQEWAQQRDGPIVVHDRYGGVQAA 154
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....
gi 1925147141 1053 TYIVLDSMLQQIQDQGTVNILGFLKHVRTQRNYLVQTEEQYVFI 1096
Cdd:cd14550    155 TFCALTTLHQQLEHESSVDVYQVAKLYHLMRPGVFTSKEDYQFL 198
PTPc-N9 cd14543
catalytic domain of tyrosine-protein phosphatase non-receptor type 9; Tyrosine-protein ...
1144-1391 1.05e-28

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: 117.08  E-value: 1.05e-28
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1925147141 1144 RRARQADYAAALREGNDDKNRTSSLMPVERSRVCLSCPVEGESSDYINASYIMGYHKSREFILTQSPLPSTVSDFWRMVW 1223
Cdd:cd14543     14 REPPAGTFLCSLAPANQEKNRYGDVLCLDQSRVKLPKRNGDERTDYINANFMDGYKQKNAYIATQGPLPKTYSDFWRMVW 93
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1925147141 1224 DHNSQLIISLpdTHTAQReGEESCA-YWPSKDQPISCEGFIVSfsgeDHMCLANEERLVVHDFLLEATQDNyvlEVR--- 1299
Cdd:cd14543     94 EQKVLVIVMT--TRVVER-GRVKCGqYWPLEEGSSLRYGDLTV----TNLSVENKEHYKKTTLEIHNTETD---ESRqvt 163
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1925147141 1300 --QYMSpcWPN---PDSPVSgtfqLLNIITEDSRQ----------------REGTIVVHDRLGGSVAGLFCALTTLAQQL 1358
Cdd:cd14543    164 hfQFTS--WPDfgvPSSAAA----LLDFLGEVRQQqalavkamgdrwkghpPGPPIVVHCSAGIGRTGTFCTLDICLSQL 237
                          250       260       270
                   ....*....|....*....|....*....|...
gi 1925147141 1359 EHQGSVDVYQVARMTNLMRPGVFNDMEQYQFMY 1391
Cdd:cd14543    238 EDVGTLNVMQTVRRMRTQRAFSIQTPDQYYFCY 270
R-PTPc-T-1 cd14630
catalytic domain of receptor-type tyrosine-protein phosphatase T, repeat 1; Receptor-type ...
1159-1395 1.30e-28

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: 115.89  E-value: 1.30e-28
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1925147141 1159 NDDKNRTSSLMPVERSRVCLSCPVEGESSDYINASYIMGYHKSREFILTQSPLPSTVSDFWRMVWDHNSQLIISLPDTHT 1238
Cdd:cd14630      3 NRNKNRYGNIISYDHSRVRLQLLDGDPHSDYINANYIDGYHRPRHYIATQGPMQETVKDFWRMIWQENSASVVMVTNLVE 82
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1925147141 1239 AqreGEESCA-YWPSKDQpiscegfivsFSGEDHMCLANEERL---VVHDFLLEATQDNYVLEVRQYMSPCWPNPDSP-- 1312
Cdd:cd14630     83 V---GRVKCVrYWPDDTE----------VYGDIKVTLIETEPLaeyVIRTFTVQKKGYHEIREIRQFHFTSWPDHGVPcy 149
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1925147141 1313 VSGTFQLLNIITEDSRQREGTIVVHDRLGGSVAGLFCALTTLAQQLEHQGSVDVYQVARMTNLMRPGVFNDMEQYQFMYR 1392
Cdd:cd14630    150 ATGLLGFVRQVKFLNPPDAGPIVVHCSAGAGRTGCFIAIDIMLDMAENEGVVDIFNCVRELRAQRVNMVQTEEQYVFVHD 229

                   ...
gi 1925147141 1393 AVL 1395
Cdd:cd14630    230 AIL 232
R-PTPc-M-1 cd14633
catalytic domain of receptor-type tyrosine-protein phosphatase M, repeat 1; Receptor-type ...
1146-1395 1.34e-28

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: 116.68  E-value: 1.34e-28
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1925147141 1146 ARQADYAAALREGNDDKNRTSSLMPVERSRVCLScPVEGES-SDYINASYIMGYHKSREFILTQSPLPSTVSDFWRMVWD 1224
Cdd:cd14633     27 GQSAPWDSAKKDENRMKNRYGNIIAYDHSRVRLQ-PIEGETsSDYINGNYIDGYHRPNHYIATQGPMQETIYDFWRMVWH 105
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1925147141 1225 HNSQLIISLpdTHTAQREGEESCAYWPSkDQPISCEGFIVSFSGEdhmcLANEerLVVHDFLLEATQDNYVLEVRQYMSP 1304
Cdd:cd14633    106 ENTASIIMV--TNLVEVGRVKCCKYWPD-DTEIYKDIKVTLIETE----LLAE--YVIRTFAVEKRGVHEIREIRQFHFT 176
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1925147141 1305 CWPNPDSP--VSGTFQLLNIITEDSRQREGTIVVHDRLGGSVAGLFCALTTLAQQLEHQGSVDVYQVARMTNLMRPGVFN 1382
Cdd:cd14633    177 GWPDHGVPyhATGLLGFVRQVKSKSPPNAGPLVVHCSAGAGRTGCFIVIDIMLDMAEREGVVDIYNCVRELRSRRVNMVQ 256
                          250
                   ....*....|...
gi 1925147141 1383 DMEQYQFMYRAVL 1395
Cdd:cd14633    257 TEEQYVFIHDAIL 269
R-PTPc-A-1 cd14621
catalytic domain of receptor-type tyrosine-protein phosphatase A, repeat 1; Receptor-type ...
1148-1395 3.29e-28

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: 116.28  E-value: 3.29e-28
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1925147141 1148 QADYAAALREGNDDKNRTSSLMPVERSRVCLScPVEG-ESSDYINASYIMGYHKSREFILTQSPLPSTVSDFWRMVWDHN 1226
Cdd:cd14621     41 QATCEAASKEENKEKNRYVNILPYDHSRVHLT-PVEGvPDSDYINASFINGYQEKNKFIAAQGPKEETVNDFWRMIWEQN 119
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1925147141 1227 SQLIISLpdTHTAQREGEESCAYWPskDQPISCEGFIvSFSGEDHMCLANeerLVVHDFLLEATQDNYVLE----VRQYM 1302
Cdd:cd14621    120 TATIVMV--TNLKERKECKCAQYWP--DQGCWTYGNI-RVSVEDVTVLVD---YTVRKFCIQQVGDVTNKKpqrlITQFH 191
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1925147141 1303 SPCWPN---PDSPVsGTFQLLNIITEDSRQREGTIVVHDRLGGSVAGLFCALTTLAQQLEHQGSVDVYQVARMTNLMRPG 1379
Cdd:cd14621    192 FTSWPDfgvPFTPI-GMLKFLKKVKNCNPQYAGAIVVHCSAGVGRTGTFIVIDAMLDMMHAERKVDVYGFVSRIRAQRCQ 270
                          250
                   ....*....|....*.
gi 1925147141 1380 VFNDMEQYQFMYRAVL 1395
Cdd:cd14621    271 MVQTDMQYVFIYQALL 286
R-PTPc-R cd14611
catalytic domain of receptor-type tyrosine-protein phosphatase R; Receptor-type ...
1162-1391 3.30e-28

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: 114.24  E-value: 3.30e-28
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1925147141 1162 KNRTSSLMPVERSRVCLSCPVEGES-SDYINASYIMGYH-KSREFILTQSPLPSTVSDFWRMVWDHNSQLIISLpdthTA 1239
Cdd:cd14611      2 KNRYKTILPNPHSRVCLKPKNSNDSlSTYINANYIRGYGgKEKAFIATQGPMINTVNDFWQMVWQEDSPVIVMI----TK 77
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1925147141 1240 QREGEESCA-YWPSKDQPI-SCEGFIVSFSGEDHMCLANeerlvvhdflLEATQDNYVLEVRQYMSPCWPNPDSPVSGT- 1316
Cdd:cd14611     78 LKEKNEKCVlYWPEKRGIYgKVEVLVNSVKECDNYTIRN----------LTLKQGSQSRSVKHYWYTSWPDHKTPDSAQp 147
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1925147141 1317 -FQLLNIITEDSR--QREGTIVVHDRLGGSVAGLFCALTTLAQQLEHQGSVDVYQVARMTNLMRPGVFNDMEQYQFMY 1391
Cdd:cd14611    148 lLQLMLDVEEDRLasPGRGPVVVHCSAGIGRTGCFIATTIGCQQLKEEGVVDVLSIVCQLRVDRGGMVQTSEQYEFVH 225
PTPc-N22 cd14602
catalytic domain of tyrosine-protein phosphatase non-receptor type 22; Tyrosine-protein ...
1162-1397 1.04e-27

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: 113.01  E-value: 1.04e-27
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1925147141 1162 KNRTSSLMPVERSRVCLSCPVEGESSDYINASYIMGYHKSREFILTQSPLPSTVSDFWRMVWDHNSQLIIslpdthTAQR 1241
Cdd:cd14602      1 KNRYKDILPYDHSRVELSLITSDEDSDYINANFIKGVYGPRAYIATQGPLSTTLLDFWRMIWEYSVLIIV------MACM 74
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1925147141 1242 E---GEESCA-YWP-SKDQPISCEGFIVSFSGEDhmclaNEERLVVHdfLLEATQDNYVLEVRQYMSPCWPNPDSPvSGT 1316
Cdd:cd14602     75 EfemGKKKCErYWAePGEMQLEFGPFSVTCEAEK-----RKSDYIIR--TLKVKFNSETRTIYQFHYKNWPDHDVP-SSI 146
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1925147141 1317 FQLLNIITE-DSRQREGT--IVVHDRLGGSVAGLFCALTTLAQQLEhQGSV----DVYQVARMTNLMRPGVFNDMEQYQF 1389
Cdd:cd14602    147 DPILELIWDvRCYQEDDSvpICIHCSAGCGRTGVICAIDYTWMLLK-DGIIpenfSVFSLIQEMRTQRPSLVQTKEQYEL 225

                   ....*...
gi 1925147141 1390 MYRAVLSL 1397
Cdd:cd14602    226 VYNAVIEL 233
R-PTPc-E-1 cd14620
catalytic domain of receptor-type tyrosine-protein phosphatase E, repeat 1; Receptor-type ...
1167-1395 1.44e-27

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: 112.34  E-value: 1.44e-27
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1925147141 1167 SLMPVERSRVCLScPVEG-ESSDYINASYIMGYHKSREFILTQSPLPSTVSDFWRMVWDHNSQLIISLpdTHTAQREGEE 1245
Cdd:cd14620      3 NILPYDHSRVILS-QLDGiPCSDYINASYIDGYKEKNKFIAAQGPKQETVNDFWRMVWEQKSATIVML--TNLKERKEEK 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1925147141 1246 SCAYWPskDQPISCEGFIvSFSGEDHMCLANeerLVVHDFLLEATQDNYVLEVR---QYMSPCWPN---PDSPVsGTFQL 1319
Cdd:cd14620     80 CYQYWP--DQGCWTYGNI-RVAVEDCVVLVD---YTIRKFCIQPQLPDGCKAPRlvtQLHFTSWPDfgvPFTPI-GMLKF 152
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1925147141 1320 LNIITEDSRQREGTIVVHDRLGGSVAGLFCALTTLAQQLEHQGSVDVYQ-VARMTNLMRPGVFNDMeQYQFMYRAVL 1395
Cdd:cd14620    153 LKKVKSVNPVHAGPIVVHCSAGVGRTGTFIVIDAMIDMMHAEQKVDVFEfVSRIRNQRPQMVQTDM-QYSFIYQALL 228
R-PTPc-B cd14617
catalytic domain of receptor-type tyrosine-protein phosphatase B; Receptor-type ...
1163-1392 2.95e-27

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: 111.55  E-value: 2.95e-27
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1925147141 1163 NRTSSLMPVERSRVCLSCPVEGESSDYINASYIMGYHKSREFILTQSPLPSTVSDFWRMVWDHNSQLIISLpdTHTAQRe 1242
Cdd:cd14617      1 NRYNNILPYDSTRVKLSNVDDDPCSDYINASYIPGNNFRREYIATQGPLPGTKDDFWKMVWEQNVHNIVMV--TQCVEK- 77
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1925147141 1243 GEESC-AYWPSKDQPISCEGFIVSFSGEDHMclaneERLVVHDF-LLEATQDNYVLEVRQYMSPCWpnPDSPVSGTFQLL 1320
Cdd:cd14617     78 GRVKCdHYWPADQDSLYYGDLIVQMLSESVL-----PEWTIREFkICSEEQLDAPRLVRHFHYTVW--PDHGVPETTQSL 150
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1925147141 1321 NIITEDSRQ------REGTIVVHDRLGGSVAGLFCALTTLAQQLEHQGSVDVYQVARMTNLMRPGVFNDMEQYQFMYR 1392
Cdd:cd14617    151 IQFVRTVRDyinrtpGSGPTVVHCSAGVGRTGTFIALDRILQQLDSKDSVDIYGAVHDLRLHRVHMVQTECQYVYLHQ 228
R-PTPc-S-1 cd14625
catalytic domain of receptor-type tyrosine-protein phosphatase S, repeat 1; Receptor-type ...
1157-1398 3.07e-27

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: 113.26  E-value: 3.07e-27
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1925147141 1157 EGNDDKNRTSSLMPVERSRVCLScPVEG-ESSDYINASYIMGYHKSREFILTQSPLPSTVSDFWRMVWDHNSQLIISLpd 1235
Cdd:cd14625     45 EVNKPKNRYANVIAYDHSRVILQ-PIEGiMGSDYINANYIDGYRKQNAYIATQGPLPETFGDFWRMVWEQRSATVVMM-- 121
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1925147141 1236 THTAQREGEESCAYWPSKDQpiSCEGFIvSFSGEDHMCLANeerLVVHDFLLEATQDNYVLEVRQYMSPCWPNPDSPVSG 1315
Cdd:cd14625    122 TKLEEKSRIKCDQYWPSRGT--ETYGMI-QVTLLDTIELAT---FCVRTFSLHKNGSSEKREVRQFQFTAWPDHGVPEYP 195
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1925147141 1316 T--FQLLNIITEDSRQREGTIVVHDRLGGSVAGLFCALTTLAQQLEHQGSVDVYQVARMTNLMRPGVFNDMEQYQFMYRA 1393
Cdd:cd14625    196 TpfLAFLRRVKTCNPPDAGPIVVHCSAGVGRTGCFIVIDAMLERIKHEKTVDIYGHVTLMRSQRNYMVQTEDQYSFIHDA 275

                   ....*
gi 1925147141 1394 VLSLV 1398
Cdd:cd14625    276 LLEAV 280
alpha_CA_V cd03118
Carbonic anhydrase alpha, CA isozyme V_like subgroup. Carbonic anhydrases (CAs) are ...
63-303 3.85e-27

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: 111.47  E-value: 3.85e-27
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1925147141   63 RQSPIDI-------DETFTQVRVEYQglqlegwekntPETTT-INNDGNTVVLGLDG---EYYVSGGGLSTRFRLGRMTF 131
Cdd:cd03118      3 RQSPINIqwrdsvyDPQLAPLRVSYD-----------PATCLyIWNNGYSFQVEFDDstdKSGISGGPLENHYRLKQFHF 71
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1925147141  132 HWGRCNASsdGSEHSLNGLKFPLEMQILCYESGLYQSIDDAVRDGGRIAALAVLFETSlDNNDNYNTILEGVNSVNRFGK 211
Cdd:cd03118     72 HWGANNEW--GSEHTVDGHTYPAELHLVHWNSVKYENFEEAVMEENGLAVIGVFLKLG-AHHEGLQKLVDALPEVRHKDT 148
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1925147141  212 TGNVEPFSLLALLPNSTDkYYTYNGSLTSPPCSETVEWIVFKHTVPISETQLEVFcEVMTMQQAGYVmlMDYLQNNFREQ 291
Cdd:cd03118    149 VVEFNPFDPSCLLPACRD-YWTYPGSLTTPPLTESVTWIIQKQPIEVSPSQLSVF-RTLLFTSRGEE--EKVMVNNFRPL 224
                          250
                   ....*....|..
gi 1925147141  292 QQQFLGQVFSSY 303
Cdd:cd03118    225 QPLMNRKVRSSF 236
R-PTPc-Q cd14616
catalytic domain of receptor-type tyrosine-protein phosphatase Q; Receptor-type ...
1163-1392 4.73e-27

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: 110.77  E-value: 4.73e-27
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1925147141 1163 NRTSSLMPVERSRVCLSCPVEGESSDYINASYIMGYHKSREFILTQSPLPSTVSDFWRMVWDHNSQLIISLPDTHtaqRE 1242
Cdd:cd14616      1 NRFPNIKPYNNNRVKLIADAGVPGSDYINASYISGYLCPNEFIATQGPLPGTVGDFWRMVWETRAKTIVMLTQCF---EK 77
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1925147141 1243 GEESC-AYWPSKDQPISCEGFIV-SFSGEDhmclaNEERLVVHDFLLEATQDnYVLeVRQYMSPCWPNPDSPVSGT--FQ 1318
Cdd:cd14616     78 GRIRChQYWPEDNKPVTVFGDIViTKLMED-----VQIDWTIRDLKIERHGD-YMM-VRQCNFTSWPEHGVPESSAplIH 150
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1925147141 1319 LLNIITEDSRQREGTIVVHDRLGGSVAGLFCALTTLAQQLEHQGSVDVYQVARMTNLMRPGVFNDMEQYQFMYR 1392
Cdd:cd14616    151 FVKLVRASRAHDNTPMIVHCSAGVGRTGVFIALDHLTQHINDHDFVDIYGLVAELRSERMCMVQNLAQYIFLHQ 224
R-PTPc-F-1 cd14626
catalytic domain of receptor-type tyrosine-protein phosphatase F, repeat 1; Receptor-type ...
1157-1395 4.98e-27

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: 112.44  E-value: 4.98e-27
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1925147141 1157 EGNDDKNRTSSLMPVERSRVCLScPVEG-ESSDYINASYIMGYHKSREFILTQSPLPSTVSDFWRMVWDHNSQLIISLpd 1235
Cdd:cd14626     39 EVNKPKNRYANVIAYDHSRVILT-SVDGvPGSDYINANYIDGYRKQNAYIATQGPLPETLSDFWRMVWEQRTATIVMM-- 115
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1925147141 1236 THTAQREGEESCAYWPSKdqpiSCEGF-IVSFSGEDHMCLANeerLVVHDFLLEATQDNYVLEVRQYMSPCWPN---PDS 1311
Cdd:cd14626    116 TRLEEKSRVKCDQYWPIR----GTETYgMIQVTLLDTVELAT---YSVRTFALYKNGSSEKREVRQFQFMAWPDhgvPEY 188
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1925147141 1312 PvSGTFQLLNIITEDSRQREGTIVVHDRLGGSVAGLFCALTTLAQQLEHQGSVDVYQVARMTNLMRPGVFNDMEQYQFMY 1391
Cdd:cd14626    189 P-TPILAFLRRVKACNPPDAGPMVVHCSAGVGRTGCFIVIDAMLERMKHEKTVDIYGHVTCMRSQRNYMVQTEDQYIFIH 267

                   ....
gi 1925147141 1392 RAVL 1395
Cdd:cd14626    268 EALL 271
R5-PTPc-1 cd14549
catalytic domain of R5 subfamily receptor-type tyrosine-protein phosphatases, repeat 1; The R5 ...
1189-1391 5.18e-27

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: 110.13  E-value: 5.18e-27
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1925147141 1189 YINASYIMGYHKSREFILTQSPLPSTVSDFWRMVWDHNSQLIISLpdTHTAQReGEESCA-YWPSKDQPiSCEGFIVSFS 1267
Cdd:cd14549      1 YINANYVDGYNKARAYIATQGPLPSTFDDFWRMVWEQNSAIIVMI--TNLVER-GRRKCDqYWPKEGTE-TYGNIQVTLL 76
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1925147141 1268 GEDHMclANeerLVVHDFLLEATQDNYVLE------VRQYMSPCWPN---PDSPVSgtfqLLNIITEDSRQR---EGTIV 1335
Cdd:cd14549     77 STEVL--AT---YTVRTFSLKNLKLKKVKGrsservVYQYHYTQWPDhgvPDYTLP----VLSFVRKSSAANppgAGPIV 147
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 1925147141 1336 VHDRLGGSVAGLFCALTTLAQQLEHQGSVDVYQVARMTNLMRPGVFNDMEQYQFMY 1391
Cdd:cd14549    148 VHCSAGVGRTGTYIVIDSMLQQIQDKGTVNVFGFLKHIRTQRNYLVQTEEQYIFIH 203
R-PTPc-typeIIb-1 cd14555
catalytic domain of type IIb (or R2B) subfamily receptor-type tyrosine-protein phosphatases, ...
1189-1395 5.50e-27

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: 110.01  E-value: 5.50e-27
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1925147141 1189 YINASYIMGYHKSREFILTQSPLPSTVSDFWRMVWDHNSQLIISLpdTHTAQREGEESCAYWPSKDQpiscegfivsFSG 1268
Cdd:cd14555      1 YINANYIDGYHRPNHYIATQGPMQETVYDFWRMVWQENSASIVMV--TNLVEVGRVKCSRYWPDDTE----------VYG 68
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1925147141 1269 EDHMCLANEERL---VVHDFLLEATQDNYVLEVRQYMSPCWPNPDSP--VSGTFQLLNIITEDSRQREGTIVVHDRLGGS 1343
Cdd:cd14555     69 DIKVTLVETEPLaeyVVRTFALERRGYHEIREVRQFHFTGWPDHGVPyhATGLLGFIRRVKASNPPSAGPIVVHCSAGAG 148
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|..
gi 1925147141 1344 VAGLFCALTTLAQQLEHQGSVDVYQVARMTNLMRPGVFNDMEQYQFMYRAVL 1395
Cdd:cd14555    149 RTGCYIVIDIMLDMAEREGVVDIYNCVKELRSRRVNMVQTEEQYIFIHDAIL 200
PTPc-N11_6 cd14544
catalytic domain of tyrosine-protein phosphatase non-receptor type 11 and type 6; ...
1159-1394 5.63e-27

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: 111.40  E-value: 5.63e-27
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1925147141 1159 NDDKNRTSSLMPVERSRVCLS-CPVEGESSDYINASYIM-------GYHKSREFILTQSPLPSTVSDFWRMVWDHNSQLI 1230
Cdd:cd14544      1 NKGKNRYKNILPFDHTRVILKdRDPNVPGSDYINANYIRnenegptTDENAKTYIATQGCLENTVSDFWSMVWQENSRVI 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1925147141 1231 ISlpdTHTAQREGEESCA-YWPSKdqpiscegfiVSFSGEDHMCLANEERLVVHDFLL------EATQDNYVLEVRQYMS 1303
Cdd:cd14544     81 VM---TTKEVERGKNKCVrYWPDE----------GMQKQYGPYRVQNVSEHDTTDYTLrelqvsKLDQGDPIREIWHYQY 147
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1925147141 1304 PCWPN---PDSPvSGTFQLLNII--TEDSRQREGTIVVHDRLGGSVAGLFCALTTLAQQLEHQG---SVDVYQVARMTNL 1375
Cdd:cd14544    148 LSWPDhgvPSDP-GGVLNFLEDVnqRQESLPHAGPIVVHCSAGIGRTGTFIVIDMLLDQIKRKGldcDIDIQKTIQMVRS 226
                          250
                   ....*....|....*....
gi 1925147141 1376 MRPGVFNDMEQYQFMYRAV 1394
Cdd:cd14544    227 QRSGMVQTEAQYKFIYVAV 245
R-PTPc-D-1 cd14624
catalytic domain of receptor-type tyrosine-protein phosphatase D, repeat 1; Receptor-type ...
1157-1398 6.72e-26

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: 109.44  E-value: 6.72e-26
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1925147141 1157 EGNDDKNRTSSLMPVERSRVCLSCpVEG-ESSDYINASYIMGYHKSREFILTQSPLPSTVSDFWRMVWDHNSQLIISLpd 1235
Cdd:cd14624     45 EVNKPKNRYANVIAYDHSRVLLSA-IEGiPGSDYINANYIDGYRKQNAYIATQGALPETFGDFWRMIWEQRSATVVMM-- 121
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1925147141 1236 THTAQREGEESCAYWPSKDQPISCegfIVSFSGEDHMCLANeerLVVHDFLLEATQDNYVLEVRQYMSPCWPNPDSPVSG 1315
Cdd:cd14624    122 TKLEERSRVKCDQYWPSRGTETYG---LIQVTLLDTVELAT---YCVRTFALYKNGSSEKREVRQFQFTAWPDHGVPEHP 195
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1925147141 1316 T--FQLLNIITEDSRQREGTIVVHDRLGGSVAGLFCALTTLAQQLEHQGSVDVYQVARMTNLMRPGVFNDMEQYQFMYRA 1393
Cdd:cd14624    196 TpfLAFLRRVKTCNPPDAGPMVVHCSAGVGRTGCFIVIDAMLERIKHEKTVDIYGHVTLMRAQRNYMVQTEDQYIFIHDA 275

                   ....*
gi 1925147141 1394 VLSLV 1398
Cdd:cd14624    276 LLEAV 280
PTPc-N1 cd14608
catalytic domain of tyrosine-protein phosphatase non-receptor type 1; Tyrosine-protein ...
1159-1395 1.10e-25

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: 108.57  E-value: 1.10e-25
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1925147141 1159 NDDKNRTSSLMPVERSRVCLscpvEGESSDYINASYIMGYHKSREFILTQSPLPSTVSDFWRMVWDHNSQLIISLpdtHT 1238
Cdd:cd14608     25 NKNRNRYRDVSPFDHSRIKL----HQEDNDYINASLIKMEEAQRSYILTQGPLPNTCGHFWEMVWEQKSRGVVML---NR 97
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1925147141 1239 AQREGEESCA-YWPSK-DQPISCE--GFIVSFSGEDHMCLANEERLVVHDFLLEATQdnyvlEVRQYMSPCWPN---PDS 1311
Cdd:cd14608     98 VMEKGSLKCAqYWPQKeEKEMIFEdtNLKLTLISEDIKSYYTVRQLELENLTTQETR-----EILHFHYTTWPDfgvPES 172
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1925147141 1312 PVSGTFQLLNIITEDSRQRE-GTIVVHDRLGGSVAGLFCALTT---LAQQLEHQGSVDVYQVARMTNLMRPGVFNDMEQY 1387
Cdd:cd14608    173 PASFLNFLFKVRESGSLSPEhGPVVVHCSAGIGRSGTFCLADTcllLMDKRKDPSSVDIKKVLLEMRKFRMGLIQTADQL 252

                   ....*...
gi 1925147141 1388 QFMYRAVL 1395
Cdd:cd14608    253 RFSYLAVI 260
R-PTPc-U-1 cd14632
catalytic domain of receptor-type tyrosine-protein phosphatase U, repeat 1; Receptor-type ...
1189-1395 1.13e-25

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: 106.29  E-value: 1.13e-25
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1925147141 1189 YINASYIMGYHKSREFILTQSPLPSTVSDFWRMVWDHNSQLIISLpdTHTAQREGEESCAYWPSKDQPIscegfivsfsG 1268
Cdd:cd14632      1 YINANYIDGYHRSNHFIATQGPKQEMVYDFWRMVWQEHCSSIVMI--TKLVEVGRVKCSKYWPDDSDTY----------G 68
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1925147141 1269 EDHMCLANEERL---VVHDFLLEATQDNYVLEVRQYMSPCWPNPDSP--VSGTFQLLNIITEDSRQREGTIVVHDRLGGS 1343
Cdd:cd14632     69 DIKITLLKTETLaeySVRTFALERRGYSARHEVKQFHFTSWPEHGVPyhATGLLAFIRRVKASTPPDAGPVVVHCSAGAG 148
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|..
gi 1925147141 1344 VAGLFCALTTLAQQLEHQGSVDVYQVARMTNLMRPGVFNDMEQYQFMYRAVL 1395
Cdd:cd14632    149 RTGCYIVLDVMLDMAECEGVVDIYNCVKTLCSRRINMIQTEEQYIFIHDAIL 200
R-PTPc-T-2 cd14634
PTP domain of receptor-type tyrosine-protein phosphatase T, repeat 2; Receptor-type ...
1189-1395 2.89e-25

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: 105.10  E-value: 2.89e-25
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1925147141 1189 YINASYIMGYHKSREFILTQSPLPSTVSDFWRMVWDHNSQLIISLPDTHTAQRegeeSCAYWPSKDQ----PISCEgFIV 1264
Cdd:cd14634      1 YINAALMDSHKQPAAFIVTQHPLPNTVADFWRLVFDYNCSSVVMLNEMDAAQL----CMQYWPEKTSccygPIQVE-FVS 75
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1925147141 1265 SFSGEDHMC----LANEERlvvhdflleaTQDNYVLeVRQYMSPCWPN-PDSPVSG-----TFQLLNIITEDSRQREGTI 1334
Cdd:cd14634     76 ADIDEDIISrifrICNMAR----------PQDGYRI-VQHLQYIGWPAyRDTPPSKrsilkVVRRLEKWQEQYDGREGRT 144
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1925147141 1335 VVHDRLGGSVAGLFCALTTLAQQLEHQGSVDVYQVARMTNLMRPGVFNDMEQYQFMYRAVL 1395
Cdd:cd14634    145 VVHCLNGGGRSGTFCAICSVCEMIQQQNIIDVFHTVKTLRNNKSNMVETLEQYKFVYEVAL 205
R-PTPc-K-1 cd14631
catalytic domain of receptor-type tyrosine-protein phosphatase K, repeat 1; Receptor-type ...
1175-1395 3.98e-25

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: 105.10  E-value: 3.98e-25
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1925147141 1175 RVCLScPVEGE-SSDYINASYIMGYHKSREFILTQSPLPSTVSDFWRMVWDHNSQLIISLPDTHTAqreGEESC-AYWPS 1252
Cdd:cd14631      1 RVILQ-PVEDDpSSDYINANYIDGYQRPSHYIATQGPVHETVYDFWRMIWQEQSACIVMVTNLVEV---GRVKCyKYWPD 76
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1925147141 1253 KDQPISceGFIVSFSGEDHMClaneeRLVVHDFLLEATQDNYVLEVRQYMSPCWPNPDSP--VSGTFQLLNIITEDSRQR 1330
Cdd:cd14631     77 DTEVYG--DFKVTCVEMEPLA-----EYVVRTFTLERRGYNEIREVKQFHFTGWPDHGVPyhATGLLSFIRRVKLSNPPS 149
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1925147141 1331 EGTIVVHDRLGGSVAGLFCALTTLAQQLEHQGSVDVYQVARMTNLMRPGVFNDMEQYQFMYRAVL 1395
Cdd:cd14631    150 AGPIVVHCSAGAGRTGCYIVIDIMLDMAEREGVVDIYNCVKALRSRRINMVQTEEQYIFIHDAIL 214
R-PTPc-G-1 cd17667
catalytic domain of receptor-type tyrosine-protein phosphatase G, repeat 1; Receptor-type ...
1159-1398 2.25e-24

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: 104.73  E-value: 2.25e-24
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1925147141 1159 NDDKNRTSSLMPVERSRVCLScPVEGESS---DYINASYIMGYHKSREFILTQSPLPSTVSDFWRMVWDHNSQLIISLpd 1235
Cdd:cd17667     27 NKHKNRYINILAYDHSRVKLR-PLPGKDSkhsDYINANYVDGYNKAKAYIATQGPLKSTFEDFWRMIWEQNTGIIVMI-- 103
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1925147141 1236 THTAQReGEESC-AYWPSKDQPISCEGFIVSFSGEDHMClaneerLVVHDFLLEATQDNYVLE-----------VRQYMS 1303
Cdd:cd17667    104 TNLVEK-GRRKCdQYWPTENSEEYGNIIVTLKSTKIHAC------YTVRRFSIRNTKVKKGQKgnpkgrqnertVIQYHY 176
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1925147141 1304 PCWPNPDSPvSGTFQLLNIITEDSRQRE---GTIVVHDRLGGSVAGLFCALTTLAQQLEHQGSVDVYQVARMTNLMRPGV 1380
Cdd:cd17667    177 TQWPDMGVP-EYALPVLTFVRRSSAARTpemGPVLVHCSAGVGRTGTYIVIDSMLQQIKDKSTVNVLGFLKHIRTQRNYL 255
                          250
                   ....*....|....*...
gi 1925147141 1381 FNDMEQYQFMYRAVLSLV 1398
Cdd:cd17667    256 VQTEEQYIFIHDALLEAI 273
PHA02746 PHA02746
protein tyrosine phosphatase; Provisional
1155-1394 2.64e-24

protein tyrosine phosphatase; Provisional


Pssm-ID: 165113 [Multi-domain]  Cd Length: 323  Bit Score: 105.50  E-value: 2.64e-24
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1925147141 1155 LREGNDDKNRTSSLMPVERSRVCLSC-------------------PVEGESSDYINASYIMGYHKSREFILTQSPLPSTV 1215
Cdd:PHA02746    47 LKKENLKKNRFHDIPCWDHSRVVINAheslkmfdvgdsdgkkievTSEDNAENYIHANFVDGFKEANKFICAQGPKEDTS 126
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1925147141 1216 SDFWRMVWDHNSQLIISLPDThtaQREGEESCAYWPS-KDQPISCEGFIVSFSGEDHMCLANEERLVVHDFLLEATQdny 1294
Cdd:PHA02746   127 EDFFKLISEHESQVIVSLTDI---DDDDEKCFELWTKeEDSELAFGRFVAKILDIIEELSFTKTRLMITDKISDTSR--- 200
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1925147141 1295 vlEVRQYMSPCWPNPDSPvSGTFQLLNIIT-------------EDSRQREGTIVVHDRLGGSVAGLFCALTTLAQQLEHQ 1361
Cdd:PHA02746   201 --EIHHFWFPDWPDNGIP-TGMAEFLELINkvneeqaelikqaDNDPQTLGPIVVHCSAGIGRAGTFCAIDNALEQLEKE 277
                          250       260       270
                   ....*....|....*....|....*....|...
gi 1925147141 1362 GSVDVYQVARMTNLMRPGVFNDMEQYQFMYRAV 1394
Cdd:PHA02746   278 KEVCLGEIVLKIRKQRHSSVFLPEQYAFCYKAL 310
PTPc-N11 cd14605
catalytic domain of tyrosine-protein phosphatase non-receptor type 11; Tyrosine-protein ...
1159-1400 2.97e-24

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: 103.56  E-value: 2.97e-24
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1925147141 1159 NDDKNRTSSLMPVERSRVCLS-CPVEGESSDYINASYIMGYHKS--------REFILTQSPLPSTVSDFWRMVWDHNSQL 1229
Cdd:cd14605      2 NKNKNRYKNILPFDHTRVVLHdGDPNEPVSDYINANIIMPEFETkcnnskpkKSYIATQGCLQNTVNDFWRMVFQENSRV 81
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1925147141 1230 IISlpDTHTAQREGEESCAYWPSKdqpiscegfiVSFSGEDHMCLANEERLVVHDFLL------EATQDNYVLEVRQYMS 1303
Cdd:cd14605     82 IVM--TTKEVERGKSKCVKYWPDE----------YALKEYGVMRVRNVKESAAHDYILrelklsKVGQGNTERTVWQYHF 149
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1925147141 1304 PCWPN---PDSPvSGTFQLLNII--TEDSRQREGTIVVHDRLGGSVAGLFCALTTLAQQLEHQG---SVDVYQVARMTNL 1375
Cdd:cd14605    150 RTWPDhgvPSDP-GGVLDFLEEVhhKQESIMDAGPVVVHCSAGIGRTGTFIVIDILIDIIREKGvdcDIDVPKTIQMVRS 228
                          250       260
                   ....*....|....*....|....*
gi 1925147141 1376 MRPGVFNDMEQYQFMYRAVLSLVDS 1400
Cdd:cd14605    229 QRSGMVQTEAQYRFIYMAVQHYIET 253
PTPc-N22_18_12 cd14542
catalytic domain of tyrosine-protein phosphatase non-receptor type 22, type 18 and type 12; ...
1189-1392 3.43e-24

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: 101.73  E-value: 3.43e-24
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1925147141 1189 YINASYIMGYHKSREFILTQSPLPSTVSDFWRMVWDHNSQLIIslpdthTAQRE---GEESCA-YWP-SKDQPISCEGFI 1263
Cdd:cd14542      1 YINANFIKGVSGSKAYIATQGPLPNTVLDFWRMIWEYNVQVIV------MACREfemGKKKCErYWPeEGEEQLQFGPFK 74
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1925147141 1264 VSFSGEDHMClaneERLVVHDFLLEATQDNYVLEVRQYMSpcWPNPDSPVSGTfQLLNIItEDSRQREGT----IVVHDR 1339
Cdd:cd14542     75 ISLEKEKRVG----PDFLIRTLKVTFQKESRTVYQFHYTA--WPDHGVPSSVD-PILDLV-RLVRDYQGSedvpICVHCS 146
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 1925147141 1340 LGGSVAGLFCALTTLAQQLEHQG---SVDVYQVARMTNLMRPGVFNDMEQYQFMYR 1392
Cdd:cd14542    147 AGCGRTGTICAIDYVWNLLKTGKipeEFSLFDLVREMRKQRPAMVQTKEQYELVYR 202
R-PTP-N cd14609
PTP-like domain of receptor-type tyrosine-protein phosphatase N; Receptor-type ...
1115-1400 4.84e-24

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: 103.58  E-value: 4.84e-24
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1925147141 1115 LVHSYVSDLLTTgpsgRTRMERQFKLVSQRRARQADYAAALREGNDDKNRTSSLMPVERSRVCLSCPVEGESSDYINASY 1194
Cdd:cd14609      2 MILAYMEDHLRN----RDRLAKEWQALCAYQAEPNTCSTAQGEANVKKNRNPDFVPYDHARIKLKAESNPSRSDYINASP 77
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1925147141 1195 IMGyHKSR--EFILTQSPLPSTVSDFWRMVWDHNSQLIISLPdthTAQREGEESC-AYWPSKDQPIScEGFIVSFSGEDH 1271
Cdd:cd14609     78 IIE-HDPRmpAYIATQGPLSHTIADFWQMVWENGCTVIVMLT---PLVEDGVKQCdRYWPDEGSSLY-HIYEVNLVSEHI 152
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1925147141 1272 MClaneERLVVHDFLLEATQDNYVLEVRQYMSPCWPNPDSPVSgTFQLLNI---ITEDSRQREGTIVVHDRLGGSVAGLF 1348
Cdd:cd14609    153 WC----EDFLVRSFYLKNVQTQETRTLTQFHFLSWPAEGIPSS-TRPLLDFrrkVNKCYRGRSCPIIVHCSDGAGRTGTY 227
                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|...
gi 1925147141 1349 CAL-TTLAQQLEHQGSVDVYQVARMTNLMRPGVFNDMEQYQFMYRAVLSLVDS 1400
Cdd:cd14609    228 ILIdMVLNRMAKGVKEIDIAATLEHVRDQRPGMVRTKDQFEFALTAVAEEVNA 280
R-PTPc-M-2 cd14635
PTP domain of receptor-type tyrosine-protein phosphatase M, repeat 2; Receptor-type ...
1189-1395 5.54e-24

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: 101.30  E-value: 5.54e-24
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1925147141 1189 YINASYIMGYHKSREFILTQSPLPSTVSDFWRMVWDHNSQLIISLPDTHTAQREGEescaYWPS----KDQPISCEgfiv 1264
Cdd:cd14635      1 YINAALMDSYKQPSAFIVTQHPLPNTVKDFWRLVLDYHCTSIVMLNDVDPAQLCPQ----YWPEngvhRHGPIQVE---- 72
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1925147141 1265 sFSGEDHmclanEERLVVHDFLL---EATQDNYVLeVRQYMSPCWP-NPDSPVSGTFQLLNIITEDSRQR-----EGTIV 1335
Cdd:cd14635     73 -FVSADL-----EEDIISRIFRIynaARPQDGYRM-VQQFQFLGWPmYRDTPVSKRSFLKLIRQVDKWQEeynggEGRTV 145
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1925147141 1336 VHDRLGGSVAGLFCALTTLAQQLEHQGSVDVYQVARMTNLMRPGVFNDMEQYQFMYRAVL 1395
Cdd:cd14635    146 VHCLNGGGRSGTFCAISIVCEMLRHQRAVDVFHAVKTLRNNKPNMVDLLDQYKFCYEVAL 205
R-PTPc-T-2 cd14634
PTP domain of receptor-type tyrosine-protein phosphatase T, repeat 2; Receptor-type ...
894-1102 8.19e-24

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: 100.87  E-value: 8.19e-24
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1925147141  894 YINANFVDGFERTRAYIAAQGPLKSGTEDFWRMVWQENVGVIVMITNLleKGRRKCDQYWPMENQEEYGHFLVTLKDTKT 973
Cdd:cd14634      1 YINAALMDSHKQPAAFIVTQHPLPNTVADFWRLVFDYNCSSVVMLNEM--DAAQLCMQYWPEKTSCCYGPIQVEFVSADI 78
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1925147141  974 LAYYTLRTFTLRDTSqkasqRGRCAERTVVQYHYTQWPDM-GVPEYTLPVLSFVRASTQARTQ---DMGPVLVHCSAGVG 1049
Cdd:cd14634     79 DEDIISRIFRICNMA-----RPQDGYRIVQHLQYIGWPAYrDTPPSKRSILKVVRRLEKWQEQydgREGRTVVHCLNGGG 153
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|...
gi 1925147141 1050 RTGTYIVLDSMLQQIQDQGTVNILGFLKHVRTQRNYLVQTEEQYVFIHDALVE 1102
Cdd:cd14634    154 RSGTFCAICSVCEMIQQQNIIDVFHTVKTLRNNKSNMVETLEQYKFVYEVALE 206
PTP_fungal cd18533
fungal protein tyrosine phosphatases; This subfamily contains Saccharomyces cerevisiae ...
1189-1391 1.44e-23

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: 100.40  E-value: 1.44e-23
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1925147141 1189 YINASYI-MGYHKSREFILTQSPLPSTVSDFWRMVWDHNSQLIISLpdthTAQRE-GEESCA-YWPSKDQPISCEGFIVS 1265
Cdd:cd18533      1 YINASYItLPGTSSKRYIATQGPLPATIGDFWKMIWQNNVGVIVML----TPLVEnGREKCDqYWPSGEYEGEYGDLTVE 76
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1925147141 1266 FSGEDHMclaNEERLVVHDFLLeATQDNYVLEVRQYMSPCWPN---PDSPVSgTFQLLNIITE--DSRQREGTIVVHDRL 1340
Cdd:cd18533     77 LVSEEEN---DDGGFIVREFEL-SKEDGKVKKVYHIQYKSWPDfgvPDSPED-LLTLIKLKRElnDSASLDPPIIVHCSA 151
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1925147141 1341 GGSVAGLFCALTTLAQQLEHQGSVD---------VYQ-VARMTNLmRPGVFNDMEQYQFMY 1391
Cdd:cd18533    152 GVGRTGTFIALDSLLDELKRGLSDSqdledsedpVYEiVNQLRKQ-RMSMVQTLRQYIFLY 211
PTPc-N1_2 cd14545
catalytic domain of tyrosine-protein phosphatase non-receptor type 1 and type 2; ...
1161-1391 5.08e-23

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: 99.39  E-value: 5.08e-23
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1925147141 1161 DKNRTSSLMPVERSRVCLscpvEGESSDYINASYIMGYHKSREFILTQSPLPSTVSDFWRMVWDHNSQLIISLpdtHTAQ 1240
Cdd:cd14545      2 NRYRDRDPYDHDRSRVKL----KQGDNDYINASLVEVEEAKRSYILTQGPLPNTSGHFWQMVWEQNSKAVIML---NKLM 74
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1925147141 1241 REGEESCA-YWPSKDQPISCEGFiVSFSGEdhmcLANEER---LVVHDFLLEATQDNYVLEVRQYMSPCWPN---PDSPv 1313
Cdd:cd14545     75 EKGQIKCAqYWPQGEGNAMIFED-TGLKVT----LLSEEDksyYTVRTLELENLKTQETREVLHFHYTTWPDfgvPESP- 148
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1925147141 1314 sGTFqlLNIITEdsrQRE--------GTIVVHDRLGGSVAGLFCALTTLAQQLEHQG--SVDVYQVARMTNLMRPGVFND 1383
Cdd:cd14545    149 -AAF--LNFLQK---VREsgslssdvGPPVVHCSAGIGRSGTFCLVDTCLVLIEKGNpsSVDVKKVLLEMRKYRMGLIQT 222

                   ....*...
gi 1925147141 1384 MEQYQFMY 1391
Cdd:cd14545    223 PDQLRFSY 230
PHA02740 PHA02740
protein tyrosine phosphatase; Provisional
860-1106 4.26e-22

protein tyrosine phosphatase; Provisional


Pssm-ID: 165107 [Multi-domain]  Cd Length: 298  Bit Score: 98.50  E-value: 4.26e-22
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1925147141  860 SSNHPDNKNK--NRYINIMAYDHSRVKLLEEGKggdYINANFVDGFERTRAYIAAQGPLKSGTEDFWRMVWQENVGVIVM 937
Cdd:PHA02740    45 ACAQAENKAKdeNLALHITRLLHRRIKLFNDEK---VLDARFVDGYDFEQKFICIINLCEDACDKFLQALSDNKVQIIVL 121
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1925147141  938 ITNLLEKgrrKC-DQYWPMENQ--EEYGHFLVTLKDTKTLAYYTLRTFTLRDtsqkasQRGRcaERTVVQYHYTQWPDMG 1014
Cdd:PHA02740   122 ISRHADK---KCfNQFWSLKEGcvITSDKFQIETLEIIIKPHFNLTLLSLTD------KFGQ--AQKISHFQYTAWPADG 190
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1925147141 1015 VPEYTLPVLSF--------VRASTQARTQDMGPVLVHCSAGVGRTGTYIVLDSMLQQIQDQGTVNILGFLKHVRTQRNYL 1086
Cdd:PHA02740   191 FSHDPDAFIDFfcniddlcADLEKHKADGKIAPIIIDCIDGISSSAVFCVFDICATEFDKTGMLSIANALKKVRQKKYGC 270
                          250       260
                   ....*....|....*....|
gi 1925147141 1087 VQTEEQYVFIHDaLVEAIVS 1106
Cdd:PHA02740   271 MNCLDDYVFCYH-LIAAYLK 289
R-PTPc-A-E-1 cd14551
catalytic domain of receptor-type tyrosine-protein phosphatase A and E, repeat 1; ...
1189-1392 5.51e-22

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: 95.36  E-value: 5.51e-22
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1925147141 1189 YINASYIMGYHKSREFILTQSPLPSTVSDFWRMVWDHNSQLIISLpdTHTAQReGEESCA-YWPskDQPISCEGFIVsFS 1267
Cdd:cd14551      1 YINASYIDGYQEKNKFIAAQGPKDETVNDFWRMIWEQGSATIVMV--TNLKER-KEKKCSqYWP--DQGCWTYGNLR-VR 74
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1925147141 1268 GEDHMCLANEerlVVHDFLLEATQDNY----VLEVRQYMSPCWPN---PDSPVsGTFQLLNIITEDSRQREGTIVVHDRL 1340
Cdd:cd14551     75 VEDTVVLVDY---TTRKFCIQKVNRGIgekrVRLVTQFHFTSWPDfgvPFTPI-GMLKFLKKVKSANPPRAGPIVVHCSA 150
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|...
gi 1925147141 1341 GGSVAGLFCALTTLAQQLEHQGSVDVYQ-VARMTNLMRPGVFNDMeQYQFMYR 1392
Cdd:cd14551    151 GVGRTGTFIVIDAMLDMMHAEGKVDVFGfVSRIRQQRSQMVQTDM-QYVFIYQ 202
R-PTP-G-2 cd17670
PTP-like domain of receptor-type tyrosine-protein phosphatase G, repeat 2; Receptor-type ...
894-1101 6.18e-22

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


Pssm-ID: 350508 [Multi-domain]  Cd Length: 205  Bit Score: 95.52  E-value: 6.18e-22
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1925147141  894 YINANFVDGFERTRAYIAAQGPLKSGTEDFWRMVWQENVGVIVMITNLLEKGRRKCdQYWPmeNQEEYGH---FLVTLKD 970
Cdd:cd17670      1 YINASYIMGYYRSNEFIITQHPLPHTTKDFWRMIWDHNAQIIVMLPDNQGLAEDEF-VYWP--SREESMNceaFTVTLIS 77
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1925147141  971 TKTLAYYTLRTFTLRDTSQKASQRGRCAErtVVQYHYTQWPDMGVP-EYTLPVLSFVRasTQARTQDmGPVLVHCSAGVG 1049
Cdd:cd17670     78 KDRLCLSNEEQIIIHDFILEATQDDYVLE--VRHFQCPKWPNPDAPiSSTFELINVIK--EEALTRD-GPTIVHDEFGAV 152
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|..
gi 1925147141 1050 RTGTYIVLDSMLQQIQDQGTVNILGFLKHVRTQRNYLVQTEEQYVFIHDALV 1101
Cdd:cd17670    153 SAGTLCALTTLSQQLENENAVDVYQVAKMINLMRPGVFTDIEQYQFLYKAML 204
PHA02747 PHA02747
protein tyrosine phosphatase; Provisional
1151-1390 1.18e-21

protein tyrosine phosphatase; Provisional


Pssm-ID: 165114 [Multi-domain]  Cd Length: 312  Bit Score: 97.38  E-value: 1.18e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1925147141 1151 YAAALREGNDDKNRTSSLMPVERSRVCLSCPvEGESSDYINASYIMGYHKSREFILTQSPLPSTVSDFWRMVWDHNSQLI 1230
Cdd:PHA02747    43 IANFEKPENQPKNRYWDIPCWDHNRVILDSG-GGSTSDYIHANWIDGFEDDKKFIATQGPFAETCADFWKAVWQEHCSII 121
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1925147141 1231 ISLpdTHTAQREGEESC-AYW-PSKDQPISCEGFIVSfsgedhmCLANEERLVVHDFLLEATQD--NYVLEVRQYMSPCW 1306
Cdd:PHA02747   122 VML--TPTKGTNGEEKCyQYWcLNEDGNIDMEDFRIE-------TLKTSVRAKYILTLIEITDKilKDSRKISHFQCSEW 192
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1925147141 1307 PNPDSPVSGT--FQLLNIItEDSRQREGT-----------IVVHDRLGGSVAGLFCALTTLAQQLEHQGSVDVYQVARMT 1373
Cdd:PHA02747   193 FEDETPSDHPdfIKFIKII-DINRKKSGKlfnpkdallcpIVVHCSDGVGKTGIFCAVDICLNQLVKRKAICLAKTAEKI 271
                          250
                   ....*....|....*..
gi 1925147141 1374 NLMRPGVFNDMEQYQFM 1390
Cdd:PHA02747   272 REQRHAGIMNFDDYLFI 288
PTPc-N13 cd14597
catalytic domain of tyrosine-protein phosphatase non-receptor type 13; Tyrosine-protein ...
1159-1395 1.69e-21

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: 94.90  E-value: 1.69e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1925147141 1159 NDDKNRTSSLMPVERSRVCLscpveGESSDYINASYIMGYHKSREF--ILTQSPLPSTVSDFWRMVWDHNSQLIISLpdt 1236
Cdd:cd14597      3 NRKKNRYKNILPYDTTRVPL-----GDEGGYINASFIKMPVGDEEFvyIACQGPLPTTVADFWQMVWEQKSTVIAMM--- 74
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1925147141 1237 hTAQREGEE-SCA-YWP---SKDQPIScEGFIVSFSGEDHMclaneERLVVHDFLLEATQDNYVLEVRQYMSPCWPNPDS 1311
Cdd:cd14597     75 -TQEVEGGKiKCQrYWPeilGKTTMVD-NRLQLTLVRMQQL-----KNFVIRVLELEDIQTREVRHITHLNFTAWPDHDT 147
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1925147141 1312 PvSGTFQLLNIITEDSR-QREGTIVVHDRLG-GSVAGLFC---ALTTLAQQLEhqgsVDVYQVARMTNLMRPGVFNDMEQ 1386
Cdd:cd14597    148 P-SQPEQLLTFISYMRHiHKSGPIITHCSAGiGRSGTLICidvVLGLISKDLD----FDISDIVRTMRLQRHGMVQTEDQ 222

                   ....*....
gi 1925147141 1387 YQFMYRAVL 1395
Cdd:cd14597    223 YIFCYQVIL 231
R-PTP-Z-2 cd17669
catalytic domain of receptor-type tyrosine-protein phosphatase Z, repeat 2; Receptor-type ...
894-1101 1.80e-21

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: 93.91  E-value: 1.80e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1925147141  894 YINANFVDGFERTRAYIAAQGPLKSGTEDFWRMVWQENVGVIVMITNLLEKGRRKCdQYWPmeNQEE---YGHFLVTLKD 970
Cdd:cd17669      1 YINASYIMGYYQSNEFIITQHPLLHTIKDFWRMIWDHNAQLIVMLPDGQNMAEDEF-VYWP--NKDEpinCETFKVTLIA 77
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1925147141  971 TKTLAYYTLRTFTLRDTSQKASQRGRCAErtVVQYHYTQWPDMGVP-EYTLPVLSFVRasTQARTQDmGPVLVHCSAGVG 1049
Cdd:cd17669     78 EEHKCLSNEEKLIIQDFILEATQDDYVLE--VRHFQCPKWPNPDSPiSKTFELISIIK--EEAANRD-GPMIVHDEHGGV 152
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|..
gi 1925147141 1050 RTGTYIVLDSMLQQIQDQGTVNILGFLKHVRTQRNYLVQTEEQYVFIHDALV 1101
Cdd:cd17669    153 TAGTFCALTTLMHQLEKENSVDVYQVAKMINLMRPGVFTDIEQYQFLYKAIL 204
R-PTPc-Z-1 cd17668
catalytic domain of receptor-type tyrosine-protein phosphatase Z, repeat 1; Receptor-type ...
1189-1395 2.88e-21

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: 93.50  E-value: 2.88e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1925147141 1189 YINASYIMGYHKSREFILTQSPLPSTVSDFWRMVWDHNSQLIISLpdTHTAQReGEESC-AYWPSKDQPiSCEGFIVSFS 1267
Cdd:cd17668      1 YINANYVDGYNKPKAYIAAQGPLKSTAEDFWRMIWEHNVEVIVMI--TNLVEK-GRRKCdQYWPADGSE-EYGNFLVTQK 76
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1925147141 1268 GEDHMCLANEERLVVHDFLL-EATQDNYVLE--VRQYMSPCWPNPDSPvSGTFQLLNIITEDSRQRE---GTIVVHDRLG 1341
Cdd:cd17668     77 SVQVLAYYTVRNFTLRNTKIkKGSQKGRPSGrvVTQYHYTQWPDMGVP-EYTLPVLTFVRKASYAKRhavGPVVVHCSAG 155
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....
gi 1925147141 1342 GSVAGLFCALTTLAQQLEHQGSVDVYQVARMTNLMRPGVFNDMEQYQFMYRAVL 1395
Cdd:cd17668    156 VGRTGTYIVLDSMLQQIQHEGTVNIFGFLKHIRSQRNYLVQTEEQYVFIHDALV 209
PHA02738 PHA02738
hypothetical protein; Provisional
1159-1400 9.55e-21

hypothetical protein; Provisional


Pssm-ID: 222923 [Multi-domain]  Cd Length: 320  Bit Score: 94.99  E-value: 9.55e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1925147141 1159 NDDKNRTSSLMPVERSRVCLscPVEGESSDYINASYIMGYHKSREFILTQSPLPSTVSDFWRMVWDHNSQLIISLpdthT 1238
Cdd:PHA02738    49 NRKLNRYLDAVCFDHSRVIL--PAERNRGDYINANYVDGFEYKKKFICGQAPTRQTCYDFYRMLWMEHVQIIVML----C 122
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1925147141 1239 AQRE-GEESC-AYWPSKDQ-PISCEGF-IVSFSGEDHMCLAnEERLVVHDFlLEATQdnyvlEVRQYMSPCWPNPDSPvS 1314
Cdd:PHA02738   123 KKKEnGREKCfPYWSDVEQgSIRFGKFkITTTQVETHPHYV-KSTLLLTDG-TSATQ-----TVTHFNFTAWPDHDVP-K 194
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1925147141 1315 GTFQLLNIITE----------------DSRQREGTIVVHDRLGGSVAGLFCALTTLAQQLEHQGSVDVYQVARMTNLMRP 1378
Cdd:PHA02738   195 NTSEFLNFVLEvrqcqkelaqeslqigHNRLQPPPIVVHCNAGLGRTPCYCVVDISISRFDACATVSIPSIVSSIRNQRY 274
                          250       260
                   ....*....|....*....|..
gi 1925147141 1379 GVFNDMEQYQFMYRAVLSLVDS 1400
Cdd:PHA02738   275 YSLFIPFQYFFCYRAVKRYVNL 296
PTPc-N2 cd14607
catalytic domain of tyrosine-protein phosphatase non-receptor type 2; Tyrosine-protein ...
1159-1394 1.30e-20

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: 93.11  E-value: 1.30e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1925147141 1159 NDDKNRTSSLMPVERSRVCLscpvEGESSDYINASYIMGYHKSREFILTQSPLPSTVSDFWRMVWDHNSQLIISLpdTHT 1238
Cdd:cd14607     24 NRNRNRYRDVSPYDHSRVKL----QNTENDYINASLVVIEEAQRSYILTQGPLPNTCCHFWLMVWQQKTKAVVML--NRI 97
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1925147141 1239 AQREGEESCAYWPSKDQPI---SCEGFIVSFSGEDhmclaNEERLVVHDFLLEATQDNYVLEVRQYMSPCWPN---PDSP 1312
Cdd:cd14607     98 VEKDSVKCAQYWPTDEEEVlsfKETGFSVKLLSED-----VKSYYTVHLLQLENINSGETRTISHFHYTTWPDfgvPESP 172
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1925147141 1313 VSGTFQLLNIITEDSRQRE-GTIVVHDRLGGSVAGLFCALTTLAQQLEHQG--SVDVYQVARMTNLMRPGVFNDMEQYQF 1389
Cdd:cd14607    173 ASFLNFLFKVRESGSLSPEhGPAVVHCSAGIGRSGTFSLVDTCLVLMEKKDpdSVDIKQVLLDMRKYRMGLIQTPDQLRF 252

                   ....*
gi 1925147141 1390 MYRAV 1394
Cdd:cd14607    253 SYMAV 257
R-PTPc-K-2 cd14636
PTP domain of receptor-type tyrosine-protein phosphatase K, repeat 2; Receptor-type ...
1189-1395 1.51e-20

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


Pssm-ID: 350484 [Multi-domain]  Cd Length: 206  Bit Score: 91.63  E-value: 1.51e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1925147141 1189 YINASYIMGYHKSREFILTQSPLPSTVSDFWRMVWDHNSQLIISLPDTHTAQregeeSC-AYWPSKDQ----PISCEGFI 1263
Cdd:cd14636      1 YINAALMDSYRQPAAFIVTQHPLPNTVKDFWRLVYDYGCTSIVMLNEVDLAQ-----GCpQYWPEEGMlrygPIQVECMS 75
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1925147141 1264 VSFsgeDHMCLANEERLVVhdflLEATQDNYVLeVRQYMSPCWPNPDSPVSGTFQLLNII------TEDSRQREGTIVVH 1337
Cdd:cd14636     76 CSM---DCDVISRIFRICN----LTRPQEGYLM-VQQFQYLGWASHREVPGSKRSFLKLIlqvekwQEECDEGEGRTIIH 147
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 1925147141 1338 DRLGGSVAGLFCALTTLAQQLEHQGSVDVYQVARMTNLMRPGVFNDMEQYQFMYRAVL 1395
Cdd:cd14636    148 CLNGGGRSGMFCAISIVCEMIKRQNVVDVFHAVKTLRNSKPNMVETPEQYRFCYDVAL 205
R-PTPc-U-2 cd14637
PTP domain of receptor-type tyrosine-protein phosphatase U, repeat 2; Receptor-type ...
894-1102 2.46e-20

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: 90.74  E-value: 2.46e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1925147141  894 YINANFVDGFERTRAYIAAQGPLKSGTEDFWRMVWQENVGVIVMITNLLEKGRR-KCDQYWPMENQEEYGHFLVTLKDTK 972
Cdd:cd14637      1 YINAALTDSYTRSAAFIVTLHPLQNTTTDFWRLVYDYGCTSVVMLNQLNQSNSAwPCLQYWPEPGLQQYGPMEVEFVSGS 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1925147141  973 TLAYYTLRTFTLRDTSqkasqRGRCAERTVVQYHYTQW-PDMGVPEYT---LPVLSFVRaSTQARTQDmGPVLVHCSAGV 1048
Cdd:cd14637     81 ADEDIVTRLFRVQNIT-----RLQEGHLMVRHFQFLRWsAYRDTPDSKkafLHLLASVE-KWQRESGE-GRTVVHCLNGG 153
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....
gi 1925147141 1049 GRTGTYIVLDSMLQQIQDQGTVNILGFLKHVRTQRNYLVQTEEQYVFIHDALVE 1102
Cdd:cd14637    154 GRSGTYCASAMILEMIRCHNIVDVFYAVKTLRNYKPNMVETLEQYRFCYEIALE 207
PTPc-N20_13 cd14538
catalytic domain of tyrosine-protein phosphatase non-receptor type 20 and type 13; ...
1189-1395 2.82e-20

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: 90.51  E-value: 2.82e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1925147141 1189 YINASYIMGYHKSREF--ILTQSPLPSTVSDFWRMVWDHNSQLIISLpdthTAQREGEE-SC-AYWP-SKDQPISCEGFI 1263
Cdd:cd14538      1 YINASHIRIPVGGDTYhyIACQGPLPNTTGDFWQMVWEQKSEVIAMV----TQDVEGGKvKChRYWPdSLNKPLICGGRL 76
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1925147141 1264 vSFSGEDHMCLANeerLVVHDFLLEATQDNYVLEVRQYMSPCWPNPDSPVSGTFQLLNIITEDSRQREGTIVVHDRLGGS 1343
Cdd:cd14538     77 -EVSLEKYQSLQD---FVIRRISLRDKETGEVHHITHLNFTTWPDHGTPQSADPLLRFIRYMRRIHNSGPIVVHCSAGIG 152
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|..
gi 1925147141 1344 VAGLFCALTTLAQQLEHQGSVDVYQVARMTNLMRPGVFNDMEQYQFMYRAVL 1395
Cdd:cd14538    153 RTGVLITIDVALGLIERDLPFDIQDIVKDLREQRQGMIQTKDQYIFCYKACL 204
R-PTPc-U-2 cd14637
PTP domain of receptor-type tyrosine-protein phosphatase U, repeat 2; Receptor-type ...
1189-1395 4.63e-20

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: 89.97  E-value: 4.63e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1925147141 1189 YINASYIMGYHKSREFILTQSPLPSTVSDFWRMVWDHNSQLIISLpdTHTAQREGEESC-AYWPskDQPISCEGFI-VSF 1266
Cdd:cd14637      1 YINAALTDSYTRSAAFIVTLHPLQNTTTDFWRLVYDYGCTSVVML--NQLNQSNSAWPClQYWP--EPGLQQYGPMeVEF 76
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1925147141 1267 sgedhMCLANEERLVVHDFLLE---ATQDNYVLeVRQYM----SPCWPNPDSPVSgTFQLLNIITEDSRQ-REGTIVVHD 1338
Cdd:cd14637     77 -----VSGSADEDIVTRLFRVQnitRLQEGHLM-VRHFQflrwSAYRDTPDSKKA-FLHLLASVEKWQREsGEGRTVVHC 149
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 1925147141 1339 RLGGSVAGLFCALTTLAQQLEHQGSVDVYQVARMTNLMRPGVFNDMEQYQFMYRAVL 1395
Cdd:cd14637    150 LNGGGRSGTYCASAMILEMIRCHNIVDVFYAVKTLRNYKPNMVETLEQYRFCYEIAL 206
R-PTPc-K-2 cd14636
PTP domain of receptor-type tyrosine-protein phosphatase K, repeat 2; Receptor-type ...
894-1102 1.04e-19

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: 88.93  E-value: 1.04e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1925147141  894 YINANFVDGFERTRAYIAAQGPLKSGTEDFWRMVWQENVGVIVMITNL-LEKGrrkCDQYWPMENQEEYGHFLVTLKDTK 972
Cdd:cd14636      1 YINAALMDSYRQPAAFIVTQHPLPNTVKDFWRLVYDYGCTSIVMLNEVdLAQG---CPQYWPEEGMLRYGPIQVECMSCS 77
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1925147141  973 TLAYYTLRTFTLRDTSQkaSQRGRCaerTVVQYHYTQWPdmGVPEYTLPVLSFVRASTQART------QDMGPVLVHCSA 1046
Cdd:cd14636     78 MDCDVISRIFRICNLTR--PQEGYL---MVQQFQYLGWA--SHREVPGSKRSFLKLILQVEKwqeecdEGEGRTIIHCLN 150
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 1925147141 1047 GVGRTGTYIVLDSMLQQIQDQGTVNILGFLKHVRTQRNYLVQTEEQYVFIHDALVE 1102
Cdd:cd14636    151 GGGRSGMFCAISIVCEMIKRQNVVDVFHAVKTLRNSKPNMVETPEQYRFCYDVALE 206
PTPc-N20 cd14596
catalytic domain of tyrosine-protein phosphatase non-receptor type 20; Tyrosine-protein ...
1189-1395 1.39e-19

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: 88.65  E-value: 1.39e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1925147141 1189 YINASYIMGYHKSRE--FILTQSPLPSTVSDFWRMVWDHNSQLIISLpdthTAQRE-GEESC-AYWPSK-DQPISCEGFi 1263
Cdd:cd14596      1 YINASYITMPVGEEElfYIATQGPLPSTIDDFWQMVWENRSDVIAMM----TREVErGKVKChRYWPETlQEPMELENY- 75
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1925147141 1264 vsfsgedHMCLANEErlVVHDFLL-------EATQDNYVLEVRQYMSpcWPNPDSPVSGTfQLLNIITEDSR-QREGTIV 1335
Cdd:cd14596     76 -------QLRLENYQ--ALQYFIIriiklveKETGENRLIKHLQFTT--WPDHGTPQSSD-QLVKFICYMRKvHNTGPIV 143
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1925147141 1336 VHDRLGGSVAGLFCALTTLAQQLEHQGSVDVYQVARMTNLMRPGVFNDMEQYQFMYRAVL 1395
Cdd:cd14596    144 VHCSAGIGRAGVLICVDVLLSLIEKDLSFNIKDIVREMRQQRYGMIQTKDQYLFCYKVVL 203
PTPc-N6 cd14606
catalytic domain of tyrosine-protein phosphatase non-receptor type 6; Tyrosine-protein ...
1156-1400 4.62e-19

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: 88.78  E-value: 4.62e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1925147141 1156 REGNDDKNRTSSLMPVERSRVCLSCP---VEGesSDYINASYIMGY-----HKSREFILTQSPLPSTVSDFWRMVWDHNS 1227
Cdd:cd14606     15 RPENKSKNRYKNILPFDHSRVILQGRdsnIPG--SDYINANYVKNQllgpdENAKTYIASQGCLEATVNDFWQMAWQENS 92
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1925147141 1228 QLIISlpdTHTAQREGEESCA-YWPSKDQPISCEGFIVSFSGEDHmclANEERLVVhdFLLEATQDN-YVLEVRQYMSPC 1305
Cdd:cd14606     93 RVIVM---TTREVEKGRNKCVpYWPEVGMQRAYGPYSVTNCGEHD---TTEYKLRT--LQVSPLDNGeLIREIWHYQYLS 164
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1925147141 1306 WPN---PDSPvSGTFQLLNIIT--EDSRQREGTIVVHDRLGGSVAGLFCALTTLAQQLEHQG---SVDVYQVARMTNLMR 1377
Cdd:cd14606    165 WPDhgvPSEP-GGVLSFLDQINqrQESLPHAGPIIVHCSAGIGRTGTIIVIDMLMENISTKGldcDIDIQKTIQMVRAQR 243
                          250       260
                   ....*....|....*....|...
gi 1925147141 1378 PGVFNDMEQYQFMYRAVLSLVDS 1400
Cdd:cd14606    244 SGMVQTEAQYKFIYVAIAQFIET 266
R-PTPc-C-1 cd14557
catalytic domain of receptor-type tyrosine-protein phosphatase C, repeat 1; Receptor-type ...
1189-1367 1.44e-18

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: 85.65  E-value: 1.44e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1925147141 1189 YINASYIMGYHKSREFILTQSPLPSTVSDFWRMVWDHNSQLIISLpdthTAQREGEES-CA-YWPSKDQPISCEGFIVSF 1266
Cdd:cd14557      1 YINASYIDGFKEPRKYIAAQGPKDETVDDFWRMIWEQKSTVIVMV----TRCEEGNRNkCAqYWPSMEEGSRAFGDVVVK 76
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1925147141 1267 SGEDHMCLANEERLVVHDFLLEATQDNYVLEVrQYMSpcWPN---PDSPvSGTFQLLNIITEDSRQREGTIVVHDRLGGS 1343
Cdd:cd14557     77 INEEKICPDYIIRKLNINNKKEKGSGREVTHI-QFTS--WPDhgvPEDP-HLLLKLRRRVNAFNNFFSGPIVVHCSAGVG 152
                          170       180
                   ....*....|....*....|....
gi 1925147141 1344 VAGLFCALTTLAQQLEHQGSVDVY 1367
Cdd:cd14557    153 RTGTYIGIDAMLEGLEAEGRVDVY 176
PTPc-N3 cd14600
catalytic domain of tyrosine-protein phosphatase non-receptor type 3; Tyrosine-protein ...
1137-1395 1.73e-18

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: 87.21  E-value: 1.73e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1925147141 1137 QFKLVSQRRARQADYAAALREgNDDKNRTSSLMPVERSRVCLScpvegESSDYINASY----IMGYHKSREFILTQSPLP 1212
Cdd:cd14600     19 QFEQLYRKKPGLAITCAKLPQ-NMDKNRYKDVLPYDATRVVLQ-----GNEDYINASYvnmeIPSANIVNKYIATQGPLP 92
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1925147141 1213 STVSDFWRMVWDHNSQLIISLPdthTAQREGEESC-AYWPskDQPISCE--GFIVSFSGED--------HMCLAN----E 1277
Cdd:cd14600     93 HTCAQFWQVVWEQKLSLIVMLT---TLTERGRTKChQYWP--DPPDVMEygGFRVQCHSEDctiayvfrEMLLTNtqtgE 167
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1925147141 1278 ERLVVHdflleatqdnyvlevRQYMSpcWPN---PDSPvSGTFQLLNIITEdSRQREGTIVVHDRLGGSVAGLFCALTTL 1354
Cdd:cd14600    168 ERTVTH---------------LQYVA--WPDhgvPDDS-SDFLEFVNYVRS-KRVENEPVLVHCSAGIGRTGVLVTMETA 228
                          250       260       270       280
                   ....*....|....*....|....*....|....*....|.
gi 1925147141 1355 AQQLEHQGSVDVYQVARMTNLMRPGVFNDMEQYQFMYRAVL 1395
Cdd:cd14600    229 MCLTERNQPVYPLDIVRKMRDQRAMMVQTSSQYKFVCEAIL 269
PHA02742 PHA02742
protein tyrosine phosphatase; Provisional
1154-1395 1.89e-18

protein tyrosine phosphatase; Provisional


Pssm-ID: 165109 [Multi-domain]  Cd Length: 303  Bit Score: 87.75  E-value: 1.89e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1925147141 1154 ALREGNDDKNRTSSLMPVERSRVCLscPVEGESSDYINASYIMGYHKSREFILTQSPLPSTVSDFWRMVWDHNSQLIISL 1233
Cdd:PHA02742    47 SLELKNMKKCRYPDAPCFDRNRVIL--KIEDGGDDFINASYVDGHNAKGRFICTQAPLEETALDFWQAIFQDQVRVIVMI 124
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1925147141 1234 PDTHtaqREGEESC-AYWPSKDQPISCEG-------FIVSFS--GEDHMCLANEERLVVHDFLLEATQD----------- 1292
Cdd:PHA02742   125 TKIM---EDGKEACyPYWMPHERGKATHGefkiktkKIKSFRnyAVTNLCLTDTNTGASLDIKHFAYEDwphgglprdpn 201
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1925147141 1293 ---NYVLEVRQYMSpcwpNPDSPVSGtfqllniiteDSRQREGTIVVHDRLGGSVAGLFCALTTLAQQLEHQGSVDVYQV 1369
Cdd:PHA02742   202 kflDFVLAVREADL----KADVDIKG----------ENIVKEPPILVHCSAGLDRAGAFCAIDICISKYNERAIIPLLSI 267
                          250       260
                   ....*....|....*....|....*.
gi 1925147141 1370 ARMTNLMRPGVFNDMEQYQFMYRAVL 1395
Cdd:PHA02742   268 VRDLRKQRHNCLSLPQQYIFCYFIVL 293
R-PTPc-M-2 cd14635
PTP domain of receptor-type tyrosine-protein phosphatase M, repeat 2; Receptor-type ...
894-1102 2.31e-18

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: 85.12  E-value: 2.31e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1925147141  894 YINANFVDGFERTRAYIAAQGPLKSGTEDFWRMVWQENVGVIVMITNLleKGRRKCDQYWPMENQEEYGHFLVTLKDTKT 973
Cdd:cd14635      1 YINAALMDSYKQPSAFIVTQHPLPNTVKDFWRLVLDYHCTSIVMLNDV--DPAQLCPQYWPENGVHRHGPIQVEFVSADL 78
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1925147141  974 LAYYTLRTFTLRDTSqkasqRGRCAERTVVQYHYTQWPDM-GVPEYTLPVLSFVRASTQARTQ---DMGPVLVHCSAGVG 1049
Cdd:cd14635     79 EEDIISRIFRIYNAA-----RPQDGYRMVQQFQFLGWPMYrDTPVSKRSFLKLIRQVDKWQEEyngGEGRTVVHCLNGGG 153
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|...
gi 1925147141 1050 RTGTYIVLDSMLQQIQDQGTVNILGFLKHVRTQRNYLVQTEEQYVFIHDALVE 1102
Cdd:cd14635    154 RSGTFCAISIVCEMLRHQRAVDVFHAVKTLRNNKPNMVDLLDQYKFCYEVALE 206
PTPc-N14 cd14599
catalytic domain of tyrosine-protein phosphatase non-receptor type 14; Tyrosine-protein ...
1137-1398 5.27e-18

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: 86.20  E-value: 5.27e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1925147141 1137 QFKLVSQRRARQADYAAALREgNDDKNRTSSLMPVERSRVCLsCPVEGESSDYINASYIMGYHKSRE--FILTQSPLPST 1214
Cdd:cd14599     17 EYEQIPKKKADGVFTTATLPE-NAERNRIREVVPYEENRVEL-VPTKENNTGYINASHIKVTVGGEEwhYIATQGPLPHT 94
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1925147141 1215 VSDFWRMVWDHNSQLIISLpdthTAQREG--EESCAYWP---SKDQPISCEGFIVSFS-GEDHMCLANEERLVVHdflLE 1288
Cdd:cd14599     95 CHDFWQMVWEQGVNVIAMV----TAEEEGgrSKSHRYWPklgSKHSSATYGKFKVTTKfRTDSGCYATTGLKVKH---LL 167
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1925147141 1289 ATQDNYVLEVrQYMSpcWPNPDSP--VSGTFQLL----------NIITEDSRQREGTIVVHDRLGGSVAGLFCALTTLAQ 1356
Cdd:cd14599    168 SGQERTVWHL-QYTD--WPDHGCPeeVQGFLSYLeeiqsvrrhtNSMLDSTKNCNPPIVVHCSAGVGRTGVVILTELMIG 244
                          250       260       270       280
                   ....*....|....*....|....*....|....*....|..
gi 1925147141 1357 QLEHQGSVDVYQVARMTNLMRPGVFNDMEQYQFMYRAVLSLV 1398
Cdd:cd14599    245 CLEHNEKVEVPVMLRHLREQRMFMIQTIAQYKFVYQVLIQFL 286
R-PTP-N-N2 cd14546
PTP-like domain of receptor-type tyrosine-protein phosphatase-like N and N2; Receptor-type ...
1189-1399 1.01e-17

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: 83.26  E-value: 1.01e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1925147141 1189 YINASYIMGyHKSRE--FILTQSPLPSTVSDFWRMVWDHNSQLIISLpdTHTAQREGEESCAYWPskDQPISCEG-FIVS 1265
Cdd:cd14546      1 YINASTIYD-HDPRNpaYIATQGPLPHTIADFWQMIWEQGCVVIVML--TRLQENGVKQCARYWP--EEGSEVYHiYEVH 75
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1925147141 1266 FSGEDHMClaneERLVVHDFLLEATQDNYVLEVRQYMSPCWPNPDSPVSgTFQLLNI---ITEDSRQREGTIVVHDRLGG 1342
Cdd:cd14546     76 LVSEHIWC----DDYLVRSFYLKNLQTSETRTVTQFHFLSWPDEGIPAS-AKPLLEFrrkVNKSYRGRSCPIVVHCSDGA 150
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1925147141 1343 SVAGLFCAL-TTLAQQLEHQGSVDVyqVARMTNL--MRPGVFNDMEQYQFMYRAVLSLVD 1399
Cdd:cd14546    151 GRTGTYILIdMVLNRMAKGAKEIDI--AATLEHLrdQRPGMVKTKDQFEFVLTAVAEEVN 208
PTP-N23 cd14539
PTP-like domain of tyrosine-protein phosphatase non-receptor type 23; Tyrosine-protein ...
1189-1391 2.41e-17

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: 82.05  E-value: 2.41e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1925147141 1189 YINASYIMGYHK-SREFILTQSPLPSTVSDFWRMVWDHNSQLIISLpdTHTAQREGEESCAYWPS-KDQPISCEGFIVsf 1266
Cdd:cd14539      1 YINASLIEDLTPyCPRFIATQAPLPGTAADFWLMVYEQQVSVIVML--VSEQENEKQKVHRYWPTeRGQALVYGAITV-- 76
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1925147141 1267 sgedhmCLANEErlvvhdflleaTQDNYV--------LEVRQYMS------PCWP---NPDSPvSGTFQLLNIITEDSRQ 1329
Cdd:cd14539     77 ------SLQSVR-----------TTPTHVeriisiqhKDTRLSRSvvhlqfTTWPelgLPDSP-NPLLRFIEEVHSHYLQ 138
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1925147141 1330 REGT---IVVHDRLGGSVAGLFCALTTLAQQLEH-QGSVDVYQVARMTNLMRPGVFNDMEQYQFMY 1391
Cdd:cd14539    139 QRSLqtpIVVHCSSGVGRTGAFCLLYAAVQEIEAgNGIPDLPQLVRKMRQQRKYMLQEKEHLKFCY 204
PTPc-N21_14 cd14540
catalytic domain of tyrosine-protein phosphatase non-receptor type 21 and type 14; ...
1189-1395 5.33e-16

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: 78.65  E-value: 5.33e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1925147141 1189 YINASYIMGY--HKSREFILTQSPLPSTVSDFWRMVWDHNSQLIISLPDThtaQREGEESC-AYWPskdqpiscegfivs 1265
Cdd:cd14540      1 YINASHITATvgGKQRFYIAAQGPLQNTVGDFWQMVWEQGVYLVVMVTAE---EEGGREKCfRYWP-------------- 63
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1925147141 1266 FSGEDHMCLANEERLVVHDFLLEAtqDNYV---LEVR-------------QYMSpcWPNPDSP--VSGTFQLLNIITE-- 1325
Cdd:cd14540     64 TLGGEHDALTFGEYKVSTKFSVSS--GCYTttgLRVKhtlsgqsrtvwhlQYTD--WPDHGCPedVSGFLDFLEEINSvr 139
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1925147141 1326 -------DSRQREGTIVVHDRLGGSVAGLFCALTTLAQQLEHQGSVDVYQVARMTNLMRPGVFNDMEQYQFMYRAVL 1395
Cdd:cd14540    140 rhtnqdvAGHNRNPPTLVHCSAGVGRTGVVILADLMLYCLDHNEELDIPRVLALLRHQRMLLVQTLAQYKFVYNVLI 216
PTPc-N3_4 cd14541
catalytic domain of tyrosine-protein phosphatase non-receptor type 21 and type 14; ...
1188-1396 7.15e-16

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: 78.14  E-value: 7.15e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1925147141 1188 DYINASYI-MGYHKS---REFILTQSPLPSTVSDFWRMVWDHNSQLIISLpdTHTAQReGEESC-AYWPSKDQPISCEGF 1262
Cdd:cd14541      1 DYINANYVnMEIPGSgivNRYIAAQGPLPNTCADFWQMVWEQKSTLIVML--TTLVER-GRVKChQYWPDLGETMQFGNL 77
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1925147141 1263 IVSFSGEDhmclaNEERLVVHDFLLEATQDNYVLEVRQYMSPCWPN---PDSPVsgtfQLLNIITEDSRQREGT---IVV 1336
Cdd:cd14541     78 QITCVSEE-----VTPSFAFREFILTNTNTGEERHITQMQYLAWPDhgvPDDSS----DFLDFVKRVRQNRVGMvepTVV 148
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1925147141 1337 HDRLGGSVAGLFCALTTLAQQLEHQGSVDVYQVARMTNLMRPGVFNDMEQYQFMYRAVLS 1396
Cdd:cd14541    149 HCSAGIGRTGVLITMETAMCLIEANEPVYPLDIVRTMRDQRAMLIQTPSQYRFVCEAILR 208
PTPc_DSPc smart00012
Protein tyrosine phosphatase, catalytic domain, undefined specificity; Protein tyrosine ...
1300-1396 5.64e-14

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: 69.31  E-value: 5.64e-14
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1925147141  1300 QYMSpcWPNPDSPVSGT--FQLLNIITEDSRQRE--GTIVVHDRLGGSVAGLFCALTTLAQQLEH-QGSVDVYQVARMTN 1374
Cdd:smart00012    6 HYTG--WPDHGVPESPDsiLELLRAVKKNLNQSEssGPVVVHCSAGVGRTGTFVAIDILLQQLEAeAGEVDIFDTVKELR 83
                            90       100
                    ....*....|....*....|..
gi 1925147141  1375 LMRPGVFNDMEQYQFMYRAVLS 1396
Cdd:smart00012   84 SQRPGMVQTEEQYLFLYRALLE 105
PTPc_motif smart00404
Protein tyrosine phosphatase, catalytic domain motif;
1300-1396 5.64e-14

Protein tyrosine phosphatase, catalytic domain motif;


Pssm-ID: 214649 [Multi-domain]  Cd Length: 105  Bit Score: 69.31  E-value: 5.64e-14
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1925147141  1300 QYMSpcWPNPDSPVSGT--FQLLNIITEDSRQRE--GTIVVHDRLGGSVAGLFCALTTLAQQLEH-QGSVDVYQVARMTN 1374
Cdd:smart00404    6 HYTG--WPDHGVPESPDsiLELLRAVKKNLNQSEssGPVVVHCSAGVGRTGTFVAIDILLQQLEAeAGEVDIFDTVKELR 83
                            90       100
                    ....*....|....*....|..
gi 1925147141  1375 LMRPGVFNDMEQYQFMYRAVLS 1396
Cdd:smart00404   84 SQRPGMVQTEEQYLFLYRALLE 105
PTPc-N4 cd14601
catalytic domain of tyrosine-protein phosphatase non-receptor type 4; Tyrosine-protein ...
1188-1399 6.05e-14

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: 72.29  E-value: 6.05e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1925147141 1188 DYINASYI-MGYHKS---REFILTQSPLPSTVSDFWRMVWDHNSQLIISLpdTHTAQREGEESCAYWPSKDQPISCEGFI 1263
Cdd:cd14601      1 DYINANYInMEIPSSsiiNRYIACQGPLPNTCSDFWQMTWEQGSSMVVML--TTQVERGRVKCHQYWPEPSGSSSYGGFQ 78
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1925147141 1264 VSFSGEDhmclaNEERLVVHDFLLEATQDNYVLEVRQYMSPCWPNPDSPVSGTfQLLNIITEDSRQREGT---IVVHDRL 1340
Cdd:cd14601     79 VTCHSEE-----GNPAYVFREMTLTNLEKNESRPLTQIQYIAWPDHGVPDDSS-DFLDFVCLVRNKRAGKdepVVVHCSA 152
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 1925147141 1341 GGSVAGLFCALTTLAQQLEHQGSVDVYQVARMTNLMRPGVFNDMEQYQFMYRAVLSLVD 1399
Cdd:cd14601    153 GIGRTGVLITMETAMCLIECNQPVYPLDIVRTMRDQRAMMIQTPSQYRFVCEAILKVYE 211
PTPc-N21 cd14598
catalytic domain of tyrosine-protein phosphatase non-receptor type 21; Tyrosine-protein ...
1189-1398 1.18e-12

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: 68.85  E-value: 1.18e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1925147141 1189 YINASYIMGYHKSRE--FILTQSPLPSTVSDFWRMVWDHNSQLIISLpdthTAQREG--EESCAYWP---SKDQPISCEG 1261
Cdd:cd14598      1 YINASHIKVTVGGKEwdYIATQGPLQNTCQDFWQMVWEQGVAIIAMV----TAEEEGgrEKSFRYWPrlgSRHNTVTYGR 76
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1925147141 1262 F-IVSFSGEDHMCLANEERLVVHdflLEATQDNYVLEVrQYMSpcWPNPDSP--VSGTFQLLNII---------TEDSRQ 1329
Cdd:cd14598     77 FkITTRFRTDSGCYATTGLKIKH---LLTGQERTVWHL-QYTD--WPEHGCPedLKGFLSYLEEIqsvrrhtnsTIDPKS 150
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1925147141 1330 REGTIVVHDRLGGSVAGLFCALTTLAQQLEHQGSVDVYQVARMTNLMRPGVFNDMEQYQFMYRAVLSLV 1398
Cdd:cd14598    151 PNPPVLVHCSAGVGRTGVVILSEIMIACLEHNEMLDIPRVLDMLRQQRMMMVQTLSQYTFVYKVLIQFL 219
PLN02179 PLN02179
carbonic anhydrase
52-256 3.50e-12

carbonic anhydrase


Pssm-ID: 177835  Cd Length: 235  Bit Score: 67.70  E-value: 3.50e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1925147141   52 WGKRYP---ACNNAR-QSPIDIdetfTQVRVEYqgLQLEGWEKN-TPETTTINNDGNTVVLGLDGEyyvsGGGLS---TR 123
Cdd:PLN02179    50 WGKLNPqwkVCSTGKyQSPIDL----TDERVSL--IHDQALSRHyKPAPAVIQSRGHDVMVSWKGD----AGKITihqTD 119
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1925147141  124 FRLgrMTFHWgrcnasSDGSEHSLNGLKFPLEMQILCYESGlyqsiddavrdgGRIAALAVLFEtsLDNNDNYNT-ILEG 202
Cdd:PLN02179   120 YKL--VQCHW------HSPSEHTINGTSYDLELHMVHTSAS------------GKTAVVGVLYK--LGEPDEFLTkLLNG 177
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1925147141  203 VNSV-NRFGKTGNVEPFSLLAllpnSTDKYYTYNGSLTSPPCSETVEWIVFKHTV 256
Cdd:PLN02179   178 IKGVgKKEINLGIVDPRDIRF----ETNNFYRYIGSLTIPPCTEGVIWTVVKRVV 228
fn3 pfam00041
Fibronectin type III domain;
316-404 5.99e-12

Fibronectin type III domain;


Pssm-ID: 394996 [Multi-domain]  Cd Length: 85  Bit Score: 62.82  E-value: 5.99e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1925147141  316 SEPQNMQADAQNETTIMVMWERPRVVyDTTIDWYSVTYQRlQDQNQPKHEYRTDGDQDvGAIIPGLLSNSSYVVQVVAVC 395
Cdd:pfam00041    1 SAPSNLTVTDVTSTSLTVSWTPPPDG-NGPITGYEVEYRP-KNSGEPWNEITVPGTTT-SVTLTGLKPGTEYEVRVQAVN 77

                   ....*....
gi 1925147141  396 TNGLtGRWS 404
Cdd:pfam00041   78 GGGE-GPPS 85
PTP_YopH-like cd14559
YopH and related bacterial protein tyrosine phosphatases; Yersinia outer protein H (YopH) ...
870-1094 2.25e-11

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: 65.11  E-value: 2.25e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1925147141  870 NRYINImaydHSRVKLLEeGKGgdyINANFVDGFERTRAyIAAQGPLKSGTEDFWRMVWQENVGVIVMITNLLEKGRRKC 949
Cdd:cd14559      1 NRFTNI----QTRVSTPV-GKN---LNANRVQIGNKNVA-IACQYPKNEQLEDHLKMLADNRTPCLVVLASNKDIQRKGL 71
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1925147141  950 DQYWPMENQeeYGHflVTLKDTKTLAYYTLRTFTLRDTSQKASQRGRCAERTVvqYHYTQWPDMGV--PEYTLPVLSFVR 1027
Cdd:cd14559     72 PPYFRQSGT--YGS--VTVKSKKTGKDELVDGLKADMYNLKITDGNKTITIPV--VHVTNWPDHTAisSEGLKELADLVN 145
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1925147141 1028 ASTQARTQDMG--------------PVlVHCSAGVGRTGTYIVLDSMLQQiqdQGTVNILGFLKHVRTQRN-YLVQTEEQ 1092
Cdd:cd14559    146 KSAEEKRNFYKskgssaindknkllPV-IHCRAGVGRTGQLAAAMELNKS---PNNLSVEDIVSDMRTSRNgKMVQKDEQ 221

                   ..
gi 1925147141 1093 YV 1094
Cdd:cd14559    222 LD 223
PTPc_plant_PTP1 cd17658
protein tyrosine phosphatase 1 from Arabidopsis thaliana and similar plant PTPs; Arabidopsis ...
1189-1391 7.08e-11

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: 63.25  E-value: 7.08e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1925147141 1189 YINASYIM--GYHKSREFILTQSPLPSTVSDFWRMVWDHNSQLIISLpdTHTAQREGEESCA-YWPSKD-QPISCEGFIV 1264
Cdd:cd17658      1 YINASLVEtpASESLPKFIATQGPLPHTFEDFWEMVIQQRCPVIIML--TRLVDNYSTAKCAdYFPAEEnESREFGRISV 78
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1925147141 1265 SFSGEDHMCLANEER-LVVHDFLLEATqdnyVLEVRQYMSPCWPN---PDS--PVSGTFQLLNIITEDsrqrEGTIVVHD 1338
Cdd:cd17658     79 TNKKLKHSQHSITLRvLEVQYIESEEP----PLSVLHIQYPEWPDhgvPKDtrSVRELLKRLYGIPPS----AGPIVVHC 150
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1925147141 1339 RLGGSVAGLFCAL-TTLAQQLEHQGS-VDVYQVARMTNLMRPGVFNDMEQYQFMY 1391
Cdd:cd17658    151 SAGIGRTGAYCTIhNTIRRILEGDMSaVDLSKTVRKFRSQRIGMVQTQDQYIFCY 205
CDC14 COG2453
Protein-tyrosine phosphatase [Signal transduction mechanisms];
1003-1098 1.68e-09

Protein-tyrosine phosphatase [Signal transduction mechanisms];


Pssm-ID: 441989 [Multi-domain]  Cd Length: 140  Bit Score: 57.67  E-value: 1.68e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1925147141 1003 VQYHYTQWPDMGVPEYTLpVLSFVRASTQARTQDmGPVLVHCSAGVGRTGT----YIVLDSM-LQQIqdqgtvnilgfLK 1077
Cdd:COG2453     48 LEYLHLPIPDFGAPDDEQ-LQEAVDFIDEALREG-KKVLVHCRGGIGRTGTvaaaYLVLLGLsAEEA-----------LA 114
                           90       100
                   ....*....|....*....|.
gi 1925147141 1078 HVRTQRNYLVQTEEQYVFIHD 1098
Cdd:COG2453    115 RVRAARPGAVETPAQRAFLER 135
PHA02740 PHA02740
protein tyrosine phosphatase; Provisional
1190-1392 3.47e-07

protein tyrosine phosphatase; Provisional


Pssm-ID: 165107 [Multi-domain]  Cd Length: 298  Bit Score: 53.82  E-value: 3.47e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1925147141 1190 INASYIMGYHKSREFILTQSPLPSTVSDFWRMVWDHNSQLIIslpdthTAQREGEESC--AYWPSKdqpiscEGFIVSFs 1267
Cdd:PHA02740    79 LDARFVDGYDFEQKFICIINLCEDACDKFLQALSDNKVQIIV------LISRHADKKCfnQFWSLK------EGCVITS- 145
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1925147141 1268 geDHMCLANEERLVVHDF---LLEAT-QDNYVLEVRQYMSPCWP------NPDSPVSGTFQLLNIITEDSRQRE----GT 1333
Cdd:PHA02740   146 --DKFQIETLEIIIKPHFnltLLSLTdKFGQAQKISHFQYTAWPadgfshDPDAFIDFFCNIDDLCADLEKHKAdgkiAP 223
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 1925147141 1334 IVVHDRLGGSVAGLFCALTTLAQQLEHQGSVDVYQVARMTNLMRPGVFNDMEQYQFMYR 1392
Cdd:PHA02740   224 IIIDCIDGISSSAVFCVFDICATEFDKTGMLSIANALKKVRQKKYGCMNCLDDYVFCYH 282
PTP_PTPDC1 cd14506
protein tyrosine phosphatase domain of PTP domain-containing protein 1; protein tyrosine ...
1005-1098 4.44e-07

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: 51.97  E-value: 4.44e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1925147141 1005 YHYT-QWPDMGVPEYTLpVLSFVRASTQArTQDMGPVLVHCSAGVGRTGTYI--VLDSMLQQIQDQGtvnilgfLKHVRT 1081
Cdd:cd14506     78 YFYNfGWKDYGVPSLTT-ILDIVKVMAFA-LQEGGKVAVHCHAGLGRTGVLIacYLVYALRMSADQA-------IRLVRS 148
                           90
                   ....*....|....*..
gi 1925147141 1082 QRNYLVQTEEQYVFIHD 1098
Cdd:cd14506    149 KRPNSIQTRGQVLCVRE 165
FN3 cd00063
Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein ...
316-409 5.29e-07

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


Pssm-ID: 238020 [Multi-domain]  Cd Length: 93  Bit Score: 49.03  E-value: 5.29e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1925147141  316 SEPQNMQADAQNETTIMVMWERPRVvYDTTIDWYSVTYQRLQDQNQpkHEYRTDGDQDVGAIIPGLLSNSSYVVQVVAVC 395
Cdd:cd00063      2 SPPTNLRVTDVTSTSVTLSWTPPED-DGGPITGYVVEYREKGSGDW--KEVEVTPGSETSYTLTGLKPGTEYEFRVRAVN 78
                           90
                   ....*....|....
gi 1925147141  396 TNGlTGRWSDQIIV 409
Cdd:cd00063     79 GGG-ESPPSESVTV 91
DUSP23 cd14504
dual specificity phosphatase 23; Dual specificity phosphatase 23 (DUSP23), also known as ...
1003-1096 9.63e-07

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: 49.58  E-value: 9.63e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1925147141 1003 VQYHYTQWPDMGVPeyTLP-VLSFVRASTQARTQDmGPVLVHCSAGVGRTGT----YIVLDSMLQQIQDqgtvnilgfLK 1077
Cdd:cd14504     50 LRYHHIPIEDYTPP--TLEqIDEFLDIVEEANAKN-EAVLVHCLAGKGRTGTmlacYLVKTGKISAVDA---------IN 117
                           90
                   ....*....|....*....
gi 1925147141 1078 HVRTQRNYLVQTEEQYVFI 1096
Cdd:cd14504    118 EIRRIRPGSIETSEQEKFV 136
PTP_DSP_cys cd14494
cys-based protein tyrosine phosphatase and dual-specificity phosphatase superfamily; This ...
1038-1098 1.30e-06

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: 48.50  E-value: 1.30e-06
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1925147141 1038 GPVLVHCSAGVGRTGTYIVLDSMLQQIqdqgtVNILGFLKHVRTQR-NYLVQTEEQYVFIHD 1098
Cdd:cd14494     57 EPVLVHCKAGVGRTGTLVACYLVLLGG-----MSAEEAVRIVRLIRpGGIPQTIEQLDFLIK 113
FN3 smart00060
Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, ...
316-398 2.79e-06

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: 46.84  E-value: 2.79e-06
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1925147141   316 SEPQNMQADAQNETTIMVMWERPRvvyDTTIDWYSVTYQRLQDQNQPKHEYRTDGDQDVGAIIPGLLSNSSYVVQVVAVC 395
Cdd:smart00060    2 SPPSNLRVTDVTSTSVTLSWEPPP---DDGITGYIVGYRVEYREEGSEWKEVNVTPSSTSYTLTGLKPGTEYEFRVRAVN 78

                    ...
gi 1925147141   396 TNG 398
Cdd:smart00060   79 GAG 81
PLN02202 PLN02202
carbonate dehydratase
36-266 1.05e-05

carbonate dehydratase


Pssm-ID: 177853 [Multi-domain]  Cd Length: 284  Bit Score: 48.90  E-value: 1.05e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1925147141   36 TDDIDWSYTGQLNQKIWGKRYP---ACNNAR-QSPIDIdetftQVRVEYQGLQLEGWEKNTPET--TTINNDGNTVVLGL 109
Cdd:PLN02202    26 TEGVVFGYKGKNGPNQWGHLNPhftKCAVGKlQSPIDI-----QRRQIFYNHKLESIHRDYYFTnaTLVNHVCNVAMFFG 100
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1925147141  110 DGeyyvSGGGLSTRFRLGRMTFHWgrcnasSDGSEHSLNGLKFPLEMQILcyesglYQSIDdavrdgGRIAALAVLFETS 189
Cdd:PLN02202   101 EG----AGDVIIDNKNYTLLQMHW------HTPSEHHLHGVQYAAELHMV------HQAKD------GSFAVVASLFKIG 158
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1925147141  190 LDN---NDNYNTILEGVNSVNRFGKTGNVEPFSL-LALLPNSTDKYYTYNGSLTSPPCSETVEWIVFKHTVPISETQLEV 265
Cdd:PLN02202   159 TEEpflSQMKDKLVKLKEERFKGNHTAQVEVGKIdTRHIERKTRKYFRYIGSLTTPPCSENVSWTILGKVRSMSKEQVEL 238

                   .
gi 1925147141  266 F 266
Cdd:PLN02202   239 L 239
CDKN3-like cd14505
cyclin-dependent kinase inhibitor 3 and similar proteins; This family is composed of ...
1011-1098 7.46e-05

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


Pssm-ID: 350355 [Multi-domain]  Cd Length: 163  Bit Score: 44.56  E-value: 7.46e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1925147141 1011 PDMGVP---EYTLPVLSFVRASTQARTQdmgpVLVHCSAGVGRTGTyiVLDSMLQQIQDQGTVNILgfLKHVRTQRNYLV 1087
Cdd:cd14505     81 PDGGVPsdiAQWQELLEELLSALENGKK----VLIHCKGGLGRTGL--IAACLLLELGDTLDPEQA--IAAVRALRPGAI 152
                           90
                   ....*....|.
gi 1925147141 1088 QTEEQYVFIHD 1098
Cdd:cd14505    153 QTPKQENFLHQ 163
TpbA-like cd14529
bacterial protein tyrosine and dual-specificity phosphatases related to Pseudomonas aeruginosa ...
969-1054 3.65e-03

bacterial protein tyrosine and dual-specificity phosphatases related to Pseudomonas aeruginosa TpbA; This subfamily contains bacterial protein tyrosine phosphatases (PTPs) and dual-specificity phosphatases (DUSPs) related to Pseudomonas aeruginosa TpbA, a DUSP that negatively regulates biofilm formation by converting extracellular quorum sensing signals and to Mycobacterium tuberculosis PtpB, a PTP virulence factor that attenuates host immune defenses by interfering with signal transduction pathways in macrophages. PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides, while DUSPs function as protein-serine/threonine phosphatases (EC 3.1.3.16) and PTPs.


Pssm-ID: 350378 [Multi-domain]  Cd Length: 158  Bit Score: 39.66  E-value: 3.65e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1925147141  969 KDTKTLAYYTLRT-FTLRDTSQKASQRGrcAERTVVQYHYTQWPDMGVpEYTLPVLSFVRASTQARTQDmGPVLVHCSAG 1047
Cdd:cd14529     24 EDRALLKKLGIKTvIDLRGADERAASEE--AAAKIDGVKYVNLPLSAT-RPTESDVQSFLLIMDLKLAP-GPVLIHCKHG 99

                   ....*..
gi 1925147141 1048 VGRTGTY 1054
Cdd:cd14529    100 KDRTGLV 106
 
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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