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Conserved domains on  [gi|1658117674|ref|XP_029103085|]
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receptor-type tyrosine-protein phosphatase zeta-like isoform X8 [Scleropages formosus]

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 ...
 755-1025 1.29e-161

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: 484.92  E-value: 1.29e-161
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658117674  755 FSQEFEEIQACTVDLGITADSSIHPENKNKNRYINILAYDHSRVKLSSSSDRNGWSADYINANYVDGFTQPKAYIATQGP 834
Cdd:cd17667      1 FSEDFEEVQRCTADMNITAEHSNHPDNKHKNRYINILAYDHSRVKLRPLPGKDSKHSDYINANYVDGYNKAKAYIATQGP 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658117674  835 LKSSMEDFWRMVWEQNASVIVMITNLVEKGRRKCDQYWPLDSQEEYGSFLVTLRSTKVLAYYTQRTFTLKNTRAKKGSQ- 913
Cdd:cd17667     81 LKSTFEDFWRMIWEQNTGIIVMITNLVEKGRRKCDQYWPTENSEEYGNIIVTLKSTKIHACYTVRRFSIRNTKVKKGQKg 160

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658117674  914 --KEQTHERTVVQYHYTQWPDMGVPEYTLPVLTFVRKSSQANLGNMGPVVVHCSAGVGRTGTYIVLDSMLRQIKEQGTVN 991
Cdd:cd17667    161 npKGRQNERTVIQYHYTQWPDMGVPEYALPVLTFVRRSSAARTPEMGPVLVHCSAGVGRTGTYIVIDSMLQQIKDKSTVN 240

                          250       260       270
                   ....*....|....*....|....*....|....
gi 1658117674  992 ILGFLKHIRTQRNYLVQTEEQYIFIHDALVEAIL 1025
Cdd:cd17667    241 VLGFLKHIRTQRNYLVQTEEQYIFIHDALLEAIL 274
R5-PTP-2 cd14550
PTP-like domain of R5 subfamily receptor-type tyrosine-protein phosphatases, repeat 2; The R5 ...
 1108-1308 3.31e-122

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: 377.43  E-value: 3.31e-122
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658117674 1108 YINASYIMGYQQSNEFIITQNPLPSTMKDFWKMIWDHSTQVVIALPDGlDLAEDECIYWPTKSQPIRFDTFTVTFMGEDH 1187
Cdd:cd14550      1 YINASYLQGYRRSNEFIITQHPLEHTIKDFWQMIWDHNSQTIVMLTDN-ELNEDEPIYWPTKEKPLECETFKVTLSGEDH 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658117674 1188 MCLSNEDMLIVQDFILEATQDDYVLEVRQYRAPRWPNPDGPISNTFELINIIKEESVSRDGPIVVHDKRGGNIAGTFCAL 1267
Cdd:cd14550     80 SCLSNEIRLIVRDFILESTQDDYVLEVRQFQCPSWPNPCSPIHTVFELINTVQEWAQQRDGPIVVHDRYGGVQAATFCAL 159

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|.
gi 1658117674 1268 MTLLHQLEMESSFDVYWVAKMINLMRPGIFTDIDQYQFLYK 1308
Cdd:cd14550    160 TTLHQQLEHESSVDVYQVAKLYHLMRPGVFTSKEDYQFLYK 200
alpha_CARP_receptor_like cd03122
Carbonic anhydrase alpha related protein, receptor_like subfamily. Carbonic anhydrase related ...
 48-301 3.20e-106

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: 336.25  E-value: 3.20e-106
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658117674   48 NQNNWAKKYPSCNNA-KQSPINIDDDlSQVK-MQFQKLKLEGFEQETSNTTtIHNDGKTVAINLND---EYYISGGGLRS 122
Cdd:cd03122      1 NPKHWAKKYPACGEGrQQSPIDIVED-TQVQrQGLQPLHFDGYEELTASTT-LENTGKTVILRLEGnssDPFVSGGPLLG 78

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658117674  123 RFKVGRITFHWGQCNasSDGSEHSLDGIKFPLEMQIYGYeAHKFQSLDSALKDGGRLTALSVLFEVSAEDNENYVAIIDG 202
Cdd:cd03122     79 RYKFSEITFHWGTCN--SDGSEHSIDGHKFPLEMQILHR-NTDFFDSFEAIKSPGGVLALAYLFELSHEDNPFLDPIIEG 155

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658117674  203 VKTVTRLGKTAVLEPFSLLGLLPNSTEKYYIYNGSLTTPPCSETVEWIVFRNTVDISDVQLETFCEVMTMQQAGyVMLMD 282
Cdd:cd03122    156 LRNVSRPGKEVELPPFPLSDLLPPFTDKYYSYEGSLTTPPCSETVEWIVFREPVPISSRQLEAFRELLTRRQDG-VMSGD 234

                          250
                   ....*....|....*....
gi 1658117674  283 YLQNNFREQQLKFVGQVFS 301
Cdd:cd03122    235 YLPNNGRPQQPLGSRTVFS 253
fn3 pfam00041
Fibronectin type III domain;
316-398 2.06e-11

Fibronectin type III domain;


:

Pssm-ID: 394996 [Multi-domain]  Cd Length: 85  Bit Score: 61.28  E-value: 2.06e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658117674  316 SEPENVEADPYNYTSLLVTWERPRAVYDVgIERYLVSYQPVGDEDlPKNEYLTDGDQDvGAIIQDLSANTSYVVQVVAVC 395
Cdd:pfam00041    1 SAPSNLTVTDVTSTSLTVSWTPPPDGNGP-ITGYEVEYRPKNSGE-PWNEITVPGTTT-SVTLTGLKPGTEYEVRVQAVN 77


                   ...
gi 1658117674  396 ING 398
Cdd:pfam00041   78 GGG 80
 
Name Accession Description Interval E-value
R-PTPc-G-1 cd17667
catalytic domain of receptor-type tyrosine-protein phosphatase G, repeat 1; Receptor-type ...
 755-1025 1.29e-161

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: 484.92  E-value: 1.29e-161
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658117674  755 FSQEFEEIQACTVDLGITADSSIHPENKNKNRYINILAYDHSRVKLSSSSDRNGWSADYINANYVDGFTQPKAYIATQGP 834
Cdd:cd17667      1 FSEDFEEVQRCTADMNITAEHSNHPDNKHKNRYINILAYDHSRVKLRPLPGKDSKHSDYINANYVDGYNKAKAYIATQGP 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658117674  835 LKSSMEDFWRMVWEQNASVIVMITNLVEKGRRKCDQYWPLDSQEEYGSFLVTLRSTKVLAYYTQRTFTLKNTRAKKGSQ- 913
Cdd:cd17667     81 LKSTFEDFWRMIWEQNTGIIVMITNLVEKGRRKCDQYWPTENSEEYGNIIVTLKSTKIHACYTVRRFSIRNTKVKKGQKg 160

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658117674  914 --KEQTHERTVVQYHYTQWPDMGVPEYTLPVLTFVRKSSQANLGNMGPVVVHCSAGVGRTGTYIVLDSMLRQIKEQGTVN 991
Cdd:cd17667    161 npKGRQNERTVIQYHYTQWPDMGVPEYALPVLTFVRRSSAARTPEMGPVLVHCSAGVGRTGTYIVIDSMLQQIKDKSTVN 240

                          250       260       270
                   ....*....|....*....|....*....|....
gi 1658117674  992 ILGFLKHIRTQRNYLVQTEEQYIFIHDALVEAIL 1025
Cdd:cd17667    241 VLGFLKHIRTQRNYLVQTEEQYIFIHDALLEAIL 274
R5-PTP-2 cd14550
PTP-like domain of R5 subfamily receptor-type tyrosine-protein phosphatases, repeat 2; The R5 ...
 1108-1308 3.31e-122

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: 377.43  E-value: 3.31e-122
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658117674 1108 YINASYIMGYQQSNEFIITQNPLPSTMKDFWKMIWDHSTQVVIALPDGlDLAEDECIYWPTKSQPIRFDTFTVTFMGEDH 1187
Cdd:cd14550      1 YINASYLQGYRRSNEFIITQHPLEHTIKDFWQMIWDHNSQTIVMLTDN-ELNEDEPIYWPTKEKPLECETFKVTLSGEDH 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658117674 1188 MCLSNEDMLIVQDFILEATQDDYVLEVRQYRAPRWPNPDGPISNTFELINIIKEESVSRDGPIVVHDKRGGNIAGTFCAL 1267
Cdd:cd14550     80 SCLSNEIRLIVRDFILESTQDDYVLEVRQFQCPSWPNPCSPIHTVFELINTVQEWAQQRDGPIVVHDRYGGVQAATFCAL 159

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|.
gi 1658117674 1268 MTLLHQLEMESSFDVYWVAKMINLMRPGIFTDIDQYQFLYK 1308
Cdd:cd14550    160 TTLHQQLEHESSVDVYQVAKLYHLMRPGVFTSKEDYQFLYK 200
PTPc smart00194
Protein tyrosine phosphatase, catalytic domain;
755-1022 6.92e-115

Protein tyrosine phosphatase, catalytic domain;


Pssm-ID: 214550 [Multi-domain]  Cd Length: 259  Bit Score: 360.05  E-value: 6.92e-115
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658117674   755 FSQEFEEIQACTVDLgITADSSIHPENKNKNRYINILAYDHSRVKLSsssDRNGWSADYINANYVDGFTQPKAYIATQGP 834
Cdd:smart00194    2 LEEEFEKLDRLKPDD-ESCTVAAFPENRDKNRYKDVLPYDHTRVKLK---PPPGEGSDYINASYIDGPNGPKAYIATQGP 77

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658117674   835 LKSSMEDFWRMVWEQNASVIVMITNLVEKGRRKCDQYWPLDSQE--EYGSFLVTLRSTKVLAYYTQRTFTLKNTrakkgs 912
Cdd:smart00194   78 LPSTVEDFWRMVWEQKVTVIVMLTELVEKGREKCAQYWPDEEGEplTYGDITVTLKSVEKVDDYTIRTLEVTNT------ 151

                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658117674   913 qkEQTHERTVVQYHYTQWPDMGVPEYTLPVLTFVRKSSQANLGNMGPVVVHCSAGVGRTGTYIVLDSMLRQIKEQGTVNI 992
Cdd:smart00194  152 --GCSETRTVTHYHYTNWPDHGVPESPESILDLIRAVRKSQSTSTGPIVVHCSAGVGRTGTFIAIDILLQQLEAGKEVDI 229

                           250       260       270
                    ....*....|....*....|....*....|
gi 1658117674   993 LGFLKHIRTQRNYLVQTEEQYIFIHDALVE 1022
Cdd:smart00194  230 FEIVKELRSQRPGMVQTEEQYIFLYRAILE 259
Y_phosphatase pfam00102
Protein-tyrosine phosphatase;
781-1022 8.57e-110

Protein-tyrosine phosphatase;


Pssm-ID: 459674 [Multi-domain]  Cd Length: 234  Bit Score: 345.38  E-value: 8.57e-110
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658117674  781 NKNKNRYINILAYDHSRVKLSSSSDRNgwsaDYINANYVDGFTQPKAYIATQGPLKSSMEDFWRMVWEQNASVIVMITNL 860
Cdd:pfam00102    1 NLEKNRYKDVLPYDHTRVKLTGDPGPS----DYINASYIDGYKKPKKYIATQGPLPNTVEDFWRMVWEEKVTIIVMLTEL 76

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658117674  861 VEKGRRKCDQYWPLDSQE--EYGSFLVTLRSTK-VLAYYTQRTFTLKNTRAKkgsqkeqtHERTVVQYHYTQWPDMGVPE 937
Cdd:pfam00102   77 EEKGREKCAQYWPEEEGEslEYGDFTVTLKKEKeDEKDYTVRTLEVSNGGSE--------ETRTVKHFHYTGWPDHGVPE 148

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658117674  938 YTLPVLTFVRK-SSQANLGNMGPVVVHCSAGVGRTGTYIVLDSMLRQIKEQGTVNILGFLKHIRTQRNYLVQTEEQYIFI 1016
Cdd:pfam00102  149 SPNSLLDLLRKvRKSSLDGRSGPIVVHCSAGIGRTGTFIAIDIALQQLEAEGEVDIFQIVKELRSQRPGMVQTLEQYIFL 228


                   ....*.
gi 1658117674 1017 HDALVE 1022
Cdd:pfam00102  229 YDAILE 234
alpha_CARP_receptor_like cd03122
Carbonic anhydrase alpha related protein, receptor_like subfamily. Carbonic anhydrase related ...
 48-301 3.20e-106

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: 336.25  E-value: 3.20e-106
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658117674   48 NQNNWAKKYPSCNNA-KQSPINIDDDlSQVK-MQFQKLKLEGFEQETSNTTtIHNDGKTVAINLND---EYYISGGGLRS 122
Cdd:cd03122      1 NPKHWAKKYPACGEGrQQSPIDIVED-TQVQrQGLQPLHFDGYEELTASTT-LENTGKTVILRLEGnssDPFVSGGPLLG 78

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658117674  123 RFKVGRITFHWGQCNasSDGSEHSLDGIKFPLEMQIYGYeAHKFQSLDSALKDGGRLTALSVLFEVSAEDNENYVAIIDG 202
Cdd:cd03122     79 RYKFSEITFHWGTCN--SDGSEHSIDGHKFPLEMQILHR-NTDFFDSFEAIKSPGGVLALAYLFELSHEDNPFLDPIIEG 155

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658117674  203 VKTVTRLGKTAVLEPFSLLGLLPNSTEKYYIYNGSLTTPPCSETVEWIVFRNTVDISDVQLETFCEVMTMQQAGyVMLMD 282
Cdd:cd03122    156 LRNVSRPGKEVELPPFPLSDLLPPFTDKYYSYEGSLTTPPCSETVEWIVFREPVPISSRQLEAFRELLTRRQDG-VMSGD 234

                          250
                   ....*....|....*....
gi 1658117674  283 YLQNNFREQQLKFVGQVFS 301
Cdd:cd03122    235 YLPNNGRPQQPLGSRTVFS 253
Carb_anhydrase pfam00194
Eukaryotic-type carbonic anhydrase;
47-303 6.35e-86

Eukaryotic-type carbonic anhydrase;


Pssm-ID: 459707 [Multi-domain]  Cd Length: 252  Bit Score: 280.31  E-value: 6.35e-86
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658117674   47 LNQNNWAKKYPSCNNAKQSPINIDDDLSQVKMQFQKLKLEGFEQeTSNTTTIHNDGKTVAINLNDEY--YISGGGLRSRF 124
Cdd:pfam00194    1 LGPEHWGKVYPSCGGKRQSPINIDTRKVRYDPSLPPLTFQGYDV-PPGKNTLTNNGHTVQVSLDDGDpsTISGGPLATRY 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658117674  125 KVGRITFHWGQCNasSDGSEHSLDGIKFPLEMQIYGYEAhKFQSLDSALKDGGRLTALSVLFEVSAEDNENYVAIIDGVK 204
Cdd:pfam00194   80 RLVQFHFHWGSTD--SRGSEHTIDGKRYPAELHIVHYNS-KYKSFDEAAKHPDGLAVLGVFFEVGDENNPYLQPIVSALD 156

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658117674  205 TVTRLGKTAVLEPFSLLGLLPNSTEKYYIYNGSLTTPPCSETVEWIVFRNTVDISDVQLETFCEVMTMQQAGYvmlMDYL 284
Cdd:pfam00194  157 NIKYKGKSVLLPPFDLSDLLPEDLTSYYTYNGSLTTPPCSESVTWIVFKEPISISEEQLEAFRTLLFSDGGEE---PRPL 233

                          250
                   ....*....|....*....
gi 1658117674  285 QNNFREQQLKFVGQVFSSY 303
Cdd:pfam00194  234 VNNFRPTQPLNGRVVFASF 252
Carb_anhydrase smart01057
Eukaryotic-type carbonic anhydrase; Carbonic anhydrases are zinc metalloenzymes which catalyse ...
 41-292 1.72e-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: 267.64  E-value: 1.72e-81
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658117674    41 WSYAGTLNQNNWAKKYPSCNNAK-QSPINIDDDLSQVKMQFQKLKlegFEQETSNTTTIHNDGKTVAINLNDE-YYISGG 118
Cdd:smart01057    1 WGYEGKNGPEHWGKLDPPFCGGKrQSPIDIVTAEAQYDPSLKPLK---LSYDQPTAKRILNNGHTVQVNFDDDgSTLSGG 77

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658117674   119 GLRSRFKVGRITFHWGQCNasSDGSEHSLDGIKFPLEMQIYGYEAHKfqSLDSALKDGGRLTALSVLFEVSAEDNENYVA 198
Cdd:smart01057   78 PLPGRYRLKQFHFHWGGSD--SEGSEHTIDGKRFPLELHLVHYNSKG--SFSEAVSKPGGLAVVAVFFKVGAEENPALQA 153

                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658117674   199 IIDGVKTVTRLGKTAVLEPFSLLGLLPNSTEKYYIYNGSLTTPPCSETVEWIVFRNTVDISDVQLETFCEVMTMQQAgyv 278
Cdd:smart01057  154 ILDHLPLIKYKGQETELTPFDLSSLLPASTRHYYTYNGSLTTPPCSEGVTWIVFKEPITISTEQLEKFRTLLPMEGN--- 230

                           250
                    ....*....|....
gi 1658117674   279 mlmDYLQNNFREQQ 292
Cdd:smart01057  231 ---EPLVNNARPLQ 241
PTPc smart00194
Protein tyrosine phosphatase, catalytic domain;
1054-1311 2.23e-69

Protein tyrosine phosphatase, catalytic domain;


Pssm-ID: 214550 [Multi-domain]  Cd Length: 259  Bit Score: 233.71  E-value: 2.23e-69
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658117674  1054 LEKQFKMITQSNAKQCDYSAALKQCNRDKNRNSSLLPVERSRVHLSTTAGEISDYINASYIMGYQQSNEFIITQNPLPST 1133
Cdd:smart00194    2 LEEEFEKLDRLKPDDESCTVAAFPENRDKNRYKDVLPYDHTRVKLKPPPGEGSDYINASYIDGPNGPKAYIATQGPLPST 81

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658117674  1134 MKDFWKMIWDHSTQVVIALPDGLDL-AEDECIYWPTK-SQPIRFDTFTVTFMGEDHMclsneDMLIVQDFILEATQDDYV 1211
Cdd:smart00194   82 VEDFWRMVWEQKVTVIVMLTELVEKgREKCAQYWPDEeGEPLTYGDITVTLKSVEKV-----DDYTIRTLEVTNTGCSET 156

                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658117674  1212 LEVRQYRAPRWP---NPDGPISnTFELINIIKEESVSRDGPIVVHDKRGGNIAGTFCALMTLLHQLEMESSFDVYWVAKM 1288
Cdd:smart00194  157 RTVTHYHYTNWPdhgVPESPES-ILDLIRAVRKSQSTSTGPIVVHCSAGVGRTGTFIAIDILLQQLEAGKEVDIFEIVKE 235

                           250       260
                    ....*....|....*....|...
gi 1658117674  1289 INLMRPGIFTDIDQYQFLYKVIM 1311
Cdd:smart00194  236 LRSQRPGMVQTEEQYIFLYRAIL 258
Y_phosphatase pfam00102
Protein-tyrosine phosphatase;
1079-1311 9.17e-63

Protein-tyrosine phosphatase;


Pssm-ID: 459674 [Multi-domain]  Cd Length: 234  Bit Score: 213.64  E-value: 9.17e-63
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658117674 1079 NRDKNRNSSLLPVERSRVHLSTTAGEiSDYINASYIMGYQQSNEFIITQNPLPSTMKDFWKMIWDHSTQVVIALPDGLDL 1158
Cdd:pfam00102    1 NLEKNRYKDVLPYDHTRVKLTGDPGP-SDYINASYIDGYKKPKKYIATQGPLPNTVEDFWRMVWEEKVTIIVMLTELEEK 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658117674 1159 AEDEC-IYWPTKS-QPIRFDTFTVTFMGEDhmclSNEDMLIVQDFILEATQDDYVLEVRQYRAPRWPNPDGP--ISNTFE 1234
Cdd:pfam00102   80 GREKCaQYWPEEEgESLEYGDFTVTLKKEK----EDEKDYTVRTLEVSNGGSEETRTVKHFHYTGWPDHGVPesPNSLLD 155

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1658117674 1235 LINIIKEESV-SRDGPIVVHDKRGGNIAGTFCALMTLLHQLEMESSFDVYWVAKMINLMRPGIFTDIDQYQFLYKVIM 1311
Cdd:pfam00102  156 LLRKVRKSSLdGRSGPIVVHCSAGIGRTGTFIAIDIALQQLEAEGEVDIFQIVKELRSQRPGMVQTLEQYIFLYDAIL 233
PHA02738 PHA02738
hypothetical protein; Provisional
 734-1020 1.66e-51

hypothetical protein; Provisional


Pssm-ID: 222923 [Multi-domain]  Cd Length: 320  Bit Score: 184.74  E-value: 1.66e-51
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658117674  734 HEALPIKQFVKHVAELHDSNTFSQEFEEIQACTVDLGITADSsihpENKNKNRYINILAYDHSRVKLSSSSDRngwsADY 813
Cdd:PHA02738     6 FRELKYAEFLALMEKSDCEEVITREHQKVISEKVDGTFNAEK----KNRKLNRYLDAVCFDHSRVILPAERNR----GDY 77

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658117674  814 INANYVDGFTQPKAYIATQGPLKSSMEDFWRMVWEQNASVIVMITNLVEKGRRKCDQYWPLDSQEE--YGSFLVTLRSTK 891
Cdd:PHA02738    78 INANYVDGFEYKKKFICGQAPTRQTCYDFYRMLWMEHVQIIVMLCKKKENGREKCFPYWSDVEQGSirFGKFKITTTQVE 157

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658117674  892 VLAYYTQRTFTLKNtrakkGSQKEQtherTVVQYHYTQWPDMGVPEYTLPVLTFVRKSSQA-------------NLGNMG 958
Cdd:PHA02738   158 THPHYVKSTLLLTD-----GTSATQ----TVTHFNFTAWPDHDVPKNTSEFLNFVLEVRQCqkelaqeslqighNRLQPP 228

                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1658117674  959 PVVVHCSAGVGRTGTYIVLDSMLRQIKEQGTVNILGFLKHIRTQRNYLVQTEEQYIFIHDAL 1020
Cdd:PHA02738   229 PIVVHCNAGLGRTPCYCVVDISISRFDACATVSIPSIVSSIRNQRYYSLFIPFQYFFCYRAV 290
COG5599 COG5599
Protein tyrosine phosphatase [Signal transduction mechanisms];
779-1016 5.19e-43

Protein tyrosine phosphatase [Signal transduction mechanisms];


Pssm-ID: 444335 [Multi-domain]  Cd Length: 282  Bit Score: 158.72  E-value: 5.19e-43
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658117674  779 PENKNKNRYINILAYDHSRVklsSSSDRngwsadYINANYVDGfTQPKAYIATQGPLKSSMEDFWRMVWEQNASVIVMIT 858
Cdd:COG5599     40 INGSPLNRFRDIQPYKETAL---RANLG------YLNANYIQV-IGNHRYIATQYPLEEQLEDFFQMLFDNNTPVLVVLA 109

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658117674  859 NLVE--KGRRKCDQYWPLDsqEEYGSFLVTLRSTKVLAYYTQ---RTFTLKntraKKGSQKEQtheRTVVQYHYTQWPDM 933
Cdd:COG5599    110 SDDEisKPKVKMPVYFRQD--GEYGKYEVSSELTESIQLRDGieaRTYVLT----IKGTGQKK---IEIPVLHVKNWPDH 180

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658117674  934 GVP--EYTLPVLTFVRKSSQANLGNMGPVVVHCSAGVGRTGTYIVLDSMLRQIKE--QGTVNILGFLKHIRTQRNY-LVQ 1008
Cdd:COG5599    181 GAIsaEALKNLADLIDKKEKIKDPDKLLPVVHCRAGVGRTGTLIACLALSKSINAlvQITLSVEEIVIDMRTSRNGgMVQ 260


                   ....*...
gi 1658117674 1009 TEEQYIFI 1016
Cdd:COG5599    261 TSEQLDVL 268
Cah COG3338
Carbonic anhydrase [Inorganic ion transport and metabolism];
36-266 3.71e-33

Carbonic anhydrase [Inorganic ion transport and metabolism];


Pssm-ID: 442567 [Multi-domain]  Cd Length: 247  Bit Score: 129.23  E-value: 3.71e-33
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658117674   36 KEDIDWSYAGTLNQNNWAK---KYPSCNNAK-QSPINIDD----DLSQVKMQFQKLKLEgfeqetsntttIHNDGKTVAI 107
Cdd:COG3338     23 ASAPHWSYEGETGPEHWGElspEFATCATGKnQSPIDIRTaikaDLPPLKFDYKPTPLE-----------IVNNGHTIQV 91

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658117674  108 NLNDEYYISGGGlrSRFKVGRITFHwgqcnassDGSEHSLDGIKFPLEMQIygyeAHKfqsldsalKDGGRLTALSVLFE 187
Cdd:COG3338     92 NVDPGSTLTVDG--KRYELKQFHFH--------TPSEHTINGKSYPMEAHL----VHK--------DADGELAVVGVLFE 149

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658117674  188 VSAEdNENYVAIIDGVKTvtRLGKTAVL-EPFSLLGLLPNSTEkYYIYNGSLTTPPCSETVEWIVFRNTVDISDVQLETF 266
Cdd:COG3338    150 EGAE-NPALAKLWANLPL--EAGEEVALdATIDLNDLLPEDRS-YYRYSGSLTTPPCSEGVLWIVLKQPITVSAEQIEAF 225
PHA02746 PHA02746
protein tyrosine phosphatase; Provisional
 1072-1310 8.45e-26

protein tyrosine phosphatase; Provisional


Pssm-ID: 165113 [Multi-domain]  Cd Length: 323  Bit Score: 109.73  E-value: 8.45e-26
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658117674 1072 SAALKQCNRDKNRNSSLLPVERSRVHLS--------------------TTAGEISDYINASYIMGYQQSNEFIITQNPLP 1131
Cdd:PHA02746    44 NHFLKKENLKKNRFHDIPCWDHSRVVINaheslkmfdvgdsdgkkievTSEDNAENYIHANFVDGFKEANKFICAQGPKE 123

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658117674 1132 STMKDFWKMIWDHSTQVVIALPDGLDLAEDECIYWPT-KSQPIRFDTFTVTFMGEDHMCLSNEDMLIVQDFILEATQddy 1210
Cdd:PHA02746   124 DTSEDFFKLISEHESQVIVSLTDIDDDDEKCFELWTKeEDSELAFGRFVAKILDIIEELSFTKTRLMITDKISDTSR--- 200

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658117674 1211 vlEVRQYRAPRWP---NPDGPiSNTFELINIIKEESV----------SRDGPIVVHDKRGGNIAGTFCALMTLLHQLEME 1277
Cdd:PHA02746   201 --EIHHFWFPDWPdngIPTGM-AEFLELINKVNEEQAelikqadndpQTLGPIVVHCSAGIGRAGTFCAIDNALEQLEKE 277

                          250       260       270
                   ....*....|....*....|....*....|...
gi 1658117674 1278 SSFDVYWVAKMINLMRPGIFTDIDQYQFLYKVI 1310
Cdd:PHA02746   278 KEVCLGEIVLKIRKQRHSSVFLPEQYAFCYKAL 310
fn3 pfam00041
Fibronectin type III domain;
316-398 2.06e-11

Fibronectin type III domain;


Pssm-ID: 394996 [Multi-domain]  Cd Length: 85  Bit Score: 61.28  E-value: 2.06e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658117674  316 SEPENVEADPYNYTSLLVTWERPRAVYDVgIERYLVSYQPVGDEDlPKNEYLTDGDQDvGAIIQDLSANTSYVVQVVAVC 395
Cdd:pfam00041    1 SAPSNLTVTDVTSTSLTVSWTPPPDGNGP-ITGYEVEYRPKNSGE-PWNEITVPGTTT-SVTLTGLKPGTEYEVRVQAVN 77


                   ...
gi 1658117674  396 ING 398
Cdd:pfam00041   78 GGG 80
FN3 smart00060
Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, ...
 316-398 8.28e-09

Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, fibronectin. The tenth fibronectin type III repeat contains a RGD cell recognition sequence in a flexible loop between 2 strands. Type III modules are present in both extracellular and intracellular proteins.


Pssm-ID: 214495 [Multi-domain]  Cd Length: 83  Bit Score: 53.77  E-value: 8.28e-09
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658117674   316 SEPENVEADPYNYTSLLVTWERPRavyDVGIERYLVSYQPVGDEDLPKNEYLTDGDQDVGAIIQDLSANTSYVVQVVAVC 395
Cdd:smart00060    2 SPPSNLRVTDVTSTSVTLSWEPPP---DDGITGYIVGYRVEYREEGSEWKEVNVTPSSTSYTLTGLKPGTEYEFRVRAVN 78


                    ...
gi 1658117674   396 ING 398
Cdd:smart00060   79 GAG 81
PLN02179 PLN02179
carbonic anhydrase
 52-263 2.27e-08

carbonic anhydrase


Pssm-ID: 177835  Cd Length: 235  Bit Score: 56.53  E-value: 2.27e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658117674   52 WAKKYPS---CNNAK-QSPINIDDDLSQVkMQFQKLKlegfEQETSNTTTIHNDGKTVAINLNDEyyisggglrsrfkVG 127
Cdd:PLN02179    50 WGKLNPQwkvCSTGKyQSPIDLTDERVSL-IHDQALS----RHYKPAPAVIQSRGHDVMVSWKGD-------------AG 111

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658117674  128 RITFHWG-----QCNASSDgSEHSLDGIKFPLEMQIYGYEAHkfqsldsalkdgGRLTALSVLFEVsAEDNENYVAIIDG 202
Cdd:PLN02179   112 KITIHQTdyklvQCHWHSP-SEHTINGTSYDLELHMVHTSAS------------GKTAVVGVLYKL-GEPDEFLTKLLNG 177

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1658117674  203 VKTVtrlGKTAVLepfslLGLL-PN----STEKYYIYNGSLTTPPCSETVEWIVFRNTVDISDVQL 263
Cdd:PLN02179   178 IKGV---GKKEIN-----LGIVdPRdirfETNNFYRYIGSLTIPPCTEGVIWTVVKRVVWFFDFNV 235
FN3 cd00063
Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein ...
 316-398 5.64e-08

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


Pssm-ID: 238020 [Multi-domain]  Cd Length: 93  Bit Score: 51.73  E-value: 5.64e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658117674  316 SEPENVEADPYNYTSLLVTWERPRAvYDVGIERYLVSYQPVGDEDLpkNEYLTDGDQDVGAIIQDLSANTSYVVQVVAVC 395
Cdd:cd00063      2 SPPTNLRVTDVTSTSVTLSWTPPED-DGGPITGYVVEYREKGSGDW--KEVEVTPGSETSYTLTGLKPGTEYEFRVRAVN 78


                   ...
gi 1658117674  396 ING 398
Cdd:cd00063     79 GGG 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 ...
 755-1025 1.29e-161

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: 484.92  E-value: 1.29e-161
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658117674  755 FSQEFEEIQACTVDLGITADSSIHPENKNKNRYINILAYDHSRVKLSSSSDRNGWSADYINANYVDGFTQPKAYIATQGP 834
Cdd:cd17667      1 FSEDFEEVQRCTADMNITAEHSNHPDNKHKNRYINILAYDHSRVKLRPLPGKDSKHSDYINANYVDGYNKAKAYIATQGP 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658117674  835 LKSSMEDFWRMVWEQNASVIVMITNLVEKGRRKCDQYWPLDSQEEYGSFLVTLRSTKVLAYYTQRTFTLKNTRAKKGSQ- 913
Cdd:cd17667     81 LKSTFEDFWRMIWEQNTGIIVMITNLVEKGRRKCDQYWPTENSEEYGNIIVTLKSTKIHACYTVRRFSIRNTKVKKGQKg 160

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658117674  914 --KEQTHERTVVQYHYTQWPDMGVPEYTLPVLTFVRKSSQANLGNMGPVVVHCSAGVGRTGTYIVLDSMLRQIKEQGTVN 991
Cdd:cd17667    161 npKGRQNERTVIQYHYTQWPDMGVPEYALPVLTFVRRSSAARTPEMGPVLVHCSAGVGRTGTYIVIDSMLQQIKDKSTVN 240

                          250       260       270
                   ....*....|....*....|....*....|....
gi 1658117674  992 ILGFLKHIRTQRNYLVQTEEQYIFIHDALVEAIL 1025
Cdd:cd17667    241 VLGFLKHIRTQRNYLVQTEEQYIFIHDALLEAIL 274
R-PTPc-Z-1 cd17668
catalytic domain of receptor-type tyrosine-protein phosphatase Z, repeat 1; Receptor-type ...
 813-1021 1.06e-138

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: 421.69  E-value: 1.06e-138
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658117674  813 YINANYVDGFTQPKAYIATQGPLKSSMEDFWRMVWEQNASVIVMITNLVEKGRRKCDQYWPLDSQEEYGSFLVTLRSTKV 892
Cdd:cd17668      1 YINANYVDGYNKPKAYIAAQGPLKSTAEDFWRMIWEHNVEVIVMITNLVEKGRRKCDQYWPADGSEEYGNFLVTQKSVQV 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658117674  893 LAYYTQRTFTLKNTRAKKGSQKEQTHERTVVQYHYTQWPDMGVPEYTLPVLTFVRKSSQANLGNMGPVVVHCSAGVGRTG 972
Cdd:cd17668     81 LAYYTVRNFTLRNTKIKKGSQKGRPSGRVVTQYHYTQWPDMGVPEYTLPVLTFVRKASYAKRHAVGPVVVHCSAGVGRTG 160

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*....
gi 1658117674  973 TYIVLDSMLRQIKEQGTVNILGFLKHIRTQRNYLVQTEEQYIFIHDALV 1021
Cdd:cd17668    161 TYIVLDSMLQQIQHEGTVNIFGFLKHIRSQRNYLVQTEEQYVFIHDALV 209
R5-PTPc-1 cd14549
catalytic domain of R5 subfamily receptor-type tyrosine-protein phosphatases, repeat 1; The R5 ...
 813-1018 1.41e-137

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: 418.68  E-value: 1.41e-137
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658117674  813 YINANYVDGFTQPKAYIATQGPLKSSMEDFWRMVWEQNASVIVMITNLVEKGRRKCDQYWPLDSQEEYGSFLVTLRSTKV 892
Cdd:cd14549      1 YINANYVDGYNKARAYIATQGPLPSTFDDFWRMVWEQNSAIIVMITNLVERGRRKCDQYWPKEGTETYGNIQVTLLSTEV 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658117674  893 LAYYTQRTFTLKNTRAKKGsqKEQTHERTVVQYHYTQWPDMGVPEYTLPVLTFVRKSSQANLGNMGPVVVHCSAGVGRTG 972
Cdd:cd14549     81 LATYTVRTFSLKNLKLKKV--KGRSSERVVYQYHYTQWPDHGVPDYTLPVLSFVRKSSAANPPGAGPIVVHCSAGVGRTG 158

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*.
gi 1658117674  973 TYIVLDSMLRQIKEQGTVNILGFLKHIRTQRNYLVQTEEQYIFIHD 1018
Cdd:cd14549    159 TYIVIDSMLQQIQDKGTVNVFGFLKHIRTQRNYLVQTEEQYIFIHD 204
R5-PTP-2 cd14550
PTP-like domain of R5 subfamily receptor-type tyrosine-protein phosphatases, repeat 2; The R5 ...
 1108-1308 3.31e-122

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: 377.43  E-value: 3.31e-122
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658117674 1108 YINASYIMGYQQSNEFIITQNPLPSTMKDFWKMIWDHSTQVVIALPDGlDLAEDECIYWPTKSQPIRFDTFTVTFMGEDH 1187
Cdd:cd14550      1 YINASYLQGYRRSNEFIITQHPLEHTIKDFWQMIWDHNSQTIVMLTDN-ELNEDEPIYWPTKEKPLECETFKVTLSGEDH 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658117674 1188 MCLSNEDMLIVQDFILEATQDDYVLEVRQYRAPRWPNPDGPISNTFELINIIKEESVSRDGPIVVHDKRGGNIAGTFCAL 1267
Cdd:cd14550     80 SCLSNEIRLIVRDFILESTQDDYVLEVRQFQCPSWPNPCSPIHTVFELINTVQEWAQQRDGPIVVHDRYGGVQAATFCAL 159

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|.
gi 1658117674 1268 MTLLHQLEMESSFDVYWVAKMINLMRPGIFTDIDQYQFLYK 1308
Cdd:cd14550    160 TTLHQQLEHESSVDVYQVAKLYHLMRPGVFTSKEDYQFLYK 200
R-PTP-Z-2 cd17669
catalytic domain of receptor-type tyrosine-protein phosphatase Z, repeat 2; Receptor-type ...
 1108-1311 2.33e-120

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: 372.79  E-value: 2.33e-120
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658117674 1108 YINASYIMGYQQSNEFIITQNPLPSTMKDFWKMIWDHSTQVVIALPDGLDLAEDECIYWPTKSQPIRFDTFTVTFMGEDH 1187
Cdd:cd17669      1 YINASYIMGYYQSNEFIITQHPLLHTIKDFWRMIWDHNAQLIVMLPDGQNMAEDEFVYWPNKDEPINCETFKVTLIAEEH 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658117674 1188 MCLSNEDMLIVQDFILEATQDDYVLEVRQYRAPRWPNPDGPISNTFELINIIKEESVSRDGPIVVHDKRGGNIAGTFCAL 1267
Cdd:cd17669     81 KCLSNEEKLIIQDFILEATQDDYVLEVRHFQCPKWPNPDSPISKTFELISIIKEEAANRDGPMIVHDEHGGVTAGTFCAL 160

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....
gi 1658117674 1268 MTLLHQLEMESSFDVYWVAKMINLMRPGIFTDIDQYQFLYKVIM 1311
Cdd:cd17669    161 TTLMHQLEKENSVDVYQVAKMINLMRPGVFTDIEQYQFLYKAIL 204
PTPc smart00194
Protein tyrosine phosphatase, catalytic domain;
755-1022 6.92e-115

Protein tyrosine phosphatase, catalytic domain;


Pssm-ID: 214550 [Multi-domain]  Cd Length: 259  Bit Score: 360.05  E-value: 6.92e-115
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658117674   755 FSQEFEEIQACTVDLgITADSSIHPENKNKNRYINILAYDHSRVKLSsssDRNGWSADYINANYVDGFTQPKAYIATQGP 834
Cdd:smart00194    2 LEEEFEKLDRLKPDD-ESCTVAAFPENRDKNRYKDVLPYDHTRVKLK---PPPGEGSDYINASYIDGPNGPKAYIATQGP 77

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658117674   835 LKSSMEDFWRMVWEQNASVIVMITNLVEKGRRKCDQYWPLDSQE--EYGSFLVTLRSTKVLAYYTQRTFTLKNTrakkgs 912
Cdd:smart00194   78 LPSTVEDFWRMVWEQKVTVIVMLTELVEKGREKCAQYWPDEEGEplTYGDITVTLKSVEKVDDYTIRTLEVTNT------ 151

                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658117674   913 qkEQTHERTVVQYHYTQWPDMGVPEYTLPVLTFVRKSSQANLGNMGPVVVHCSAGVGRTGTYIVLDSMLRQIKEQGTVNI 992
Cdd:smart00194  152 --GCSETRTVTHYHYTNWPDHGVPESPESILDLIRAVRKSQSTSTGPIVVHCSAGVGRTGTFIAIDILLQQLEAGKEVDI 229

                           250       260       270
                    ....*....|....*....|....*....|
gi 1658117674   993 LGFLKHIRTQRNYLVQTEEQYIFIHDALVE 1022
Cdd:smart00194  230 FEIVKELRSQRPGMVQTEEQYIFLYRAILE 259
Y_phosphatase pfam00102
Protein-tyrosine phosphatase;
781-1022 8.57e-110

Protein-tyrosine phosphatase;


Pssm-ID: 459674 [Multi-domain]  Cd Length: 234  Bit Score: 345.38  E-value: 8.57e-110
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658117674  781 NKNKNRYINILAYDHSRVKLSSSSDRNgwsaDYINANYVDGFTQPKAYIATQGPLKSSMEDFWRMVWEQNASVIVMITNL 860
Cdd:pfam00102    1 NLEKNRYKDVLPYDHTRVKLTGDPGPS----DYINASYIDGYKKPKKYIATQGPLPNTVEDFWRMVWEEKVTIIVMLTEL 76

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658117674  861 VEKGRRKCDQYWPLDSQE--EYGSFLVTLRSTK-VLAYYTQRTFTLKNTRAKkgsqkeqtHERTVVQYHYTQWPDMGVPE 937
Cdd:pfam00102   77 EEKGREKCAQYWPEEEGEslEYGDFTVTLKKEKeDEKDYTVRTLEVSNGGSE--------ETRTVKHFHYTGWPDHGVPE 148

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658117674  938 YTLPVLTFVRK-SSQANLGNMGPVVVHCSAGVGRTGTYIVLDSMLRQIKEQGTVNILGFLKHIRTQRNYLVQTEEQYIFI 1016
Cdd:pfam00102  149 SPNSLLDLLRKvRKSSLDGRSGPIVVHCSAGIGRTGTFIAIDIALQQLEAEGEVDIFQIVKELRSQRPGMVQTLEQYIFL 228


                   ....*.
gi 1658117674 1017 HDALVE 1022
Cdd:pfam00102  229 YDAILE 234
R-PTP-G-2 cd17670
PTP-like domain of receptor-type tyrosine-protein phosphatase G, repeat 2; Receptor-type ...
 1108-1312 9.32e-110

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: 343.97  E-value: 9.32e-110
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658117674 1108 YINASYIMGYQQSNEFIITQNPLPSTMKDFWKMIWDHSTQVVIALPDGLDLAEDECIYWPTKSQPIRFDTFTVTFMGEDH 1187
Cdd:cd17670      1 YINASYIMGYYRSNEFIITQHPLPHTTKDFWRMIWDHNAQIIVMLPDNQGLAEDEFVYWPSREESMNCEAFTVTLISKDR 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658117674 1188 MCLSNEDMLIVQDFILEATQDDYVLEVRQYRAPRWPNPDGPISNTFELINIIKEESVSRDGPIVVHDKRGGNIAGTFCAL 1267
Cdd:cd17670     81 LCLSNEEQIIIHDFILEATQDDYVLEVRHFQCPKWPNPDAPISSTFELINVIKEEALTRDGPTIVHDEFGAVSAGTLCAL 160

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*
gi 1658117674 1268 MTLLHQLEMESSFDVYWVAKMINLMRPGIFTDIDQYQFLYKVIMS 1312
Cdd:cd17670    161 TTLSQQLENENAVDVYQVAKMINLMRPGVFTDIEQYQFLYKAMLS 205
R-PTPc-LAR-1 cd14553
catalytic domain of LAR family receptor-type tyrosine-protein phosphatases, repeat 1; The LAR ...
 781-1026 1.40e-109

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: 344.77  E-value: 1.40e-109
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658117674  781 NKNKNRYINILAYDHSRVKLSSSSDRNGwsADYINANYVDGFTQPKAYIATQGPLKSSMEDFWRMVWEQNASVIVMITNL 860
Cdd:cd14553      3 NKPKNRYANVIAYDHSRVILQPIEGVPG--SDYINANYCDGYRKQNAYIATQGPLPETFGDFWRMVWEQRSATIVMMTKL 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658117674  861 VEKGRRKCDQYWPLDSQEEYGSFLVTLRSTKVLAYYTQRTFTLKntraKKGSqkeqTHERTVVQYHYTQWPDMGVPEYTL 940
Cdd:cd14553     81 EERSRVKCDQYWPTRGTETYGLIQVTLLDTVELATYTVRTFALH----KNGS----SEKREVRQFQFTAWPDHGVPEHPT 152

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658117674  941 PVLTFVRKSSQANLGNMGPVVVHCSAGVGRTGTYIVLDSMLRQIKEQGTVNILGFLKHIRTQRNYLVQTEEQYIFIHDAL 1020
Cdd:cd14553    153 PFLAFLRRVKACNPPDAGPIVVHCSAGVGRTGCFIVIDSMLERIKHEKTVDIYGHVTCLRAQRNYMVQTEDQYIFIHDAL 232


                   ....*.
gi 1658117674 1021 VEAILS 1026
Cdd:cd14553    233 LEAVTC 238
alpha_CARP_receptor_like cd03122
Carbonic anhydrase alpha related protein, receptor_like subfamily. Carbonic anhydrase related ...
 48-301 3.20e-106

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: 336.25  E-value: 3.20e-106
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658117674   48 NQNNWAKKYPSCNNA-KQSPINIDDDlSQVK-MQFQKLKLEGFEQETSNTTtIHNDGKTVAINLND---EYYISGGGLRS 122
Cdd:cd03122      1 NPKHWAKKYPACGEGrQQSPIDIVED-TQVQrQGLQPLHFDGYEELTASTT-LENTGKTVILRLEGnssDPFVSGGPLLG 78

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658117674  123 RFKVGRITFHWGQCNasSDGSEHSLDGIKFPLEMQIYGYeAHKFQSLDSALKDGGRLTALSVLFEVSAEDNENYVAIIDG 202
Cdd:cd03122     79 RYKFSEITFHWGTCN--SDGSEHSIDGHKFPLEMQILHR-NTDFFDSFEAIKSPGGVLALAYLFELSHEDNPFLDPIIEG 155

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658117674  203 VKTVTRLGKTAVLEPFSLLGLLPNSTEKYYIYNGSLTTPPCSETVEWIVFRNTVDISDVQLETFCEVMTMQQAGyVMLMD 282
Cdd:cd03122    156 LRNVSRPGKEVELPPFPLSDLLPPFTDKYYSYEGSLTTPPCSETVEWIVFREPVPISSRQLEAFRELLTRRQDG-VMSGD 234

                          250
                   ....*....|....*....
gi 1658117674  283 YLQNNFREQQLKFVGQVFS 301
Cdd:cd03122    235 YLPNNGRPQQPLGSRTVFS 253
R-PTPc-F-1 cd14626
catalytic domain of receptor-type tyrosine-protein phosphatase F, repeat 1; Receptor-type ...
 750-1024 5.74e-95

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: 306.58  E-value: 5.74e-95
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658117674  750 HDSNTFSQEFEEIqactvDLG--ITADSSIHPENKNKNRYINILAYDHSRVKLSSSSDRNGwsADYINANYVDGFTQPKA 827
Cdd:cd14626     13 NDGLKFSQEYESI-----DPGqqFTWENSNLEVNKPKNRYANVIAYDHSRVILTSVDGVPG--SDYINANYIDGYRKQNA 85

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658117674  828 YIATQGPLKSSMEDFWRMVWEQNASVIVMITNLVEKGRRKCDQYWPLDSQEEYGSFLVTLRSTKVLAYYTQRTFTLKntr 907
Cdd:cd14626     86 YIATQGPLPETLSDFWRMVWEQRTATIVMMTRLEEKSRVKCDQYWPIRGTETYGMIQVTLLDTVELATYSVRTFALY--- 162

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658117674  908 aKKGSqkeqTHERTVVQYHYTQWPDMGVPEYTLPVLTFVRKSSQANLGNMGPVVVHCSAGVGRTGTYIVLDSMLRQIKEQ 987
Cdd:cd14626    163 -KNGS----SEKREVRQFQFMAWPDHGVPEYPTPILAFLRRVKACNPPDAGPMVVHCSAGVGRTGCFIVIDAMLERMKHE 237

                          250       260       270
                   ....*....|....*....|....*....|....*..
gi 1658117674  988 GTVNILGFLKHIRTQRNYLVQTEEQYIFIHDALVEAI 1024
Cdd:cd14626    238 KTVDIYGHVTCMRSQRNYMVQTEDQYIFIHEALLEAA 274
PTPc cd00047
catalytic domain of protein tyrosine phosphatases; Protein tyrosine phosphatases (PTP, EC 3.1. ...
 813-1018 1.50e-93

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: 299.20  E-value: 1.50e-93
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658117674  813 YINANYVDGFTQPKAYIATQGPLKSSMEDFWRMVWEQNASVIVMITNLVEKGRRKCDQYWPLDSQE--EYGSFLVTLRST 890
Cdd:cd00047      1 YINASYIDGYRGPKEYIATQGPLPNTVEDFWRMVWEQKVSVIVMLTNLVEKGREKCERYWPEEGGKplEYGDITVTLVSE 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658117674  891 KVLAYYTQRTFTLKNTRAKKgsqkeqthERTVVQYHYTQWPDMGVPEYTLPVLTFVRKSSQANLGNMGPVVVHCSAGVGR 970
Cdd:cd00047     81 EELSDYTIRTLELSPKGCSE--------SREVTHLHYTGWPDHGVPSSPEDLLALVRRVRKEARKPNGPIVVHCSAGVGR 152

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*...
gi 1658117674  971 TGTYIVLDSMLRQIKEQGTVNILGFLKHIRTQRNYLVQTEEQYIFIHD 1018
Cdd:cd00047    153 TGTFIAIDILLERLEAEGEVDVFEIVKALRKQRPGMVQTLEQYEFIYE 200
R3-PTPc cd14548
catalytic domain of R3 subfamily receptor-type tyrosine-protein phosphatases and similar ...
 786-1017 9.58e-90

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: 289.64  E-value: 9.58e-90
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658117674  786 RYINILAYDHSRVKLSSSSDRNGwsADYINANYVDGFTQPKAYIATQGPLKSSMEDFWRMVWEQNASVIVMITNLVEKGR 865
Cdd:cd14548      1 RYTNILPYDHSRVKLIPINEEEG--SDYINANYIPGYNSPREFIATQGPLPGTKDDFWRMVWEQNSHTIVMLTQCMEKGR 78

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658117674  866 RKCDQYWPLDSQE-EYGSFLVTLRSTKVLAYYTQRTFTLKNTRAkkgsqkeqthERTVVQYHYTQWPDMGVPEYTLPVLT 944
Cdd:cd14548     79 VKCDHYWPFDQDPvYYGDITVTMLSESVLPDWTIREFKLERGDE----------VRSVRQFHFTAWPDHGVPEAPDSLLR 148

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1658117674  945 FVRKSSQANLGNMGPVVVHCSAGVGRTGTYIVLDSMLRQIKEQGTVNILGFLKHIRTQRNYLVQTEEQYIFIH 1017
Cdd:cd14548    149 FVRLVRDYIKQEKGPTIVHCSAGVGRTGTFIALDRLLQQIESEDYVDIFGIVYDLRKHRPLMVQTEAQYIFLH 221
PTPc-N9 cd14543
catalytic domain of tyrosine-protein phosphatase non-receptor type 9; Tyrosine-protein ...
 757-1017 1.21e-88

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: 288.49  E-value: 1.21e-88
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658117674  757 QEFEEIQACTVdlGITADSSIHPENKNKNRYINILAYDHSRVKLSS-SSDRNgwsADYINANYVDGFTQPKAYIATQGPL 835
Cdd:cd14543      7 EEYEDIRREPP--AGTFLCSLAPANQEKNRYGDVLCLDQSRVKLPKrNGDER---TDYINANFMDGYKQKNAYIATQGPL 81

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658117674  836 KSSMEDFWRMVWEQNASVIVMITNLVEKGRRKCDQYWPLD--SQEEYGSFLVTLRSTKVLAYYTQRTFTLKNTrakkgsq 913
Cdd:cd14543     82 PKTYSDFWRMVWEQKVLVIVMTTRVVERGRVKCGQYWPLEegSSLRYGDLTVTNLSVENKEHYKKTTLEIHNT------- 154

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658117674  914 keQTHE-RTVVQYHYTQWPDMGVPEYTLPVLTF---VRKSSQANLGNMG----------PVVVHCSAGVGRTGTYIVLDS 979
Cdd:cd14543    155 --ETDEsRQVTHFQFTSWPDFGVPSSAAALLDFlgeVRQQQALAVKAMGdrwkghppgpPIVVHCSAGIGRTGTFCTLDI 232

                          250       260       270
                   ....*....|....*....|....*....|....*...
gi 1658117674  980 MLRQIKEQGTVNILGFLKHIRTQRNYLVQTEEQYIFIH 1017
Cdd:cd14543    233 CLSQLEDVGTLNVMQTVRRMRTQRAFSIQTPDQYYFCY 270
R-PTPc-S-1 cd14625
catalytic domain of receptor-type tyrosine-protein phosphatase S, repeat 1; Receptor-type ...
 734-1024 3.06e-88

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: 288.14  E-value: 3.06e-88
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658117674  734 HEALPIKQFVKHVAEL--HDSNTFSQEFEEIqactvDLG--ITADSSIHPENKNKNRYINILAYDHSRVKLSSSSDRNGw 809
Cdd:cd14625      1 HPPIPISELAEHTERLkaNDNLKLSQEYESI-----DPGqqFTWEHSNLEVNKPKNRYANVIAYDHSRVILQPIEGIMG- 74

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658117674  810 sADYINANYVDGFTQPKAYIATQGPLKSSMEDFWRMVWEQNASVIVMITNLVEKGRRKCDQYWPLDSQEEYGSFLVTLRS 889
Cdd:cd14625     75 -SDYINANYIDGYRKQNAYIATQGPLPETFGDFWRMVWEQRSATVVMMTKLEEKSRIKCDQYWPSRGTETYGMIQVTLLD 153

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658117674  890 TKVLAYYTQRTFTLKntraKKGSqkeqTHERTVVQYHYTQWPDMGVPEYTLPVLTFVRKSSQANLGNMGPVVVHCSAGVG 969
Cdd:cd14625    154 TIELATFCVRTFSLH----KNGS----SEKREVRQFQFTAWPDHGVPEYPTPFLAFLRRVKTCNPPDAGPIVVHCSAGVG 225

                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1658117674  970 RTGTYIVLDSMLRQIKEQGTVNILGFLKHIRTQRNYLVQTEEQYIFIHDALVEAI 1024
Cdd:cd14625    226 RTGCFIVIDAMLERIKHEKTVDIYGHVTLMRSQRNYMVQTEDQYSFIHDALLEAV 280
R-PTPc-D-1 cd14624
catalytic domain of receptor-type tyrosine-protein phosphatase D, repeat 1; Receptor-type ...
 734-1024 1.98e-87

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: 285.86  E-value: 1.98e-87
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658117674  734 HEALPIKQFVKHVAEL--HDSNTFSQEFEeiqacTVDLG--ITADSSIHPENKNKNRYINILAYDHSRVKLSSSSDRNGw 809
Cdd:cd14624      1 HPPIPILELADHIERLkaNDNLKFSQEYE-----SIDPGqqFTWEHSNLEVNKPKNRYANVIAYDHSRVLLSAIEGIPG- 74

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658117674  810 sADYINANYVDGFTQPKAYIATQGPLKSSMEDFWRMVWEQNASVIVMITNLVEKGRRKCDQYWPLDSQEEYGSFLVTLRS 889
Cdd:cd14624     75 -SDYINANYIDGYRKQNAYIATQGALPETFGDFWRMIWEQRSATVVMMTKLEERSRVKCDQYWPSRGTETYGLIQVTLLD 153

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658117674  890 TKVLAYYTQRTFTLkntrAKKGSqkeqTHERTVVQYHYTQWPDMGVPEYTLPVLTFVRKSSQANLGNMGPVVVHCSAGVG 969
Cdd:cd14624    154 TVELATYCVRTFAL----YKNGS----SEKREVRQFQFTAWPDHGVPEHPTPFLAFLRRVKTCNPPDAGPMVVHCSAGVG 225

                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1658117674  970 RTGTYIVLDSMLRQIKEQGTVNILGFLKHIRTQRNYLVQTEEQYIFIHDALVEAI 1024
Cdd:cd14624    226 RTGCFIVIDAMLERIKHEKTVDIYGHVTLMRAQRNYMVQTEDQYIFIHDALLEAV 280
Carb_anhydrase pfam00194
Eukaryotic-type carbonic anhydrase;
47-303 6.35e-86

Eukaryotic-type carbonic anhydrase;


Pssm-ID: 459707 [Multi-domain]  Cd Length: 252  Bit Score: 280.31  E-value: 6.35e-86
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658117674   47 LNQNNWAKKYPSCNNAKQSPINIDDDLSQVKMQFQKLKLEGFEQeTSNTTTIHNDGKTVAINLNDEY--YISGGGLRSRF 124
Cdd:pfam00194    1 LGPEHWGKVYPSCGGKRQSPINIDTRKVRYDPSLPPLTFQGYDV-PPGKNTLTNNGHTVQVSLDDGDpsTISGGPLATRY 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658117674  125 KVGRITFHWGQCNasSDGSEHSLDGIKFPLEMQIYGYEAhKFQSLDSALKDGGRLTALSVLFEVSAEDNENYVAIIDGVK 204
Cdd:pfam00194   80 RLVQFHFHWGSTD--SRGSEHTIDGKRYPAELHIVHYNS-KYKSFDEAAKHPDGLAVLGVFFEVGDENNPYLQPIVSALD 156

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658117674  205 TVTRLGKTAVLEPFSLLGLLPNSTEKYYIYNGSLTTPPCSETVEWIVFRNTVDISDVQLETFCEVMTMQQAGYvmlMDYL 284
Cdd:pfam00194  157 NIKYKGKSVLLPPFDLSDLLPEDLTSYYTYNGSLTTPPCSESVTWIVFKEPISISEEQLEAFRTLLFSDGGEE---PRPL 233

                          250
                   ....*....|....*....
gi 1658117674  285 QNNFREQQLKFVGQVFSSY 303
Cdd:pfam00194  234 VNNFRPTQPLNGRVVFASF 252
R-PTPc-T-1 cd14630
catalytic domain of receptor-type tyrosine-protein phosphatase T, repeat 1; Receptor-type ...
 780-1025 3.62e-82

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: 269.20  E-value: 3.62e-82
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658117674  780 ENKNKNRYINILAYDHSRVKLSSSSDRNgwSADYINANYVDGFTQPKAYIATQGPLKSSMEDFWRMVWEQNASVIVMITN 859
Cdd:cd14630      2 ENRNKNRYGNIISYDHSRVRLQLLDGDP--HSDYINANYIDGYHRPRHYIATQGPMQETVKDFWRMIWQENSASVVMVTN 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658117674  860 LVEKGRRKCDQYWPlDSQEEYGSFLVTLRSTKVLAYYTQRTFTLkntrakkgsQKEQTHE-RTVVQYHYTQWPDMGVPEY 938
Cdd:cd14630     80 LVEVGRVKCVRYWP-DDTEVYGDIKVTLIETEPLAEYVIRTFTV---------QKKGYHEiREIRQFHFTSWPDHGVPCY 149

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658117674  939 TLPVLTFVRKSSQANLGNMGPVVVHCSAGVGRTGTYIVLDSMLRQIKEQGTVNILGFLKHIRTQRNYLVQTEEQYIFIHD 1018
Cdd:cd14630    150 ATGLLGFVRQVKFLNPPDAGPIVVHCSAGAGRTGCFIAIDIMLDMAENEGVVDIFNCVRELRAQRVNMVQTEEQYVFVHD 229


                   ....*..
gi 1658117674 1019 ALVEAIL 1025
Cdd:cd14630    230 AILEACL 236
Carb_anhydrase smart01057
Eukaryotic-type carbonic anhydrase; Carbonic anhydrases are zinc metalloenzymes which catalyse ...
 41-292 1.72e-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: 267.64  E-value: 1.72e-81
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658117674    41 WSYAGTLNQNNWAKKYPSCNNAK-QSPINIDDDLSQVKMQFQKLKlegFEQETSNTTTIHNDGKTVAINLNDE-YYISGG 118
Cdd:smart01057    1 WGYEGKNGPEHWGKLDPPFCGGKrQSPIDIVTAEAQYDPSLKPLK---LSYDQPTAKRILNNGHTVQVNFDDDgSTLSGG 77

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658117674   119 GLRSRFKVGRITFHWGQCNasSDGSEHSLDGIKFPLEMQIYGYEAHKfqSLDSALKDGGRLTALSVLFEVSAEDNENYVA 198
Cdd:smart01057   78 PLPGRYRLKQFHFHWGGSD--SEGSEHTIDGKRFPLELHLVHYNSKG--SFSEAVSKPGGLAVVAVFFKVGAEENPALQA 153

                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658117674   199 IIDGVKTVTRLGKTAVLEPFSLLGLLPNSTEKYYIYNGSLTTPPCSETVEWIVFRNTVDISDVQLETFCEVMTMQQAgyv 278
Cdd:smart01057  154 ILDHLPLIKYKGQETELTPFDLSSLLPASTRHYYTYNGSLTTPPCSEGVTWIVFKEPITISTEQLEKFRTLLPMEGN--- 230

                           250
                    ....*....|....
gi 1658117674   279 mlmDYLQNNFREQQ 292
Cdd:smart01057  231 ---EPLVNNARPLQ 241
R-PTPc-J cd14615
catalytic domain of receptor-type tyrosine-protein phosphatase J; Receptor-type ...
 785-1016 4.35e-77

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: 254.36  E-value: 4.35e-77
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658117674  785 NRYINILAYDHSRVKLSSSSDRngwSADYINANYVDGFTQPKAYIATQGPLKSSMEDFWRMVWEQNASVIVMITNLVEKG 864
Cdd:cd14615      1 NRYNNVLPYDISRVKLSVQSHS---TDDYINANYMPGYNSKKEFIAAQGPLPNTVKDFWRMVWEKNVYAIVMLTKCVEQG 77

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658117674  865 RRKCDQYWPLDSQEEYGSFLVTLRSTKVLAYYTQRTFTLKNTrakkgsqkeQTHE-RTVVQYHYTQWPDMGVPEYTLPVL 943
Cdd:cd14615     78 RTKCEEYWPSKQKKDYGDITVTMTSEIVLPEWTIRDFTVKNA---------QTNEsRTVRHFHFTSWPDHGVPETTDLLI 148

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1658117674  944 TF---VRKSSQANLGNmGPVVVHCSAGVGRTGTYIVLDSMLRQIKEQGTVNILGFLKHIRTQRNYLVQTEEQYIFI 1016
Cdd:cd14615    149 NFrhlVREYMKQNPPN-SPILVHCSAGVGRTGTFIAIDRLIYQIENENVVDVYGIVYDLRMHRPLMVQTEDQYVFL 223
R-PTPc-M-1 cd14633
catalytic domain of receptor-type tyrosine-protein phosphatase M, repeat 1; Receptor-type ...
 774-1025 1.28e-76

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: 254.97  E-value: 1.28e-76
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658117674  774 DSSIHPENKNKNRYINILAYDHSRVKLSSSSDRNGwsADYINANYVDGFTQPKAYIATQGPLKSSMEDFWRMVWEQNASV 853
Cdd:cd14633     33 DSAKKDENRMKNRYGNIIAYDHSRVRLQPIEGETS--SDYINGNYIDGYHRPNHYIATQGPMQETIYDFWRMVWHENTAS 110

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658117674  854 IVMITNLVEKGRRKCDQYWPlDSQEEYGSFLVTLRSTKVLAYYTQRTFTLkntrakkgsQKEQTHE-RTVVQYHYTQWPD 932
Cdd:cd14633    111 IIMVTNLVEVGRVKCCKYWP-DDTEIYKDIKVTLIETELLAEYVIRTFAV---------EKRGVHEiREIRQFHFTGWPD 180

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658117674  933 MGVPEYTLPVLTFVRKSSQANLGNMGPVVVHCSAGVGRTGTYIVLDSMLRQIKEQGTVNILGFLKHIRTQRNYLVQTEEQ 1012
Cdd:cd14633    181 HGVPYHATGLLGFVRQVKSKSPPNAGPLVVHCSAGAGRTGCFIVIDIMLDMAEREGVVDIYNCVRELRSRRVNMVQTEEQ 260

                          250
                   ....*....|...
gi 1658117674 1013 YIFIHDALVEAIL 1025
Cdd:cd14633    261 YVFIHDAILEACL 273
R-PTPc-typeIIb-1 cd14555
catalytic domain of type IIb (or R2B) subfamily receptor-type tyrosine-protein phosphatases, ...
 813-1025 3.97e-76

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: 250.60  E-value: 3.97e-76
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658117674  813 YINANYVDGFTQPKAYIATQGPLKSSMEDFWRMVWEQNASVIVMITNLVEKGRRKCDQYWPLDSqEEYGSFLVTLRSTKV 892
Cdd:cd14555      1 YINANYIDGYHRPNHYIATQGPMQETVYDFWRMVWQENSASIVMVTNLVEVGRVKCSRYWPDDT-EVYGDIKVTLVETEP 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658117674  893 LAYYTQRTFTLkntrakkgsQKEQTHE-RTVVQYHYTQWPDMGVPEYTLPVLTFVRKSSQANLGNMGPVVVHCSAGVGRT 971
Cdd:cd14555     80 LAEYVVRTFAL---------ERRGYHEiREVRQFHFTGWPDHGVPYHATGLLGFIRRVKASNPPSAGPIVVHCSAGAGRT 150

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....
gi 1658117674  972 GTYIVLDSMLRQIKEQGTVNILGFLKHIRTQRNYLVQTEEQYIFIHDALVEAIL 1025
Cdd:cd14555    151 GCYIVIDIMLDMAEREGVVDIYNCVKELRSRRVNMVQTEEQYIFIHDAILEACL 204
R-PTPc-A-1 cd14621
catalytic domain of receptor-type tyrosine-protein phosphatase A, repeat 1; Receptor-type ...
 751-1031 5.31e-76

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: 254.18  E-value: 5.31e-76
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658117674  751 DSNTFSQEFEEIQACTVDlgITADSSIHPENKNKNRYINILAYDHSRVKLSSSSDRNgwSADYINANYVDGFTQPKAYIA 830
Cdd:cd14621     24 DNKLFREEFNALPACPIQ--ATCEAASKEENKEKNRYVNILPYDHSRVHLTPVEGVP--DSDYINASFINGYQEKNKFIA 99

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658117674  831 TQGPLKSSMEDFWRMVWEQNASVIVMITNLVEKGRRKCDQYWPLDSQEEYGSFLVTLRSTKVLAYYTQRTFTLKNTrakk 910
Cdd:cd14621    100 AQGPKEETVNDFWRMIWEQNTATIVMVTNLKERKECKCAQYWPDQGCWTYGNIRVSVEDVTVLVDYTVRKFCIQQV---- 175

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658117674  911 GSQKEQTHERTVVQYHYTQWPDMGVPEYTLPVLTFVRKSSQANLGNMGPVVVHCSAGVGRTGTYIVLDSMLRQIKEQGTV 990
Cdd:cd14621    176 GDVTNKKPQRLITQFHFTSWPDFGVPFTPIGMLKFLKKVKNCNPQYAGAIVVHCSAGVGRTGTFIVIDAMLDMMHAERKV 255

                          250       260       270       280
                   ....*....|....*....|....*....|....*....|.
gi 1658117674  991 NILGFLKHIRTQRNYLVQTEEQYIFIHDALVEAILSKETEV 1031
Cdd:cd14621    256 DVYGFVSRIRAQRCQMVQTDMQYVFIYQALLEHYLYGDTEL 296
R-PTPc-B cd14617
catalytic domain of receptor-type tyrosine-protein phosphatase B; Receptor-type ...
 785-1017 1.15e-75

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


Pssm-ID: 350465 [Multi-domain]  Cd Length: 228  Bit Score: 250.22  E-value: 1.15e-75
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658117674  785 NRYINILAYDHSRVKLSSSSDRNGwsADYINANYVDGFTQPKAYIATQGPLKSSMEDFWRMVWEQNASVIVMITNLVEKG 864
Cdd:cd14617      1 NRYNNILPYDSTRVKLSNVDDDPC--SDYINASYIPGNNFRREYIATQGPLPGTKDDFWKMVWEQNVHNIVMVTQCVEKG 78

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658117674  865 RRKCDQYWPLDSQE-EYGSFLVTLRSTKVLAYYTQRTFtlkntraKKGSQKEQTHERTVVQYHYTQWPDMGVPEYTLPVL 943
Cdd:cd14617     79 RVKCDHYWPADQDSlYYGDLIVQMLSESVLPEWTIREF-------KICSEEQLDAPRLVRHFHYTVWPDHGVPETTQSLI 151

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1658117674  944 TFVR--KSSQANLGNMGPVVVHCSAGVGRTGTYIVLDSMLRQIKEQGTVNILGFLKHIRTQRNYLVQTEEQYIFIH 1017
Cdd:cd14617    152 QFVRtvRDYINRTPGSGPTVVHCSAGVGRTGTFIALDRILQQLDSKDSVDIYGAVHDLRLHRVHMVQTECQYVYLH 227
R-PTPc-H cd14619
catalytic domain of receptor-type tyrosine-protein phosphatase H; Receptor-type ...
 785-1024 1.90e-75

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


Pssm-ID: 350467 [Multi-domain]  Cd Length: 233  Bit Score: 249.81  E-value: 1.90e-75
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658117674  785 NRYINILAYDHSRVKLSSSSDRNGwsADYINANYVDGFTQPKAYIATQGPLKSSMEDFWRMVWEQNASVIVMITNLVEKG 864
Cdd:cd14619      1 NRFRNVLPYDWSRVPLKPIHEEPG--SDYINANYMPGYWSSQEFIATQGPLPQTVGDFWRMIWEQQSSTIVMLTNCMEAG 78

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658117674  865 RRKCDQYWPLDSQE-EYGSFLVTLRSTKVLAYYTQRTFTLKNtrakkgsqKEQTHERTVVQYHYTQWPDMGVPEYTLPVL 943
Cdd:cd14619     79 RVKCEHYWPLDYTPcTYGHLRVTVVSEEVMENWTVREFLLKQ--------VEEQKTLSVRHFHFTAWPDHGVPSSTDTLL 150

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658117674  944 TFVRKSSQANLGNM--GPVVVHCSAGVGRTGTYIVLDSMLRQIKEQGTVNILGFLKHIRTQRNYLVQTEEQYIFIHDALV 1021
Cdd:cd14619    151 AFRRLLRQWLDQTMsgGPTVVHCSAGVGRTGTLIALDVLLQQLQSEGLLGPFSFVQKMRENRPLMVQTESQYVFLHQCIL 230


                   ...
gi 1658117674 1022 EAI 1024
Cdd:cd14619    231 DFL 233
PTPc-KIM cd14547
catalytic domain of the kinase interaction motif (KIM) family of protein-tyrosine phosphatases; ...
 785-1017 1.11e-73

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: 244.61  E-value: 1.11e-73
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658117674  785 NRYINILAYDHSRVKLSSSSdrNGWSADYINANYVDGFT-QPKAYIATQGPLKSSMEDFWRMVWEQNASVIVMITNLVEK 863
Cdd:cd14547      1 NRYKTILPNEHSRVCLPSVD--DDPLSSYINANYIRGYDgEEKAYIATQGPLPNTVADFWRMVWQEKTPIIVMITNLTEA 78

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658117674  864 gRRKCDQYWPLDSQEEYGSFLVTLRSTKVLAYYTQRTFTLKNtrakkgsqkeQTHERTVVQYHYTQWPDMGVPEYTLPVL 943
Cdd:cd14547     79 -KEKCAQYWPEEENETYGDFEVTVQSVKETDGYTVRKLTLKY----------GGEKRYLKHYWYTSWPDHKTPEAAQPLL 147

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1658117674  944 TFVRKSSQA--NLGNMGPVVVHCSAGVGRTGTYIVLDSMLRQIKEQGTVNILGFLKHIRTQRNYLVQTEEQYIFIH 1017
Cdd:cd14547    148 SLVQEVEEArqTEPHRGPIVVHCSAGIGRTGCFIATSIGCQQLREEGVVDVLGIVCQLRLDRGGMVQTAEQYEFVH 223
PTPc-N11_6 cd14544
catalytic domain of tyrosine-protein phosphatase non-receptor type 11 and type 6; ...
 781-1024 4.86e-73

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: 243.91  E-value: 4.86e-73
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658117674  781 NKNKNRYINILAYDHSRVKLSSSsDRNGWSADYINANYV-------DGFTQPKAYIATQGPLKSSMEDFWRMVWEQNASV 853
Cdd:cd14544      1 NKGKNRYKNILPFDHTRVILKDR-DPNVPGSDYINANYIrnenegpTTDENAKTYIATQGCLENTVSDFWSMVWQENSRV 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658117674  854 IVMITNLVEKGRRKCDQYWP-LDSQEEYGSFLVTLRSTKVLAYYTQRTFTLKNTrakkgsqKEQTHERTVVQYHYTQWPD 932
Cdd:cd14544     80 IVMTTKEVERGKNKCVRYWPdEGMQKQYGPYRVQNVSEHDTTDYTLRELQVSKL-------DQGDPIREIWHYQYLSWPD 152

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658117674  933 MGVPEYTLPVLTFVRK--SSQANLGNMGPVVVHCSAGVGRTGTYIVLDSMLRQIKEQG---TVNILGFLKHIRTQRNYLV 1007
Cdd:cd14544    153 HGVPSDPGGVLNFLEDvnQRQESLPHAGPIVVHCSAGIGRTGTFIVIDMLLDQIKRKGldcDIDIQKTIQMVRSQRSGMV 232

                          250
                   ....*....|....*..
gi 1658117674 1008 QTEEQYIFIHDALVEAI 1024
Cdd:cd14544    233 QTEAQYKFIYVAVAQYI 249
R-PTPc-O cd14614
catalytic domain of receptor-type tyrosine-protein phosphatase O; Receptor-type ...
 779-1017 1.45e-71

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: 239.41  E-value: 1.45e-71
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658117674  779 PENKNKNRYINILAYDHSRVKLSSSSDRNGwsADYINANYVDGFTQPKAYIATQGPLKSSMEDFWRMVWEQNASVIVMIT 858
Cdd:cd14614     10 PVNRCKNRYTNILPYDFSRVKLVSMHEEEG--SDYINANYIPGYNSPQEYIATQGPLPETRNDFWKMVLQQKSQIIVMLT 87

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658117674  859 NLVEKGRRKCDQYWPLDSQE-EYGSFLVTLRSTKVLAYYTQRTFTLkntrakkgSQKEQTHErtVVQYHYTQWPDMGVPE 937
Cdd:cd14614     88 QCNEKRRVKCDHYWPFTEEPvAYGDITVEMLSEEEQPDWAIREFRV--------SYADEVQD--VMHFNYTAWPDHGVPT 157

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658117674  938 YTL--PVLTFVRKSSQANLGNMGPVVVHCSAGVGRTGTYIVLDSMLRQIKEQGTVNILGFLKHIRTQRNYLVQTEEQYIF 1015
Cdd:cd14614    158 ANAaeSILQFVQMVRQQAVKSKGPMIIHCSAGVGRTGTFIALDRLLQHIRDHEFVDILGLVSEMRSYRMSMVQTEEQYIF 237


                   ..
gi 1658117674 1016 IH 1017
Cdd:cd14614    238 IH 239
R-PTPc-K-1 cd14631
catalytic domain of receptor-type tyrosine-protein phosphatase K, repeat 1; Receptor-type ...
 810-1025 1.88e-71

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: 238.00  E-value: 1.88e-71
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658117674  810 SADYINANYVDGFTQPKAYIATQGPLKSSMEDFWRMVWEQNASVIVMITNLVEKGRRKCDQYWPlDSQEEYGSFLVTLRS 889
Cdd:cd14631     12 SSDYINANYIDGYQRPSHYIATQGPVHETVYDFWRMIWQEQSACIVMVTNLVEVGRVKCYKYWP-DDTEVYGDFKVTCVE 90

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658117674  890 TKVLAYYTQRTFTLKntraKKGSQKEqtheRTVVQYHYTQWPDMGVPEYTLPVLTFVRKSSQANLGNMGPVVVHCSAGVG 969
Cdd:cd14631     91 MEPLAEYVVRTFTLE----RRGYNEI----REVKQFHFTGWPDHGVPYHATGLLSFIRRVKLSNPPSAGPIVVHCSAGAG 162

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 1658117674  970 RTGTYIVLDSMLRQIKEQGTVNILGFLKHIRTQRNYLVQTEEQYIFIHDALVEAIL 1025
Cdd:cd14631    163 RTGCYIVIDIMLDMAEREGVVDIYNCVKALRSRRINMVQTEEQYIFIHDAILEACL 218
alpha_CA cd00326
Carbonic anhydrase alpha (vertebrate-like) group. Carbonic anhydrases (CAs) are ...
 63-292 1.33e-70

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: 236.03  E-value: 1.33e-70
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658117674   63 KQSPINIDDDLSQVKMQFQKLKLEGFEQETsntTTIHNDGKTVAINLNDE-YYISGGGLRSRFKVGRITFHWGQCNasSD 141
Cdd:cd00326      3 RQSPINIVTSAVVYDPSLPPLNFDYYPTTS---LTLVNNGHTVQVNFDDDgGTLSGGGLPGRYKLVQFHFHWGSEN--SP 77

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658117674  142 GSEHSLDGIKFPLEMQIYGYEAHKFQSldSALKDGGRLTALSVLFEVSAEDNENYVAIIDGVKTVTRLGKTAVLEPFSLL 221
Cdd:cd00326     78 GSEHTIDGKRYPLELHLVHYNSDYYSS--EAAKKPGGLAVLGVFFEVGEKENPFLKKILDALPKIKYKGKETTLPPFDLS 155

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1658117674  222 GLLPNSTEKYYIYNGSLTTPPCSETVEWIVFRNTVDISDVQLETFCEVMTMQqagyvmlMDYLQNNFREQQ 292
Cdd:cd00326    156 DLLPSSLRDYYTYEGSLTTPPCSEGVTWIVFKEPITISKEQLEAFRSLLDRE-------GKPLVNNYRPVQ 219
R-PTPc-V cd14618
catalytic domain of receptor-type tyrosine-protein phosphatase V; Receptor-type ...
 785-1021 2.01e-70

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: 235.61  E-value: 2.01e-70
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658117674  785 NRYINILAYDHSRVKLSSSSDRNgwSADYINANYVDGFTQPKAYIATQGPLKSSMEDFWRMVWEQNASVIVMITNLVEKG 864
Cdd:cd14618      1 NRYPHVLPYDHSRVRLSQLGGEP--HSDYINANFIPGYTSPQEFIATQGPLKKTIEDFWRLVWEQQVCNIIMLTVGMENG 78

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658117674  865 RRKCDQYWPLDSQE-EYGSFLVTLRSTKVLAYYTQRTFTLKNTRAKKgsqkeqthERTVVQYHYTQWPDMGVPEYTLPVL 943
Cdd:cd14618     79 RVLCDHYWPSESTPvSYGHITVHLLAQSSEDEWTRREFKLWHEDLRK--------ERRVKHLHYTAWPDHGIPESTSSLM 150

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658117674  944 TF---VRKSSQANLGNmGPVVVHCSAGVGRTGTYIVLDSMLRQIKEQGTVNILGFLKHIRTQRNYLVQTEEQYIFIHDAL 1020
Cdd:cd14618    151 AFrelVREHVQATKGK-GPTLVHCSAGVGRSGTFIALDRLLRQLKEEKVVDVFNTVYILRMHRYLMIQTLSQYIFLHSCI 229


                   .
gi 1658117674 1021 V 1021
Cdd:cd14618    230 L 230
R-PTPc-U-1 cd14632
catalytic domain of receptor-type tyrosine-protein phosphatase U, repeat 1; Receptor-type ...
 813-1025 3.69e-70

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: 233.79  E-value: 3.69e-70
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658117674  813 YINANYVDGFTQPKAYIATQGPLKSSMEDFWRMVWEQNASVIVMITNLVEKGRRKCDQYWPlDSQEEYGSFLVTLRSTKV 892
Cdd:cd14632      1 YINANYIDGYHRSNHFIATQGPKQEMVYDFWRMVWQEHCSSIVMITKLVEVGRVKCSKYWP-DDSDTYGDIKITLLKTET 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658117674  893 LAYYTQRTFTLKntraKKGSQKEqtHErtVVQYHYTQWPDMGVPEYTLPVLTFVRKSSQANLGNMGPVVVHCSAGVGRTG 972
Cdd:cd14632     80 LAEYSVRTFALE----RRGYSAR--HE--VKQFHFTSWPEHGVPYHATGLLAFIRRVKASTPPDAGPVVVHCSAGAGRTG 151

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|...
gi 1658117674  973 TYIVLDSMLRQIKEQGTVNILGFLKHIRTQRNYLVQTEEQYIFIHDALVEAIL 1025
Cdd:cd14632    152 CYIVLDVMLDMAECEGVVDIYNCVKTLCSRRINMIQTEEQYIFIHDAILEACL 204
R-PTPc-E-1 cd14620
catalytic domain of receptor-type tyrosine-protein phosphatase E, repeat 1; Receptor-type ...
 787-1022 1.50e-69

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: 232.91  E-value: 1.50e-69
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658117674  787 YINILAYDHSRVKLSSSSdrNGWSADYINANYVDGFTQPKAYIATQGPLKSSMEDFWRMVWEQNASVIVMITNLVEKGRR 866
Cdd:cd14620      1 YPNILPYDHSRVILSQLD--GIPCSDYINASYIDGYKEKNKFIAAQGPKQETVNDFWRMVWEQKSATIVMLTNLKERKEE 78

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658117674  867 KCDQYWPLDSQEEYGSFLVTLRSTKVLAYYTQRTFTLKnTRAKKGSQKEqtheRTVVQYHYTQWPDMGVPEYTLPVLTFV 946
Cdd:cd14620     79 KCYQYWPDQGCWTYGNIRVAVEDCVVLVDYTIRKFCIQ-PQLPDGCKAP----RLVTQLHFTSWPDFGVPFTPIGMLKFL 153

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1658117674  947 RKSSQANLGNMGPVVVHCSAGVGRTGTYIVLDSMLRQIKEQGTVNILGFLKHIRTQRNYLVQTEEQYIFIHDALVE 1022
Cdd:cd14620    154 KKVKSVNPVHAGPIVVHCSAGVGRTGTFIVIDAMIDMMHAEQKVDVFEFVSRIRNQRPQMVQTDMQYSFIYQALLE 229
PTPc smart00194
Protein tyrosine phosphatase, catalytic domain;
1054-1311 2.23e-69

Protein tyrosine phosphatase, catalytic domain;


Pssm-ID: 214550 [Multi-domain]  Cd Length: 259  Bit Score: 233.71  E-value: 2.23e-69
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658117674  1054 LEKQFKMITQSNAKQCDYSAALKQCNRDKNRNSSLLPVERSRVHLSTTAGEISDYINASYIMGYQQSNEFIITQNPLPST 1133
Cdd:smart00194    2 LEEEFEKLDRLKPDDESCTVAAFPENRDKNRYKDVLPYDHTRVKLKPPPGEGSDYINASYIDGPNGPKAYIATQGPLPST 81

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658117674  1134 MKDFWKMIWDHSTQVVIALPDGLDL-AEDECIYWPTK-SQPIRFDTFTVTFMGEDHMclsneDMLIVQDFILEATQDDYV 1211
Cdd:smart00194   82 VEDFWRMVWEQKVTVIVMLTELVEKgREKCAQYWPDEeGEPLTYGDITVTLKSVEKV-----DDYTIRTLEVTNTGCSET 156

                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658117674  1212 LEVRQYRAPRWP---NPDGPISnTFELINIIKEESVSRDGPIVVHDKRGGNIAGTFCALMTLLHQLEMESSFDVYWVAKM 1288
Cdd:smart00194  157 RTVTHYHYTNWPdhgVPESPES-ILDLIRAVRKSQSTSTGPIVVHCSAGVGRTGTFIAIDILLQQLEAGKEVDIFEIVKE 235

                           250       260
                    ....*....|....*....|...
gi 1658117674  1289 INLMRPGIFTDIDQYQFLYKVIM 1311
Cdd:smart00194  236 LRSQRPGMVQTEEQYIFLYRAIL 258
R-PTP-LAR-2 cd14554
PTP-like domain of the LAR family receptor-type tyrosine-protein phosphatases, repeat 2; The ...
 779-1019 2.20e-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: 230.10  E-value: 2.20e-68
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658117674  779 PENKNKNRYINILAYDHSRVKLSSSSDRNGwsADYINANYVDGFTQPKAYIATQGPLKSSMEDFWRMVWEQNASVIVMIT 858
Cdd:cd14554      4 PCNKFKNRLVNILPYESTRVCLQPIRGVEG--SDYINASFIDGYRQRGAYIATQGPLAETTEDFWRMLWEHNSTIIVMLT 81

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658117674  859 NLVEKGRRKCDQYWPLDSQEEYGSFLVTLRSTKVLAYYTQRTFtlKNTRAKKGSQkeqtheRTVVQYHYTQWPDMGVPEY 938
Cdd:cd14554     82 KLREMGREKCHQYWPAERSARYQYFVVDPMAEYNMPQYILREF--KVTDARDGQS------RTVRQFQFTDWPEQGVPKS 153

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658117674  939 TLPVLTFVRK--SSQANLGNMGPVVVHCSAGVGRTGTYIVLDSMLRQIKEQGTVNILGFLKHIRTQRNYLVQTEEQYIFI 1016
Cdd:cd14554    154 GEGFIDFIGQvhKTKEQFGQEGPITVHCSAGVGRTGVFITLSIVLERMRYEGVVDVFQTVKLLRTQRPAMVQTEDQYQFC 233


                   ...
gi 1658117674 1017 HDA 1019
Cdd:cd14554    234 YRA 236
PTP_fungal cd18533
fungal protein tyrosine phosphatases; This subfamily contains Saccharomyces cerevisiae ...
 813-1018 9.07e-68

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: 227.13  E-value: 9.07e-68
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658117674  813 YINANYVD-GFTQPKAYIATQGPLKSSMEDFWRMVWEQNASVIVMITNLVEKGRRKCDQYWPLDS-QEEYGSFLVTLRST 890
Cdd:cd18533      1 YINASYITlPGTSSKRYIATQGPLPATIGDFWKMIWQNNVGVIVMLTPLVENGREKCDQYWPSGEyEGEYGDLTVELVSE 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658117674  891 KVL--AYYTQRTFTLKntrakkgsqKEQTHERTVVQYHYTQWPDMGVPEYTLPVLTFVR--KSSQANLGNMGPVVVHCSA 966
Cdd:cd18533     81 EENddGGFIVREFELS---------KEDGKVKKVYHIQYKSWPDFGVPDSPEDLLTLIKlkRELNDSASLDPPIIVHCSA 151

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1658117674  967 GVGRTGTYIVLDSMLRQIKEQGTVN---------ILGFLKHIRTQRNYLVQTEEQYIFIHD 1018
Cdd:cd18533    152 GVGRTGTFIALDSLLDELKRGLSDSqdledsedpVYEIVNQLRKQRMSMVQTLRQYIFLYD 212
R-PTPc-A-E-1 cd14551
catalytic domain of receptor-type tyrosine-protein phosphatase A and E, repeat 1; ...
 813-1017 6.19e-66

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: 221.71  E-value: 6.19e-66
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658117674  813 YINANYVDGFTQPKAYIATQGPLKSSMEDFWRMVWEQNASVIVMITNLVEKGRRKCDQYWPLDSQEEYGSFLVTLRSTKV 892
Cdd:cd14551      1 YINASYIDGYQEKNKFIAAQGPKDETVNDFWRMIWEQGSATIVMVTNLKERKEKKCSQYWPDQGCWTYGNLRVRVEDTVV 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658117674  893 LAYYTQRTFTLKNTRAKKGSQKEqtheRTVVQYHYTQWPDMGVPEYTLPVLTFVRKSSQANLGNMGPVVVHCSAGVGRTG 972
Cdd:cd14551     81 LVDYTTRKFCIQKVNRGIGEKRV----RLVTQFHFTSWPDFGVPFTPIGMLKFLKKVKSANPPRAGPIVVHCSAGVGRTG 156

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*
gi 1658117674  973 TYIVLDSMLRQIKEQGTVNILGFLKHIRTQRNYLVQTEEQYIFIH 1017
Cdd:cd14551    157 TFIVIDAMLDMMHAEGKVDVFGFVSRIRQQRSQMVQTDMQYVFIY 201
R-PTPc-C-1 cd14557
catalytic domain of receptor-type tyrosine-protein phosphatase C, repeat 1; Receptor-type ...
 813-1017 2.82e-65

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: 219.70  E-value: 2.82e-65
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658117674  813 YINANYVDGFTQPKAYIATQGPLKSSMEDFWRMVWEQNASVIVMITNLVEKGRRKCDQYWPL--DSQEEYGSFLVTLRST 890
Cdd:cd14557      1 YINASYIDGFKEPRKYIAAQGPKDETVDDFWRMIWEQKSTVIVMVTRCEEGNRNKCAQYWPSmeEGSRAFGDVVVKINEE 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658117674  891 KVLAYYTQRTFTLKNTRaKKGSQKEQTHertvVQYhyTQWPDMGVPEYTLPVLTFVRKSSQANLGNMGPVVVHCSAGVGR 970
Cdd:cd14557     81 KICPDYIIRKLNINNKK-EKGSGREVTH----IQF--TSWPDHGVPEDPHLLLKLRRRVNAFNNFFSGPIVVHCSAGVGR 153

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*..
gi 1658117674  971 TGTYIVLDSMLRQIKEQGTVNILGFLKHIRTQRNYLVQTEEQYIFIH 1017
Cdd:cd14557    154 TGTYIGIDAMLEGLEAEGRVDVYGYVVKLRRQRCLMVQVEAQYILIH 200
PTPc-N11 cd14605
catalytic domain of tyrosine-protein phosphatase non-receptor type 11; Tyrosine-protein ...
 780-1020 4.37e-64

catalytic domain of tyrosine-protein phosphatase non-receptor type 11; Tyrosine-protein phosphatase non-receptor type 11 (PTPN11), also called SH2 domain-containing tyrosine phosphatase 2 (SHP-2 or SHP2), belongs to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. PTPN11 promotes the activation of the RAS/Mitogen-Activated Protein Kinases (MAPK) Extracellular-Regulated Kinases 1/2 (ERK1/2) pathway, a canonical signaling cascade that plays key roles in various cellular processes, including proliferation, survival, differentiation, migration, or metabolism. It also regulates the phosphoinositide 3-kinase (PI3K)/AKT pathway, a fundamental cascade that functions in cell survival, proliferation, migration, morphogenesis, and metabolism. PTPN11 dysregulation is associated with several developmental diseases and malignancies, such as Noonan syndrome and juvenile myelomonocytic leukemia. It contains two tandem SH2 domains, a catalytic PTP domain, and a C-terminal tail with regulatory properties.


Pssm-ID: 350453 [Multi-domain]  Cd Length: 253  Bit Score: 218.35  E-value: 4.37e-64
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658117674  780 ENKNKNRYINILAYDHSRVKLSSSsDRNGWSADYINANYV--------DGFTQPKAYIATQGPLKSSMEDFWRMVWEQNA 851
Cdd:cd14605      1 ENKNKNRYKNILPFDHTRVVLHDG-DPNEPVSDYINANIImpefetkcNNSKPKKSYIATQGCLQNTVNDFWRMVFQENS 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658117674  852 SVIVMITNLVEKGRRKCDQYWPLD-SQEEYGSFLVtlRSTKVLAYYTQRTFTLKNTRAKKGSQkeqthERTVVQYHYTQW 930
Cdd:cd14605     80 RVIVMTTKEVERGKSKCVKYWPDEyALKEYGVMRV--RNVKESAAHDYILRELKLSKVGQGNT-----ERTVWQYHFRTW 152

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658117674  931 PDMGVPEYTLPVLTFVR--KSSQANLGNMGPVVVHCSAGVGRTGTYIVLDSMLRQIKEQGT---VNILGFLKHIRTQRNY 1005
Cdd:cd14605    153 PDHGVPSDPGGVLDFLEevHHKQESIMDAGPVVVHCSAGIGRTGTFIVIDILIDIIREKGVdcdIDVPKTIQMVRSQRSG 232

                          250
                   ....*....|....*
gi 1658117674 1006 LVQTEEQYIFIHDAL 1020
Cdd:cd14605    233 MVQTEAQYRFIYMAV 247
R-PTP-F-2 cd14629
PTP-like domain of receptor-type tyrosine-protein phosphatase F, repeat 2; Receptor-type ...
 734-1022 5.34e-64

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


Pssm-ID: 350477 [Multi-domain]  Cd Length: 291  Bit Score: 219.60  E-value: 5.34e-64
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658117674  734 HEALPIKQFVKHVAELHDSntfsQEFEEIQACTVDLGITADSSIH---------PENKNKNRYINILAYDHSRVKLSSSS 804
Cdd:cd14629      1 NTEVPARNLYAHIQKLTQV----PPGESVTAMELEFKLLANSKAHtsrfisanlPCNKFKNRLVNIMPYELTRVCLQPIR 76

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658117674  805 DRNGwsADYINANYVDGFTQPKAYIATQGPLKSSMEDFWRMVWEQNASVIVMITNLVEKGRRKCDQYWPLDSQEEYGSFL 884
Cdd:cd14629     77 GVEG--SDYINASFIDGYRQQKAYIATQGPLAETTEDFWRMLWEHNSTIVVMLTKLREMGREKCHQYWPAERSARYQYFV 154

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658117674  885 VTLRSTKVLAYYTQRTFtlKNTRAKKGsqkeqtHERTVVQYHYTQWPDMGVPEYTLPVLTFVRK--SSQANLGNMGPVVV 962
Cdd:cd14629    155 VDPMAEYNMPQYILREF--KVTDARDG------QSRTIRQFQFTDWPEQGVPKTGEGFIDFIGQvhKTKEQFGQDGPITV 226

                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658117674  963 HCSAGVGRTGTYIVLDSMLRQIKEQGTVNILGFLKHIRTQRNYLVQTEEQYIFIHDALVE 1022
Cdd:cd14629    227 HCSAGVGRTGVFITLSIVLERMRYEGVVDMFQTVKTLRTQRPAMVQTEDQYQLCYRAALE 286
PTPc-N1_2 cd14545
catalytic domain of tyrosine-protein phosphatase non-receptor type 1 and type 2; ...
 782-1015 8.36e-64

catalytic domain of tyrosine-protein phosphatase non-receptor type 1 and type 2; Tyrosine-protein phosphatase non-receptor type 1 (PTPN1) type 2 (PTPN2) belong to the family of classical tyrosine-specific protein tyrosine phosphatases, (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. PTPN1 (or PTP-1B) is the first PTP to be purified and characterized and is the prototypical intracellular PTP found in a wide variety of human tissues. It dephosphorylates and regulates the activity of a number of receptor tyrosine kinases, including the insulin receptor, the EGF receptor, and the PDGF receptor. PTPN2 (or TCPTP), a tumor suppressor, dephosphorylates and inactivates EGFRs, Src family kinases, Janus-activated kinases (JAKs)-1 and -3, and signal transducer and activators of transcription (STATs)-1, -3 and -5, in a cell type and context-dependent manner.


Pssm-ID: 350393 [Multi-domain]  Cd Length: 231  Bit Score: 216.49  E-value: 8.36e-64
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658117674  782 KNKNRYINILAYDHSRVKLssssdrNGWSADYINANYVDGFTQPKAYIATQGPLKSSMEDFWRMVWEQNASVIVMITNLV 861
Cdd:cd14545      1 LNRYRDRDPYDHDRSRVKL------KQGDNDYINASLVEVEEAKRSYILTQGPLPNTSGHFWQMVWEQNSKAVIMLNKLM 74

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658117674  862 EKGRRKCDQYWPLDSQE----EYGSFLVTLRSTKVLAYYTQRTFTLKNtraKKGSQkeqthERTVVQYHYTQWPDMGVPE 937
Cdd:cd14545     75 EKGQIKCAQYWPQGEGNamifEDTGLKVTLLSEEDKSYYTVRTLELEN---LKTQE-----TREVLHFHYTTWPDFGVPE 146

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658117674  938 YTLPVLTFVRKSSQANL--GNMGPVVVHCSAGVGRTGTYIVLDSMLRQIKEQGT--VNILGFLKHIRTQRNYLVQTEEQY 1013
Cdd:cd14545    147 SPAAFLNFLQKVRESGSlsSDVGPPVVHCSAGIGRSGTFCLVDTCLVLIEKGNPssVDVKKVLLEMRKYRMGLIQTPDQL 226


                   ..
gi 1658117674 1014 IF 1015
Cdd:cd14545    227 RF 228
R-PTP-D-2 cd14628
PTP-like domain of receptor-type tyrosine-protein phosphatase D, repeat 2; Receptor-type ...
 779-1022 1.20e-63

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: 218.45  E-value: 1.20e-63
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658117674  779 PENKNKNRYINILAYDHSRVKLSSSSDRNGwsADYINANYVDGFTQPKAYIATQGPLKSSMEDFWRMVWEQNASVIVMIT 858
Cdd:cd14628     50 PCNKFKNRLVNIMPYESTRVCLQPIRGVEG--SDYINASFIDGYRQQKAYIATQGPLAETTEDFWRMLWEHNSTIVVMLT 127

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658117674  859 NLVEKGRRKCDQYWPLDSQEEYGSFLVTLRSTKVLAYYTQRTFtlKNTRAKKGsqkeqtHERTVVQYHYTQWPDMGVPEY 938
Cdd:cd14628    128 KLREMGREKCHQYWPAERSARYQYFVVDPMAEYNMPQYILREF--KVTDARDG------QSRTVRQFQFTDWPEQGVPKS 199

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658117674  939 TLPVLTFVRK--SSQANLGNMGPVVVHCSAGVGRTGTYIVLDSMLRQIKEQGTVNILGFLKHIRTQRNYLVQTEEQYIFI 1016
Cdd:cd14628    200 GEGFIDFIGQvhKTKEQFGQDGPISVHCSAGVGRTGVFITLSIVLERMRYEGVVDIFQTVKMLRTQRPAMVQTEDQYQFC 279


                   ....*.
gi 1658117674 1017 HDALVE 1022
Cdd:cd14628    280 YRAALE 285
R-PTP-S-2 cd14627
PTP-like domain of receptor-type tyrosine-protein phosphatase S, repeat 2; Receptor-type ...
 779-1022 1.61e-63

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: 218.06  E-value: 1.61e-63
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658117674  779 PENKNKNRYINILAYDHSRVKLSSSSDRNGwsADYINANYVDGFTQPKAYIATQGPLKSSMEDFWRMVWEQNASVIVMIT 858
Cdd:cd14627     51 PCNKFKNRLVNIMPYETTRVCLQPIRGVEG--SDYINASFIDGYRQQKAYIATQGPLAETTEDFWRMLWENNSTIVVMLT 128

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658117674  859 NLVEKGRRKCDQYWPLDSQEEYGSFLVTLRSTKVLAYYTQRTFtlKNTRAKKGsqkeqtHERTVVQYHYTQWPDMGVPEY 938
Cdd:cd14627    129 KLREMGREKCHQYWPAERSARYQYFVVDPMAEYNMPQYILREF--KVTDARDG------QSRTVRQFQFTDWPEQGVPKS 200

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658117674  939 TLPVLTFVRK--SSQANLGNMGPVVVHCSAGVGRTGTYIVLDSMLRQIKEQGTVNILGFLKHIRTQRNYLVQTEEQYIFI 1016
Cdd:cd14627    201 GEGFIDFIGQvhKTKEQFGQDGPISVHCSAGVGRTGVFITLSIVLERMRYEGVVDIFQTVKMLRTQRPAMVQTEDEYQFC 280


                   ....*.
gi 1658117674 1017 HDALVE 1022
Cdd:cd14627    281 YQAALE 286
PTPc-N6 cd14606
catalytic domain of tyrosine-protein phosphatase non-receptor type 6; Tyrosine-protein ...
 779-1026 3.11e-63

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: 216.28  E-value: 3.11e-63
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658117674  779 PENKNKNRYINILAYDHSRVKLSSSsDRNGWSADYINANYVD----GFTQP-KAYIATQGPLKSSMEDFWRMVWEQNASV 853
Cdd:cd14606     16 PENKSKNRYKNILPFDHSRVILQGR-DSNIPGSDYINANYVKnqllGPDENaKTYIASQGCLEATVNDFWQMAWQENSRV 94

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658117674  854 IVMITNLVEKGRRKCDQYWP-LDSQEEYGSFLVTLRSTKVLAYYTQRTF---TLKNTRAKkgsqkeqtheRTVVQYHYTQ 929
Cdd:cd14606     95 IVMTTREVEKGRNKCVPYWPeVGMQRAYGPYSVTNCGEHDTTEYKLRTLqvsPLDNGELI----------REIWHYQYLS 164

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658117674  930 WPDMGVPEYTLPVLTFVRK--SSQANLGNMGPVVVHCSAGVGRTGTYIVLDSMLRQIKEQGT---VNILGFLKHIRTQRN 1004
Cdd:cd14606    165 WPDHGVPSEPGGVLSFLDQinQRQESLPHAGPIIVHCSAGIGRTGTIIVIDMLMENISTKGLdcdIDIQKTIQMVRAQRS 244

                          250       260
                   ....*....|....*....|..
gi 1658117674 1005 YLVQTEEQYIFIHDALVEAILS 1026
Cdd:cd14606    245 GMVQTEAQYKFIYVAIAQFIET 266
Y_phosphatase pfam00102
Protein-tyrosine phosphatase;
1079-1311 9.17e-63

Protein-tyrosine phosphatase;


Pssm-ID: 459674 [Multi-domain]  Cd Length: 234  Bit Score: 213.64  E-value: 9.17e-63
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658117674 1079 NRDKNRNSSLLPVERSRVHLSTTAGEiSDYINASYIMGYQQSNEFIITQNPLPSTMKDFWKMIWDHSTQVVIALPDGLDL 1158
Cdd:pfam00102    1 NLEKNRYKDVLPYDHTRVKLTGDPGP-SDYINASYIDGYKKPKKYIATQGPLPNTVEDFWRMVWEEKVTIIVMLTELEEK 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658117674 1159 AEDEC-IYWPTKS-QPIRFDTFTVTFMGEDhmclSNEDMLIVQDFILEATQDDYVLEVRQYRAPRWPNPDGP--ISNTFE 1234
Cdd:pfam00102   80 GREKCaQYWPEEEgESLEYGDFTVTLKKEK----EDEKDYTVRTLEVSNGGSEETRTVKHFHYTGWPDHGVPesPNSLLD 155

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1658117674 1235 LINIIKEESV-SRDGPIVVHDKRGGNIAGTFCALMTLLHQLEMESSFDVYWVAKMINLMRPGIFTDIDQYQFLYKVIM 1311
Cdd:pfam00102  156 LLRKVRKSSLdGRSGPIVVHCSAGIGRTGTFIAIDIALQQLEAEGEVDIFQIVKELRSQRPGMVQTLEQYIFLYDAIL 233
PTPc-N18 cd14603
catalytic domain of tyrosine-protein phosphatase non-receptor type 18; Tyrosine-protein ...
 756-1022 1.70e-60

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


Pssm-ID: 350451 [Multi-domain]  Cd Length: 266  Bit Score: 208.53  E-value: 1.70e-60
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658117674  756 SQEFEEIQACTV----DLGITADSSIHPENKNKNRYINILAYDHSRVKLSSSSDRNGwsADYINANYVDGFTQPKAYIAT 831
Cdd:cd14603      1 AGEFSEIRACSAafkaDYVCSTVAGGRKENVKKNRYKDILPYDQTRVILSLLQEEGH--SDYINANFIKGVDGSRAYIAT 78

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658117674  832 QGPLKSSMEDFWRMVWEQNASVIVMITNLVEKGRRKCDQYWPLDSQE-EYGSFLVT-LRSTKVLAYYTQRTFTLKntrak 909
Cdd:cd14603     79 QGPLSHTVLDFWRMIWQYGVKVILMACREIEMGKKKCERYWAQEQEPlQTGPFTITlVKEKRLNEEVILRTLKVT----- 153

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658117674  910 kgSQKEqthERTVVQYHYTQWPDMGVPEYTLPVLTFVRKSSQANLGNMGPVVVHCSAGVGRTGTYIVLD---SMLRQIKE 986
Cdd:cd14603    154 --FQKE---SRSVSHFQYMAWPDHGIPDSPDCMLAMIELARRLQGSGPEPLCVHCSAGCGRTGVICTVDyvrQLLLTQRI 228

                          250       260       270
                   ....*....|....*....|....*....|....*.
gi 1658117674  987 QGTVNILGFLKHIRTQRNYLVQTEEQYIFIHDALVE 1022
Cdd:cd14603    229 PPDFSIFDVVLEMRKQRPAAVQTEEQYEFLYHTVAQ 264
R-PTP-N cd14609
PTP-like domain of receptor-type tyrosine-protein phosphatase N; Receptor-type ...
 781-1024 1.82e-60

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: 209.12  E-value: 1.82e-60
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658117674  781 NKNKNRYINILAYDHSRVKLSSssDRNGWSADYINAN-YVDGFTQPKAYIATQGPLKSSMEDFWRMVWEQNASVIVMITN 859
Cdd:cd14609     42 NVKKNRNPDFVPYDHARIKLKA--ESNPSRSDYINASpIIEHDPRMPAYIATQGPLSHTIADFWQMVWENGCTVIVMLTP 119

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658117674  860 LVEKGRRKCDQYWPLDSQEEYGSFLVTLRSTKVLAY-YTQRTFTLKNTrakkgsqkeQTHE-RTVVQYHYTQWPDMGVPE 937
Cdd:cd14609    120 LVEDGVKQCDRYWPDEGSSLYHIYEVNLVSEHIWCEdFLVRSFYLKNV---------QTQEtRTLTQFHFLSWPAEGIPS 190

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658117674  938 YTLPVLTFVRKSSQANLGNMGPVVVHCSAGVGRTGTYIVLDSML-RQIKEQGTVNILGFLKHIRTQRNYLVQTEEQYIFI 1016
Cdd:cd14609    191 STRPLLDFRRKVNKCYRGRSCPIIVHCSDGAGRTGTYILIDMVLnRMAKGVKEIDIAATLEHVRDQRPGMVRTKDQFEFA 270


                   ....*...
gi 1658117674 1017 HDALVEAI 1024
Cdd:cd14609    271 LTAVAEEV 278
R-PTP-N2 cd14610
PTP-like domain of receptor-type tyrosine-protein phosphatase N2; Receptor-type ...
 749-1024 4.64e-60

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: 207.99  E-value: 4.64e-60
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658117674  749 LHDSNTFSQEFEEIQACTVDLGITAdSSIHPENKNKNRYINILAYDHSRVKLSSSSDRNgwSADYINANYV-DGFTQPKA 827
Cdd:cd14610     13 LKNKNRLEKEWEALCAYQAEPNATN-VAQREENVQKNRSLAVLPYDHSRIILKAENSHS--HSDYINASPImDHDPRNPA 89

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658117674  828 YIATQGPLKSSMEDFWRMVWEQNASVIVMITNLVEKGRRKCDQYWPLDSQEEYGSFLVTLRSTKVLAY-YTQRTFTLKNT 906
Cdd:cd14610     90 YIATQGPLPATVADFWQMVWESGCVVIVMLTPLAENGVKQCYHYWPDEGSNLYHIYEVNLVSEHIWCEdFLVRSFYLKNL 169

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658117674  907 rakkgsqkeQTHE-RTVVQYHYTQWPDMGVPEYTLPVLTFVRKSSQANLGNMGPVVVHCSAGVGRTGTYIVLDSMLRQI- 984
Cdd:cd14610    170 ---------QTNEtRTVTQFHFLSWNDQGVPASTRSLLDFRRKVNKCYRGRSCPIIVHCSDGAGRSGTYILIDMVLNKMa 240

                          250       260       270       280
                   ....*....|....*....|....*....|....*....|
gi 1658117674  985 KEQGTVNILGFLKHIRTQRNYLVQTEEQYIFIHDALVEAI 1024
Cdd:cd14610    241 KGAKEIDIAATLEHLRDQRPGMVQTKEQFEFALTAVAEEV 280
PTPc-N7 cd14612
catalytic domain of tyrosine-protein phosphatase non-receptor type 7; Tyrosine-protein ...
 779-1020 1.00e-59

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


Pssm-ID: 350460 [Multi-domain]  Cd Length: 247  Bit Score: 205.45  E-value: 1.00e-59
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658117674  779 PENKNKNRYINILAYDHSRVKLSSSSDRNGwSADYINANYVDGFT-QPKAYIATQGPLKSSMEDFWRMVWEQNASVIVMI 857
Cdd:cd14612     13 PGHASKDRYKTILPNPQSRVCLRRAGSQEE-EGSYINANYIRGYDgKEKAYIATQGPMLNTVSDFWEMVWQEECPIIVMI 91

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658117674  858 TNLVEKgRRKCDQYWPlDSQEEYGSFLVTLRSTKVLAYYTQRTFTLKNtrakkgsqkeQTHERTVVQYHYTQWPDMGVPE 937
Cdd:cd14612     92 TKLKEK-KEKCVHYWP-EKEGTYGRFEIRVQDMKECDGYTIRDLTIQL----------EEESRSVKHYWFSSWPDHQTPE 159

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658117674  938 YTLPVLTFVRK--SSQANLGNMGPVVVHCSAGVGRTGTYIVLDSMLRQIKEQGTVNILGFLKHIRTQRNYLVQTEEQYIF 1015
Cdd:cd14612    160 SAGPLLRLVAEveESRQTAASPGPIVVHCSAGIGRTGCFIATSIGCQQLKDTGKVDILGIVCQLRLDRGGMIQTSEQYQF 239


                   ....*
gi 1658117674 1016 IHDAL 1020
Cdd:cd14612    240 LHHTL 244
R-PTPc-A-E-2 cd14552
catalytic domain of receptor-type tyrosine-protein phosphatase A and E, repeat 2; ...
 813-1021 2.57e-59

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


Pssm-ID: 350400 [Multi-domain]  Cd Length: 202  Bit Score: 202.50  E-value: 2.57e-59
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658117674  813 YINANYVDGFTQPKAYIATQGPLKSSMEDFWRMVWEQNASVIVMITNLVEKGRRKCDQYWPLDSQEEYGSFLVTLRSTKV 892
Cdd:cd14552      1 YINASFIDGYRQKDAYIATQGPLDHTVEDFWRMIWEWKSCSIVMLTEIKERSQNKCAQYWPEDGSVSSGDITVELKDQTD 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658117674  893 LAYYTQRTFTLKNTRAKKgsqkeqthERTVVQYHYTQWPDMGVPEY---TLPVLTFVRKSSQANlGNmGPVVVHCSAGVG 969
Cdd:cd14552     81 YEDYTLRDFLVTKGKGGS--------TRTVRQFHFHGWPEVGIPDNgkgMIDLIAAVQKQQQQS-GN-HPITVHCSAGAG 150

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|..
gi 1658117674  970 RTGTYIVLDSMLRQIKEQGTVNILGFLKHIRTQRNYLVQTEEQYIFIHDALV 1021
Cdd:cd14552    151 RTGTFCALSTVLERVKAEGVLDVFQVVKSLRLQRPHMVQTLEQYEFCYKVVQ 202
PTPc-N3_4 cd14541
catalytic domain of tyrosine-protein phosphatase non-receptor type 21 and type 14; ...
 812-1026 3.70e-59

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: 202.56  E-value: 3.70e-59
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658117674  812 DYINANYVD----GFTQPKAYIATQGPLKSSMEDFWRMVWEQNASVIVMITNLVEKGRRKCDQYWP-LDSQEEYGSFLVT 886
Cdd:cd14541      1 DYINANYVNmeipGSGIVNRYIAAQGPLPNTCADFWQMVWEQKSTLIVMLTTLVERGRVKCHQYWPdLGETMQFGNLQIT 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658117674  887 LRSTKVLAYYTQRTFTLKNTrakkgsqkEQTHERTVVQYHYTQWPDMGVPEYTLPVLTFVRKSSQANLGNMGPVVVHCSA 966
Cdd:cd14541     81 CVSEEVTPSFAFREFILTNT--------NTGEERHITQMQYLAWPDHGVPDDSSDFLDFVKRVRQNRVGMVEPTVVHCSA 152

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658117674  967 GVGRTGTYIVLDSMLRQIKEQGTVNILGFLKHIRTQRNYLVQTEEQYIFIhdalVEAILS 1026
Cdd:cd14541    153 GIGRTGVLITMETAMCLIEANEPVYPLDIVRTMRDQRAMLIQTPSQYRFV----CEAILR 208
PTPc-N12 cd14604
catalytic domain of tyrosine-protein phosphatase non-receptor type 12; Tyrosine-protein ...
 739-1022 4.85e-59

catalytic domain of tyrosine-protein phosphatase non-receptor type 12; Tyrosine-protein phosphatase non-receptor type 12 (PTPN12), also called PTP-PEST or protein-tyrosine phosphatase G1 (PTPG1), belongs to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. PTPN12 is characterized as a tumor suppressor and a pivotal regulator of EGFR/HER2 signaling. It regulates various physiological processes, including cell migration, immune response, and neuronal activity, by dephosphorylating multiple substrates including HER2, FAK, PYK2, PSTPIP, WASP, p130Cas, paxillin, Shc, catenin, c-Abl, ArgBP2, p190RhoGAP, RhoGDI, cell adhesion kinase beta, and Rho GTPase.


Pssm-ID: 350452 [Multi-domain]  Cd Length: 297  Bit Score: 205.55  E-value: 4.85e-59
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658117674  739 IKQFVKHVAELHDS-----NTFSQEFEEIQACTVDLgitADSSIHP-------ENKNKNRYINILAYDHSRVKLS---SS 803
Cdd:cd14604      6 LKKFIERVQAMKSTdhngeDNFASDFMRLRRLSTKY---RTEKIYPtatgekeENVKKNRYKDILPFDHSRVKLTlktSS 82

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658117674  804 SDrngwsADYINANYVDGFTQPKAYIATQGPLKSSMEDFWRMVWEQNASVIVMITNLVEKGRRKCDQYWPLDSQE--EYG 881
Cdd:cd14604     83 QD-----SDYINANFIKGVYGPKAYIATQGPLANTVIDFWRMIWEYNVAIIVMACREFEMGRKKCERYWPLYGEEpmTFG 157

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658117674  882 SFLVTLRSTKVLAYYTQRTFTLKNtrakkgsqkeQTHERTVVQYHYTQWPDMGVP---EYTLPVLTFVRKSSQAnlgNMG 958
Cdd:cd14604    158 PFRISCEAEQARTDYFIRTLLLEF----------QNETRRLYQFHYVNWPDHDVPssfDSILDMISLMRKYQEH---EDV 224

                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1658117674  959 PVVVHCSAGVGRTGTYIVLD---SMLRQIKEQGTVNILGFLKHIRTQRNYLVQTEEQYIFIHDALVE 1022
Cdd:cd14604    225 PICIHCSAGCGRTGAICAIDytwNLLKAGKIPEEFNVFNLIQEMRTQRHSAVQTKEQYELVHRAIAQ 291
R-PTPc-Q cd14616
catalytic domain of receptor-type tyrosine-protein phosphatase Q; Receptor-type ...
 785-1017 1.19e-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: 201.67  E-value: 1.19e-58
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658117674  785 NRYINILAYDHSRVKLSSSSDRNGwsADYINANYVDGFTQPKAYIATQGPLKSSMEDFWRMVWEQNASVIVMITNLVEKG 864
Cdd:cd14616      1 NRFPNIKPYNNNRVKLIADAGVPG--SDYINASYISGYLCPNEFIATQGPLPGTVGDFWRMVWETRAKTIVMLTQCFEKG 78

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658117674  865 RRKCDQYWPLDSQ--EEYGSFLVTLRSTKVLAYYTQRTFTLKntraKKGsqkeqtHERTVVQYHYTQWPDMGVPEYTLPV 942
Cdd:cd14616     79 RIRCHQYWPEDNKpvTVFGDIVITKLMEDVQIDWTIRDLKIE----RHG------DYMMVRQCNFTSWPEHGVPESSAPL 148

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1658117674  943 LTFVRKSSQANLGNMGPVVVHCSAGVGRTGTYIVLDSMLRQIKEQGTVNILGFLKHIRTQRNYLVQTEEQYIFIH 1017
Cdd:cd14616    149 IHFVKLVRASRAHDNTPMIVHCSAGVGRTGVFIALDHLTQHINDHDFVDIYGLVAELRSERMCMVQNLAQYIFLH 223
PTPc-N20_13 cd14538
catalytic domain of tyrosine-protein phosphatase non-receptor type 20 and type 13; ...
 813-1024 1.79e-58

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: 200.29  E-value: 1.79e-58
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658117674  813 YINANYV--DGFTQPKAYIATQGPLKSSMEDFWRMVWEQNASVIVMITNLVEKGRRKCDQYWPLDSQE---EYGSFLVTL 887
Cdd:cd14538      1 YINASHIriPVGGDTYHYIACQGPLPNTTGDFWQMVWEQKSEVIAMVTQDVEGGKVKCHRYWPDSLNKpliCGGRLEVSL 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658117674  888 RSTKVLAYYTQRTFTLKntrakkgsQKEQTHERTVVQYHYTQWPDMGVPEYTLPVLTFVRKSSQanLGNMGPVVVHCSAG 967
Cdd:cd14538     81 EKYQSLQDFVIRRISLR--------DKETGEVHHITHLNFTTWPDHGTPQSADPLLRFIRYMRR--IHNSGPIVVHCSAG 150

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 1658117674  968 VGRTGTYIVLDSMLRQIKEQGTVNILGFLKHIRTQRNYLVQTEEQYIFIHDALVEAI 1024
Cdd:cd14538    151 IGRTGVLITIDVALGLIERDLPFDIQDIVKDLREQRQGMIQTKDQYIFCYKACLEVL 207
PTPc-N22 cd14602
catalytic domain of tyrosine-protein phosphatase non-receptor type 22; Tyrosine-protein ...
 784-1022 8.70e-58

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: 199.68  E-value: 8.70e-58
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658117674  784 KNRYINILAYDHSRVKLS-SSSDRNgwsADYINANYVDGFTQPKAYIATQGPLKSSMEDFWRMVWEQNASVIVMITNLVE 862
Cdd:cd14602      1 KNRYKDILPYDHSRVELSlITSDED---SDYINANFIKGVYGPRAYIATQGPLSTTLLDFWRMIWEYSVLIIVMACMEFE 77

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658117674  863 KGRRKCDQYW--PLDSQEEYGSFLVTLRSTKVLAYYTQRTFtlkntRAKKGSQKeqtheRTVVQYHYTQWPDMGVPEYTL 940
Cdd:cd14602     78 MGKKKCERYWaePGEMQLEFGPFSVTCEAEKRKSDYIIRTL-----KVKFNSET-----RTIYQFHYKNWPDHDVPSSID 147

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658117674  941 PVLTFVRKSSQANLGNMGPVVVHCSAGVGRTGTYIVLDSMLRQIKEqGTV----NILGFLKHIRTQRNYLVQTEEQYIFI 1016
Cdd:cd14602    148 PILELIWDVRCYQEDDSVPICIHCSAGCGRTGVICAIDYTWMLLKD-GIIpenfSVFSLIQEMRTQRPSLVQTKEQYELV 226


                   ....*.
gi 1658117674 1017 HDALVE 1022
Cdd:cd14602    227 YNAVIE 232
PTPc-N2 cd14607
catalytic domain of tyrosine-protein phosphatase non-receptor type 2; Tyrosine-protein ...
 778-1020 1.20e-57

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


Pssm-ID: 350455 [Multi-domain]  Cd Length: 257  Bit Score: 200.19  E-value: 1.20e-57
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658117674  778 HPENKNKNRYINILAYDHSRVKLSSSSDrngwsaDYINANYVDGFTQPKAYIATQGPLKSSMEDFWRMVWEQNASVIVMI 857
Cdd:cd14607     21 YPENRNRNRYRDVSPYDHSRVKLQNTEN------DYINASLVVIEEAQRSYILTQGPLPNTCCHFWLMVWQQKTKAVVML 94

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658117674  858 TNLVEKGRRKCDQYWPLDSQEEYG----SFLVTLRSTKVLAYYTQRTFTLKNtrAKKGSQKEQTHertvvqYHYTQWPDM 933
Cdd:cd14607     95 NRIVEKDSVKCAQYWPTDEEEVLSfketGFSVKLLSEDVKSYYTVHLLQLEN--INSGETRTISH------FHYTTWPDF 166

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658117674  934 GVPEYTLPVLTF---VRKSSQANLGNmGPVVVHCSAGVGRTGTYIVLDS--MLRQIKEQGTVNILGFLKHIRTQRNYLVQ 1008
Cdd:cd14607    167 GVPESPASFLNFlfkVRESGSLSPEH-GPAVVHCSAGIGRSGTFSLVDTclVLMEKKDPDSVDIKQVLLDMRKYRMGLIQ 245

                          250
                   ....*....|..
gi 1658117674 1009 TEEQYIFIHDAL 1020
Cdd:cd14607    246 TPDQLRFSYMAV 257
R-PTPc-R cd14611
catalytic domain of receptor-type tyrosine-protein phosphatase R; Receptor-type ...
 784-1017 2.10e-57

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: 198.22  E-value: 2.10e-57
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658117674  784 KNRYINILAYDHSRVKLSSSSDRNGWSAdYINANYVDGFT-QPKAYIATQGPLKSSMEDFWRMVWEQNASVIVMITNLVE 862
Cdd:cd14611      2 KNRYKTILPNPHSRVCLKPKNSNDSLST-YINANYIRGYGgKEKAFIATQGPMINTVNDFWQMVWQEDSPVIVMITKLKE 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658117674  863 KGRrKCDQYWPlDSQEEYGSFLVTLRSTKVLAYYTQRTFTLKNtrakkGSQKeqtheRTVVQYHYTQWPDMGVPEYTLPV 942
Cdd:cd14611     81 KNE-KCVLYWP-EKRGIYGKVEVLVNSVKECDNYTIRNLTLKQ-----GSQS-----RSVKHYWYTSWPDHKTPDSAQPL 148

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1658117674  943 LTF---VRKSSQANLGNmGPVVVHCSAGVGRTGTYIVLDSMLRQIKEQGTVNILGFLKHIRTQRNYLVQTEEQYIFIH 1017
Cdd:cd14611    149 LQLmldVEEDRLASPGR-GPVVVHCSAGIGRTGCFIATTIGCQQLKEEGVVDVLSIVCQLRVDRGGMVQTSEQYEFVH 225
R-PTP-N-N2 cd14546
PTP-like domain of receptor-type tyrosine-protein phosphatase-like N and N2; Receptor-type ...
 813-1024 2.13e-57

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: 197.28  E-value: 2.13e-57
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658117674  813 YINANYV-DGFTQPKAYIATQGPLKSSMEDFWRMVWEQNASVIVMITNLVEKGRRKCDQYWPLDSQEEYGSFLVTLRSTK 891
Cdd:cd14546      1 YINASTIyDHDPRNPAYIATQGPLPHTIADFWQMIWEQGCVVIVMLTRLQENGVKQCARYWPEEGSEVYHIYEVHLVSEH 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658117674  892 VL-AYYTQRTFTLKNTrakkgsqkeQTHE-RTVVQYHYTQWPDMGVPEYTLPVLTFVRKSSQANLGNMGPVVVHCSAGVG 969
Cdd:cd14546     81 IWcDDYLVRSFYLKNL---------QTSEtRTVTQFHFLSWPDEGIPASAKPLLEFRRKVNKSYRGRSCPIVVHCSDGAG 151

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 1658117674  970 RTGTYIVLD----SMLRQIKEqgtVNILGFLKHIRTQRNYLVQTEEQYIFIHDALVEAI 1024
Cdd:cd14546    152 RTGTYILIDmvlnRMAKGAKE---IDIAATLEHLRDQRPGMVKTKDQFEFVLTAVAEEV 207
PTPc-N3 cd14600
catalytic domain of tyrosine-protein phosphatase non-receptor type 3; Tyrosine-protein ...
 751-1025 2.88e-57

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: 199.69  E-value: 2.88e-57
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658117674  751 DSNTFSQEFEEIQACTVDLGITADSSihPENKNKNRYINILAYDHSRVKLSSSSDrngwsadYINANYVDgfTQPKA--- 827
Cdd:cd14600     12 ESGTVLIQFEQLYRKKPGLAITCAKL--PQNMDKNRYKDVLPYDATRVVLQGNED-------YINASYVN--MEIPSani 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658117674  828 ---YIATQGPLKSSMEDFWRMVWEQNASVIVMITNLVEKGRRKCDQYWPlDSQE--EYGSFLVTLRSTKVLAYYTQRTFT 902
Cdd:cd14600     81 vnkYIATQGPLPHTCAQFWQVVWEQKLSLIVMLTTLTERGRTKCHQYWP-DPPDvmEYGGFRVQCHSEDCTIAYVFREML 159

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658117674  903 LKNTrakkgsqkEQTHERTVVQYHYTQWPDMGVPEYTLPVLTFVRKSSQANLGNMgPVVVHCSAGVGRTGTYIVLDSMLR 982
Cdd:cd14600    160 LTNT--------QTGEERTVTHLQYVAWPDHGVPDDSSDFLEFVNYVRSKRVENE-PVLVHCSAGIGRTGVLVTMETAMC 230

                          250       260       270       280
                   ....*....|....*....|....*....|....*....|...
gi 1658117674  983 QIKEQGTVNILGFLKHIRTQRNYLVQTEEQYIFIhdalVEAIL 1025
Cdd:cd14600    231 LTERNQPVYPLDIVRKMRDQRAMMVQTSSQYKFV----CEAIL 269
PTPc-N1 cd14608
catalytic domain of tyrosine-protein phosphatase non-receptor type 1; Tyrosine-protein ...
 778-1022 4.75e-57

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: 199.10  E-value: 4.75e-57
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658117674  778 HPENKNKNRYINILAYDHSRVKLSSSSDrngwsaDYINANYVDGFTQPKAYIATQGPLKSSMEDFWRMVWEQNASVIVMI 857
Cdd:cd14608     22 LPKNKNRNRYRDVSPFDHSRIKLHQEDN------DYINASLIKMEEAQRSYILTQGPLPNTCGHFWEMVWEQKSRGVVML 95

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658117674  858 TNLVEKGRRKCDQYWPLDSQEEY----GSFLVTLRSTKVLAYYTQRTFTLKNTRAKKgsqkeqthERTVVQYHYTQWPDM 933
Cdd:cd14608     96 NRVMEKGSLKCAQYWPQKEEKEMifedTNLKLTLISEDIKSYYTVRQLELENLTTQE--------TREILHFHYTTWPDF 167

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658117674  934 GVPEYTLPVLTF---VRKSSQANlGNMGPVVVHCSAGVGRTGTYIVLDS---MLRQIKEQGTVNILGFLKHIRTQRNYLV 1007
Cdd:cd14608    168 GVPESPASFLNFlfkVRESGSLS-PEHGPVVVHCSAGIGRSGTFCLADTcllLMDKRKDPSSVDIKKVLLEMRKFRMGLI 246

                          250
                   ....*....|....*
gi 1658117674 1008 QTEEQYIFIHDALVE 1022
Cdd:cd14608    247 QTADQLRFSYLAVIE 261
PTPc-N5 cd14613
catalytic domain of tyrosine-protein phosphatase non-receptor type 5; Tyrosine-protein ...
 784-1020 1.54e-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: 1.54e-56
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658117674  784 KNRYINILAYDHSRVKLSSSSDRNGWSAdYINANYVDGF-TQPKAYIATQGPLKSSMEDFWRMVWEQNASVIVMITNLVE 862
Cdd:cd14613     28 KNRYKTILPNPHSRVCLTSPDQDDPLSS-YINANYIRGYgGEEKVYIATQGPTVNTVGDFWRMVWQERSPIIVMITNIEE 106

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658117674  863 KGRrKCDQYWPlDSQEEYGSFLVTLRSTKVLAYYTQRTFTLKNtrakkgsqkeQTHERTVVQYHYTQWPDMGVPEYTLPV 942
Cdd:cd14613    107 MNE-KCTEYWP-EEQVTYEGIEITVKQVIHADDYRLRLITLKS----------GGEERGLKHYWYTSWPDQKTPDNAPPL 174

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658117674  943 LTFVRK---SSQANLGNMGPVVVHCSAGVGRTGTYIVLDSMLRQIKEQGTVNILGFLKHIRTQRNYLVQTEEQYIFIHDA 1019
Cdd:cd14613    175 LQLVQEveeARQQAEPNCGPVIVHCSAGIGRTGCFIATSICCKQLRNEGVVDILRTTCQLRLDRGGMIQTCEQYQFVHHV 254


                   .
gi 1658117674 1020 L 1020
Cdd:cd14613    255 L 255
alpha_CA_IV_XV_like cd03117
Carbonic anhydrase alpha, CA_IV, CA_XV, like isozymes. Carbonic anhydrases (CAs) are ...
 63-292 1.75e-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: 195.57  E-value: 1.75e-56
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658117674   63 KQSPINIDDDLSQVKMQFQKLKLEGFeQETSNTTTIHNDGKTVAINLNDEYYISGGGLRSRFKVGRITFHWGqcNASSDG 142
Cdd:cd03117      3 RQSPINIVTKKVQYDENLTPFTFTGY-DDTTTNWTITNNGHTVQVTLPDGAKISGGGLPGTYKALQFHFHWG--SNGSPG 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658117674  143 SEHSLDGIKFPLEMQIYGYEAhKFQSLDSALKDGGRLTALSVLFEVSAEDNENYVAIIDGVKTVTRLGKTAVLEPFSLLG 222
Cdd:cd03117     80 SEHTIDGERYPMELHIVHIKE-SYNSLLEALKDSDGLAVLGFFIEEGEEENTNFDPLISALSNIPQKGGSTNLTPFSLRS 158

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1658117674  223 LLP-NSTEKYYIYNGSLTTPPCSETVEWIVFRNTVDISDVQLETFCEVMTMQQAGYVMLMdylqNNFREQQ 292
Cdd:cd03117    159 LLPsVLLTKYYRYNGSLTTPGCNEAVIWTVFEEPIPISRAQLDAFSTVLFFDTDNGQPMV----NNFRPVQ 225
R-PTPc-A-2 cd14623
catalytic domain of receptor-type tyrosine-protein phosphatase A, repeat 2; Receptor-type ...
 786-1022 4.73e-56

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


Pssm-ID: 350471 [Multi-domain]  Cd Length: 228  Bit Score: 194.49  E-value: 4.73e-56
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658117674  786 RYINILAYDHSRVKLSSSsdRNGWSADYINANYVDGFTQPKAYIATQGPLKSSMEDFWRMVWEQNASVIVMITNLVEKGR 865
Cdd:cd14623      1 RVLQIIPYEFNRVIIPVK--RGEENTDYVNASFIDGYRQKDSYIASQGPLQHTIEDFWRMIWEWKSCSIVMLTELEERGQ 78

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658117674  866 RKCDQYWPLDSQEEYGSFLVTLRSTKVLAYYTQRTFTLKNTRAKKgsqkeqthERTVVQYHYTQWPDMGVP---EYTLPV 942
Cdd:cd14623     79 EKCAQYWPSDGSVSYGDITIELKKEEECESYTVRDLLVTNTRENK--------SRQIRQFHFHGWPEVGIPsdgKGMINI 150

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658117674  943 LTFVRKSSQANlGNMgPVVVHCSAGVGRTGTYIVLDSMLRQIKEQGTVNILGFLKHIRTQRNYLVQTEEQYIFIHDALVE 1022
Cdd:cd14623    151 IAAVQKQQQQS-GNH-PITVHCSAGAGRTGTFCALSTVLERVKAEGILDVFQTVKSLRLQRPHMVQTLEQYEFCYKVVQE 228
alpha_CA_VI_IX_XII_XIV cd03123
Carbonic anhydrase alpha, isozymes VI, IX, XII and XIV. Carbonic anhydrases (CAs) are ...
 49-292 5.48e-56

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: 194.83  E-value: 5.48e-56
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658117674   49 QNNWAKKYPSCNNAKQSPINIDDDLSQVKMQFQKLKLEGFEQETSNTTTIHNDGKTVAINLNDEYYIsGGGLRSRFKVGR 128
Cdd:cd03123      2 EDHWPKKYPACGGKRQSPIDIQTDIVQFDPSLPPLELVGYDLPGTEEFTLTNNGHTVQLSLPPTMHI-RGGPGTEYTAAQ 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658117674  129 ITFHWGQCNASSdGSEHSLDGIKFPLEMQIYGYEAHKFQSLDSALKDGGRLTALSVLFEVSAEDNENYVAIIDGVKTVTR 208
Cdd:cd03123     81 LHLHWGGRGSLS-GSEHTIDGIRFAAELHIVHYNSDKYSSFDEAADKPDGLAVLAILIEVGYPENTYYEKIISHLHEIKY 159

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658117674  209 LGKTAVLEPFSLLGLLPNSTEKYYIYNGSLTTPPCSETVEWIVFRNTVDISDVQLEtfcevmTMQQAgyvmLMDY----L 284
Cdd:cd03123    160 KGQETTVPGFNVRELLPEDLSHYYRYEGSLTTPPCYESVLWTVFRDPVTLSKEQLE------TLENT----LMDThnktL 229


                   ....*...
gi 1658117674  285 QNNFREQQ 292
Cdd:cd03123    230 QNNYRATQ 237
PTPc-N22_18_12 cd14542
catalytic domain of tyrosine-protein phosphatase non-receptor type 22, type 18 and type 12; ...
 813-1017 2.18e-55

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


Pssm-ID: 350390 [Multi-domain]  Cd Length: 202  Bit Score: 191.48  E-value: 2.18e-55
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658117674  813 YINANYVDGFTQPKAYIATQGPLKSSMEDFWRMVWEQNASVIVMITNLVEKGRRKCDQYWPlDSQEE---YGSFLVTLRS 889
Cdd:cd14542      1 YINANFIKGVSGSKAYIATQGPLPNTVLDFWRMIWEYNVQVIVMACREFEMGKKKCERYWP-EEGEEqlqFGPFKISLEK 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658117674  890 TKVLAY-YTQRtfTLKNTRakkgsQKEqthERTVVQYHYTQWPDMGVPEYTLPVLTFVRKSSQANLGNMGPVVVHCSAGV 968
Cdd:cd14542     80 EKRVGPdFLIR--TLKVTF-----QKE---SRTVYQFHYTAWPDHGVPSSVDPILDLVRLVRDYQGSEDVPICVHCSAGC 149

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|..
gi 1658117674  969 GRTGTYIVLD---SMLRQIKEQGTVNILGFLKHIRTQRNYLVQTEEQYIFIH 1017
Cdd:cd14542    150 GRTGTICAIDyvwNLLKTGKIPEEFSLFDLVREMRKQRPAMVQTKEQYELVY 201
R-PTPc-E-2 cd14622
catalytic domain of receptor-type tyrosine-protein phosphatase E, repeat 2; Receptor-type ...
 812-1017 4.54e-53

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: 184.82  E-value: 4.54e-53
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658117674  812 DYINANYVDGFTQPKAYIATQGPLKSSMEDFWRMVWEQNASVIVMITNLVEKGRRKCDQYWPLDSQEEYGSFLVTLRSTK 891
Cdd:cd14622      1 DYINASFIDGYRQKDYFIATQGPLAHTVEDFWRMVWEWKCHTIVMLTELQEREQEKCVQYWPSEGSVTHGEITIEIKNDT 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658117674  892 VLAYYTQRTFTLKNtrakkgSQKEQTheRTVVQYHYTQWPDMGVP---EYTLPVLTFVRKSSQANlGNmGPVVVHCSAGV 968
Cdd:cd14622     81 LLETISIRDFLVTY------NQEKQT--RLVRQFHFHGWPEIGIPaegKGMIDLIAAVQKQQQQT-GN-HPIVVHCSAGA 150

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*....
gi 1658117674  969 GRTGTYIVLDSMLRQIKEQGTVNILGFLKHIRTQRNYLVQTEEQYIFIH 1017
Cdd:cd14622    151 GRTGTFIALSNILERVKAEGLLDVFQTVKSLRLQRPHMVQTLEQYEFCY 199
PTPc-N13 cd14597
catalytic domain of tyrosine-protein phosphatase non-receptor type 13; Tyrosine-protein ...
 780-1015 1.32e-52

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: 184.65  E-value: 1.32e-52
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658117674  780 ENKNKNRYINILAYDHSRVKLssssdrnGWSADYINANYVD---GFTQpKAYIATQGPLKSSMEDFWRMVWEQNASVIVM 856
Cdd:cd14597      2 ENRKKNRYKNILPYDTTRVPL-------GDEGGYINASFIKmpvGDEE-FVYIACQGPLPTTVADFWQMVWEQKSTVIAM 73

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658117674  857 ITNLVEKGRRKCDQYWPldsqEEYGSFL-------VTLRSTKVLAYYTQRTFTLKNTrakkgsqkeQTHE-RTVVQYHYT 928
Cdd:cd14597     74 MTQEVEGGKIKCQRYWP----EILGKTTmvdnrlqLTLVRMQQLKNFVIRVLELEDI---------QTREvRHITHLNFT 140

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658117674  929 QWPDMGVPEYTLPVLTFVrkSSQANLGNMGPVVVHCSAGVGRTGTYIVLDSMLRQIKEQGTVNILGFLKHIRTQRNYLVQ 1008
Cdd:cd14597    141 AWPDHDTPSQPEQLLTFI--SYMRHIHKSGPIITHCSAGIGRSGTLICIDVVLGLISKDLDFDISDIVRTMRLQRHGMVQ 218


                   ....*..
gi 1658117674 1009 TEEQYIF 1015
Cdd:cd14597    219 TEDQYIF 225
PTP-N23 cd14539
PTP-like domain of tyrosine-protein phosphatase non-receptor type 23; Tyrosine-protein ...
 813-1018 1.40e-52

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: 183.35  E-value: 1.40e-52
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658117674  813 YINANYVDGFTQPKA-YIATQGPLKSSMEDFWRMVWEQNASVIVMITNLVEKGRRKCDQYWPLD--SQEEYGSFLVTLRS 889
Cdd:cd14539      1 YINASLIEDLTPYCPrFIATQAPLPGTAADFWLMVYEQQVSVIVMLVSEQENEKQKVHRYWPTErgQALVYGAITVSLQS 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658117674  890 TKVLAYYTQRTFTLKNtrakkgsqKEQTHERTVVQYHYTQWPDMGVPEYTLPVLTF---VRKSSQANLGNMGPVVVHCSA 966
Cdd:cd14539     81 VRTTPTHVERIISIQH--------KDTRLSRSVVHLQFTTWPELGLPDSPNPLLRFieeVHSHYLQQRSLQTPIVVHCSS 152

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|...
gi 1658117674  967 GVGRTGTYIVLDSMLRQIKE-QGTVNILGFLKHIRTQRNYLVQTEEQYIFIHD 1018
Cdd:cd14539    153 GVGRTGAFCLLYAAVQEIEAgNGIPDLPQLVRKMRQQRKYMLQEKEHLKFCYE 205
PTPc-N21_14 cd14540
catalytic domain of tyrosine-protein phosphatase non-receptor type 21 and type 14; ...
 813-1022 2.55e-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: 183.04  E-value: 2.55e-52
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658117674  813 YINANYVDGFTQPKA--YIATQGPLKSSMEDFWRMVWEQNASVIVMITNLVEKGRRKCDQYWPLDSQEE----YGSFLVT 886
Cdd:cd14540      1 YINASHITATVGGKQrfYIAAQGPLQNTVGDFWQMVWEQGVYLVVMVTAEEEGGREKCFRYWPTLGGEHdaltFGEYKVS 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658117674  887 LRSTKVLAYYTQRTFTLKNTRAKKgsqkeqthERTVVQYHYTQWPDMGVPEYTLPVLTFVRKSSQANLGNMG-------- 958
Cdd:cd14540     81 TKFSVSSGCYTTTGLRVKHTLSGQ--------SRTVWHLQYTDWPDHGCPEDVSGFLDFLEEINSVRRHTNQdvaghnrn 152

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1658117674  959 -PVVVHCSAGVGRTGTYIVLDSMLRQIKEQGTVNILGFLKHIRTQRNYLVQTEEQYIFIHDALVE 1022
Cdd:cd14540    153 pPTLVHCSAGVGRTGVVILADLMLYCLDHNEELDIPRVLALLRHQRMLLVQTLAQYKFVYNVLIQ 217
PTPc cd00047
catalytic domain of protein tyrosine phosphatases; Protein tyrosine phosphatases (PTP, EC 3.1. ...
 1108-1308 4.16e-52

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: 181.71  E-value: 4.16e-52
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658117674 1108 YINASYIMGYQQSNEFIITQNPLPSTMKDFWKMIWDHSTQVVIALPDGLDLAEDECI-YWPTK-SQPIRFDTFTVTFMGE 1185
Cdd:cd00047      1 YINASYIDGYRGPKEYIATQGPLPNTVEDFWRMVWEQKVSVIVMLTNLVEKGREKCErYWPEEgGKPLEYGDITVTLVSE 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658117674 1186 DHMclsneDMLIVQDFILEATQDDYVLEVRQYRAPRWPNPDGP--ISNTFELINIIKEESVSRDGPIVVHDKRGGNIAGT 1263
Cdd:cd00047     81 EEL-----SDYTIRTLELSPKGCSESREVTHLHYTGWPDHGVPssPEDLLALVRRVRKEARKPNGPIVVHCSAGVGRTGT 155

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*
gi 1658117674 1264 FCALMTLLHQLEMESSFDVYWVAKMINLMRPGIFTDIDQYQFLYK 1308
Cdd:cd00047    156 FIAIDILLERLEAEGEVDVFEIVKALRKQRPGMVQTLEQYEFIYE 200
PHA02738 PHA02738
hypothetical protein; Provisional
 734-1020 1.66e-51

hypothetical protein; Provisional


Pssm-ID: 222923 [Multi-domain]  Cd Length: 320  Bit Score: 184.74  E-value: 1.66e-51
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658117674  734 HEALPIKQFVKHVAELHDSNTFSQEFEEIQACTVDLGITADSsihpENKNKNRYINILAYDHSRVKLSSSSDRngwsADY 813
Cdd:PHA02738     6 FRELKYAEFLALMEKSDCEEVITREHQKVISEKVDGTFNAEK----KNRKLNRYLDAVCFDHSRVILPAERNR----GDY 77

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658117674  814 INANYVDGFTQPKAYIATQGPLKSSMEDFWRMVWEQNASVIVMITNLVEKGRRKCDQYWPLDSQEE--YGSFLVTLRSTK 891
Cdd:PHA02738    78 INANYVDGFEYKKKFICGQAPTRQTCYDFYRMLWMEHVQIIVMLCKKKENGREKCFPYWSDVEQGSirFGKFKITTTQVE 157

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658117674  892 VLAYYTQRTFTLKNtrakkGSQKEQtherTVVQYHYTQWPDMGVPEYTLPVLTFVRKSSQA-------------NLGNMG 958
Cdd:PHA02738   158 THPHYVKSTLLLTD-----GTSATQ----TVTHFNFTAWPDHDVPKNTSEFLNFVLEVRQCqkelaqeslqighNRLQPP 228

                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1658117674  959 PVVVHCSAGVGRTGTYIVLDSMLRQIKEQGTVNILGFLKHIRTQRNYLVQTEEQYIFIHDAL 1020
Cdd:PHA02738   229 PIVVHCNAGLGRTPCYCVVDISISRFDACATVSIPSIVSSIRNQRYYSLFIPFQYFFCYRAV 290
alpha_CA_XII_XIV cd03126
Carbonic anhydrase alpha, isozymes XII and XIV. Carbonic anhydrases (CAs) are zinc-containing ...
 49-292 3.88e-50

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: 178.11  E-value: 3.88e-50
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658117674   49 QNNWAKKYPSCNNAKQSPINIDDDLSQVKMQFQKLKLEGFEQETSNTTTIHNDGKTVAINLNDEYYIsgGGLRSRFKVGR 128
Cdd:cd03126      2 ENSWPKKYPFCGGVAQSPIDIHTDILQYDSSLPPLEFHGYNVSGTEQFTLTNNGHTVQLSLPPTMHI--GGLPFKYTASQ 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658117674  129 ITFHWGQCNaSSDGSEHSLDGIKFPLEMQIYGYEAHKFQSLDSALKDGGRLTALSVLFEVsAEDNENYVAIIDGVKTVTR 208
Cdd:cd03126     80 LHLHWGQRG-SPEGSEHTISGKHFAAELHIVHYNSDKYPDISTAMNKSQGLAVLGILIEV-GPFNPSYEKIFSHLHEVKY 157

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658117674  209 LGKTAVLEPFSLLGLLPNSTEKYYIYNGSLTTPPCSETVEWIVFRNTVDISDVQLEtfcevmTMQQAGYVMLMD---YLQ 285
Cdd:cd03126    158 KDQKVSVPGFNVQELLPKRLDEYYRYEGSLTTPPCYPSVLWTVFRNPVQISQEQLL------ALETALYSTEEDesrEMV 231


                   ....*..
gi 1658117674  286 NNFREQQ 292
Cdd:cd03126    232 NNYRQVQ 238
PHA02747 PHA02747
protein tyrosine phosphatase; Provisional
 772-1017 3.54e-49

protein tyrosine phosphatase; Provisional


Pssm-ID: 165114 [Multi-domain]  Cd Length: 312  Bit Score: 177.50  E-value: 3.54e-49
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658117674  772 TADSSIHPENKNKNRYINILAYDHSRVKLSSSSdrnGWSADYINANYVDGFTQPKAYIATQGPLKSSMEDFWRMVWEQNA 851
Cdd:PHA02747    42 LIANFEKPENQPKNRYWDIPCWDHNRVILDSGG---GSTSDYIHANWIDGFEDDKKFIATQGPFAETCADFWKAVWQEHC 118

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658117674  852 SVIVMIT-NLVEKGRRKCDQYWPL--DSQEEYGSFLVTLRSTKVLAYYTQRTFTLKNtrakkgsqKEQTHERTVVQYHYT 928
Cdd:PHA02747   119 SIIVMLTpTKGTNGEEKCYQYWCLneDGNIDMEDFRIETLKTSVRAKYILTLIEITD--------KILKDSRKISHFQCS 190

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658117674  929 QWPDMGVPEYTLPVLTF------VRKSSQANLGN----MGPVVVHCSAGVGRTGTYIVLDSMLRQIKEQGTVNILGFLKH 998
Cdd:PHA02747   191 EWFEDETPSDHPDFIKFikiidiNRKKSGKLFNPkdalLCPIVVHCSDGVGKTGIFCAVDICLNQLVKRKAICLAKTAEK 270

                          250
                   ....*....|....*....
gi 1658117674  999 IRTQRNYLVQTEEQYIFIH 1017
Cdd:PHA02747   271 IREQRHAGIMNFDDYLFIQ 289
PHA02746 PHA02746
protein tyrosine phosphatase; Provisional
 760-1025 4.92e-49

protein tyrosine phosphatase; Provisional


Pssm-ID: 165113 [Multi-domain]  Cd Length: 323  Bit Score: 177.53  E-value: 4.92e-49
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658117674  760 EEIQACTVDLGITADSSIHPENKNKNRYINILAYDHSRVKLSS-----SSDRNGW------------SADYINANYVDGF 822
Cdd:PHA02746    30 EHAEVMDIPIRGTTNHFLKKENLKKNRFHDIPCWDHSRVVINAheslkMFDVGDSdgkkievtsednAENYIHANFVDGF 109

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658117674  823 TQPKAYIATQGPLKSSMEDFWRMVWEQNASVIVMITNlVEKGRRKCDQYW--PLDSQEEYGSFLVtlrstKVLAYYTQRT 900
Cdd:PHA02746   110 KEANKFICAQGPKEDTSEDFFKLISEHESQVIVSLTD-IDDDDEKCFELWtkEEDSELAFGRFVA-----KILDIIEELS 183

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658117674  901 FTlkNTRAKKGSQKEQThERTVVQYHYTQWPDMGVPEYTLPVLTFV----------RKSSQANLGNMGPVVVHCSAGVGR 970
Cdd:PHA02746   184 FT--KTRLMITDKISDT-SREIHHFWFPDWPDNGIPTGMAEFLELInkvneeqaelIKQADNDPQTLGPIVVHCSAGIGR 260

                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1658117674  971 TGTYIVLDSMLRQIKEQGTVNILGFLKHIRTQRNYLVQTEEQYIFIHDALVEAIL 1025
Cdd:PHA02746   261 AGTFCAIDNALEQLEKEKEVCLGEIVLKIRKQRHSSVFLPEQYAFCYKALKYAII 315
PTPc-N4 cd14601
catalytic domain of tyrosine-protein phosphatase non-receptor type 4; Tyrosine-protein ...
 812-1025 1.22e-48

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


Pssm-ID: 350449 [Multi-domain]  Cd Length: 212  Bit Score: 172.44  E-value: 1.22e-48
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658117674  812 DYINANYVD----GFTQPKAYIATQGPLKSSMEDFWRMVWEQNASVIVMITNLVEKGRRKCDQYWPLDS-QEEYGSFLVT 886
Cdd:cd14601      1 DYINANYINmeipSSSIINRYIACQGPLPNTCSDFWQMTWEQGSSMVVMLTTQVERGRVKCHQYWPEPSgSSSYGGFQVT 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658117674  887 LRSTKVLAYYTQRTFTLKNTrakkgsqkEQTHERTVVQYHYTQWPDMGVPEYTLPVLTFVRKSSQANLGNMGPVVVHCSA 966
Cdd:cd14601     81 CHSEEGNPAYVFREMTLTNL--------EKNESRPLTQIQYIAWPDHGVPDDSSDFLDFVCLVRNKRAGKDEPVVVHCSA 152

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 1658117674  967 GVGRTGTYIVLDSMLRQIKEQGTVNILGFLKHIRTQRNYLVQTEEQYIFIhdalVEAIL 1025
Cdd:cd14601    153 GIGRTGVLITMETAMCLIECNQPVYPLDIVRTMRDQRAMMIQTPSQYRFV----CEAIL 207
PTPc-N14 cd14599
catalytic domain of tyrosine-protein phosphatase non-receptor type 14; Tyrosine-protein ...
 758-1022 1.27e-48

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: 175.19  E-value: 1.27e-48
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658117674  758 EFEEIQACTVDlGITADSSIhPENKNKNRYINILAYDHSRVKLSSSSDRNgwsADYINANYVDGFTQPKA--YIATQGPL 835
Cdd:cd14599     17 EYEQIPKKKAD-GVFTTATL-PENAERNRIREVVPYEENRVELVPTKENN---TGYINASHIKVTVGGEEwhYIATQGPL 91

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658117674  836 KSSMEDFWRMVWEQNASVIVMITNLVEKGRRKCDQYWP----LDSQEEYGSFLVTLRSTKVLAYYTQRTFTLKNTRAKKg 911
Cdd:cd14599     92 PHTCHDFWQMVWEQGVNVIAMVTAEEEGGRSKSHRYWPklgsKHSSATYGKFKVTTKFRTDSGCYATTGLKVKHLLSGQ- 170

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658117674  912 sqkeqthERTVVQYHYTQWPDMGVPEYTLPVLTF------VRKSSQANLGNMG----PVVVHCSAGVGRTGTYIVLDSML 981
Cdd:cd14599    171 -------ERTVWHLQYTDWPDHGCPEEVQGFLSYleeiqsVRRHTNSMLDSTKncnpPIVVHCSAGVGRTGVVILTELMI 243

                          250       260       270       280
                   ....*....|....*....|....*....|....*....|.
gi 1658117674  982 RQIKEQGTVNILGFLKHIRTQRNYLVQTEEQYIFIHDALVE 1022
Cdd:cd14599    244 GCLEHNEKVEVPVMLRHLREQRMFMIQTIAQYKFVYQVLIQ 284
PTPc_plant_PTP1 cd17658
protein tyrosine phosphatase 1 from Arabidopsis thaliana and similar plant PTPs; Arabidopsis ...
 813-1017 8.54e-48

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: 169.57  E-value: 8.54e-48
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658117674  813 YINANYV--DGFTQPKAYIATQGPLKSSMEDFWRMVWEQNASVIVMITNLVEKGRR-KCDQYWPLD--SQEEYGSFLVTL 887
Cdd:cd17658      1 YINASLVetPASESLPKFIATQGPLPHTFEDFWEMVIQQRCPVIIMLTRLVDNYSTaKCADYFPAEenESREFGRISVTN 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658117674  888 RSTKvlayYTQRTFTLKNTRAKKGSQKEQTheRTVVQYHYTQWPDMGVPEYTLPVLTFVRKSSQANlGNMGPVVVHCSAG 967
Cdd:cd17658     81 KKLK----HSQHSITLRVLEVQYIESEEPP--LSVLHIQYPEWPDHGVPKDTRSVRELLKRLYGIP-PSAGPIVVHCSAG 153

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|..
gi 1658117674  968 VGRTGTYIVLDSMLRQIKE--QGTVNILGFLKHIRTQRNYLVQTEEQYIFIH 1017
Cdd:cd17658    154 IGRTGAYCTIHNTIRRILEgdMSAVDLSKTVRKFRSQRIGMVQTQDQYIFCY 205
PTPc-N20 cd14596
catalytic domain of tyrosine-protein phosphatase non-receptor type 20; Tyrosine-protein ...
 813-1024 9.49e-48

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


Pssm-ID: 350444 [Multi-domain]  Cd Length: 207  Bit Score: 169.54  E-value: 9.49e-48
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658117674  813 YINANYVdgfTQPKA-----YIATQGPLKSSMEDFWRMVWEQNASVIVMITNLVEKGRRKCDQYWPLDSQE--EYGSFLV 885
Cdd:cd14596      1 YINASYI---TMPVGeeelfYIATQGPLPSTIDDFWQMVWENRSDVIAMMTREVERGKVKCHRYWPETLQEpmELENYQL 77

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658117674  886 TLRSTKVLAYYTQRTFTLkntrakkgSQKEQTHERTVVQYHYTQWPDMGVPEYTLPVLTFVRKSSQANlgNMGPVVVHCS 965
Cdd:cd14596     78 RLENYQALQYFIIRIIKL--------VEKETGENRLIKHLQFTTWPDHGTPQSSDQLVKFICYMRKVH--NTGPIVVHCS 147

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 1658117674  966 AGVGRTGTYIVLDSMLRQIKEQGTVNILGFLKHIRTQRNYLVQTEEQYIFIHDALVEAI 1024
Cdd:cd14596    148 AGIGRAGVLICVDVLLSLIEKDLSFNIKDIVREMRQQRYGMIQTKDQYLFCYKVVLEVL 206
R-PTP-C-2 cd14558
PTP-like domain of receptor-type tyrosine-protein phosphatase C, repeat 2; Receptor-type ...
 813-1018 1.29e-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: 169.11  E-value: 1.29e-47
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658117674  813 YINANYVDGFTQPKAYIATQGPLKSSMEDFWRMVWEQNASVIVMITNLVEKGRRKCDQYWPlDSQEEYGSFLVTLRSTKV 892
Cdd:cd14558      1 YINASFIDGYWGPKSLIATQGPLPDTIADFWQMIFQKKVKVIVMLTELKEGDQEQCAQYWG-DEKKTYGDIEVELKDTEK 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658117674  893 LAYYTQRTFTLKNTRAKKgsqkeqthERTVVQYHYTQWPDMGVPEYTLPVLTFVR------KSSQANLGNMGPVVVHCSA 966
Cdd:cd14558     80 SPTYTVRVFEITHLKRKD--------SRTVYQYQYHKWKGEELPEKPKDLVDMIKsikqklPYKNSKHGRSVPIVVHCSD 151

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|..
gi 1658117674  967 GVGRTGTYIVLDSMLRQIKEQGTVNILGFLKHIRTQRNYLVQTEEQYIFIHD 1018
Cdd:cd14558    152 GSSRTGIFCALWNLLESAETEKVVDVFQVVKALRKQRPGMVSTLEQYQFLYD 203
R-PTP-D-2 cd14628
PTP-like domain of receptor-type tyrosine-protein phosphatase D, repeat 2; Receptor-type ...
 1029-1311 3.09e-44

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: 162.59  E-value: 3.09e-44
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658117674 1029 TEVHSSHIHTYVNELL-IPGPSGQTPLEKQFKMITQSNAKQCDYSAALKQCNRDKNRNSSLLPVERSRVHLSTTAG-EIS 1106
Cdd:cd14628      1 TEVPARNLYAYIQKLTqIETGENVTGMELEFKRLASSKAHTSRFISANLPCNKFKNRLVNIMPYESTRVCLQPIRGvEGS 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658117674 1107 DYINASYIMGYQQSNEFIITQNPLPSTMKDFWKMIWDHSTQVVIALPDGLDLAEDEC-IYWPTKsQPIRFDTFTVTFMGE 1185
Cdd:cd14628     81 DYINASFIDGYRQQKAYIATQGPLAETTEDFWRMLWEHNSTIVVMLTKLREMGREKChQYWPAE-RSARYQYFVVDPMAE 159

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658117674 1186 DHMclsneDMLIVQDFILEATQDDYVLEVRQYRAPRWPNPDGPISNTfELINIIKE-----ESVSRDGPIVVHDKRGGNI 1260
Cdd:cd14628    160 YNM-----PQYILREFKVTDARDGQSRTVRQFQFTDWPEQGVPKSGE-GFIDFIGQvhktkEQFGQDGPISVHCSAGVGR 233

                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|.
gi 1658117674 1261 AGTFCALMTLLHQLEMESSFDVYWVAKMINLMRPGIFTDIDQYQFLYKVIM 1311
Cdd:cd14628    234 TGVFITLSIVLERMRYEGVVDIFQTVKMLRTQRPAMVQTEDQYQFCYRAAL 284
R-PTPc-typeIIb-2 cd14556
PTP domain of type IIb (or R2B) subfamily receptor-type tyrosine-protein phosphatases, repeat ...
 813-1018 1.42e-43

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


Pssm-ID: 350404 [Multi-domain]  Cd Length: 201  Bit Score: 157.57  E-value: 1.42e-43
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658117674  813 YINANYVDGFTQPKAYIATQGPLKSSMEDFWRMVWEQNASVIVMItNLVEKGRRKCDQYWPLDSQEEYGSFLVTLRSTKV 892
Cdd:cd14556      1 YINAALLDSYKQPAAFIVTQHPLPNTVTDFWRLVYDYGCTSIVML-NQLDPKDQSCPQYWPDEGSGTYGPIQVEFVSTTI 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658117674  893 LAYYTQRTFTLKNTRakkgsqKEQTHERTVVQYHYTQWPDMG----VPEYTLPVLTFVRKsSQANLGNmGPVVVHCSAGV 968
Cdd:cd14556     80 DEDVISRIFRLQNTT------RPQEGYRMVQQFQFLGWPRDRdtppSKRALLKLLSEVEK-WQEQSGE-GPIVVHCLNGV 151

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|
gi 1658117674  969 GRTGTYIVLDSMLRQIKEQGTVNILGFLKHIRTQRNYLVQTEEQYIFIHD 1018
Cdd:cd14556    152 GRSGVFCAISSVCERIKVENVVDVFQAVKTLRNHRPNMVETEEQYKFCYD 201
COG5599 COG5599
Protein tyrosine phosphatase [Signal transduction mechanisms];
779-1016 5.19e-43

Protein tyrosine phosphatase [Signal transduction mechanisms];


Pssm-ID: 444335 [Multi-domain]  Cd Length: 282  Bit Score: 158.72  E-value: 5.19e-43
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658117674  779 PENKNKNRYINILAYDHSRVklsSSSDRngwsadYINANYVDGfTQPKAYIATQGPLKSSMEDFWRMVWEQNASVIVMIT 858
Cdd:COG5599     40 INGSPLNRFRDIQPYKETAL---RANLG------YLNANYIQV-IGNHRYIATQYPLEEQLEDFFQMLFDNNTPVLVVLA 109

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658117674  859 NLVE--KGRRKCDQYWPLDsqEEYGSFLVTLRSTKVLAYYTQ---RTFTLKntraKKGSQKEQtheRTVVQYHYTQWPDM 933
Cdd:COG5599    110 SDDEisKPKVKMPVYFRQD--GEYGKYEVSSELTESIQLRDGieaRTYVLT----IKGTGQKK---IEIPVLHVKNWPDH 180

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658117674  934 GVP--EYTLPVLTFVRKSSQANLGNMGPVVVHCSAGVGRTGTYIVLDSMLRQIKE--QGTVNILGFLKHIRTQRNY-LVQ 1008
Cdd:COG5599    181 GAIsaEALKNLADLIDKKEKIKDPDKLLPVVHCRAGVGRTGTLIACLALSKSINAlvQITLSVEEIVIDMRTSRNGgMVQ 260


                   ....*...
gi 1658117674 1009 TEEQYIFI 1016
Cdd:COG5599    261 TSEQLDVL 268
R-PTP-S-2 cd14627
PTP-like domain of receptor-type tyrosine-protein phosphatase S, repeat 2; Receptor-type ...
 1029-1311 7.47e-43

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: 158.74  E-value: 7.47e-43
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658117674 1029 TEVHSSHIHTYVNELLIPGPSGQ-TPLEKQFKMITQSNAKQCDYSAALKQCNRDKNRNSSLLPVERSRVHLSTTAG-EIS 1106
Cdd:cd14627      2 TEVPARNLYSYIQKLAQVEVGEHvTGMELEFKRLANSKAHTSRFISANLPCNKFKNRLVNIMPYETTRVCLQPIRGvEGS 81

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658117674 1107 DYINASYIMGYQQSNEFIITQNPLPSTMKDFWKMIWDHSTQVVIALPDGLDLAEDEC-IYWPTKsQPIRFDTFTVTFMGE 1185
Cdd:cd14627     82 DYINASFIDGYRQQKAYIATQGPLAETTEDFWRMLWENNSTIVVMLTKLREMGREKChQYWPAE-RSARYQYFVVDPMAE 160

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658117674 1186 DHMclsneDMLIVQDFILEATQDDYVLEVRQYRAPRWPNPDGPISNTfELINIIKE-----ESVSRDGPIVVHDKRGGNI 1260
Cdd:cd14627    161 YNM-----PQYILREFKVTDARDGQSRTVRQFQFTDWPEQGVPKSGE-GFIDFIGQvhktkEQFGQDGPISVHCSAGVGR 234

                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|.
gi 1658117674 1261 AGTFCALMTLLHQLEMESSFDVYWVAKMINLMRPGIFTDIDQYQFLYKVIM 1311
Cdd:cd14627    235 TGVFITLSIVLERMRYEGVVDIFQTVKMLRTQRPAMVQTEDEYQFCYQAAL 285
R-PTP-LAR-2 cd14554
PTP-like domain of the LAR family receptor-type tyrosine-protein phosphatases, repeat 2; The ...
 1078-1308 1.27e-42

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: 156.15  E-value: 1.27e-42
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658117674 1078 CNRDKNRNSSLLPVERSRVHLSTTAG-EISDYINASYIMGYQQSNEFIITQNPLPSTMKDFWKMIWDHSTQVVIALPDGL 1156
Cdd:cd14554      5 CNKFKNRLVNILPYESTRVCLQPIRGvEGSDYINASFIDGYRQRGAYIATQGPLAETTEDFWRMLWEHNSTIIVMLTKLR 84

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658117674 1157 DLAEDECI-YWPTKsQPIRFDTFTVTFMGEDHMclsneDMLIVQDFILEATQDDYVLEVRQYRAPRWPNPDGPISNTfEL 1235
Cdd:cd14554     85 EMGREKCHqYWPAE-RSARYQYFVVDPMAEYNM-----PQYILREFKVTDARDGQSRTVRQFQFTDWPEQGVPKSGE-GF 157

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1658117674 1236 INIIKE-----ESVSRDGPIVVHDKRGGNIAGTFCALMTLLHQLEMESSFDVYWVAKMINLMRPGIFTDIDQYQFLYK 1308
Cdd:cd14554    158 IDFIGQvhktkEQFGQEGPITVHCSAGVGRTGVFITLSIVLERMRYEGVVDVFQTVKLLRTQRPAMVQTEDQYQFCYR 235
PHA02742 PHA02742
protein tyrosine phosphatase; Provisional
 720-1015 3.61e-42

protein tyrosine phosphatase; Provisional


Pssm-ID: 165109 [Multi-domain]  Cd Length: 303  Bit Score: 157.09  E-value: 3.61e-42
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658117674  720 IGAPPSLALSAAENHEALPIKQFVKHVaelhdsntFSQEFEEIQACTVdlGITADSSIHPENKNKNRYINILAYDHSRVK 799
Cdd:PHA02742     1 MGAHCSKKNSFAKNCEQLIEESNLAEI--------LKEEHEHIMQEIV--AFSCNESLELKNMKKCRYPDAPCFDRNRVI 70

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658117674  800 LSSssdRNGWSaDYINANYVDGFTQPKAYIATQGPLKSSMEDFWRMVWEQNASVIVMITNLVEKGRRKCDQYWPLD--SQ 877
Cdd:PHA02742    71 LKI---EDGGD-DFINASYVDGHNAKGRFICTQAPLEETALDFWQAIFQDQVRVIVMITKIMEDGKEACYPYWMPHerGK 146

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658117674  878 EEYGSFLVTLRSTKVLAYYTQRTFTLKNTRAkkGSQKEQTHertvvqYHYTQWPDMGVPEYTLPVLTFVRKSSQA----- 952
Cdd:PHA02742   147 ATHGEFKIKTKKIKSFRNYAVTNLCLTDTNT--GASLDIKH------FAYEDWPHGGLPRDPNKFLDFVLAVREAdlkad 218

                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1658117674  953 ------NLGNMGPVVVHCSAGVGRTGTYIVLDSMLRQIKEQGTVNILGFLKHIRTQRNYLVQTEEQYIF 1015
Cdd:PHA02742   219 vdikgeNIVKEPPILVHCSAGLDRAGAFCAIDICISKYNERAIIPLLSIVRDLRKQRHNCLSLPQQYIF 287
R-PTP-F-2 cd14629
PTP-like domain of receptor-type tyrosine-protein phosphatase F, repeat 2; Receptor-type ...
 1029-1311 1.04e-41

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: 155.27  E-value: 1.04e-41
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658117674 1029 TEVHSSHIHTYVNEL-LIPGPSGQTPLEKQFKMITQSNAKQCDYSAALKQCNRDKNRNSSLLPVERSRVHLSTTAG-EIS 1106
Cdd:cd14629      2 TEVPARNLYAHIQKLtQVPPGESVTAMELEFKLLANSKAHTSRFISANLPCNKFKNRLVNIMPYELTRVCLQPIRGvEGS 81

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658117674 1107 DYINASYIMGYQQSNEFIITQNPLPSTMKDFWKMIWDHSTQVVIALPDGLDLAEDEC-IYWPTKsQPIRFDTFTVTFMGE 1185
Cdd:cd14629     82 DYINASFIDGYRQQKAYIATQGPLAETTEDFWRMLWEHNSTIVVMLTKLREMGREKChQYWPAE-RSARYQYFVVDPMAE 160

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658117674 1186 DHMclsneDMLIVQDFILEATQDDYVLEVRQYRAPRWPNPDGPISNTfELINIIKE-----ESVSRDGPIVVHDKRGGNI 1260
Cdd:cd14629    161 YNM-----PQYILREFKVTDARDGQSRTIRQFQFTDWPEQGVPKTGE-GFIDFIGQvhktkEQFGQDGPITVHCSAGVGR 234

                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|.
gi 1658117674 1261 AGTFCALMTLLHQLEMESSFDVYWVAKMINLMRPGIFTDIDQYQFLYKVIM 1311
Cdd:cd14629    235 TGVFITLSIVLERMRYEGVVDMFQTVKTLRTQRPAMVQTEDQYQLCYRAAL 285
alpha_CA_IX cd03150
Carbonic anhydrase alpha, isozyme IX. Carbonic anhydrases (CAs) are zinc-containing enzymes ...
 48-293 1.40e-40

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: 150.49  E-value: 1.40e-40
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658117674   48 NQNNWAKKYPSCNNAKQSPINIDDDLSQVKMQFQKLKLEGFEQETSNTTTIHNDGKTVAINLNDEYYISGGGLRSrFKVG 127
Cdd:cd03150      1 GQPPWPSVSPACAGRFQSPVDIRPHLVAFCPALRPLELLGFDLPPSPSLRLLNNGHTVQLSLPSGLRMALGPGQE-YRAL 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658117674  128 RITFHWGQcnASSDGSEHSLDGIKFPLEMQIYGYEAhKFQSLDSALKDGGRLTALSVLFEVSAEDNENYVAIIDGVKTVT 207
Cdd:cd03150     80 QLHLHWGA--AGRPGSEHTVDGHRFPAEIHVVHLST-AFANLDEALGRPGGLAVLAAFLAEGLHENSAYEQLLSRLSEIS 156

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658117674  208 RLGKTAVLEPFSLLGLLPNSTEKYYIYNGSLTTPPCSETVEWIVFRNTVDISDVQLETFCEVMTMQQAgyvmlmDYLQNN 287
Cdd:cd03150    157 EEESETVVPGLDVSALLPSDLSRYFRYEGSLTTPPCAQGVIWTVFNQTVRLSAKQLHTLSDSLWGPHD------SRLQLN 230


                   ....*.
gi 1658117674  288 FREQQL 293
Cdd:cd03150    231 FRATQP 236
PTPc-N21 cd14598
catalytic domain of tyrosine-protein phosphatase non-receptor type 21; Tyrosine-protein ...
 813-1022 2.91e-40

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: 148.58  E-value: 2.91e-40
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658117674  813 YINANYVDGFTQPKA--YIATQGPLKSSMEDFWRMVWEQNASVIVMITNLVEKGRRKCDQYWP-LDSQEE---YGSFLVT 886
Cdd:cd14598      1 YINASHIKVTVGGKEwdYIATQGPLQNTCQDFWQMVWEQGVAIIAMVTAEEEGGREKSFRYWPrLGSRHNtvtYGRFKIT 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658117674  887 LRSTKVLAYYTQRTFTLKNTRAKKgsqkeqthERTVVQYHYTQWPDMGVPEYTLPVLTF------VRKSSQANLGNMG-- 958
Cdd:cd14598     81 TRFRTDSGCYATTGLKIKHLLTGQ--------ERTVWHLQYTDWPEHGCPEDLKGFLSYleeiqsVRRHTNSTIDPKSpn 152

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1658117674  959 -PVVVHCSAGVGRTGTYIVLDSMLRQIKEQGTVNILGFLKHIRTQRNYLVQTEEQYIFIHDALVE 1022
Cdd:cd14598    153 pPVLVHCSAGVGRTGVVILSEIMIACLEHNEMLDIPRVLDMLRQQRMMMVQTLSQYTFVYKVLIQ 217
R3-PTPc cd14548
catalytic domain of R3 subfamily receptor-type tyrosine-protein phosphatases and similar ...
 1084-1308 5.22e-40

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: 147.89  E-value: 5.22e-40
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658117674 1084 RNSSLLPVERSRVHLSTTAGEI-SDYINASYIMGYQQSNEFIITQNPLPSTMKDFWKMIWDHSTQVVIALPDGLDLAEDE 1162
Cdd:cd14548      1 RYTNILPYDHSRVKLIPINEEEgSDYINANYIPGYNSPREFIATQGPLPGTKDDFWRMVWEQNSHTIVMLTQCMEKGRVK 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658117674 1163 CI-YWPTKSQPIRFDTFTVTFMGEDHMclsneDMLIVQDFILEatQDDYVLEVRQYRAPRWPN---PDGPISntfeLINI 1238
Cdd:cd14548     81 CDhYWPFDQDPVYYGDITVTMLSESVL-----PDWTIREFKLE--RGDEVRSVRQFHFTAWPDhgvPEAPDS----LLRF 149

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1658117674 1239 IK---EESVSRDGPIVVHDKRGGNIAGTFCALMTLLHQLEMESSFDVYWVAKMINLMRPGIFTDIDQYQFLYK 1308
Cdd:cd14548    150 VRlvrDYIKQEKGPTIVHCSAGVGRTGTFIALDRLLQQIESEDYVDIFGIVYDLRKHRPLMVQTEAQYIFLHQ 222
PTPc_motif smart00404
Protein tyrosine phosphatase, catalytic domain motif;
921-1022 1.80e-39

Protein tyrosine phosphatase, catalytic domain motif;


Pssm-ID: 214649 [Multi-domain]  Cd Length: 105  Bit Score: 142.11  E-value: 1.80e-39
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658117674   921 TVVQYHYTQWPDMGVPEYTLPVLTFVR--KSSQANLGNMGPVVVHCSAGVGRTGTYIVLDSMLRQI-KEQGTVNILGFLK 997
Cdd:smart00404    1 TVKHYHYTGWPDHGVPESPDSILELLRavKKNLNQSESSGPVVVHCSAGVGRTGTFVAIDILLQQLeAEAGEVDIFDTVK 80

                            90       100
                    ....*....|....*....|....*
gi 1658117674   998 HIRTQRNYLVQTEEQYIFIHDALVE 1022
Cdd:smart00404   81 ELRSQRPGMVQTEEQYLFLYRALLE 105
PTPc_DSPc smart00012
Protein tyrosine phosphatase, catalytic domain, undefined specificity; Protein tyrosine ...
 921-1022 1.80e-39

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


Pssm-ID: 214469 [Multi-domain]  Cd Length: 105  Bit Score: 142.11  E-value: 1.80e-39
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658117674   921 TVVQYHYTQWPDMGVPEYTLPVLTFVR--KSSQANLGNMGPVVVHCSAGVGRTGTYIVLDSMLRQI-KEQGTVNILGFLK 997
Cdd:smart00012    1 TVKHYHYTGWPDHGVPESPDSILELLRavKKNLNQSESSGPVVVHCSAGVGRTGTFVAIDILLQQLeAEAGEVDIFDTVK 80

                            90       100
                    ....*....|....*....|....*
gi 1658117674   998 HIRTQRNYLVQTEEQYIFIHDALVE 1022
Cdd:smart00012   81 ELRSQRPGMVQTEEQYLFLYRALLE 105
R-PTPc-A-E-2 cd14552
catalytic domain of receptor-type tyrosine-protein phosphatase A and E, repeat 2; ...
 1108-1310 3.08e-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: 142.02  E-value: 3.08e-38
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658117674 1108 YINASYIMGYQQSNEFIITQNPLPSTMKDFWKMIWDHSTQVVIALPDGLDLAEDEC-IYWPTKSQpIRFDTFTVTFMGEd 1186
Cdd:cd14552      1 YINASFIDGYRQKDAYIATQGPLDHTVEDFWRMIWEWKSCSIVMLTEIKERSQNKCaQYWPEDGS-VSSGDITVELKDQ- 78

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658117674 1187 hmclSNEDMLIVQDFILEATQDDYVLEVRQYRAPRWPNPDGPiSNTFELINII----KEESVSRDGPIVVHDKRGGNIAG 1262
Cdd:cd14552     79 ----TDYEDYTLRDFLVTKGKGGSTRTVRQFHFHGWPEVGIP-DNGKGMIDLIaavqKQQQQSGNHPITVHCSAGAGRTG 153

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*...
gi 1658117674 1263 TFCALMTLLHQLEMESSFDVYWVAKMINLMRPGIFTDIDQYQFLYKVI 1310
Cdd:cd14552    154 TFCALSTVLERVKAEGVLDVFQVVKSLRLQRPHMVQTLEQYEFCYKVV 201
R-PTPc-H cd14619
catalytic domain of receptor-type tyrosine-protein phosphatase H; Receptor-type ...
 1083-1314 5.94e-38

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: 142.34  E-value: 5.94e-38
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658117674 1083 NRNSSLLPVERSRVHLSTT-AGEISDYINASYIMGYQQSNEFIITQNPLPSTMKDFWKMIWDHSTQVVIALPDGLDLAED 1161
Cdd:cd14619      1 NRFRNVLPYDWSRVPLKPIhEEPGSDYINANYMPGYWSSQEFIATQGPLPQTVGDFWRMIWEQQSSTIVMLTNCMEAGRV 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658117674 1162 EC-IYWPTKSQPIRFDTFTVTFMGEDHMclsneDMLIVQDFILEATQDDYVLEVRQYRAPRWPNPDGPiSNTFELI---N 1237
Cdd:cd14619     81 KCeHYWPLDYTPCTYGHLRVTVVSEEVM-----ENWTVREFLLKQVEEQKTLSVRHFHFTAWPDHGVP-SSTDTLLafrR 154

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1658117674 1238 IIKE--ESVSRDGPIVVHDKRGGNIAGTFCALMTLLHQLEMESSFDVYWVAKMINLMRPGIFTDIDQYQFLYKVIMSLV 1314
Cdd:cd14619    155 LLRQwlDQTMSGGPTVVHCSAGVGRTGTLIALDVLLQQLQSEGLLGPFSFVQKMRENRPLMVQTESQYVFLHQCILDFL 233
R-PTPc-V cd14618
catalytic domain of receptor-type tyrosine-protein phosphatase V; Receptor-type ...
 1083-1311 6.81e-38

catalytic domain of receptor-type tyrosine-protein phosphatase V; Receptor-type tyrosine-protein phosphatase V (PTPRV or R-PTP-V), also known as embryonic stem cell protein-tyrosine phosphatase (ES cell phosphatase) or osteotesticular protein-tyrosine phosphatase (OST-PTP), belongs to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. PTPRV is a member of the R3 subfamily of receptor-type phosphotyrosine phosphatases (RPTP), characterized by a unique modular composition consisting of multiple extracellular fibronectin type III (FN3) repeats and a single (most RPTP subtypes have two) cytoplasmic catalytic PTP domain. In rodents, it may play a role in the maintenance of pluripotency and may function in signaling pathways during bone remodeling. It is the only PTP whose function has been lost between rodent and human. The human OST-PTP gene is a pseudogene.


Pssm-ID: 350466 [Multi-domain]  Cd Length: 230  Bit Score: 142.00  E-value: 6.81e-38
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658117674 1083 NRNSSLLPVERSRVHLSTTAGEI-SDYINASYIMGYQQSNEFIITQNPLPSTMKDFWKMIWDHSTQVVIALPDGLDLAED 1161
Cdd:cd14618      1 NRYPHVLPYDHSRVRLSQLGGEPhSDYINANFIPGYTSPQEFIATQGPLKKTIEDFWRLVWEQQVCNIIMLTVGMENGRV 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658117674 1162 ECI-YWPTKSQPIRFDTFTVTFMGEdhmclSNEDMLIVQDFILEATQDDYVLEVRQYRAPRWPN---PDGPiSNTFELIN 1237
Cdd:cd14618     81 LCDhYWPSESTPVSYGHITVHLLAQ-----SSEDEWTRREFKLWHEDLRKERRVKHLHYTAWPDhgiPEST-SSLMAFRE 154

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1658117674 1238 IIKEE--SVSRDGPIVVHDKRGGNIAGTFCALMTLLHQLEMESSFDVYWVAKMINLMRPGIFTDIDQYQFLYKVIM 1311
Cdd:cd14618    155 LVREHvqATKGKGPTLVHCSAGVGRSGTFIALDRLLRQLKEEKVVDVFNTVYILRMHRYLMIQTLSQYIFLHSCIL 230
R-PTPc-J cd14615
catalytic domain of receptor-type tyrosine-protein phosphatase J; Receptor-type ...
 1083-1311 1.03e-37

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: 141.49  E-value: 1.03e-37
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658117674 1083 NRNSSLLPVERSRVHLSTTAGEISDYINASYIMGYQQSNEFIITQNPLPSTMKDFWKMIWDHSTQVVIALPDGLDLAEDE 1162
Cdd:cd14615      1 NRYNNVLPYDISRVKLSVQSHSTDDYINANYMPGYNSKKEFIAAQGPLPNTVKDFWRMVWEKNVYAIVMLTKCVEQGRTK 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658117674 1163 C-IYWPTKsQPIRFDTFTVTfmgedhmcLSNEDML---IVQDFILEATQDDYVLEVRQYRAPRWpnPDGPISNTFELI-- 1236
Cdd:cd14615     81 CeEYWPSK-QKKDYGDITVT--------MTSEIVLpewTIRDFTVKNAQTNESRTVRHFHFTSW--PDHGVPETTDLLin 149

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1658117674 1237 --NIIKE--ESVSRDGPIVVHDKRGGNIAGTFCALMTLLHQLEMESSFDVYWVAKMINLMRPGIFTDIDQYQFLYKVIM 1311
Cdd:cd14615    150 frHLVREymKQNPPNSPILVHCSAGVGRTGTFIAIDRLIYQIENENVVDVYGIVYDLRMHRPLMVQTEDQYVFLNQCAL 228
R-PTP-C-2 cd14558
PTP-like domain of receptor-type tyrosine-protein phosphatase C, repeat 2; Receptor-type ...
 1108-1307 3.67e-37

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: 139.06  E-value: 3.67e-37
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658117674 1108 YINASYIMGYQQSNEFIITQNPLPSTMKDFWKMIWDHSTQVVIALPDGLDLAEDECI-YWPTKSQpirfdtftvTFmGED 1186
Cdd:cd14558      1 YINASFIDGYWGPKSLIATQGPLPDTIADFWQMIFQKKVKVIVMLTELKEGDQEQCAqYWGDEKK---------TY-GDI 70

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658117674 1187 HMCLSNEDM---LIVQDFILEATQDDYVLEVRQYRAPRWpNPDGPISNTFELINIIKE---------ESVSRDGPIVVHD 1254
Cdd:cd14558     71 EVELKDTEKsptYTVRVFEITHLKRKDSRTVYQYQYHKW-KGEELPEKPKDLVDMIKSikqklpyknSKHGRSVPIVVHC 149

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|...
gi 1658117674 1255 KRGGNIAGTFCALMTLLHQLEMESSFDVYWVAKMINLMRPGIFTDIDQYQFLY 1307
Cdd:cd14558    150 SDGSSRTGIFCALWNLLESAETEKVVDVFQVVKALRKQRPGMVSTLEQYQFLY 202
R-PTPc-E-2 cd14622
catalytic domain of receptor-type tyrosine-protein phosphatase E, repeat 2; Receptor-type ...
 1107-1310 1.06e-36

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: 137.83  E-value: 1.06e-36
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658117674 1107 DYINASYIMGYQQSNEFIITQNPLPSTMKDFWKMIWDHSTQVVIALPDGLDLAEDECI-YWPTKSqpirfdtfTVTFmGE 1185
Cdd:cd14622      1 DYINASFIDGYRQKDYFIATQGPLAHTVEDFWRMVWEWKCHTIVMLTELQEREQEKCVqYWPSEG--------SVTH-GE 71

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658117674 1186 DHMCLSNE---DMLIVQDFILEATQDDYVLEVRQYRAPRWPNPDGPiSNTFELINII----KEESVSRDGPIVVHDKRGG 1258
Cdd:cd14622     72 ITIEIKNDtllETISIRDFLVTYNQEKQTRLVRQFHFHGWPEIGIP-AEGKGMIDLIaavqKQQQQTGNHPIVVHCSAGA 150

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|..
gi 1658117674 1259 NIAGTFCALMTLLHQLEMESSFDVYWVAKMINLMRPGIFTDIDQYQFLYKVI 1310
Cdd:cd14622    151 GRTGTFIALSNILERVKAEGLLDVFQTVKSLRLQRPHMVQTLEQYEFCYRVV 202
R-PTPc-A-2 cd14623
catalytic domain of receptor-type tyrosine-protein phosphatase A, repeat 2; Receptor-type ...
 1088-1310 1.19e-35

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: 135.56  E-value: 1.19e-35
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658117674 1088 LLPVERSRVHLSTTAGEI-SDYINASYIMGYQQSNEFIITQNPLPSTMKDFWKMIWDHSTQVVIALPDGLDLAEDECI-Y 1165
Cdd:cd14623      5 IIPYEFNRVIIPVKRGEEnTDYVNASFIDGYRQKDSYIASQGPLQHTIEDFWRMIWEWKSCSIVMLTELEERGQEKCAqY 84

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658117674 1166 WPTKSQpIRFDTFTVTFMGEDHmCLSnedmLIVQDFILEATQDDYVLEVRQYRAPRWPNPDGPiSNTFELINII----KE 1241
Cdd:cd14623     85 WPSDGS-VSYGDITIELKKEEE-CES----YTVRDLLVTNTRENKSRQIRQFHFHGWPEVGIP-SDGKGMINIIaavqKQ 157

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1658117674 1242 ESVSRDGPIVVHDKRGGNIAGTFCALMTLLHQLEMESSFDVYWVAKMINLMRPGIFTDIDQYQFLYKVI 1310
Cdd:cd14623    158 QQQSGNHPITVHCSAGAGRTGTFCALSTVLERVKAEGILDVFQTVKSLRLQRPHMVQTLEQYEFCYKVV 226
alpha_CA_VI cd03125
Carbonic anhydrase alpha, isozyme VI. Carbonic anhydrases (CAs) are zinc-containing enzymes ...
 48-292 1.31e-35

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: 136.07  E-value: 1.31e-35
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658117674   48 NQNNWAKKYPSCNNAKQSPINIDDDLSQVKMQFQKLKLEGFEQETSnTTTIHNDGKTVAINLNDEYYISGGgLRSRFKVG 127
Cdd:cd03125      1 DESHWPEKYPACGGKRQSPIDIQRREVRFNPSLLQLELVGYEKEQG-EFTMTNNGHTVQIDLPPTMSITTG-DGTVYTAV 78

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658117674  128 RITFHWGQCNASSDGSEHSLDGIKFPLEMQIYGYEAhKFQSLDSALKDGGRLTALSVLFEVSAE-DNENYVAIIDGVKTV 206
Cdd:cd03125     79 QMHFHWGGRDSEISGSEHTIDGMRYVAELHIVHYNS-KYKSYEEAKDKPDGLAVLAFLYKVGHYaENTYYSDFISKLAKI 157

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658117674  207 TRLGKTAVLEPFSLLGLLPNSTEKYYIYNGSLTTPPCSETVEWIVFRNTVDISDVQLETFCEVmtmqqagyvmLMDY--- 283
Cdd:cd03125    158 KYAGQTTTLTSLDVRDMLPENLHHYYTYQGSLTTPPCTENVLWFVFDDPVTLSKTQIVKLENT----------LMDHhnk 227

                          250
                   ....*....|
gi 1658117674  284 -LQNNFREQQ 292
Cdd:cd03125    228 tIRNDYRRTQ 237
R-PTPc-typeIIb-2 cd14556
PTP domain of type IIb (or R2B) subfamily receptor-type tyrosine-protein phosphatases, repeat ...
 1108-1307 2.13e-35

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: 134.07  E-value: 2.13e-35
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658117674 1108 YINASYIMGYQQSNEFIITQNPLPSTMKDFWKMIWDHSTQVVIALPDgLDLAEDECI-YWPTKSQPiRFDTFTVTFMGED 1186
Cdd:cd14556      1 YINAALLDSYKQPAAFIVTQHPLPNTVTDFWRLVYDYGCTSIVMLNQ-LDPKDQSCPqYWPDEGSG-TYGPIQVEFVSTT 78

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658117674 1187 hmclsNEDMLIVQDFILEAT---QDDYVLeVRQYRAPRWP-NPDGPIS--NTFELINII-KEESVSRDGPIVVHDKRGGN 1259
Cdd:cd14556     79 -----IDEDVISRIFRLQNTtrpQEGYRM-VQQFQFLGWPrDRDTPPSkrALLKLLSEVeKWQEQSGEGPIVVHCLNGVG 152

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*...
gi 1658117674 1260 IAGTFCALMTLLHQLEMESSFDVYWVAKMINLMRPGIFTDIDQYQFLY 1307
Cdd:cd14556    153 RSGVFCAISSVCERIKVENVVDVFQAVKTLRNHRPNMVETEEQYKFCY 200
Cah COG3338
Carbonic anhydrase [Inorganic ion transport and metabolism];
36-266 3.71e-33

Carbonic anhydrase [Inorganic ion transport and metabolism];


Pssm-ID: 442567 [Multi-domain]  Cd Length: 247  Bit Score: 129.23  E-value: 3.71e-33
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658117674   36 KEDIDWSYAGTLNQNNWAK---KYPSCNNAK-QSPINIDD----DLSQVKMQFQKLKLEgfeqetsntttIHNDGKTVAI 107
Cdd:COG3338     23 ASAPHWSYEGETGPEHWGElspEFATCATGKnQSPIDIRTaikaDLPPLKFDYKPTPLE-----------IVNNGHTIQV 91

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658117674  108 NLNDEYYISGGGlrSRFKVGRITFHwgqcnassDGSEHSLDGIKFPLEMQIygyeAHKfqsldsalKDGGRLTALSVLFE 187
Cdd:COG3338     92 NVDPGSTLTVDG--KRYELKQFHFH--------TPSEHTINGKSYPMEAHL----VHK--------DADGELAVVGVLFE 149

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658117674  188 VSAEdNENYVAIIDGVKTvtRLGKTAVL-EPFSLLGLLPNSTEkYYIYNGSLTTPPCSETVEWIVFRNTVDISDVQLETF 266
Cdd:COG3338    150 EGAE-NPALAKLWANLPL--EAGEEVALdATIDLNDLLPEDRS-YYRYSGSLTTPPCSEGVLWIVLKQPITVSAEQIEAF 225
PTPc-N18 cd14603
catalytic domain of tyrosine-protein phosphatase non-receptor type 18; Tyrosine-protein ...
 1056-1313 7.03e-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: 128.79  E-value: 7.03e-33
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658117674 1056 KQFKMI-TQSNAKQCDYS----AALKQCNRDKNRNSSLLPVERSRVHLSTTAGEI-SDYINASYIMGYQQSNEFIITQNP 1129
Cdd:cd14603      2 GEFSEIrACSAAFKADYVcstvAGGRKENVKKNRYKDILPYDQTRVILSLLQEEGhSDYINANFIKGVDGSRAYIATQGP 81

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658117674 1130 LPSTMKDFWKMIWDHSTQVVIALPDGLDLAEDEC-IYWPTKSQPIRFDTFTVTFMGEDHMclsNEDmLIVQDFILEATQD 1208
Cdd:cd14603     82 LSHTVLDFWRMIWQYGVKVILMACREIEMGKKKCeRYWAQEQEPLQTGPFTITLVKEKRL---NEE-VILRTLKVTFQKE 157

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658117674 1209 DYVLEVRQYRAprWPN---PDGPiSNTFELINIIKEESVSRDGPIVVHDKRGGNIAGTFCAL---MTLLHQLEMESSFDV 1282
Cdd:cd14603    158 SRSVSHFQYMA--WPDhgiPDSP-DCMLAMIELARRLQGSGPEPLCVHCSAGCGRTGVICTVdyvRQLLLTQRIPPDFSI 234

                          250       260       270
                   ....*....|....*....|....*....|.
gi 1658117674 1283 YWVAKMINLMRPGIFTDIDQYQFLYKVIMSL 1313
Cdd:cd14603    235 FDVVLEMRKQRPAAVQTEEQYEFLYHTVAQM 265
R5-PTP-2 cd14550
PTP-like domain of R5 subfamily receptor-type tyrosine-protein phosphatases, repeat 2; The R5 ...
 813-1016 1.79e-32

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


Pssm-ID: 350398 [Multi-domain]  Cd Length: 200  Bit Score: 125.51  E-value: 1.79e-32
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658117674  813 YINANYVDGFTQPKAYIATQGPLKSSMEDFWRMVWEQNASVIVMITNLVEKGrrKCDQYWPLDSQE-EYGSFLVTLRSTK 891
Cdd:cd14550      1 YINASYLQGYRRSNEFIITQHPLEHTIKDFWQMIWDHNSQTIVMLTDNELNE--DEPIYWPTKEKPlECETFKVTLSGED 78

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658117674  892 VLAY-----YTQRTFTLKNTrakkgsqkEQTHERTVVQYHYTQWPDMGVPEYTlpVLTFVRKSSQANLGNMGPVVVHCSA 966
Cdd:cd14550     79 HSCLsneirLIVRDFILEST--------QDDYVLEVRQFQCPSWPNPCSPIHT--VFELINTVQEWAQQRDGPIVVHDRY 148

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|
gi 1658117674  967 GVGRTGTYIVLDSMLRQIKEQGTVNILGFLKHIRTQRNYLVQTEEQYIFI 1016
Cdd:cd14550    149 GGVQAATFCALTTLHQQLEHESSVDVYQVAKLYHLMRPGVFTSKEDYQFL 198
R-PTPc-O cd14614
catalytic domain of receptor-type tyrosine-protein phosphatase O; Receptor-type ...
 1079-1310 2.74e-32

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: 126.54  E-value: 2.74e-32
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658117674 1079 NRDKNRNSSLLPVERSRVHL-STTAGEISDYINASYIMGYQQSNEFIITQNPLPSTMKDFWKMIWDHSTQVVIALPDGLD 1157
Cdd:cd14614     12 NRCKNRYTNILPYDFSRVKLvSMHEEEGSDYINANYIPGYNSPQEYIATQGPLPETRNDFWKMVLQQKSQIIVMLTQCNE 91

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658117674 1158 LAEDECI-YWPTKSQPIRFDTFTVTFMGEdhmclSNEDMLIVQDFILeaTQDDYVLEVRQYRAPRWPNPDGPISNTFE-- 1234
Cdd:cd14614     92 KRRVKCDhYWPFTEEPVAYGDITVEMLSE-----EEQPDWAIREFRV--SYADEVQDVMHFNYTAWPDHGVPTANAAEsi 164

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1658117674 1235 --LINIIKEESVSRDGPIVVHDKRGGNIAGTFCALMTLLHQLEMESSFDVYWVAKMINLMRPGIFTDIDQYQFLYKVI 1310
Cdd:cd14614    165 lqFVQMVRQQAVKSKGPMIIHCSAGVGRTGTFIALDRLLQHIRDHEFVDILGLVSEMRSYRMSMVQTEEQYIFIHQCV 242
alpha_CA_prokaryotic_like cd03124
Carbonic anhydrase alpha, prokaryotic-like subfamily. Carbonic anhydrases (CAs) are ...
 51-270 4.74e-32

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: 124.69  E-value: 4.74e-32
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658117674   51 NWA---KKYPSCNNAK-QSPINIDDDLSQVKmqfqklKLEGFEQETSNTT-TIHNDGKTVAINLNDEyyisGGGLR---S 122
Cdd:cd03124      4 HWGnldPEFALCATGKnQSPIDITTKAVVSD------KLPPLNYNYKPTSaTLVNNGHTIQVNFEGN----GGTLTidgE 73

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658117674  123 RFKVGRITFHwgqcnassDGSEHSLDGIKFPLEMQIygyeAHKfqsldsalKDGGRLTALSVLFEVSAEdNENYVAIIDG 202
Cdd:cd03124     74 TYQLLQFHFH--------SPSEHLINGKRYPLEAHL----VHK--------SKDGQLAVVAVLFEEGKE-NPFLKKILDN 132

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1658117674  203 VKTVTrLGKTAVLEPFSLLGLLPNSTeKYYIYNGSLTTPPCSETVEWIVFRNTVDISDVQLETFCEVM 270
Cdd:cd03124    133 MPKKE-GTEVNLPAILDPNELLPESR-SYYRYEGSLTTPPCSEGVRWIVLKQPITISKEQLAKFRAAV 198
R-PTPc-T-2 cd14634
PTP domain of receptor-type tyrosine-protein phosphatase T, repeat 2; Receptor-type ...
 813-1022 1.54e-31

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


Pssm-ID: 350482 [Multi-domain]  Cd Length: 206  Bit Score: 123.21  E-value: 1.54e-31
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658117674  813 YINANYVDGFTQPKAYIATQGPLKSSMEDFWRMVWEQNASVIVMITNLveKGRRKCDQYWPLDSQEEYGSFLVTLRSTKV 892
Cdd:cd14634      1 YINAALMDSHKQPAAFIVTQHPLPNTVADFWRLVFDYNCSSVVMLNEM--DAAQLCMQYWPEKTSCCYGPIQVEFVSADI 78

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658117674  893 LAYYTQRTFTLKNTrakkgsQKEQTHERTVVQYHYTQWPDM-GVPEYTLPVLTFVR---KSSQANLGNMGPVVVHCSAGV 968
Cdd:cd14634     79 DEDIISRIFRICNM------ARPQDGYRIVQHLQYIGWPAYrDTPPSKRSILKVVRrleKWQEQYDGREGRTVVHCLNGG 152

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....
gi 1658117674  969 GRTGTYIVLDSMLRQIKEQGTVNILGFLKHIRTQRNYLVQTEEQYIFIHDALVE 1022
Cdd:cd14634    153 GRSGTFCAICSVCEMIQQQNIIDVFHTVKTLRNNKSNMVETLEQYKFVYEVALE 206
alpha_CA_I_II_III_XIII cd03119
Carbonic anhydrase alpha, isozymes I, II, and III and XIII. Carbonic anhydrases (CAs) are ...
 40-266 2.32e-31

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: 124.47  E-value: 2.32e-31
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658117674   40 DWSYAGTLNQNNWAKKYPSCNNAKQSPINIDDDLSQVKMQFQKLKlegFEQETSNTTTIHNDGKTVAINLNDEYYIS--- 116
Cdd:cd03119      4 HWGYDSHNGPEHWHELFPIAKGDRQSPIDIKTKDAKHDPSLKPLS---VSYDPATAKTILNNGHSFNVEFDDTDDRSvlr 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658117674  117 GGGLRSRFKVGRITFHWGQCNasSDGSEHSLDGIKFPLEMQIYGYEAhKFQSLDSALKDGGRLTALSVLFEVSAEdNENY 196
Cdd:cd03119     81 GGPLTGSYRLRQFHFHWGSSD--DHGSEHTVDGVKYAAELHLVHWNS-KYGSFGEAAKQPDGLAVVGVFLKVGEA-NPEL 156

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658117674  197 VAIIDGVKTVTRLGKTAVLEPFSLLGLLPNSTEkYYIYNGSLTTPPCSETVEWIVFRNTVDISDVQLETF 266
Cdd:cd03119    157 QKVLDALDSIKTKGKQAPFTNFDPSCLLPASLD-YWTYPGSLTTPPLLECVTWIVLKEPISVSSEQMAKF 225
PTPc-N9 cd14543
catalytic domain of tyrosine-protein phosphatase non-receptor type 9; Tyrosine-protein ...
 1071-1308 1.13e-30

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: 122.47  E-value: 1.13e-30
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658117674 1071 YSAALKQCNRDKNRNSSLLPVERSRVHLSTTAG-EISDYINASYIMGYQQSNEFIITQNPLPSTMKDFWKMIWDHSTQVV 1149
Cdd:cd14543     21 FLCSLAPANQEKNRYGDVLCLDQSRVKLPKRNGdERTDYINANFMDGYKQKNAYIATQGPLPKTYSDFWRMVWEQKVLVI 100

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658117674 1150 IALPDGLDLAEDEC-IYWP-TKSQPIRFDTFTVTFMG----EDHM---------------CLSNEDMLIVQDFIL---EA 1205
Cdd:cd14543    101 VMTTRVVERGRVKCgQYWPlEEGSSLRYGDLTVTNLSvenkEHYKkttleihntetdesrQVTHFQFTSWPDFGVpssAA 180

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658117674 1206 TQDDYVLEVRQYRA-------PRWP-NPDGPisntfeliniikeesvsrdgPIVVHDKRGGNIAGTFCALMTLLHQLEME 1277
Cdd:cd14543    181 ALLDFLGEVRQQQAlavkamgDRWKgHPPGP--------------------PIVVHCSAGIGRTGTFCTLDICLSQLEDV 240

                          250       260       270
                   ....*....|....*....|....*....|.
gi 1658117674 1278 SSFDVYWVAKMINLMRPGIFTDIDQYQFLYK 1308
Cdd:cd14543    241 GTLNVMQTVRRMRTQRAFSIQTPDQYYFCYK 271
R-PTPc-LAR-1 cd14553
catalytic domain of LAR family receptor-type tyrosine-protein phosphatases, repeat 1; The LAR ...
 1077-1315 1.85e-29

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: 118.27  E-value: 1.85e-29
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658117674 1077 QCNRDKNRNSSLLPVERSRVHLSTTAG-EISDYINASYIMGYQQSNEFIITQNPLPSTMKDFWKMIWDHSTQVVIALPDG 1155
Cdd:cd14553      1 EVNKPKNRYANVIAYDHSRVILQPIEGvPGSDYINANYCDGYRKQNAYIATQGPLPETFGDFWRMVWEQRSATIVMMTKL 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658117674 1156 LDLAEDEC-IYWPTKSQPIrFDTFTVTFMgeDHMCLSNedmLIVQDFILEATQDDYVLEVRQYRAPRWPN---PDGPISn 1231
Cdd:cd14553     81 EERSRVKCdQYWPTRGTET-YGLIQVTLL--DTVELAT---YTVRTFALHKNGSSEKREVRQFQFTAWPDhgvPEHPTP- 153

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658117674 1232 TFELINIIKEESVSRDGPIVVHDKRGGNIAGTFCALMTLLHQLEMESSFDVYWVAKMINLMRPGIFTDIDQYQFLYKVIM 1311
Cdd:cd14553    154 FLAFLRRVKACNPPDAGPIVVHCSAGVGRTGCFIVIDSMLERIKHEKTVDIYGHVTCLRAQRNYMVQTEDQYIFIHDALL 233


                   ....
gi 1658117674 1312 SLVA 1315
Cdd:cd14553    234 EAVT 237
R-PTPc-B cd14617
catalytic domain of receptor-type tyrosine-protein phosphatase B; Receptor-type ...
 1083-1308 1.95e-29

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


Pssm-ID: 350465 [Multi-domain]  Cd Length: 228  Bit Score: 117.71  E-value: 1.95e-29
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658117674 1083 NRNSSLLPVERSRVHLSTTAGE-ISDYINASYIMGYQQSNEFIITQNPLPSTMKDFWKMIWDHSTQVVIALPDGLDLAED 1161
Cdd:cd14617      1 NRYNNILPYDSTRVKLSNVDDDpCSDYINASYIPGNNFRREYIATQGPLPGTKDDFWKMVWEQNVHNIVMVTQCVEKGRV 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658117674 1162 ECI-YWPTKSQPIRFDTFTVTFMGEdhmclSNEDMLIVQDF-ILEATQDDYVLEVRQYRAPRWPNPDGPiSNTFELINII 1239
Cdd:cd14617     81 KCDhYWPADQDSLYYGDLIVQMLSE-----SVLPEWTIREFkICSEEQLDAPRLVRHFHYTVWPDHGVP-ETTQSLIQFV 154

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1658117674 1240 K--EESVSRD---GPIVVHDKRGGNIAGTFCALMTLLHQLEMESSFDVYWVAKMINLMRPGIFTDIDQYQFLYK 1308
Cdd:cd14617    155 RtvRDYINRTpgsGPTVVHCSAGVGRTGTFIALDRILQQLDSKDSVDIYGAVHDLRLHRVHMVQTECQYVYLHQ 228
R-PTPc-A-1 cd14621
catalytic domain of receptor-type tyrosine-protein phosphatase A, repeat 1; Receptor-type ...
 1068-1311 2.40e-29

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


Pssm-ID: 350469 [Multi-domain]  Cd Length: 296  Bit Score: 119.74  E-value: 2.40e-29
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658117674 1068 QCDYSAALKQCNRDKNRNSSLLPVERSRVHLSTTAG-EISDYINASYIMGYQQSNEFIITQNPLPSTMKDFWKMIWDHST 1146
Cdd:cd14621     41 QATCEAASKEENKEKNRYVNILPYDHSRVHLTPVEGvPDSDYINASFINGYQEKNKFIAAQGPKEETVNDFWRMIWEQNT 120

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658117674 1147 QVVIALPDGLDLAEDECI-YWPtksqpirfDTFTVTFmgeDHMCLSNEDMLIVQDFIL---------EATQDDYVLEVRQ 1216
Cdd:cd14621    121 ATIVMVTNLKERKECKCAqYWP--------DQGCWTY---GNIRVSVEDVTVLVDYTVrkfciqqvgDVTNKKPQRLITQ 189

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658117674 1217 YRAPRWPN---PDGPISnTFELINIIKEESVSRDGPIVVHDKRGGNIAGTFCALMTLLHQLEMESSFDVYWVAKMINLMR 1293
Cdd:cd14621    190 FHFTSWPDfgvPFTPIG-MLKFLKKVKNCNPQYAGAIVVHCSAGVGRTGTFIVIDAMLDMMHAERKVDVYGFVSRIRAQR 268

                          250
                   ....*....|....*...
gi 1658117674 1294 PGIFTDIDQYQFLYKVIM 1311
Cdd:cd14621    269 CQMVQTDMQYVFIYQALL 286
R-PTPc-Q cd14616
catalytic domain of receptor-type tyrosine-protein phosphatase Q; Receptor-type ...
 1083-1308 4.85e-29

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: 116.54  E-value: 4.85e-29
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658117674 1083 NRNSSLLPVERSRVHLSTTAGEI-SDYINASYIMGYQQSNEFIITQNPLPSTMKDFWKMIWDHSTQVVIALPDGLDLAED 1161
Cdd:cd14616      1 NRFPNIKPYNNNRVKLIADAGVPgSDYINASYISGYLCPNEFIATQGPLPGTVGDFWRMVWETRAKTIVMLTQCFEKGRI 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658117674 1162 EC-IYWPTKSQPIR-FDTFTVTFMGEDhmclsNEDMLIVQDFILEaTQDDYVLeVRQYRAPRWPNPDGPiSNTFELINII 1239
Cdd:cd14616     81 RChQYWPEDNKPVTvFGDIVITKLMED-----VQIDWTIRDLKIE-RHGDYMM-VRQCNFTSWPEHGVP-ESSAPLIHFV 152

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1658117674 1240 KEESVSRDG---PIVVHDKRGGNIAGTFCALMTLLHQLEMESSFDVYWVAKMINLMRPGIFTDIDQYQFLYK 1308
Cdd:cd14616    153 KLVRASRAHdntPMIVHCSAGVGRTGVFIALDHLTQHINDHDFVDIYGLVAELRSERMCMVQNLAQYIFLHQ 224
PTP_fungal cd18533
fungal protein tyrosine phosphatases; This subfamily contains Saccharomyces cerevisiae ...
 1108-1307 7.34e-29

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: 115.42  E-value: 7.34e-29
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658117674 1108 YINASYI-MGYQQSNEFIITQNPLPSTMKDFWKMIWDHSTQVVIALPDGLDLAEDEC-IYWPTKSQPIRFDTFTVTFMGE 1185
Cdd:cd18533      1 YINASYItLPGTSSKRYIATQGPLPATIGDFWKMIWQNNVGVIVMLTPLVENGREKCdQYWPSGEYEGEYGDLTVELVSE 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658117674 1186 DHmclsNEDM-LIVQDFILeATQDDYVLEVRQYRAPRWPN---PDGPISnTFELINIIKE--ESVSRDGPIVVHDKRGGN 1259
Cdd:cd18533     81 EE----NDDGgFIVREFEL-SKEDGKVKKVYHIQYKSWPDfgvPDSPED-LLTLIKLKRElnDSASLDPPIIVHCSAGVG 154

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 1658117674 1260 IAGTFCALMTLLHQLEMESSFDVYW------VAKMINLM---RPGIFTDIDQYQFLY 1307
Cdd:cd18533    155 RTGTFIALDSLLDELKRGLSDSQDLedsedpVYEIVNQLrkqRMSMVQTLRQYIFLY 211
alpha_CA_VII cd03149
Carbonic anhydrase alpha, CA isozyme VII_like subgroup. Carbonic anhydrases (CAs) are ...
 63-292 8.67e-29

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: 116.09  E-value: 8.67e-29
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658117674   63 KQSPINIDDDLSQVKMQFQKLKLEgFEQETSntTTIHNDGKTVAINLND---EYYISGGGLRSRFKVGRITFHWGQcnAS 139
Cdd:cd03149      3 RQSPIDIVSSEAVYDPKLKPLSLS-YDPCTS--LSISNNGHSVMVEFDDsddKTVITGGPLENPYRLKQFHFHWGA--KH 77

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658117674  140 SDGSEHSLDGIKFPLEMQIYGYEAHKFQSLDSALKDGGRLTALSVLFEVSAEdNENYVAIIDGVKTVTRLGKTAVLEPFS 219
Cdd:cd03149     78 GSGSEHTVDGKTFPSELHLVHWNAKKYKSFGEAAAAPDGLAVLGVFLETGDE-HPGLNRLTDALYMVRFKGTKAQFLDFN 156

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1658117674  220 LLGLLPNSTEkYYIYNGSLTTPPCSETVEWIVFRNTVDISDVQLETFCEVMTMQQAGYVMLMdylQNNFREQQ 292
Cdd:cd03149    157 PKCLLPKSLD-YWTYPGSLTTPPLNESVTWIVLKEPIPVSEKQMGKFRELLFTSEEDQRNHM---VNNFRPPQ 225
PTPc-N22 cd14602
catalytic domain of tyrosine-protein phosphatase non-receptor type 22; Tyrosine-protein ...
 1082-1313 1.43e-28

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: 115.32  E-value: 1.43e-28
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658117674 1082 KNRNSSLLPVERSRVHLS-TTAGEISDYINASYIMGYQQSNEFIITQNPLPSTMKDFWKMIWDHSTQVVIALPDGLDLAE 1160
Cdd:cd14602      1 KNRYKDILPYDHSRVELSlITSDEDSDYINANFIKGVYGPRAYIATQGPLSTTLLDFWRMIWEYSVLIIVMACMEFEMGK 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658117674 1161 DEC-IYWP-TKSQPIRFDTFTVTFMGEDhmclsNEDMLIVQdfILEATQDDYVLEVRQYRAPRWPNPDGP--ISNTFELI 1236
Cdd:cd14602     81 KKCeRYWAePGEMQLEFGPFSVTCEAEK-----RKSDYIIR--TLKVKFNSETRTIYQFHYKNWPDHDVPssIDPILELI 153

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658117674 1237 NIIKEESVSRDGPIVVHDKRGGNIAGTFCAL---MTLLHQLEMESSFDVYWVAKMINLMRPGIFTDIDQYQFLYKVIMSL 1313
Cdd:cd14602    154 WDVRCYQEDDSVPICIHCSAGCGRTGVICAIdytWMLLKDGIIPENFSVFSLIQEMRTQRPSLVQTKEQYELVYNAVIEL 233
alpha_CARP_X_XI_like cd03121
Carbonic anhydrase alpha related protein: groups X, XI and related proteins. This subgroup ...
 59-292 1.82e-28

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: 115.97  E-value: 1.82e-28
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658117674   59 CNNAK-QSPINIDDDlsqvKMQFQ----KLKLEGFEQETSnttTIHNDGKTVAINLNDEY--YISGGGLRSRFKVGRITF 131
Cdd:cd03121     15 CSKGRrQSPVDIEPS----RLLFDpfltPLRIDTGRKVSG---TFYNTGRHVSFRPDKDPvvNISGGPLSYRYRLEEIRL 87

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658117674  132 HWGQCNasSDGSEHSLDGIKFPLEMQIYGYEAHKFQSLDSALKDGGRLTALSVLFEVSAEDNE--NYVAIIDGVKTVTRL 209
Cdd:cd03121     88 HFGRED--EQGSEHTVNGQAFPGEVQLIHYNSELYPNFSEASKSPNGLVIVSLFVKIGETSNPelRRLTNRDTITSIRYK 165

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658117674  210 GKTAVLEPFSLLGLLPNsTEKYYIYNGSLTTPPCSETVEWIVFRNTVDISDVQLEtfcEVMTMQQAGYVMLMDYLQNNFR 289
Cdd:cd03121    166 GDAYFLQDLSIELLLPE-TDHYITYEGSLTSPGCHETVTWIILNKPIYITKEQMH---SLRLLSQNSPSQEKAPMSPNFR 241


                   ...
gi 1658117674  290 EQQ 292
Cdd:cd03121    242 PVQ 244
PTPc-KIM cd14547
catalytic domain of the kinase interaction motif (KIM) family of protein-tyrosine phosphatases; ...
 1083-1307 2.59e-28

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: 114.42  E-value: 2.59e-28
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658117674 1083 NRNSSLLPVERSRVHL-STTAGEISDYINASYIMGYQQSNE-FIITQNPLPSTMKDFWKMIWDHSTQVVIALPDgLDLAE 1160
Cdd:cd14547      1 NRYKTILPNEHSRVCLpSVDDDPLSSYINANYIRGYDGEEKaYIATQGPLPNTVADFWRMVWQEKTPIIVMITN-LTEAK 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658117674 1161 DECI-YWPTKsQPIRFDTFTVTFMGEDHmclsnEDMLIVQDFILEatqddYVLEVR---QYRAPRWPN---PD--GPISN 1231
Cdd:cd14547     80 EKCAqYWPEE-ENETYGDFEVTVQSVKE-----TDGYTVRKLTLK-----YGGEKRylkHYWYTSWPDhktPEaaQPLLS 148

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1658117674 1232 TFELINIIKEESVSRdGPIVVHDKRGGNIAGTFCALMTLLHQLEMESSFDVYWVAKMINLMRPGIFTDIDQYQFLY 1307
Cdd:cd14547    149 LVQEVEEARQTEPHR-GPIVVHCSAGIGRTGCFIATSIGCQQLREEGVVDVLGIVCQLRLDRGGMVQTAEQYEFVH 223
PTPc-N12 cd14604
catalytic domain of tyrosine-protein phosphatase non-receptor type 12; Tyrosine-protein ...
 1076-1317 3.63e-28

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: 116.19  E-value: 3.63e-28
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658117674 1076 KQCNRDKNRNSSLLPVERSRVHLS-TTAGEISDYINASYIMGYQQSNEFIITQNPLPSTMKDFWKMIWDHSTQVVIALPD 1154
Cdd:cd14604     54 KEENVKKNRYKDILPFDHSRVKLTlKTSSQDSDYINANFIKGVYGPKAYIATQGPLANTVIDFWRMIWEYNVAIIVMACR 133

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658117674 1155 GLDLAEDEC-IYWPT-KSQPIRFDTFTVTFMGEDhmclSNEDMLIvQDFILEATQDDYvlEVRQYRAPRWPNPDGPIS-- 1230
Cdd:cd14604    134 EFEMGRKKCeRYWPLyGEEPMTFGPFRISCEAEQ----ARTDYFI-RTLLLEFQNETR--RLYQFHYVNWPDHDVPSSfd 206

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658117674 1231 NTFELINIIKEESVSRDGPIVVHDKRGGNIAGTFCAL---MTLLHQLEMESSFDVYWVAKMINLMRPGIFTDIDQYQFLY 1307
Cdd:cd14604    207 SILDMISLMRKYQEHEDVPICIHCSAGCGRTGAICAIdytWNLLKAGKIPEEFNVFNLIQEMRTQRHSAVQTKEQYELVH 286

                          250
                   ....*....|
gi 1658117674 1308 KVIMSLVAKK 1317
Cdd:cd14604    287 RAIAQLFEKQ 296
R-PTPc-M-1 cd14633
catalytic domain of receptor-type tyrosine-protein phosphatase M, repeat 1; Receptor-type ...
 1071-1311 4.14e-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: 115.14  E-value: 4.14e-28
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658117674 1071 YSAALKQCNRDKNRNSSLLPVERSRVHLSTTAGEI-SDYINASYIMGYQQSNEFIITQNPLPSTMKDFWKMIWDHSTQVV 1149
Cdd:cd14633     32 WDSAKKDENRMKNRYGNIIAYDHSRVRLQPIEGETsSDYINGNYIDGYHRPNHYIATQGPMQETIYDFWRMVWHENTASI 111

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658117674 1150 IALPDGLDLAEDECI-YWPTKSQPIRfdTFTVTFMGEDHMClsnedMLIVQDFILEATQDDYVLEVRQYRAPRWPNPDGP 1228
Cdd:cd14633    112 IMVTNLVEVGRVKCCkYWPDDTEIYK--DIKVTLIETELLA-----EYVIRTFAVEKRGVHEIREIRQFHFTGWPDHGVP 184

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658117674 1229 ISNT--FELINIIKEESVSRDGPIVVHDKRGGNIAGTFCALMTLLHQLEMESSFDVYWVAKMINLMRPGIFTDIDQYQFL 1306
Cdd:cd14633    185 YHATglLGFVRQVKSKSPPNAGPLVVHCSAGAGRTGCFIVIDIMLDMAEREGVVDIYNCVRELRSRRVNMVQTEEQYVFI 264


                   ....*
gi 1658117674 1307 YKVIM 1311
Cdd:cd14633    265 HDAIL 269
R-PTPc-F-1 cd14626
catalytic domain of receptor-type tyrosine-protein phosphatase F, repeat 1; Receptor-type ...
 1077-1311 6.41e-28

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: 114.75  E-value: 6.41e-28
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658117674 1077 QCNRDKNRNSSLLPVERSRVHLSTTAG-EISDYINASYIMGYQQSNEFIITQNPLPSTMKDFWKMIWDHSTQVVIALPDG 1155
Cdd:cd14626     39 EVNKPKNRYANVIAYDHSRVILTSVDGvPGSDYINANYIDGYRKQNAYIATQGPLPETLSDFWRMVWEQRTATIVMMTRL 118

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658117674 1156 LDLAEDEC-IYWPTKSQPIrFDTFTVTFMgeDHMCLSNedmLIVQDFILEATQDDYVLEVRQYRAPRWPN---PDGPiSN 1231
Cdd:cd14626    119 EEKSRVKCdQYWPIRGTET-YGMIQVTLL--DTVELAT---YSVRTFALYKNGSSEKREVRQFQFMAWPDhgvPEYP-TP 191

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658117674 1232 TFELINIIKEESVSRDGPIVVHDKRGGNIAGTFCALMTLLHQLEMESSFDVYWVAKMINLMRPGIFTDIDQYQFLYKVIM 1311
Cdd:cd14626    192 ILAFLRRVKACNPPDAGPMVVHCSAGVGRTGCFIVIDAMLERMKHEKTVDIYGHVTCMRSQRNYMVQTEDQYIFIHEALL 271
PTPc-N11_6 cd14544
catalytic domain of tyrosine-protein phosphatase non-receptor type 11 and type 6; ...
 1079-1310 9.49e-28

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: 113.71  E-value: 9.49e-28
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658117674 1079 NRDKNRNSSLLPVERSRVHL----STTAGeiSDYINASYIM-------GYQQSNEFIITQNPLPSTMKDFWKMIWDHSTQ 1147
Cdd:cd14544      1 NKGKNRYKNILPFDHTRVILkdrdPNVPG--SDYINANYIRnenegptTDENAKTYIATQGCLENTVSDFWSMVWQENSR 78

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658117674 1148 VVIALPDGLDLAEDECI-YWPTKSQPIRFDTFTVTFMGEDhmclSNEDMlIVQDFILEAT-QDDYVLEVRQYRAPRWPN- 1224
Cdd:cd14544     79 VIVMTTKEVERGKNKCVrYWPDEGMQKQYGPYRVQNVSEH----DTTDY-TLRELQVSKLdQGDPIREIWHYQYLSWPDh 153

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658117674 1225 --PDGP--ISNTFELINiIKEESVSRDGPIVVHDKRGGNIAGTFCALMTLLHQLE---MESSFDVYWVAKMINLMRPGIF 1297
Cdd:cd14544    154 gvPSDPggVLNFLEDVN-QRQESLPHAGPIVVHCSAGIGRTGTFIVIDMLLDQIKrkgLDCDIDIQKTIQMVRSQRSGMV 232

                          250
                   ....*....|...
gi 1658117674 1298 TDIDQYQFLYKVI 1310
Cdd:cd14544    233 QTEAQYKFIYVAV 245
R-PTPc-G-1 cd17667
catalytic domain of receptor-type tyrosine-protein phosphatase G, repeat 1; Receptor-type ...
 1079-1314 1.13e-27

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: 113.98  E-value: 1.13e-27
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658117674 1079 NRDKNRNSSLLPVERSRVHLSTTAGEIS---DYINASYIMGYQQSNEFIITQNPLPSTMKDFWKMIWDHSTQVVIALPDG 1155
Cdd:cd17667     27 NKHKNRYINILAYDHSRVKLRPLPGKDSkhsDYINANYVDGYNKAKAYIATQGPLKSTFEDFWRMIWEQNTGIIVMITNL 106

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658117674 1156 LDLAEDEC-IYWPTKSQPiRFDTFTVTFMGED-HMCLSnedmliVQDFILEATQDDYVLE-----------VRQYRAPRW 1222
Cdd:cd17667    107 VEKGRRKCdQYWPTENSE-EYGNIIVTLKSTKiHACYT------VRRFSIRNTKVKKGQKgnpkgrqnertVIQYHYTQW 179

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658117674 1223 PNPDGPiSNTFELINIIKEESVSRD---GPIVVHDKRGGNIAGTFCALMTLLHQLEMESSFDVYWVAKMINLMRPGIFTD 1299
Cdd:cd17667    180 PDMGVP-EYALPVLTFVRRSSAARTpemGPVLVHCSAGVGRTGTYIVIDSMLQQIKDKSTVNVLGFLKHIRTQRNYLVQT 258

                          250
                   ....*....|....*
gi 1658117674 1300 IDQYQFLYKVIMSLV 1314
Cdd:cd17667    259 EEQYIFIHDALLEAI 273
R-PTPc-T-1 cd14630
catalytic domain of receptor-type tyrosine-protein phosphatase T, repeat 1; Receptor-type ...
 1079-1311 1.15e-27

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: 112.81  E-value: 1.15e-27
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658117674 1079 NRDKNRNSSLLPVERSRVHLSTTAGEI-SDYINASYIMGYQQSNEFIITQNPLPSTMKDFWKMIWDHSTQVVIALPDGLD 1157
Cdd:cd14630      3 NRNKNRYGNIISYDHSRVRLQLLDGDPhSDYINANYIDGYHRPRHYIATQGPMQETVKDFWRMIWQENSASVVMVTNLVE 82

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658117674 1158 LAEDECI-YWPTKSQPirFDTFTVTFMGEDHMClsnedMLIVQDFILEATQDDYVLEVRQYRAPRWPNPDGPISNT--FE 1234
Cdd:cd14630     83 VGRVKCVrYWPDDTEV--YGDIKVTLIETEPLA-----EYVIRTFTVQKKGYHEIREIRQFHFTSWPDHGVPCYATglLG 155

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1658117674 1235 LINIIKEESVSRDGPIVVHDKRGGNIAGTFCALMTLLHQLEMESSFDVYWVAKMINLMRPGIFTDIDQYQFLYKVIM 1311
Cdd:cd14630    156 FVRQVKFLNPPDAGPIVVHCSAGAGRTGCFIAIDIMLDMAENEGVVDIFNCVRELRAQRVNMVQTEEQYVFVHDAIL 232
R-PTPc-S-1 cd14625
catalytic domain of receptor-type tyrosine-protein phosphatase S, repeat 1; Receptor-type ...
 1077-1315 2.83e-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: 2.83e-27
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658117674 1077 QCNRDKNRNSSLLPVERSRVHLSTTAGEI-SDYINASYIMGYQQSNEFIITQNPLPSTMKDFWKMIWDHSTQVVIALPDG 1155
Cdd:cd14625     45 EVNKPKNRYANVIAYDHSRVILQPIEGIMgSDYINANYIDGYRKQNAYIATQGPLPETFGDFWRMVWEQRSATVVMMTKL 124

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658117674 1156 LDLAEDEC-IYWPTKSQPIrFDTFTVTFMgeDHMCLSNedmLIVQDFILEATQDDYVLEVRQYRAPRWPNPDGPISNT-- 1232
Cdd:cd14625    125 EEKSRIKCdQYWPSRGTET-YGMIQVTLL--DTIELAT---FCVRTFSLHKNGSSEKREVRQFQFTAWPDHGVPEYPTpf 198

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658117674 1233 FELINIIKEESVSRDGPIVVHDKRGGNIAGTFCALMTLLHQLEMESSFDVYWVAKMINLMRPGIFTDIDQYQFLYKVIMS 1312
Cdd:cd14625    199 LAFLRRVKTCNPPDAGPIVVHCSAGVGRTGCFIVIDAMLERIKHEKTVDIYGHVTLMRSQRNYMVQTEDQYSFIHDALLE 278


                   ...
gi 1658117674 1313 LVA 1315
Cdd:cd14625    279 AVA 281
PTPc-N13 cd14597
catalytic domain of tyrosine-protein phosphatase non-receptor type 13; Tyrosine-protein ...
 1079-1311 4.05e-27

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: 111.08  E-value: 4.05e-27
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658117674 1079 NRDKNRNSSLLPVERSRVHLsttaGEISDYINASYIMGYQQSNEF--IITQNPLPSTMKDFWKMIWDHSTQVVIALPDGL 1156
Cdd:cd14597      3 NRKKNRYKNILPYDTTRVPL----GDEGGYINASFIKMPVGDEEFvyIACQGPLPTTVADFWQMVWEQKSTVIAMMTQEV 78

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658117674 1157 DLAEDECI-YWPtksqpirfDTFTVTFMGEDHMCLSNEDMLIVQDFI-----LEATQDDYVLEVRQYRAPRWPNPDGPiS 1230
Cdd:cd14597     79 EGGKIKCQrYWP--------EILGKTTMVDNRLQLTLVRMQQLKNFVirvleLEDIQTREVRHITHLNFTAWPDHDTP-S 149

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658117674 1231 NTFELINIIK-EESVSRDGPIVVHDKRGGNIAGTFCALMTLLHQLEMESSFDVYWVAKMINLMRPGIFTDIDQYQFLYKV 1309
Cdd:cd14597    150 QPEQLLTFISyMRHIHKSGPIITHCSAGIGRSGTLICIDVVLGLISKDLDFDISDIVRTMRLQRHGMVQTEDQYIFCYQV 229


                   ..
gi 1658117674 1310 IM 1311
Cdd:cd14597    230 IL 231
alpha_CARP_VIII cd03120
Carbonic anhydrase alpha related protein, group VIII. Carbonic anhydrase related proteins ...
 52-292 6.62e-27

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: 111.10  E-value: 6.62e-27
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658117674   52 WAKKYPSCNNAKQSPINIDDDLSQVKMQFQKLKLEGFEQETSNTTTIhNDGKTVAINLNDEYYISGGGL--RSRFKVGRI 129
Cdd:cd03120      4 WGLLFPEANGEYQSPINLNSREARYDPSLLEVRLSPNYVVCRDCEVI-NDGHTIQIILKSKSVLSGGPLpqGHEFELAEV 82

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658117674  130 TFHWGQCNasSDGSEHSLDGIKFPLEMQIYGYEAHKFQSLDSALKDGGRLTALSVLFEVSAEdNENYVAIIDGVKTVTRL 209
Cdd:cd03120     83 RFHWGREN--QRGSEHTVNFKAFPMELHLIHWNSTLYSSLEEAMGKPHGIAIIALFVQIGKE-HVGLKAVTEILQDIQYK 159

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658117674  210 GKTAVLEPFSLLGLLPNSTEK-YYIYNGSLTTPPCSETVEWIVFRNTVDISDVQLETFCEVMT-MQQAGYVMLMDY-LQN 286
Cdd:cd03120    160 GKSKTIPCFNPNTLLPDPLLRdYWVYEGSLTTPPCSEGVTWILFRYPLTISQSQIEEFRRLRThVKGAELVEGCDGlLGD 239


                   ....*.
gi 1658117674  287 NFREQQ 292
Cdd:cd03120    240 NFRPTQ 245
R-PTPc-E-1 cd14620
catalytic domain of receptor-type tyrosine-protein phosphatase E, repeat 1; Receptor-type ...
 1087-1311 9.87e-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: 110.03  E-value: 9.87e-27
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658117674 1087 SLLPVERSRVHLSTTAGEI-SDYINASYIMGYQQSNEFIITQNPLPSTMKDFWKMIWDHSTQVVIALPDGLDLAEDECI- 1164
Cdd:cd14620      3 NILPYDHSRVILSQLDGIPcSDYINASYIDGYKEKNKFIAAQGPKQETVNDFWRMVWEQKSATIVMLTNLKERKEEKCYq 82

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658117674 1165 YWPTKSQPIrfdtftvtfMGEDHMCLsnEDMLIVQDFILEATQDDYVLEvRQYRAPR---------WPN---PDGPISnT 1232
Cdd:cd14620     83 YWPDQGCWT---------YGNIRVAV--EDCVVLVDYTIRKFCIQPQLP-DGCKAPRlvtqlhftsWPDfgvPFTPIG-M 149

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1658117674 1233 FELINIIKEESVSRDGPIVVHDKRGGNIAGTFCALMTLLHQLEMESSFDVYWVAKMINLMRPGIFTDIDQYQFLYKVIM 1311
Cdd:cd14620    150 LKFLKKVKSVNPVHAGPIVVHCSAGVGRTGTFIVIDAMIDMMHAEQKVDVFEFVSRIRNQRPQMVQTDMQYSFIYQALL 228
R5-PTPc-1 cd14549
catalytic domain of R5 subfamily receptor-type tyrosine-protein phosphatases, repeat 1; The R5 ...
 1108-1307 1.55e-26

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: 108.59  E-value: 1.55e-26
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658117674 1108 YINASYIMGYQQSNEFIITQNPLPSTMKDFWKMIWDHSTQVVIALPDGLDLAEDEC-IYWPTKSQPiRFDTFTVTFMGED 1186
Cdd:cd14549      1 YINANYVDGYNKARAYIATQGPLPSTFDDFWRMVWEQNSAIIVMITNLVERGRRKCdQYWPKEGTE-TYGNIQVTLLSTE 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658117674 1187 HM--------CLSNEDmlivqdfILEATQDDYVLEVRQYRAPRWPN---PDGPISntfeLINIIKEESVSRD---GPIVV 1252
Cdd:cd14549     80 VLatytvrtfSLKNLK-------LKKVKGRSSERVVYQYHYTQWPDhgvPDYTLP----VLSFVRKSSAANPpgaGPIVV 148

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1658117674 1253 HDKRGGNIAGTFCALMTLLHQLEMESSFDVYWVAKMINLMRPGIFTDIDQYQFLY 1307
Cdd:cd14549    149 HCSAGVGRTGTYIVIDSMLQQIQDKGTVNVFGFLKHIRTQRNYLVQTEEQYIFIH 203
R-PTP-N2 cd14610
PTP-like domain of receptor-type tyrosine-protein phosphatase N2; Receptor-type ...
 1054-1320 1.89e-26

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: 110.92  E-value: 1.89e-26
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658117674 1054 LEKQFKMITQSNAKQCDYSAALKQCNRDKNRNSSLLPVERSRVHLST-TAGEISDYINASYIMGYQQSN-EFIITQNPLP 1131
Cdd:cd14610     19 LEKEWEALCAYQAEPNATNVAQREENVQKNRSLAVLPYDHSRIILKAeNSHSHSDYINASPIMDHDPRNpAYIATQGPLP 98

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658117674 1132 STMKDFWKMIWDHSTQVVIALPdglDLAED---ECI-YWPTKSQPIrFDTFTVTFMGEDHMClsnEDMLiVQDFILEATQ 1207
Cdd:cd14610     99 ATVADFWQMVWESGCVVIVMLT---PLAENgvkQCYhYWPDEGSNL-YHIYEVNLVSEHIWC---EDFL-VRSFYLKNLQ 170

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658117674 1208 DDYVLEVRQYRAPRWPNPDGPiSNTFELINIIKEESV---SRDGPIVVHDKRGGNIAGTFCALMTLLHQL-EMESSFDVY 1283
Cdd:cd14610    171 TNETRTVTQFHFLSWNDQGVP-ASTRSLLDFRRKVNKcyrGRSCPIIVHCSDGAGRSGTYILIDMVLNKMaKGAKEIDIA 249

                          250       260       270
                   ....*....|....*....|....*....|....*..
gi 1658117674 1284 WVAKMINLMRPGIFTDIDQYQFlykvimSLVAKKEEV 1320
Cdd:cd14610    250 ATLEHLRDQRPGMVQTKEQFEF------ALTAVAEEV 280
alpha_CA_V cd03118
Carbonic anhydrase alpha, CA isozyme V_like subgroup. Carbonic anhydrases (CAs) are ...
 63-303 5.60e-26

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: 108.01  E-value: 5.60e-26
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658117674   63 KQSPINIDDDLSQVKMQFQKLKLEgfeQETSNTTTIHNDGKTVAINLND---EYYISGGGLRSRFKVGRITFHWGQCNAS 139
Cdd:cd03118      3 RQSPINIQWRDSVYDPQLAPLRVS---YDPATCLYIWNNGYSFQVEFDDstdKSGISGGPLENHYRLKQFHFHWGANNEW 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658117674  140 sdGSEHSLDGIKFPLEMQIYGYEAHKFQSLDSALKDGGRLTALSVLFEVSAEdNENYVAIIDGVKTVTRLGKTAVLEPFS 219
Cdd:cd03118     80 --GSEHTVDGHTYPAELHLVHWNSVKYENFEEAVMEENGLAVIGVFLKLGAH-HEGLQKLVDALPEVRHKDTVVEFNPFD 156

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658117674  220 LLGLLPNSTEkYYIYNGSLTTPPCSETVEWIVFRNTVDISDVQLETFcEVMTMQQAGYVmlMDYLQNNFREQQLKFVGQV 299
Cdd:cd03118    157 PSCLLPACRD-YWTYPGSLTTPPLTESVTWIIQKQPIEVSPSQLSVF-RTLLFTSRGEE--EKVMVNNFRPLQPLMNRKV 232


                   ....
gi 1658117674  300 FSSY 303
Cdd:cd03118    233 RSSF 236
R-PTPc-K-2 cd14636
PTP domain of receptor-type tyrosine-protein phosphatase K, repeat 2; Receptor-type ...
 813-1022 7.65e-26

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: 106.65  E-value: 7.65e-26
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658117674  813 YINANYVDGFTQPKAYIATQGPLKSSMEDFWRMVWEQNASVIVMITNL-VEKGrrkCDQYWPLDSQEEYGSFLVTLRSTK 891
Cdd:cd14636      1 YINAALMDSYRQPAAFIVTQHPLPNTVKDFWRLVYDYGCTSIVMLNEVdLAQG---CPQYWPEEGMLRYGPIQVECMSCS 77

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658117674  892 VLAYYTQRTFTLKN-TRAKKGSQkeqtherTVVQYHYTQWPDM----GVPEYTLPVLTFVRKSSQANLGNMGPVVVHCSA 966
Cdd:cd14636     78 MDCDVISRIFRICNlTRPQEGYL-------MVQQFQYLGWASHrevpGSKRSFLKLILQVEKWQEECDEGEGRTIIHCLN 150

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 1658117674  967 GVGRTGTYIVLDSMLRQIKEQGTVNILGFLKHIRTQRNYLVQTEEQYIFIHDALVE 1022
Cdd:cd14636    151 GGGRSGMFCAISIVCEMIKRQNVVDVFHAVKTLRNSKPNMVETPEQYRFCYDVALE 206
R-PTPc-K-1 cd14631
catalytic domain of receptor-type tyrosine-protein phosphatase K, repeat 1; Receptor-type ...
 1106-1311 7.92e-26

catalytic domain of receptor-type tyrosine-protein phosphatase K, repeat 1; Receptor-type tyrosine-protein phosphatase K (PTPRK), also known as receptor-type tyrosine-protein phosphatase kappa (RPTP-kappa or PTPkappa), belongs to the type IIb subfamily of receptor protein tyrosine phosphatases (RPTPs), which belong to the larger family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. PTPRK is widely expressed and has been shown to stimulate cell motility and neurite outgrowth. It is required for anti-proliferative and pro-migratory effects of TGF-beta, suggesting a role in regulation, maintenance, and restoration of cell adhesion. It is a potential tumour suppressor in primary central nervous system lymphomas, colorectal cancer, and breast cancer. It contains an extracellular region with an Meprin-A5 (neuropilin)-mu (MAM) domain, an immunoglobulin (Ig) domain, and four fibronectin type III (FN3) repeats, a transmembrane domain, and an intracellular segment with a juxtamembrane domain similar to the cytoplasmic domain of classical cadherins and two tandem PTP domains. This model represents the first (repeat 1) PTP domain.


Pssm-ID: 350479 [Multi-domain]  Cd Length: 218  Bit Score: 107.03  E-value: 7.92e-26
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658117674 1106 SDYINASYIMGYQQSNEFIITQNPLPSTMKDFWKMIWDHSTQVVIALPDGLDLAEDECI-YWPTKSQpiRFDTFTVTFMG 1184
Cdd:cd14631     13 SDYINANYIDGYQRPSHYIATQGPVHETVYDFWRMIWQEQSACIVMVTNLVEVGRVKCYkYWPDDTE--VYGDFKVTCVE 90

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658117674 1185 EDHMClsnedMLIVQDFILEATQDDYVLEVRQYRAPRWPNPDGPISNT--FELINIIKEESVSRDGPIVVHDKRGGNIAG 1262
Cdd:cd14631     91 MEPLA-----EYVVRTFTLERRGYNEIREVKQFHFTGWPDHGVPYHATglLSFIRRVKLSNPPSAGPIVVHCSAGAGRTG 165

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*....
gi 1658117674 1263 TFCALMTLLHQLEMESSFDVYWVAKMINLMRPGIFTDIDQYQFLYKVIM 1311
Cdd:cd14631    166 CYIVIDIMLDMAEREGVVDIYNCVKALRSRRINMVQTEEQYIFIHDAIL 214
PHA02746 PHA02746
protein tyrosine phosphatase; Provisional
 1072-1310 8.45e-26

protein tyrosine phosphatase; Provisional


Pssm-ID: 165113 [Multi-domain]  Cd Length: 323  Bit Score: 109.73  E-value: 8.45e-26
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658117674 1072 SAALKQCNRDKNRNSSLLPVERSRVHLS--------------------TTAGEISDYINASYIMGYQQSNEFIITQNPLP 1131
Cdd:PHA02746    44 NHFLKKENLKKNRFHDIPCWDHSRVVINaheslkmfdvgdsdgkkievTSEDNAENYIHANFVDGFKEANKFICAQGPKE 123

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658117674 1132 STMKDFWKMIWDHSTQVVIALPDGLDLAEDECIYWPT-KSQPIRFDTFTVTFMGEDHMCLSNEDMLIVQDFILEATQddy 1210
Cdd:PHA02746   124 DTSEDFFKLISEHESQVIVSLTDIDDDDEKCFELWTKeEDSELAFGRFVAKILDIIEELSFTKTRLMITDKISDTSR--- 200

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658117674 1211 vlEVRQYRAPRWP---NPDGPiSNTFELINIIKEESV----------SRDGPIVVHDKRGGNIAGTFCALMTLLHQLEME 1277
Cdd:PHA02746   201 --EIHHFWFPDWPdngIPTGM-AEFLELINKVNEEQAelikqadndpQTLGPIVVHCSAGIGRAGTFCAIDNALEQLEKE 277

                          250       260       270
                   ....*....|....*....|....*....|...
gi 1658117674 1278 SSFDVYWVAKMINLMRPGIFTDIDQYQFLYKVI 1310
Cdd:PHA02746   278 KEVCLGEIVLKIRKQRHSSVFLPEQYAFCYKAL 310
R-PTP-N cd14609
PTP-like domain of receptor-type tyrosine-protein phosphatase N; Receptor-type ...
 1054-1320 9.04e-26

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: 108.59  E-value: 9.04e-26
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658117674 1054 LEKQFKMITQSNAKQCDYSAALKQCNRDKNRNSSLLPVERSRVHL-STTAGEISDYINASYIMGYQ-QSNEFIITQNPLP 1131
Cdd:cd14609     17 LAKEWQALCAYQAEPNTCSTAQGEANVKKNRNPDFVPYDHARIKLkAESNPSRSDYINASPIIEHDpRMPAYIATQGPLS 96

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658117674 1132 STMKDFWKMIWDHSTQVVIALPDGLDLAEDEC-IYWPTKSQPIrFDTFTVTFMGEDHMClsnEDMLiVQDFILEATQDDY 1210
Cdd:cd14609     97 HTIADFWQMVWENGCTVIVMLTPLVEDGVKQCdRYWPDEGSSL-YHIYEVNLVSEHIWC---EDFL-VRSFYLKNVQTQE 171

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658117674 1211 VLEVRQYRAPRWPnPDGPISNTFELINIIKEESVS---RDGPIVVHDKRGGNIAGTFCAL-MTLLHQLEMESSFDVYWVA 1286
Cdd:cd14609    172 TRTLTQFHFLSWP-AEGIPSSTRPLLDFRRKVNKCyrgRSCPIIVHCSDGAGRTGTYILIdMVLNRMAKGVKEIDIAATL 250

                          250       260       270
                   ....*....|....*....|....*....|....
gi 1658117674 1287 KMINLMRPGIFTDIDQYQFlykvimSLVAKKEEV 1320
Cdd:cd14609    251 EHVRDQRPGMVRTKDQFEF------ALTAVAEEV 278
PTPc-N7 cd14612
catalytic domain of tyrosine-protein phosphatase non-receptor type 7; Tyrosine-protein ...
 1082-1307 1.05e-25

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: 107.61  E-value: 1.05e-25
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658117674 1082 KNRNSSLLPVERSRVHLSTTA--GEISDYINASYIMGYQ-QSNEFIITQNPLPSTMKDFWKMIWDHSTQVVIALPDgLDL 1158
Cdd:cd14612     18 KDRYKTILPNPQSRVCLRRAGsqEEEGSYINANYIRGYDgKEKAYIATQGPMLNTVSDFWEMVWQEECPIIVMITK-LKE 96

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658117674 1159 AEDECI-YWPTKSQpiRFDTFTVTFMGedhmcLSNEDMLIVQDFILEATQDDYvlEVRQYRAPRWPNPDGPISnTFELIN 1237
Cdd:cd14612     97 KKEKCVhYWPEKEG--TYGRFEIRVQD-----MKECDGYTIRDLTIQLEEESR--SVKHYWFSSWPDHQTPES-AGPLLR 166

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1658117674 1238 IIKEESVSRD-----GPIVVHDKRGGNIAGTFCALMTLLHQLEMESSFDVYWVAKMINLMRPGIFTDIDQYQFLY 1307
Cdd:cd14612    167 LVAEVEESRQtaaspGPIVVHCSAGIGRTGCFIATSIGCQQLKDTGKVDILGIVCQLRLDRGGMIQTSEQYQFLH 241
R-PTPc-D-1 cd14624
catalytic domain of receptor-type tyrosine-protein phosphatase D, repeat 1; Receptor-type ...
 1077-1314 1.07e-25

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: 108.67  E-value: 1.07e-25
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658117674 1077 QCNRDKNRNSSLLPVERSRVHLSTTAG-EISDYINASYIMGYQQSNEFIITQNPLPSTMKDFWKMIWDHSTQVVIALPDG 1155
Cdd:cd14624     45 EVNKPKNRYANVIAYDHSRVLLSAIEGiPGSDYINANYIDGYRKQNAYIATQGALPETFGDFWRMIWEQRSATVVMMTKL 124

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658117674 1156 LDLAEDEC-IYWPTKSQPIRfDTFTVTFMgeDHMCLSNedmLIVQDFILEATQDDYVLEVRQYRAPRWPN---PDGPiSN 1231
Cdd:cd14624    125 EERSRVKCdQYWPSRGTETY-GLIQVTLL--DTVELAT---YCVRTFALYKNGSSEKREVRQFQFTAWPDhgvPEHP-TP 197

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658117674 1232 TFELINIIKEESVSRDGPIVVHDKRGGNIAGTFCALMTLLHQLEMESSFDVYWVAKMINLMRPGIFTDIDQYQFLYKVIM 1311
Cdd:cd14624    198 FLAFLRRVKTCNPPDAGPMVVHCSAGVGRTGCFIVIDAMLERIKHEKTVDIYGHVTLMRAQRNYMVQTEDQYIFIHDALL 277


                   ...
gi 1658117674 1312 SLV 1314
Cdd:cd14624    278 EAV 280
R-PTPc-typeIIb-1 cd14555
catalytic domain of type IIb (or R2B) subfamily receptor-type tyrosine-protein phosphatases, ...
 1108-1311 1.13e-25

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: 106.15  E-value: 1.13e-25
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658117674 1108 YINASYIMGYQQSNEFIITQNPLPSTMKDFWKMIWDHSTQVVIALPDGLDLAEDECI-YWPTKSQPirFDTFTVTfmged 1186
Cdd:cd14555      1 YINANYIDGYHRPNHYIATQGPMQETVYDFWRMVWQENSASIVMVTNLVEVGRVKCSrYWPDDTEV--YGDIKVT----- 73

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658117674 1187 hmCLSNEDM--LIVQDFILEATQDDYVLEVRQYRAPRWPNPDGPISNT--FELINIIKEESVSRDGPIVVHDKRGGNIAG 1262
Cdd:cd14555     74 --LVETEPLaeYVVRTFALERRGYHEIREVRQFHFTGWPDHGVPYHATglLGFIRRVKASNPPSAGPIVVHCSAGAGRTG 151

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*....
gi 1658117674 1263 TFCALMTLLHQLEMESSFDVYWVAKMINLMRPGIFTDIDQYQFLYKVIM 1311
Cdd:cd14555    152 CYIVIDIMLDMAEREGVVDIYNCVKELRSRRVNMVQTEEQYIFIHDAIL 200
PTPc-N1 cd14608
catalytic domain of tyrosine-protein phosphatase non-receptor type 1; Tyrosine-protein ...
 1079-1307 4.28e-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: 106.65  E-value: 4.28e-25
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658117674 1079 NRDKNRNSSLLPVERSRVHLSTtagEISDYINASYIMGYQQSNEFIITQNPLPSTMKDFWKMIWDHSTQVVIALPDGLDL 1158
Cdd:cd14608     25 NKNRNRYRDVSPFDHSRIKLHQ---EDNDYINASLIKMEEAQRSYILTQGPLPNTCGHFWEMVWEQKSRGVVMLNRVMEK 101

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658117674 1159 AEDECI-YWPTKSQ-PIRFD--TFTVTFMGEDhmclsNEDMLIVQDFILEATQDDYVLEVRQYRAPRWPN---PDGPISN 1231
Cdd:cd14608    102 GSLKCAqYWPQKEEkEMIFEdtNLKLTLISED-----IKSYYTVRQLELENLTTQETREILHFHYTTWPDfgvPESPASF 176

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658117674 1232 TFELINIIKEESVSRD-GPIVVHDKRGGNIAGTFCALMT---LLHQLEMESSFDVYWVAKMINLMRPGIFTDIDQYQFLY 1307
Cdd:cd14608    177 LNFLFKVRESGSLSPEhGPVVVHCSAGIGRSGTFCLADTcllLMDKRKDPSSVDIKKVLLEMRKFRMGLIQTADQLRFSY 256
R-PTPc-U-2 cd14637
PTP domain of receptor-type tyrosine-protein phosphatase U, repeat 2; Receptor-type ...
 813-1022 6.11e-25

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: 104.22  E-value: 6.11e-25
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658117674  813 YINANYVDGFTQPKAYIATQGPLKSSMEDFWRMVWEQNASVIVMITNLVEKGRR-KCDQYWPLDSQEEYGSFLVTLRSTK 891
Cdd:cd14637      1 YINAALTDSYTRSAAFIVTLHPLQNTTTDFWRLVYDYGCTSVVMLNQLNQSNSAwPCLQYWPEPGLQQYGPMEVEFVSGS 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658117674  892 VLAYYTQRTFTLKN-TRAKKGsqkeqthERTVVQYHYTQW-PDMGVPEYT---LPVLTFVRKsSQANLGNmGPVVVHCSA 966
Cdd:cd14637     81 ADEDIVTRLFRVQNiTRLQEG-------HLMVRHFQFLRWsAYRDTPDSKkafLHLLASVEK-WQRESGE-GRTVVHCLN 151

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 1658117674  967 GVGRTGTYIVLDSMLRQIKEQGTVNILGFLKHIRTQRNYLVQTEEQYIFIHDALVE 1022
Cdd:cd14637    152 GGGRSGTYCASAMILEMIRCHNIVDVFYAVKTLRNYKPNMVETLEQYRFCYEIALE 207
R-PTPc-M-2 cd14635
PTP domain of receptor-type tyrosine-protein phosphatase M, repeat 2; Receptor-type ...
 813-1022 6.69e-25

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: 104.00  E-value: 6.69e-25
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658117674  813 YINANYVDGFTQPKAYIATQGPLKSSMEDFWRMVWEQNASVIVMITNLveKGRRKCDQYWPLDSQEEYGSFLVTLRSTKV 892
Cdd:cd14635      1 YINAALMDSYKQPSAFIVTQHPLPNTVKDFWRLVLDYHCTSIVMLNDV--DPAQLCPQYWPENGVHRHGPIQVEFVSADL 78

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658117674  893 LAYYTQRTFTLKNtrakkgSQKEQTHERTVVQYHYTQWP---DMGVPEYT-LPVLTFVRKSSQANLGNMGPVVVHCSAGV 968
Cdd:cd14635     79 EEDIISRIFRIYN------AARPQDGYRMVQQFQFLGWPmyrDTPVSKRSfLKLIRQVDKWQEEYNGGEGRTVVHCLNGG 152

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....
gi 1658117674  969 GRTGTYIVLDSMLRQIKEQGTVNILGFLKHIRTQRNYLVQTEEQYIFIHDALVE 1022
Cdd:cd14635    153 GRSGTFCAISIVCEMLRHQRAVDVFHAVKTLRNNKPNMVDLLDQYKFCYEVALE 206
R-PTPc-T-2 cd14634
PTP domain of receptor-type tyrosine-protein phosphatase T, repeat 2; Receptor-type ...
 1108-1311 1.23e-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: 103.18  E-value: 1.23e-24
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658117674 1108 YINASYIMGYQQSNEFIITQNPLPSTMKDFWKMIWDHSTQVVIALPDgLDLAEDECIYWPTKSQ----PIRfdtftVTFM 1183
Cdd:cd14634      1 YINAALMDSHKQPAAFIVTQHPLPNTVADFWRLVFDYNCSSVVMLNE-MDAAQLCMQYWPEKTSccygPIQ-----VEFV 74

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658117674 1184 GEDhmclSNEDML--IVQDFILEATQDDYVLeVRQYRAPRWPN-PDGPISNTFEL-----INIIKEESVSRDGPIVVHDK 1255
Cdd:cd14634     75 SAD----IDEDIIsrIFRICNMARPQDGYRI-VQHLQYIGWPAyRDTPPSKRSILkvvrrLEKWQEQYDGREGRTVVHCL 149

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 1658117674 1256 RGGNIAGTFCALMTLLHQLEMESSFDVYWVAKMINLMRPGIFTDIDQYQFLYKVIM 1311
Cdd:cd14634    150 NGGGRSGTFCAICSVCEMIQQQNIIDVFHTVKTLRNNKSNMVETLEQYKFVYEVAL 205
PTPc-N5 cd14613
catalytic domain of tyrosine-protein phosphatase non-receptor type 5; Tyrosine-protein ...
 1082-1313 1.58e-24

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: 104.56  E-value: 1.58e-24
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658117674 1082 KNRNSSLLPVERSRVHLSTTAGE--ISDYINASYIMGY-QQSNEFIITQNPLPSTMKDFWKMIWDHSTQVVIALPDGLDL 1158
Cdd:cd14613     28 KNRYKTILPNPHSRVCLTSPDQDdpLSSYINANYIRGYgGEEKVYIATQGPTVNTVGDFWRMVWQERSPIIVMITNIEEM 107

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658117674 1159 AEDECIYWPTKSqpirfdtftVTFMGEDhmclsnedmLIVQDFILEatqDDYVLEV------------RQYRAPRWPNPD 1226
Cdd:cd14613    108 NEKCTEYWPEEQ---------VTYEGIE---------ITVKQVIHA---DDYRLRLitlksggeerglKHYWYTSWPDQK 166

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658117674 1227 GPiSNTFELINIIKEESVSR------DGPIVVHDKRGGNIAGTFCALMTLLHQLEMESSFDVYWVAKMINLMRPGIFTDI 1300
Cdd:cd14613    167 TP-DNAPPLLQLVQEVEEARqqaepnCGPVIVHCSAGIGRTGCFIATSICCKQLRNEGVVDILRTTCQLRLDRGGMIQTC 245

                          250
                   ....*....|...
gi 1658117674 1301 DQYQFLYKViMSL 1313
Cdd:cd14613    246 EQYQFVHHV-LSL 257
PTPc-N22_18_12 cd14542
catalytic domain of tyrosine-protein phosphatase non-receptor type 22, type 18 and type 12; ...
 1108-1308 1.60e-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: 102.50  E-value: 1.60e-24
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658117674 1108 YINASYIMGYQQSNEFIITQNPLPSTMKDFWKMIWDHSTQVVIALPDGLDLAEDEC-IYWPTKSQP-IRFDTFTVTFMGE 1185
Cdd:cd14542      1 YINANFIKGVSGSKAYIATQGPLPNTVLDFWRMIWEYNVQVIVMACREFEMGKKKCeRYWPEEGEEqLQFGPFKISLEKE 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658117674 1186 DHMClsnEDMLIVQdfiLEATQDDYVLEVRQYRAPRWPNPDGPISNT--FELINIIKEESVSRDGPIVVHDKRGGNIAGT 1263
Cdd:cd14542     81 KRVG---PDFLIRT---LKVTFQKESRTVYQFHYTAWPDHGVPSSVDpiLDLVRLVRDYQGSEDVPICVHCSAGCGRTGT 154

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*...
gi 1658117674 1264 FCAL---MTLLHQLEMESSFDVYWVAKMINLMRPGIFTDIDQYQFLYK 1308
Cdd:cd14542    155 ICAIdyvWNLLKTGKIPEEFSLFDLVREMRKQRPAMVQTKEQYELVYR 202
R-PTPc-U-1 cd14632
catalytic domain of receptor-type tyrosine-protein phosphatase U, repeat 1; Receptor-type ...
 1108-1311 1.80e-24

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: 102.82  E-value: 1.80e-24
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658117674 1108 YINASYIMGYQQSNEFIITQNPLPSTMKDFWKMIWDHSTQVVIALPDGLDLAEDECI-YWPTKSqpirfDTFtvtfmGED 1186
Cdd:cd14632      1 YINANYIDGYHRSNHFIATQGPKQEMVYDFWRMVWQEHCSSIVMITKLVEVGRVKCSkYWPDDS-----DTY-----GDI 70

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658117674 1187 HMCLSNEDML---IVQDFILEATQDDYVLEVRQYRAPRWPNPDGPISNT--FELINIIKEESVSRDGPIVVHDKRGGNIA 1261
Cdd:cd14632     71 KITLLKTETLaeySVRTFALERRGYSARHEVKQFHFTSWPEHGVPYHATglLAFIRRVKASTPPDAGPVVVHCSAGAGRT 150

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|
gi 1658117674 1262 GTFCALMTLLHQLEMESSFDVYWVAKMINLMRPGIFTDIDQYQFLYKVIM 1311
Cdd:cd14632    151 GCYIVLDVMLDMAECEGVVDIYNCVKTLCSRRINMIQTEEQYIFIHDAIL 200
R-PTPc-M-2 cd14635
PTP domain of receptor-type tyrosine-protein phosphatase M, repeat 2; Receptor-type ...
 1108-1311 2.06e-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: 102.46  E-value: 2.06e-24
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658117674 1108 YINASYIMGYQQSNEFIITQNPLPSTMKDFWKMIWDHSTQVVIALPDgLDLAEDECIYWPTKSQPiRFDTFTVTFMGEDh 1187
Cdd:cd14635      1 YINAALMDSYKQPSAFIVTQHPLPNTVKDFWRLVLDYHCTSIVMLND-VDPAQLCPQYWPENGVH-RHGPIQVEFVSAD- 77

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658117674 1188 mclSNEDML--IVQDFILEATQDDYVLeVRQYRAPRWP-NPDGPISNT--FELINII---KEESVSRDGPIVVHDKRGGN 1259
Cdd:cd14635     78 ---LEEDIIsrIFRIYNAARPQDGYRM-VQQFQFLGWPmYRDTPVSKRsfLKLIRQVdkwQEEYNGGEGRTVVHCLNGGG 153

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|..
gi 1658117674 1260 IAGTFCALMTLLHQLEMESSFDVYWVAKMINLMRPGIFTDIDQYQFLYKVIM 1311
Cdd:cd14635    154 RSGTFCAISIVCEMLRHQRAVDVFHAVKTLRNNKPNMVDLLDQYKFCYEVAL 205
PTPc-N1_2 cd14545
catalytic domain of tyrosine-protein phosphatase non-receptor type 1 and type 2; ...
 1080-1308 3.69e-24

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: 102.47  E-value: 3.69e-24
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658117674 1080 RDKNRNSSLLPVERSRVHLSttaGEISDYINASYIMGYQQSNEFIITQNPLPSTMKDFWKMIWDHSTQVVIALPDGLDLA 1159
Cdd:cd14545      1 LNRYRDRDPYDHDRSRVKLK---QGDNDYINASLVEVEEAKRSYILTQGPLPNTSGHFWQMVWEQNSKAVIMLNKLMEKG 77

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658117674 1160 EDECI-YWPTKSQP---IRFDTFTVTFMGEDhmclSNEDmLIVQDFILEATQDDYVLEVRQYRAPRWPN---PDGPISNT 1232
Cdd:cd14545     78 QIKCAqYWPQGEGNamiFEDTGLKVTLLSEE----DKSY-YTVRTLELENLKTQETREVLHFHYTTWPDfgvPESPAAFL 152

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1658117674 1233 FELINIIKEESVSRD-GPIVVHDKRGGNIAGTFCALMTLLHQLEME--SSFDVYWVAKMINLMRPGIFTDIDQYQFLYK 1308
Cdd:cd14545    153 NFLQKVRESGSLSSDvGPPVVHCSAGIGRSGTFCLVDTCLVLIEKGnpSSVDVKKVLLEMRKYRMGLIQTPDQLRFSYL 231
PHA02747 PHA02747
protein tyrosine phosphatase; Provisional
 1071-1320 2.13e-23

protein tyrosine phosphatase; Provisional


Pssm-ID: 165114 [Multi-domain]  Cd Length: 312  Bit Score: 102.39  E-value: 2.13e-23
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658117674 1071 YSAALKQCNRDKNRNSSLLPVERSRVHLSTTAGEISDYINASYIMGYQQSNEFIITQNPLPSTMKDFWKMIWDHSTQVVI 1150
Cdd:PHA02747    43 IANFEKPENQPKNRYWDIPCWDHNRVILDSGGGSTSDYIHANWIDGFEDDKKFIATQGPFAETCADFWKAVWQEHCSIIV 122

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658117674 1151 AL-PDGLDLAEDECI-YWptksqpirfdtftvtfmgedhmCLSNEDMLIVQDFILE----ATQDDYVL------------ 1212
Cdd:PHA02747   123 MLtPTKGTNGEEKCYqYW----------------------CLNEDGNIDMEDFRIEtlktSVRAKYILtlieitdkilkd 180

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658117674 1213 --EVRQYRAPRWPNPDGPISNT-----FELINIIKEESVSRDG-------PIVVHDKRGGNIAGTFCALMTLLHQLEMES 1278
Cdd:PHA02747   181 srKISHFQCSEWFEDETPSDHPdfikfIKIIDINRKKSGKLFNpkdallcPIVVHCSDGVGKTGIFCAVDICLNQLVKRK 260

                          250       260       270       280
                   ....*....|....*....|....*....|....*....|....*
gi 1658117674 1279 SFDVYWVAKMINLMRPGIFTDIDQYQFL---YKVIMSLVAKKEEV 1320
Cdd:PHA02747   261 AICLAKTAEKIREQRHAGIMNFDDYLFIqpgYEVLHYFLSKIKAI 305
PTPc-N2 cd14607
catalytic domain of tyrosine-protein phosphatase non-receptor type 2; Tyrosine-protein ...
 1079-1310 3.63e-23

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: 100.43  E-value: 3.63e-23
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658117674 1079 NRDKNRNSSLLPVERSRVHLSTTAgeiSDYINASYIMGYQQSNEFIITQNPLPSTMKDFWKMIWDHSTQVVIALPDGLDL 1158
Cdd:cd14607     24 NRNRNRYRDVSPYDHSRVKLQNTE---NDYINASLVVIEEAQRSYILTQGPLPNTCCHFWLMVWQQKTKAVVMLNRIVEK 100

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658117674 1159 AEDECI-YWPTKSQPIRF--DT-FTVTFMGEDHMCLSNEDMLIVQDFILEATQDdyvleVRQYRAPRWPN---PDGPISN 1231
Cdd:cd14607    101 DSVKCAqYWPTDEEEVLSfkETgFSVKLLSEDVKSYYTVHLLQLENINSGETRT-----ISHFHYTTWPDfgvPESPASF 175

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658117674 1232 TFELINIIKEESVSRD-GPIVVHDKRGGNIAGTFCALMTLLHQLEMESSFDVYWVAKMINL--MRPGIFTDIDQYQFLYK 1308
Cdd:cd14607    176 LNFLFKVRESGSLSPEhGPAVVHCSAGIGRSGTFSLVDTCLVLMEKKDPDSVDIKQVLLDMrkYRMGLIQTPDQLRFSYM 255


                   ..
gi 1658117674 1309 VI 1310
Cdd:cd14607    256 AV 257
PTPc-N11 cd14605
catalytic domain of tyrosine-protein phosphatase non-receptor type 11; Tyrosine-protein ...
 1079-1310 6.48e-23

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: 99.71  E-value: 6.48e-23
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658117674 1079 NRDKNRNSSLLPVERSRV--HLSTTAGEISDYINASYIM--------GYQQSNEFIITQNPLPSTMKDFWKMIWDHSTQV 1148
Cdd:cd14605      2 NKNKNRYKNILPFDHTRVvlHDGDPNEPVSDYINANIIMpefetkcnNSKPKKSYIATQGCLQNTVNDFWRMVFQENSRV 81

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658117674 1149 VIALPDGLDLAEDECI-YWPtksqpirfDTFTVTFMGEdhMCLSNEDMLIVQDFIL------EATQDDYVLEVRQYRAPR 1221
Cdd:cd14605     82 IVMTTKEVERGKSKCVkYWP--------DEYALKEYGV--MRVRNVKESAAHDYILrelklsKVGQGNTERTVWQYHFRT 151

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658117674 1222 WPN---PDGP--ISNTFELINIiKEESVSRDGPIVVHDKRGGNIAGTFCA---LMTLLHQLEMESSFDVYWVAKMINLMR 1293
Cdd:cd14605    152 WPDhgvPSDPggVLDFLEEVHH-KQESIMDAGPVVVHCSAGIGRTGTFIVidiLIDIIREKGVDCDIDVPKTIQMVRSQR 230

                          250
                   ....*....|....*..
gi 1658117674 1294 PGIFTDIDQYQFLYKVI 1310
Cdd:cd14605    231 SGMVQTEAQYRFIYMAV 247
R-PTPc-A-E-1 cd14551
catalytic domain of receptor-type tyrosine-protein phosphatase A and E, repeat 1; ...
 1108-1308 8.80e-23

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: 97.68  E-value: 8.80e-23
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658117674 1108 YINASYIMGYQQSNEFIITQNPLPSTMKDFWKMIWDHSTQVVIALPDGLDLAEDECI-YWPTKSQpirfdtftvTFMGED 1186
Cdd:cd14551      1 YINASYIDGYQEKNKFIAAQGPKDETVNDFWRMIWEQGSATIVMVTNLKERKEKKCSqYWPDQGC---------WTYGNL 71

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658117674 1187 HMCLsnEDMLIVQDFILEATQDDYVLEVRQYRAPR---------WPN---PDGPISnTFELINIIKEESVSRDGPIVVHD 1254
Cdd:cd14551     72 RVRV--EDTVVLVDYTTRKFCIQKVNRGIGEKRVRlvtqfhftsWPDfgvPFTPIG-MLKFLKKVKSANPPRAGPIVVHC 148

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....
gi 1658117674 1255 KRGGNIAGTFCALMTLLHQLEMESSFDVYWVAKMINLMRPGIFTDIDQYQFLYK 1308
Cdd:cd14551    149 SAGVGRTGTFIVIDAMLDMMHAEGKVDVFGFVSRIRQQRSQMVQTDMQYVFIYQ 202
PTPc-N6 cd14606
catalytic domain of tyrosine-protein phosphatase non-receptor type 6; Tyrosine-protein ...
 1079-1314 2.08e-22

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


Pssm-ID: 350454 [Multi-domain]  Cd Length: 266  Bit Score: 98.41  E-value: 2.08e-22
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658117674 1079 NRDKNRNSSLLPVERSRVHLSTTAGEI--SDYINASYI----MGYQQSNE-FIITQNPLPSTMKDFWKMIWDHSTQVVIA 1151
Cdd:cd14606     18 NKSKNRYKNILPFDHSRVILQGRDSNIpgSDYINANYVknqlLGPDENAKtYIASQGCLEATVNDFWQMAWQENSRVIVM 97

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658117674 1152 LPDGLDLAEDECI-YWPTKSQPIRFDTFTVTFMGEdhMCLSNEDMLIVQDFILEATqdDYVLEVRQYRAPRWP------N 1224
Cdd:cd14606     98 TTREVEKGRNKCVpYWPEVGMQRAYGPYSVTNCGE--HDTTEYKLRTLQVSPLDNG--ELIREIWHYQYLSWPdhgvpsE 173

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658117674 1225 PDGPISnTFELINiIKEESVSRDGPIVVHDKRGGNIAGTFCALMTLLHQLEM---ESSFDVYWVAKMINLMRPGIFTDID 1301
Cdd:cd14606    174 PGGVLS-FLDQIN-QRQESLPHAGPIIVHCSAGIGRTGTIIVIDMLMENISTkglDCDIDIQKTIQMVRAQRSGMVQTEA 251

                          250
                   ....*....|...
gi 1658117674 1302 QYQFLYKVIMSLV 1314
Cdd:cd14606    252 QYKFIYVAIAQFI 264
R-PTP-Z-2 cd17669
catalytic domain of receptor-type tyrosine-protein phosphatase Z, repeat 2; Receptor-type ...
 813-1021 3.69e-22

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


Pssm-ID: 350507 [Multi-domain]  Cd Length: 204  Bit Score: 95.83  E-value: 3.69e-22
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658117674  813 YINANYVDGFTQPKAYIATQGPLKSSMEDFWRMVWEQNASVIVMITNLVEKGRRKCdQYWPldSQEE---YGSFLVTLRS 889
Cdd:cd17669      1 YINASYIMGYYQSNEFIITQHPLLHTIKDFWRMIWDHNAQLIVMLPDGQNMAEDEF-VYWP--NKDEpinCETFKVTLIA 77

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658117674  890 TKVLAYYTQRTFTLKNTrAKKGSQKEQTHErtVVQYHYTQWPDMGVPEYTLPVLTFVRKSSQANlgNMGPVVVHCSAGVG 969
Cdd:cd17669     78 EEHKCLSNEEKLIIQDF-ILEATQDDYVLE--VRHFQCPKWPNPDSPISKTFELISIIKEEAAN--RDGPMIVHDEHGGV 152

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|..
gi 1658117674  970 RTGTYIVLDSMLRQIKEQGTVNILGFLKHIRTQRNYLVQTEEQYIFIHDALV 1021
Cdd:cd17669    153 TAGTFCALTTLMHQLEKENSVDVYQVAKMINLMRPGVFTDIEQYQFLYKAIL 204
R-PTPc-Z-1 cd17668
catalytic domain of receptor-type tyrosine-protein phosphatase Z, repeat 1; Receptor-type ...
 1108-1311 4.03e-22

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: 96.20  E-value: 4.03e-22
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658117674 1108 YINASYIMGYQQSNEFIITQNPLPSTMKDFWKMIWDHSTQVVIALPDGLDLAEDEC-IYWPTKSQPiRFDTFTVTFMGED 1186
Cdd:cd17668      1 YINANYVDGYNKPKAYIAAQGPLKSTAEDFWRMIWEHNVEVIVMITNLVEKGRRKCdQYWPADGSE-EYGNFLVTQKSVQ 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658117674 1187 HMCLSNEDMLIVQDF-ILEATQDDYVLE--VRQYRAPRWPNPDGPiSNTFELINIIKEESVSRD---GPIVVHDKRGGNI 1260
Cdd:cd17668     80 VLAYYTVRNFTLRNTkIKKGSQKGRPSGrvVTQYHYTQWPDMGVP-EYTLPVLTFVRKASYAKRhavGPVVVHCSAGVGR 158

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|.
gi 1658117674 1261 AGTFCALMTLLHQLEMESSFDVYWVAKMINLMRPGIFTDIDQYQFLYKVIM 1311
Cdd:cd17668    159 TGTYIVLDSMLQQIQHEGTVNIFGFLKHIRSQRNYLVQTEEQYVFIHDALV 209
R-PTP-G-2 cd17670
PTP-like domain of receptor-type tyrosine-protein phosphatase G, repeat 2; Receptor-type ...
 813-1021 1.33e-21

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


Pssm-ID: 350508 [Multi-domain]  Cd Length: 205  Bit Score: 94.36  E-value: 1.33e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658117674  813 YINANYVDGFTQPKAYIATQGPLKSSMEDFWRMVWEQNASVIVMITN---LVEkgrrkcDQ--YWPldSQEEY---GSFL 884
Cdd:cd17670      1 YINASYIMGYYRSNEFIITQHPLPHTTKDFWRMIWDHNAQIIVMLPDnqgLAE------DEfvYWP--SREESmncEAFT 72

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658117674  885 VTLRSTKVLAYYTQRTFTLKNTRAkkgsqkEQTHERTVVQYHYTQ---WPDMGVP-EYTLPVLTFVRKSSqanLGNMGPV 960
Cdd:cd17670     73 VTLISKDRLCLSNEEQIIIHDFIL------EATQDDYVLEVRHFQcpkWPNPDAPiSSTFELINVIKEEA---LTRDGPT 143

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1658117674  961 VVHCSAGVGRTGTYIVLDSMLRQIKEQGTVNILGFLKHIRTQRNYLVQTEEQYIFIHDALV 1021
Cdd:cd17670    144 IVHDEFGAVSAGTLCALTTLSQQLENENAVDVYQVAKMINLMRPGVFTDIEQYQFLYKAML 204
R-PTPc-K-2 cd14636
PTP domain of receptor-type tyrosine-protein phosphatase K, repeat 2; Receptor-type ...
 1108-1309 1.63e-21

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: 94.32  E-value: 1.63e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658117674 1108 YINASYIMGYQQSNEFIITQNPLPSTMKDFWKMIWDHSTQVVIALPDgLDLAEDECIYWPTKSQpIRFDTFTVTFMGedh 1187
Cdd:cd14636      1 YINAALMDSYRQPAAFIVTQHPLPNTVKDFWRLVYDYGCTSIVMLNE-VDLAQGCPQYWPEEGM-LRYGPIQVECMS--- 75

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658117674 1188 mCLSNEDML--IVQDFILEATQDDYVLeVRQYRAPRWPNPDGPISNTFELINII------KEESVSRDGPIVVHDKRGGN 1259
Cdd:cd14636     76 -CSMDCDVIsrIFRICNLTRPQEGYLM-VQQFQYLGWASHREVPGSKRSFLKLIlqvekwQEECDEGEGRTIIHCLNGGG 153

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|
gi 1658117674 1260 IAGTFCALMTLLHQLEMESSFDVYWVAKMINLMRPGIFTDIDQYQFLYKV 1309
Cdd:cd14636    154 RSGMFCAISIVCEMIKRQNVVDVFHAVKTLRNSKPNMVETPEQYRFCYDV 203
R-PTPc-U-2 cd14637
PTP domain of receptor-type tyrosine-protein phosphatase U, repeat 2; Receptor-type ...
 1108-1311 3.65e-21

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: 93.05  E-value: 3.65e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658117674 1108 YINASYIMGYQQSNEFIITQNPLPSTMKDFWKMIWDHSTQVVIALpDGLDLAEDE--CI-YWPtKSQPIRFDTFTVTFMG 1184
Cdd:cd14637      1 YINAALTDSYTRSAAFIVTLHPLQNTTTDFWRLVYDYGCTSVVML-NQLNQSNSAwpCLqYWP-EPGLQQYGPMEVEFVS 78

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658117674 1185 edhmcLSNEDMLIVQDFILE--ATQDDYVLEVRQYRAPRWP----NPDGPISNTFELINIIKEESVSRDGPIVVHDKRGG 1258
Cdd:cd14637     79 -----GSADEDIVTRLFRVQniTRLQEGHLMVRHFQFLRWSayrdTPDSKKAFLHLLASVEKWQRESGEGRTVVHCLNGG 153

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|...
gi 1658117674 1259 NIAGTFCALMTLLHQLEMESSFDVYWVAKMINLMRPGIFTDIDQYQFLYKVIM 1311
Cdd:cd14637    154 GRSGTYCASAMILEMIRCHNIVDVFYAVKTLRNYKPNMVETLEQYRFCYEIAL 206
PTPc-N20_13 cd14538
catalytic domain of tyrosine-protein phosphatase non-receptor type 20 and type 13; ...
 1108-1311 4.15e-21

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: 92.82  E-value: 4.15e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658117674 1108 YINASYIMGYQQSNEF--IITQNPLPSTMKDFWKMIWDHSTQVVIALPDGLDLAEDECI-YWPtksqpirfDTFTVTFMG 1184
Cdd:cd14538      1 YINASHIRIPVGGDTYhyIACQGPLPNTTGDFWQMVWEQKSEVIAMVTQDVEGGKVKCHrYWP--------DSLNKPLIC 72

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658117674 1185 EDHMCLSNEDMLIVQDFI-----LEATQDDYVLEVRQYRAPRWPNPDGPiSNTFELINIIKE-ESVSRDGPIVVHDKRGG 1258
Cdd:cd14538     73 GGRLEVSLEKYQSLQDFVirrisLRDKETGEVHHITHLNFTTWPDHGTP-QSADPLLRFIRYmRRIHNSGPIVVHCSAGI 151

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|...
gi 1658117674 1259 NIAGTFCALMTLLHQLEMESSFDVYWVAKMINLMRPGIFTDIDQYQFLYKVIM 1311
Cdd:cd14538    152 GRTGVLITIDVALGLIERDLPFDIQDIVKDLREQRQGMIQTKDQYIFCYKACL 204
R-PTPc-R cd14611
catalytic domain of receptor-type tyrosine-protein phosphatase R; Receptor-type ...
 1082-1307 4.93e-21

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: 93.44  E-value: 4.93e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658117674 1082 KNRNSSLLPVERSRVHLST--TAGEISDYINASYIMGYQ-QSNEFIITQNPLPSTMKDFWKMIWDHSTQVVIALPDGLDL 1158
Cdd:cd14611      2 KNRYKTILPNPHSRVCLKPknSNDSLSTYINANYIRGYGgKEKAFIATQGPMINTVNDFWQMVWQEDSPVIVMITKLKEK 81

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658117674 1159 AEDECIYWPTKSQPIRFDTFTVTfmgedhmCLSNEDMLIVQDFILEatQDDYVLEVRQYRAPRWPNPDGPISNT--FELI 1236
Cdd:cd14611     82 NEKCVLYWPEKRGIYGKVEVLVN-------SVKECDNYTIRNLTLK--QGSQSRSVKHYWYTSWPDHKTPDSAQplLQLM 152

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1658117674 1237 NIIKEE---SVSRdGPIVVHDKRGGNIAGTFCALMTLLHQLEMESSFDVYWVAKMINLMRPGIFTDIDQYQFLY 1307
Cdd:cd14611    153 LDVEEDrlaSPGR-GPVVVHCSAGIGRTGCFIATTIGCQQLKEEGVVDVLSIVCQLRVDRGGMVQTSEQYEFVH 225
PHA02738 PHA02738
hypothetical protein; Provisional
 1071-1310 2.90e-20

hypothetical protein; Provisional


Pssm-ID: 222923 [Multi-domain]  Cd Length: 320  Bit Score: 93.45  E-value: 2.90e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658117674 1071 YSAALKqcNRDKNRNSSLLPVERSRVHLSTTAGEiSDYINASYIMGYQQSNEFIITQNPLPSTMKDFWKMIWDHSTQVVI 1150
Cdd:PHA02738    43 FNAEKK--NRKLNRYLDAVCFDHSRVILPAERNR-GDYINANYVDGFEYKKKFICGQAPTRQTCYDFYRMLWMEHVQIIV 119

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658117674 1151 ALPDGLDLAEDECI-YWPTKSQ-PIRFDTFTVTFMGEDHMCLSNEDMLIVQDFIlEATQddyvlEVRQYRAPRWPNPDGP 1228
Cdd:PHA02738   120 MLCKKKENGREKCFpYWSDVEQgSIRFGKFKITTTQVETHPHYVKSTLLLTDGT-SATQ-----TVTHFNFTAWPDHDVP 193

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658117674 1229 iSNTFELINIIKE----------------ESVSRDGPIVVHDKRGGNIAGTFCALMTLLHQLEMESSFDVYWVAKMINLM 1292
Cdd:PHA02738   194 -KNTSEFLNFVLEvrqcqkelaqeslqigHNRLQPPPIVVHCNAGLGRTPCYCVVDISISRFDACATVSIPSIVSSIRNQ 272

                          250
                   ....*....|....*...
gi 1658117674 1293 RPGIFTDIDQYQFLYKVI 1310
Cdd:PHA02738   273 RYYSLFIPFQYFFCYRAV 290
PHA02740 PHA02740
protein tyrosine phosphatase; Provisional
 775-1026 5.49e-20

protein tyrosine phosphatase; Provisional


Pssm-ID: 165107 [Multi-domain]  Cd Length: 298  Bit Score: 92.34  E-value: 5.49e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658117674  775 SSIHPENKNK--NRYINILAYDHSRVKLSSSSDrngwsadYINANYVDGFTQPKAYIATQGPLKSSMEDFWRMVWEQNAS 852
Cdd:PHA02740    45 ACAQAENKAKdeNLALHITRLLHRRIKLFNDEK-------VLDARFVDGYDFEQKFICIINLCEDACDKFLQALSDNKVQ 117

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658117674  853 VIVMITNLVEKgrrKC-DQYWPLDSQ--EEYGSFLVtlrstKVLAYYTQRTF--TLKNTRAKKGSQKEQTHertvvqYHY 927
Cdd:PHA02740   118 IIVLISRHADK---KCfNQFWSLKEGcvITSDKFQI-----ETLEIIIKPHFnlTLLSLTDKFGQAQKISH------FQY 183

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658117674  928 TQWPDMGVPEYTLPVLTF--------VRKSSQANLGNMGPVVVHCSAGVGRTGTYIVLDSMLRQIKEQGTVNILGFLKHI 999
Cdd:PHA02740   184 TAWPADGFSHDPDAFIDFfcniddlcADLEKHKADGKIAPIIIDCIDGISSSAVFCVFDICATEFDKTGMLSIANALKKV 263

                          250       260
                   ....*....|....*....|....*..
gi 1658117674 1000 RTQRNYLVQTEEQYIFIHDaLVEAILS 1026
Cdd:PHA02740   264 RQKKYGCMNCLDDYVFCYH-LIAAYLK 289
PHA02742 PHA02742
protein tyrosine phosphatase; Provisional
 1054-1311 5.73e-20

protein tyrosine phosphatase; Provisional


Pssm-ID: 165109 [Multi-domain]  Cd Length: 303  Bit Score: 92.37  E-value: 5.73e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658117674 1054 LEKQFKMITQSN-AKQCDYSAALKqcNRDKNRNSSLLPVERSRVHLSTTAGeISDYINASYIMGYQQSNEFIITQNPLPS 1132
Cdd:PHA02742    28 LKEEHEHIMQEIvAFSCNESLELK--NMKKCRYPDAPCFDRNRVILKIEDG-GDDFINASYVDGHNAKGRFICTQAPLEE 104

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658117674 1133 TMKDFWKMIWDHSTQVVIALPDGLDLAEDECI-YWPTKSQ--------PIR------FDTFTVTfmgedHMCLSNedmli 1197
Cdd:PHA02742   105 TALDFWQAIFQDQVRVIVMITKIMEDGKEACYpYWMPHERgkathgefKIKtkkiksFRNYAVT-----NLCLTD----- 174

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658117674 1198 vqdfileaTQDDYVLEVRQYRAPRWPNPDGP--ISNTFELINIIKE-----------ESVSRDGPIVVHDKRGGNIAGTF 1264
Cdd:PHA02742   175 --------TNTGASLDIKHFAYEDWPHGGLPrdPNKFLDFVLAVREadlkadvdikgENIVKEPPILVHCSAGLDRAGAF 246

                          250       260       270       280
                   ....*....|....*....|....*....|....*....|....*..
gi 1658117674 1265 CALMTLLHQLEMESSFDVYWVAKMINLMRPGIFTDIDQYQFLYKVIM 1311
Cdd:PHA02742   247 CAIDICISKYNERAIIPLLSIVRDLRKQRHNCLSLPQQYIFCYFIVL 293
PTPc-N20 cd14596
catalytic domain of tyrosine-protein phosphatase non-receptor type 20; Tyrosine-protein ...
 1108-1311 6.45e-20

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


Pssm-ID: 350444 [Multi-domain]  Cd Length: 207  Bit Score: 89.42  E-value: 6.45e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658117674 1108 YINASYIMGYQQSNE--FIITQNPLPSTMKDFWKMIWDHSTQVVIALPDGLDLAEDECI-YWP-TKSQPIRFDTFtvtfm 1183
Cdd:cd14596      1 YINASYITMPVGEEElfYIATQGPLPSTIDDFWQMVWENRSDVIAMMTREVERGKVKCHrYWPeTLQEPMELENY----- 75

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658117674 1184 gedHMCLSNEDMLivQDFILEATQddyVLE--------VRQYRAPRWPNPDGPISNTFELINIIKEESVSRDGPIVVHDK 1255
Cdd:cd14596     76 ---QLRLENYQAL--QYFIIRIIK---LVEketgenrlIKHLQFTTWPDHGTPQSSDQLVKFICYMRKVHNTGPIVVHCS 147

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 1658117674 1256 RGGNIAGTFCALMTLLHQLEMESSFDVYWVAKMINLMRPGIFTDIDQYQFLYKVIM 1311
Cdd:cd14596    148 AGIGRAGVLICVDVLLSLIEKDLSFNIKDIVREMRQQRYGMIQTKDQYLFCYKVVL 203
R-PTP-N-N2 cd14546
PTP-like domain of receptor-type tyrosine-protein phosphatase-like N and N2; Receptor-type ...
 1108-1320 9.11e-20

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


Pssm-ID: 350394 [Multi-domain]  Cd Length: 208  Bit Score: 89.04  E-value: 9.11e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658117674 1108 YINASYIMGYQQSNE-FIITQNPLPSTMKDFWKMIWDHSTQVVIALPDGLDLAEDECI-YWPTKSQPIrFDTFTVTFMGE 1185
Cdd:cd14546      1 YINASTIYDHDPRNPaYIATQGPLPHTIADFWQMIWEQGCVVIVMLTRLQENGVKQCArYWPEEGSEV-YHIYEVHLVSE 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658117674 1186 DHMClsneDMLIVQDFILEATQDDYVLEVRQYRAPRWPNPDGPIS--NTFELINIIKEESVSRDGPIVVHDKRGGNIAGT 1263
Cdd:cd14546     80 HIWC----DDYLVRSFYLKNLQTSETRTVTQFHFLSWPDEGIPASakPLLEFRRKVNKSYRGRSCPIVVHCSDGAGRTGT 155

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 1658117674 1264 FCAL-MTLLHQLEMESSFDVYWVAKMINLMRPGIFTDIDQYQFlykvimSLVAKKEEV 1320
Cdd:cd14546    156 YILIdMVLNRMAKGAKEIDIAATLEHLRDQRPGMVKTKDQFEF------VLTAVAEEV 207
R-PTPc-C-1 cd14557
catalytic domain of receptor-type tyrosine-protein phosphatase C, repeat 1; Receptor-type ...
 1108-1288 1.01e-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: 86.03  E-value: 1.01e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658117674 1108 YINASYIMGYQQSNEFIITQNPLPSTMKDFWKMIWDHSTQVVIALPDGLDLAEDECI-YWPTKSQPIR-FDTFTVTFMGE 1185
Cdd:cd14557      1 YINASYIDGFKEPRKYIAAQGPKDETVDDFWRMIWEQKSTVIVMVTRCEEGNRNKCAqYWPSMEEGSRaFGDVVVKINEE 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658117674 1186 DHMclsnEDMLIVQDFILEATQDDYVLEVRQYRAPRWPN---PDGPiSNTFELINIIKEESVSRDGPIVVHDKRGGNIAG 1262
Cdd:cd14557     81 KIC----PDYIIRKLNINNKKEKGSGREVTHIQFTSWPDhgvPEDP-HLLLKLRRRVNAFNNFFSGPIVVHCSAGVGRTG 155

                          170       180
                   ....*....|....*....|....*..
gi 1658117674 1263 TFCALMTLLHQLEMESSFDVY-WVAKM 1288
Cdd:cd14557    156 TYIGIDAMLEGLEAEGRVDVYgYVVKL 182
PTPc_DSPc smart00012
Protein tyrosine phosphatase, catalytic domain, undefined specificity; Protein tyrosine ...
 1213-1312 1.70e-18

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: 82.02  E-value: 1.70e-18
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658117674  1213 EVRQYRAPRWPNPDGPISNT--FELINIIKEESVSRD--GPIVVHDKRGGNIAGTFCALMTLLHQLEMES-SFDVYWVAK 1287
Cdd:smart00012    1 TVKHYHYTGWPDHGVPESPDsiLELLRAVKKNLNQSEssGPVVVHCSAGVGRTGTFVAIDILLQQLEAEAgEVDIFDTVK 80

                            90       100
                    ....*....|....*....|....*
gi 1658117674  1288 MINLMRPGIFTDIDQYQFLYKVIMS 1312
Cdd:smart00012   81 ELRSQRPGMVQTEEQYLFLYRALLE 105
PTPc_motif smart00404
Protein tyrosine phosphatase, catalytic domain motif;
1213-1312 1.70e-18

Protein tyrosine phosphatase, catalytic domain motif;


Pssm-ID: 214649 [Multi-domain]  Cd Length: 105  Bit Score: 82.02  E-value: 1.70e-18
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658117674  1213 EVRQYRAPRWPNPDGPISNT--FELINIIKEESVSRD--GPIVVHDKRGGNIAGTFCALMTLLHQLEMES-SFDVYWVAK 1287
Cdd:smart00404    1 TVKHYHYTGWPDHGVPESPDsiLELLRAVKKNLNQSEssGPVVVHCSAGVGRTGTFVAIDILLQQLEAEAgEVDIFDTVK 80

                            90       100
                    ....*....|....*....|....*
gi 1658117674  1288 MINLMRPGIFTDIDQYQFLYKVIMS 1312
Cdd:smart00404   81 ELRSQRPGMVQTEEQYLFLYRALLE 105
PTPc-N3 cd14600
catalytic domain of tyrosine-protein phosphatase non-receptor type 3; Tyrosine-protein ...
 1079-1311 1.05e-17

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: 84.90  E-value: 1.05e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658117674 1079 NRDKNRNSSLLPVERSRVHLSttagEISDYINASY----IMGYQQSNEFIITQNPLPSTMKDFWKMIWDHSTQVVIALPD 1154
Cdd:cd14600     40 NMDKNRYKDVLPYDATRVVLQ----GNEDYINASYvnmeIPSANIVNKYIATQGPLPHTCAQFWQVVWEQKLSLIVMLTT 115

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658117674 1155 GLDLAEDEC-IYWPTKSQPIRFDTFTVTFMGED-HMCLSNEDMLIVQdfiLEATQDDYVLEVrQYRAprWPN---PDGPi 1229
Cdd:cd14600    116 LTERGRTKChQYWPDPPDVMEYGGFRVQCHSEDcTIAYVFREMLLTN---TQTGEERTVTHL-QYVA--WPDhgvPDDS- 188

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658117674 1230 SNTFELINIIKEESVSRDgPIVVHDKRGGNIAGTFCALMTLLHQLEMESSFDVYWVAKMINLMRPGIFTDIDQYQFLYKV 1309
Cdd:cd14600    189 SDFLEFVNYVRSKRVENE-PVLVHCSAGIGRTGVLVTMETAMCLTERNQPVYPLDIVRKMRDQRAMMVQTSSQYKFVCEA 267


                   ..
gi 1658117674 1310 IM 1311
Cdd:cd14600    268 IL 269
PTPc-N4 cd14601
catalytic domain of tyrosine-protein phosphatase non-receptor type 4; Tyrosine-protein ...
 1107-1311 1.79e-16

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


Pssm-ID: 350449 [Multi-domain]  Cd Length: 212  Bit Score: 79.60  E-value: 1.79e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658117674 1107 DYINASYI-MGYQQS---NEFIITQNPLPSTMKDFWKMIWDHSTQVVIALPDGLDLAEDEC-IYWPTKSQPIRFDTFTVT 1181
Cdd:cd14601      1 DYINANYInMEIPSSsiiNRYIACQGPLPNTCSDFWQMTWEQGSSMVVMLTTQVERGRVKChQYWPEPSGSSSYGGFQVT 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658117674 1182 fmgedhmCLSNE--DMLIVQDFILEATQDDYVLEVRQYRAPRWPN---PDGPiSNTFELINIIKEESVSRDGPIVVHDKR 1256
Cdd:cd14601     81 -------CHSEEgnPAYVFREMTLTNLEKNESRPLTQIQYIAWPDhgvPDDS-SDFLDFVCLVRNKRAGKDEPVVVHCSA 152

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1658117674 1257 GGNIAGTFCALMTLLHQLEMESSFDVYWVAKMINLMRPGIFTDIDQYQFLYKVIM 1311
Cdd:cd14601    153 GIGRTGVLITMETAMCLIECNQPVYPLDIVRTMRDQRAMMIQTPSQYRFVCEAIL 207
PTPc_plant_PTP1 cd17658
protein tyrosine phosphatase 1 from Arabidopsis thaliana and similar plant PTPs; Arabidopsis ...
 1108-1307 6.35e-16

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


Pssm-ID: 350496 [Multi-domain]  Cd Length: 206  Bit Score: 77.89  E-value: 6.35e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658117674 1108 YINASYIMGYQQSN--EFIITQNPLPSTMKDFWKMIWDHSTQVVIALPDGLD-LAEDECI-YWPTKS-QPIRFDTFTVTF 1182
Cdd:cd17658      1 YINASLVETPASESlpKFIATQGPLPHTFEDFWEMVIQQRCPVIIMLTRLVDnYSTAKCAdYFPAEEnESREFGRISVTN 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658117674 1183 MGEDHMCLSNE-DMLIVQDFILEatqdDYVLEVRQYRAPRWPNPDGPiSNTFELINIIKEESVSRD--GPIVVHDKRGGN 1259
Cdd:cd17658     81 KKLKHSQHSITlRVLEVQYIESE----EPPLSVLHIQYPEWPDHGVP-KDTRSVRELLKRLYGIPPsaGPIVVHCSAGIG 155

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|.
gi 1658117674 1260 IAGTFCALMTLLHQLeME---SSFDVYWVAKMINLMRPGIFTDIDQYQFLY 1307
Cdd:cd17658    156 RTGAYCTIHNTIRRI-LEgdmSAVDLSKTVRKFRSQRIGMVQTQDQYIFCY 205
PTPc-N14 cd14599
catalytic domain of tyrosine-protein phosphatase non-receptor type 14; Tyrosine-protein ...
 1072-1314 7.40e-16

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: 79.66  E-value: 7.40e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658117674 1072 SAALKQcNRDKNRNSSLLPVERSRVHLSTTAGEISDYINASYIMGYQQSNE--FIITQNPLPSTMKDFWKMIWDHSTQVV 1149
Cdd:cd14599     32 TATLPE-NAERNRIREVVPYEENRVELVPTKENNTGYINASHIKVTVGGEEwhYIATQGPLPHTCHDFWQMVWEQGVNVI 110

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658117674 1150 ialpdGLDLAEDEC------IYWP---TKSQPIRFDTFTVTF-MGEDHMCLSNEDMLIVQdfiLEATQDDYVLEVrQYra 1219
Cdd:cd14599    111 -----AMVTAEEEGgrskshRYWPklgSKHSSATYGKFKVTTkFRTDSGCYATTGLKVKH---LLSGQERTVWHL-QY-- 179

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658117674 1220 PRWPN---PD---GPISNTFEL------INIIKEESVSRDGPIVVHDKRGGNIAGTFCALMTLLHQLEMESSFDVYWVAK 1287
Cdd:cd14599    180 TDWPDhgcPEevqGFLSYLEEIqsvrrhTNSMLDSTKNCNPPIVVHCSAGVGRTGVVILTELMIGCLEHNEKVEVPVMLR 259

                          250       260
                   ....*....|....*....|....*..
gi 1658117674 1288 MINLMRPGIFTDIDQYQFLYKVIMSLV 1314
Cdd:cd14599    260 HLREQRMFMIQTIAQYKFVYQVLIQFL 286
PTP-N23 cd14539
PTP-like domain of tyrosine-protein phosphatase non-receptor type 23; Tyrosine-protein ...
 1108-1308 1.34e-15

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: 77.04  E-value: 1.34e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658117674 1108 YINASYIMGYQQ-SNEFIITQNPLPSTMKDFWKMIWDHSTQVVIALPDGLDLAEDECI-YWPT-KSQPIRFDTFTVTFMG 1184
Cdd:cd14539      1 YINASLIEDLTPyCPRFIATQAPLPGTAADFWLMVYEQQVSVIVMLVSEQENEKQKVHrYWPTeRGQALVYGAITVSLQS 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658117674 1185 EDHMCLSNEDMLIVQDfileatqddyvLEVRQYRA------PRWPNPDGPiSNTFELINIIKE------ESVSRDGPIVV 1252
Cdd:cd14539     81 VRTTPTHVERIISIQH-----------KDTRLSRSvvhlqfTTWPELGLP-DSPNPLLRFIEEvhshylQQRSLQTPIVV 148

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 1658117674 1253 HDKRGGNIAGTFCALMTLLHQLEMESSF-DVYWVAKMINLMRPGIFTDIDQYQFLYK 1308
Cdd:cd14539    149 HCSSGVGRTGAFCLLYAAVQEIEAGNGIpDLPQLVRKMRQQRKYMLQEKEHLKFCYE 205
PTP_YopH-like cd14559
YopH and related bacterial protein tyrosine phosphatases; Yersinia outer protein H (YopH) ...
 785-1013 1.39e-14

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: 74.74  E-value: 1.39e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658117674  785 NRYINIlaydHSRVKLssssdrngWSADYINANYVDGFTQPKAyIATQGPLKSSMEDFWRMVWEQNASVIVMITNLVEKG 864
Cdd:cd14559      1 NRFTNI----QTRVST--------PVGKNLNANRVQIGNKNVA-IACQYPKNEQLEDHLKMLADNRTPCLVVLASNKDIQ 67

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658117674  865 RRKCDQYWPLDSQeeYGSflVTLRSTKVLAYYtQRTFTLKNTRAKKGSQKEQTHERTVvqYHYTQWPDMGV--PEYTLPV 942
Cdd:cd14559     68 RKGLPPYFRQSGT--YGS--VTVKSKKTGKDE-LVDGLKADMYNLKITDGNKTITIPV--VHVTNWPDHTAisSEGLKEL 140

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658117674  943 LTFVRKSSQANLG-------------NMGPVVVHCSAGVGRTGTYIVLDSMlrqIKEQGTVNILGFLKHIRTQRN-YLVQ 1008
Cdd:cd14559    141 ADLVNKSAEEKRNfykskgssaindkNKLLPVIHCRAGVGRTGQLAAAMEL---NKSPNNLSVEDIVSDMRTSRNgKMVQ 217


                   ....*
gi 1658117674 1009 TEEQY 1013
Cdd:cd14559    218 KDEQL 222
PTPc-N3_4 cd14541
catalytic domain of tyrosine-protein phosphatase non-receptor type 21 and type 14; ...
 1107-1253 1.92e-14

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: 73.90  E-value: 1.92e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658117674 1107 DYINASYI-MGYQQS---NEFIITQNPLPSTMKDFWKMIWDHSTQVVIALPDGLDLAEDEC-IYWPTKSQPIRFDTFTVT 1181
Cdd:cd14541      1 DYINANYVnMEIPGSgivNRYIAAQGPLPNTCADFWQMVWEQKSTLIVMLTTLVERGRVKChQYWPDLGETMQFGNLQIT 80

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1658117674 1182 fmgedhmCLSNED--MLIVQDFILEATQDDYVLEVRQYRAPRWPNPDGPiSNTFELINIIKEESVSRDG---PIVVH 1253
Cdd:cd14541     81 -------CVSEEVtpSFAFREFILTNTNTGEERHITQMQYLAWPDHGVP-DDSSDFLDFVKRVRQNRVGmvePTVVH 149
PTPc-N21_14 cd14540
catalytic domain of tyrosine-protein phosphatase non-receptor type 21 and type 14; ...
 1108-1311 9.28e-13

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: 69.02  E-value: 9.28e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658117674 1108 YINASYIMGYQQSNE--FIITQNPLPSTMKDFWKMIWDHSTQVVIALPDGLDLAEDECI-YWPtksqpirfdtftvtFMG 1184
Cdd:cd14540      1 YINASHITATVGGKQrfYIAAQGPLQNTVGDFWQMVWEQGVYLVVMVTAEEEGGREKCFrYWP--------------TLG 66

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658117674 1185 EDHMCLSNEDMLIVQDFILEAtqDDYV--------LEVRQYRA------PRWPN---PDGPisNTF----ELINIIKEES 1243
Cdd:cd14540     67 GEHDALTFGEYKVSTKFSVSS--GCYTttglrvkhTLSGQSRTvwhlqyTDWPDhgcPEDV--SGFldflEEINSVRRHT 142

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1658117674 1244 VS------RDGPIVVHDKRGGNIAGTFCALMTLLHQLEMESSFDVYWVAKMINLMRPGIFTDIDQYQFLYKVIM 1311
Cdd:cd14540    143 NQdvaghnRNPPTLVHCSAGVGRTGVVILADLMLYCLDHNEELDIPRVLALLRHQRMLLVQTLAQYKFVYNVLI 216
fn3 pfam00041
Fibronectin type III domain;
316-398 2.06e-11

Fibronectin type III domain;


Pssm-ID: 394996 [Multi-domain]  Cd Length: 85  Bit Score: 61.28  E-value: 2.06e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658117674  316 SEPENVEADPYNYTSLLVTWERPRAVYDVgIERYLVSYQPVGDEDlPKNEYLTDGDQDvGAIIQDLSANTSYVVQVVAVC 395
Cdd:pfam00041    1 SAPSNLTVTDVTSTSLTVSWTPPPDGNGP-ITGYEVEYRPKNSGE-PWNEITVPGTTT-SVTLTGLKPGTEYEVRVQAVN 77


                   ...
gi 1658117674  396 ING 398
Cdd:pfam00041   78 GGG 80
PHA02740 PHA02740
protein tyrosine phosphatase; Provisional
 1076-1317 4.86e-10

protein tyrosine phosphatase; Provisional


Pssm-ID: 165107 [Multi-domain]  Cd Length: 298  Bit Score: 62.29  E-value: 4.86e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658117674 1076 KQCNRDKNR---NSSLLPVER---SRVHLSTTAGEISdyinASYIMGYQQSNEFIITQNPLPSTMKDFWKMIWDHSTQVV 1149
Cdd:PHA02740    44 KACAQAENKakdENLALHITRllhRRIKLFNDEKVLD----ARFVDGYDFEQKFICIINLCEDACDKFLQALSDNKVQII 119

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658117674 1150 IALPdglDLAEDECI--YWPTKSQPIR-FDTF---TVTFMGEDHMCLSnedMLIVQDFILEATQddyvLEVRQYRAprWP 1223
Cdd:PHA02740   120 VLIS---RHADKKCFnqFWSLKEGCVItSDKFqieTLEIIIKPHFNLT---LLSLTDKFGQAQK----ISHFQYTA--WP 187

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658117674 1224 ------NPDGPISNTFEL----INIIKEESVSRDGPIVVHDKRGGNIAGTFCALMTLLHQLEMESSFDVYWVAKMINLMR 1293
Cdd:PHA02740   188 adgfshDPDAFIDFFCNIddlcADLEKHKADGKIAPIIIDCIDGISSSAVFCVFDICATEFDKTGMLSIANALKKVRQKK 267

                          250       260
                   ....*....|....*....|....
gi 1658117674 1294 PGIFTDIDQYQFLYKVIMSLVAKK 1317
Cdd:PHA02740   268 YGCMNCLDDYVFCYHLIAAYLKEK 291
PTPc-N21 cd14598
catalytic domain of tyrosine-protein phosphatase non-receptor type 21; Tyrosine-protein ...
 1108-1314 1.33e-09

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: 59.60  E-value: 1.33e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658117674 1108 YINASYIMGYQQSNE--FIITQNPLPSTMKDFWKMIWDHSTQVVIALPDGLDLAEDECI-YWP---TKSQPIRFDTFTVT 1181
Cdd:cd14598      1 YINASHIKVTVGGKEwdYIATQGPLQNTCQDFWQMVWEQGVAIIAMVTAEEEGGREKSFrYWPrlgSRHNTVTYGRFKIT 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658117674 1182 F-MGEDHMCLSNEDMLIVQdfiLEATQDDYVLEVrQYraPRWPNPDGPiSNTFELINIIKE-ESVSR-----------DG 1248
Cdd:cd14598     81 TrFRTDSGCYATTGLKIKH---LLTGQERTVWHL-QY--TDWPEHGCP-EDLKGFLSYLEEiQSVRRhtnstidpkspNP 153

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1658117674 1249 PIVVHDKRGGNIAGTFCALMTLLHQLEMESSFDVYWVAKMINLMRPGIFTDIDQYQFLYKVIMSLV 1314
Cdd:cd14598    154 PVLVHCSAGVGRTGVVILSEIMIACLEHNEMLDIPRVLDMLRQQRMMMVQTLSQYTFVYKVLIQFL 219
FN3 smart00060
Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, ...
 316-398 8.28e-09

Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, fibronectin. The tenth fibronectin type III repeat contains a RGD cell recognition sequence in a flexible loop between 2 strands. Type III modules are present in both extracellular and intracellular proteins.


Pssm-ID: 214495 [Multi-domain]  Cd Length: 83  Bit Score: 53.77  E-value: 8.28e-09
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658117674   316 SEPENVEADPYNYTSLLVTWERPRavyDVGIERYLVSYQPVGDEDLPKNEYLTDGDQDVGAIIQDLSANTSYVVQVVAVC 395
Cdd:smart00060    2 SPPSNLRVTDVTSTSVTLSWEPPP---DDGITGYIVGYRVEYREEGSEWKEVNVTPSSTSYTLTGLKPGTEYEFRVRAVN 78


                    ...
gi 1658117674   396 ING 398
Cdd:smart00060   79 GAG 81
PLN02179 PLN02179
carbonic anhydrase
 52-263 2.27e-08

carbonic anhydrase


Pssm-ID: 177835  Cd Length: 235  Bit Score: 56.53  E-value: 2.27e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658117674   52 WAKKYPS---CNNAK-QSPINIDDDLSQVkMQFQKLKlegfEQETSNTTTIHNDGKTVAINLNDEyyisggglrsrfkVG 127
Cdd:PLN02179    50 WGKLNPQwkvCSTGKyQSPIDLTDERVSL-IHDQALS----RHYKPAPAVIQSRGHDVMVSWKGD-------------AG 111

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658117674  128 RITFHWG-----QCNASSDgSEHSLDGIKFPLEMQIYGYEAHkfqsldsalkdgGRLTALSVLFEVsAEDNENYVAIIDG 202
Cdd:PLN02179   112 KITIHQTdyklvQCHWHSP-SEHTINGTSYDLELHMVHTSAS------------GKTAVVGVLYKL-GEPDEFLTKLLNG 177

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1658117674  203 VKTVtrlGKTAVLepfslLGLL-PN----STEKYYIYNGSLTTPPCSETVEWIVFRNTVDISDVQL 263
Cdd:PLN02179   178 IKGV---GKKEIN-----LGIVdPRdirfETNNFYRYIGSLTIPPCTEGVIWTVVKRVVWFFDFNV 235
CDC14 COG2453
Protein-tyrosine phosphatase [Signal transduction mechanisms];
923-1018 5.31e-08

Protein-tyrosine phosphatase [Signal transduction mechanisms];


Pssm-ID: 441989 [Multi-domain]  Cd Length: 140  Bit Score: 53.05  E-value: 5.31e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658117674  923 VQYHYTQWPDMGVPEYT--LPVLTFVRKSSQANlgnmGPVVVHCSAGVGRTGT----YIVLDSM-LRQIkeqgtvnilgf 995
Cdd:COG2453     48 LEYLHLPIPDFGAPDDEqlQEAVDFIDEALREG----KKVLVHCRGGIGRTGTvaaaYLVLLGLsAEEA----------- 112

                           90       100
                   ....*....|....*....|...
gi 1658117674  996 LKHIRTQRNYLVQTEEQYIFIHD 1018
Cdd:COG2453    113 LARVRAARPGAVETPAQRAFLER 135
FN3 cd00063
Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein ...
 316-398 5.64e-08

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


Pssm-ID: 238020 [Multi-domain]  Cd Length: 93  Bit Score: 51.73  E-value: 5.64e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658117674  316 SEPENVEADPYNYTSLLVTWERPRAvYDVGIERYLVSYQPVGDEDLpkNEYLTDGDQDVGAIIQDLSANTSYVVQVVAVC 395
Cdd:cd00063      2 SPPTNLRVTDVTSTSVTLSWTPPED-DGGPITGYVVEYREKGSGDW--KEVEVTPGSETSYTLTGLKPGTEYEFRVRAVN 78


                   ...
gi 1658117674  396 ING 398
Cdd:cd00063     79 GGG 81
PTP_DSP_cys cd14494
cys-based protein tyrosine phosphatase and dual-specificity phosphatase superfamily; This ...
 942-1018 1.50e-07

cys-based protein tyrosine phosphatase and dual-specificity phosphatase superfamily; This superfamily is composed of cys-based phosphatases, which includes classical protein tyrosine phosphatases (PTPs) as well as dual-specificity phosphatases (DUSPs or DSPs). They are characterized by a CxxxxxR conserved catalytic loop (where C is the catalytic cysteine, x is any amino acid, and R is an arginine). PTPs are part of the tyrosine phosphorylation/dephosphorylation regulatory mechanism, and are important in the response of the cells to physiologic and pathologic changes in their environment. DUSPs show more substrate diversity (including RNA and lipids) and include pTyr, pSer, and pThr phosphatases.


Pssm-ID: 350344 [Multi-domain]  Cd Length: 113  Bit Score: 51.20  E-value: 1.50e-07
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1658117674  942 VLTFVRKSSQANLGNmGPVVVHCSAGVGRTGTYIVLDSMLRQIKeqgtvNILGFLKHIRTQR-NYLVQTEEQYIFIHD 1018
Cdd:cd14494     42 VDRFLEVLDQAEKPG-EPVLVHCKAGVGRTGTLVACYLVLLGGM-----SAEEAVRIVRLIRpGGIPQTIEQLDFLIK 113
DUSP23 cd14504
dual specificity phosphatase 23; Dual specificity phosphatase 23 (DUSP23), also known as ...
 923-1016 3.87e-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: 50.74  E-value: 3.87e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658117674  923 VQYHYTQWPDMGVPeyTLPVLT-FVRKSSQANLGNmGPVVVHCSAGVGRTGT----YIVLDSMLR---QIKEqgtvnilg 994
Cdd:cd14504     50 LRYHHIPIEDYTPP--TLEQIDeFLDIVEEANAKN-EAVLVHCLAGKGRTGTmlacYLVKTGKISavdAINE-------- 118

                           90       100
                   ....*....|....*....|..
gi 1658117674  995 flkhIRTQRNYLVQTEEQYIFI 1016
Cdd:cd14504    119 ----IRRIRPGSIETSEQEKFV 136
PLN02202 PLN02202
carbonate dehydratase
 9-264 4.76e-07

carbonate dehydratase


Pssm-ID: 177853 [Multi-domain]  Cd Length: 284  Bit Score: 53.14  E-value: 4.76e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658117674    9 LMMLCQICFIcQIANLAHGYYRTQrkfKEDIDWSYAGTLNQNNWAKKYP---SCNNAK-QSPINIdddlsQVKMQFQKLK 84
Cdd:PLN02202     3 IMMMIKLCFF-AIALICIAPADAQ---TEGVVFGYKGKNGPNQWGHLNPhftKCAVGKlQSPIDI-----QRRQIFYNHK 73

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658117674   85 LEGFEQETSNTT-TIHNDGKTVAInlndeYYISGGG--LRSRFKVGRITFHWgqcnasSDGSEHSLDGIKFPLEMQ-IYG 160
Cdd:PLN02202    74 LESIHRDYYFTNaTLVNHVCNVAM-----FFGEGAGdvIIDNKNYTLLQMHW------HTPSEHHLHGVQYAAELHmVHQ 142

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658117674  161 YEAHKFQSLDSALKDGGRLTALSVLFEVSAEDNE-----NYVAIIDGVKTVTRLgktavlepfsllglLPNSTEKYYIYN 235
Cdd:PLN02202   143 AKDGSFAVVASLFKIGTEEPFLSQMKDKLVKLKEerfkgNHTAQVEVGKIDTRH--------------IERKTRKYFRYI 208

                          250       260
                   ....*....|....*....|....*....
gi 1658117674  236 GSLTTPPCSETVEWIVFRNTVDISDVQLE 264
Cdd:PLN02202   209 GSLTTPPCSENVSWTILGKVRSMSKEQVE 237
PTP_PTPDC1 cd14506
protein tyrosine phosphatase domain of PTP domain-containing protein 1; protein tyrosine ...
 925-1018 2.71e-06

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: 49.65  E-value: 2.71e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658117674  925 YHYT-QWPDMGVPEYTLpVLTFVRKSSQAnLGNMGPVVVHCSAGVGRTGTYI--VLDSMLRQIKEQGtvnILGFlkhiRT 1001
Cdd:cd14506     78 YFYNfGWKDYGVPSLTT-ILDIVKVMAFA-LQEGGKVAVHCHAGLGRTGVLIacYLVYALRMSADQA---IRLV----RS 148

                           90
                   ....*....|....*..
gi 1658117674 1002 QRNYLVQTEEQYIFIHD 1018
Cdd:cd14506    149 KRPNSIQTRGQVLCVRE 165
CDKN3-like cd14505
cyclin-dependent kinase inhibitor 3 and similar proteins; This family is composed of ...
 931-1018 1.67e-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: 46.49  E-value: 1.67e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658117674  931 PDMGVP---EYTLPVLTFVRKssqaNLGNMGPVVVHCSAGVGRTGTyiVLDSMLRQIKEQGTVNILgfLKHIRTQRNYLV 1007
Cdd:cd14505     81 PDGGVPsdiAQWQELLEELLS----ALENGKKVLIHCKGGLGRTGL--IAACLLLELGDTLDPEQA--IAAVRALRPGAI 152

                           90
                   ....*....|.
gi 1658117674 1008 QTEEQYIFIHD 1018
Cdd:cd14505    153 QTPKQENFLHQ 163
PTP_DSP_cys cd14494
cys-based protein tyrosine phosphatase and dual-specificity phosphatase superfamily; This ...
 1241-1308 1.20e-03

cys-based protein tyrosine phosphatase and dual-specificity phosphatase superfamily; This superfamily is composed of cys-based phosphatases, which includes classical protein tyrosine phosphatases (PTPs) as well as dual-specificity phosphatases (DUSPs or DSPs). They are characterized by a CxxxxxR conserved catalytic loop (where C is the catalytic cysteine, x is any amino acid, and R is an arginine). PTPs are part of the tyrosine phosphorylation/dephosphorylation regulatory mechanism, and are important in the response of the cells to physiologic and pathologic changes in their environment. DUSPs show more substrate diversity (including RNA and lipids) and include pTyr, pSer, and pThr phosphatases.


Pssm-ID: 350344 [Multi-domain]  Cd Length: 113  Bit Score: 40.03  E-value: 1.20e-03
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658117674 1241 EESVSRDGPIVVHDKRGGNIAGTFCALMTLLHQLE-MESSFDVYWVAkminlmRPGIFTD-IDQYQFLYK 1308
Cdd:cd14494     50 DQAEKPGEPVLVHCKAGVGRTGTLVACYLVLLGGMsAEEAVRIVRLI------RPGGIPQtIEQLDFLIK 113
 
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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